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\n \n 2023\n \n \n (4)\n \n \n

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\n \n\n \n \n \n \n \n \n Structure Evolution of CaCO₃ Precipitates Formed during the Bacillus cereus Induced Biomineralization.\n \n \n \n \n\n\n \n Ivanova, L. A.; Golovkina, D. A.; Zhurishkina, E. V.; Gorshkova, Y. E.; Yapryntsev, A. D.; Baranchikov, A. E.; Tsvigun, N. V.; Kopitsa, G. P.; Kulminskaya, A. A.; and Lebedev, D. V.\n\n\n \n\n\n\n Minerals, 13(740): 740. 05 2023.\n \n\n\n\n
\n\n\n\n \n \n $\"Structure$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Ivanova2023,\n  author    = {Lyubov A. Ivanova and Darya A. Golovkina and Elena V. Zhurishkina and Yulia E. Gorshkova and Alexey D. Yapryntsev and Alexander E. Baranchikov and Natalia V. Tsvigun and Gennady P. Kopitsa and Anna A. Kulminskaya and Dmitry V. Lebedev},\n  journal   = {Minerals},\n  title     = {Structure Evolution of CaCO<sub>3</sub> Precipitates Formed during the <i>Bacillus cereus</i> Induced Biomineralization},\n  year      = {2023},\n  issn      = {2075-163X},\n  month     = {05},\n  number    = {740},\n  pages     = {740},\n  volume    = {13},\n  abstract  = {Biomineralization is a universal process that has implications in a variety of areas, from civil engineering to medicine. While crystallization of amorphous CaCO<sub>3</sub> formed in vitro is known to precede the vaterite-calcite/aragonite pathway, this process could be significantly altered when induced by bacteria, particularly within the extracellular matrix (ECM) of microbial cells. We used a combination of SEM, SANS, SAXS, FTIR and XRD methods to investigate the structure of CaCO<sub>3</sub> formed during biomineralization induced by planktonic <i>Bacillus cereus.</i> Formation of precipitates in the presence of CaCl<sub>2</sub> and urea was observed both during bacterial growth and in the medium devoid of bacteria and ECM (cell-free system). The pathway for polymorphic transformations of CaCO<sub>3</sub> from the amorphous phase to vaterite and further to calcite was confirmed for the bacterium-induced mineralization and did not depend on the concentration of Ca<sup>2+</sup> and urea. The structure of CaCO<sub>3</sub> sediments differed when formed in cell-free and bacterial systems and varied depending on time and the medium composition. The rate of precipitation was accelerated in the presence of DNA, which had little effect on the solid phase structure in the cell-free system, while strongly affecting the structure and polymorphic composition of the precipitates in bacterial culture.},\n  doi       = {10.3390/min13060740},\n  keywords  = {bacterial biomineralization, calcium carbonate, mesostructure, SAXS, SANS, extracellular matrix},\n  publisher = {MDPI AG},\n  url       = {https://www.mdpi.com/2075-163X/13/6/740},\n}\n\n

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\n \n\n \n \n \n \n \n Matrix is everywhere: extracellular DNA is a link between biofilm and mineralization in Bacillus cereus planktonic lifestyle.\n \n \n \n\n\n \n Ivanova, L. A.; Egorov, V. V.; Zabrodskaya, Y. A.; Shaldzhyan, A. A.; Baranchikov, A. Y.; Tsvigun, N. V.; Lykholay, A. N.; Yapryntsev, A. D.; Lebedev, D. V.; and Kulminskaya, A. A.\n\n\n \n\n\n\n NPJ biofilms and microbiomes, 9: 9. February 2023.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n\n\n\n

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@Article{Ivanova2023a,\n  author          = {Ivanova, Lyubov A. and Egorov, Vladimir V. and Zabrodskaya, Yana A. and Shaldzhyan, Aram A. and Baranchikov, Alexander Ye and Tsvigun, Natalia V. and Lykholay, Anna N. and Yapryntsev, Alexey D. and Lebedev, Dmitry V. and Kulminskaya, Anna A.},\n  journal         = {NPJ biofilms and microbiomes},\n  title           = {Matrix is everywhere: extracellular DNA is a link between biofilm and mineralization in Bacillus cereus planktonic lifestyle.},\n  year            = {2023},\n  issn            = {2055-5008},\n  month           = feb,\n  pages           = {9},\n  volume          = {9},\n  abstract        = {To date, the mechanisms of biomineralization induced by bacterial cells in the context of biofilm formation remain the subject of intensive studies. In this study, we analyzed the influence of the medium components on the induction of CaCO (3)precipitation by the Bacillus cereus cells and composition of the extracellular matrix (ECM) formed in the submerged culture. While the accumulation of extracellular polysaccharides and amyloids appeared to be independent of the presence of calcium and urea during the growth, the accumulation of extracellular DNA (eDNA), as well as precipitation of calcium carbonate, required the presence of both ingredients in the medium. Removal of eDNA, which was sensitive to treatment by DNase, did not affect other matrix components but resulted in disruption of cell network formation and a sixfold decrease in the precipitate yield. An experiment with a cell-free system confirmed the acceleration of mineral formation after the addition of exogenous salmon sperm DNA. The observed pathway for the formation of CaCO (3)minerals in B. cereus planktonic culture included a production of exopolysaccharides and negatively charged eDNA lattice promoting local Ca (2+)supersaturation, which, together with an increase in the concentration of carbonate ions due to pH rise, resulted in the formation of an insoluble precipitate of calcium carbonate. Precipitation of amorphous CaCO (3)on eDNA matrix was followed by crystal formation via the ACC-vaterite-calcite/aragonite pathway and further formation of larger mineral aggregates in complex with extracellular polymeric substances. Taken together, our data showed that DNA in extracellular matrix is an essential factor for triggering the biomineralization in B. cereus planktonic culture.},\n  chemicals       = {Calcium Carbonate, DNA},\n  citation-subset = {IM},\n  completed       = {2023-03-02},\n  country         = {United States},\n  doi             = {10.1038/s41522-023-00377-5},\n  issn-linking    = {2055-5008},\n  issue           = {1},\n  keywords        = {Male; Humans; Bacillus cereus, genetics; Semen; Biofilms; Calcium Carbonate; DNA},\n  nlm-id          = {101666944},\n  owner           = {NLM},\n  pii             = {9},\n  pmc             = {PMC9975174},\n  pmid            = {36854956},\n  pubmodel        = {Electronic},\n  pubstate        = {epublish},\n  revised         = {2023-04-12},\n}\n\n

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\n \n\n \n \n \n \n \n Whole-Cell PVA Cryogel-Immobilized Microbial Consortium LE-C1 for Xanthan Depolymerization.\n \n \n \n\n\n \n Zhurishkina, E.\n\n\n \n\n\n\n Catalysts, 13(9). 2023.\n Query date: 2024-02-01 13:12:36\n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Zhurishkina2023,\n  author   = {E.V. Zhurishkina},\n  journal  = {Catalysts},\n  title    = {Whole-Cell PVA Cryogel-Immobilized Microbial Consortium LE-C1 for Xanthan Depolymerization},\n  year     = {2023},\n  issn     = {2073-4344},\n  note     = {Query date: 2024-02-01 13:12:36},\n  number   = {9},\n  volume   = {13},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/85172477906},\n  doi      = {10.3390/catal13091249},\n  type     = {Article},\n}\n\n

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\n \n\n \n \n \n \n \n Structural and Functional Features of Ketose-3-Epimerases and Their Use for D-Allulose Production.\n \n \n \n\n\n \n Ivanova, N.\n\n\n \n\n\n\n Russian Journal of Bioorganic Chemistry, 49(4): 731–741. 2023.\n Query date: 2024-02-01 13:12:36\n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Ivanova2023b,\n  author   = {N.S. Ivanova},\n  journal  = {Russian Journal of Bioorganic Chemistry},\n  title    = {Structural and Functional Features of Ketose-3-Epimerases and Their Use for D-Allulose Production},\n  year     = {2023},\n  issn     = {1068-1620},\n  note     = {Query date: 2024-02-01 13:12:36},\n  number   = {4},\n  pages    = {731--741},\n  volume   = {49},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/85168509098},\n  doi      = {10.1134/S106816202304012X},\n  type     = {Review},\n}\n\n

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\n \n 2022\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Forgotten Actors: Glycoside Hydrolases During Elongation Growth of Maize Primary Root.\n \n \n \n \n\n\n \n Nazipova, A.; Gorshkov, O.; Eneyskaya, E.; Petrova, N.; Kulminskaya, A.; Kulminskaya, A.; Gorshkova, T.; and Kozlova, L.\n\n\n \n\n\n\n Frontiers in Plant Science, 12. 2 2022.\n \n\n\n\n
\n\n\n\n \n \n $\"Forgotten$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Nazipova2022,\n  author    = {Alsu Nazipova and Oleg Gorshkov and Elena Eneyskaya and Natalia Petrova and Anna Kulminskaya and Anna Kulminskaya and Tatyana Gorshkova and Liudmila Kozlova},\n  journal   = {Frontiers in Plant Science},\n  title     = {Forgotten Actors: Glycoside Hydrolases During Elongation Growth of Maize Primary Root},\n  year      = {2022},\n  issn      = {1664-462X},\n  month     = {2},\n  volume    = {12},\n  abstract  = {Plant cell enlargement is coupled to dynamic changes in cell wall composition and properties. Such rearrangements are provided, besides the differential synthesis of individual cell wall components, by enzymes that modify polysaccharides in muro. To reveal enzymes that may contribute to these modifications and relate them to stages of elongation growth in grasses, we carried out a transcriptomic study of five zones of the primary maize root. In the initiation of elongation, significant changes occur with xyloglucan: once synthesized in the meristem, it can be linked to other polysaccharides through the action of hetero-specific xyloglucan endotransglycosidases, whose expression boosts at this stage. Later, genes for xyloglucan hydrolases are upregulated. Two different sets of enzymes capable of modifying glucuronoarabinoxylans, mainly bifunctional α-arabinofuranosidases/β-xylosidases and β-xylanases, are expressed in the maize root to treat the xylans of primary and secondary cell walls, respectively. The first set is highly pronounced in the stage of active elongation, while the second is at elongation termination. Genes encoding several glycoside hydrolases that are able to degrade mixed-linkage glucan are downregulated specifically at the active elongation. It indicates the significance of mixed-linkage glucans for the cell elongation process. The possibility that many glycoside hydrolases act as transglycosylases in muro is discussed.},\n  doi       = {10.3389/fpls.2021.802424},\n  keywords  = {cell wall, elongation (growth), maize (Zea mays L.), root, glycoside hydrolase, RNA-seq},\n  publisher = {Frontiers Media S.A.},\n  url       = {https://www.frontiersin.org/articles/10.3389/fpls.2021.802424/full},\n}\n\n

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\n \n\n \n \n \n \n \n Effect of Brown Algae and Lichen Extracts on the SCOBY Microbiome and Kombucha Properties.\n \n \n \n\n\n \n Golovkina, D. A.; Zhurishkina, E. V.; Ayrapetyan, O. N.; Komissarov, A. E.; Krylova, A. S.; Vinogradova, E. N.; Toshchakov, S. V.; Ermilov, F. K.; Barsegyan, A. M.; Kulminskaya, A. A.; and Lapina, I. M.\n\n\n \n\n\n\n Foods (Basel, Switzerland), 12. December 2022.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n\n\n\n

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@Article{Golovkina2022,\n  author       = {Golovkina, Darya A. and Zhurishkina, Elena V. and Ayrapetyan, Olga N. and Komissarov, Artem E. and Krylova, Anastasiya S. and Vinogradova, Elizaveta N. and Toshchakov, Stepan V. and Ermilov, Filipp K. and Barsegyan, Artak M. and Kulminskaya, Anna A. and Lapina, Irina M.},\n  journal      = {Foods (Basel, Switzerland)},\n  title        = {Effect of Brown Algae and Lichen Extracts on the SCOBY Microbiome and Kombucha Properties.},\n  year         = {2022},\n  issn         = {2304-8158},\n  month        = dec,\n  volume       = {12},\n  abstract     = {Kombucha tea was made by the fermentation of SCOBY culture of green tea broth with the addition of Fucus vesiculosus algae extract, Cetraria islandica lichen extract and their mixture. Kombucha was also made without the herbal supplements as a control. After 11 days of fermentation, in addition to the yeast Brettanomyces bruxellensis and the bacteria Komagataeibacter rhaeticus and Komagataeibacter hansenii contained in all of the samples, the yeast Zygosaccharomyces bailii and bacteria Komagataeibacter cocois were detected in the samples with the herbal extracts. In all of the kombucha with herbal additives, the total fraction of yeast was decreased as compared to the control. The total content of polyphenols and the antioxidant activity of the beverages with and without the addition of herbal extracts were comparable. The kombucha made with the algae extract showed an increased content of sucrose and organic acids, while the fructose and glucose content in the samples with algae and the mixture of extracts were lower than in the other samples. The samples with the algae extract had the highest organoleptic indicators "aroma", "clarity" and "acidity", while the control samples had slightly higher indicators of "taste" and "aftertaste". The results of this study indicate the potential of algae and lichens as functional supplements for obtaining non-alcoholic fermented beverages with additional nutraceutical value.},\n  country      = {Switzerland},\n  doi          = {10.3390/foods12010047},\n  issn-linking = {2304-8158},\n  issue        = {1},\n  keywords     = {Cetraria islandica; Fucus vesiculosus; antioxidant activity; kombucha; metagenomic analysis; nutraceutical; sugar content; synbiotics},\n  nlm-id       = {101670569},\n  owner        = {NLM},\n  pii          = {47},\n  pmc          = {PMC9818207},\n  pmid         = {36613265},\n  pubmodel     = {Electronic},\n  pubstate     = {epublish},\n  revised      = {2023-01-11},\n}\n\n

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\n \n 2021\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Antibacterial Properties of Fucoidans from the Brown Algae Fucus vesiculosus L. of the Barents Sea.\n \n \n \n \n\n\n \n Ayrapetyan, O. N.; Obluchinskaya, E. D.; Zhurishkina, E. V.; Skorik, Y. A.; Lebedev, D. V.; Kulminskaya, A. A.; and Lapina, I. M.\n\n\n \n\n\n\n Biology, 10(67): 67. 01 2021.\n \n\n\n\n
\n\n\n\n \n \n $\"Antibacterial$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Ayrapetyan2021,\n  author    = {Olga N. Ayrapetyan and Ekaterina D. Obluchinskaya and Elena V. Zhurishkina and Yury A. Skorik and Dmitry V. Lebedev and Anna A. Kulminskaya and Irina M. Lapina},\n  journal   = {Biology},\n  title     = {Antibacterial Properties of Fucoidans from the Brown Algae <i>Fucus vesiculosus</i> L. of the Barents Sea},\n  year      = {2021},\n  issn      = {2079-7737},\n  month     = {01},\n  number    = {67},\n  pages     = {67},\n  volume    = {10},\n  abstract  = {Fucoidans, sulfated polysaccharides found in cell walls of brown algae, are considered as a promising antimicrobial component for various applications in medicine and the food industry. In this study, we compare the antibacterial properties of two fractions of fucoidan from the brown algae <i>Fucus vesiculosus</i> gathered in the littoral of the Barents Sea and sampled at different stages of purification. The crude fraction of fucoidan was isolated from algae by extraction with aqueous ethanol and sonication. The purified fraction was obtained by additional treatment of the crude fraction with a solution of calcium chloride. The structural features of both fractions were characterized in detail and their antibacterial effects against several Gram-positive and Gram-negative bacteria were compared by photometry, acridine orange staining assay, and atomic force microscopy. Fucoidan inhibited growth in all of the above microorganisms, showing a bacteriostatic effect with minimum inhibitory concentrations (MIC) in the range between 4 and 6 mg/mL, with <i>E. coli</i> being the most sensitive to both fractions. Changes in the chemical composition after treatment of the crude fraction with a solution of calcium chloride led to a decrease in the content of sulfates and uronic acids and diminished antibacterial activity.},\n  doi       = {10.3390/biology10010067},\n  keywords  = {<i > Fucus vesiculosus</i, fucoidan, antibacterial activity, atomic force microscopy},\n  publisher = {MDPI AG},\n  url       = {https://www.mdpi.com/2079-7737/10/1/67},\n}\n\n

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\n \n 2020\n \n \n (7)\n \n \n

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\n \n\n \n \n \n \n \n \n The effect of polydisperse fucoidans from Fucus vesiculosus on Hep G2 and Chang liver cells.\n \n \n \n \n\n\n \n Zhurishkina, E.; Stepanov, S.; Ayrapetyan, O.; Skorik, Y.; Vlasova, E.; Kruchina-Bogdanov, I.; Lebedev, D.; Kulminskaya, A.; and Lapina, I.\n\n\n \n\n\n\n Bioactive Carbohydrates and Dietary Fibre, 21. 2020.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Zhurishkina2020,\nauthor={Zhurishkina, E.V. and Stepanov, S.I. and Ayrapetyan, O.N. and Skorik, Y.A. and Vlasova, E.N. and Kruchina-Bogdanov, I.V. and Lebedev, D.V. and Kulminskaya, A.A. and Lapina, I.M.},\ntitle={The effect of polydisperse fucoidans from Fucus vesiculosus on Hep G2 and Chang liver cells},\njournal={Bioactive Carbohydrates and Dietary Fibre},\nyear={2020},\nvolume={21},\ndoi={10.1016/j.bcdf.2019.100209},\nart_number={100209},\nnote={cited By 3},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85077001443&doi=10.1016%2fj.bcdf.2019.100209&partnerID=40&md5=fe22c757b68b40df378f3bc4e5b2386a},\naffiliation={Petersburg Nuclear Physics Institute named by B.P. Konstantinov of National Research Centre «Kurchatov Institute», Gatchina, Russian Federation; Kurchatov Genome Center – PNPI, Gatchina, Russian Federation; Saint Petersburg National Research University of Information Technologies, Mechanics and Optics, St. Petersburg, Russian Federation; Institute of Macromolecular Compounds of the Russian Academy of Sciences, St. Petersburg, Russian Federation; Analytics. Materials. Technologies Ltd, St. Petersburg, Russian Federation; National Research Centre «Kurchatov Institute», Moscow, Russian Federation},\nauthor_keywords={Chang liver;  Fucoidan;  Hep G2},\nkeywords={fucoidin;  polysaccharide, antineoplastic activity;  apoptosis;  Article;  autophagy;  cell organelle;  cell proliferation;  Chang Liver cell line;  comparative study;  dispersity;  endocytosis;  Fucus vesiculosus;  Hep-G2 cell line;  human;  human cell;  hydrolysis;  internalization;  molecular weight;  priority journal},\nchemicals_cas={fucoidin, 9072-19-9},\ncorrespondence_address1={Lapina, I.M.; Petersburg Nuclear Physics Institute named by B.P. Konstantinov of National Research Centre «Kurchatov Institute», Gatchina, Russian Federation; email: lapina_im@pnpi.nrcki.ru},\npublisher={Elsevier Ltd},\nissn={22126198},\nlanguage={English},\nabbrev_source_title={Bioact. Carbohydr. Dietary Fibre},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Calcifying Bacteria Flexibility in Induction of CaCO₃ Mineralization.\n \n \n \n \n\n\n \n Golovkina, D. A.; Zhurishkina, E. V.; Ivanova, L. A.; Baranchikov, A. E.; Sokolov, A. Y.; Bobrov, K. S.; Masharsky, A. E.; Tsvigun, N. V.; Kopitsa, G. P.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Life, 10(317): 317. 11 2020.\n \n\n\n\n
\n\n\n\n \n \n $\"Calcifying$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Golovkina2020,\n  author    = {Darya A. Golovkina and Elena V. Zhurishkina and Lyubov A. Ivanova and Alexander E. Baranchikov and Alexey Y. Sokolov and Kirill S. Bobrov and Alexey E. Masharsky and Natalia V. Tsvigun and Gennady P. Kopitsa and Anna A. Kulminskaya},\n  journal   = {Life},\n  title     = {Calcifying Bacteria Flexibility in Induction of CaCO<sub>3</sub> Mineralization},\n  year      = {2020},\n  issn      = {2075-1729},\n  month     = {11},\n  number    = {317},\n  pages     = {317},\n  volume    = {10},\n  abstract  = {Microbially induced CaCO<sub>3</sub> precipitation (MICP) is considered as an alternative green technology for cement self-healing and a basis for the development of new biomaterials. However, some issues about the role of bacteria in the induction of biogenic CaCO<sub>3</sub> crystal nucleation, growth and aggregation are still debatable. Our aims were to screen for ureolytic calcifying microorganisms and analyze their MICP abilities during their growth in urea-supplemented and urea-deficient media. Nine candidates showed a high level of urease specific activity, and a sharp increase in the urea-containing medium pH resulted in efficient CaCO<sub>3</sub> biomineralization. In the urea-deficient medium, all ureolytic bacteria also induced CaCO<sub>3</sub> precipitation although at lower pH values. Five strains (<i>B. licheniformis</i> DSMZ 8782, <i>B. cereus</i> 4b, <i>S. epidermidis</i> 4a, <i>M. luteus</i> BS52, <i>M. luteus</i> 6) were found to completely repair micro-cracks in the cement samples. Detailed studies of the most promising strain <i>B. licheniformis</i> DSMZ 8782 revealed a slower rate of the polymorph transformation in the urea-deficient medium than in urea-containing one. We suppose that a ureolytic microorganism retains its ability to induce CaCO<sub>3</sub> biomineralization regardless the origin of carbonate ions in a cell environment by switching between mechanisms of urea-degradation and metabolism of calcium organic salts.},\n  doi       = {10.3390/life10120317},\n  keywords  = {calcium carbonate, biomineralization, ureolytic bacteria, polymorph},\n  publisher = {MDPI AG},\n  url       = {https://www.mdpi.com/2075-1729/10/12/317},\n}\n\n

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\n \n\n \n \n \n \n \n Nonspecific enzymatic hydrolysis of a highly ordered chitopolysaccharide substrate.\n \n \n \n\n\n \n Poshina, D. N.; Raik, S. V.; Sukhova, A. A.; Tyshkunova, I. V.; Romanov, D. P.; Eneyskaya, E. V.; Kulminskaya, A. A.; and Skorik, Y. A.\n\n\n \n\n\n\n Carbohydrate research, 498: 108191. December 2020.\n \n\n\n\n
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@Article{Poshina2020,\n  author          = {Poshina, Daria N. and Raik, Sergei V. and Sukhova, Arina A. and Tyshkunova, Irina V. and Romanov, Dmitry P. and Eneyskaya, Elena V. and Kulminskaya, Anna A. and Skorik, Yury A.},\n  journal         = {Carbohydrate research},\n  title           = {Nonspecific enzymatic hydrolysis of a highly ordered chitopolysaccharide substrate.},\n  year            = {2020},\n  issn            = {1873-426X},\n  month           = dec,\n  pages           = {108191},\n  volume          = {498},\n  abstract        = {Chitin and chitosan can undergo nonspecific enzymatic hydrolysis by several different hydrolases. This susceptibility to nonspecific enzymes opens up many opportunities for producing chitooligosaccharides and low molecular weight chitopolysaccharides, since specific chitinases and chitosanases are rare and not commercially available. In this study, chitosan and chitin were hydrolyzed using several commercially available hydrolases. Among them, cellulases with the highest specific activity demonstrated the best activity, as indicated by the rapid decrease in viscosity of a chitosan solution. The hydrolysis of chitosan by nonspecific enzymes generated a sugar release that corresponded to the decrease in the degree of polymerization. This decrease reached a maximum of 3.3-fold upon hydrolysis of 10% of the sample. Cellulases were better than lysozyme or amylases at hydrolyzing chitosan and chitin. Analysis of (13)C CP-MAS NMR and FTIR spectra of chitin after cellulase treatment revealed changes in the chitin crystal structure related to rearrangement of inter- and intramolecular H-bonds. The structural changes and decreases in crystallinity allowed dissolution of chitin molecules of high molecular weight and enhanced the solubility of chitin in alkali by 10-12% compared to untreated chitin.},\n  chemicals       = {Chitin, Chitosan, Hydrolases},\n  citation-subset = {IM},\n  completed       = {2021-08-23},\n  country         = {Netherlands},\n  doi             = {10.1016/j.carres.2020.108191},\n  issn-linking    = {0008-6215},\n  keywords        = {Chitin, chemistry; Chitosan, chemistry; Hydrogen Bonding; Hydrolases, metabolism; Hydrolysis; Viscosity; Cellulases; Cellulose-binding domain; Chitin; Chitosan; Crystalline structure},\n  nlm-id          = {0043535},\n  owner           = {NLM},\n  pii             = {S0008-6215(20)30562-0},\n  pmid            = {33157460},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2021-08-23},\n}\n\n

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\n \n\n \n \n \n \n \n A novel acid-tolerant β-xylanase from Scytalidium candidum 3C for the synthesis of o-nitrophenyl xylooligosaccharides.\n \n \n \n\n\n \n Eneyskaya, E. V.; Bobrov, K. S.; Kashina, M. V.; Borisova, A. S.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Journal of basic microbiology, 60: 971–982. November 2020.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Eneyskaya2020,\n  author          = {Eneyskaya, Elena V. and Bobrov, Kirill S. and Kashina, Maria V. and Borisova, Anna S. and Kulminskaya, Anna A.},\n  journal         = {Journal of basic microbiology},\n  title           = {A novel acid-tolerant β-xylanase from Scytalidium candidum 3C for the synthesis of o-nitrophenyl xylooligosaccharides.},\n  year            = {2020},\n  issn            = {1521-4028},\n  month           = nov,\n  pages           = {971--982},\n  volume          = {60},\n  abstract        = {Endo-β-xylanases are hemicellulases involved in the conversion of xylans in plant biomass. Here, we report a novel acidophilic β-xylanase (ScXynA) with high transglycosylation abilities that was isolated from the filamentous fungus Scytalidium candidum 3C. ScXynA was identified as a glycoside hydrolase family 10 (GH10) dimeric protein, with a molecular weight of 38 ± 5 kDa per subunit. The enzyme catalyzed the hydrolysis of different xylans under acidic conditions and was stable in the pH range 2.6-4.5. The kinetic parameters of ScXynA were determined in hydrolysis reactions with p-nitrophenyl-β-d-cellobioside (pNP-β-Cel) and p-nitrophenyl-β-d-xylobioside (pNP-β-Xyl (2)), and k (cat)/K (m)was found to be 0.43 ± 0.02 (s·mM) (-1)and 57 ± 3 (s·mM) (-1), respectively. In the catalysis of the transglycosylation o-nitrophenyl-β-d-xylobioside (oNP-β-Xyl (2)) acted both as a donor and an acceptor, resulting in the efficient production of o-nitrophenyl xylooligosaccharides, with a degree of polymerization of 3-10 and o-nitrophenyl-β-d-xylotetraose (oNP-β-Xyl (4)) as the major product (18.5% yield). The modeled ScXynA structure showed a favorable position for ligand entry and o-nitrophenyl group accommodation in the relatively open -3 subsite, while the cleavage site was covered with an extended loop. These structural features provide favorable conditions for transglycosylation with oNP-β-Xyl (2). The acidophilic properties and high transglycosylation activity make ScXynA a suitable choice for various biotechnological applications, including the synthesis of valuable xylooligosaccharides.},\n  chemicals       = {Glucuronates, Oligosaccharides, Xylans, xylooligosaccharide, Endo-1,4-beta Xylanases},\n  citation-subset = {IM},\n  completed       = {2021-07-02},\n  country         = {Germany},\n  doi             = {10.1002/jobm.202000303},\n  issn-linking    = {0233-111X},\n  issue           = {11-12},\n  keywords        = {Ascomycota, enzymology; Catalysis; Endo-1,4-beta Xylanases, chemistry, isolation & purification, metabolism; Glucuronates, metabolism; Glycosylation; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Models, Molecular; Molecular Weight; Oligosaccharides, metabolism; Protein Multimerization; Substrate Specificity; Temperature; Xylans, metabolism; glycoside hydrolase family 10; o-nitrophenyl xylooligosaccharides; transglycosylation; β-xylanase},\n  nlm-id          = {8503885},\n  owner           = {NLM},\n  pmid            = {33103248},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2021-07-02},\n}\n\n

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\n \n\n \n \n \n \n \n Crystal and Supramolecular Structure of Bacterial Cellulose Hydrolyzed by Cellobiohydrolase from Scytalidium Candidum 3C: A Basis for Development of Biodegradable Wound Dressings.\n \n \n \n\n\n \n Ivanova, L. A.; Ustinovich, K. B.; Khamova, T. V.; Eneyskaya, E. V.; Gorshkova, Y. E.; Tsvigun, N. V.; Burdakov, V. S.; Verlov, N. A.; Zinovev, E. V.; Asadulaev, M. S.; Shabunin, A. S.; Fedyk, A. M.; Baranchikov, A. Y.; Kopitsa, G. P.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Materials (Basel, Switzerland), 13. May 2020.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n\n\n\n

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@Article{Ivanova2020,\n  author       = {Ivanova, Lyubov A. and Ustinovich, Konstantin B. and Khamova, Tamara V. and Eneyskaya, Elena V. and Gorshkova, Yulia E. and Tsvigun, Natalia V. and Burdakov, Vladimir S. and Verlov, Nikolay A. and Zinovev, Evgenii V. and Asadulaev, Marat S. and Shabunin, Anton S. and Fedyk, Andrey M. and Baranchikov, Alexander Ye and Kopitsa, Gennady P. and Kulminskaya, Anna A.},\n  journal      = {Materials (Basel, Switzerland)},\n  title        = {Crystal and Supramolecular Structure of Bacterial Cellulose Hydrolyzed by Cellobiohydrolase from Scytalidium Candidum 3C: A Basis for Development of Biodegradable Wound Dressings.},\n  year         = {2020},\n  issn         = {1996-1944},\n  month        = may,\n  volume       = {13},\n  abstract     = {The crystal and supramolecular structure of the bacterial cellulose (BC) has been studied at different stages of cellobiohydrolase hydrolysis using various physical and microscopic methods. Enzymatic hydrolysis significantly affected the crystal and supramolecular structure of native BC, in which the 3D polymer network consisted of nanoribbons with a thickness T ≈ 8 nm and a width W ≈ 50 nm, and with a developed specific surface S (BET)≈ 260 m (2)·g (-1). Biodegradation for 24 h led to a ten percent decrease in the mean crystal size D (hkl)of BC, to two-fold increase in the sizes of nanoribbons, and in the specific surface area S (BET)up to ≈ 100 m (2)·g (-1). Atomic force and scanning electron microscopy images showed BC microstructure "loosening"after enzymatic treatment, as well as the formation and accumulation of submicron particles in the cells of the 3D polymer network. Experiments in vitro and in vivo did not reveal cytotoxic effect by the enzyme addition to BC dressings and showed a generally positive influence on the treatment of extensive III-degree burns, significantly accelerating wound healing in rats. Thus, in our opinion, the results obtained can serve as a basis for further development of effective biodegradable dressings for wound healing.},\n  country      = {Switzerland},\n  doi          = {10.3390/ma13092087},\n  issn-linking = {1996-1944},\n  issue        = {9},\n  keywords     = {bacterial cellulose; cellobiohydrolase; enzymatic hydrolysis; meso- and microstructure; wound dressing},\n  nlm-id       = {101555929},\n  owner        = {NLM},\n  pii          = {2087},\n  pmc          = {PMC7254194},\n  pmid         = {32369952},\n  pubmodel     = {Electronic},\n  pubstate     = {epublish},\n  revised      = {2020-09-28},\n}\n\n

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\n \n\n \n \n \n \n \n Branched architecture of fucoidan characterized by dynamic and static light scattering.\n \n \n \n\n\n \n Gasilova, E.\n\n\n \n\n\n\n Colloid and Polymer Science, 298(10): 1349–1359. 2020.\n 5 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85088498134&origin=inward\n\n\n\n
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@Article{Gasilova2020,\n  author   = {E.R. Gasilova},\n  journal  = {Colloid and Polymer Science},\n  title    = {Branched architecture of fucoidan characterized by dynamic and static light scattering},\n  year     = {2020},\n  issn     = {0303-402X},\n  note     = {5 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=85088498134\\&origin=inward},\n  number   = {10},\n  pages    = {1349--1359},\n  volume   = {298},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/85088498134},\n  doi      = {10.1007/s00396-020-04706-4},\n  type     = {Article},\n}\n\n

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\n \n\n \n \n \n \n \n Structural Organization of the Active Center of Unmodified Recombinant Sulfatase from the Mycelial Fungi Fusarium proliferatum LE1.\n \n \n \n\n\n \n Kolchina, N.\n\n\n \n\n\n\n Russian Journal of Bioorganic Chemistry, 46(4): 563–571. 2020.\n Query date: 2024-02-01 13:12:36\n\n\n\n
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@Article{Kolchina2020,\n  author   = {N.V. Kolchina},\n  journal  = {Russian Journal of Bioorganic Chemistry},\n  title    = {Structural Organization of the Active Center of Unmodified Recombinant Sulfatase from the Mycelial Fungi Fusarium proliferatum LE1},\n  year     = {2020},\n  issn     = {1068-1620},\n  note     = {Query date: 2024-02-01 13:12:36},\n  number   = {4},\n  pages    = {563--571},\n  volume   = {46},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/85091461329},\n  doi      = {10.1134/S1068162020040081},\n  type     = {Article},\n}\n\n

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\n \n 2019\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Erratum: Retraction for polev et al., \"Draft genome sequence of Geotrichum candidum Strain 3C\" (Microbiol Resour Announc (2019) 8:e00561-19. doi.10.1128/genomeA.00956-14).\n \n \n \n \n\n\n \n Polev, D.; Bobrov, K.; Eneyskaya, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Microbiology Resource Announcements, 8(24). 2019.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Erratum:$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n\n\n\n

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@ARTICLE{Polev2019,\nauthor={Polev, D.E. and Bobrov, K.S. and Eneyskaya, E.V. and Kulminskaya, A.A.},\ntitle={Erratum: Retraction for polev et al., "Draft genome sequence of Geotrichum candidum Strain 3C" (Microbiol Resour Announc (2019) 8:e00561-19. doi.10.1128/genomeA.00956-14)},\njournal={Microbiology Resource Announcements},\nyear={2019},\nvolume={8},\nnumber={24},\ndoi={10.1128/MRA.00561-19},\nart_number={e00561-19},\nnote={cited By 0},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85069478479&doi=10.1128%2fMRA.00561-19&partnerID=40&md5=7b812082ec64d305fb2e108b02888af7},\naffiliation={Research Resource Center for Molecular and Cell Technologies, St. Petersburg State University, St. Petersburg, Russian Federation; National Research Centre, Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova Roscha, Russian Federation; St. Petersburg State Polytechnical University, St. Petersburg, Russian Federation},\nkeywords={retraction notice},\ncorrespondence_address1={Polev, D.E.; Research Resource Center for Molecular and Cell Technologies, Russian Federation; email: dmitry.polev@gmail.com},\npublisher={American Society for Microbiology},\nissn={2576098X},\nlanguage={English},\nabbrev_source_title={Micro. Res. Ann},\ndocument_type={Erratum},\nsource={Scopus},\n}\n\n

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\n \n 2018\n \n \n (5)\n \n \n

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\n \n\n \n \n \n \n \n Microbial Sulfatases.\n \n \n \n\n\n \n Shvetsova, S. V.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Moscow University Chemistry Bulletin, 73(4): 139-151. July 2018.\n \n\n\n\n
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@Article{Shvetsova2018,\n  author    = {S. V. Shvetsova and A. A. Kulminskaya},\n  journal   = {Moscow University Chemistry Bulletin},\n  title     = {Microbial Sulfatases},\n  year      = {2018},\n  issn      = {0027-1314},\n  month     = jul,\n  number    = {4},\n  pages     = {139-151},\n  volume    = {73},\n  doi       = {10.3103/s0027131418040090},\n  publisher = {Allerton Press},\n}\n\n

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\n \n\n \n \n \n \n \n \n Corrigendum: Pleiotropic Meta-Analyses of Longitudinal Studies Discover Novel Genetic Variants Associated with Age-Related Diseases.\n \n \n \n \n\n\n \n He, L.; Kernogitski, Y.; Kulminskaya, I.; Loika, Y.; Arbeev, K. G.; Loiko, E.; Bagley, O.; Duan, M.; Yashkin, A.; Ukraintseva, S. V.; Kovtun, M.; Yashin, A. I.; and Kulminski, A. M.\n\n\n \n\n\n\n Frontiers in Genetics, 8. 01 2018.\n \n\n\n\n
\n\n\n\n \n \n $\"Corrigendum:$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{He2018,\n  author    = {Liang He and Yelena Kernogitski and Irina Kulminskaya and Yury Loika and Konstantin G. Arbeev and Elena Loiko and Olivia Bagley and Matt Duan and Arseniy Yashkin and Svetlana V. Ukraintseva and Mikhail Kovtun and Anatoliy I. Yashin and Alexander M. Kulminski},\n  journal   = {Frontiers in Genetics},\n  title     = {Corrigendum: Pleiotropic Meta-Analyses of Longitudinal Studies Discover Novel Genetic Variants Associated with Age-Related Diseases},\n  year      = {2018},\n  issn      = {1664-8021},\n  month     = {01},\n  volume    = {8},\n  doi       = {10.3389/fgene.2017.00226},\n  keywords  = {pleiotropic analysis, age-related traits, CVDs, genetic association study, mediation analysis, age-dependent effects},\n  publisher = {Frontiers Media S.A.},\n  url       = {http://journal.frontiersin.org/article/10.3389/fgene.2017.00226/full},\n}\n\n

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\n \n\n \n \n \n \n \n Comprehensive Analysis of Carbohydrate-Active Enzymes from the Filamentous Fungus Scytalidium candidum 3C.\n \n \n \n\n\n \n Pavlov, I. Y.; Eneyskaya, E. V.; Bobrov, K. S.; Polev, D. E.; Ivanen, D. R.; Kopylov, A. T.; Naryzhny, S. N.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Biochemistry. Biokhimiia, 83: 1399–1410. November 2018.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Pavlov2018,\n  author          = {Pavlov, I. Yu and Eneyskaya, E. V. and Bobrov, K. S. and Polev, D. E. and Ivanen, D. R. and Kopylov, A. T. and Naryzhny, S. N. and Kulminskaya, A. A.},\n  journal         = {Biochemistry. Biokhimiia},\n  title           = {Comprehensive Analysis of Carbohydrate-Active Enzymes from the Filamentous Fungus Scytalidium candidum 3C.},\n  year            = {2018},\n  issn            = {1608-3040},\n  month           = nov,\n  pages           = {1399--1410},\n  volume          = {83},\n  abstract        = {Complete enzymatic degradation of plant polysaccharides is a result of combined action of various carbohydrate-active enzymes (CAZymes). In this paper, we demonstrate the potential of the filamentous fungus Scytalidium candidum 3C for processing of plant biomass. Structural annotation of the improved assembly of S. candidum 3C genome and functional annotation of CAZymes revealed putative gene sequences encoding such proteins. A total of 190 CAZyme-encoding genes were identified, including 104 glycoside hydrolases, 52 glycosyltransferases, 28 oxidative enzymes, and 6 carbohydrate esterases. In addition, 14 carbohydrate-binding modules were found. Glycoside hydrolases secreted during the growth of S. candidum 3C in three media were analyzed with a variety of substrates. Mass spectrometry analysis of the fungal culture liquid revealed the presence of peptides identical to 36 glycoside hydrolases, three proteins without known enzymatic function belonging to the same group of families, and 11 oxidative enzymes. The activity of endo-hemicellulases was determined using specially synthesized substrates in which the glycosidic bond between monosaccharide residues was replaced by a thio-linkage. During analysis of the CAZyme profile of S. candidum 3C, four β-xylanases from the GH10 family and two β-glucanases from the GH7 and GH55 families were detected, partially purified, and identified.},\n  chemicals       = {Fungal Proteins, Oxidoreductases},\n  citation-subset = {IM},\n  completed       = {2018-12-11},\n  country         = {United States},\n  doi             = {10.1134/S000629791811010X},\n  issn-linking    = {0006-2979},\n  issue           = {11},\n  keywords        = {Ascomycota, enzymology, genetics; Fungal Proteins, genetics; Genome, Fungal; Oxidoreductases, biosynthesis, genetics},\n  nlm-id          = {0376536},\n  owner           = {NLM},\n  pii             = {BCM83111722},\n  pmid            = {30482151},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2018-12-11},\n}\n\n

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\n \n\n \n \n \n \n \n Scytalidium candidum 3C is a new name for the Geotrichum candidum Link 3C strain.\n \n \n \n\n\n \n Pavlov, I. Y.; Bobrov, K. S.; Sumacheva, A. D.; Masharsky, A. E.; Polev, D. E.; Zhurishkina, E. V.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Journal of basic microbiology, 58: 883–891. October 2018.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Pavlov2018a,\n  author          = {Pavlov, Ivan Yu and Bobrov, Kirill S. and Sumacheva, Anastasiya D. and Masharsky, Alexey E. and Polev, Dmitrii E. and Zhurishkina, Elena V. and Kulminskaya, Anna A.},\n  journal         = {Journal of basic microbiology},\n  title           = {Scytalidium candidum 3C is a new name for the Geotrichum candidum Link 3C strain.},\n  year            = {2018},\n  issn            = {1521-4028},\n  month           = oct,\n  pages           = {883--891},\n  volume          = {58},\n  abstract        = {In the 1970s, the strain Geotrichum candidum Link 3C was isolated from rotting rope and since then has been extensively studied as a source of cellulose and xylan-degrading enzymes. The original identification of the strain was based only on morphological characters of the fungal mycelium in culture. Recent comparison of the internal transcribed spacer (ITS) fragments derived from the draft genome published in 2015 did not show its similarity to G. candidum species. Given the value of the strain 3C in lignocellulosic biomass degradation, we performed morphological and molecular studies to find the appropriate taxonomic placement for this fungal strain within the Ascomycota phylum. ITS, 18S rDNA, 28S rDNA sequences, and RPB2 encoding genes were used to construct phylogenetic trees with Maximum likelihood and Bayesian inference methods. Based on sequence comparison and multiple gene sequencing, we conclude that the fungal strain designated as Geotrichum candidum Link 3C should be placed into the genus Scytalidium (Pezizomycotina, Leotiomycetes) and is redescribed herein as Scytalidium candidum 3C comb. nov.},\n  chemicals       = {DNA, Bacterial, DNA, Ribosomal, RNA Polymerase II},\n  citation-subset = {IM},\n  completed       = {2018-11-20},\n  country         = {Germany},\n  doi             = {10.1002/jobm.201800066},\n  issn-linking    = {0233-111X},\n  issue           = {10},\n  keywords        = {Ascomycota, classification, genetics, growth & development, physiology; Classification; DNA, Bacterial, genetics; DNA, Ribosomal, genetics; Genome, Bacterial, genetics; Hydrogen-Ion Concentration; Mycelium; Phylogeny; RNA Polymerase II, genetics; Sequence Analysis, DNA; Spores, Fungal; Temperature; Geotrichum; Scytalidium; multiple gene sequencing; re-classification},\n  nlm-id          = {8503885},\n  owner           = {NLM},\n  pmid            = {30067294},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2018-11-20},\n}\n\n

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\n \n\n \n \n \n \n \n Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from trichoderma atroviride, T. Reesei and T. Harzianum.\n \n \n \n\n\n \n Borisova, A.\n\n\n \n\n\n\n Biotechnology for Biofuels, 11(1). 2018.\n 23 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85054292210&origin=inward\n\n\n\n
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@Article{Borisova2018,\n  author   = {A.S. Borisova},\n  journal  = {Biotechnology for Biofuels},\n  title    = {Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from trichoderma atroviride, T. Reesei and T. Harzianum},\n  year     = {2018},\n  issn     = {1754-6834},\n  note     = {23 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=85054292210\\&origin=inward},\n  number   = {1},\n  volume   = {11},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/85054292210},\n  doi      = {10.1186/s13068-017-1006-7},\n  type     = {Article},\n}\n\n

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\n \n 2017\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n A comparison of the effect of fucoidan from alga Fucus vesiculosus and its fractions obtained by anion-exchange chromatography on HeLa G-63, Hep G2, and Chang liver cells.\n \n \n \n \n\n\n \n Zhurishkina, E.; Stepanov, S.; Shvetsova, S.; Kulminskaya, A.; and Lapina, I.\n\n\n \n\n\n\n Cell and Tissue Biology, 11(3): 242-249. 2017.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"A$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Zhurishkina2017242,\nauthor={Zhurishkina, E.V. and Stepanov, S.I. and Shvetsova, S.V. and Kulminskaya, A.A. and Lapina, I.M.},\ntitle={A comparison of the effect of fucoidan from alga Fucus vesiculosus and its fractions obtained by anion-exchange chromatography on HeLa G-63, Hep G2, and Chang liver cells},\njournal={Cell and Tissue Biology},\nyear={2017},\nvolume={11},\nnumber={3},\npages={242-249},\ndoi={10.1134/S1990519X17030117},\nnote={cited By 4},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85020387177&doi=10.1134%2fS1990519X17030117&partnerID=40&md5=d27abe92e2332552ac7f56409535a045},\naffiliation={Russian Research Centre Kurchatov Institute, Gatchina, Leningrad oblast  188300, Russian Federation; Department of Medical Physics, Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251, Russian Federation},\nauthor_keywords={fucoidan;  human cell lines;  sulfated polysaccharides},\ncorrespondence_address1={Zhurishkina, E.V.; Russian Research Centre Kurchatov InstituteRussian Federation; email: furfur@yandex.ru},\npublisher={Maik Nauka-Interperiodica Publishing},\nissn={1990519X},\nlanguage={English},\nabbrev_source_title={Cell Tissue Biol.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n Heterologous expression in Pichia pastoris and biochemical characterization of the unmodified sulfatase from Fusarium proliferatum LE1.\n \n \n \n\n\n \n Korban, S. A.; Bobrov, K. S.; Maynskova, M. A.; Naryzhny, S. N.; Vlasova, O. L.; Eneyskaya, E. V.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Protein engineering, design & selection : PEDS, 30: 477–488. July 2017.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Korban2017,\n  author          = {Korban, Svetlana A. and Bobrov, Kirill S. and Maynskova, Maria A. and Naryzhny, Stanislav N. and Vlasova, Olga L. and Eneyskaya, Elena V. and Kulminskaya, Anna A.},\n  journal         = {Protein engineering, design & selection : PEDS},\n  title           = {Heterologous expression in Pichia pastoris and biochemical characterization of the unmodified sulfatase from Fusarium proliferatum LE1.},\n  year            = {2017},\n  issn            = {1741-0134},\n  month           = jul,\n  pages           = {477--488},\n  volume          = {30},\n  abstract        = {Sulfatases are a family of enzymes (sulfuric ester hydrolases, EC 3.1.6.-) that catalyze the hydrolysis of a wide array of sulfate esters. To date, despite the discovery of many sulfatase genes and the accumulation of data on numerous sulfated molecules, the number of characterized enzymes that are key players in sulfur metabolism remains extremely limited. While mammalian sulfatases are well studied due to their involvement in a wide range of normal and pathological biological processes, lower eukaryotic sulfatases, especially fungal sulfatases, have not been thoroughly investigated at the biochemical and structural level. In this paper, we describe the molecular cloning of Fusarium proliferatum sulfatase (F.p.Sulf-6His), its recombinant expression in Pichia pastoris as a soluble and active cytosolic enzyme and its detailed characterization. Gel filtration and native electrophoretic experiments showed that this recombinant enzyme exists as a tetramer in solution. The enzyme is thermo-sensitive, with an optimal temperature of 25°C. The optimal pH value for the hydrolysis of sulfate esters and stability of the enzyme was 6.0. Despite the absence of the post-translational modification of cysteine into Cα-formylglycine, the recombinant F.p.Sulf-6His has remarkably stable catalytic activity against p-nitrophenol sulfate, with kcat = 0.28 s-1 and Km = 2.45 mM, which indicates potential use in the desulfating processes. The currently proposed enzymatic mechanisms of sulfate ester hydrolysis do not explain the appearance of catalytic activity for the unmodified enzyme. According to the available models, the unmodified enzyme is not able to perform multiple catalytic acts; therefore, the enzymatic mechanism of sulfate esters hydrolysis remains to be fully elucidated.},\n  chemicals       = {Sulfatases},\n  citation-subset = {IM},\n  completed       = {2017-10-16},\n  country         = {England},\n  doi             = {10.1093/protein/gzx033},\n  issn-linking    = {1741-0126},\n  issue           = {7},\n  keywords        = {Amino Acid Sequence, genetics; Binding Sites; Cloning, Molecular; Fusarium, enzymology; Gene Expression Regulation, Enzymologic; Pichia, genetics; Protein Processing, Post-Translational, genetics; Protein Structure, Quaternary; Substrate Specificity; Sulfatases, biosynthesis, chemistry, genetics; Fusarium proliferatum; p-nitrophenol sulfate; sulfatase},\n  nlm-id          = {101186484},\n  owner           = {NLM},\n  pii             = {3885836},\n  pmid            = {28651356},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2018-09-06},\n}\n\n

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\n \n\n \n \n \n \n \n Characterization of a new α-l-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-l-fucosidic linkage in the hydrolysis of α-l-fucobiosides.\n \n \n \n\n\n \n Shvetsova, S. V.; Shabalin, K. A.; Bobrov, K. S.; Ivanen, D. R.; Ustyuzhanina, N. E.; Krylov, V. B.; Nifantiev, N. E.; Naryzhny, S. N.; Zgoda, V. G.; Eneyskaya, E. V.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Biochimie, 132: 54–65. January 2017.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Shvetsova2017,\n  author          = {Shvetsova, Svetlana V. and Shabalin, Konstantin A. and Bobrov, Kirill S. and Ivanen, Dina R. and Ustyuzhanina, Nadezhda E. and Krylov, Vadim B. and Nifantiev, Nikolay E. and Naryzhny, Stanislav N. and Zgoda, Victor G. and Eneyskaya, Elena V. and Kulminskaya, Anna A.},\n  journal         = {Biochimie},\n  title           = {Characterization of a new α-l-fucosidase isolated from Fusarium proliferatum LE1 that is regioselective to α-(1 → 4)-l-fucosidic linkage in the hydrolysis of α-l-fucobiosides.},\n  year            = {2017},\n  issn            = {1638-6183},\n  month           = jan,\n  pages           = {54--65},\n  volume          = {132},\n  abstract        = {Here, we report the biochemical characterization of a novel α-l-fucosidase with broad substrate specificity (FpFucA) isolated from the mycelial fungus Fusarium proliferatum LE1. Highly purified α-l-fucosidase was obtained from several chromatographic steps after growth in the presence of l-fucose. The purified α-l-fucosidase appeared to be a monomeric protein of 67 ± 1 kDa that was able to hydrolyze the synthetic substrate p-nitrophenyl α-l-fucopyranoside (pNPFuc), with K (m) = 1.1 ± 0.1 mM and k (cat) = 39.8 ± 1.8 s (-1). l-fucose, 1-deoxyfuconojirimycin and tris(hydroxymethyl)aminomethane inhibited pNPFuc hydrolysis, with inhibition constants of 0.2 ± 0.05 mM, 7.1 ± 0.05 nM, and 12.2 ± 0.1 mM, respectively. We assumed that the enzyme belongs to subfamily A of the GH29 family (CAZy database) based on its ability to hydrolyze practically all fucose-containing oligosaccharides used in the study and the phylogenetic analysis. We found that this enzyme was a unique α-l-fucosidase that preferentially hydrolyzes the α-(1 → 4)-L-fucosidic linkage present in α-L-fucobiosides with different types of linkages. As a retaining glycosidase, FpFucA is capable of catalyzing the transglycosylation reaction with alcohols (methanol, ethanol, and 1-propanol) and pNP-containing monosaccharides as acceptors. These features make the enzyme an important tool that can be used in the various modifications of valuable fucose-containing compounds.},\n  chemicals       = {Alcohols, Disaccharides, Fungal Proteins, Glycosides, Oligosaccharides, Polysaccharides, fucopyranosyl-1-3-fucopyranose, Fucose, fucoidan, alpha-L-Fucosidase},\n  citation-subset = {IM},\n  completed       = {2017-01-30},\n  country         = {France},\n  doi             = {10.1016/j.biochi.2016.10.014},\n  issn-linking    = {0300-9084},\n  keywords        = {Alcohols, metabolism; Amino Acid Sequence; Disaccharides, metabolism; Fucose, metabolism; Fungal Proteins, genetics, isolation & purification, metabolism; Fusarium, enzymology, genetics; Glycosides, metabolism; Glycosylation; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Mass Spectrometry; Oligosaccharides, metabolism; Polysaccharides, metabolism; Stereoisomerism; Substrate Specificity; Temperature; alpha-L-Fucosidase, genetics, isolation & purification, metabolism; Fusarium proliferatum; Translycosylation; α-(1 → 4)-l-fucosidic linkage; α-l-fucobiosides; α-l-fucosidase},\n  nlm-id          = {1264604},\n  owner           = {NLM},\n  pii             = {S0300-9084(16)30302-9},\n  pmid            = {27984201},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2017-11-16},\n}\n\n

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\n \n 2016\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.\n \n \n \n \n\n\n \n Zhemkov, V.; Kulminskaya, A.; Bezprozvanny, I.; and Kim, M.\n\n\n \n\n\n\n FEBS Open Bio, 6(3): 168-178. 2016.\n cited By 9\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Zhemkov2016168,\nauthor={Zhemkov, V.A. and Kulminskaya, A.A. and Bezprozvanny, I.B. and Kim, M.},\ntitle={The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3},\njournal={FEBS Open Bio},\nyear={2016},\nvolume={6},\nnumber={3},\npages={168-178},\ndoi={10.1002/2211-5463.12029},\nnote={cited By 9},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84975760011&doi=10.1002%2f2211-5463.12029&partnerID=40&md5=20145a54e32e78938457758cf8de8577},\naffiliation={Laboratory of Molecular Neurodegeneration, St Petersburg State Polytechnical University, Russian Federation; Laboratory of Enzymology, National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Russian Federation; Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, United States},\nauthor_keywords={Ataxia;  Ataxins;  Huntington's disease;  Polyglutamine;  Triplet repeat disorder},\nkeywords={ataxin 3;  glutamine;  maltose binding protein;  polyglutamine, alpha helix;  Article;  carboxy terminal sequence;  conformation;  crystal structure;  hydrogen bond;  pathogenesis;  priority journal;  protein secondary structure},\nchemicals_cas={glutamine, 56-85-9, 6899-04-3; polyglutamine, 26700-71-0, 69864-43-3},\ncorrespondence_address1={Kim, M.; Department of Physiology, United States; email: Meewhi.Kim@UTSouthwestern.edu},\npublisher={Elsevier B.V.},\nissn={22115463},\nlanguage={English},\nabbrev_source_title={FEBS Open Bio.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n 2015\n \n \n (8)\n \n \n

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\n \n\n \n \n \n \n \n \n Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C.\n \n \n \n \n\n\n \n Borisova, A.; Eneyskaya, E.; Bobrov, K.; Jana, S.; Logachev, A.; Polev, D.; Lapidus, A.; Ibatullin, F.; Saleem, U.; Sandgren, M.; Payne, C.; Kulminskaya, A.; and Stahlberg, J.\n\n\n \n\n\n\n FEBS Journal, 282(23): 4515-4537. October 2015.\n cited By 21\n\n\n\n
\n\n\n\n \n \n $\"Sequencing,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n \n \n 3 downloads\n \n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Borisova20154515,\n  author                  = {Borisova, A.S. and Eneyskaya, E.V. and Bobrov, K.S. and Jana, S. and Logachev, A. and Polev, D.E. and Lapidus, A.L. and Ibatullin, F.M. and Saleem, U. and Sandgren, M. and Payne, C.M. and Kulminskaya, A.A. and Stahlberg, J.},\n  journal                 = {FEBS Journal},\n  title                   = {Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C},\n  year                    = {2015},\n  issn                    = {1742464X},\n  month                   = oct,\n  note                    = {cited By 21},\n  number                  = {23},\n  pages                   = {4515-4537},\n  volume                  = {282},\n  abbrev_source_title     = {FEBS J.},\n  affiliation             = {Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, PO Box 7015, Uppsala, SE-750 07, Sweden; National Research Centre Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova roscha, 188300, Russian Federation; Department of Chemical and Materials Engineering, University of Kentucky, 177 F. Paul Anderson Tower, Lexington, KY 40506, United States; Theodosius Dobzhansky Center for Genome Bioinformatics, St. Petersburg State University, Russian Federation; Research Resource Centre Molecular and Cell Technologies, St. Petersburg State University, Russian Federation; Centre for Algorithmic Biotechnology, St. Petersburg Academic University, Russian Federation; Department of Medical Physics, Peter the Great St. Petersburg Polytechnic University, Russian Federation; Umair Saleem, Birkedommervej 17 3TH, København NV, 2400, Denmark},\n  author_keywords         = {biomass degradation; cellulase; Geotrichum candidum; molecular dynamics; X-ray structure},\n  chemicals_cas           = {cellulose 1,4 beta cellobiosidase, 37329-65-0; Cellulose 1,4-beta-Cellobiosidase},\n  coden                   = {FJEOA},\n  correspondence_address1 = {Stahlberg, J.; Department of Chemistry and Biotechnology, PO Box 7015, Sweden; email: Jerry.Stahlberg@slu.se},\n  document_type           = {Article},\n  doi                     = {10.1111/febs.13509},\n  keywords                = {cellulose 1,4 beta cellobiosidase; glycan; oligosaccharide; cellulose 1,4 beta cellobiosidase, Article; comparative study; controlled study; crystal structure; enzyme active site; enzyme activity; enzyme analysis; enzyme conformation; enzyme glycosylation; enzyme kinetics; enzyme specificity; enzyme stability; enzyme structure; enzyme substrate complex; fungal strain; gene sequence; Geotrichum candidum; Hypocrea jecorina; molecular dynamics; nonhuman; nucleotide sequence; nucleotide sequence; pH; priority journal; structure activity relation; temperature dependence; amino acid sequence; chemistry; enzymology; genetics; Geotrichum; kinetics; metabolism; molecular genetics; protein conformation; sequence alignment; temperature, Amino Acid Sequence; Cellulose 1,4-beta-Cellobiosidase; Geotrichum; Hydrogen-Ion Concentration; Kinetics; Molecular Dynamics Simulation; Molecular Sequence Data; Protein Conformation; Sequence Alignment; Temperature},\n  language                = {English},\n  molecular_seqnumbers    = {GENBANK: KJ958925},\n  publisher               = {Blackwell Publishing Ltd},\n  pubmed_id               = {26367132},\n  source                  = {Scopus},\n  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84961331730&doi=10.1111%2ffebs.13509&partnerID=40&md5=b1587711d771fe0a70ea4e28e8780d03},\n}\n\n

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\n \n\n \n \n \n \n \n \n The novel strain Fusarium proliferatum LE1 (RCAM02409) produces α-L-fucosidase and arylsulfatase during the growth on fucoidan.\n \n \n \n \n\n\n \n Shvetsova, S.; Zhurishkina, E.; Bobrov, K.; Ronzhina, N.; Lapina, I.; Ivanen, D.; Gagkaeva, T.; and Kulminskaya, A.\n\n\n \n\n\n\n Journal of Basic Microbiology, 55(4): 471-479. 2015.\n cited By 13\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Shvetsova2015471,\nauthor={Shvetsova, S.V. and Zhurishkina, E.V. and Bobrov, K.S. and Ronzhina, N.L. and Lapina, I.M. and Ivanen, D.R. and Gagkaeva, T.Y. and Kulminskaya, A.A.},\ntitle={The novel strain Fusarium proliferatum LE1 (RCAM02409) produces α-L-fucosidase and arylsulfatase during the growth on fucoidan},\njournal={Journal of Basic Microbiology},\nyear={2015},\nvolume={55},\nnumber={4},\npages={471-479},\ndoi={10.1002/jobm.201400309},\nnote={cited By 13},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964296282&doi=10.1002%2fjobm.201400309&partnerID=40&md5=5abfbe90837307b502556b4393fc9c2e},\naffiliation={National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Russian Federation; St. Petersburg State Polytechnical University, St. Petersburg, Russian Federation; All-Russian Institute of Plant Protection, Russian Academy of Agricultural Sciences, St. Petersburg, Pushkin, Russian Federation},\nauthor_keywords={Arylsulfatase;  Fucoidan;  Fusarium proliferatum;  α-L-Fucosidase},\nkeywords={4-nitrophenyl;  4-nitrophenyl sulfate;  alpha levo fucosidase;  arylsulfatase;  fucoidin;  nitrobenzene derivative;  nitrophenol;  polysaccharide;  ribosome DNA, Fucus;  Fusarium;  growth, development and aging;  isolation and purification;  Laminaria;  metabolism;  sequence analysis, alpha-L-Fucosidase;  Arylsulfatases;  DNA, Ribosomal;  Fucus;  Fusarium;  growth and development;  isolation and purification;  Laminaria;  metabolism;  metabolism;  metabolism;  metabolism;  metabolism;  metabolism;  Nitrobenzenes;  Nitrophenols;  Polysaccharides;  Sequence Analysis, Bacteria (microorganisms);  Fucus vesiculosus;  Fungi;  Fusarium;  Fusarium proliferatum;  Invertebrata;  Laminaria digitata;  Phaeophyceae},\nchemicals_cas={alpha levo fucosidase, 9037-65-4; arylsulfatase, 9016-17-5; fucoidin, 9072-19-9; nitrophenol, 25154-55-6; 4-nitrophenyl; 4-nitrophenyl sulfate; alpha-L-Fucosidase; Arylsulfatases; DNA, Ribosomal; fucoidan; Nitrobenzenes; Nitrophenols; Polysaccharides},\ncorrespondence_address1={Kulminskaya, A.A.; Laboratory of Enzymology, Russian Federation; email: kulm@omrb.pnpi.spb.ru},\npublisher={Wiley-VCH Verlag},\nissn={0233111X},\ncoden={JBMIE},\npubmed_id={25346501},\nlanguage={English},\nabbrev_source_title={J. Basic Microbiol.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Enzymatic degradation of Xylan for production of xylooligosaccharides and xylose.\n \n \n \n \n\n\n \n Volokitina, M.; Bobrov, K.; Kulminskaya, A.; Tennikova, T.; and Vlakh, E.\n\n\n \n\n\n\n Proceedings of the Estonian Academy of Sciences, 64(2014): 106. 2015.\n cited By 0; Conference of 14th Baltic Polymer Symposium 2014, BPS 2014 ; Conference Date: 24 September 2014 Through 26 September 2014; Conference Code:113706\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Volokitina2015106,\nauthor={Volokitina, M. and Bobrov, K. and Kulminskaya, A. and Tennikova, T. and Vlakh, E.},\ntitle={Enzymatic degradation of Xylan for production of xylooligosaccharides and xylose},\njournal={Proceedings of the Estonian Academy of Sciences},\nyear={2015},\nvolume={64},\nnumber={2014},\npages={106},\nnote={cited By 0; Conference of 14th Baltic Polymer Symposium 2014, BPS 2014 ; Conference Date: 24 September 2014 Through 26 September 2014;  Conference Code:113706},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84988979474&partnerID=40&md5=59749aaf4ff7a1b461df0bb2661d05b3},\naffiliation={Faculty of Chemical and Biochemical Technology, Saint-Petersburg State Institute of Technology (Technical Univercity), Moskovsky pr. 26, St. Petersburg, 190013, Russian Federation; Institute of Macromolecular Compounds, Russian Academy of Sciences, Bolshoy pr. 31, St. Petersburg, 199004, Russian Federation; Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Molecular and Radiation Biology Division, Gatchina, 188300, Russian Federation; Institute of Chemistry, Saint-Petersburg State University, Universitetskiy pr. 26, St. Petersburg, Russian Federation},\ncorrespondence_address1={Volokitina, M.; Faculty of Chemical and Biochemical Technology, Moskovsky pr. 26, Russian Federation},\nsponsors={},\npublisher={Estonian Academy Publishers},\nissn={17366046},\nlanguage={English},\nabbrev_source_title={Proc. Est. Acad. Sci.},\ndocument_type={Conference Paper},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β-xylosidase from Aspergillus awamori X-100 and Grindamyl H121 β-xylanase.\n \n \n \n \n\n\n \n Volokitina, M.; Bobrov, K.; Piens, K.; Eneyskaya, E.; Tennikova, T.; Vlakh, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Biotechnology Journal, 10(1): 210-221. 2015.\n cited By 5\n\n\n\n
\n\n\n\n \n \n $\"Xylan$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Volokitina2015210,\nauthor={Volokitina, M.V. and Bobrov, K.S. and Piens, K. and Eneyskaya, E.V. and Tennikova, T.B. and Vlakh, E.G. and Kulminskaya, A.A.},\ntitle={Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β-xylosidase from Aspergillus awamori X-100 and Grindamyl H121 β-xylanase},\njournal={Biotechnology Journal},\nyear={2015},\nvolume={10},\nnumber={1},\npages={210-221},\ndoi={10.1002/biot.201400417},\nnote={cited By 5},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84921527685&doi=10.1002%2fbiot.201400417&partnerID=40&md5=1d1119ed1e45a14decf086be0a4ec5d9},\naffiliation={Russian Academy of Sciences, Institute of Macromolecular Compounds, St. Petersburg, Russian Federation; National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova roscha, Russian Federation; Ghent University, Department of Biochemistry and Microbiology, Ghent, Belgium; Saint-Petersburg State University, Institute of Chemistry, St. Petersburg, Russian Federation; St.Petersburg State Polytechnical University, St. Petersburg, Russian Federation},\nauthor_keywords={Immobilized enzyme reactors;  Macroporous monoliths;  Xylan degradation;  Xylanase;  β-xylosidase},\nkeywords={Aspergillus;  Bioconversion;  Biomolecules;  Biopolymers;  Efficiency;  Enzymes;  Hydrolysis, Immobilized enzyme reactors;  Macroporous monoliths;  Xylan degradations;  Xylanases;  Xylosidase, Bioreactors, xylan;  xylan 1,4 beta xylosidase;  xylan endo 1,3 beta xylosidase;  endo 1,4 beta xylanase;  exo-1,4-beta-D-xylosidase;  fungal protein;  immobilized enzyme;  recombinant protein;  xylan;  xylan 1,4 beta xylosidase, amino acid sequence;  Article;  Aspergillus awamori;  bioreactor;  carbohydrate metabolism;  complex formation;  conformational transition;  enzyme immobilization;  enzyme kinetics;  gene expression;  glycosylation;  high performance liquid chromatography;  hydrolysis;  immobilized enzyme reactor;  molecular weight;  nonhuman;  nucleotide sequence;  online monitoring;  priority journal;  Aspergillus;  bioreactor;  chemistry;  enzymology;  genetics;  metabolism;  Pichia;  porosity, Aspergillus awamori, Aspergillus;  Bioreactors;  Endo-1,4-beta Xylanases;  Enzymes, Immobilized;  Fungal Proteins;  Pichia;  Porosity;  Recombinant Proteins;  Xylans;  Xylosidases},\nmolecular_seqnumbers={GENBANK: EU854433},\nchemicals_cas={xylan, 9014-63-5; xylan 1,4 beta xylosidase, 9025-53-0; xylan endo 1,3 beta xylosidase, 37278-89-0, 9025-55-2; endo 1,4 beta xylanase, 9025-57-4; Endo-1,4-beta Xylanases; Enzymes, Immobilized; exo-1,4-beta-D-xylosidase; Fungal Proteins; Recombinant Proteins; Xylans; Xylosidases},\ncorrespondence_address1={Kulminskaya, A.A.; National Research Center Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics InstituteRussian Federation},\npublisher={Wiley-VCH Verlag},\nissn={18606768},\npubmed_id={25367775},\nlanguage={English},\nabbrev_source_title={Biotechnol. J.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n EFFECT OF FUCOIDANS ISOLATED FROM SEAWEEDS LAMINARIA DIGITATA AND FUCUS VESICULOSUS ON CELL LINES HELA G-63, ECV 304 AND PC 12.\n \n \n \n \n\n\n \n Zhurishkina, E.; Lapina, I.; Ivanen, D.; Stepanov, S.; Shvetsova, S.; Shavarda, A.; Giliano, N.; and Kulminskaya, A.\n\n\n \n\n\n\n Tsitologiia, 57(10): 727-735. 2015.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"EFFECT$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Zhurishkina2015727,\nauthor={Zhurishkina, E.V. and Lapina, I.M. and Ivanen, D.R. and Stepanov, S.I. and Shvetsova, S.V. and Shavarda, A.L. and Giliano, N.Y. and Kulminskaya, A.A.},\ntitle={EFFECT OF FUCOIDANS ISOLATED FROM SEAWEEDS LAMINARIA DIGITATA AND FUCUS VESICULOSUS ON CELL LINES HELA G-63, ECV 304 AND PC 12},\njournal={Tsitologiia},\nyear={2015},\nvolume={57},\nnumber={10},\npages={727-735},\nnote={cited By 2},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964695769&partnerID=40&md5=dc7d1a17857cb900156646bd14df7310},\nkeywords={fucoidin;  polysaccharide, animal;  apoptosis;  cell proliferation;  chemistry;  drug effects;  endothelium cell;  Fucus;  HeLa cell line;  human;  Laminaria;  PC12 cell line;  rat;  seaweed, Animals;  Apoptosis;  Cell Proliferation;  Endothelial Cells;  Fucus;  HeLa Cells;  Humans;  Laminaria;  PC12 Cells;  Polysaccharides;  Rats;  Seaweed},\nchemicals_cas={fucoidin, 9072-19-9; fucoidan; Polysaccharides},\nissn={00413771},\npubmed_id={26863772},\nlanguage={Russian},\nabbrev_source_title={Tsitologiia},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n The method of integrated kinetics and its applicability to the exo-glycosidase-catalyzed hydrolysis of p-nitrophenyl glycosides.\n \n \n \n\n\n \n Borisova, A. S.; Reddy, S. K.; Ivanen, D. R.; Bobrov, K. S.; Eneyskaya, E. V.; Rychkov, G. N.; Sandgren, M.; Stålbrand, H.; Sinnott, M. L.; Kulminskaya, A. A.; and Shabalin, K. A.\n\n\n \n\n\n\n Carbohydrate research, 412: 43–49. August 2015.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Borisova2015,\n  author          = {Borisova, Anna S. and Reddy, Sumitha K. and Ivanen, Dina R. and Bobrov, Kirill S. and Eneyskaya, Elena V. and Rychkov, Georgy N. and Sandgren, Mats and Stålbrand, Henrik and Sinnott, Michael L. and Kulminskaya, Anna A. and Shabalin, Konstantin A.},\n  journal         = {Carbohydrate research},\n  title           = {The method of integrated kinetics and its applicability to the exo-glycosidase-catalyzed hydrolysis of p-nitrophenyl glycosides.},\n  year            = {2015},\n  issn            = {1873-426X},\n  month           = aug,\n  pages           = {43--49},\n  volume          = {412},\n  abstract        = {In the present work we suggest an efficient method, using the whole time course of the reaction, whereby parameters kcat, Km and product KI for the hydrolysis of a p-nitrophenyl glycoside by an exo-acting glycoside hydrolase can be estimated in a single experiment. Its applicability was demonstrated for three retaining exo-glycoside hydrolases, β-xylosidase from Aspergillus awamori, β-galactosidase from Penicillium sp. and α-galactosidase from Thermotoga maritima (TmGalA). During the analysis of the reaction course catalyzed by the TmGalA enzyme we had observed that a non-enzymatic process, mutarotation of the liberated α-d-galactose, affected the reaction significantly.},\n  chemicals       = {Glycosides, Xylosidases, alpha-Galactosidase, beta-Galactosidase, exo-1,4-beta-D-xylosidase, Galactose},\n  citation-subset = {IM},\n  completed       = {2016-05-17},\n  country         = {Netherlands},\n  doi             = {10.1016/j.carres.2015.03.021},\n  issn-linking    = {0008-6215},\n  keywords        = {Aspergillus, chemistry; Galactose, chemistry; Glycosides, chemistry; Hydrolysis; Kinetics; Penicillium, chemistry; Thermotoga maritima, chemistry; Xylosidases, chemistry; alpha-Galactosidase, chemistry; beta-Galactosidase, chemistry; Integrated kinetics; Mutarotation; Retaining glycoside hydrolase},\n  nlm-id          = {0043535},\n  owner           = {NLM},\n  pii             = {S0008-6215(15)00122-6},\n  pmid            = {26005928},\n  publisher       = {Elsevier BV},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2015-07-06},\n}\n\n

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\n \n\n \n \n \n \n \n α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.\n \n \n \n\n\n \n Borisova, A. S.; Ivanen, D. R.; Bobrov, K. S.; Eneyskaya, E. V.; Rychkov, G. N.; Sandgren, M.; Kulminskaya, A. A.; Sinnott, M. L.; and Shabalin, K. A.\n\n\n \n\n\n\n Carbohydrate research, 401: 115–121. January 2015.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Borisova2015a,\n  author          = {Borisova, Anna S. and Ivanen, Dina R. and Bobrov, Kirill S. and Eneyskaya, Elena V. and Rychkov, Georgy N. and Sandgren, Mats and Kulminskaya, Anna A. and Sinnott, Michael L. and Shabalin, Konstantin A.},\n  journal         = {Carbohydrate research},\n  title           = {α-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima.},\n  year            = {2015},\n  issn            = {1873-426X},\n  month           = jan,\n  pages           = {115--121},\n  volume          = {401},\n  abstract        = {Broad regioselectivity of α-galactosidase from Thermotoga maritima (TmGal36A) is a limiting factor for application of the enzyme in the directed synthesis of oligogalactosides. However, this property can be used as a convenient tool in studies of thermodynamics of a glycosidic bond. Here, a novel approach to energy difference estimation is suggested. Both transglycosylation and hydrolysis of three types of galactosidic linkages were investigated using total kinetics of formation and hydrolysis of pNP-galactobiosides catalysed by monomeric glycoside hydrolase family 36 α-galactosidase from T. maritima, a retaining exo-acting glycoside hydrolase. We have estimated transition state free energy differences between the 1,2- and 1,3-linkage (ΔΔG(‡)0 values were equal 5.34 ± 0.85 kJ/mol) and between 1,6-linkage and 1,3-linkage (ΔΔG(‡)0=1.46 ± 0.23 kJ/mol) in pNP-galactobiosides over the course of the reaction catalysed by TmGal36A. Using the free energy difference for formation and hydrolysis of glycosidic linkages (ΔΔG(‡)F-ΔΔG(‡)H), we found that the 1,2-linkage was 2.93 ± 0.47 kJ/mol higher in free energy than the 1,3-linkage, and the 1,6-linkage 4.44 ± 0.71 kJ/mol lower.},\n  chemicals       = {Disaccharides, 6-O-galactopyranosylgalactose, alpha-Galactosidase},\n  citation-subset = {IM},\n  completed       = {2015-09-04},\n  country         = {Netherlands},\n  doi             = {10.1016/j.carres.2014.11.003},\n  issn-linking    = {0008-6215},\n  keywords        = {Biocatalysis; Disaccharides, chemistry, metabolism; Glycosylation; Hydrolysis; Kinetics; Stereoisomerism; Substrate Specificity; Thermotoga maritima, enzymology; alpha-Galactosidase, metabolism; Free energy differences; Kinetics; Regioselectivity; Thermotoga maritima; Transglycosylation; α-Galactosidase},\n  nlm-id          = {0043535},\n  owner           = {NLM},\n  pii             = {S0008-6215(14)00419-4},\n  pmid            = {25486100},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2014-12-29},\n}\n\n

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\n \n\n \n \n \n \n \n Enzymatic degradation of Xylan for production of xylooligosaccharides and xylose.\n \n \n \n\n\n \n Volokitina, M.\n\n\n \n\n\n\n Proceedings of the Estonian Academy of Sciences, 64(2014): 106–106. 2015.\n Query date: 2024-02-01 13:12:36\n\n\n\n
\n\n\n\n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Volokitina2015,\n  author   = {M. Volokitina},\n  journal  = {Proceedings of the Estonian Academy of Sciences},\n  title    = {Enzymatic degradation of Xylan for production of xylooligosaccharides and xylose},\n  year     = {2015},\n  issn     = {1736-6046},\n  note     = {Query date: 2024-02-01 13:12:36},\n  number   = {2014},\n  pages    = {106--106},\n  volume   = {64},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/84988979474},\n  type     = {Conference Paper},\n}\n\n

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\n \n 2014\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Draft genome sequence of Geotrichum candidum strain 3C.\n \n \n \n \n\n\n \n Polev, D.; Bobrov, K.; Eneyskaya, E.; and Kulminskaya, A.\n\n\n \n\n\n\n Genome Announcements, 2(5). 2014.\n cited By 9\n\n\n\n
\n\n\n\n \n \n $\"Draft$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Polev2014,\nauthor={Polev, D.E. and Bobrov, K.S. and Eneyskaya, E.V. and Kulminskaya, A.A.},\ntitle={Draft genome sequence of Geotrichum candidum strain 3C},\njournal={Genome Announcements},\nyear={2014},\nvolume={2},\nnumber={5},\ndoi={10.1128/genomeA.00956-14},\nart_number={e00956-14},\nnote={cited By 9},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85004168771&doi=10.1128%2fgenomeA.00956-14&partnerID=40&md5=67ae8307bc8e28faf9683dec80f2a97f},\naffiliation={Research Resource Center for Molecular and Cell Technologies, St. Petersburg State University, St. Petersburg, Russian Federation; National Research Centre, Kurchatov Institute, B.P. Konstantinov Petersburg Nuclear Physics Institute, Gatchina, Orlova Roscha, Russian Federation; St. Petersburg State Polytechnical University, St. Petersburg, Russian Federation},\nfunding_details={Russian Foundation for Basic ResearchRussian Foundation for Basic Research, РФФИ, 14-08-01041},\ncorrespondence_address1={Polev, D.E.; Research Resource Center for Molecular and Cell Technologies, Russian Federation; email: dmitry.polev@gmail.com},\npublisher={American Society for Microbiology},\nissn={21698287},\nlanguage={English},\nabbrev_source_title={Genome Announce.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Impact of an N-terminal extension on the stability and activity of the GH11 xylanase from Thermobacillus xylanilyticus.\n \n \n \n \n\n\n \n Song, L.\n\n\n \n\n\n\n Journal of Biotechnology, 174(1): 64–72. 2014.\n 15 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=84894326081&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Impact$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Song2014,\n  author   = {L. Song},\n  journal  = {Journal of Biotechnology},\n  title    = {Impact of an N-terminal extension on the stability and activity of the GH11 xylanase from Thermobacillus xylanilyticus},\n  year     = {2014},\n  issn     = {0168-1656},\n  note     = {15 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=84894326081\\&origin=inward},\n  number   = {1},\n  pages    = {64--72},\n  volume   = {174},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/84894326081},\n  doi      = {10.1016/j.jbiotec.2014.01.004},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S0168165614000054},\n}\n\n

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\n \n 2013\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n Improvement of the efficiency of transglycosylation catalyzed by α-galactosidase from Thermotoga maritima by protein engineering.\n \n \n \n\n\n \n Bobrov, K. S.; Borisova, A. S.; Eneyskaya, E. V.; Ivanen, D. R.; Shabalin, K. A.; Kulminskaya, A. A.; and Rychkov, G. N.\n\n\n \n\n\n\n Biochemistry. Biokhimiia, 78: 1112–1123. October 2013.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Bobrov2013,\n  author          = {Bobrov, K. S. and Borisova, A. S. and Eneyskaya, E. V. and Ivanen, D. R. and Shabalin, K. A. and Kulminskaya, A. A. and Rychkov, G. N.},\n  journal         = {Biochemistry. Biokhimiia},\n  title           = {Improvement of the efficiency of transglycosylation catalyzed by α-galactosidase from Thermotoga maritima by protein engineering.},\n  year            = {2013},\n  issn            = {1608-3040},\n  month           = oct,\n  pages           = {1112--1123},\n  volume          = {78},\n  abstract        = {At high concentrations of p-nitrophenyl-α-D-galactopyranoside (pNPGal) as a substrate, its hydrolysis catalyzed by α-galactosidase from Thermotoga maritima (TmGalA) is accompanied by transglycosylation resulting in production of a mixture of (α1,2)-, (α1,3)-, and (α1,6)-p-nitrophenyl (pNP)-digalactosides. Molecular modeling of the reaction stage preceding the formation of the pNP-digalactosides within the active site of the enzyme revealed amino acid residues which modification was expected to increase the efficiency of transglycosylation. Upon the site-directed mutagenesis to the predicted substitutions of the amino acid residues, genes encoding the wild type TmGalA and its mutants were expressed in E. coli, and the corresponding enzymes were isolated and tested for the presence of the transglycosylating activity in synthesis of different pNP-digalactosides. Three mutants, F328A, P402D, and G385L, were shown to markedly increase the total transglycosylation as compared to the wild type enzyme. Moreover, the F328A mutant displayed an ability to produce a regio-isomer with the (α1,2)-bond at yield 16-times higher than the wild type TmGalA.},\n  chemicals       = {Nitrophenylgalactosides, 4-nitrophenylgalactoside, alpha-Galactosidase},\n  citation-subset = {IM},\n  completed       = {2015-01-06},\n  country         = {United States},\n  doi             = {10.1134/S0006297913100052},\n  issn-linking    = {0006-2979},\n  issue           = {10},\n  keywords        = {Biocatalysis; Glycosylation; Hydrolysis; Models, Molecular; Mutation; Nitrophenylgalactosides, metabolism; Protein Engineering; Thermotoga maritima, enzymology, genetics; alpha-Galactosidase, genetics, metabolism},\n  nlm-id          = {0376536},\n  owner           = {NLM},\n  pii             = {BCM78101422},\n  pmid            = {24237145},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2013-11-18},\n}\n\n

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\n \n 2010\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Mutagenesis and subsite mapping underpin the importance for substrate specificity of the aglycon subsites of glycoside hydrolase family 11 xylanases.\n \n \n \n \n\n\n \n Pollet, A.; Lagaert, S.; Eneyskaya, E.; Kulminskaya, A.; Delcour, J.; and Courtin, C.\n\n\n \n\n\n\n Biochimica et Biophysica Acta - Proteins and Proteomics, 1804(4): 977-985. April 2010.\n cited By 29\n\n\n\n
\n\n\n\n \n \n $\"Mutagenesis$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Pollet2010977,\n  author                  = {Pollet, A. and Lagaert, S. and Eneyskaya, E. and Kulminskaya, A. and Delcour, J.A. and Courtin, C.M.},\n  journal                 = {Biochimica et Biophysica Acta - Proteins and Proteomics},\n  title                   = {Mutagenesis and subsite mapping underpin the importance for substrate specificity of the aglycon subsites of glycoside hydrolase family 11 xylanases},\n  year                    = {2010},\n  issn                    = {15709639},\n  month                   = apr,\n  note                    = {cited By 29},\n  number                  = {4},\n  pages                   = {977-985},\n  volume                  = {1804},\n  abbrev_source_title     = {Biochim. Biophys. Acta Proteins Proteomics},\n  affiliation             = {Laboratory of Food Chemistry and Biochemistry, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20 - bus 2463, B-3001 Leuven, Belgium; Leuven Food Science and Nutrition Research Centre (LFoRCe), Katholieke Universiteit Leuven, Kasteelpark Arenberg 20 - bus 2463, B-3001 Leuven, Belgium; Division of Gene Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21 - bus 2462, B-3001 Leuven, Belgium; Petersburg Nuclear Physics Institute, Molecular and Radiation Biophysics Department, Russian Academy of Sciences, Gatchina, St. Petersburg, 188350, Russian Federation},\n  author_keywords         = {Active site amino acids; Glycoside hydrolase family 11; Site-directed mutagenesis; Subsite mapping; Substrate specificity; Xylanase},\n  chemicals_cas           = {amino acid, 65072-01-7; glycosidase, 9032-92-2; xylan endo 1,3 beta xylosidase, 37278-89-0, 9025-55-2; Bacterial Proteins; Endo-1,4-beta Xylanases, 3.2.1.8; Mutant Proteins; Oligosaccharides; Recombinant Proteins; Xylans},\n  coden                   = {BBAPB},\n  correspondence_address1 = {Courtin, C.M.; Laboratory of Food Chemistry and Biochemistry, Kasteelpark Arenberg 20 - bus 2463, B-3001 Leuven, Belgium; email: christophe.courtin@biw.kuleuven.be},\n  document_type           = {Article},\n  doi                     = {10.1016/j.bbapap.2010.01.009},\n  keywords                = {aglycone; amino acid; glycosidase; oligosaccharide; xylan endo 1,3 beta xylosidase, article; Bacillus subtilis; enzyme activity; enzyme binding; enzyme specificity; hydrolysis; nonhuman; priority journal; protein interaction; site directed mutagenesis; structure analysis; wild type, Amino Acid Substitution; Bacillus subtilis; Bacterial Proteins; Catalytic Domain; Endo-1,4-beta Xylanases; Hydrolysis; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Oligosaccharides; Protein Engineering; Recombinant Proteins; Substrate Specificity; Thermodynamics; Xylans, Bacillus subtilis},\n  language                = {English},\n  publisher               = {Elsevier BV},\n  pubmed_id               = {20096384},\n  source                  = {Scopus},\n  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-76849112864&doi=10.1016%2fj.bbapap.2010.01.009&partnerID=40&md5=7522ad706478d3e045dbee2d1fa16f94},\n}\n\n

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\n \n\n \n \n \n \n \n \n Catalytic mechanism of human α-galactosidase.\n \n \n \n \n\n\n \n Guce, A.; Clark, N.; Salgado, E.; Ivanen, D.; Kulminskaya, A.; Brumer III, H.; and Garman, S.\n\n\n \n\n\n\n Journal of Biological Chemistry, 285(6): 3625-3632. February 2010.\n cited By 82\n\n\n\n
\n\n\n\n \n \n $\"Catalytic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@Article{Guce20103625,\n  author                  = {Guce, A.I. and Clark, N.E. and Salgado, E.N. and Ivanen, D.R. and Kulminskaya, A.A. and Brumer III, H. and Garman, S.C.},\n  journal                 = {Journal of Biological Chemistry},\n  title                   = {Catalytic mechanism of human α-galactosidase},\n  year                    = {2010},\n  issn                    = {00219258},\n  month                   = feb,\n  note                    = {cited By 82},\n  number                  = {6},\n  pages                   = {3625-3632},\n  volume                  = {285},\n  abbrev_source_title     = {J. Biol. Chem.},\n  affiliation             = {Dept. of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant St., Amherst, MA, United States; Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States; Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Leningrad District, Orlova Roscha, Gatchina 188300, Russian Federation; Department of Biotechnology, Royal Insitute of Technology (KTH), 10691 Stockholm, Sweden},\n  chemicals_cas           = {alpha galactosidase, 9025-35-8; glycosidase, 9032-92-2; Ligands; alpha-Galactosidase, 3.2.1.22},\n  coden                   = {JBCHA},\n  correspondence_address1 = {Garman, S. C.; Dept. of Biochemistry and Molecular Biology, 710 North Pleasant St., Amherst, MA, United States; email: garman@biochem.umass.edu},\n  document_type           = {Article},\n  doi                     = {10.1074/jbc.M109.060145},\n  funding_details         = {National Institute of Diabetes and Digestive and Kidney DiseasesNational Institute of Diabetes and Digestive and Kidney Diseases, NIDDK, R01DK076877},\n  keywords                = {Boat conformations; Catalytic cycles; Catalytic mechanisms; Clinical research; Clinical trial; Displacement reactions; Drug Design; Fabry disease; Galactopyranoside; Galactosidases; Glycoside hydrolases; High-resolution structures; Lysosomal storage disorder; Reaction cycles; Recombinant enzymes; Second ligand; X ray crystal structures, Binding energy; Conformations; Ligands; Substitution reactions; Sugars, Enzymes, alpha galactosidase; glycosidase; ligand, animal cell; article; catalysis; conformational transition; controlled study; enzyme active site; enzyme kinetics; enzyme structure; Fabry disease; human; ligand binding; nonhuman; priority journal; animal; binding site; catalysis; cell line; chemical structure; chemistry; enzyme specificity; enzymology; genetics; metabolism; mutation; pathology; protein binding; protein conformation; protein tertiary structure; X ray crystallography, alpha-Galactosidase; Animals; Binding Sites; Catalysis; Catalytic Domain; Cell Line; Crystallography, X-Ray; Fabry Disease; Humans; Ligands; Models, Molecular; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Substrate Specificity},\n  language                = {English},\n  publisher               = {Elsevier BV},\n  pubmed_id               = {19940122},\n  source                  = {Scopus},\n  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-77950511400&doi=10.1074%2fjbc.M109.060145&partnerID=40&md5=d7be48e5b0e0006198e363b1127b3879},\n}\n\n

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\n \n 2009\n \n \n (2)\n \n \n

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\n \n \n

\n \n\n \n \n \n \n \n Transglycosylating and hydrolytic activities of the beta-mannosidase from Trichoderma reesei.\n \n \n \n\n\n \n Eneyskaya, E. V.; Sundqvist, G.; Golubev, A. M.; Ibatullin, F. M.; Ivanen, D. R.; Shabalin, K. A.; Brumer, H.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Biochimie, 91: 632–638. May 2009.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@Article{Eneyskaya2009,\n  author          = {Eneyskaya, Elena V. and Sundqvist, Gustav and Golubev, Alexander M. and Ibatullin, Farid M. and Ivanen, Dina R. and Shabalin, Konstantin A. and Brumer, Harry and Kulminskaya, Anna A.},\n  journal         = {Biochimie},\n  title           = {Transglycosylating and hydrolytic activities of the beta-mannosidase from Trichoderma reesei.},\n  year            = {2009},\n  issn            = {1638-6183},\n  month           = may,\n  pages           = {632--638},\n  volume          = {91},\n  abstract        = {A purified beta-mannosidase (EC 3.2.1.25) from the fungus Trichoderma reesei has been identified as a member of glycoside hydrolase family 2 through mass spectrometry analysis of tryptic peptides. In addition to hydrolysis, the enzyme catalyzes substrate transglycosylation with p-nitrophenyl beta-mannopyranoside. Structures of the major and minor products of this reaction were identified by NMR analysis as p-nitrophenyl mannobiosides and p-nitrophenyl mannotriosides containing beta-(1-->4) and beta-(1-->3) linkages. The rate of donor substrate hydrolysis increased in presence of acetonitrile and dimethylformamide, while transglycosylation was weakly suppressed by these organic solvents. Differential ultraviolet spectra of the protein indicate that a rearrangement of the hydrophobic environment of the active site following the addition of the organic solvents may be responsible for this hydrolytic activation.},\n  chemicals       = {Fungal Proteins, Solvents, beta-Mannosidase, Trypsin},\n  citation-subset = {IM},\n  completed       = {2009-06-25},\n  country         = {France},\n  doi             = {10.1016/j.biochi.2009.03.009},\n  issn-linking    = {0300-9084},\n  issue           = {5},\n  keywords        = {Chromatography, High Pressure Liquid; Fungal Proteins, metabolism; Glycosylation; Hydrogen-Ion Concentration; Hydrolysis; Magnetic Resonance Spectroscopy; Mass Spectrometry; Protein Structure, Secondary; Solvents; Trichoderma, enzymology; Trypsin, metabolism; beta-Mannosidase, chemistry, metabolism},\n  nlm-id          = {1264604},\n  owner           = {NLM},\n  pii             = {S0300-9084(09)00070-4},\n  pmid            = {19327384},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2009-04-14},\n}\n\n

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\n \n\n \n \n \n \n \n Novel precipitated fluorescent substrates for the screening of cellulolytic microorganisms.\n \n \n \n\n\n \n Ivanen, D. R.; Rongjina, N. L.; Shishlyannikov, S. M.; Litviakova, G. I.; Isaeva-Ivanova, L. S.; Shabalin, K. A.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Journal of microbiological methods, 76: 295–300. March 2009.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Ivanen2009,\n  author          = {Ivanen, Dina R. and Rongjina, Natalia L. and Shishlyannikov, Sergey M. and Litviakova, Galina I. and Isaeva-Ivanova, Luidmila S. and Shabalin, Konstantin A. and Kulminskaya, Anna A.},\n  journal         = {Journal of microbiological methods},\n  title           = {Novel precipitated fluorescent substrates for the screening of cellulolytic microorganisms.},\n  year            = {2009},\n  issn            = {0167-7012},\n  month           = mar,\n  pages           = {295--300},\n  volume          = {76},\n  abstract        = {New substrates, 2-(2'-benzothiazolyl)-phenyl (BTP) cellooligosaccharides with degree of polymerization (d.p.) 2-4 (BTPG(2-4)) were synthesized for the screening of microbial cellulolytic activity in plate assays. The substrates were very efficient that was shown for several cellulolytic bacteria, including yeast-like isolates from Kamchatka hot springs. Three tested bacterial strains and eighteen of 30 of the yeast isolates showed ability to degrade cellulose with cellobiohydrolase, beta-glucosidase and endo-cellulase activities measured with standard substrates. The structures of 2-(2'-benzothiazolyl)-phenyl oligosaccharides were solved by NMR- and mass-spectrometry. The usefulness of the 2-(2'-benzothiazolyl)-phenyl substrates were also shown during purification of the B. polymyxa cellulolytic complex, which consists of at least three types of the enzymes: cellobiohydrolase, endo-beta-d-glucanase and beta-glucosidase.},\n  chemicals       = {Benzothiazoles, Fluorescent Dyes, Oligosaccharides, Cellulose, Cellulases, beta-Glucosidase, Cellulose 1,4-beta-Cellobiosidase},\n  citation-subset = {IM},\n  completed       = {2009-04-13},\n  country         = {Netherlands},\n  doi             = {10.1016/j.mimet.2008.12.008},\n  issn-linking    = {0167-7012},\n  issue           = {3},\n  keywords        = {Bacteria, enzymology, isolation & purification; Benzothiazoles, chemistry; Cellulases, metabolism; Cellulose, metabolism; Cellulose 1,4-beta-Cellobiosidase, metabolism; Fluorescent Dyes, chemical synthesis, chemistry; Oligosaccharides, chemistry; Substrate Specificity; Yeasts, enzymology, isolation & purification; beta-Glucosidase, metabolism},\n  nlm-id          = {8306883},\n  owner           = {NLM},\n  pii             = {S0167-7012(08)00441-7},\n  pmid            = {19150471},\n  pubmodel        = {Print-Electronic},\n  pubstate        = {ppublish},\n  revised         = {2009-02-23},\n}\n\n

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\n \n 2008\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Crystallization and preliminary crystallographic analysis of laminarinase from Rhodothermus marinus: A case of pseudomerohedral twinning.\n \n \n \n \n\n\n \n Golubev, A.; Rojas, A.; Nascimento, A.; Bleicher, L.; Kulminskaya, A.; Eneyskaya, E.; and Polikarpov, I.\n\n\n \n\n\n\n Protein and Peptide Letters, 15(10): 1142-1144. 2008.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Crystallization$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Golubev20081142,\nauthor={Golubev, A.M. and Rojas, A.L. and Nascimento, A.S. and Bleicher, L. and Kulminskaya, A.A. and Eneyskaya, E.V. and Polikarpov, I.},\ntitle={Crystallization and preliminary crystallographic analysis of laminarinase from Rhodothermus marinus: A case of pseudomerohedral twinning},\njournal={Protein and Peptide Letters},\nyear={2008},\nvolume={15},\nnumber={10},\npages={1142-1144},\ndoi={10.2174/092986608786071139},\nnote={cited By 1},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-54249097528&doi=10.2174%2f092986608786071139&partnerID=40&md5=ed7b68584148c82d770a92eb81124ed8},\naffiliation={Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, 188300, Russian Federation; Instituto de Física de São Carlos, Universidade de São Paulo, Av Trabalhador Saocarlense 400, CEP 13560-970, São Carlos, SP, Brazil; National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, United States},\nauthor_keywords={Crystallization;  Laminarinase;  Pseudomerohedral twinning;  Rhodothermus marinus},\nkeywords={endo 1,3(4) beta glucanase, article;  chemistry;  crystallization;  enzymology;  genetics;  glycosylation;  metabolism;  mutation;  Rhodothermus;  X ray crystallography, Crystallization;  Crystallography, X-Ray;  Endo-1,3(4)-beta-Glucanase;  Glycosylation;  Mutation;  Rhodothermus, Rhodothermus;  Rhodothermus marinus},\nchemicals_cas={endo 1,3(4) beta glucanase, 62213-14-3; Endo-1,3(4)-beta-Glucanase, EC 3.2.1.6},\ncorrespondence_address1={Polikarpov, I.; Instituto de Física de São Carlos, Av Trabalhador Saocarlense 400, CEP 13560-970, São Carlos, SP, Brazil; email: ipolikarpov@if.sc.usp.br},\nissn={09298665},\ncoden={PPELE},\npubmed_id={19075828},\nlanguage={English},\nabbrev_source_title={Protein Pept. Lett.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Enzymatic hydrolysis of 1,3-1,4-β-glucosyl oligosaccharides by 1,3-1,4-β-glucanase from Synechocystis PCC6803: A comparison with assays using polymer and chromophoric oligosaccharide substrates.\n \n \n \n \n\n\n \n Fukamizo, T.\n\n\n \n\n\n\n Archives of Biochemistry and Biophysics, 478(2): 187–194. October 2008.\n 9 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=52249117218&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Fukamizo2008,\n  author    = {T. Fukamizo},\n  journal   = {Archives of Biochemistry and Biophysics},\n  title     = {Enzymatic hydrolysis of 1,3-1,4-β-glucosyl oligosaccharides by 1,3-1,4-β-glucanase from Synechocystis PCC6803: A comparison with assays using polymer and chromophoric oligosaccharide substrates},\n  year      = {2008},\n  issn      = {0003-9861},\n  month     = oct,\n  note      = {9 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=52249117218\\&origin=inward},\n  number    = {2},\n  pages     = {187--194},\n  volume    = {478},\n  citation  = {https://api.elsevier.com/content/abstract/scopus_id/52249117218},\n  doi       = {10.1016/j.abb.2008.07.019},\n  publisher = {Elsevier BV},\n  type      = {Article},\n  url       = {https://api.elsevier.com/content/article/eid/1-s2.0-S0003986108003512},\n}\n

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\n \n 2007\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases.\n \n \n \n \n\n\n \n Comfort, D.; Bobrov, K.; Ivanen, D.; Shabalin, K.; Harris, J.; Kulminskaya, A.; Brumer, H.; and Kelly, R.\n\n\n \n\n\n\n Biochemistry, 46(11): 3319-3330. 2007.\n cited By 72\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@ARTICLE{Comfort20073319,\nauthor={Comfort, D.A. and Bobrov, K.S. and Ivanen, D.R. and Shabalin, K.A. and Harris, J.M. and Kulminskaya, A.A. and Brumer, H. and Kelly, R.M.},\ntitle={Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases},\njournal={Biochemistry},\nyear={2007},\nvolume={46},\nnumber={11},\npages={3319-3330},\ndoi={10.1021/bi061521n},\nnote={cited By 72},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-33947433621&doi=10.1021%2fbi061521n&partnerID=40&md5=0052f204a32353c216bae321a8599fe1},\naffiliation={Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St. Petersburg 188300, Russian Federation; School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, Stockholm, Sweden},\nkeywords={Anomeric stereochemistry;  Glycoside hydrolase (GH);  Mechanistic commonality, Addition reactions;  Biochemistry;  Catalyst activity;  Mutagens;  pH effects;  Stereochemistry, Enzymes, 4 nitrophenylgalactoside;  alpha galactopyranoside;  alpha galactosidase;  aspartic acid;  azide;  glucopyranoside;  glycine;  glycosidase;  mutant protein;  pyranoside;  unclassified drug, amino acid substitution;  article;  catalysis;  controlled study;  enzyme activity;  enzyme analysis;  enzyme kinetics;  enzyme mechanism;  enzyme structure;  hydrolysis;  nonhuman;  pH;  priority journal;  protein family;  site directed mutagenesis;  stereochemistry;  Thermotoga maritima, alpha-Galactosidase;  Amino Acid Sequence;  Azides;  Catalysis;  Cloning, Molecular;  Heat;  Hydrogen-Ion Concentration;  Kinetics;  Models, Molecular;  Molecular Sequence Data;  Mutagenesis, Site-Directed;  Protein Denaturation;  Sequence Alignment;  Substrate Specificity;  Thermotoga maritima, Thermotoga maritima},\nchemicals_cas={4 nitrophenylgalactoside, 3150-24-1; alpha galactosidase, 9023-01-2; aspartic acid, 56-84-8, 6899-03-2; azide, 12596-60-0, 14343-69-2; glycine, 56-40-6, 6000-43-7, 6000-44-8; glycosidase, 9032-92-2; Azides; alpha-Galactosidase, 3.2.1.22},\ncorrespondence_address1={Kelly, R.M.; Department of Chemical and Biomolecular Engineering, , Raleigh, NC 27695-7905, United States; email: rmkelly@eos.ncsu.edu},\nissn={00062960},\ncoden={BICHA},\npubmed_id={17323919},\nlanguage={English},\nabbrev_source_title={Biochemistry},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Biochemical and kinetic analysis of the GH3 family β-xylosidase from Aspergillus awamori X-100.\n \n \n \n \n\n\n \n Eneyskaya, E.\n\n\n \n\n\n\n Archives of Biochemistry and Biophysics, 457(2): 225–234. 2007.\n 37 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=33846088514&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Eneyskaya2007,\n  author   = {E.V. Eneyskaya},\n  journal  = {Archives of Biochemistry and Biophysics},\n  title    = {Biochemical and kinetic analysis of the GH3 family β-xylosidase from Aspergillus awamori X-100},\n  year     = {2007},\n  issn     = {0003-9861},\n  note     = {37 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=33846088514\\&origin=inward},\n  number   = {2},\n  pages    = {225--234},\n  volume   = {457},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/33846088514},\n  doi      = {10.1016/j.abb.2006.10.024},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S0003986106004103},\n}\n\n

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\n \n 2006\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n Human milk antibodies with polysaccharide kinase activity.\n \n \n \n\n\n \n Karataeva, N. A.; Gorbunov, D.; Prokudin, I. V.; Buneva, V. N.; Kulminskaya, A. A.; Neustroev, K. N.; and Nevinsky, G. A.\n\n\n \n\n\n\n Immunology Letters, 103(1): 58-67. February 2006.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Karataeva2006,\n  author    = {Natal’ya A. Karataeva and Dmitry Gorbunov and Ivan V. Prokudin and Valentina N. Buneva and Anna A. Kulminskaya and Kirill N. Neustroev and Georgy A. Nevinsky},\n  journal   = {Immunology Letters},\n  title     = {Human milk antibodies with polysaccharide kinase activity},\n  year      = {2006},\n  issn      = {0165-2478},\n  month     = feb,\n  number    = {1},\n  pages     = {58-67},\n  volume    = {103},\n  doi       = {10.1016/j.imlet.2005.10.009},\n  publisher = {Elsevier BV},\n}\n\n

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\n \n\n \n \n \n \n \n Transferase and hydrolytic activities of the laminarinase from Rhodothermus marinus and its M133A, M133C, and M133W mutants.\n \n \n \n\n\n \n Neustroev, K. N.; Golubev, A. M.; Sinnott, M. L.; Borriss, R.; Krah, M.; Brumer, H.; Eneyskaya, E. V.; Shishlyannikov, S.; Shabalin, K. A.; Peshechonov, V. T.; Korolev, V. G.; and Kulminskaya, A. A.\n\n\n \n\n\n\n Glycoconjugate journal, 23: 501–511. November 2006.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Neustroev2006,\n  author          = {Neustroev, Kirill N. and Golubev, Alexander M. and Sinnott, Michael L. and Borriss, Rainer and Krah, Martin and Brumer, Harry and Eneyskaya, Elena V. and Shishlyannikov, Sergey and Shabalin, Konstantin A. and Peshechonov, Viacheslav T. and Korolev, Vladimir G. and Kulminskaya, Anna A.},\n  journal         = {Glycoconjugate journal},\n  title           = {Transferase and hydrolytic activities of the laminarinase from Rhodothermus marinus and its M133A, M133C, and M133W mutants.},\n  year            = {2006},\n  issn            = {0282-0080},\n  month           = nov,\n  pages           = {501--511},\n  volume          = {23},\n  abstract        = {Comparative studies of the transglycosylation and hydrolytic activities have been performed on the Rhodothermus marinus beta-1,3-glucanase (laminarinase) and its M133A, M133C, and M133W mutants. The M133C mutant demonstrated near 20% greater rate of transglycosylation activity in comparison with the M133A and M133W mutants that was measured by NMR quantitation of nascent beta(1-4) and beta(1-6) linkages. To obtain kinetic probes for the wild-type enzyme and Met-133 mutants, p-nitrophenyl beta-laminarin oligosaccharides of degree of polymerisation 2-8 were synthesized enzymatically. Catalytic efficiency values, k (cat)/K (m), of the laminarinase catalysed hydrolysis of these oligosaccharides suggested possibility of four negative and at least three positive binding subsites in the active site. Comparison of action patterns of the wild-type and M133C mutant in the hydrolysis of the p-nitrophenyl-beta-D-oligosac- charides indicated that the increased transglycosylation activity of the M133C mutant did not result from altered subsite affinities. The stereospecificity of the transglycosylation reaction also was unchanged in all mutants; the major transglycosylation products in hydrolysis of p-nitrophenyl laminaribioside were beta-glucopyranosyl-beta-1,3-D-glucopy- ranosyl-beta-1,3-D-glucopyranose and beta-glucopyranosyl-beta-1, 3-D-glucopyranosyl-beta-1,3-D-glucpyranosyl-beta-1,3-D- glucopyranoxside.},\n  chemicals       = {Glucans, Polysaccharides, laminaran, Cellulases},\n  citation-subset = {IM},\n  completed       = {2007-04-11},\n  country         = {United States},\n  doi             = {10.1007/s10719-006-6733-0},\n  issn-linking    = {0282-0080},\n  issue           = {7-8},\n  keywords        = {Amino Acid Sequence; Amino Acid Substitution; Carbohydrate Sequence; Catalytic Domain, genetics; Cellulases, genetics, metabolism; Glucans; Glycosylation; Hydrolysis; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Mutation; Polysaccharides, chemistry; Rhodothermus, enzymology, genetics; Sequence Homology, Amino Acid; Substrate Specificity; Tandem Mass Spectrometry},\n  nlm-id          = {8603310},\n  owner           = {NLM},\n  pmid            = {17006642},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2022-07-16},\n}\n\n

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\n \n 2005\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Structural insights into the β-xylosidase from Trichoderma reesei obtained by synchrotron small-angle x-ray scattering and circular dichroism spectroscopy.\n \n \n \n \n\n\n \n Rojas, A.; Fischer, H.; Eneiskaya, E.; Kulminskaya, A.; Shabalin, K.; Neustroev, K.; Craievich, A.; Golubev, A.; and Polikarpov, I.\n\n\n \n\n\n\n Biochemistry, 44(47): 15578-15584. 2005.\n cited By 9\n\n\n\n
\n\n\n\n \n \n $\"Structural$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Rojas200515578,\nauthor={Rojas, A.L. and Fischer, H. and Eneiskaya, E.V. and Kulminskaya, A.A. and Shabalin, K.A. and Neustroev, K.N. and Craievich, A.F. and Golubev, A.M. and Polikarpov, I.},\ntitle={Structural insights into the β-xylosidase from Trichoderma reesei obtained by synchrotron small-angle x-ray scattering and circular dichroism spectroscopy},\njournal={Biochemistry},\nyear={2005},\nvolume={44},\nnumber={47},\npages={15578-15584},\ndoi={10.1021/bi050826j},\nnote={cited By 9},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-28244477099&doi=10.1021%2fbi050826j&partnerID=40&md5=a4b10b3dd7e1cbc9cc39cc98e1f48297},\naffiliation={Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador Sao-carlense 400, CEP 13560-970, São Carlos, SP, Brazil; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, 188300, Russian Federation; Instituto de Física, Universidade de São Paulo, São Paulo, SP, Brazil},\nkeywords={Alcohols;  Algorithms;  Monomers;  Solutions;  Spectroscopy;  X ray scattering, Arabinofuranoside;  Circular dichroism spectroscopy;  Distinct structural modules;  Hexosaminidase;  Low-resolution molecular envelope, Enzymes, 1,4 beta xylooligosaccharide;  4 nitrophenylarabinofuranoside;  alpha arabinofuranosidase;  beta glucan hydrolase;  beta n acetylhexosaminidase;  glycosidase;  glycosyl hydrolase 3;  monomer;  oligosaccharide;  unclassified drug;  xylan 1,4 beta xylosidase, ab initio calculation;  algorithm;  amino acid sequence;  animal cell;  article;  circular dichroism;  computer prediction;  controlled study;  enzyme analysis;  enzyme structure;  molecular recognition;  nonhuman;  priority journal;  protein conformation;  protein domain;  protein secondary structure;  simulation;  structure analysis;  synchrotron;  Trichoderma reesei;  Vibrio cholerae;  X ray crystallography, Algorithms;  Circular Dichroism;  Models, Molecular;  Protein Conformation;  Protein Structure, Secondary;  Scattering, Radiation;  Solutions;  Trichoderma;  X-Rays;  Xylosidases, Animalia;  Hordeum vulgare subsp. vulgare;  Hypocrea jecorina;  Vibrio cholerae},\nchemicals_cas={alpha arabinofuranosidase, 9067-74-7; beta n acetylhexosaminidase, 37211-57-7, 9027-52-5; glycosidase, 9032-92-2; xylan 1,4 beta xylosidase, 9025-53-0; exo-1,4-beta-D-xylosidase, EC 3.2.1.37; Solutions; Xylosidases, EC 3.2.1.-},\ncorrespondence_address1={Polikarpov, I.; Instituto de Física de São Carlos, Av. Trabalhador Sao-carlense 400, CEP 13560-970, São Carlos, SP, Brazil; email: ipolikarpov@if.sc.usp.br},\nissn={00062960},\ncoden={BICHA},\npubmed_id={16300407},\nlanguage={English},\nabbrev_source_title={Biochemistry},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Chemo-enzymatic synthesis of 4-methylumbelliferyl β-(1→4)-D-xylooligosides: New substrates for β-D-xylanase assays.\n \n \n \n \n\n\n \n Eneyskaya, E.; Ivanen, D.; Shabalin, K.; Kulminskaya, A.; Backinowsky, L.; Brumer III, H.; and Neustroev, K.\n\n\n \n\n\n\n Organic and Biomolecular Chemistry, 3(1): 146-151. 2005.\n cited By 22\n\n\n\n
\n\n\n\n \n \n $\"Chemo-enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Eneyskaya2005146,\nauthor={Eneyskaya, E.V. and Ivanen, D.R. and Shabalin, K.A. and Kulminskaya, A.A. and Backinowsky, L.V. and Brumer III, H. and Neustroev, K.N.},\ntitle={Chemo-enzymatic synthesis of 4-methylumbelliferyl β-(1→4)-D-xylooligosides: New substrates for β-D-xylanase assays},\njournal={Organic and Biomolecular Chemistry},\nyear={2005},\nvolume={3},\nnumber={1},\npages={146-151},\ndoi={10.1039/b409583a},\nnote={cited By 22},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-11844304068&doi=10.1039%2fb409583a&partnerID=40&md5=03142869ce72c091ef461d3d8b59f0b9},\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molec. and Radiat. Biology Division, Gatchina, 188300, Russian Federation; N.D.Zelinsky Inst. of Organ. Chem., Russian Academy of Sciences, Leninsky prosp. 47, Moscow, 119991, Russian Federation; Department of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, S-106 91, Stockholm, Sweden},\nkeywords={Carbohydrates;  Catalysis;  Enzymes;  Hydrolysis;  Reaction kinetics;  Substrates;  Synthesis (chemical), Chemo-enzymatic synthesis;  Glycosides;  Kinetic properties;  Polymeric substrates, Glucose, carbon;  exo 1,4 beta D xylosidase;  exo-1,4-beta-D-xylosidase;  oligosaccharide;  proton;  xylan 1,4 beta xylosidase, article;  Aspergillus;  carbohydrate analysis;  catalysis;  chemical structure;  chemistry;  electrospray mass spectrometry;  enzymology;  glycosylation;  methodology;  molecular genetics;  nuclear magnetic resonance spectroscopy;  sensitivity and specificity;  synthesis;  Trichoderma, Aspergillus;  Carbohydrate Sequence;  Carbon Isotopes;  Catalysis;  Glycosylation;  Magnetic Resonance Spectroscopy;  Molecular Sequence Data;  Molecular Structure;  Oligosaccharides;  Protons;  Sensitivity and Specificity;  Spectrometry, Mass, Electrospray Ionization;  Trichoderma;  Xylosidases, Aspergillus orizae;  Aspergillus sp.;  Hypocrea jecorina;  Trichoderma},\nchemicals_cas={carbon, 7440-44-0; proton, 12408-02-5, 12586-59-3; xylan 1,4 beta xylosidase, 9025-53-0; Carbon Isotopes; exo-1,4-beta-D-xylosidase, EC 3.2.1.37; Oligosaccharides; Protons; Xylosidases, EC 3.2.1.-},\ncorrespondence_address1={Kulminskaya, A.A.; Petersburg Nuclear Physics Institute, , Gatchina, 188300, Russian Federation; email: kulm@omrb.pnpi.spb.ru},\nissn={14770520},\npubmed_id={15602610},\nlanguage={English},\nabbrev_source_title={Org. Biomol. Chem.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Synthesis of arabinitol 1-phosphate and its use for characterization of arabinitol-phosphate dehydrogenase.\n \n \n \n \n\n\n \n Soroka, N.\n\n\n \n\n\n\n Carbohydrate Research, 340(4): 539–546. 2005.\n 3 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=13844318805&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Synthesis$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Soroka2005,\n  author   = {N.V. Soroka},\n  journal  = {Carbohydrate Research},\n  title    = {Synthesis of arabinitol 1-phosphate and its use for characterization of arabinitol-phosphate dehydrogenase},\n  year     = {2005},\n  issn     = {0008-6215},\n  note     = {3 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=13844318805\\&origin=inward},\n  number   = {4},\n  pages    = {539--546},\n  volume   = {340},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/13844318805},\n  doi      = {10.1016/j.carres.2004.11.030},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S0008621504005439},\n}\n\n

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\n \n 2004\n \n \n (5)\n \n \n

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\n \n\n \n \n \n \n \n \n Crystal structure of exo-inulinase from Aspergillus awamori: The enzyme fold and structural determinants of substrate recognition.\n \n \n \n \n\n\n \n Nagem, R.; Rojas, A.; Golubev, A.; Korneeva, O.; Eneyskaya, E.; Kulminskaya, A.; Neustroev, K.; and Polikarpov, I.\n\n\n \n\n\n\n Journal of Molecular Biology, 344(2): 471-480. November 2004.\n cited By 130\n\n\n\n
\n\n\n\n \n \n $\"Crystal$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Nagem2004471,\n  author               = {Nagem, R.A.P. and Rojas, A.L. and Golubev, A.M. and Korneeva, O.S. and Eneyskaya, E.V. and Kulminskaya, A.A. and Neustroev, K.N. and Polikarpov, I.},\n  journal              = {Journal of Molecular Biology},\n  title                = {Crystal structure of exo-inulinase from Aspergillus awamori: The enzyme fold and structural determinants of substrate recognition},\n  year                 = {2004},\n  issn                 = {00222836},\n  month                = nov,\n  note                 = {cited By 130},\n  number               = {2},\n  pages                = {471-480},\n  volume               = {344},\n  abbrev_source_title  = {J. Mol. Biol.},\n  affiliation          = {Inst. de Fís. de S. Carlos, Universidade de São Paulo, Av. Trabalhador S.-carlense 400, C., Brazil; Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188300, Russia, Russian Federation; Voronezh State Technological Academy, Pr. Revolutsii 19, Voronezh, 394017, Russia, Russian Federation},\n  author_keywords      = {Aspergillus awamori; crystallographic structure; exo-inulinase; glycoside hydrolase; X-ray structure},\n  chemicals_cas        = {arginine, 1119-34-2, 15595-35-4, 7004-12-8, 74-79-3; aspartic acid, 56-84-8, 6899-03-2; beta fructofuranosidase, 9001-57-4; fructose, 30237-26-4, 57-48-7, 7660-25-5, 77907-44-9; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; glycosidase, 9032-92-2; inulinase, 9025-67-6; proline, 147-85-3, 7005-20-1},\n  coden                = {JMOBA},\n  document_type        = {Article},\n  doi                  = {10.1016/j.jmb.2004.09.024},\n  keywords             = {acid; arginine; asparagine linked oligosaccharide; aspartic acid; base; beta fructofuranosidase; enzyme; fructose; glutamic acid; glycoprotein; glycosidase; inulinase; proline, amino acid substitution; amino terminal sequence; article; Aspergillus awamori; atom; catalysis; controlled study; crystal structure; crystallization; enzyme structure; hydrogen bond; molecular recognition; nonhuman; nucleotide sequence; priority journal; protein domain; protein family; protein folding; protein glycosylation; protein motif; Thermotoga maritima; X ray; X ray crystallography, Aspergillus; Aspergillus awamori; Thermotoga; Thermotoga maritima},\n  language             = {English},\n  molecular_seqnumbers = {GENBANK: AAD36485, AAF16405, CAA04131, CAA07345, CAC44220},\n  publisher            = {Academic Press},\n  pubmed_id            = {15522299},\n  source               = {Scopus},\n  url                  = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-7444232112&doi=10.1016%2fj.jmb.2004.09.024&partnerID=40&md5=492321cd11eb0b00716a957cf862d721},\n}\n\n

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\n \n\n \n \n \n \n \n \n Catalytic properties of IgMs with amylolytic activity isolated from patients with multiple sclerosis.\n \n \n \n \n\n\n \n Ivanen, D.; Kulminskaya, A.; Shabalin, K.; Isaeva-Ivanova, L.; Ershova, N.; Saveliev, A.; Nevinsky, G.; and Neustroev, K.\n\n\n \n\n\n\n Medical Science Monitor, 10(8): BR273-BR280. 2004.\n cited By 16\n\n\n\n
\n\n\n\n \n \n $\"Catalytic$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Ivanen2004,\nauthor={Ivanen, D.R. and Kulminskaya, A.A. and Shabalin, K.A. and Isaeva-Ivanova, L.V. and Ershova, N.A. and Saveliev, A.N. and Nevinsky, G.A. and Neustroev, K.N.},\ntitle={Catalytic properties of IgMs with amylolytic activity isolated from patients with multiple sclerosis},\njournal={Medical Science Monitor},\nyear={2004},\nvolume={10},\nnumber={8},\npages={BR273-BR280},\nnote={cited By 16},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-4444373080&partnerID=40&md5=f7cf0fbd8ee67057a1c7571eec95efd2},\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation; Novosibirsk Inst. of Bioorg. Chem., Siberian Div. Russ. Acad. Sci., Novosibirsk, Russian Federation; Biophysics Department, St. Petersburg Technical University, St. Petersburg, Russian Federation},\nauthor_keywords={Abzymes;  Amylolytic activity;  IgM;  Multiple sclerosis},\nkeywords={alpha glucosidase;  amylase;  glucoside;  immunoglobulin M;  oligosaccharide, adult;  article;  carbon nuclear magnetic resonance;  catalysis;  enzyme activity;  female;  human;  hydrolysis;  major clinical study;  male;  Michaelis constant;  multiple sclerosis;  polyacrylamide gel electrophoresis;  polymerization;  proton nuclear magnetic resonance;  reversed phase high performance liquid chromatography;  thin layer chromatography, Adult;  Amylases;  Antibodies, Catalytic;  Chromatography, High Pressure Liquid;  Female;  Humans;  Immunoglobulin M;  Male;  Middle Aged;  Multiple Sclerosis;  Nitrobenzenes;  Oligosaccharides},\nchemicals_cas={alpha glucosidase, 9001-42-7; amylase, 9000-90-2, 9000-92-4, 9001-19-8; glucoside, 50986-29-3; immunoglobulin M, 9007-85-6; 4-nitrophenyl maltopentaoside, 66068-38-0; Amylases, 3.2.1.-; Antibodies, Catalytic; Immunoglobulin M; Nitrobenzenes; Oligosaccharides},\ncorrespondence_address1={Ivanen, D.R.; Molec. and Radiat. Biophys. Division, , Gatchina, Russian Federation},\nissn={12341010},\ncoden={MSMOF},\npubmed_id={15277988},\nlanguage={English},\nabbrev_source_title={Med. Sci. Monit.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Human abzymes with amylolytic activity.\n \n \n \n \n\n\n \n Kulminskaya, A.; Saveliev, A.; and Neustroev, K.\n\n\n \n\n\n\n Trends in Glycoscience and Glycotechnology, 16(87): 17-31. 2004.\n cited By 12\n\n\n\n
\n\n\n\n \n \n $\"Human$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Kulminskaya200417,\nauthor={Kulminskaya, A.A. and Saveliev, A.N. and Neustroev, K.N.},\ntitle={Human abzymes with amylolytic activity},\njournal={Trends in Glycoscience and Glycotechnology},\nyear={2004},\nvolume={16},\nnumber={87},\npages={17-31},\ndoi={10.4052/tigg.16.17},\nnote={cited By 12},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-1942454781&doi=10.4052%2ftigg.16.17&partnerID=40&md5=a1f5d60fa308f499596c135dbbb0648e},\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation; Biophysics Department, St.-Petersburg Technical University, St. Petersburg, Russian Federation; Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg, 188300, Russian Federation; St. Petersburg Technol. Institute, Russian Federation; Petersburg Nuclear Physics Institute, Russian Federation; Laboratory of Enzymology; Biophysics Department, St. Petersburg Polytech. University, Russian Federation; Leningrad Nuclear Physics Institute, Russian Federation},\nauthor_keywords={Abzymes;  Amylolytic activity;  Autoimmune pothotogies},\nkeywords={amylase;  glucopyranoside;  glucose;  glycogen;  immunoglobulin;  immunoglobulin A;  immunoglobulin G;  oligosaccharide;  starch, autoimmune disease;  catalysis;  catalyst;  enzyme activity;  enzyme degradation;  enzyme substrate;  fluorescence;  human;  hydrolysis;  Michaelis constant;  milk;  multiple sclerosis;  short survey;  systemic lupus erythematosus},\nchemicals_cas={amylase, 9000-90-2, 9000-92-4, 9001-19-8; glucose, 50-99-7, 84778-64-3; glycogen, 9005-79-2; immunoglobulin, 9007-83-4; immunoglobulin G, 97794-27-9; starch, 9005-25-8, 9005-84-9},\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, , Gatchina, St. Petersburg, 188300, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\npublisher={Gakushin Publishing Company},\nissn={09157352},\nlanguage={English; Japanese},\nabbrev_source_title={Trends Glycosci. Glycotechnol.},\ndocument_type={Short Survey},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose.\n \n \n \n\n\n \n Rojas, A. L.; Nagem, R. A. P.; Neustroev, K. N.; Arand, M.; Adamska, M.; Eneyskaya, E. V.; Kulminskaya, A. A.; Garratt, R. C.; Golubev, A. M.; and Polikarpov, I.\n\n\n \n\n\n\n Journal of molecular biology, 343: 1281–1292. November 2004.\n \n\n\n\n
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@Article{Rojas2004,\n  author          = {Rojas, A. L. and Nagem, R. A. P. and Neustroev, K. N. and Arand, M. and Adamska, M. and Eneyskaya, E. V. and Kulminskaya, A. A. and Garratt, R. C. and Golubev, A. M. and Polikarpov, I.},\n  journal         = {Journal of molecular biology},\n  title           = {Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose.},\n  year            = {2004},\n  issn            = {0022-2836},\n  month           = nov,\n  pages           = {1281--1292},\n  volume          = {343},\n  abstract        = {Beta-galactosidases catalyze the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and transglycosylation. Here we report the crystallographic structures of Penicillium sp. beta-galactosidase and its complex with galactose solved by the SIRAS quick cryo-soaking technique at 1.90 A and 2.10 A resolution, respectively. The amino acid sequence of this 120 kDa protein was first assigned putatively on the basis of inspection of the experimental electron density maps and then determined by nucleotide sequence analysis. Primary structure alignments reveal that Penicillium sp. beta-galactosidase belongs to family 35 of glycosyl hydrolases (GHF-35). This model is the first 3D structure for a member of GHF-35. Five distinct domains which comprise the structure are assembled in a way previously unobserved for beta-galactosidases. Superposition of this complex with other beta-galactosidase complexes from several hydrolase families allowed the identification of residue Glu200 as the proton donor and residue Glu299 as the nucleophile involved in catalysis. Penicillium sp. beta-galactosidase is a glycoprotein containing seven N-linked oligosaccharide chains and is the only structure of a glycosylated beta-galactosidase described to date.},\n  chemicals       = {beta-Galactosidase, Galactose},\n  citation-subset = {IM},\n  completed       = {2004-12-14},\n  country         = {Netherlands},\n  doi             = {10.1016/j.jmb.2004.09.012},\n  issn-linking    = {0022-2836},\n  issue           = {5},\n  keywords        = {Amino Acid Sequence; Binding Sites; Carbohydrate Metabolism; Crystallography, X-Ray; Galactose, chemistry, metabolism; Glycosylation; Molecular Sequence Data; Penicillium, enzymology, metabolism; Protein Structure, Tertiary; Sequence Analysis, Protein; beta-Galactosidase, chemistry, metabolism},\n  nlm-id          = {2985088R},\n  owner           = {NLM},\n  pii             = {S0022-2836(04)01141-6},\n  pmid            = {15491613},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2013-11-21},\n}\n\n

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\n \n\n \n \n \n \n \n Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.\n \n \n \n\n\n \n Golubev, A. M.; Nagem, R. A. P.; Brandão Neto, J. R.; Neustroev, K. N.; Eneyskaya, E. V.; Kulminskaya, A. A.; Shabalin, K. A.; Savel'ev, A. N.; and Polikarpov, I.\n\n\n \n\n\n\n Journal of molecular biology, 339: 413–422. May 2004.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Golubev2004,\n  author          = {Golubev, A. M. and Nagem, R. A. P. and Brandão Neto, J. R. and Neustroev, K. N. and Eneyskaya, E. V. and Kulminskaya, A. A. and Shabalin, K. A. and Savel'ev, A. N. and Polikarpov, I.},\n  journal         = {Journal of molecular biology},\n  title           = {Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.},\n  year            = {2004},\n  issn            = {0022-2836},\n  month           = may,\n  pages           = {413--422},\n  volume          = {339},\n  abstract        = {The crystal structures of alpha-galactosidase from the mesophilic fungus Trichoderma reesei and its complex with the competitive inhibitor, beta-d-galactose, have been determined at 1.54 A and 2.0 A resolution, respectively. The alpha-galactosidase structure was solved by the quick cryo-soaking method using a single Cs derivative. The refined crystallographic model of the alpha-galactosidase consists of two domains, an N-terminal catalytic domain of the (beta/alpha)8 barrel topology and a C-terminal domain which is formed by an antiparallel beta-structure. The protein contains four N-glycosylation sites located in the catalytic domain. Some of the oligosaccharides were found to participate in inter-domain contacts. The galactose molecule binds to the active site pocket located in the center of the barrel of the catalytic domain. Analysis of the alpha-galactosidase- galactose complex reveals the residues of the active site and offers a structural basis for identification of the putative mechanism of the enzymatic reaction. The structure of the alpha-galactosidase closely resembles those of the glycoside hydrolase family 27. The conservation of two catalytic Asp residues, identified for this family, is consistent with a double-displacement reaction mechanism for the alpha-galactosidase. Modeling of possible substrates into the active site reveals specific hydrogen bonds and hydrophobic interactions that could explain peculiarities of the enzyme kinetics.},\n  chemicals       = {alpha-Galactosidase, Galactose},\n  citation-subset = {IM},\n  completed       = {2004-07-13},\n  country         = {Netherlands},\n  doi             = {10.1016/j.jmb.2004.03.062},\n  issn-linking    = {0022-2836},\n  issue           = {2},\n  keywords        = {Binding Sites; Catalysis; Crystallography, X-Ray; Galactose, metabolism; Models, Molecular; Protein Conformation; Trichoderma, enzymology; alpha-Galactosidase, chemistry, metabolism},\n  nlm-id          = {2985088R},\n  owner           = {NLM},\n  pii             = {S002228360400378X},\n  pmid            = {15136043},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2013-11-21},\n}\n\n

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\n \n 2003\n \n \n (4)\n \n \n

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\n \n\n \n \n \n \n \n \n Multiple enzymic activities of human milk lactoferrin.\n \n \n \n \n\n\n \n Kanyshkova, T.; Babina, S.; Semenov, D.; Isaeva, N.; Vlassov, A.; Neustroev, K.; Kul'minskaya, A.; Buneva, V.; and Nevinsky, G.\n\n\n \n\n\n\n European Journal of Biochemistry, 270(16): 3353-3361. July 2003.\n cited By 63\n\n\n\n
\n\n\n\n \n \n $\"Multiple$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Kanyshkova20033353,\n  author                  = {Kanyshkova, T.G. and Babina, S.E. and Semenov, D.V. and Isaeva, N. and Vlassov, A.V. and Neustroev, K.N. and Kul'minskaya, A.A. and Buneva, V.N. and Nevinsky, G.A.},\n  journal                 = {European Journal of Biochemistry},\n  title                   = {Multiple enzymic activities of human milk lactoferrin},\n  year                    = {2003},\n  issn                    = {00142956},\n  month                   = jul,\n  note                    = {cited By 63},\n  number                  = {16},\n  pages                   = {3353-3361},\n  volume                  = {270},\n  abbrev_source_title     = {Eur. J. Biochem.},\n  affiliation             = {Novosibirsk Inst. of Bioorg. Chem., Siberian Div. of Russ. Acad. of Sci., Novosibirsk, Russian Federation; Novosibirsk State University, Novosibirsk, Russian Federation; Institute of Cytology and Genetics, Siberian Div. Russ. Acad. of Sci., Novosibirsk, Russian Federation; Petersburg Nucl. Phys. Inst. R., St Peterburg, Russian Federation; Laboratory of Repair Enzymes, Novosibirsk Inst. of Bioorg. Chem., 8, Lavrentieva Ave., 630090, Novosibirsk, Russian Federation},\n  author_keywords         = {Enzymic activities; Human milk; Lactoferrin; Protection},\n  chemicals_cas           = {adenosine triphosphatase, 37289-25-1, 9000-83-3; deoxyribonuclease, 37211-67-9; lactoferrin, 55599-62-7; phosphatase, 9013-05-2; ribonuclease, 59794-03-5, 9001-99-4; Adenosine Triphosphatases, EC 3.6.1.-; Deoxyribonucleases, EC 3.1.-; Lactoferrin; Oligosaccharides; Phosphoric Monoester Hydrolases, EC 3.1.3.-; Ribonucleases, EC 3.1.-},\n  coden                   = {EJBCA},\n  correspondence_address1 = {Nevinsky, G.A.; Laboratory of Repair Enzymes, 8, Lavrentieva Ave., 630090, Novosibirsk, Russian Federation; email: nevinsky@niboch.nsc.ru},\n  document_type           = {Article},\n  doi                     = {10.1046/j.1432-1033.2003.03715.x},\n  keywords                = {adenosine triphosphatase; deoxyribonuclease; iron binding protein; lactoferrin; oligosaccharide; phosphatase; ribonuclease, apoptosis; article; breast milk; cell growth; cytotoxicity; DNA binding; enzyme activity; host resistance; human; hydrolysis; immunomodulation; lipid peroxidation; microbial immunity; priority journal; protection; protein function; protein purification; transcription initiation; virus infection, Adenosine Triphosphatases; Deoxyribonucleases; Female; Humans; Lactoferrin; Milk, Human; Oligosaccharides; Phosphoric Monoester Hydrolases; Ribonucleases; Substrate Specificity},\n  language                = {English},\n  publisher               = {Wiley},\n  pubmed_id               = {12899692},\n  source                  = {Scopus},\n  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042928467&doi=10.1046%2fj.1432-1033.2003.03715.x&partnerID=40&md5=f17181fc4f39dda0aab4846a7354d100},\n}\n\n

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\n \n\n \n \n \n \n \n \n Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase.\n \n \n \n \n\n\n \n Povelainen, M.; Eneyskaya, E.; Kulminskaya, A.; Ivanen, D.; Kalkkinen, N.; Neustroev, K.; and Miasnikov, A.\n\n\n \n\n\n\n Biochemical Journal, 371(1): 191-197. 2003.\n cited By 13\n\n\n\n
\n\n\n\n \n \n $\"Biochemical$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Povelainen2003191,\nauthor={Povelainen, M. and Eneyskaya, E.V. and Kulminskaya, A.A. and Ivanen, D.R. and Kalkkinen, N. and Neustroev, K.N. and Miasnikov, A.N.},\ntitle={Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase},\njournal={Biochemical Journal},\nyear={2003},\nvolume={371},\nnumber={1},\npages={191-197},\ndoi={10.1042/BJ20021096},\nnote={cited By 13},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242286156&doi=10.1042%2fBJ20021096&partnerID=40&md5=df69825a9a36085bf9b1f3869e73e4b1},\naffiliation={Danisco Cultor Innovation, Sokeritehtaantie 20, Kantvik 02460, Finland; Petersburg Nuclear Physics Institute, Gatchina, Leningrad District 188300, Russian Federation; Institute of Biotechnology, University of Helsinki, Viikinkaari 9, Helsinki 00014, Finland},\nauthor_keywords={Enterococcus avium;  NADH-dependent dehydrogenase;  Pentitol phosphate metabolism;  Xylulose 5-phosphate},\nkeywords={DNA;  Enzymes;  Genetic engineering;  Proteins, Molecular mass, Biochemistry, arabinitol;  dextro arabitol phosphate dehydrogenase;  manganese;  nicotinamide adenine dinucleotide;  nicotinamide adenine dinucleotide phosphate;  oxidoreductase;  phosphotransferase;  ribitol;  unclassified drug;  xylitol;  xylulose;  zinc;  aldehyde reductase;  arabitol 5 phosphate;  arabitol-5-phosphate;  bacterial protein;  metal;  nicotinamide adenine dinucleotide;  nicotinamide adenine dinucleotide phosphate;  pentose phosphate;  recombinant protein;  sugar phosphate;  xylulose 5 phosphate;  xylulose-5-phosphate, amino acid sequence;  article;  biochemistry;  catabolism;  cell lysate;  DNA sequence;  Enterococcus avium;  enzyme metabolism;  enzyme purification;  enzyme specificity;  genetics;  Gram positive bacterium;  molecular weight;  nonhuman;  operon;  oxidation;  priority journal;  sequence homology;  chemistry;  Enterococcus;  enzymology;  isolation and purification;  kinetics;  metabolism;  methodology;  molecular genetics;  nucleotide sequence;  oxidation reduction reaction;  sequence analysis, Bacteria (microorganisms);  Enterococcus avium;  Posibacteria;  Prokaryota, Amino Acid Sequence;  Bacterial Proteins;  Base Sequence;  Biochemistry;  Enterococcus;  Kinetics;  Metals;  Molecular Sequence Data;  NAD;  NADP;  Oxidation-Reduction;  Pentosephosphates;  Recombinant Proteins;  Sequence Analysis;  Substrate Specificity;  Sugar Alcohol Dehydrogenases;  Sugar Phosphates},\nmolecular_seqnumbers={GENBANK: AY078980},\nchemicals_cas={arabinitol, 2152-56-9; manganese, 16397-91-4, 7439-96-5; nicotinamide adenine dinucleotide phosphate, 53-59-8; nicotinamide adenine dinucleotide, 53-84-9; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; phosphotransferase, 9031-09-8, 9031-44-1; ribitol, 488-81-3; xylitol, 87-99-0; xylulose, 551-84-8, 5962-29-8; zinc, 7440-66-6; aldehyde reductase, 58591-34-7, 9023-11-4, 9028-31-3; pentose phosphate, 27710-24-3; xylulose 5 phosphate, 4212-65-1; arabitol-5-phosphate; Bacterial Proteins; Metals; NAD, 53-84-9; NADP, 53-59-8; Pentosephosphates; Recombinant Proteins; Sugar Alcohol Dehydrogenases, EC 1.1.-; Sugar Phosphates; xylulose-5-phosphate, 60802-29-1},\ncorrespondence_address1={Miasnikov, A.N.; Danisco Cultor Innovation, Sokeritehtaantie 20, Kantvik 02460, Finland; email: andrei.miasnikov@danisco.com},\nissn={02646021},\ncoden={BIJOA},\npubmed_id={12467497},\nlanguage={English},\nabbrev_source_title={Biochem. J.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis.\n \n \n \n\n\n \n Saveliev, A. N.; Ivanen, D. R.; Kulminskaya, A. A.; Ershova, N. A.; Kanyshkova, T. G.; Buneva, V. N.; Mogelnitskii, A. S.; Doronin, B. M.; Favorova, O. O.; Nevinsky, G. A.; and Neustroev, K. N.\n\n\n \n\n\n\n Immunology letters, 86: 291–297. May 2003.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@Article{Saveliev2003,\n  author          = {Saveliev, Andrew N. and Ivanen, Dina R. and Kulminskaya, Anna A. and Ershova, Nadezhda A. and Kanyshkova, Tat'yana G. and Buneva, Valentina N. and Mogelnitskii, Alexander S. and Doronin, Boris M. and Favorova, Olga O. and Nevinsky, Georgy A. and Neustroev, Kirill N.},\n  journal         = {Immunology letters},\n  title           = {Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis.},\n  year            = {2003},\n  issn            = {0165-2478},\n  month           = may,\n  pages           = {291--297},\n  volume          = {86},\n  abstract        = {IgG and IgM antibodies from the sera of patients with multiple sclerosis (MS) were found to possess amylolytic activity hydrolyzing alpha-(1-->4)-glucosyl linkages of maltooligosaccharides, glycogen, and several artificial substrates. Individual IgM fractions isolated from 54 analyzed patients with the clinically definite diagnoses of MS had approximately three orders of magnitude higher specific amylolytic activity than that for healthy donors, whereas IgG from only a few patients had high amylolytic activity. Strict criteria were used to prove that the amylolytic activity of IgMs and IgGs is their intrinsic property and is not due to any enzyme contamination. Fab fragments produced from IgM and IgG fractions of the MS patients displayed the same amylolytic activity. IgMs from various patients demonstrated different modes of action in hydrolyzing maltooligosaccharides.},\n  chemicals       = {Antibodies, Catalytic, Immunoglobulin G, Immunoglobulin M, Oligosaccharides, maltooligosaccharides, Amylases},\n  citation-subset = {IM},\n  completed       = {2003-12-24},\n  country         = {Netherlands},\n  doi             = {10.1016/s0165-2478(03)00042-7},\n  issn-linking    = {0165-2478},\n  issue           = {3},\n  keywords        = {Adult; Amylases, metabolism; Antibodies, Catalytic, blood, chemistry, metabolism; Electrophoresis, Polyacrylamide Gel; Female; Humans; Hydrolysis; Immunoglobulin G, blood, chemistry, metabolism; Immunoglobulin M, blood, chemistry, metabolism; Male; Middle Aged; Multiple Sclerosis, blood, enzymology, immunology; Oligosaccharides, metabolism},\n  nlm-id          = {7910006},\n  owner           = {NLM},\n  pii             = {S0165247803000427},\n  pmid            = {12706534},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2019-08-26},\n}\n\n

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\n \n\n \n \n \n \n \n \n Enzymatic synthesis of β-xylanase substrates: Transglycosylation reactions of the β-xylosidase from Aspergillus sp.\n \n \n \n \n\n\n \n Eneyskaya, E.\n\n\n \n\n\n\n Carbohydrate Research, 338(4): 313–325. 2003.\n 62 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0347895063&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@Article{Eneyskaya2003,\n  author   = {E.V. Eneyskaya},\n  journal  = {Carbohydrate Research},\n  title    = {Enzymatic synthesis of β-xylanase substrates: Transglycosylation reactions of the β-xylosidase from Aspergillus sp.},\n  year     = {2003},\n  issn     = {0008-6215},\n  note     = {62 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=0347895063\\&origin=inward},\n  number   = {4},\n  pages    = {313--325},\n  volume   = {338},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/0347895063},\n  doi      = {10.1016/S0008-6215(02)00467-6},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S0008621502004676},\n}\n\n

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\n \n\n \n \n \n \n \n \n Human autoantibodies with amylolytic activity.\n \n \n \n \n\n\n \n Ivanen, D.; Kulminskaya, A.; Ershova, N.; Eneyskaya, E.; Shabalin, K.; Savel'ev, A.; Kanyshkova, T.; Buneva, V.; Nevinsky, G.; and Neustroev, K.\n\n\n \n\n\n\n Biologia - Section Cellular and Molecular Biology, 57(SUPPL. 11): 253-260. 2002.\n cited By 7\n\n\n\n
\n\n\n\n \n \n $\"Human$ Paper\n \n \n\n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Ivanen2002253,\nauthor={Ivanen, D.R. and Kulminskaya, A.A. and Ershova, N.A. and Eneyskaya, E.V. and Shabalin, K.A. and Savel'ev, A.N. and Kanyshkova, T.G. and Buneva, V.N. and Nevinsky, G.A. and Neustroev, K.N.},\ntitle={Human autoantibodies with amylolytic activity},\njournal={Biologia - Section Cellular and Molecular Biology},\nyear={2002},\nvolume={57},\nnumber={SUPPL. 11},\npages={253-260},\nnote={cited By 7},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-19044395559&partnerID=40&md5=7b3dc1b59273e9e8db00ebaa3013ce73},\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nucl. Phys. Inst. R., 188350, Gatchina, St. Petersburg, Russian Federation; Novosibirsk Inst. of Bioorg. Chem., Siberian Div. of Russ. Acad. of Sci., Novosibirsk, Russian Federation; Biophysics Department, St. Petersburg Technical University, St. Petersburg, Russian Federation},\nauthor_keywords={α-amylase;  Autoantibodies from human;  Autoimmunity disease},\ncorrespondence_address1={Neustroev, K.N.; Molec. and Radiat. Biophys. Division, , 188350, Gatchina, St. Petersburg, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\nissn={13356399},\nlanguage={English},\nabbrev_source_title={Biol. Sect. Cell. Mol. Biol.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Structural insights into the β-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography.\n \n \n \n \n\n\n \n Aparicio, R.; Fischer, H.; Scott, D.; Verschueren, K.; Kulminskaya, A.; Eneiskaya, E.; Neustroev, K.; Craievich, A.; Golubev, A.; and Polikarpov, I.\n\n\n \n\n\n\n Biochemistry, 41(30): 9370-9375. 2002.\n cited By 13\n\n\n\n
\n\n\n\n \n \n $\"Structural$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Aparicio20029370,\nauthor={Aparicio, R. and Fischer, H. and Scott, D.J. and Verschueren, K.H.G. and Kulminskaya, A.A. and Eneiskaya, E.V. and Neustroev, K.N. and Craievich, A.F. and Golubev, A.M. and Polikarpov, I.},\ntitle={Structural insights into the β-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography},\njournal={Biochemistry},\nyear={2002},\nvolume={41},\nnumber={30},\npages={9370-9375},\ndoi={10.1021/bi025811p},\nnote={cited By 13},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037199487&doi=10.1021%2fbi025811p&partnerID=40&md5=993fa9e3c01e8e6234bfe0cce91b71f8},\naffiliation={Instituto de Física Gleb Wataghin, Universidade Estadual de Campinas, Campinas, SP, Brazil; Instituto de Física, Universidade de Sao Paulo, Sao Paulo, SP, Brazil; Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom; Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom; Instituto de Física de Sao Carlos, Universidade de Sao Paulo, CP 369, 13560-970, Sao Carlos, SP, Brazil; Division of Molecular Carcinogenesis, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, 188300, Russian Federation},\nkeywords={Circular dichroism, Enzymes;  Genes;  Molecular structure;  Synchrotrons;  X ray analysis;  X ray crystallography, Biotechnology, beta mannosidase, article;  catalysis;  circular dichroism;  enzyme mechanism;  nonhuman;  priority journal;  protein secondary structure;  stereochemistry;  synchrotron;  Trichoderma reesei;  X ray crystallography, beta-Mannosidase;  Circular Dichroism;  Crystallography, X-Ray;  Mannosidases;  Protein Conformation;  Protein Folding;  Scattering, Radiation;  Trichoderma, Hypocrea jecorina;  Trichoderma},\nchemicals_cas={beta mannosidase, 60748-69-8, 9025-43-8; Mannosidases, 3.2.1.-; beta-Mannosidase, 3.2.1.25},\ncorrespondence_address1={Polikarpov, I.; Instituto de Fisica de Sao Carlos, CP 369, 13560-970 São Carlos, SP, Brazil; email: ipolikarpov@if.sc.usp.br},\nissn={00062960},\ncoden={BICHA},\npubmed_id={12135358},\nlanguage={English},\nabbrev_source_title={Biochemistry},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori.\n \n \n \n \n\n\n \n Arand, M.; Golubev, A.; Neto, J.; Polikarpov, I.; Wattiez, R.; Korneeva, O.; Eneyskaya, E.; Kulminskaya, A.; Shabalin, K.; Shishliannikov, S.; Chepurnaya, O.; and Neustroev, K.\n\n\n \n\n\n\n Biochemical Journal, 362(1): 131-135. 2002.\n cited By 69\n\n\n\n
\n\n\n\n \n \n $\"Purification,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@ARTICLE{Arand2002131,\nauthor={Arand, M. and Golubev, A.M. and Neto, J.R.B. and Polikarpov, I. and Wattiez, R. and Korneeva, O.S. and Eneyskaya, E.V. and Kulminskaya, A.A. and Shabalin, K.A. and Shishliannikov, S.M. and Chepurnaya, O.V. and Neustroev, K.N.},\ntitle={Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori},\njournal={Biochemical Journal},\nyear={2002},\nvolume={362},\nnumber={1},\npages={131-135},\ndoi={10.1042/0264-6021:3620131},\nnote={cited By 69},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037084266&doi=10.1042%2f0264-6021%3a3620131&partnerID=40&md5=2fed1a311246671244653a7304594bc8},\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg 188350, Russian Federation},\nauthor_keywords={Family 32;  Inulin degradation;  Levan},\nkeywords={Amino acids;  Cloning;  Enzymes;  Hydrolysis;  Monomers;  pH effects;  Purification;  X ray analysis, Molecular mass, Fungi, complementary DNA;  glycosidase;  inulin;  inulinase;  levan, amino acid sequence;  article;  Aspergillus awamori;  enzyme analysis;  hydrolysis;  Michaelis constant;  molecular cloning;  molecular weight;  nonhuman;  nucleotide sequence;  priority journal;  protein family;  protein purification;  sequence analysis;  sequence homology;  X ray diffraction, Amino Acid Sequence;  Aspergillus;  Base Sequence;  Crystallography, X-Ray;  DNA Primers;  DNA, Complementary;  Glycoside Hydrolases;  Molecular Sequence Data;  Reverse Transcriptase Polymerase Chain Reaction, Aspergillus;  Aspergillus awamori;  Aspergillus foetidus;  Fungi},\nmolecular_seqnumbers={EMBL: AJ315793; GENBANK: AJ315793},\nchemicals_cas={DNA Primers; DNA, Complementary; Glycoside Hydrolases, EC 3.2.1.-; inulinase, EC 3.2.1.7},\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, , Gatchina, St. Petersburg 188350, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\nissn={02646021},\ncoden={BIJOA},\npubmed_id={11829749},\nlanguage={English},\nabbrev_source_title={Biochem. J.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

\n

\n\n\n\n

\n\n\n

\n \n\n \n \n \n \n \n \n 1-O-Acetyl-β-D-galactopyranose: A novel substrate for the transglycosylation reaction catalyzed by the β-galactosidase from Penicillium sp.\n \n \n \n \n\n\n \n Zinin, A.\n\n\n \n\n\n\n Carbohydrate Research, 337(7): 635–642. 2002.\n 20 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0036128984&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"1-O-Acetyl-β-D-galactopyranose:$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@Article{Zinin2002,\n  author   = {A. Zinin},\n  journal  = {Carbohydrate Research},\n  title    = {1-O-Acetyl-β-D-galactopyranose: A novel substrate for the transglycosylation reaction catalyzed by the β-galactosidase from Penicillium sp.},\n  year     = {2002},\n  issn     = {0008-6215},\n  note     = {20 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=0036128984\\&origin=inward},\n  number   = {7},\n  pages    = {635--642},\n  volume   = {337},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/0036128984},\n  doi      = {10.1016/S0008-6215(02)00027-7},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S0008621502000277},\n}\n\n

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\n \n\n \n \n \n \n \n \n Enzymatic properties of α-galactosidase from Trichoderma reesei in the hydrolysis of galactooligosaccharides.\n \n \n \n \n\n\n \n Shabalin, K.\n\n\n \n\n\n\n Enzyme and Microbial Technology, 30(2): 231–239. 2002.\n 36 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0037074922&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@Article{Shabalin2002,\n  author   = {K.A. Shabalin},\n  journal  = {Enzyme and Microbial Technology},\n  title    = {Enzymatic properties of α-galactosidase from Trichoderma reesei in the hydrolysis of galactooligosaccharides},\n  year     = {2002},\n  issn     = {0141-0229},\n  note     = {36 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=0037074922\\&origin=inward},\n  number   = {2},\n  pages    = {231--239},\n  volume   = {30},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/0037074922},\n  doi      = {10.1016/S0141-0229(01)00482-3},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S0141022901004823},\n}\n\n

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\n \n 2001\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Isolation, enzymatic properties, and mode of action of an exo-1,3-β-glucanase from Trichoderma viride.\n \n \n \n \n\n\n \n Kulminskaya, A.; Thomsen, K.; Shabalin, K.; Sidorenko, I.; Eneyskaya, E.; Savel'Ev, A.; and Neustroev, K.\n\n\n \n\n\n\n European Journal of Biochemistry, 268(23): 6123-6131. 2001.\n cited By 34\n\n\n\n
\n\n\n\n \n \n $\"Isolation,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@ARTICLE{Kulminskaya20016123,\nauthor={Kulminskaya, A.A. and Thomsen, K.K. and Shabalin, K.A. and Sidorenko, I.A. and Eneyskaya, E.V. and Savel'Ev, A.N. and Neustroev, K.N.},\ntitle={Isolation, enzymatic properties, and mode of action of an exo-1,3-β-glucanase from Trichoderma viride},\njournal={European Journal of Biochemistry},\nyear={2001},\nvolume={268},\nnumber={23},\npages={6123-6131},\ndoi={10.1046/j.0014-2956.2001.02558.x},\nnote={cited By 34},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035206899&doi=10.1046%2fj.0014-2956.2001.02558.x&partnerID=40&md5=63957ac4cbf45c675d617c1643b28948},\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Russian Federation; Carlsberg Laboratory, Department of Physiology, Copenhagen, Denmark; St Petersburg Technical University, Biophysics Department, Russian Federation; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation},\nauthor_keywords={3-β-glucanase;  Anomerity of hydrolysis;  Exo-1;  Trichoderma viride},\nkeywords={curdlan;  gentiobiose;  glucan glucosidase;  glucose;  isoenzyme;  laminaran, amino terminal sequence;  article;  binding affinity;  binding site;  biodegradation;  calculation;  controlled study;  enzyme active site;  enzyme activity;  enzyme mechanism;  enzyme purification;  enzyme specificity;  enzyme substrate;  fungus culture;  hydrolysis;  Michaelis constant;  molecular weight;  nonhuman;  polymerization;  priority journal;  protein isolation;  sequence homology;  stereochemistry;  Trichoderma viride, Amino Acid Sequence;  Carbohydrate Conformation;  Carbohydrate Sequence;  Catalytic Domain;  Glucan 1,3-beta-Glucosidase;  Glucans;  Glycoside Hydrolases;  Hydrolysis;  Kinetics;  Magnetic Resonance Spectroscopy;  Molecular Sequence Data;  Oligosaccharides;  Polysaccharides;  Stereoisomerism;  Substrate Specificity;  Trichoderma, Fungi;  Trichoderma viride},\nchemicals_cas={beta-1,3-exoglucanase, EC 3.2.1.58; Glucan 1,3-beta-Glucosidase, EC 3.2.1.58; Glucans; Glycoside Hydrolases, EC 3.2.1.-; laminaran, 9008-22-4; Oligosaccharides; Polysaccharides},\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Gatchina, St Petersburg 188350, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\nissn={00142956},\ncoden={EJBCA},\npubmed_id={11733006},\nlanguage={English},\nabbrev_source_title={Eur. J. Biochem.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Amylolytic activity of IgG and sIgA immunoglobulins from human milk.\n \n \n \n \n\n\n \n Savel'ev, A.\n\n\n \n\n\n\n Clinica Chimica Acta, 314(1): 141–152. 2001.\n 53 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0035165749&origin=inward\n\n\n\n
\n\n\n\n \n \n $\"Amylolytic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@Article{Savelev2001,\n  author   = {A.N. Savel'ev},\n  journal  = {Clinica Chimica Acta},\n  title    = {Amylolytic activity of IgG and sIgA immunoglobulins from human milk},\n  year     = {2001},\n  issn     = {0009-8981},\n  note     = {53 cites: https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b\\&scp=0035165749\\&origin=inward},\n  number   = {1},\n  pages    = {141--152},\n  volume   = {314},\n  citation = {https://api.elsevier.com/content/abstract/scopus_id/0035165749},\n  doi      = {10.1016/S0009-8981(01)00691-X},\n  type     = {Article},\n  url      = {https://api.elsevier.com/content/article/eid/1-s2.0-S000989810100691X},\n}\n\n

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\n\n\n\n\n\n

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\n \n 2000\n \n \n (3)\n \n \n

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\n \n \n

\n \n\n \n \n \n \n \n \n Purification, crystallization and preliminary diffraction study of β-galactosidase from Penicillium sp.\n \n \n \n \n\n\n \n Neustroev, K.; De Sousa, E.; Golubev, A.; Brandao Neto, J.; Eneyskaya, E.; Kulminskaya, A.; and Polikarpov, I.\n\n\n \n\n\n\n Acta Crystallographica Section D: Biological Crystallography, 56(11): 1508-1509. 2000.\n cited By 5\n\n\n\n
\n\n\n\n \n \n $\"Purification,$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@ARTICLE{Neustroev20001508,\nauthor={Neustroev, K.N. and De Sousa, E.A. and Golubev, A.M. and Brandao Neto, J.R. and Eneyskaya, E.V. and Kulminskaya, A.A. and Polikarpov, I.},\ntitle={Purification, crystallization and preliminary diffraction study of β-galactosidase from Penicillium sp.},\njournal={Acta Crystallographica Section D: Biological Crystallography},\nyear={2000},\nvolume={56},\nnumber={11},\npages={1508-1509},\ndoi={10.1107/S0907444900011756},\nnote={cited By 5},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033731794&doi=10.1107%2fS0907444900011756&partnerID=40&md5=30d861582afdd34d206fa1f6c68ec7bf},\naffiliation={LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, Brazil},\nkeywords={beta galactosidase, article;  chemistry;  crystallization;  enzymology;  glycosylation;  isolation and purification;  metabolism;  Penicillium;  protein conformation;  X ray crystallography, beta-Galactosidase;  Crystallization;  Crystallography, X-Ray;  Glycosylation;  Penicillium;  Protein Conformation, Penicillium;  Penicillium sp.},\nchemicals_cas={beta-Galactosidase, EC 3.2.1.23},\ncorrespondence_address1={Polikarpov, I.; LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, Brazil; email: igor@lnls.br},\nissn={09074449},\ncoden={ABCRE},\npubmed_id={11053867},\nlanguage={English},\nabbrev_source_title={Acta Crystallogr. Sect. D Biol. Crystallogr.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n \n Crystallization and preliminary X-ray study of β-Mannosidase from Trichoderma reesei.\n \n \n \n \n\n\n \n Aparicio, R.; Eneiskaya, E.; Kulminskaya, A.; Savel'ev, A.; Golubev, A.; Neustroev, K.; Kobarg, J.; and Polikarpov, I.\n\n\n \n\n\n\n Acta Crystallographica Section D: Biological Crystallography, 56(3): 342-343. 2000.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Crystallization$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@ARTICLE{Aparicio2000342,\nauthor={Aparicio, R. and Eneiskaya, E.V. and Kulminskaya, A.A. and Savel'ev, A.N. and Golubev, A.M. and Neustroev, K.N. and Kobarg, J. and Polikarpov, I.},\ntitle={Crystallization and preliminary X-ray study of β-Mannosidase from Trichoderma reesei},\njournal={Acta Crystallographica Section D: Biological Crystallography},\nyear={2000},\nvolume={56},\nnumber={3},\npages={342-343},\ndoi={10.1107/S0907444999016625},\nnote={cited By 1},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034096065&doi=10.1107%2fS0907444999016625&partnerID=40&md5=5575fe505e58c1a9d3ce0f4492a33d61},\naffiliation={Natl. Synchrotron Light Laboratory, LNLS, Caixa Postal 6192, CEP 13083-970, Campinas, SP, Brazil; Gleb Wataghin Physics Institute, State University at Campinas, UNICAMP, Caixa Postal 6165, CEP 13083-970, Campinas, SP, Brazil; Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188350, Russian Federation; St. Petersburg Technical University, 29 Politechnicheskaya Str., St Petersburg, 195251, Russian Federation},\nkeywords={beta mannosidase;  fungal protein;  mannosidase, article;  chemical structure;  chemistry;  crystallization;  enzymology;  isolation and purification;  protein conformation;  Trichoderma;  X ray crystallography, beta-Mannosidase;  Crystallization;  Crystallography, X-Ray;  Fungal Proteins;  Mannosidases;  Models, Molecular;  Protein Conformation;  Trichoderma, Hypocrea jecorina;  Trichoderma},\nchemicals_cas={beta-Mannosidase, EC 3.2.1.25; Fungal Proteins; Mannosidases, EC 3.2.1.-},\ncorrespondence_address1={Polikarpov, I.; Natl. Synchrotron Light Laboratory, Caixa Postal 6192, CEP 13083-970, Campinas, SP, Brazil; email: igor@lnls.br},\nissn={09074449},\ncoden={ABCRE},\npubmed_id={10713521},\nlanguage={English},\nabbrev_source_title={Acta Crystallogr. Sect. D Biol. Crystallogr.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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\n \n\n \n \n \n \n \n Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei.\n \n \n \n\n\n \n Golubev, A. M.; Brandão Neto, J. R.; Eneyskaya, E. V.; Kulminskaya, A. V.; Kerzhner, M. A.; Neustroev, K. N.; and Polikarpov, I.\n\n\n \n\n\n\n Acta crystallographica. Section D, Biological crystallography, 56: 1058–1060. August 2000.\n \n\n\n\n
\n\n\n\n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n

\n

@Article{Golubev2000,\n  author          = {Golubev, A. M. and Brandão Neto, J. R. and Eneyskaya, E. V. and Kulminskaya, A. V. and Kerzhner, M. A. and Neustroev, K. N. and Polikarpov, I.},\n  journal         = {Acta crystallographica. Section D, Biological crystallography},\n  title           = {Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei.},\n  year            = {2000},\n  issn            = {0907-4449},\n  month           = aug,\n  pages           = {1058--1060},\n  volume          = {56},\n  abstract        = {An extracellular multifunctional beta-xylosidase was purified from a culture of the fungus Trichoderma reesei. The active 95 +/- 5 kDa enzyme has been crystallized from sodium acetate buffer using PEG as a precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.75, b = 98.54, c = 227.25 A, and diffract beyond 2.7 A resolution. X-ray data were collected from frozen crystals on a synchrotron source.},\n  chemicals       = {Xylosidases, exo-1,4-beta-D-xylosidase},\n  citation-subset = {IM},\n  completed       = {2000-10-23},\n  country         = {United States},\n  doi             = {10.1107/s0907444900008210},\n  issn-linking    = {0907-4449},\n  issue           = {Pt 8},\n  keywords        = {Crystallization; Crystallography, X-Ray; Molecular Weight; Trichoderma, enzymology; Xylosidases, chemistry, isolation & purification},\n  nlm-id          = {9305878},\n  owner           = {NLM},\n  pii             = {S0907444900008210},\n  pmid            = {10944353},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2019-06-05},\n}\n\n

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\n\n\n\n\n\n

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\n \n 1998\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Multiple attack of action of α-galactosidase from Trichoderma Reesei.\n \n \n \n \n\n\n \n Shabalin, K.; Eneyskaya, E.; Kulminskaya, A.; Savel'ev, A.; and Neustroev, K.\n\n\n \n\n\n\n Protein and Peptide Letters, 5(6): 341-348. 1998.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Multiple$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@Article{Shabalin1998341,\n  author                  = {Shabalin, K.A. and Eneyskaya, E.V. and Kulminskaya, A.A. and Savel'ev, A.N. and Neustroev, K.N.},\n  journal                 = {Protein and Peptide Letters},\n  title                   = {Multiple attack of action of α-galactosidase from Trichoderma Reesei},\n  year                    = {1998},\n  issn                    = {09298665},\n  note                    = {cited By 0},\n  number                  = {6},\n  pages                   = {341-348},\n  volume                  = {5},\n  abbrev_source_title     = {Protein Pept. Lett.},\n  affiliation             = {Petersburg Nuclear Physics Institute, Molec. Radiat. Biophys. Div. G., St.-Petersburg, 188350, Russian Federation; St.Petersburg Technical University, Biophysics Department, 29 Polytechnicheskaya str, St.Petersburg, 195251, Russian Federation},\n  coden                   = {PPELE},\n  correspondence_address1 = {Neustroev, K.N.; Petersburg Nuclear Physics Institute, , St.-Petersburg, 188350, Russian Federation},\n  document_type           = {Article},\n  doi                     = {10.2174/092986650506221111111218},\n  language                = {English},\n  source                  = {Scopus},\n  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-17344373675&partnerID=40&md5=aef664cfd348ed524d61bc11e6ca9c7a},\n}\n\n

\n

\n\n\n\n

\n\n\n

\n \n\n \n \n \n \n \n \n Enzymatic properties of α-mannosidase from Trichoderma reesel.\n \n \n \n \n\n\n \n Kulminskaya, A.; Eneyskaya, E.; Isaeva-Ivanova, L.; Shabalin, K.; Savel'ev, A.; Backinowsky, L.; Abronina, P.; and Neustroev, K.\n\n\n \n\n\n\n Protein and Peptide Letters, 5(3): 163-170. 1998.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"Enzymatic$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@Article{Kulminskaya1998163,\n  author                  = {Kulminskaya, A.A. and Eneyskaya, E.V. and Isaeva-Ivanova, L.S. and Shabalin, K.A. and Savel'ev, A.N. and Backinowsky, L.V. and Abronina, P.I. and Neustroev, K.N.},\n  journal                 = {Protein and Peptide Letters},\n  title                   = {Enzymatic properties of α-mannosidase from Trichoderma reesel},\n  year                    = {1998},\n  issn                    = {09298665},\n  note                    = {cited By 3},\n  number                  = {3},\n  pages                   = {163-170},\n  volume                  = {5},\n  abbrev_source_title     = {Protein Pept. Lett.},\n  affiliation             = {Petersburg Nuclear Physics Institute, Molecular Division, St.Petersburg 188350, Russian Federation; St.Petersburg Technical University, Biophysics Department, 29 Polytechnicheskaya str., St.Petersburg 195251, Russian Federation; N.D.Zelinsky Inst. of Organ. Chem., 47 Leninsky av., 117913 Moscow, Russian Federation},\n  coden                   = {PPELE},\n  correspondence_address1 = {Neustroev, K.N.; Petersburg Nuclear Physics Institute, , St.Petersburg 188350, Russian Federation},\n  document_type           = {Article},\n  doi                     = {10.2174/092986650503221108111110},\n  language                = {English},\n  source                  = {Scopus},\n  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344245335&partnerID=40&md5=be4614ab5a300a4c1838611c326677b2},\n}\n\n

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\n \n\n \n \n \n \n \n alpha-Mannosidase from Trichoderma reesei participates in the postsecretory deglycosylation of glycoproteins.\n \n \n \n\n\n \n Eneyskaya, E. V.; Kulminskaya, A. A.; Savel'ev, A. N.; Shabalin, K. A.; Golubev, A. M.; and Neustroev, K. N.\n\n\n \n\n\n\n Biochemical and biophysical research communications, 245: 43–49. April 1998.\n \n\n\n\n
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@Article{Eneyskaya1998,\n  author          = {Eneyskaya, E. V. and Kulminskaya, A. A. and Savel'ev, A. N. and Shabalin, K. A. and Golubev, A. M. and Neustroev, K. N.},\n  journal         = {Biochemical and biophysical research communications},\n  title           = {alpha-Mannosidase from Trichoderma reesei participates in the postsecretory deglycosylation of glycoproteins.},\n  year            = {1998},\n  issn            = {0006-291X},\n  month           = apr,\n  pages           = {43--49},\n  volume          = {245},\n  abstract        = {The 160 kDa alpha-mannosidase (E.C. 3.2.1.24) isolated from culture filtrate of Trichoderma reesei has wide aglycon specificity but cleaves the alpha1 --> 2 and alpha1 --> 3 mannosidic bonds with higher rate than alpha1 --> 6 bond and slowly hydrolyses yeast mannan and 1,6-alpha-mannan. The specific activity of the enzyme and rate constant in the reaction with p-nitrophenyl-alpha-D-mannopyranoside were 0.15 U/mg and 1.62 x 10(-4) microM/min/microg, respectively, at optimal pH 6.5. We have found that in vitro enzyme is able to cleave off 30% of total alpha-mannopyranosyl residues from N- and O-linked glycans of secreted glycoproteins. The activity of the alpha-mannosidase toward glycoproteins in vivo was studied comparing the structures of O- and N-linked glycans of glycoproteins isolated from the cultures growing with and without 1-deoxymannojirimycin, an inhibitor of alpha-mannosidases. Difference in structures of these glycans may be explained by postsecretory deglycosylation catalysed by the alpha-mannosidase.},\n  chemicals       = {Enzyme Inhibitors, Fungal Proteins, Glycoproteins, Mannans, 1-Deoxynojirimycin, Mannosidases, alpha-Mannosidase, Mannose},\n  citation-subset = {IM},\n  completed       = {1998-05-14},\n  country         = {United States},\n  doi             = {10.1006/bbrc.1998.8382},\n  issn-linking    = {0006-291X},\n  issue           = {1},\n  keywords        = {1-Deoxynojirimycin, pharmacology; Enzyme Inhibitors, pharmacology; Fungal Proteins, metabolism; Glycoproteins, metabolism; Glycosylation; Kinetics; Mannans, metabolism; Mannose, metabolism; Mannosidases, metabolism; Substrate Specificity; Trichoderma, enzymology; alpha-Mannosidase},\n  nlm-id          = {0372516},\n  owner           = {NLM},\n  pii             = {S0006-291X(98)98382-6},\n  pmid            = {9535780},\n  pubmodel        = {Print},\n  pubstate        = {ppublish},\n  revised         = {2013-11-21},\n}\n\n

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\n \n\n \n \n \n \n \n \n The action of α-mannosidase from oerskovia sp. on the mannose-rich O-linked sugar chains of glycoproteins.\n \n \n \n \n\n\n \n Bagiyan, F.; Eneyskaya, E.; Kulminskaya, A.; Savel'ev, A.; Shabalin, K.; and Neustroev, K.\n\n\n \n\n\n\n European Journal of Biochemistry, 249(1): 286-292. 1997.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n\n\n\n

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@ARTICLE{Bagiyan1997286,\nauthor={Bagiyan, F.G. and Eneyskaya, E.V. and Kulminskaya, A.A. and Savel'ev, A.K. and Shabalin, K.A. and Neustroev, K.N.},\ntitle={The action of α-mannosidase from oerskovia sp. on the mannose-rich O-linked sugar chains of glycoproteins},\njournal={European Journal of Biochemistry},\nyear={1997},\nvolume={249},\nnumber={1},\npages={286-292},\ndoi={10.1111/j.1432-1033.1997.t01-1-00286.x},\nnote={cited By 10},\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030792737&doi=10.1111%2fj.1432-1033.1997.t01-1-00286.x&partnerID=40&md5=90009634edc08ac6476a12f86b654690},\naffiliation={Petersburg Nuclear Physics Institute, Molec. and Radiat. Biophys. Division, St Petersburg, Russian Federation; St. Petersburg Technical University, Biophysics Department, St Petersburg, Russian Federation; Petersburg Nuclear Physics Institute, Gatchina, 188350 St Petersburg, Russian Federation},\nauthor_keywords={1-Deoxymannojirimycin;  Deglycosylation;  exo-α-mannanase;  Glucoamylase;  Yeast mannan},\nkeywords={mannan;  mannosidase, article;  cell culture;  enzyme activity;  enzyme purification;  molecular weight;  priority journal, Felis catus;  Oerskovia},\nchemicals_cas={mannan, 51395-96-1, 9036-88-8; mannosidase, 37211-66-8},\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Gatchina, 188350 St Petersburg, Russian Federation; email: neustk@omrb.pnpi.spb.ru},\npublisher={Blackwell Publishing Ltd},\nissn={00142956},\ncoden={EJBCA},\npubmed_id={9363781},\nlanguage={English},\nabbrev_source_title={EUR. J. BIOCHEM.},\ndocument_type={Article},\nsource={Scopus},\n}\n\n

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