\n

\n \n 2015\n \n \n (2)\n \n \n

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\n \n \n

\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. 2015.\n cited By 14\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 abstract \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

@ARTICLE{Borisova20154515,\r\nauthor={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.},\r\ntitle={Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C},\r\njournal={FEBS Journal},\r\nyear={2015},\r\nvolume={282},\r\nnumber={23},\r\npages={4515-4537},\r\ndoi={10.1111/febs.13509},\r\nnote={cited By 14},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84961331730&doi=10.1111%2ffebs.13509&partnerID=40&md5=b1587711d771fe0a70ea4e28e8780d03},\r\naffiliation={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},\r\nabstract={The ascomycete Geotrichum candidum is a versatile and efficient decay fungus that is involved, for example, in biodeterioration of compact discs; notably, the 3C strain was previously shown to degrade filter paper and cotton more efficiently than several industrial enzyme preparations. Glycoside hydrolase (GH) family 7 cellobiohydrolases (CBHs) are the primary constituents of industrial cellulase cocktails employed in biomass conversion, and feature tunnel-enclosed active sites that enable processive hydrolytic cleavage of cellulose chains. Understanding the structure-function relationships defining the activity and stability of GH7 CBHs is thus of keen interest. Accordingly, we report the comprehensive characterization of the GH7 CBH secreted by G. candidum (GcaCel7A). The bimodular cellulase consists of a family 1 cellulose-binding module (CBM) and linker connected to a GH7 catalytic domain that shares 64% sequence identity with the archetypal industrial GH7 CBH of Hypocrea jecorina (HjeCel7A). GcaCel7A shows activity on Avicel cellulose similar to HjeCel7A, with less product inhibition, but has a lower temperature optimum (50 °C versus 60-65 °C, respectively). Five crystal structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4 not reported previously in GH7. Also, the first O-glycosylation site in a GH7 crystal structure is reported - on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface. The GcaCel7A structures indicate higher loop flexibility than HjeCel7A, in accordance with sequence modifications. However, GcaCel7A retains small fluctuations in molecular simulations, suggesting high processivity and low endo-initiation probability, similar to HjeCel7A. Database Structural data are available in the Protein Data Bank under the accession numbers 5AMP, 4ZZV, 4ZZW, 4ZZT, and 4ZZU. The Geotrichum candidum GH family 7 cellobiohydrolase nucleotide sequence is available in GenBank under accession number KJ958925. Enzymes Glycoside hydrolase family 7 reducing end acting cellobiohydrolase We report the characterization of the GH7 CBH secreted by ascomycete G. candidum (GcaCel7A). X-ray data revealed the first O-glycosylation in a GH7 crystal structure on a loop where the glycan influences loop contacts and interactions with the cellulose surface. Even though GcaCel7A structures indicate higher loop flexibility than H. jecorina Cel7A, molecular simulations suggest high processivity and low endo-initiation probability similar to HjeCel7A. © 2015 FEBS.},\r\nauthor_keywords={biomass degradation;  cellulase;  Geotrichum candidum;  molecular dynamics;  X-ray structure},\r\ncorrespondence_address1={Stahlberg, J.; Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, PO Box 7015, Sweden; email: Jerry.Stahlberg@slu.se},\r\npublisher={Blackwell Publishing Ltd},\r\nissn={1742464X},\r\ncoden={FJEOA},\r\npubmed_id={26367132},\r\nlanguage={English},\r\nabbrev_source_title={FEBS J.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

\n\n\n

\n The ascomycete Geotrichum candidum is a versatile and efficient decay fungus that is involved, for example, in biodeterioration of compact discs; notably, the 3C strain was previously shown to degrade filter paper and cotton more efficiently than several industrial enzyme preparations. Glycoside hydrolase (GH) family 7 cellobiohydrolases (CBHs) are the primary constituents of industrial cellulase cocktails employed in biomass conversion, and feature tunnel-enclosed active sites that enable processive hydrolytic cleavage of cellulose chains. Understanding the structure-function relationships defining the activity and stability of GH7 CBHs is thus of keen interest. Accordingly, we report the comprehensive characterization of the GH7 CBH secreted by G. candidum (GcaCel7A). The bimodular cellulase consists of a family 1 cellulose-binding module (CBM) and linker connected to a GH7 catalytic domain that shares 64% sequence identity with the archetypal industrial GH7 CBH of Hypocrea jecorina (HjeCel7A). GcaCel7A shows activity on Avicel cellulose similar to HjeCel7A, with less product inhibition, but has a lower temperature optimum (50 °C versus 60-65 °C, respectively). Five crystal structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4 not reported previously in GH7. Also, the first O-glycosylation site in a GH7 crystal structure is reported - on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface. The GcaCel7A structures indicate higher loop flexibility than HjeCel7A, in accordance with sequence modifications. However, GcaCel7A retains small fluctuations in molecular simulations, suggesting high processivity and low endo-initiation probability, similar to HjeCel7A. Database Structural data are available in the Protein Data Bank under the accession numbers 5AMP, 4ZZV, 4ZZW, 4ZZT, and 4ZZU. The Geotrichum candidum GH family 7 cellobiohydrolase nucleotide sequence is available in GenBank under accession number KJ958925. Enzymes Glycoside hydrolase family 7 reducing end acting cellobiohydrolase We report the characterization of the GH7 CBH secreted by ascomycete G. candidum (GcaCel7A). X-ray data revealed the first O-glycosylation in a GH7 crystal structure on a loop where the glycan influences loop contacts and interactions with the cellulose surface. Even though GcaCel7A structures indicate higher loop flexibility than H. jecorina Cel7A, molecular simulations suggest high processivity and low endo-initiation probability similar to HjeCel7A. © 2015 FEBS.\n

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\n \n\n \n \n \n \n \n \n Transcriptional and hormonal regulation of gravitropism of woody stems in populus.\n \n \n \n \n\n\n \n Gerttula, S.; Zinkgraf, M.; Muday, G.; Lewis, D.; Ibatullin, F.; Brumer, H.; Hart, F.; Mansfield, S.; Filkov, V.; and Groover, A.\n\n\n \n\n\n\n Plant Cell, 27(10): 2800-2813. 2015.\n cited By 40\n\n\n\n
\n\n\n\n \n \n $\"Transcriptional$ 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

@ARTICLE{Gerttula20152800,\r\nauthor={Gerttula, S. and Zinkgraf, M. and Muday, G.K. and Lewis, D.R. and Ibatullin, F.M. and Brumer, H. and Hart, F. and Mansfield, S.D. and Filkov, V. and Groover, A.},\r\ntitle={Transcriptional and hormonal regulation of gravitropism of woody stems in populus},\r\njournal={Plant Cell},\r\nyear={2015},\r\nvolume={27},\r\nnumber={10},\r\npages={2800-2813},\r\ndoi={10.1105/tpc.15.00531},\r\nnote={cited By 40},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84946782272&doi=10.1105%2ftpc.15.00531&partnerID=40&md5=8659cec6d2c7fa4de3afbcca80b83ac2},\r\naffiliation={US Forest Service, Pacific Southwest Research Station, Davis, CA  95618, United States; Wake Forest University, Winston-Salem, NC  27106, United States; Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, Stockholm, S-106 91, Sweden; Biophysics Division, Petersburg Nuclear Physics Institute, National Research Center Kurchatov Institute, Gatchina, 188300, Russian Federation; Michael Smith Laboratories and Department of Chemistry, University of British Columbia, Vancouver, BC  V6T 1Z4, Canada; Department of Wood Science, University of British Columbia, Vancouver, BC  V6T 1Z4, Canada; Department of Computer Science, University of California, Davis, CA  95618, United States; Department of Plant Biology, University of California, Davis, CA  95618, United States},\r\nabstract={Angiosperm trees reorient their woody stems by asymmetrically producing a specialized xylem tissue, tension wood, which exerts a strong contractile force resulting in negative gravitropism of the stem. Here, we show, in Populus trees, that initial gravity perception and response occurs in specialized cells through sedimentation of starch-filled amyloplasts and relocalization of the auxin transport protein, PIN3. Gibberellic acid treatment stimulates the rate of tension wood formation and gravibending and enhances tissue-specific expression of an auxin-responsive reporter. Gravibending, maturation of contractile fibers, and gibberellic acid (GA) stimulation of tension wood formation are all sensitive to transcript levels of the Class I KNOX homeodomain transcription factor-encoding gene ARBORKNOX2 (ARK2). We generated genome-wide transcriptomes for trees in which gene expression was perturbed by gravistimulation, GA treatment, and modulation of ARK2 expression. These data were employed in computational analyses to model the transcriptional networks underlying wood formation, including identification and dissection of gene coexpression modules associated with wood phenotypes, GA response, and ARK2 binding to genes within modules. We propose a model for gravitropism in the woody stem in which the peripheral location of PIN3-expressing cells relative to the cambium results in auxin transport toward the cambium in the top of the stem, triggering tension wood formation, while transport away from the cambium in the bottom of the stem triggers opposite wood formation. © 2015 American Society of Plant Biologists. All rights reserved.},\r\nfunding_details={National Aeronautics and Space AdministrationNNX09AK82G},\r\ncorrespondence_address1={Groover, A.; US Forest Service, Pacific Southwest Research StationUnited States},\r\npublisher={American Society of Plant Biologists},\r\nissn={10404651},\r\ncoden={PLCEE},\r\npubmed_id={26410302},\r\nlanguage={English},\r\nabbrev_source_title={Plant Cell},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2014\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Glycoside hydrolase activities in cell walls of sclerenchyma cells in the inflorescence stems of Arabidopsis thaliana visualized in situ.\n \n \n \n \n\n\n \n Banasiak, A.; Ibatullin, F.; Brumer, H.; and Mellerowicz, E.\n\n\n \n\n\n\n Plants, 3(4): 513-525. 2014.\n cited By 3\n\n\n\n
\n\n\n\n \n \n $\"Glycoside$ 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

@ARTICLE{Banasiak2014513,\r\nauthor={Banasiak, A. and Ibatullin, F.M. and Brumer, H. and Mellerowicz, E.J.},\r\ntitle={Glycoside hydrolase activities in cell walls of sclerenchyma cells in the inflorescence stems of Arabidopsis thaliana visualized in situ},\r\njournal={Plants},\r\nyear={2014},\r\nvolume={3},\r\nnumber={4},\r\npages={513-525},\r\ndoi={10.3390/plants3040513},\r\nnote={cited By 3},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84976220749&doi=10.3390%2fplants3040513&partnerID=40&md5=d52c265bcb81a0d0495291fc31cdbf07},\r\naffiliation={Institute of Experimental Biology, University of Wroclaw, Wroclaw, 50-328, Poland; Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm, 106 91, Sweden; Biophysics Division, Petersburg Nuclear Physics Institute, National Research Center Kurchatov Institute, Gatchina, 188300, Russian Federation; Michael Smith Laboratories, University of British Columbia, 2185 East Mall, Vancouver, BC  V6T 1Z1, Canada; Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, BC  V6T 1Z1, Canada; Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umea Plant Science Centre, Umea, 90183, Sweden},\r\nabstract={Techniques for in situ localization of gene products provide indispensable information for understanding biological function. In the case of enzymes, biological function is directly related to activity, and therefore, knowledge of activity patterns is central to understanding the molecular controls of plant development. We have previously developed a novel type of fluorogenic substrate for revealing glycoside hydrolase activity in planta, based on resorufin β-glycosides Here, we explore a wider range of such substrates to visualize glycoside hydrolase activities in Arabidopsis inflorescence stems in real time, especially highlighting distinct distribution patterns of these activities in the secondary cell walls of sclerenchyma cells. The results demonstrate that β-1,4-glucosidase, β-1,4-glucanase and β-1,4-galactosidase activities accompany secondary wall deposition. In contrast, xyloglucanase activity follows a different pattern, with the highest signal observed in mature cells, concentrated in the middle lamella. These data further the understanding of the process of cell wall deposition and function in sclerenchymatic tissues of plants. © 2014 by the authors; licensee MDPI, Basel, Switzerland.},\r\nauthor_keywords={Cell wall;  Glycoside hydrolase activity;  In situ activity;  Sclerenchyma;  Wood;  Xylem},\r\nfunding_details={European Cooperation in Science and TechnologyCOST-STSM-E50-03056},\r\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 \n Group III-A XTH genes of Arabidopsis encode predominant xyloglucan endohydrolases that are dispensable for normal growth.\n \n \n \n \n\n\n \n Kaewthai, N.; Gendre, D.; Eklöf, J.; Ibatullin, F.; Ezcurra, I.; Bhalerao, R.; and Brumer, H.\n\n\n \n\n\n\n Plant Physiology, 161(1): 440-454. 2013.\n cited By 29\n\n\n\n
\n\n\n\n \n \n $\"Group$ 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

@ARTICLE{Kaewthai2013440,\r\nauthor={Kaewthai, N. and Gendre, D. and Eklöf, J.M. and Ibatullin, F.M. and Ezcurra, I. and Bhalerao, R.P. and Brumer, H.},\r\ntitle={Group III-A XTH genes of Arabidopsis encode predominant xyloglucan endohydrolases that are dispensable for normal growth},\r\njournal={Plant Physiology},\r\nyear={2013},\r\nvolume={161},\r\nnumber={1},\r\npages={440-454},\r\ndoi={10.1104/pp.112.207308},\r\nnote={cited By 29},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84871817930&doi=10.1104%2fpp.112.207308&partnerID=40&md5=40ef4840d1656f3e310b15b082b2e11f},\r\naffiliation={Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, S-106 91 Stockholm, Sweden; Umeå Plant Science Center, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, SE-901 83 Umea, Sweden; Biophysics Division, Petersburg Nuclear Physics Institute, National Research Center Kurchatov Institute, Gatchina 188300, Russian Federation; Michael Smith Laboratories and Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z4, Canada},\r\nabstract={The molecular basis of primary wall extension endures as one of the central enigmas in plant cell morphogenesis. Classical cell wall models suggest that xyloglucan endo-transglycosylase activity is the primary catalyst (together with expansins) of controlled cell wall loosening through the transient cleavage and religation of xyloglucan-cellulose cross links. The genome of Arabidopsis (Arabidopsis thaliana) contains 33 phylogenetically diverse XYLOGLUCAN ENDO-TRANSGLYCOSYLASE/ HYDROLASE (XTH) gene products, two of which were predicted to be predominant xyloglucan endohydrolases due to clustering into group III-A. Enzyme kinetic analysis of recombinant AtXTH31 confirmed this prediction and indicated that this enzyme had similar catalytic properties to the nasturtium (Tropaeolum majus) xyloglucanase1 responsible for storage xyloglucan hydrolysis during germination. Global analysis of Genevestigator data indicated that AtXTH31 and the paralogous AtXTH32 were abundantly expressed in expanding tissues. Microscopy analysis, utilizing the resorufin β-glycoside of the xyloglucan oligosaccharide XXXG as an in situ probe, indicated significant xyloglucan endohydrolase activity in specific regions of both roots and hypocotyls, in good correlation with transcriptomic data. Moreover, this hydrolytic activity was essentially completely eliminated in AtXTH31/AtXTH32 double knockout lines. However, single and double knockout lines, as well as individual overexpressing lines, of AtXTH31 and AtXTH32 did not demonstrate significant growth or developmental phenotypes. These results suggest that although xyloglucan polysaccharide hydrolysis occurs in parallel with primary wall expansion, morphological effects are subtle or may be compensated by other mechanisms. We hypothesize that there is likely to be an interplay between these xyloglucan endohydrolases and recently discovered apoplastic exo-glycosidases in the hydrolytic modification of matrix xyloglucans. © 2012 American Society of Plant Biologists. All Rights Reserved.},\r\ncorrespondence_address1={Brumer, H.; Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, S-106 91 Stockholm, Sweden; email: brumer@msl.ubc.ca},\r\nissn={00320889},\r\ncoden={PLPHA},\r\npubmed_id={23104861},\r\nlanguage={English},\r\nabbrev_source_title={Plant Physiol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

\n\n\n

\n The molecular basis of primary wall extension endures as one of the central enigmas in plant cell morphogenesis. Classical cell wall models suggest that xyloglucan endo-transglycosylase activity is the primary catalyst (together with expansins) of controlled cell wall loosening through the transient cleavage and religation of xyloglucan-cellulose cross links. The genome of Arabidopsis (Arabidopsis thaliana) contains 33 phylogenetically diverse XYLOGLUCAN ENDO-TRANSGLYCOSYLASE/ HYDROLASE (XTH) gene products, two of which were predicted to be predominant xyloglucan endohydrolases due to clustering into group III-A. Enzyme kinetic analysis of recombinant AtXTH31 confirmed this prediction and indicated that this enzyme had similar catalytic properties to the nasturtium (Tropaeolum majus) xyloglucanase1 responsible for storage xyloglucan hydrolysis during germination. Global analysis of Genevestigator data indicated that AtXTH31 and the paralogous AtXTH32 were abundantly expressed in expanding tissues. Microscopy analysis, utilizing the resorufin β-glycoside of the xyloglucan oligosaccharide XXXG as an in situ probe, indicated significant xyloglucan endohydrolase activity in specific regions of both roots and hypocotyls, in good correlation with transcriptomic data. Moreover, this hydrolytic activity was essentially completely eliminated in AtXTH31/AtXTH32 double knockout lines. However, single and double knockout lines, as well as individual overexpressing lines, of AtXTH31 and AtXTH32 did not demonstrate significant growth or developmental phenotypes. These results suggest that although xyloglucan polysaccharide hydrolysis occurs in parallel with primary wall expansion, morphological effects are subtle or may be compensated by other mechanisms. We hypothesize that there is likely to be an interplay between these xyloglucan endohydrolases and recently discovered apoplastic exo-glycosidases in the hydrolytic modification of matrix xyloglucans. © 2012 American Society of Plant Biologists. All Rights Reserved.\n

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\n \n 2012\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n In vitro potential of histone deacetylase inhibitors for anticancer therapy.\n \n \n \n \n\n\n \n Kovalev, R.; Shtam, T.; Ibatullin, F.; Bondarev, G.; and Filatov, M.\n\n\n \n\n\n\n Voprosy Onkologii, 58(6): 800-807. 2012.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"In$ Paper\n \n \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

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@ARTICLE{Kovalev2012800,\r\nauthor={Kovalev, R.A. and Shtam, T.A. and Ibatullin, F.M. and Bondarev, G.N. and Filatov, M.V.},\r\ntitle={In vitro potential of histone deacetylase inhibitors for anticancer therapy},\r\njournal={Voprosy Onkologii},\r\nyear={2012},\r\nvolume={58},\r\nnumber={6},\r\npages={800-807},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84875510733&partnerID=40&md5=330a4b66718da144b754fc8a404b3fd9},\r\naffiliation={Nuclear Physics Institute, Saint-Petersburg, Russian Federation},\r\nabstract={Research during the past decade has shown that epigenetic events have a key role in carcinogenesis and tumour progression. Histone deacetylase inhibitors (HDACi) comprise structurally diverse compounds that are a group of targeted epigenetic anticancer agents. Here we explored the in vitro efficacy of HDACi such as sodium butyrate (BuNa), valproic acid (VaNa) and several novel HDAC inhibitors for the treatment of cancer. Both BuNa and VaNa inhibited cancer cell proliferation in a time - and dose-dependent fashion. In the present study we demonstrated the significant effect of two novel HDACi, Adipo or BuNHOH, able to induce apoptosis of cancer cells, but not of normal line. Since HDAC inhibitors have been proposed as radio - or chemosensitizers in cancer therapy, we have studied the radiosensitizing effect of sodium butyrate on cancer cells. The combination of BuNa and radiation significantly inhibited tumor cell growth. Besides, combining Cisplatin or Gemzar with HDAC inhibitors results in synergistic antiproliferative activity that could be therapeutically exploited. These results suggest that HDACi acts as an antitumor agent and that combining HDAC inhibitors with radio or - chemotherapeutic strategy may provide a novel chemotherapeutic treatment of cancers insensitive to traditional antitumor agents.},\r\ncorrespondence_address1={Kovalev, R.A.; Nuclear Physics Institute, Saint-Petersburg, Russian Federation},\r\nissn={05073758},\r\ncoden={VOONA},\r\npubmed_id={23600307},\r\nlanguage={Russian},\r\nabbrev_source_title={Vopr. Onkol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n [Absorption of iodofolic acids by the cells of malignant tumors].\n \n \n \n \n\n\n \n Soroka, N.; Filatov, M.; Korolev, V.; Bagiian, G.; Aplin, K.; and Gridasov, G.\n\n\n \n\n\n\n Bioorganicheskaia khimiia, 38(6): 734-744. 2012.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"[Absorption$ Paper\n \n \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

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@ARTICLE{Soroka2012734,\r\nauthor={Soroka, N.V. and Filatov, M.V. and Korolev, V.G. and Bagiian, G.A. and Aplin, K.D. and Gridasov, G.G.},\r\ntitle={[Absorption of iodofolic acids by the cells of malignant tumors].},\r\njournal={Bioorganicheskaia khimiia},\r\nyear={2012},\r\nvolume={38},\r\nnumber={6},\r\npages={734-744},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84878876945&partnerID=40&md5=551a1ed8267ba2c6cffd52472fbc6df1},\r\nabstract={The uptake of 125-iodine labeled 3' iodofolic acid (I*F) and 3' iodo, 5 formyl tetrahydrofolic acid (I*FT) by the cells HeLa, ECV, L-41, human glioma, and rat glioma was studied. Human Embrionic Lung Fibroblasts (HELF) were taken for comparison as healthy cells. It was shown for *IF that its long-term uptake by cells L-41 and ECV is hundreds oftimes higher than those of HELF cells. The short-term uptake phase was studied for *IFT uptake. The dissociation constant was determined for a complex formed by *IFT and an acceptor in the HeLa cells, which is supposed to cause concentrative uptake of *IFT in cells. The dissociation constants of this acceptor complexes with folic acid, 3' iodofolic acid and 3',5'-diiodofolic acid were determined by competition with I*FT. The distribution ratio of *IF and *IFT in tissues of different organs of healthy mice and rats and rats with a sarcoma grafted on his thigh and glioma grafted into the brain was studied. As was shown there are large differences in the concentration of *IF and *IFT in the tumor and in the healthy tissue, *IF concentration in thigh muscle of healthy being 5 times lower than those in tumor grafted to the thigh, and *IFT concentration in healthy brain being 10 times lower than in brain tumor.},\r\ncorrespondence_address1={Soroka, N.V.},\r\nissn={01323423},\r\npubmed_id={23547477},\r\nlanguage={Russian},\r\nabbrev_source_title={Bioorg. Khim.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Absorption of iodofolic acids by the cells of malignant tumors.\n \n \n \n \n\n\n \n Soroka, N.; Filatov, M.; Korolev, V.; Bagiyan, G.; Aplin, K.; and Gridasov, G.\n\n\n \n\n\n\n Russian Journal of Bioorganic Chemistry, 38(6): 652-661. 2012.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Absorption$ 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

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@ARTICLE{Soroka2012652,\r\nauthor={Soroka, N.V. and Filatov, M.V. and Korolev, V.G. and Bagiyan, G.A. and Aplin, K.D. and Gridasov, G.G.},\r\ntitle={Absorption of iodofolic acids by the cells of malignant tumors},\r\njournal={Russian Journal of Bioorganic Chemistry},\r\nyear={2012},\r\nvolume={38},\r\nnumber={6},\r\npages={652-661},\r\ndoi={10.1134/S1068162012060131},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84870426049&doi=10.1134%2fS1068162012060131&partnerID=40&md5=f27639cceea9ebc8bc5cd19271332c20},\r\naffiliation={Institute of Nuclear Physics, Russian Academy of Sciences, Gatchina, Leningradskaya oblast, 188350, Russian Federation; Khlopin Radium Institute, Russian Federation},\r\nabstract={The uptake of our synthesized 125-iodine labeled 3'-iodofolic acid ( *IF) and 3'-iodo-5-formyltetrahyrofolic acid ( *IFT) by the HeLa, EVC, L-41, human glioma, and rat glioma cells has been studied. The Human Embryonic Lung Fibroblasts (HELFs) were used as healthy control cells for comparison. It was shown for the quantity of *IF absorbed at its long-term uptake phase by the L-41 and ECV cells is hundreds of times higher than that of the HELF cells. The short-term *IFT uptake phase by the cells was studied. For the HeLa cells, the dissociation constant was determined for the *IFT complex with an acceptor, which is supposed to be responsible for *IFT accumulation in the cells. Using competitive sorption approach, the dissociation constants of folic, 3'-iodofolic, and 3',5'-diiodofolic acid complexes with this acceptor were assessed. The distribution ratio of *IF and *IFT in tissues of different organs of healthy mice and rats and also in rats with sarcoma grafted on their thigh and glioma grafted into the brain was studied. A considerable differences were shown in the concentrations of *IF and *IFT in the tumor and in the healthy tissue, i.e., *IF in the healthy thigh muscle is five times lower than in the tumor grafted to the thigh, and *IFT concentration is 10 times lower in the healthy brain compared to the brain tumor. © Pleiades Publishing, Ltd., 2012.},\r\nauthor_keywords={Absorption;  Folates;  Iodine derivatives;  Isotope 125I;  Malignant cells},\r\ncorrespondence_address1={Filatov, M.V.; Institute of Nuclear Physics, Russian Academy of Sciences, Gatchina, Leningradskaya oblast, 188350, Russian Federation; email: fil53ster@gmail.ru},\r\nissn={10681620},\r\ncoden={RJBCE},\r\nlanguage={English},\r\nabbrev_source_title={Russ. J. Bioorg. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2011\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n Building custom polysaccharides in vitro with an efficient, broad-specificity xyloglucan glycosynthase and a fucosyltransferase.\n \n \n \n \n\n\n \n Spadiut, O.; Ibatullin, F.; Peart, J.; Gullfot, F.; Martinez-Fleites, C.; Ruda, M.; Xu, C.; Sundqvist, G.; Davies, G.; and Brumer, H.\n\n\n \n\n\n\n Journal of the American Chemical Society, 133(28): 10892-10900. 2011.\n cited By 30\n\n\n\n
\n\n\n\n \n \n $\"Building$ 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

@ARTICLE{Spadiut201110892,\r\nauthor={Spadiut, O. and Ibatullin, F.M. and Peart, J. and Gullfot, F. and Martinez-Fleites, C. and Ruda, M. and Xu, C. and Sundqvist, G. and Davies, G.J. and Brumer, H.},\r\ntitle={Building custom polysaccharides in vitro with an efficient, broad-specificity xyloglucan glycosynthase and a fucosyltransferase},\r\njournal={Journal of the American Chemical Society},\r\nyear={2011},\r\nvolume={133},\r\nnumber={28},\r\npages={10892-10900},\r\ndoi={10.1021/ja202788q},\r\nnote={cited By 30},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-79960267493&doi=10.1021%2fja202788q&partnerID=40&md5=75c081b939a5dbf8d783d695f017645b},\r\naffiliation={Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), 106 91 Stockholm, Sweden; Wallenberg Wood Science Center, Royal Institute of Technology (KTH), 100 44 Stockholm, Sweden; York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom; Swetree Technologies AB, P.O. Box 4095, 904 03 Umeå, Sweden; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St. Petersburg 188300, Russian Federation},\r\nabstract={The current drive for applications of biomass-derived compounds, for energy and advanced materials, has led to a resurgence of interest in the manipulation of plant polymers. The xyloglucans, a family of structurally complex plant polysaccharides, have attracted significant interest due to their intrinsic high affinity for cellulose, both in muro and in technical applications. Moreover, current cell wall models are limited by the lack of detailed structure-property relationships of xyloglucans, due to a lack of molecules with well-defined branching patterns. Here, we have developed a new, broad-specificity "xyloglucan glycosynthase", selected from active-site mutants of a bacterial endoxyloglucanase, which catalyzed the synthesis of high molar mass polysaccharides, with complex side-chain structures, from suitable glycosyl fluoride donor substrates. The product range was further extended by combination with an Arabidopsis thaliana α(1→2)-fucosyltransferase to achieve the in vitro synthesis of fucosylated xyloglucans typical of dicot primary cell walls. These enzymes thus comprise a toolkit for the controlled enzymatic synthesis of xyloglucans that are otherwise impossible to obtain from native sources. Moreover, this study demonstrates the validity of a chemo-enzymatic approach to polysaccharide synthesis, in which the simplicity and economy of glycosynthase technology is harnessed together with the exquisite specificity of glycosyltransferases to control molecular complexity. © 2011 American Chemical Society.},\r\ncorrespondence_address1={Brumer, H.; Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), 106 91 Stockholm, Sweden; email: harry@biotech.kth.se},\r\nissn={00027863},\r\ncoden={JACSA},\r\npubmed_id={21618981},\r\nlanguage={English},\r\nabbrev_source_title={J. Am. Chem. Soc.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification.\n \n \n \n \n\n\n \n Larsbrink, J.; Izumi, A.; Ibatullin, F.; Nakhai, A.; Gilbert, H.; Davies, G.; and Brumer, H.\n\n\n \n\n\n\n Biochemical Journal, 436(3): 567-580. 2011.\n cited By 44\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 abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Larsbrink2011567,\r\nauthor={Larsbrink, J. and Izumi, A. and Ibatullin, F.M. and Nakhai, A. and Gilbert, H.J. and Davies, G.J. and Brumer, H.},\r\ntitle={Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification},\r\njournal={Biochemical Journal},\r\nyear={2011},\r\nvolume={436},\r\nnumber={3},\r\npages={567-580},\r\ndoi={10.1042/BJ20110299},\r\nnote={cited By 44},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-79957714498&doi=10.1042%2fBJ20110299&partnerID=40&md5=fe1d132569b29c481f0ca28d4a85cc06},\r\naffiliation={Division of Glycoscience, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, United Kingdom; Institute for Cell and Molecular Biosciences, Newcastle University, Medical School, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St Petersburg 188300, Russian Federation},\r\nabstract={The desire for improved methods of biomass conversion into fuels and feedstocks has re-awakened interest in the enzymology of plant cell wall degradation. The complex polysaccharide xyloglucan is abundant in plant matter, where it may account for up to 20% of the total primary cell wall carbohydrates. Despite this, few studies have focused on xyloglucan saccharification, which requires a consortium of enzymes including endo-xyloglucanases, α-xylosidases, β-galactosidases and α-L-fucosidases, among others. In the present paper, we show the characterization of Xyl31A, a key α-xylosidase in xyloglucan utilization by the model Gram-negative soil saprophyte Cellvibrio japonicus. CjXyl31A exhibits high regiospecificity for the hydrolysis of XGOs (xylogluco-oligosaccharides), with a particular preference for longer substrates. Crystallographic structures of both the apo enzyme and the trapped covalent 5-fluoro-β-xylosyl-enzyme intermediate, together with docking studies with the XXXG heptasaccharide, revealed, for the first time in GH31 (glycoside hydrolase family 31), the importance of a PA14 domain insert in the recognition of longer oligosaccharides by extension of the active-site pocket. The observation that CjXyl31A was localized to the outer membrane provided support for a biological model of xyloglucan utilization by C. japonicus, in which XGOs generated by the action of a secreted endoxyloglucanase are ultimately degraded in close proximity to the cell surface. Moreover, the present study diversifies the toolbox of glycosidases for the specific modification and saccharification of cell wall polymers for biotechnological applications. © The Authors Journal compilation © 2011 Biochemical Society.},\r\nauthor_keywords={Enzymology;  Hemicellulose;  Plant cell wall;  Saccharification;  Xyloglucan},\r\ncorrespondence_address1={Brumer, H.; Division of Glycoscience, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; email: harry@biotech.kth.se},\r\nissn={02646021},\r\ncoden={BIJOA},\r\npubmed_id={21426303},\r\nlanguage={English},\r\nabbrev_source_title={Biochem. J.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2009\n \n \n (5)\n \n \n

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\n \n\n \n \n \n \n \n \n A real-time fluorogenic assay for the visualization of glycoside hydrolase activity in planta.\n \n \n \n \n\n\n \n Ibatullin, F.; Banasiak, A.; Baumann, M.; Greffe, L.; Takahashi, J.; Mellerowicz, E.; and Brumer, H.\n\n\n \n\n\n\n Plant Physiology, 151(4): 1741-1750. 2009.\n cited By 17\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 abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Ibatullin20091741,\r\nauthor={Ibatullin, F.M. and Banasiak, A. and Baumann, M.J. and Greffe, L. and Takahashi, J. and Mellerowicz, E.J. and Brumer, H.},\r\ntitle={A real-time fluorogenic assay for the visualization of glycoside hydrolase activity in planta},\r\njournal={Plant Physiology},\r\nyear={2009},\r\nvolume={151},\r\nnumber={4},\r\npages={1741-1750},\r\ndoi={10.1104/pp.109.147439},\r\nnote={cited By 17},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-71049171637&doi=10.1104%2fpp.109.147439&partnerID=40&md5=ab771a8e83aebb30992520d40ba96710},\r\naffiliation={School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, SE-10691 Stockholm, Sweden; Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biology Division, Gatchina, St. Petersburg 188300, Russian Federation; Department of Forest Genetics and Plant Physiology, SLU, Umea Plant Science Centre, 90183 Umea, Sweden; Institute of Plant Biology, University of Wroclaw, 50-328 Wroclaw, Poland},\r\nabstract={There currently exists a diverse array of molecular probes for the in situ localization of polysaccharides, nucleic acids, and proteins in plant cells, including reporter enzyme strategies (e.g. protein-glucuronidase fusions). In contrast, however, there is a paucity of methods for the direct analysis of endogenous glycoside hydrolases and transglycosidases responsible for cell wall remodeling. To exemplify the potential of fluorogenic resorufin glycosides to address this issue, a resorufin β-glycoside of a xylogluco-oligosaccharide (XXXG-β-Res) was synthesized as a specific substrate for in planta analysis of XEH activity. The resorufin aglycone is particularly distinguished for high sensitivity in muro assays due to a low pKa (5.8) and large extinction coefficient (ε 62,000 M-1cm-1), long-wavelength fluorescence (excitation 571 nm/emission 585 nm), and high quantum yield (0.74) of the corresponding anion. In vitro analyses demonstrated that XXXG-β-Res is hydrolyzed by the archetypal plant XEH, nasturtium (Tropaeolum majus) NXG1, with classical Michaelis-Menten substrate saturation kinetics and a linear dependence on both enzyme concentration and incubation time. Further, XEH activity could be visualized in real time by observing the localized increase in fluorescence in germinating nasturtium seeds and Arabidopsis (Arabidopsis thaliana) inflorescent stems by confocal microscopy. Importantly, this new in situ XEH assay provides an essential complement to the in situ xyloglucan endotransglycosylase assay, thus allowing delineation of the disparate activities encoded by xyloglucan endotransglycosylase/hydrolase genes directly in plant tissues. The observation that XXXG-β-Res is also hydrolyzed by diverse microbial XEHs indicates that this substrate, and resorufin glycosides in general, may find broad applicability for the analysis of wall restructuring by polysaccharide hydrolases during morphogenesis and plant-microbe interactions. © 2009 American Society of Plant Biologists.},\r\ncorrespondence_address1={Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, SE-10691 Stockholm, Sweden; email: harry@biotech.kth.se},\r\nissn={00320889},\r\ncoden={PLPHA},\r\npubmed_id={19783642},\r\nlanguage={English},\r\nabbrev_source_title={Plant Physiol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n There currently exists a diverse array of molecular probes for the in situ localization of polysaccharides, nucleic acids, and proteins in plant cells, including reporter enzyme strategies (e.g. protein-glucuronidase fusions). In contrast, however, there is a paucity of methods for the direct analysis of endogenous glycoside hydrolases and transglycosidases responsible for cell wall remodeling. To exemplify the potential of fluorogenic resorufin glycosides to address this issue, a resorufin β-glycoside of a xylogluco-oligosaccharide (XXXG-β-Res) was synthesized as a specific substrate for in planta analysis of XEH activity. The resorufin aglycone is particularly distinguished for high sensitivity in muro assays due to a low pKa (5.8) and large extinction coefficient (ε 62,000 M-1cm-1), long-wavelength fluorescence (excitation 571 nm/emission 585 nm), and high quantum yield (0.74) of the corresponding anion. In vitro analyses demonstrated that XXXG-β-Res is hydrolyzed by the archetypal plant XEH, nasturtium (Tropaeolum majus) NXG1, with classical Michaelis-Menten substrate saturation kinetics and a linear dependence on both enzyme concentration and incubation time. Further, XEH activity could be visualized in real time by observing the localized increase in fluorescence in germinating nasturtium seeds and Arabidopsis (Arabidopsis thaliana) inflorescent stems by confocal microscopy. Importantly, this new in situ XEH assay provides an essential complement to the in situ xyloglucan endotransglycosylase assay, thus allowing delineation of the disparate activities encoded by xyloglucan endotransglycosylase/hydrolase genes directly in plant tissues. The observation that XXXG-β-Res is also hydrolyzed by diverse microbial XEHs indicates that this substrate, and resorufin glycosides in general, may find broad applicability for the analysis of wall restructuring by polysaccharide hydrolases during morphogenesis and plant-microbe interactions. © 2009 American Society of Plant Biologists.\n

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\n \n\n \n \n \n \n \n \n Reaction of N-Fmoc aspartic anhydride with glycosylamines: a simple entry to N-glycosyl asparagines.\n \n \n \n \n\n\n \n Ibatullin, F.; and Selivanov, S.\n\n\n \n\n\n\n Tetrahedron Letters, 50(46): 6351-6354. 2009.\n cited By 6\n\n\n\n
\n\n\n\n \n \n $\"Reaction$ 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

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@ARTICLE{Ibatullin20096351,\r\nauthor={Ibatullin, F.M. and Selivanov, S.I.},\r\ntitle={Reaction of N-Fmoc aspartic anhydride with glycosylamines: a simple entry to N-glycosyl asparagines},\r\njournal={Tetrahedron Letters},\r\nyear={2009},\r\nvolume={50},\r\nnumber={46},\r\npages={6351-6354},\r\ndoi={10.1016/j.tetlet.2009.08.106},\r\nnote={cited By 6},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-70349769609&doi=10.1016%2fj.tetlet.2009.08.106&partnerID=40&md5=23b38427c9b98a114e65059accac2e3c},\r\naffiliation={Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina, 188300, Russian Federation; Chemical Department, Petersburg State University, St.-Petersburg, Russian Federation},\r\nabstract={The reaction of N-Fmoc-aspartic anhydride with glycosyl amines in DMSO selectively leads to the formation of β-substituted products, thus providing a simple and efficient route to N-glycosyl asparagine derivatives, the building blocks for glycopeptide synthesis. © 2009 Elsevier Ltd. All rights reserved.},\r\ncorrespondence_address1={Ibatullin, F.M.; Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina, 188300, Russian Federation; email: ibatullin@omrb.pnpi.spb.ru},\r\nissn={00404039},\r\ncoden={TELEA},\r\nlanguage={English},\r\nabbrev_source_title={Tetrahedron Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Functional characterization of xyloglucan glycosynthases from GH7, GH12, and GH16 scaffolds.\n \n \n \n \n\n\n \n Gullfot, F.; Ibatullin, F.; Sundqvist, G.; Davies, G.; and Brumer, H.\n\n\n \n\n\n\n Biomacromolecules, 10(7): 1782-1788. 2009.\n cited By 14\n\n\n\n
\n\n\n\n \n \n $\"Functional$ 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

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@ARTICLE{Gullfot20091782,\r\nauthor={Gullfot, F. and Ibatullin, F.M. and Sundqvist, G. and Davies, G.J. and Brumer, H.},\r\ntitle={Functional characterization of xyloglucan glycosynthases from GH7, GH12, and GH16 scaffolds},\r\njournal={Biomacromolecules},\r\nyear={2009},\r\nvolume={10},\r\nnumber={7},\r\npages={1782-1788},\r\ndoi={10.1021/bm900215p},\r\nnote={cited By 14},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-67650459915&doi=10.1021%2fbm900215p&partnerID=40&md5=e9731792db7c4f0140361b762f4a62c4},\r\naffiliation={Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), 106 91 Stockholm, Sweden; Petersburg Nuclear Physics Institute, Molecular and Radiation Biology Division, Russian Academy of Science, Gatchina, St. Petersburg 188300, Russian Federation; York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5YW, United Kingdom},\r\nabstract={Glycosynthases, hydrolytically inactive mutant glycosidases that catalyze glycosylation reactions using glycosyl fluoride donor substrates, are emerging as useful tools for the synthesis of large, complex polysaccharides [Faijes, M.; Planas, A. Carbohydr. Res. 2007, 342, 1581-1594]. Guided by wild-type xyloglucanase activity, we have produced and characterized new glycosynthases for the synthesis of xyloglucan oligo- and polysaccharides, based on family GH7, GH12, and GH16 scaffolds. The Humicola insolens GH7 glycosynthase, HiCel7B E197S, is capable of synthesizing nongalactosylated, XXXG-based homoxyloglucan up to Mw 60000 [G = Glcβ (1→4); X = Xylα(1→6) Glcβ(1→4); L = Galβ(1→2)Xylα(1→6) Glcβ(1→4)], which is among the largest products so far obtained with glycosynthase technology. Novel glycosynthases based on the GH16 xyloglucan hydrolase from Tropaeolum majus (nasturtium), TmNXG1, are capable of synthesizing XLLG-based xyloglucan oligosaccharides at rates feasible for preparative synthesis, thus providing an essential expansion of product range. Finally, a new glycosynthase based on the recently characterized GH12 xyloglucanase from Bacillus licheniformis, BlXG12 E155A, can perform the condensation of xyloglucosyl fluorides, albeit at poor rates. Altogether, the high catalytic efficiency demonstrated by HiCel7B E197S and the extended product range provided by TmNXG1 E94A are key achievements toward a robust and versatile method for the preparative synthesis of homogeneous xyloglucans with regular substitution patterns not available in nature. Such compounds enable in vitro experimental studies regarding the role of particular structural elements for xyloglucan properties and its interaction with cellulose. © 2009 American Chemical Society.},\r\ncorrespondence_address1={Brumer, H.; Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), 106 91 Stockholm, Sweden; email: harry@biotech.kth.se},\r\nissn={15257797},\r\ncoden={BOMAF},\r\npubmed_id={19419143},\r\nlanguage={English},\r\nabbrev_source_title={Biomacromolecules},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n KORRIGAN1 and its aspen homolog PttCel9A1 decrease cellulose crystallinity in arabidopsis stems.\n \n \n \n \n\n\n \n \n\n\n \n\n\n\n Plant and Cell Physiology, 50(6): 1099-1115. 2009.\n cited By 82\n\n\n\n
\n\n\n\n \n \n $\"KORRIGAN1$ 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

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\n \n\n \n \n \n \n \n \n Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei.\n \n \n \n \n\n\n \n Eneyskaya, E.; Sundqvist, G.; Golubev, A.; Ibatullin, F.; Ivanen, D.; Shabalin, K.; Brumer, H.; and Kulminskaya, A.\n\n\n \n\n\n\n Biochimie, 91(5): 632-638. 2009.\n cited By 18\n\n\n\n
\n\n\n\n \n \n $\"Transglycosylating$ 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

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@ARTICLE{Eneyskaya2009632,\r\nauthor={Eneyskaya, E.V. and Sundqvist, G. and Golubev, A.M. and Ibatullin, F.M. and Ivanen, D.R. and Shabalin, K.A. and Brumer, H. and Kulminskaya, A.A.},\r\ntitle={Transglycosylating and hydrolytic activities of the β-mannosidase from Trichoderma reesei},\r\njournal={Biochimie},\r\nyear={2009},\r\nvolume={91},\r\nnumber={5},\r\npages={632-638},\r\ndoi={10.1016/j.biochi.2009.03.009},\r\nnote={cited By 18},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-64049097092&doi=10.1016%2fj.biochi.2009.03.009&partnerID=40&md5=2eb0f1a7d4883969c402b5c2be2284dd},\r\naffiliation={Petersburg Nuclear Physics Institute, Russian Academy of Science, Molecular and Radiation Biophysics Division, Orlova Roscha, Gatchina, 188300 Leningrad District, Russian Federation; School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, 106 91 Stockholm, Sweden},\r\nabstract={A purified β-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 β-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 β-(1 → 4) and β-(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. © 2009 Elsevier Masson SAS. All rights reserved.},\r\nauthor_keywords={β-Mannosidase;  Organic solvents;  p-Nitrophenyl β-mannooligosaccharides;  Transglycosylation},\r\nfunding_details={Российский Фонд Фундаментальных Исследований (РФФИ)07-04-01071-a},\r\n}

\n

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

\n

\n \n 2008\n \n \n (1)\n \n \n

\n

\n \n \n

\n \n\n \n \n \n \n \n \n Kinetic analyses of retaining endo-(Xylo)glucanases from plant and microbial sources using new chromogenic xylogluco-oligosaccharide aryl glycosides.\n \n \n \n \n\n\n \n Ibatullin, F.; Baumann, M.; Greffe, L.; and Brumer, H.\n\n\n \n\n\n\n Biochemistry, 47(29): 7762-7769. 2008.\n cited By 24\n\n\n\n
\n\n\n\n \n \n $\"Kinetic$ 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

@ARTICLE{Ibatullin20087762,\r\nauthor={Ibatullin, F.M. and Baumann, M.J. and Greffe, L. and Brumer, H.},\r\ntitle={Kinetic analyses of retaining endo-(Xylo)glucanases from plant and microbial sources using new chromogenic xylogluco-oligosaccharide aryl glycosides},\r\njournal={Biochemistry},\r\nyear={2008},\r\nvolume={47},\r\nnumber={29},\r\npages={7762-7769},\r\ndoi={10.1021/bi8009168},\r\nnote={cited By 24},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-47649125408&doi=10.1021%2fbi8009168&partnerID=40&md5=66aea507deaaf913166a027f9f76526d},\r\naffiliation={School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, SE-106 91 Stockholm, Sweden; Petersburg Nuclear Physics Institute, Molecular and Radiation Biology Division, Russian Academy of Science, Gatchina, St. Petersburg 188300, Russian Federation},\r\nabstract={A library of phenyl β-glycosides of xylogluco-oligosaccharides was synthesized via a chemoenzymatic approach to produce new, specific substrates for xyloglucanases. Tamarind xyloglucan was completely hydrolyzed to four, variably galactosylated component oligosaccharides based on Glc4 backbones, using a Trichoderma endo-glucanase mixture. Oligosaccharide complexity could be further reduced by β-galactosidase treament. Subsequent per-O-acetylation, α-bromination, phase-transfer glycosylation, and Zemplén deprotection yielded phenyl glycosides of XXXG and XLLG oligosaccharides with a broad range of aglycon pKa values. Kinetic and product analysis of the action of the archetypal plant endo-xyloglucanase, Tropaeolum majus NXG1, on these compounds indicated that formation of the glycosyl-enzyme intermediate was rate-limiting in the case of phenol leaving groups with pKa values of &gt;7, leading exclusively to substrate hydrolysis. Conversely, substrates with aglycon pKa values of 5.4 gave rise to a significant amount of transglycosylation products, indicating a change in the relative rates of formation and breakdown of the glycosyl-enzyme intermediate for these faster substrates. Notably, comparison of the initial rates of XXXG-Ar and XLLG-Ar conversion indicated that catalysis by TmNXG1 was essentially insensitive to the presence of galactose in the negative subsites for all leaving groups. More broadly, analysis of a selection of enzymes from CAZy families GH 5, 12, and 16 indicated that the phenyl glycosides are substrates for anomeric configuration-retaining endo-xyloglucanases but are not substrates for strict xyloglucan endo-transglycosylases (XETs). The relative activities of the GH 5, 12, and 16 endo-xyloglucanases toward GGGG-CNP, XXXG-CNP, and XLLG-CNP reflected those observed using analogous high molar mass polysaccharides. These new chromogenic substrates may thus find wide application in the discovery, screening, and detailed kinetic analysis of new xyloglucan-active enzymes. © 2008 American Chemical Society.},\r\ncorrespondence_address1={Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, SE-106 91 Stockholm, Sweden; email: harry@biotech.kth.se},\r\nissn={00062960},\r\ncoden={BICHA},\r\npubmed_id={18627132},\r\nlanguage={English},\r\nabbrev_source_title={Biochemistry},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

\n\n\n

\n A library of phenyl β-glycosides of xylogluco-oligosaccharides was synthesized via a chemoenzymatic approach to produce new, specific substrates for xyloglucanases. Tamarind xyloglucan was completely hydrolyzed to four, variably galactosylated component oligosaccharides based on Glc4 backbones, using a Trichoderma endo-glucanase mixture. Oligosaccharide complexity could be further reduced by β-galactosidase treament. Subsequent per-O-acetylation, α-bromination, phase-transfer glycosylation, and Zemplén deprotection yielded phenyl glycosides of XXXG and XLLG oligosaccharides with a broad range of aglycon pKa values. Kinetic and product analysis of the action of the archetypal plant endo-xyloglucanase, Tropaeolum majus NXG1, on these compounds indicated that formation of the glycosyl-enzyme intermediate was rate-limiting in the case of phenol leaving groups with pKa values of >7, leading exclusively to substrate hydrolysis. Conversely, substrates with aglycon pKa values of 5.4 gave rise to a significant amount of transglycosylation products, indicating a change in the relative rates of formation and breakdown of the glycosyl-enzyme intermediate for these faster substrates. Notably, comparison of the initial rates of XXXG-Ar and XLLG-Ar conversion indicated that catalysis by TmNXG1 was essentially insensitive to the presence of galactose in the negative subsites for all leaving groups. More broadly, analysis of a selection of enzymes from CAZy families GH 5, 12, and 16 indicated that the phenyl glycosides are substrates for anomeric configuration-retaining endo-xyloglucanases but are not substrates for strict xyloglucan endo-transglycosylases (XETs). The relative activities of the GH 5, 12, and 16 endo-xyloglucanases toward GGGG-CNP, XXXG-CNP, and XLLG-CNP reflected those observed using analogous high molar mass polysaccharides. These new chromogenic substrates may thus find wide application in the discovery, screening, and detailed kinetic analysis of new xyloglucan-active enzymes. © 2008 American Chemical Society.\n

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\n \n 2007\n \n \n (3)\n \n \n

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\n \n \n

\n \n\n \n \n \n \n \n \n Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12.\n \n \n \n \n\n\n \n Gloster, T.; Ibatullin, F.; Macauley, K.; Eklöf, J.; Roberts, S.; Turkenburg, J.; Bjørnvad, M.; Jørgensen, P.; Danielsen, S.; Johansen, K.; Borchert, T.; Wilson, K.; Brumer, H.; and Davies, G.\n\n\n \n\n\n\n Journal of Biological Chemistry, 282(26): 19177-19189. 2007.\n cited By 74\n\n\n\n
\n\n\n\n \n \n $\"Characterization$ 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

@ARTICLE{Gloster200719177,\r\nauthor={Gloster, T.M. and Ibatullin, F.M. and Macauley, K. and Eklöf, J.M. and Roberts, S. and Turkenburg, J.P. and Bjørnvad, M.E. and Jørgensen, P.L. and Danielsen, S. and Johansen, K.S. and Borchert, T.V. and Wilson, K.S. and Brumer, H. and Davies, G.J.},\r\ntitle={Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12},\r\njournal={Journal of Biological Chemistry},\r\nyear={2007},\r\nvolume={282},\r\nnumber={26},\r\npages={19177-19189},\r\ndoi={10.1074/jbc.M700224200},\r\nnote={cited By 74},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34547134972&doi=10.1074%2fjbc.M700224200&partnerID=40&md5=bbe6f4b1572c278887981d71ebbc6bee},\r\naffiliation={York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; Novozymes A/S, Brudelysvej 26, 1U1.23, DK-2880 Bagsvaerd, Denmark; Swedish Research Council, Sweden},\r\nabstract={The plant cell wall is a complex material in which the cellulose microfibrils are embedded within a mesh of other polysaccharides, some of which are loosely termed "hemicellulose." One such hemicellulose is xyloglucan, which displays a β-1,4-linked D-glucose backbone substituted with xylose, galactose, and occasionally fucose moieties. Both xyloglucan and the enzymes responsible for its modification and degradation are finding increasing prominence, reflecting both the drive for enzymatic biomass conversion, their role in detergent applications, and the utility of modified xyloglucans for cellulose fiber modification. Here we present the enzymatic characterization and three-dimensional structures in ligand-free and xyloglucan-oligosaccharide complexed forms of two distinct xyloglucanases from glycoside hydrolase families GH5 and GH12. The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (β/α)8 and β-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated. For the β-jelly roll enzyme topology of GH12, binding of xylosyl and pendant galactosyl moieties is tolerated, but the enzyme is similarly competent in the degradation of unbranched glucans. In the case of the (β/α)8 GH5 enzyme, kinetically productive interactions are made with both xylose and galactose substituents, as reflected in both a high specific activity on xyloglucan and the kinetics of a series of aryl glycosides. The differential strategies for the accommodation of the side chains of xyloglucan presumably facilitate the action of these microbial hydrolases in milieus where diverse and differently substituted substrates may be encountered. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.},\r\ncorrespondence_address1={Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; email: harry@biotech.kth.se},\r\nissn={00219258},\r\ncoden={JBCHA},\r\npubmed_id={17376777},\r\nlanguage={English},\r\nabbrev_source_title={J. Biol. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Xyloglucan endo-transglycosylase (XET) functions in gelatinous layers of tension wood fibers in poplar - A glimpse into the mechanism of the balancing act of trees.\n \n \n \n \n\n\n \n Nishikubo, N.; Awano, T.; Banasiak, A.; Bourquin, V.; Ibatullin, F.; Funada, R.; Brumer, H.; Teeri, T.; Hayashi, T.; Sundberg, B.; and Mellerowicz, E.\n\n\n \n\n\n\n Plant and Cell Physiology, 48(6): 843-855. 2007.\n cited By 121\n\n\n\n
\n\n\n\n \n \n $\"Xyloglucan$ 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

@ARTICLE{Nishikubo2007843,\r\nauthor={Nishikubo, N. and Awano, T. and Banasiak, A. and Bourquin, V. and Ibatullin, F. and Funada, R. and Brumer, H. and Teeri, T.T. and Hayashi, T. and Sundberg, B. and Mellerowicz, E.J.},\r\ntitle={Xyloglucan endo-transglycosylase (XET) functions in gelatinous layers of tension wood fibers in poplar - A glimpse into the mechanism of the balancing act of trees},\r\njournal={Plant and Cell Physiology},\r\nyear={2007},\r\nvolume={48},\r\nnumber={6},\r\npages={843-855},\r\ndoi={10.1093/pcp/pcm055},\r\nnote={cited By 121},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34548424199&doi=10.1093%2fpcp%2fpcm055&partnerID=40&md5=d5a6a4fd113f104ee74f0f91ffe68c9a},\r\naffiliation={Department of Forest Genetics and Plant Physiology, Umea Plant Science Center, SLU, S901 83 Umea, Sweden; Department of Biotechnology, Royal Insitute of Technology (KTH), S-106 91 Stockholm, Sweden; Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu-Tokyo 183-8509, Japan; Research Institute for Sustainable Humanosphere, Kyoto University, Kyoto, 611-0011, Japan; RIKEN, Plant Science Center, 1-7-22 Suehiro-cho, Yokohama, Kanagawa, 230-0045, Japan; Division of Forest and Biomaterials Science, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan; Institute of Plant Biology, University of Wroclaw, Kanonia 6/8, 50-328, Wroclaw, Poland},\r\nabstract={Tension wood is a specialized tissue of deciduous trees that functions in bending woody stems to optimize their position in space. Tension wood fibers that develop on one side of the stem have an increased potency to shrink compared with fibers on the opposite side, thus creating a bending moment. It is believed that the gelatinous (G) cell wall layer containing almost pure cellulose of tension wood fibers is pivotal to their shrinking. By analyzing saccharide composition and linkage in isolated G-layers of poplar, we found that they contain some matrix components in addition to cellulose, of which xyloglucan is the most abundant. Xyloglucan, xyloglucan endo-transglycosylase (XET) activity and xyloglucan endo-transglycosylase/hydrolase (XTH) gene products were detected in developing G-layers by labeling using CCRC-M1 monoclonal antibody, in situ incorporation of XXXG-SR and the polyclonal antibody to poplar PttXET16-34, respectively, indicating that xyloglucan is incorporated into the G-layer during its development. Moreover, several XTH transcripts were altered and were generally up-regulated in developing tension wood compared with normal wood. In mature G-fibers, XTH gene products were detected in the G-layers while the XET activity was evident in the adjacent S2 wall layer. We propose that XET activity is essential for G-fiber shrinking by repairing xyloglucan cross-links between G- and S 2-layers and thus maintaining their contact. Surprisingly, XTH gene products and XET activity persisted in mature G-fibers for several years, suggesting that the enzyme functions after cell death repairing the cross-links as they are being broken during the shrinking process. © The Author 2005. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.},\r\nauthor_keywords={Gravity responses;  Populus;  Reaction wood;  Secondary wall;  Wood formation;  Xylogenesis},\r\ncorrespondence_address1={Mellerowicz, E.J.; Department of Forest Genetics and Plant Physiology, Umea Plant Science Center, SLU, S901 83 Umea, Sweden; email: ewa.mellerowicz@genfys.slu.se},\r\nissn={00320781},\r\ncoden={PCPHA},\r\npubmed_id={17504814},\r\nlanguage={English},\r\nabbrev_source_title={Plant Cell Physiol.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n\n\n

\n \n\n \n \n \n \n \n \n Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants.\n \n \n \n \n\n\n \n Piens, K.; Henriksson, A.; Gullfot, F.; Lopez, M.; Fauré, R.; Ibatullin, F.; Teeri, T.; Driguez, H.; and Brumer, H.\n\n\n \n\n\n\n Organic and Biomolecular Chemistry, 5(24): 3971-3978. 2007.\n cited By 20\n\n\n\n
\n\n\n\n \n \n $\"Glycosynthase$ 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

@ARTICLE{Piens20073971,\r\nauthor={Piens, K. and Henriksson, A.-M. and Gullfot, F. and Lopez, M. and Fauré, R. and Ibatullin, F.M. and Teeri, T.T. and Driguez, H. and Brumer, H.},\r\ntitle={Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants},\r\njournal={Organic and Biomolecular Chemistry},\r\nyear={2007},\r\nvolume={5},\r\nnumber={24},\r\npages={3971-3978},\r\ndoi={10.1039/b714570e},\r\nnote={cited By 20},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-36749095084&doi=10.1039%2fb714570e&partnerID=40&md5=2db6d80ea903a5f97675e2ec94acd10b},\r\naffiliation={School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; Laboratory for Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry, Physiology and Microbiology, Ghent University, K.L.-Ledeganckstraat 35, 9000, Ghent, Belgium; Centre de Recherches sur les Macromolécules Végé tales, (CERMAV-CNRS), B.P. 53, F-38041, Grenoble cedex 9, France; Joseph Fourier University, France; Institut de Chimie Moléculaire de Grenoble FR-CNRS 2607, France},\r\nabstract={Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509-519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of α-xylogluco- oligosaccharyl fluoride donors XXXGαF and XLLGαF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGαF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications. © The Royal Society of Chemistry.},\r\ncorrespondence_address1={Brumer, H.; School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91, Stockholm, Sweden; email: harry@biotech.kth.se},\r\npublisher={Royal Society of Chemistry},\r\nissn={14770520},\r\ncoden={OBCRA},\r\nlanguage={English},\r\nabbrev_source_title={Org. Biomol. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2005\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Ionic-molecular mechanisms of catalytic oxidation of thiole compounds in presence of copper ions.\n \n \n \n \n\n\n \n Bagnyan, G.; Koroleva, I.; Soroka, N.; Ufimtsev, A.; Skurlatov, Y.; Dedenchuk, I.; Semenyak, L.; and Shtamm, E.\n\n\n \n\n\n\n Khimicheskaya Fizika, 24(6): 51-63. 2005.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"Ionic-molecular$ 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{Bagnyan200551,\r\nauthor={Bagnyan, G.A. and Koroleva, I.K. and Soroka, N.V. and Ufimtsev, A.V. and Skurlatov, Yu.I. and Dedenchuk, I.V. and Semenyak, L.V. and Shtamm, E.V.},\r\ntitle={Ionic-molecular mechanisms of catalytic oxidation of thiole compounds in presence of copper ions},\r\njournal={Khimicheskaya Fizika},\r\nyear={2005},\r\nvolume={24},\r\nnumber={6},\r\npages={51-63},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-26844535066&partnerID=40&md5=8f153e37bc64d969f302adf9fd9a5cc0},\r\nissn={0207401X},\r\ncoden={KHFID},\r\nabbrev_source_title={Khim. Fiz.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2004\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Kinetics of the catalytic oxidation reactions of thiol compounds in aqueous solutions in the presence of copper ions.\n \n \n \n \n\n\n \n Bagiyan, G.; Koroleva, I.; Soroka, N.; and Ufimtsev, A.\n\n\n \n\n\n\n Kinetics and Catalysis, 45(3): 372-380. 2004.\n cited By 15\n\n\n\n
\n\n\n\n \n \n $\"Kinetics$ 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

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@ARTICLE{Bagiyan2004372,\r\nauthor={Bagiyan, G.A. and Koroleva, I.K. and Soroka, N.V. and Ufimtsev, A.V.},\r\ntitle={Kinetics of the catalytic oxidation reactions of thiol compounds in aqueous solutions in the presence of copper ions},\r\njournal={Kinetics and Catalysis},\r\nyear={2004},\r\nvolume={45},\r\nnumber={3},\r\npages={372-380},\r\ndoi={10.1023/B:KICA.0000032171.81652.91},\r\nnote={cited By 15},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042711385&doi=10.1023%2fB%3aKICA.0000032171.81652.91&partnerID=40&md5=80319408f65972a0210cc5b6919581aa},\r\naffiliation={Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, Leningrad O., Russian Federation},\r\nabstract={The kinetics of the catalytic oxidation reactions of thiol compounds with molecular oxygen in aqueous solutions in the presence of copper ions was studied in relation to the structures of oxidized thiols and the pH of the solution. A modified procedure used for the determination of O 2 allowed us to obtain the kinetic characteristics of more than 30 thiols over a wide pH range. We found that weakly chelating thiols exhibited a first order of reaction with respect to Cu + and O 2 under conditions when the (Cu +)(RS -) 2 complex occurred. In the oxidation of strongly chelating thiols in an alkaline medium, the order of reaction with respect to Cu + was equal to 2, and the rate of reaction was independent of O 2. We found that the introduction of small amounts of strongly chelating thiols into Cu + solutions containing difficult-to-oxidize mercaptans resulted in a dramatic acceleration of mercaptan oxidation. We hypothesized that O 2 was effectively bound to the (Cu +)(RS -) 2 complexes in an alkaline medium in the case of strongly chelating thiols, and this was not the case with the complexes of weakly chelating thiols.},\r\ncorrespondence_address1={Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, Leningrad O.Russian Federation},\r\nissn={00231584},\r\ncoden={KICAA},\r\nlanguage={English},\r\nabbrev_source_title={Kinet. Catal.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\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 Reaction of 1,2-trans-glycosyl acetates with thiourea: A new entry to 1-thiosugars.\n \n \n \n \n\n\n \n Ibatullin, F.; Shabalin, K.; Jänis, J.; and Shavva, A.\n\n\n \n\n\n\n Tetrahedron Letters, 44(43): 7961-7964. 2003.\n cited By 63\n\n\n\n
\n\n\n\n \n \n $\"Reaction$ 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

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@ARTICLE{Ibatullin20037961,\r\nauthor={Ibatullin, F.M. and Shabalin, K.A. and Jänis, J.V. and Shavva, A.G.},\r\ntitle={Reaction of 1,2-trans-glycosyl acetates with thiourea: A new entry to 1-thiosugars},\r\njournal={Tetrahedron Letters},\r\nyear={2003},\r\nvolume={44},\r\nnumber={43},\r\npages={7961-7964},\r\ndoi={10.1016/j.tetlet.2003.08.120},\r\nnote={cited By 63},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141485298&doi=10.1016%2fj.tetlet.2003.08.120&partnerID=40&md5=9f2d0d8eeca517c0fc439d6beec3b1df},\r\naffiliation={Molec./Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation; Department of Chemistry, University of Joensuu, Joensuu, Finland; Chemical Department, Petersburg State University, St.-Petersburg, Russian Federation},\r\nabstract={The reaction of 1,2-trans-glycosyl acetates with thiourea under boron trifluoride etherate catalysis affording acetylated S-glycosyl isothiourea derivatives is described. The isothiourea derivatives obtained can be readily transformed into the desired 1-thiosugar derivative by reaction with triethylamine and subsequent alkylation or acylation of the in situ formed 1-thioaldose. © 2003 Elsevier Ltd. All rights reserved.},\r\ncorrespondence_address1={Ibatullin, F.M.; Molec./Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation},\r\npublisher={Elsevier Ltd},\r\nissn={00404039},\r\ncoden={TELEA},\r\nlanguage={English},\r\nabbrev_source_title={Tetrahedron Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n\n\n

\n \n\n \n \n \n \n \n \n Oxidation of aminothiols by molecular oxygen catalyzed by copper ions. Stoichiometry of the reaction.\n \n \n \n \n\n\n \n Bagiyan, G.; Koroleva, I.; Soroka, N.; and Ufimtsev, A.\n\n\n \n\n\n\n Russian Chemical Bulletin, 52(5): 1129-1134. 2003.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"Oxidation$ 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

@ARTICLE{Bagiyan20031129,\r\nauthor={Bagiyan, G.A. and Koroleva, I.K. and Soroka, N.V. and Ufimtsev, A.V.},\r\ntitle={Oxidation of aminothiols by molecular oxygen catalyzed by copper ions. Stoichiometry of the reaction},\r\njournal={Russian Chemical Bulletin},\r\nyear={2003},\r\nvolume={52},\r\nnumber={5},\r\npages={1129-1134},\r\ndoi={10.1023/A:1024757207872},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037491907&doi=10.1023%2fA%3a1024757207872&partnerID=40&md5=eecab9b4d48260e2c63e8259ac9ad98d},\r\naffiliation={B. P. Konstantinov Petersburg I., Russian Academy of Sciences, 1 Orlova Roshcha, 188300 Gatchina, Leningrad Region, Russian Federation},\r\nabstract={Catalysis of oxidation of aminothiols by copper ions was studied depending on the structure of aminothiols and pH of the medium. The catalytic reaction proceeds in the inner coordination sphere of Cu+. At pH 7-9, oxidation of bidentate aminothiols involves reduction of O2 to H 2O2. At pH 9-13, oxidation of chelating aminothiols is accompanied by reduction of O2 to H2O, whereas oxidation of weak-chelating aminothiols still proceeds by the former mechanism. In this process, the thiolate anions coordinated to the Cu+ ions lose one electron each and are oxidized to amino disulfides, which go from the inner sphere of the Cu+ complex into a solution. Procedures developed for the determination of amino disulfides, the chemiluminescence determination of H2O2 in the presence of aminothiols as luminescence quenchers, and a modified polarographic procedure for the determination of O2 allowed us to establish that oxidation of aminothiols is not accompanied by catalytic decomposition of H2O2 that formed.},\r\nauthor_keywords={Amino disulfides;  Aminothiols;  Catalysis;  Copper ions;  Hydrogen peroxide;  Molecular oxygen;  Oxidation;  Stoichiometry;  Water},\r\ncorrespondence_address1={Bagiyan, G.A.; B. P. Konstantinov Petersburg I., Russian Academy of Sciences, 1 Orlova Roshcha, 188300 Gatchina, Leningrad Region, Russian Federation; email: heinrich@omrb.pnpi.spb.ru},\r\nissn={10665285},\r\nlanguage={English},\r\nabbrev_source_title={Russ. Chem. Bull.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

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

\n\n\n

\n \n\n \n \n \n \n \n \n Oxidation of thiol compounds by molecular oxygen in aqueous solutions.\n \n \n \n \n\n\n \n Bagiyan, G.; Koroleva, I.; Soroka, N.; and Ufimtsev, A.\n\n\n \n\n\n\n Russian Chemical Bulletin, 52(5): 1135-1141. 2003.\n cited By 88\n\n\n\n
\n\n\n\n \n \n $\"Oxidation$ 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

@ARTICLE{Bagiyan20031135,\r\nauthor={Bagiyan, G.A. and Koroleva, I.K. and Soroka, N.V. and Ufimtsev, A.V.},\r\ntitle={Oxidation of thiol compounds by molecular oxygen in aqueous solutions},\r\njournal={Russian Chemical Bulletin},\r\nyear={2003},\r\nvolume={52},\r\nnumber={5},\r\npages={1135-1141},\r\ndoi={10.1023/A:1024761324710},\r\nnote={cited By 88},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037491906&doi=10.1023%2fA%3a1024761324710&partnerID=40&md5=065c254e54e52e2a60aed43d1e481d55},\r\naffiliation={B. P. Konstantinov Petersburg I., Russian Academy of Sciences, 1 Orlova Roshcha, 188300 Gatchina, Leningrad Region, Russian Federation},\r\nabstract={Side self-oxidation of thiols was studied. It was found that these reactions in neutral and alkaline solutions are induced by impurities of variable-valence metals. The ability of transition metals to catalyze oxidation of thiols changes in the order Cu > Mn > Fe > Ni ≫ Co. The plot of the self-oxidation rate vs. pH passes through a maximum whose position on the pH scale depends on both the nature of metal and the structure of the thiol oxidized. For thiols having different structures, the kinetic orders in reactions catalyzed by copper ions differently vary with pH, which is apparently associated with the formation of complexes possessing different catalytic activity.},\r\nauthor_keywords={Catalysis by copper ions;  Effect of the thiol structure on the kinetics;  Oxidation by molecular oxygen;  Thiols},\r\ncorrespondence_address1={Bagiyan, G.A.; B. P. Konstantinov Petersburg I., Russian Academy of Sciences, 1 Orlova Roshcha, 188300 Gatchina, Leningrad Region, Russian Federation; email: heinrich@omrb.pnpi.spb.ru},\r\nissn={10665285},\r\nlanguage={English},\r\nabbrev_source_title={Russ. Chem. Bull.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Complexes of Copper(I) with Dimercapto Compounds as Catalysts for Oxidation of Mercaptans and Hydrogen Sulfide with Molecular Oxygen in Aqueous Solutions.\n \n \n \n \n\n\n \n Bagiyan, G.; Koroleva, I.; Soroka, N.; and Ufimtsev, A.\n\n\n \n\n\n\n Russian Journal of Applied Chemistry, 76(1): 88-94. 2003.\n cited By 2\n\n\n\n
\n\n\n\n \n \n $\"Complexes$ 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

@ARTICLE{Bagiyan200388,\r\nauthor={Bagiyan, G.A. and Koroleva, I.K. and Soroka, N.V. and Ufimtsev, A.V.},\r\ntitle={Complexes of Copper(I) with Dimercapto Compounds as Catalysts for Oxidation of Mercaptans and Hydrogen Sulfide with Molecular Oxygen in Aqueous Solutions},\r\njournal={Russian Journal of Applied Chemistry},\r\nyear={2003},\r\nvolume={76},\r\nnumber={1},\r\npages={88-94},\r\ndoi={10.1023/A:1023300101895},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-1642491983&doi=10.1023%2fA%3a1023300101895&partnerID=40&md5=bdcca1f433e19c60441e5ac3786fd665},\r\naffiliation={Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, Leningrad Oblast, Russian Federation},\r\nabstract={The conditions for formation of complexes of copper(I) with mercapto compounds in aqueousalkaline solutions and the catalytic activity of these complexes in oxidation of mercaptans and hydrogen sulfide was studied. The kinetic characteristics of these catalysts were compared with those of catalysts based on cobalt phthalocyanines. A method was proposed for suppressing formation of the thiosulfate ion in oxidation of H2S to elemental sulfur.},\r\ncorrespondence_address1={Bagiyan, G.A.; Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, Leningrad Oblast, Russian Federation},\r\nissn={10704272},\r\ncoden={RJACE},\r\nlanguage={English},\r\nabbrev_source_title={Russ. J. Appl. Chem.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2002\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Reaction of 1,2-trans-glycosyl acetates with phosphorus pentachloride: New efficient approach to 1,2-trans-glycosyl chlorides.\n \n \n \n \n\n\n \n Ibatullin, F.; and Selivanov, S.\n\n\n \n\n\n\n Tetrahedron Letters, 43(52): 9577-9580. 2002.\n cited By 24\n\n\n\n
\n\n\n\n \n \n $\"Reaction$ 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

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@ARTICLE{Ibatullin20029577,\r\nauthor={Ibatullin, F.M. and Selivanov, S.I.},\r\ntitle={Reaction of 1,2-trans-glycosyl acetates with phosphorus pentachloride: New efficient approach to 1,2-trans-glycosyl chlorides},\r\njournal={Tetrahedron Letters},\r\nyear={2002},\r\nvolume={43},\r\nnumber={52},\r\npages={9577-9580},\r\ndoi={10.1016/S0040-4039(02)02446-2},\r\nnote={cited By 24},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037164650&doi=10.1016%2fS0040-4039%2802%2902446-2&partnerID=40&md5=3fe64676a52506da09de369c817a791e},\r\naffiliation={Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation; Chemical Department, Petersburg State University, St. Petersburg, Russian Federation},\r\nabstract={Reaction of phosphorus pentachloride with 1,2-trans-glycosyl esters is described. The reaction mechanism presumably involves formation of a tetrachlorophosphonium ion as one of the key reactive intermediates, which can be induced either by Lewis acids or by using acetonitrile as the reaction solvent. Two novel, efficient methods for the synthesis of the thermodynamically unstable glycosyl chlorides were developed based on this reaction. © 2002 Elsevier Science Ltd. All rights reserved.},\r\ncorrespondence_address1={Ibatullin, F.M.; Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation; email: ibatullin@omrb.pnpi.spb.ru},\r\nissn={00404039},\r\ncoden={TELEA},\r\nlanguage={English},\r\nabbrev_source_title={Tetrahedron Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\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 Stereoselective synthesis of thioxylooligosaccharides from S-glycosyl isothiourea precursors.\n \n \n \n \n\n\n \n Ibatullin, F.; Shabalin, K.; Jänis, J.; and Selivanov, S.\n\n\n \n\n\n\n Tetrahedron Letters, 42(27): 4565-4567. 2001.\n cited By 22\n\n\n\n
\n\n\n\n \n \n $\"Stereoselective$ 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

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@ARTICLE{Ibatullin20014565,\r\nauthor={Ibatullin, F.M. and Shabalin, K.A. and Jänis, J.V. and Selivanov, S.I.},\r\ntitle={Stereoselective synthesis of thioxylooligosaccharides from S-glycosyl isothiourea precursors},\r\njournal={Tetrahedron Letters},\r\nyear={2001},\r\nvolume={42},\r\nnumber={27},\r\npages={4565-4567},\r\ndoi={10.1016/S0040-4039(01)00775-4},\r\nnote={cited By 22},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035797058&doi=10.1016%2fS0040-4039%2801%2900775-4&partnerID=40&md5=ec61fc0be3aa4bc5e6348300ecbf285f},\r\naffiliation={Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation; Department of Chemistry, University of Joensuu, Joensuu, Finland; Chemical Department of Petersburg State University, St Petersburg, Russian Federation},\r\nabstract={A stereoselective synthesis of thioxylo-di-, -tri-, -tetra- and -penta-saccharides from S-glycosyl isothiourea precursors is described. The synthesis was performed starting from 2,3,4-tri-O-acetyl-β-D-xylopyranosyl isothiouronium bromide using a triethylamine promoted reaction with 1,2,3-tri-O-benzoyl-4-O-trifluoromethanesulphonyl-β-L-arabinopyranose. The resulting 4-thioxylobiose was then converted into the corresponding isothiouronium bromide and used for the synthesis of 4,4′-dithioxylotriose. Higher homologues of the series and their α-methyl glycosides were also prepared. © 2001 Elsevier Science Ltd.},\r\nauthor_keywords={S-glycosyl isothiourea derivatives;  Thiooligosaccharides},\r\ncorrespondence_address1={Ibatullin, F.M.; Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation; email: ibatullin@omrb.pnpi.spb.ru},\r\nissn={00404039},\r\ncoden={TELEA},\r\nlanguage={English},\r\nabbrev_source_title={Tetrahedron Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n A general procedure for conversion of S-glycosyl isothiourea derivatives into thioglycosides, thiooligosaccharides and glycosyl thioesters.\n \n \n \n \n\n\n \n Ibatullin, F.; Selivanov, S.; and Shavva, A.\n\n\n \n\n\n\n Synthesis, (3): 419-422. 2001.\n cited By 44\n\n\n\n
\n\n\n\n \n \n $\"A$ Paper\n \n \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

@ARTICLE{Ibatullin2001419,\r\nauthor={Ibatullin, F.M. and Selivanov, S.I. and Shavva, A.G.},\r\ntitle={A general procedure for conversion of S-glycosyl isothiourea derivatives into thioglycosides, thiooligosaccharides and glycosyl thioesters},\r\njournal={Synthesis},\r\nyear={2001},\r\nnumber={3},\r\npages={419-422},\r\nnote={cited By 44},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035099479&partnerID=40&md5=217a95e1228df4617fca1f11b24ba7f8},\r\naffiliation={Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation},\r\nabstract={A simple procedure for conversion of S-glycosyl isothiourea derivatives into thioglycosides by promotion with triethylamine is described. The reaction conditions allow the synthesis of glycosyl thioesters and some thioglycosides, which cannot be prepared using the traditional approach. The procedure has been successfully applied for preparation of thiooligosaccharides, shown by syntheses of methyl 4-thio-α-cellobioside and methyl 4-thio-α-lactoside derivatives.},\r\nauthor_keywords={Alkyl halides;  Carbohydrates;  Thioesters;  Thioglycosides;  Thiooligosaccharides},\r\ncorrespondence_address1={Ibatullin, F.M.; Molec./Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Gatchina 188300, Russian Federation; email: ibatullin@omrb.pnpi.spb.ru},\r\npublisher={Georg Thieme Verlag},\r\nissn={00397881},\r\ncoden={SYNTB},\r\nlanguage={English},\r\nabbrev_source_title={Synthesis},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 2000\n \n \n (2)\n \n \n

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\n \n\n \n \n \n \n \n \n A new approach to synthesis of glycosyl azides from 1,2-trans-glycosyl esters.\n \n \n \n \n\n\n \n Ibatullin, F.; and Shabalin, K.\n\n\n \n\n\n\n Carbohydrate Letters, 3(6): 427-429. 2000.\n cited By 4\n\n\n\n
\n\n\n\n \n \n $\"A$ Paper\n \n \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

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@ARTICLE{Ibatullin2000427,\r\nauthor={Ibatullin, F.M. and Shabalin, K.A.},\r\ntitle={A new approach to synthesis of glycosyl azides from 1,2-trans-glycosyl esters},\r\njournal={Carbohydrate Letters},\r\nyear={2000},\r\nvolume={3},\r\nnumber={6},\r\npages={427-429},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033498350&partnerID=40&md5=df95d78e728764c00c37f755e905d7da},\r\naffiliation={Molecular/Radiation Biophysics Div., Petersburg Nuclear Physics Inst., Gatchina 188350, Russian Federation},\r\nabstract={The combination of boron trifluoride etherate and sodium azide was used for a direct stereoselective conversion of 1,2-trans-glycosyl esters into 1,2-trans-per-O-acetyl-glycosyl azides.},\r\nauthor_keywords={Acyloxonium ion;  Glycosyl azides;  Glycosyl esters},\r\ncorrespondence_address1={Ibatullin, F.M.; Molecular/Radiation Biophysics Div., Petersburg Nuclear Physics Inst., Gatchina 188350, Russian Federation; email: farid@omrb.pnpi.spb.ru},\r\nissn={10735070},\r\ncoden={CLETE},\r\nlanguage={English},\r\nabbrev_source_title={Carbohydr. Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n\n\n

\n \n\n \n \n \n \n \n \n A simple and convenient synthesis of glycosyl azides.\n \n \n \n \n\n\n \n Ibatullin, F.; and Shabalin, K.\n\n\n \n\n\n\n Synthetic Communications, 30(15): 2819-2823. 2000.\n cited By 24\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 abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Ibatullin20002819,\r\nauthor={Ibatullin, F.M. and Shabalin, K.A.},\r\ntitle={A simple and convenient synthesis of glycosyl azides},\r\njournal={Synthetic Communications},\r\nyear={2000},\r\nvolume={30},\r\nnumber={15},\r\npages={2819-2823},\r\ndoi={10.1080/00397910008086908},\r\nnote={cited By 24},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034099689&doi=10.1080%2f00397910008086908&partnerID=40&md5=2b1bb27ff6d54a7bacfa3ec236d2cfdc},\r\naffiliation={Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Gatchina, 188350, Russian Federation},\r\nabstract={Treatment of glycosyl halides with NaN3 in aqueous acetone or acetonitrile is a convenient method for the stereoselective synthesis of 1,2- transper-O-acetyl-glycosyl azides.},\r\ncorrespondence_address1={Ibatullin, F.M.; Molecular/Radiation Biophysics Div., Petersburg Nuclear Physics Institute, Gatchina 188350, Russian Federation; email: farid@omrb.pnpi.spb.ru},\r\npublisher={Marcel Dekker Inc.},\r\nissn={00397911},\r\ncoden={SYNCA},\r\nlanguage={English},\r\nabbrev_source_title={Synth. Commun.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 1993\n \n \n (5)\n \n \n

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\n \n \n

\n \n\n \n \n \n \n \n \n Cleavage of O-glycosyl bonds in glycopeptides [Rasshchepleniia O-glikozil'nykh sviazeǐ v glikopeptidakh.].\n \n \n \n \n\n\n \n Ibatullin, F.; Neustroev, K.; Golubev, A.; and Firsov, L.\n\n\n \n\n\n\n Biokhimiya, 58(6): 852-856. 1993.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Cleavage$ Paper\n \n \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

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@ARTICLE{Ibatullin1993852,\r\nauthor={Ibatullin, F.M. and Neustroev, K.N. and Golubev, A.M. and Firsov, L.M.},\r\ntitle={Cleavage of O-glycosyl bonds in glycopeptides [Rasshchepleniia O-glikozil'nykh sviazeǐ v glikopeptidakh.]},\r\njournal={Biokhimiya},\r\nyear={1993},\r\nvolume={58},\r\nnumber={6},\r\npages={852-856},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027621258&partnerID=40&md5=a32c7f6c40742af91819a3d7bd957d61},\r\nabstract={The possibility of cleavage of the alpha-bond between mannose (or galactose) and serine (or threonine) in the presence of alpha-mannosidase and alpha-galactosidase has been studied. Using model compounds simulating the O-glycosyl bond in glycoproteins, several glycopeptides have been synthesized: N-tertbutyloxycarbonyl-O-alpha-mannopyranosyl-seryl-glycine methylamide (alpha-Man-Ser-Gly), tertbutyl-oxycarbonyl-O-alpha-mannopyranosyl-threonyl- glycine methylamide (alpha-Man-Thr-Gly), N-tertbutyloxy-carbonyl-O-alpha-galactopyranosyl-seryl-glycine methylamide (alpha-Gal-Ser-Gly) as well as N-tertbutyloxy-carbonyl-O-beta-mannopyranosyl-seryl-glycine methylamide (beta-Man-Ser-Gly). The cleavage has been shown to occur in glucoamylase after proteolytic degradation.},\r\ncorrespondence_address1={Ibatullin, F.M.},\r\nissn={03209725},\r\npubmed_id={8395900},\r\nlanguage={Russian},\r\nabbrev_source_title={Biokhimiia},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n A model for cleavage of O-glycosidic bonds in glycoproteins.\n \n \n \n \n\n\n \n Ibatullin, F.; Golubev, A.; Firsov, L.; and Neustroev, K.\n\n\n \n\n\n\n Glycoconjugate Journal, 10(3): 214-218. 1993.\n cited By 7\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 abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

\n

@ARTICLE{Ibatullin1993214,\r\nauthor={Ibatullin, F.M. and Golubev, A.M. and Firsov, L.M. and Neustroev, K.N.},\r\ntitle={A model for cleavage of O-glycosidic bonds in glycoproteins},\r\njournal={Glycoconjugate Journal},\r\nyear={1993},\r\nvolume={10},\r\nnumber={3},\r\npages={214-218},\r\ndoi={10.1007/BF00702202},\r\nnote={cited By 7},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027308281&doi=10.1007%2fBF00702202&partnerID=40&md5=bd2411c71793d9bc1b6ea28433511a61},\r\naffiliation={Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188 350, Russian Federation},\r\nabstract={The present work investigated the possibility of cleavage of α-linkages between mannose or galactose and serine/threonine residues by α-mannosidase and α-galactosidase. The study was carried out initially with model synthetic compounds imitating the O-glycosidic bond in glycoproteins, and further with glucoamylase. It was shown that α-mannosidase and α-galactosidase can hydrolyse these linkages after proteolytic digestion of glucosamylase. © 1993 Chapman & Hall.},\r\nauthor_keywords={α-galactosidase;  α-mannosidase;  glucoamylase;  O-glycoprotein},\r\ncorrespondence_address1={Neustroev, K.N.; Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, 188 350, Russian Federation},\r\npublisher={Kluwer Academic Publishers},\r\nissn={02820080},\r\ncoden={GLJOE},\r\npubmed_id={8257849},\r\nlanguage={English},\r\nabbrev_source_title={Glycoconjugate J},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

\n

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

\n\n\n

\n \n\n \n \n \n \n \n \n Effect of modification of carbohydrate component on properties of glucoamylase.\n \n \n \n \n\n\n \n Neustroev, K.; Golubev, A.; Firsov, L.; Ibatullin, F.; Protasevich, I.; and Makarov, A.\n\n\n \n\n\n\n FEBS Letters, 316(2): 157-160. 1993.\n cited By 35\n\n\n\n
\n\n\n\n \n \n $\"Effect$ 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

@ARTICLE{Neustroev1993157,\r\nauthor={Neustroev, K.N. and Golubev, A.M. and Firsov, L.M. and Ibatullin, F.M. and Protasevich, I.I. and Makarov, A.A.},\r\ntitle={Effect of modification of carbohydrate component on properties of glucoamylase},\r\njournal={FEBS Letters},\r\nyear={1993},\r\nvolume={316},\r\nnumber={2},\r\npages={157-160},\r\ndoi={10.1016/0014-5793(93)81206-F},\r\nnote={cited By 35},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027392251&doi=10.1016%2f0014-5793%2893%2981206-F&partnerID=40&md5=ba0c0aa85859f1d6d54fa972ba683279},\r\naffiliation={Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation; Institute of Molecular Biology, Moscow, Russian Federation},\r\nabstract={In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-Linked sugars were modified by treatment with α-mannosidase and N-linked sugars were removed using endo-β-N-acetylglucosaminidase F. Analysis ofconformational changes following deglycosylation suggests that O-linked sugars essentially contribute to the stabilization of glucoamylase domains. Modification of the carbohydrate component by adding 1-deoxymannojirimycin to the culture medium induced inhibition of α-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme. © 1993.},\r\nauthor_keywords={Deglycosylation;  Glucoamylase;  Glycoprotein},\r\ncorrespondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation},\r\nissn={00145793},\r\ncoden={FEBLA},\r\npubmed_id={8420800},\r\nlanguage={English},\r\nabbrev_source_title={FEBS Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n The interaction of nuclear proteins with bent DNA located in an autonomously replicating DARC146 sequence [Vzaimodeǐstvie iadernykh belkov s izognutoǐ DNK, raspolozhennoǐ v avtonomno replitsiruiushcheǐsia posledovatel'nosti DARC146.].\n \n \n \n \n\n\n \n Luniak, V.; Filatov, M.; Ibatullin, F.; and Timchenko, N.\n\n\n \n\n\n\n Tsitologiya, 35(5): 84-90. 1993.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"The$ Paper\n \n \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

@ARTICLE{Luniak199384,\r\nauthor={Luniak, V.V. and Filatov, M.V. and Ibatullin, F.M. and Timchenko, N.A.},\r\ntitle={The interaction of nuclear proteins with bent DNA located in an autonomously replicating DARC146 sequence [Vzaimodeǐstvie iadernykh belkov s izognutoǐ DNK, raspolozhennoǐ v avtonomno replitsiruiushcheǐsia posledovatel'nosti DARC146.]},\r\njournal={Tsitologiya},\r\nyear={1993},\r\nvolume={35},\r\nnumber={5},\r\npages={84-90},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027343268&partnerID=40&md5=a0bd6d6a1eee3ff3c287dde1598ec2f6},\r\nabstract={The binding of nuclear proteins to a DARC146 DNA fragment is described. The DARC146 was isolated from a complex form of DNA polymerase alpha. BrdUrd substitution experiments indicate that DARC146 can support an autonomous replication in mammalian cells. Three AAA blocks separated by 10 nucleotides were identified in the DARC146 sequence. Measuring electrophoretical mobility under appropriate conditions showed that these AAA blocks form a bent DNA. We have used a synthetic oligonucleotide covering the bent DNA to study the interaction of nuclear proteins with this DNA region. Four DNA-protein complexes with the bent DNA region were registered. One of them is formed by binding nuclear factor p65 to TCTATTA nucleotides. The molecular weight and binding site of p65 are very similar to those of c-myc protein. However, antibodies against c-myc protein exert no effect on the formation of the p65-DNA complex. We suggest that p65 is an unknown nuclear factor.},\r\ncorrespondence_address1={Luniak, V.V.},\r\nissn={00413771},\r\npubmed_id={8379011},\r\nlanguage={Russian},\r\nabbrev_source_title={Tsitologiia},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Microheterogeneity in o-type sugar chains of carbohydrases secreted by Asp. awamori.\n \n \n \n \n\n\n \n Neustroev, K.; Golubev, A.; Ibatullin, F.; and Moseichuk, A.\n\n\n \n\n\n\n Biochemistry and Molecular Biology International, 30(1): 107-113. 1993.\n cited By 9\n\n\n\n
\n\n\n\n \n \n $\"Microheterogeneity$ Paper\n \n \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

@ARTICLE{Neustroev1993107,\r\nauthor={Neustroev, K.N. and Golubev, A.M. and Ibatullin, F.M. and Moseichuk, A.V.},\r\ntitle={Microheterogeneity in o-type sugar chains of carbohydrases secreted by Asp. awamori},\r\njournal={Biochemistry and Molecular Biology International},\r\nyear={1993},\r\nvolume={30},\r\nnumber={1},\r\npages={107-113},\r\nnote={cited By 9},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027241317&partnerID=40&md5=6e40e78e777164f40d499bfcb811c56e},\r\naffiliation={Dept. of Molecular/, Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina, 188 350 St. Petersburg, Russian Federation},\r\nabstract={This paper deals with microheterogeneity in the structure of O-linked sugars of carbohydrases secreted by Asp. awamori, namely glucoamylase, α-galactosidase and α-glucosidase. Microheterogeneity was found to be related both to post-secretion deglycosylation and to changes in transferase activity induced by the differences in culturing conditions.},\r\ncorrespondence_address1={Neustroev, K.N.; Dept. of Molecular/, Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina, 188 350 St. Petersburg, Russian Federation},\r\nissn={01585231},\r\ncoden={BMBIE},\r\npubmed_id={8358322},\r\nlanguage={English},\r\nabbrev_source_title={BIOCHEM. MOL. BIOL. INT.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 1992\n \n \n (3)\n \n \n

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\n \n\n \n \n \n \n \n \n Tunneling transfer of an electron in oxidation of the HS- ion by an I3- complex in aqueous solution.\n \n \n \n \n\n\n \n Ufimtsev, A.; Soroka, N.; and Bagiyan, G.\n\n\n \n\n\n\n Bulletin of the Russian Academy of Sciences Division of Chemical Science, 41(3): 410-421. 1992.\n cited By 1\n\n\n\n
\n\n\n\n \n \n $\"Tunneling$ 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

@ARTICLE{Ufimtsev1992410,\r\nauthor={Ufimtsev, A.V. and Soroka, N.V. and Bagiyan, G.A.},\r\ntitle={Tunneling transfer of an electron in oxidation of the HS- ion by an I3- complex in aqueous solution},\r\njournal={Bulletin of the Russian Academy of Sciences Division of Chemical Science},\r\nyear={1992},\r\nvolume={41},\r\nnumber={3},\r\npages={410-421},\r\ndoi={10.1007/BF00863053},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0043192364&doi=10.1007%2fBF00863053&partnerID=40&md5=5469a25a532e27dd79ab7222af6188bb},\r\nabstract={Methods of chemical kinetics have been used in a study of the mechanism of hydrogen sulfide oxidation by iodine. It has been shown that the stage of electron transfer from HS- to the I3/- complex proceeds through a tunneling mechanism. A proposed "twinkling" model of the reaction mechanism provides an explanation for the observed experimental facts: the dependence of the rate constant on the acidity, viscosity, and ionic strength of the solution; the inverse temperature dependence of the reaction rate constant; the dependence of the reaction rate constant on the concentrations of iodide ion and maleic acid, which are not involved directly in the reaction. © 1992 Plenum Publishing Corporation.},\r\nauthor_keywords={chemical kinetics;  oxidation of hydrogen sulfide;  tunneling transfer},\r\npublisher={Kluwer Academic Publishers-Plenum Publishers},\r\nissn={10635211},\r\nlanguage={English},\r\nabbrev_source_title={Russ Chem Bull},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Study of intermediates formed in the oxidation of thiols.\n \n \n \n \n\n\n \n Soroka, N.; and Bagiyan, G.\n\n\n \n\n\n\n Bulletin of the Russian Academy of Sciences Division of Chemical Science, 41(2): 205-214. 1992.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Study$ 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

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@ARTICLE{Soroka1992205,\r\nauthor={Soroka, N.V. and Bagiyan, G.A.},\r\ntitle={Study of intermediates formed in the oxidation of thiols},\r\njournal={Bulletin of the Russian Academy of Sciences Division of Chemical Science},\r\nyear={1992},\r\nvolume={41},\r\nnumber={2},\r\npages={205-214},\r\ndoi={10.1007/BF00869502},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34249841850&doi=10.1007%2fBF00869502&partnerID=40&md5=d07fc2edab0e9cd45e791cd1a2c22f1b},\r\nabstract={The oxidation of aminoethanethiol (1) was investigated in acid solutions on a glass carbon anode. It was shown that at relatively low anode potentials thiyl radicals RS· are released into the solution, but this does not lead to binding of the oxygen in the solution. Raising the anode potential leads to binding of oxygen, which is probably due to the formation of the intermediate RS+. The oxidation of 1 was studied in Ce(SO4)2+H2SO4 solution. It was shown that under certain conditions the intermediate is RS+, which subsequently converts to a product that could not be identified as any previously described product of the oxidation of thiols. Proposals are made regarding its structure and conversion pathways. © 1992 Plenum Publishing Corporation.},\r\nauthor_keywords={aqueous solutions;  electrochemical oxidation;  intermediates;  oxidation by cerium(IV) sulfate;  RS· radicals;  RS+ cations;  thiols},\r\npublisher={Kluwer Academic Publishers-Plenum Publishers},\r\nissn={10635211},\r\nlanguage={English},\r\nabbrev_source_title={Russ Chem Bull},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n\n \n \n \n \n \n \n Universally primed polymerase chain reaction: Primer and genome DNA patterns characteristics.\n \n \n \n \n\n\n \n Bulat, S.; Kobaev, O.; Mironenko, N.; Ibatullin, F.; Luchkina, L.; and Suslov, A.\n\n\n \n\n\n\n Genetika, 28(5): 19-28. 1992.\n cited By 10\n\n\n\n
\n\n\n\n \n \n $\"Universally$ Paper\n \n \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

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@ARTICLE{Bulat199219,\r\nauthor={Bulat, S.A. and Kobaev, O.K. and Mironenko, N.V. and Ibatullin, F.M. and Luchkina, L.A. and Suslov, A.V.},\r\ntitle={Universally primed polymerase chain reaction: Primer and genome DNA patterns characteristics},\r\njournal={Genetika},\r\nyear={1992},\r\nvolume={28},\r\nnumber={5},\r\npages={19-28},\r\nnote={cited By 10},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026862795&partnerID=40&md5=d70b1c12c001879c0ca833e6e06f9501},\r\naffiliation={Leningrad Inst. of Nuclear Physics, Russian Academy of Sciences, Gatchina, Russia},\r\nabstract={Universal primer ability of generating conservative and variable UP-PCR (universally primed polymerase chain reaction) species-specific patterns was analysed on bacteria to serve as an example. Also, two important properties of the UP-PCR patterns (species/primer DNA hybridization specificity) are characterized.},\r\ncorrespondence_address1={Bulat, S.A.; Leningrad Inst. of Nuclear Physics, Russian Academy of Sciences, Gatchina, Russia},\r\nissn={00166758},\r\ncoden={GNKAA},\r\npubmed_id={1639258},\r\nlanguage={Russian},\r\nabbrev_source_title={GENETIKA},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 1981\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Production of thiyl radicals and investigation of their reactions with oxygen and 2-sulfoethanethiosulfuric acid.\n \n \n \n \n\n\n \n Grachev, S.; and Soroka, N.\n\n\n \n\n\n\n Bulletin of the Academy of Sciences of the USSR Division of Chemical Science, 30(8): 1426-1432. 1981.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Production$ 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

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@ARTICLE{Grachev19811426,\r\nauthor={Grachev, S.A. and Soroka, N.V.},\r\ntitle={Production of thiyl radicals and investigation of their reactions with oxygen and 2-sulfoethanethiosulfuric acid},\r\njournal={Bulletin of the Academy of Sciences of the USSR Division of Chemical Science},\r\nyear={1981},\r\nvolume={30},\r\nnumber={8},\r\npages={1426-1432},\r\ndoi={10.1007/BF00952189},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34250229218&doi=10.1007%2fBF00952189&partnerID=40&md5=9e31ffd7ee5f4bd64859f42b59e3c198},\r\naffiliation={B. P. Konstantinov Leningrad Institute of Nuclear Physics},\r\nabstract={1. The kinetics of the oxidation of 2-aminoethanethiol, 3-aminopropanethiol, 4-aminobutanethiol, (dimethylamino)ethanethiol, and 2-mercaptoethanol by the 1,10-phenanthroline complex [Fe(phen)3]3+ were studied. The complex [Fe(phen)3]3+ only reacts with thiols containing a deprotonated mercapto group. 2. The stoichiometry and the reaction products in the 2-aminoethanethiol + [Fe(phen)3]3+ +oxygen system were studied. 3. 2-Sulfo-1-ethanethiosulfuric acid can be used as reagent for thiyl radicals. 4. The differences between the processes occurring in the thiol+[Fe(phen)3]3++O2 system at pH &gt; 1.5 and the reactions in which RS. radicals participate during radiolysis of the thiols in the presence of oxygen were determined. © 1982 Plenum Publishing Corporation.},\r\ncorrespondence_address1={Grachev, S.A.; B. P. Konstantinov Leningrad Institute of Nuclear Physics},\r\npublisher={Kluwer Academic Publishers-Plenum Publishers},\r\nissn={05685230},\r\nlanguage={English},\r\nabbrev_source_title={Russ Chem Bull},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 1976\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n The kinetics and mechanism of the reaction of the oxidation of aminothiols by hydrogen peroxide in aqueous solutions.\n \n \n \n \n\n\n \n Bagiyan, G.; Grachev, S.; Koroleva, I.; and Soroka, N.\n\n\n \n\n\n\n Bulletin of the Academy of Sciences of the USSR Division of Chemical Science, 25(5): 966-971. 1976.\n cited By 1\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 abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n

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@ARTICLE{Bagiyan1976966,\r\nauthor={Bagiyan, G.A. and Grachev, S.A. and Koroleva, I.K. and Soroka, N.V.},\r\ntitle={The kinetics and mechanism of the reaction of the oxidation of aminothiols by hydrogen peroxide in aqueous solutions},\r\njournal={Bulletin of the Academy of Sciences of the USSR Division of Chemical Science},\r\nyear={1976},\r\nvolume={25},\r\nnumber={5},\r\npages={966-971},\r\ndoi={10.1007/BF00921973},\r\nnote={cited By 1},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344653256&doi=10.1007%2fBF00921973&partnerID=40&md5=aa38555dc411cba3964c2bb6aa87c5ee},\r\naffiliation={B. P. Konstantin Institute of Nuclear Physics, Leningrad, Russian Federation; The Academy of Sciences of the USSR, Gatchina, Russian Federation},\r\nabstract={1. A study was made of the interaction of aminothiols (AT) with H 2 O 2 , as affected by the acidity of the medium, the temperature, the ionic strength of the solution, and the structure of the AT; the reacting particles were the thiolate anion and the molecular form of hydrogen peroxide. 2. The reaction was promoted by hydrogen bonding between the OH - group splitting off and the amino group of the AT, and by the attraction between the OH - group and the positively charged end of the zwitterion form of the AT. 3. Intermolecular hydrogen bonding and the electrostatic effect introduced equal contributions to the activation of the reaction. © 1976 Plenum Publishing Corporation.},\r\ncorrespondence_address1={Bagiyan, G.A.; B. P. Konstantin Institute of Nuclear Physics, Leningrad, Russian Federation},\r\npublisher={Kluwer Academic Publishers-Plenum Publishers},\r\nissn={05685230},\r\nlanguage={English},\r\nabbrev_source_title={Russ Chem Bull},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n

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\n \n 1975\n \n \n (1)\n \n \n

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\n \n\n \n \n \n \n \n \n Chemiluminescent determination of small hydrogen peroxide concentrations in aqueous solutions in the presence of aminothiols.\n \n \n \n \n\n\n \n Bagiyan, G.; Grachev, S.; and Soroka, N.\n\n\n \n\n\n\n Bulletin of the Academy of Sciences of the USSR Division of Chemical Science, 24(2): 363-365. 1975.\n cited By 0\n\n\n\n
\n\n\n\n \n \n $\"Chemiluminescent$ 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

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@ARTICLE{Bagiyan1975363,\r\nauthor={Bagiyan, G.A. and Grachev, S.A. and Soroka, N.V.},\r\ntitle={Chemiluminescent determination of small hydrogen peroxide concentrations in aqueous solutions in the presence of aminothiols},\r\njournal={Bulletin of the Academy of Sciences of the USSR Division of Chemical Science},\r\nyear={1975},\r\nvolume={24},\r\nnumber={2},\r\npages={363-365},\r\ndoi={10.1007/BF00925788},\r\nnote={cited By 0},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34250398790&doi=10.1007%2fBF00925788&partnerID=40&md5=b85e1d021a873af495df7a3324e1c9d5},\r\naffiliation={B. P. Konstantinov Institute of Nuclear Physics, Academy of Sciences of the USSR, Leningrad, Russian Federation},\r\nabstract={1. A method was developed for the chemiluminescent determination of hydrogen peroxide in amounts down to 5·10-9 mole, with an accuracy of ±5%, in the presence of 10-5 mole of an aminothiol in the same sample. 2. To bind the aminothiol, which causes a quenching of the luminescence, it is necessary to add HgCl2 to the solution, which in the presence of ethyienediaminetetraacetic acid forms with the aminothiol a water-soluble complex of postulated composition [RS-Hg-Edta]-3, which does not cause a quenching of the luminescence. © 1975 Plenum Publishing Corporation.},\r\ncorrespondence_address1={Bagiyan, G.A.; B. P. Konstantinov Institute of Nuclear Physics, Academy of Sciences of the USSR, Leningrad, Russian Federation},\r\npublisher={Kluwer Academic Publishers-Plenum Publishers},\r\nissn={05685230},\r\nlanguage={English},\r\nabbrev_source_title={Russ Chem Bull},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n

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