@ARTICLE{Egorov2007471,
author={Egorov, V.V. and Solovyov, K.V. and Grudinina, N.A. and Lebedev, D.V. and Isaev-Ivanov, V.V. and Kiselev, O.I. and Shawlovsky, M.M.},
title={Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins},
journal={Protein and Peptide Letters},
year={2007},
volume={14},
number={5},
pages={471-474},
doi={10.2174/092986607780782858},
note={cited By 4},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34249743235&doi=10.2174%2f092986607780782858&partnerID=40&md5=b627ff86500ddc6e21422c29aeab5a55},
affiliation={Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russian Federation; Petersburg Nuclear Physics Institute RAS, Orlova Roscha, Gatchina, Russian Federation; Influenza Institute RAMS, 15/17 Prof. Popova St., Saint Petersburg, Russian Federation},
abstract={Symmetrical peptide GYDTQAIVENNESTEYG (WT, Wild Type) identical to 35-51 aminoacid residues of human alpha-lactalbumin (HLA) and peptide GYDTQTVVNNNGHTDYG (ID, IDeal symmetry) homologous to beta-domain of mammalian alpha-lactalbumins can form amyloid-like fibrils in conditions required for fibrillogenesis of HLA. The latter peptide can also form fibrils in deionized water. Fibrils formed by these peptides can cause forming of HLA amyloid-like aggregates in physiological conditions. These results provide an evidence for presence of amyloidogenic determinant in beta-domain of alpha-lactalbumin. Thus, symmetry in the primary structure may play the role in fibrillogenesis of proteins. © 2007 Bentham Science Publishers Ltd.},
author_keywords={Alpha-lactalbumin;  Atomic force microscopy;  Fibrillogenesis;  GYDTQAIVENNESTEYG;  GYDTQTVVNNNGHTDYG;  Symmetry},
correspondence_address1={Egorov, V.V.; Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russian Federation; email: olivejra@yahoo.com},
issn={09298665},
coden={PPELE},
pubmed_id={17584173},
language={English},
abbrev_source_title={Protein Pept. Lett.},
document_type={Article},
source={Scopus},
}

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Pavlova St., Saint Petersburg, Russian Federation; Petersburg Nuclear Physics Institute RAS, Orlova Roscha, Gatchina, Russian Federation; Influenza Institute RAMS, 15/17 Prof. Popova St., Saint Petersburg, Russian Federation","abstract":"Symmetrical peptide GYDTQAIVENNESTEYG (WT, Wild Type) identical to 35-51 aminoacid residues of human alpha-lactalbumin (HLA) and peptide GYDTQTVVNNNGHTDYG (ID, IDeal symmetry) homologous to beta-domain of mammalian alpha-lactalbumins can form amyloid-like fibrils in conditions required for fibrillogenesis of HLA. The latter peptide can also form fibrils in deionized water. Fibrils formed by these peptides can cause forming of HLA amyloid-like aggregates in physiological conditions. These results provide an evidence for presence of amyloidogenic determinant in beta-domain of alpha-lactalbumin. Thus, symmetry in the primary structure may play the role in fibrillogenesis of proteins. © 2007 Bentham Science Publishers Ltd.","author_keywords":"Alpha-lactalbumin; Atomic force microscopy; Fibrillogenesis; GYDTQAIVENNESTEYG; GYDTQTVVNNNGHTDYG; Symmetry","correspondence_address1":"Egorov, V.V.; Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russian Federation; email: olivejra@yahoo.com","issn":"09298665","coden":"PPELE","pubmed_id":"17584173","language":"English","abbrev_source_title":"Protein Pept. Lett.","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Egorov2007471,\r\nauthor={Egorov, V.V. and Solovyov, K.V. and Grudinina, N.A. and Lebedev, D.V. and Isaev-Ivanov, V.V. and Kiselev, O.I. and Shawlovsky, M.M.},\r\ntitle={Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins},\r\njournal={Protein and Peptide Letters},\r\nyear={2007},\r\nvolume={14},\r\nnumber={5},\r\npages={471-474},\r\ndoi={10.2174/092986607780782858},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-34249743235&doi=10.2174%2f092986607780782858&partnerID=40&md5=b627ff86500ddc6e21422c29aeab5a55},\r\naffiliation={Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russian Federation; Petersburg Nuclear Physics Institute RAS, Orlova Roscha, Gatchina, Russian Federation; Influenza Institute RAMS, 15/17 Prof. Popova St., Saint Petersburg, Russian Federation},\r\nabstract={Symmetrical peptide GYDTQAIVENNESTEYG (WT, Wild Type) identical to 35-51 aminoacid residues of human alpha-lactalbumin (HLA) and peptide GYDTQTVVNNNGHTDYG (ID, IDeal symmetry) homologous to beta-domain of mammalian alpha-lactalbumins can form amyloid-like fibrils in conditions required for fibrillogenesis of HLA. The latter peptide can also form fibrils in deionized water. Fibrils formed by these peptides can cause forming of HLA amyloid-like aggregates in physiological conditions. These results provide an evidence for presence of amyloidogenic determinant in beta-domain of alpha-lactalbumin. Thus, symmetry in the primary structure may play the role in fibrillogenesis of proteins. © 2007 Bentham Science Publishers Ltd.},\r\nauthor_keywords={Alpha-lactalbumin; Atomic force microscopy; Fibrillogenesis; GYDTQAIVENNESTEYG; GYDTQTVVNNNGHTDYG; Symmetry},\r\ncorrespondence_address1={Egorov, V.V.; Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russian Federation; email: olivejra@yahoo.com},\r\nissn={09298665},\r\ncoden={PPELE},\r\npubmed_id={17584173},\r\nlanguage={English},\r\nabbrev_source_title={Protein Pept. Lett.},\r\ndocument_type={Article},\r\nsource={Scopus},\r\n}\r\n\r\n","author_short":["Egorov, V.","Solovyov, K.","Grudinina, N.","Lebedev, D.","Isaev-Ivanov, V.","Kiselev, O.","Shawlovsky, M."],"key":"Egorov2007471","id":"Egorov2007471","bibbaseid":"egorov-solovyov-grudinina-lebedev-isaevivanov-kiselev-shawlovsky-atomicforcemicroscopystudyofpeptideshomologoustobetadomainofalphalactalbumins-2007","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-34249743235&doi=10.2174%2f092986607780782858&partnerID=40&md5=b627ff86500ddc6e21422c29aeab5a55"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lbm_2019_10.txt","dataSources":["YYLjupmCazkNqWNEJ"],"keywords":[],"search_terms":["atomic","force","microscopy","study","peptides","homologous","beta","domain","alpha","lactalbumins","egorov","solovyov","grudinina","lebedev","isaev-ivanov","kiselev","shawlovsky"],"title":"Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins","year":2007}