{"_id":"6oo5qc7ZrDJKw2EQv","bibbaseid":"anonymous-aconservativemutantofaproteolyticfragmentproducedduringfibrilformationenhancesfibrillogenesis-2014","bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Egorov"],"firstnames":["V.V."],"suffixes":[]},{"propositions":[],"lastnames":["Lebedev"],"firstnames":["D.V."],"suffixes":[]},{"propositions":[],"lastnames":["Shaldzhyan"],"firstnames":["A.A."],"suffixes":[]},{"propositions":[],"lastnames":["Sirotkin"],"firstnames":["A.K."],"suffixes":[]},{"propositions":[],"lastnames":["Gorshkov"],"firstnames":["A.N."],"suffixes":[]},{"propositions":[],"lastnames":["Mirgorodskaya"],"firstnames":["O.A."],"suffixes":[]},{"propositions":[],"lastnames":["Grudinina"],"firstnames":["N.A."],"suffixes":[]},{"propositions":[],"lastnames":["Vasin"],"firstnames":["A.V."],"suffixes":[]},{"propositions":[],"lastnames":["Shavlovsky"],"firstnames":["M.M."],"suffixes":[]}],"title":"A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis","journal":"Prion","year":"2014","volume":"8","number":"5","pages":"369-373","doi":"10.4161/19336896.2014.983745","note":"cited By 2","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-84920764416&doi=10.4161%2f19336896.2014.983745&partnerID=40&md5=e8fc9cac57be1f1f37c10266b82a70a0","affiliation":"FSBI Research Institute of Influenza, Ministry of Healthcare of the Russian Federation, St. Petersburg, Russian Federation; Kurchatov Institute, FSBI Petersburg Nuclear Physics Institute, Gatchina, Russian Federation; FSBI Institute of Experimental Medicine NWB RAMS, St. Petersburg, Russian Federation; State Polytechnical University, St. Petersburg, Russian Federation","abstract":"The fibrillogenesis of a peptide corresponding to residues 35-51 of human α-lactalbumin (1GYDTQAIVENNESTEYG17) can be dramatically enhanced by the addition of a tetrapeptide TDYG homologous to its C-terminus (TEYG). Generation of spontaneous hydrolytic products similar to this peptide was demonstrated by mass-spectrometry analysis of GYDTQAIVE NNESTEYG peptide solution components during fibrillogenesis. Possible mechanisms and roles of short peptides in protein metabolism are discussed. © 2014 Taylor & Francis Group, LLC.","author_keywords":"Conformation transmission; Fibrillogenesis; GYDTQAIVENNESTEYG; Lactalbumin; Short peptides; Spontaneous hydrolysis","funding_details":"Российский Фонд Фундаментальных Исследований (РФФИ)No.14-24-01103","key":"Egorov2014369","id":"Egorov2014369","bibbaseid":"anonymous-aconservativemutantofaproteolyticfragmentproducedduringfibrilformationenhancesfibrillogenesis-2014","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-84920764416&doi=10.4161%2f19336896.2014.983745&partnerID=40&md5=e8fc9cac57be1f1f37c10266b82a70a0"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lbm_2019_10.txt","dataSources":["YYLjupmCazkNqWNEJ"],"keywords":[],"search_terms":["conservative","mutant","proteolytic","fragment","produced","during","fibril","formation","enhances","fibrillogenesis"],"title":"A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis","year":2014}