{"_id":"xYeP733XDh6ovvhYb","bibbaseid":"anonymous-characterizationofoligomerizationofapeptidefromtheebolavirusglycoproteinbysmallangleneutronscattering-2016","bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Egorov"],"firstnames":["V.V."],"suffixes":[]},{"propositions":[],"lastnames":["Gorshkov"],"firstnames":["A.N."],"suffixes":[]},{"propositions":[],"lastnames":["Murugova"],"firstnames":["T.N."],"suffixes":[]},{"propositions":[],"lastnames":["Vasin"],"firstnames":["A.V."],"suffixes":[]},{"propositions":[],"lastnames":["Lebedev"],"firstnames":["D.V."],"suffixes":[]},{"propositions":[],"lastnames":["Isaev-Ivanov"],"firstnames":["V.V."],"suffixes":[]},{"propositions":[],"lastnames":["Kiselev"],"firstnames":["O.I."],"suffixes":[]}],"title":"Characterization of oligomerization of a peptide from the ebola virus glycoprotein by small-angle neutron scattering","journal":"Crystallography Reports","year":"2016","volume":"61","number":"1","pages":"94-97","doi":"10.1134/S1063774516010065","note":"cited By 0","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-84955574220&doi=10.1134%2fS1063774516010065&partnerID=40&md5=87c9a94b3f508099ce7dd469be80a846","affiliation":"Konstantinov Petersburg Nuclear Physics Institute, National Research Center “Kurchatov Institute”, Orlova Roshcha, Gatchina, Leningrad oblast, 188300, Russian Federation; Research Institute of Influenza, Ministry of Health of the Russian Federation, ul. Professora Popova 15/17, St. Petersburg, 197376, Russian Federation; Joint Institute for Nuclear Research, ul. Joliot-Curie 6, Dubna, Moscow region, 141980, Russian Federation; Institute of Physics, Nanotechnology and Telecommunications, St. Petersburg State Polytechnical University, Politekhnicheskaya ul. 29, St. Petersburg, 195251, Russian Federation","abstract":"Transmission electron microscopy (TEM) and small-angle neutron scattering (SANS) studies showed that model peptides QNALVCGLRQ (G33) and QNALVCGLRG (G31) corresponding to region 551–560 of the GP protein of the Sudan Ebola virus are prone to oligomerization in solution. Both peptides can form amyloid-like fibrills. The G33 peptide forms fibrils within one day of incubation, whereas the fibrillogenesis of the G31 peptide is observed only after incubation for several months. The possible role of the observed processes in the pathogenesis and the possibility of applying a combination of the TEM and SANS techniques to search for new compounds that are able to influence the protein oligomerization are discussed. © 2016, Pleiades Publishing, Inc.","funding_details":"Российский Фонд Фундаментальных Исследований (РФФИ)14-24-01103 ofi-m","key":"Egorov201694","id":"Egorov201694","bibbaseid":"anonymous-characterizationofoligomerizationofapeptidefromtheebolavirusglycoproteinbysmallangleneutronscattering-2016","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-84955574220&doi=10.1134%2fS1063774516010065&partnerID=40&md5=87c9a94b3f508099ce7dd469be80a846"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lbm_2019_10.txt","dataSources":["YYLjupmCazkNqWNEJ"],"keywords":[],"search_terms":["characterization","oligomerization","peptide","ebola","virus","glycoprotein","small","angle","neutron","scattering"],"title":"Characterization of oligomerization of a peptide from the ebola virus glycoprotein by small-angle neutron scattering","year":2016}