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How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: aggregation morphology, kinetics, and sizes of nuclei.
Selivanova OM, Suvorina MY, Dovidchenko NV, Eliseeva IA, Surin AK, Finkelstein AV, Schmatchenko VV, Galzitskaya OV. Selivanova OM, et al. Among authors: surin ak. J Phys Chem B. 2014 Feb 6;118(5):1198-206. doi: 10.1021/jp4083568. Epub 2014 Jan 24. J Phys Chem B. 2014. PMID: 24428561
One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42.
Dovidchenko NV, Glyakina AV, Selivanova OM, Grigorashvili EI, Suvorina MY, Dzhus UF, Mikhailina AO, Shiliaev NG, Marchenkov VV, Surin AK, Galzitskaya OV. Dovidchenko NV, et al. Among authors: surin ak. J Struct Biol. 2016 Jun;194(3):404-14. doi: 10.1016/j.jsb.2016.03.020. Epub 2016 Mar 22. J Struct Biol. 2016. PMID: 27016282
Peptide Aβ(16-25) Forms Nanofilms in the Process of Its Aggregation.
Selivanova OM, Gorbunova EY, Mustaeva LG, Grigorashvili EI, Suvorina MY, Surin AK, Galzitskaya OV. Selivanova OM, et al. Among authors: surin ak. Biochemistry (Mosc). 2016 Jul;81(7):755-61. doi: 10.1134/S0006297916070129. Biochemistry (Mosc). 2016. PMID: 27449622 Free article.
Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p-glucantransferase of S. cerevisiae cell wall and its modifying analog. New morphology of amyloid fibrils.
Selivanova OM, Glyakina AV, Gorbunova EY, Mustaeva LG, Suvorina MY, Grigorashvili EI, Nikulin AD, Dovidchenko NV, Rekstina VV, Kalebina TS, Surin AK, Galzitskaya OV. Selivanova OM, et al. Among authors: surin ak. Biochim Biophys Acta. 2016 Nov;1864(11):1489-99. doi: 10.1016/j.bbapap.2016.08.002. Epub 2016 Aug 6. Biochim Biophys Acta. 2016. PMID: 27500912
54 results