| Literature DB >> 20132817 |
Gergely Agócs1, Katalin Solymosi, Andrea Varga, Károly Módos, Miklós Kellermayer, Péter Závodszky, Judit Fidy, Szabolcs Osváth.
Abstract
Amyloid deposits, which accumulate in numerous diseases, are the final stage of multi-step protein conformational-conversion and oligomerization processes. The underlying molecular mechanisms are not fully understood, and particularly little is known about the reverse reaction. Here we show that phosphoglycerate kinase amyloid fibrils can be converted back into native protein. We achieved recovery with 60% efficiency, which is comparable to the success rate of the unfolding-refolding studies, and the recovered enzyme was folded, stable and fully active. The key intermediate stages in the recovery process are fibril disassembly and unfolding followed by spontaneous protein folding. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID: 20132817 DOI: 10.1016/j.febslet.2010.01.058
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124