Matches in SemOpenAlex for { <https://semopenalex.org/work/W2006654567> ?p ?o ?g. }
- W2006654567 endingPage "287" @default.
- W2006654567 startingPage "260" @default.
- W2006654567 abstract "Aggregation and subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. The accumulated data support the model where protein fibrillogenesis proceeds via the formation of a relatively unfolded amyloidogenic conformation, which shares many structural properties with the pre-molten globule state, a partially folded intermediate first found during the equilibrium and kinetic (un)folding studies of several globular proteins and later described as one of the structural forms of natively unfolded proteins. The flexibility of this structural form is essential for the conformational rearrangements driving the formation of the core cross-beta structure of the amyloid fibril. Obviously, molecular mechanisms describing amyloidogenesis of ordered and natively unfolded proteins are different. For ordered protein to fibrillate, its unique and rigid structure has to be destabilized and partially unfolded. On the other hand, fibrillogenesis of a natively unfolded protein involves the formation of partially folded conformation; i.e., partial folding rather than unfolding. In this review recent findings are surveyed to illustrate some unique features of the natively unfolded proteins amyloidogenesis." @default.
- W2006654567 created "2016-06-24" @default.
- W2006654567 creator A5083199032 @default.
- W2006654567 date "2008-06-01" @default.
- W2006654567 modified "2023-10-10" @default.
- W2006654567 title "Amyloidogenesis of Natively Unfolded Proteins" @default.
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