Amyloid formation by globular proteins under native conditions.

By Fabrizio Chiti, Christopher M. Dobson. Nature Chemical Biology, 2009

829 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/6a05eef95c7154bbae9799293cef8d1b7e42bf5c

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Citations in the corpus

PASTA 2.0: an improved server for protein aggregation prediction (2014, background): “In fact, the presence of native structure plays a protective role against aggregation (23).”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “Thus, fully folded proteins must convert into a partially unstructured ensemble that is competent for aggregation, before self-assembly can proceed through one of the mechanisms described above (Figure 5a) (151).”
Intrinsically Semi-disordered State and Its Role in Induced Folding and Protein Aggregation (2013, background): “This instability of semi-disorder can initiate aggregation in structured proteins by local unfolding [53] (or as meta-stable states/regions [54–56]) and exposes self-complementary amyloidogenic segments protected by evolution [57].”
Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans (2010, background): “Indeed, studies have shown that many proteins have the potential, when misfolded, to aggregate via selfcomplementary sequences [9,10].”
De novo protein design, a retrospective (2020, background): “It is also interesting to note that the misfolding of the same protein sequences into amyloids (Chiti and Dobson, 2009) generally occurs through aggregation, presumably on a much rougher landscape.”
Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “However, the self-assembly of nativelike proteins can give rise to large fibrillar structures capable of binding ThT [53], such as observed for β2-microglobulin [54] and transthyretin [55].”
Spatiotemporal control of intracellular phase transitions using light-activated optoDroplets (2016, positive): “However, our data in living cells suggest that the severely slowed molecular dynamics inside the gel state may be important for promoting stable multi-protein contacts key for amyloid fiber assembly ((Chiti and Dobson, 2009), (Plakoutsi et al., 2005)).”