Identifying the amylome, proteins capable of forming amyloid-like fibrils

By Lukasz Goldschmidt, Poh K. Teng, Roland Riek, David S. Eisenberg. Proceedings of the National Academy of Sciences of the United States of America, 2010

792 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “Amyloidogenic aggregation is observed with many protein sequences (Chiti and Dobson, 2006; Goldschmidt et al., 2010) and is often associated with the accumulation of soluble, oligomeric species that precede fibril formation and are thought to be responsible for toxicity (Campioni et al.”
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].”
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “However, the physiological relevance of these short peptides that do not occur naturally is unclear, and practically all proteins harbor short peptides that can adopt the amyloid form in isolation (Goldschmidt et al., 2010).”
Mass Spectrometry and Machine Learning Reveal Determinants of Client Recognition by Antiamyloid Chaperones (2022, background): “Some clues for targeted intervention can be gathered from nature, as the ability to form fibrils is widespread in the proteome (8).”