Ontology highlight
ABSTRACT:
SUBMITTER: Walsh I
PROVIDER: S-EPMC4086119 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Walsh Ian I Seno Flavio F Tosatto Silvio C E SC Trovato Antonio A
Nucleic acids research 20140521 Web Server issue
The formation of amyloid aggregates upon protein misfolding is related to several devastating degenerative diseases. The propensities of different protein sequences to aggregate into amyloids, how they are enhanced by pathogenic mutations, the presence of aggregation hot spots stabilizing pathological interactions, the establishing of cross-amyloid interactions between co-aggregating proteins, all rely at the molecular level on the stability of the amyloid cross-beta structure. Our redesigned se ...[more]