PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores.

ABSTRACT: Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. Prion-like conversion underlies important biological processes but is also connected to human disease. Yeast prions are the best understood transmissible amyloids. In these proteins, prion formation from an initially soluble state involves a structural conversion, driven, in many cases, by specific domains enriched in glutamine/asparagine (Q/N) residues. Importantly, domains sharing this compositional bias are also present in the proteomes of higher organisms, thus suggesting that prion-like conversion might be an evolutionary conserved mechanism. We have recently shown that the identification and evaluation of the potency of amyloid nucleating sequences in putative prion domains allows disc

SUBMITTER: Zambrano R 

PROVIDER: S-EPMC4489250 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature