Ontology highlight
ABSTRACT:
SUBMITTER: Paramore R
PROVIDER: S-EPMC3469841 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Paramore Robert R Morgan Gareth J GJ Davis Peter J PJ Sharma Carrie-Anne CA Hounslow Andrea A Taler-Verčič Ajda A Zerovnik Eva E Waltho Jonathan P JP Cliff Matthew J MJ Staniforth Rosemary A RA
Frontiers in molecular neuroscience 20121012
Unlike a number of amyloid-forming proteins, stefins, and in particular stefin B (cystatin B) form amyloids under conditions where the native state predominates. In order to trigger oligomerization processes, the stability of the protein needs to be compromised, favoring structural re-arrangement however, accelerating fibril formation is not a simple function of protein stability. We report here on how optimal conditions for amyloid formation lead to the destabilization of dimeric and tetrameric ...[more]