Ontology highlight
ABSTRACT:
SUBMITTER: Falsone SF
PROVIDER: S-EPMC3807654 | biostudies-literature | 2012 Aug
REPOSITORIES: biostudies-literature
Falsone S Fabio SF Meyer N Helge NH Schrank Evelyne E Leitinger Gerd G Pham Chi L L CL Fodero-Tavoletti Michelle T MT Holmberg Mats M Dulle Martin M Scicluna Benjamin B Gesslbauer Bernd B Rückert Hanna-Marie HM Wagner Gabriel E GE Merle David A DA Nollen Ellen A EA Kungl Andreas J AJ Hill Andrew F AF Cappai Roberto R Zangger Klaus K
Cell reports 20120726 2
The inherent cytotoxicity of aberrantly folded protein aggregates contributes substantially to the pathogenesis of amyloid diseases. It was recently shown that a class of evolutionary conserved proteins, called MOAG-4/SERF, profoundly alter amyloid toxicity via an autonomous but yet unexplained mode. We show that the biological function of human SERF1a originates from its atypical ability to specifically distinguish between amyloid and nonamyloid aggregation. This inherently unstructured protein ...[more]