Ontology highlight
ABSTRACT:
SUBMITTER: Bieschke J
PROVIDER: S-EPMC2867908 | biostudies-other | 2010 Apr
REPOSITORIES: biostudies-other
Bieschke Jan J Russ Jenny J Friedrich Ralf P RP Ehrnhoefer Dagmar E DE Wobst Heike H Neugebauer Katja K Wanker Erich E EE
Proceedings of the National Academy of Sciences of the United States of America 20100412 17
Protein misfolding and formation of beta-sheet-rich amyloid fibrils or aggregates is related to cellular toxicity and decay in various human disorders including Alzheimer's and Parkinson's disease. Recently, we demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibits alpha-synuclein and amyloid-beta fibrillogenesis. It associates with natively unfolded polypeptides and promotes the self-assembly of unstructured oligomers of a new type. Whether EGCG disassembles preformed a ...[more]