Ontology highlight
ABSTRACT:
SUBMITTER: Koharudin LM
PROVIDER: S-EPMC2872412 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Koharudin Leonardus M I LM Liu Hao H Di Maio Roberto R Kodali Ravindra B RB Graham Steven H SH Gronenborn Angela M AM
Proceedings of the National Academy of Sciences of the United States of America 20100315 15
Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) has been implicated in Parkinson's disease (PD) and is present in neurofibrillary tangles or Lewy bodies. However, the molecular basis for UCH-L1s involvement in proteinacious fibril formation is still elusive, especially in regard to the pathogenicity of the I93M mutation. Here we show that modification of UCH-L1 by cyclopentenone prostaglandins causes unfolding and aggregation. A single thiol group on Cys152 reacts with the alpha,beta-unsaturat ...[more]