Ontology highlight
ABSTRACT:
SUBMITTER: Barglow KT
PROVIDER: S-EPMC3167493 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Barglow Katherine T KT Knutson Charles G CG Wishnok John S JS Tannenbaum Steven R SR Marletta Michael A MA
Proceedings of the National Academy of Sciences of the United States of America 20110817 35
Protein S-nitrosation on cysteine residues has emerged as an important posttranslational modification in mammalian cells. Previous studies have suggested a primary role for thioredoxin (Trx) in controlling protein S-nitrosation reactions. Human Trx contains five conserved Cys, including two redox-active catalytic Cys (Cys32 and Cys35) and three non-active-site Cys (Cys62, Cys69, and Cys73), all of which have been reported as targets of S-nitrosation. Prior reports have studied thermodynamic end ...[more]