Ontology highlight
ABSTRACT:
SUBMITTER: Iwakiri Y
PROVIDER: S-EPMC1750883 | biostudies-other | 2006 Dec
REPOSITORIES: biostudies-other
Iwakiri Yasuko Y Satoh Ayano A Chatterjee Suvro S Toomre Derek K DK Chalouni Cecile M CM Fulton David D Groszmann Roberto J RJ Shah Vijay H VH Sessa William C WC
Proceedings of the National Academy of Sciences of the United States of America 20061214 52
Nitric oxide (NO) is a highly diffusible and short-lived physiological messenger. Despite its diffusible nature, NO modifies thiol groups of specific cysteine residues in target proteins and alters protein function via S-nitrosylation. Although intracellular S-nitrosylation is a specific posttranslational modification, the defined localization of an NO source (nitric oxide synthase, NOS) with protein S-nitrosylation has never been directly demonstrated. Endothelial NOS (eNOS) is localized mainly ...[more]