2011
S-nitrosylation of proteins: A new insight into endothelial cell function regulated by eNOS-derived NO
Iwakiri Y. S-nitrosylation of proteins: A new insight into endothelial cell function regulated by eNOS-derived NO. Nitric Oxide 2011, 25: 95-101. PMID: 21554971, PMCID: PMC3152628, DOI: 10.1016/j.niox.2011.04.014.BooksConceptsS-nitrosylationCellular processesGolgi apparatusIntracellular membrane domainPlasma membrane caveolaeEndothelial cell functionCell functionProtein traffickingMembrane caveolaeMembrane domainsCytoplasmic faceTarget proteinsCell cycleSignaling mechanismMessenger moleculesCell growthRedox stateProteinNitric oxide synthaseIntracellular reactionsNew insightsEndothelial NOSNitric oxideEndothelial nitric oxide synthaseFamily members
2006
Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking
Iwakiri Y, Satoh A, Chatterjee S, Toomre DK, Chalouni CM, Fulton D, Groszmann RJ, Shah VH, Sessa WC. Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 19777-19782. PMID: 17170139, PMCID: PMC1750883, DOI: 10.1073/pnas.0605907103.Peer-Reviewed Original ResearchConceptsProtein S-nitrosylationS-nitrosylationN-ethylmaleimide-sensitive factorPlasma membrane caveolaeAlters protein functionSpecific cysteine residuesSpecific posttranslational modificationsSpecific S-nitrosylationS-nitrosylation reactionsIntracellular transport processesProtein traffickingMembrane caveolaeProtein functionProtein transportPosttranslational modificationsCysteine residuesPlasma membraneTarget proteinsENOS localizationGolgi apparatusEndoplasmic reticulumGolgiDiffusible natureNOS actionGenerate nitric oxide