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
2005
Akt1/protein kinase Bα is critical for ischemic and VEGF-mediated angiogenesis
Ackah E, Yu J, Zoellner S, Iwakiri Y, Skurk C, Shibata R, Ouchi N, Easton RM, Galasso G, Birnbaum MJ, Walsh K, Sessa WC. Akt1/protein kinase Bα is critical for ischemic and VEGF-mediated angiogenesis. Journal Of Clinical Investigation 2005, 115: 2119-2127. PMID: 16075056, PMCID: PMC1180542, DOI: 10.1172/jci24726.Peer-Reviewed Original ResearchConceptsSerine-threonine protein kinaseAkt1/protein kinase BαProtein kinase BαProtein kinase BAkt1-/- miceIndividual Akt isoformsLoss of Akt1Substrate phosphorylationCellular functionsAkt substrateProtein kinaseAkt isoformsAkt1 knockout miceGene expressionGenetic lossKinase BBasal phosphorylationCell metabolismPostnatal angiogenesisCellular migrationVivo roleCell migrationAKT1Essential rolePhosphorylation