2001
Dynamic regulation of metabolism and respiration by endogenously produced nitric oxide protects against oxidative stress
Paxinou E, Weisse M, Chen Q, Souza J, Hertkorn C, Selak M, Daikhin E, Yudkoff M, Sowa G, Sessa W, Ischiropoulos H. Dynamic regulation of metabolism and respiration by endogenously produced nitric oxide protects against oxidative stress. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 11575-11580. PMID: 11562476, PMCID: PMC58771, DOI: 10.1073/pnas.201293198.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseNitric oxideOxidative stressProtective effectNitric oxide protectsNitric oxide synthaseNitric oxide synthesisECV304 cellsSteady-state levelsMechanism of protectionOxide synthaseOxide synthesisENOS cDNAHuman ECV304 cellsMitochondria respirationDeathMitochondrial respirationExposureSame extentCellsCell metabolismDynamic regulationMetabolismLow steady-state levelsGlycolytic pathway
2000
Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation*
McCabe T, Fulton D, Roman L, Sessa W. Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by Phosphorylation*. Journal Of Biological Chemistry 2000, 275: 6123-6128. PMID: 10692402, DOI: 10.1074/jbc.275.9.6123.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalmodulinCattleDimerizationEgtazic AcidElectronsEnzyme ActivationKineticsMutationNADH DehydrogenaseNADPNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktStatic ElectricityConceptsSerine 1179Reductase domainCalmodulin dissociationProtein kinase AktWild-type eNOSBovine endothelial nitric oxide synthaseEndothelial nitric oxide synthaseKinase AktRate-limiting stepReductase activityPhosphorylationENOS activationNOS functionPotential mechanismsAspartateENOS catalytic activityENOS activityCytochrome c reductionAktCalmodulinDomainProteinMutationsProductionActivity
1997
Substrate Binding and Calmodulin Binding to Endothelial Nitric Oxide Synthase Coregulate Its Enzymatic Activity
Presta A, Liu J, Sessa W, Stuehr D. Substrate Binding and Calmodulin Binding to Endothelial Nitric Oxide Synthase Coregulate Its Enzymatic Activity. Nitric Oxide 1997, 1: 74-87. PMID: 9701047, DOI: 10.1006/niox.1996.0110.Peer-Reviewed Original Research