Subcellular localization of Nox-containing oxidases provides unique insight into their role in vascular oxidant signaling.
Wolin
Michael S
MS
D000818:Animals; D021941:Caveolae / Q000201:enzymology*; D022001:Focal Adhesions / Q000201:enzymology*; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D008954:Models, Biological; D009131:Muscle, Smooth, Vascular / Q000201:enzymology*; D000074663:NADPH Oxidase 4; D019255:NADPH Oxidases / Q000502:physiology*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010544:Peroxidases / Q000378:metabolism; D010750:Phosphoproteins / Q000502:physiology; D017382:Reactive Oxygen Species / Q000378:metabolism; D015290:Second Messenger Systems; D013482:Superoxide Dismutase / Q000378:metabolism; D013481:Superoxides / Q000378:metabolism
D010750:Phosphoproteins; D017382:Reactive Oxygen Species; D013481:Superoxides; D006861:Hydrogen Peroxide; D010544:Peroxidases; D013482:Superoxide Dismutase; D000074663:NADPH Oxidase 4; D019255:NADPH Oxidases; C498910:NOX4 protein, human; C060505:neutrophil cytosolic factor 1