Oxidation of the zinc-thiolate complex and uncoupling of endothelial nitric oxide synthase by peroxynitrite.
By M. Zou, Chaomei Shi, R. Cohen. 2002
664 citations recorded by the source corpus.
Subfields: Biophysics, Inorganic Chemistry, Physiology
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Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “This results in the disruption of the dimer and a transition to the monomeric state, parallelled by the disruption of the enzyme activity (46,55).”
- Endothelial Dysfunction and Diabetes: Effects on Angiogenesis, Vascular Remodeling, and Wound Healing (2012, background): “In addition, peroxynitrite causes eNOS uncoupling through 26S proteasomedependent degradation of GCH leading to the release of zinc from the zinc-thiolate cluster of eNOS, which presumably leads to the formation of disulfide bonds between monomers [146].”
- Oxidative stress and reactive oxygen species in endothelial dysfunction associated with cardiovascular and metabolic diseases. (2018, background): “When endothelial cells in culture are exposed to different stimuli that mimic the metabolic alterations underlying endothelial dysfunction, such as native and oxidized low density lipoproteins (LDL) [66], angiostatin [67], homocysteine [68] and high glucose [69, 70], they become more susceptible to ”
- The role of oxidative stress in diabetic complications (2007, background): “enzymes that incorporate O2 into L-arginine and require flavin, NADPH, heme, and tetrahydrobiopterin cofactors (72,73).”
- New insights on oxidative stress and diabetic complications may lead to a "causal" antioxidant therapy. (2003, background): “uncoupling state of eNOS, presumably via a zinc depletion of the enzyme, favoring superoxide overproduction (38).”
- Adiponectin: A novel adipokine linking adipocytes and vascular function. (2004, positive): “ROS can reduce NO availability, consuming NO in the chemical formation of peroxynitrite, which has also been postulated to alter the catalytic activity of endothelial NO synthase (eNOS), diverting its synthesis from NO toward increased superoxide production (10).”