Results 211 to 220 of about 188,440 (262)
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Biochemical Society Transactions, 1996
Nitric oxide (NO) is a biologically active product enzymatically formed from a terminal guanidino-nitrogen of L-arginine by members of the NO synthase (NOS) gene family. Members of NO synthases are classified into three isoforms NOS 1, 2, and 3. This original classification of NOS was based on the physical and biochemical characteristics of the ...
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Nitric oxide (NO) is a biologically active product enzymatically formed from a terminal guanidino-nitrogen of L-arginine by members of the NO synthase (NOS) gene family. Members of NO synthases are classified into three isoforms NOS 1, 2, and 3. This original classification of NOS was based on the physical and biochemical characteristics of the ...
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Nitric oxide synthases and osteoarthritis
Current Rheumatology Reports, 2007The production of nitric oxide (NO) by chondrocytes is increased in human osteoarthritis. The excessive production of NO inhibits matrix synthesis and promotes its degradation. Furthermore, by reacting with oxidants such as superoxide anion, NO promotes cellular injury and renders the chondrocyte susceptible to cytokine-induced apoptosis.
Jose U, Scher +2 more
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Nitric oxide synthase and hypertension
Current Opinion in Nephrology and Hypertension, 2002Nitric oxide, the metabolic product of L-arginine by the enzyme nitric oxide synthase, plays a pivotal role in the regulation of vascular homeostasis. Its complex interaction with the autocrine and paracrine systems, particularly angiotensin II, modulates vasoconstriction and vasodilatation as well as the architectural remodeling of the vascular bed ...
Baudouin, Leclercq +2 more
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Bacterial Nitric Oxide Synthases
Annual Review of Biochemistry, 2010Nitric oxide synthases (NOSs) are multidomain metalloproteins first identified in mammals as being responsible for the synthesis of the wide-spread signaling and protective agent nitric oxide (NO). Over the past 10 years, prokaryotic proteins that are homologous to animal NOSs have been identified and characterized, both in terms of enzymology and ...
Brian R, Crane +2 more
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Mitochondrial nitric oxide synthase
Frontiers in Bioscience, 2007Nitric oxide (NO) regulates several cellular functions via reversible regulation of mitochondrial respiration. Nitric oxide also reacts with mitochondrial superoxide anion to produce the potent oxidative species peroxynitrite that irreversibly hinders mitochondrial activities. Recent findings demonstrating that mitochondria produce NO via mitochondrial
Pedram, Ghafourifar, Chandan K, Sen
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Endothelial Nitric Oxide Synthase
2011Diabetic nephropathy remains a leading cause for end-stage renal disease indicating a failure of current therapeutic strategies. One factor that impairs our ability to make advances has been the inadequacy of most animal models in manifesting advanced diabetic renal disease.
Takahiko, Nakagawa, Richard J, Johnson
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Mitochondrial nitric oxide synthase
Trends in Pharmacological Sciences, 2005Mitochondria produce nitric oxide (NO) through a Ca(2+)-sensitive mitochondrial NO synthase (mtNOS). The NO produced by mtNOS regulates mitochondrial oxygen consumption and transmembrane potential via a reversible reaction with cytochrome c oxidase.
Pedram, Ghafourifar, Enrique, Cadenas
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Regulation of nitric oxide synthase by nitric oxide.
Molecular Pharmacology, 1993Nitric oxide (NO) is a recently discovered messenger for the activation of soluble guanylate cyclase in a wide variety of cell types. Although enzymes involved in NO synthesis have been discovered, the regulation of their action is not clear. The possibility of NO regulating the activity of a crude NO synthase (EC 1.14.23) preparation from bovine ...
A, Rengasamy, R A, Johns
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Nitric oxide synthase in invertebrates
The Histochemical Journal, 1995The gas nitric oxide is now recognized as an important signalling molecule that is synthesized from L-arginine by the enzyme nitric oxide synthase. This enzyme can be localized by different methods, including immunocytochemistry and the histochemical reaction for NADPH diaphorase.
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Chemical Research in Toxicology, 1998
Inhibitory action of a variety of quinoid compounds on neuronal nitric oxide synthase (nNOS) activity was examined with a 20000g rat cerebellar supernatant preparation and purified nNOS. The inhibition of citrulline formation from l-arginine by quinones, which exhibit one-electron reduction potentials (E17) ranging between -240 and -100 mV, increased ...
Y, Kumagai +4 more
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Inhibitory action of a variety of quinoid compounds on neuronal nitric oxide synthase (nNOS) activity was examined with a 20000g rat cerebellar supernatant preparation and purified nNOS. The inhibition of citrulline formation from l-arginine by quinones, which exhibit one-electron reduction potentials (E17) ranging between -240 and -100 mV, increased ...
Y, Kumagai +4 more
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