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(6R,S)-Methyl-tetrahydropterin
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activation in the absence of biopterin, not as effective as tetrahydrobiopterin
2',3'-bis-O-(carboxymethyl)-5'-deoxy-5'-(4-([methyl(4-[(1E,3E)-4-[4-(methylamino)phenyl]buta-1,3-dien-1-yl]phenyl)amino]methyl)-1H-1,2,3-triazol-1-yl)adenosine
nanotrigger NT2-2
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2'-O-(carboxymethyl)-5'-deoxy-5'-(4-([methyl(4-[(1E,3E)-4-[4-(methylamino)phenyl]buta-1,3-dien-1-yl]phenyl)amino]methyl)-1H-1,2,3-triazol-1-yl)adenosine
nanotrigger NT2-6
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3'-O-(carboxymethyl)-5'-deoxy-5'-(4-([methyl(4-[(1E,3E)-4-[4-(methylamino)phenyl]buta-1,3-dien-1-yl]phenyl)amino]methyl)-1H-1,2,3-triazol-1-yl)adenosine
nanotrigger NT2-4
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5'-(4-([(4-[(1E,3E)-4-(4-aminophenyl)buta-1,3-dien-1-yl]phenyl)(methyl)amino]methyl)-1H-1,2,3-triazol-1-yl)-2',3'-bis-O-(carboxymethyl)-5'-deoxyadenosine
nanotrigger NT2-3
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5'-(4-([(4-[(1E,3E)-4-(4-aminophenyl)buta-1,3-dien-1-yl]phenyl)(methyl)amino]methyl)-1H-1,2,3-triazol-1-yl)-2'-O-(carboxymethyl)-5'-deoxyadenosine
nanotrigger NT2-7
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5'-(4-([(4-[(1E,3E)-4-(4-aminophenyl)buta-1,3-dien-1-yl]phenyl)(methyl)amino]methyl)-1H-1,2,3-triazol-1-yl)-3'-O-(carboxymethyl)-5'-deoxyadenosine
nanotrigger NT2-5
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5'-(4-([(4-[(1E,3E)-4-(4-aminophenyl)buta-1,3-dien-1-yl]phenyl)(methyl)amino]methyl)-1H-1,2,3-triazol-1-yl)-5'-deoxyadenosine
nanotrigger NT2-9
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5'-[2-[ethyl[4-[4-(4-aminophenyl)-1,3-butadienyl]phenyl]amino]ethylamino]-5'-oxo-5'-deoxyadenosine 2'-phosphoric acid
nanotrigger NT1
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A-23187
low levels of A-23187 stimulate nNOS activity
Acetylsalicylic acid
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maximal activation at 0.004 mM
heat shock protein 90
heat shock protein 90 enhances the affinity of wild-type enzyme to NADPH, L-arginine, and calmodulin but not to Ca2+ and BH4
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interferon gamma
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activates
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L-arginine
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L-arginine strongly stimulates oxygen consumption of eNOS and inhibits that of nNOS, nonhydrolyzable L-arginine analogues are not stimulatory
lipopolysaccharide
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from Escherichia coli, activates
thyroxin
0.001 mg thyroxin significantly increases nNOS activity and nNOS protein level to 153% compared to control
Ca2+/calmodulin
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activate the electron transfer
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Ca2+/calmodulin
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme
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Ca2+/calmodulin
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calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme
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Ca2+/calmodulin
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme
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Calmodulin
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Calmodulin
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substrate 2,6-dichlorophenolindophenol, about 10fold increase in activity in presence of calmodulin
Calmodulin
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required for catalysis
Calmodulin
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activates O2 consumption of eNOS
Calmodulin
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activates the neuronal NOS by binding and inhibiting the suppression through the C-terminal tail of the enzyme, overview
Calmodulin
Ca2+-calmodulin binds between the reductase and oxygenase domains to activate nitric-oxide synthesis. The enzyme adopts an ensemble of open and closed conformational states and that Ca2+-calmodulin binding induces a dramatic rearrangement of the reductase domain. Calmodulin-specific activation triggers release and rotation of the FMN subdomain to expose the flavin for electron transfer to the heme
Calmodulin
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry. An important effect of calmodulin binding is to suppress adventitious electron transfer from nNOS to molecular oxygen and thereby preventing accumulation of reactive oxygen species
dithiothreitol
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dithiothreitol
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requirement
tetrahydrobiopterin
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additional information
iNOS is induced by pathogens and their components, e.g. induction in alveolar macropages by infection with the intracellular pathogen Mycobacterium bovis
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additional information
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iNOS is induced by pathogens and their components, e.g. induction in alveolar macropages by infection with the intracellular pathogen Mycobacterium bovis
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additional information
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neopterin derivatives are completely inactive and do not bind to the enzyme
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additional information
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neopterin derivatives are completely inactive and do not bind to the enzyme
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additional information
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short-term (20-30 min) treatment of endothelial cells with the synthetic NO donor (Z)-1-[2-(2-aminoethyl)-N-(2-aminoethyl)amino](diazen-1-ium-1,2-diolate) increases the Ser1177 phosphorylation of the constitutively expressed endothelial NOS and the production of endogenous NO generated by eNOS from L-arginine, the phosphorylation of eNOS is Akt-dependent and completely reverted by the phosphatidylinositol-3 kinase inhibitor LY-294002
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additional information
design and synthesis of a series of two-photon absorbing and photoactivatable NADPH analogues (NT 1 and NT2). These compounds bear one or two carboxymethyl group(s) on the 2'- or/and 3'-position(s) of the ribose in the adenosine moiety, instead of a 2'-phosphate group, and differ by the nature of the electron donor in their photoactivatable chromophore (replacing the nicotinamide moiety). Ability of NTs to photoinduce eNOS-dependent NO production in endothelial cells. Two compounds, those bearing a single carboxymethyl group on the 3'-position of the ribose, colocalize with the Golgi apparatus (the main intracellular location of eNOS) and display high intracellular two-photon brightness. Furthermore, a eNOS-dependent photooxidation is observed for these two compounds only, which is accompanied by a substantial intracellular NO production accounting for specific photocytotoxic effects. NT photoactivation efficiently triggers electron flow at the eNOS level and increases the basal production of NO by endothelial cells, structure-activity relationship of NTs in the cell context, overview
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additional information
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fibroblast growth factor-2 teratment up-regulates the enzyme in tectume, but down-regultes it in the optic nerve, overview
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additional information
hepatic isozyme iNOS expression is induced in chronic liver cirrhosis early stages
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