PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10503941-6 1999 7-ER binds to nNOS with a Km value of 0.68 +/- 0.07 microM, as calculated from the nNOS-dependent NADPH oxidation in the absence of L-arginine. NADP 98-103 nitric oxide synthase 1 Homo sapiens 14-18 10503941-6 1999 7-ER binds to nNOS with a Km value of 0.68 +/- 0.07 microM, as calculated from the nNOS-dependent NADPH oxidation in the absence of L-arginine. NADP 98-103 nitric oxide synthase 1 Homo sapiens 83-87 10503941-7 1999 nNOS catalyzes the reduction of 7-ER at the expense of NADPH. NADP 55-60 nitric oxide synthase 1 Homo sapiens 0-4 9688579-6 1998 The IC50 for nNOS was 18 +/- 6 microM GST-PIN with 63 nM nNOS after 30 min at 37 degrees C. Uncoupled NADPH oxidation was inhibited similarly, whereas cytochrome c reductase activity, the K(M) for L-arginine, and dimerization were unaffected. NADP 102-107 nitric oxide synthase 1 Homo sapiens 13-17 9398256-2 1997 CaM binding to nNOS facilitates the transfer of NADPH-derived electrons from the reductase domain to the oxygenase domain, resulting in the conversion of L-arginine to L-citrulline with the concomitant formation of a guanylate cyclase activating factor, putatively nitric oxide. NADP 48-53 nitric oxide synthase 1 Homo sapiens 15-19 9535869-2 1998 Nitric oxide synthase (NOS) catalyzes the NADPH- and O2-dependent conversion of L-arginine to nitric oxide (NO) and citrulline; three isoforms, the neuronal (nNOS), endothelial, and inducible, have been identified. NADP 42-47 nitric oxide synthase 1 Homo sapiens 0-21 9535869-2 1998 Nitric oxide synthase (NOS) catalyzes the NADPH- and O2-dependent conversion of L-arginine to nitric oxide (NO) and citrulline; three isoforms, the neuronal (nNOS), endothelial, and inducible, have been identified. NADP 42-47 nitric oxide synthase 1 Homo sapiens 158-162 9535869-7 1998 However, in the presence of NADPH and O2, L-VNIO irreversibly inactivates nNOS (kinact = 0.078 min-1; KI = 90 nM); inactivation is Ca2+/calmodulin-dependent. NADP 28-33 nitric oxide synthase 1 Homo sapiens 74-78 8955074-1 1996 Neuronal nitric-oxide synthase (NOS-1) is a hemeprotein that generates NO and citrulline from L-arginine, O2, and NADPH. NADP 114-119 nitric oxide synthase 1 Homo sapiens 32-37 9312270-10 1997 Thus supplying a single electron from NADPH to the heme iron permits nNOS to catalyze one full round of citrulline and NO synthesis from NOHA upon exposure to O2. NADP 38-43 nitric oxide synthase 1 Homo sapiens 69-73 9312270-11 1997 These data provide a molecular explanation for the NADPH requirement in the second step of the biosynthetic reaction, implicate ferrous-dioxy nNOS as a critical reactant in that step, and eliminate a number of possible alternative catalytic mechanisms or products. NADP 51-56 nitric oxide synthase 1 Homo sapiens 142-146 9312270-5 1997 The heme iron in calmodulin-bound nNOS was reduced with excess NADPH under anaerobic conditions, calmodulin was then dissociated from nNOS to prevent subsequent heme iron reduction, NOHA was added, and the reaction initiated by exposure to air. NADP 63-68 nitric oxide synthase 1 Homo sapiens 34-38 7578122-2 1995 Zn2+ blocks NADPH-dependent reduction of heme iron in nNOS and also blocks the calmodulin-dependent superoxide-mediated cytochrome c reductase activity exhibited by nNOS. NADP 12-17 nitric oxide synthase 1 Homo sapiens 54-58 8927232-3 1996 HP also inhibited the CaM-dependent NADPH consumption by n-NOS (IC50 = 221 microM). NADP 36-41 nitric oxide synthase 1 Homo sapiens 57-62 24737326-7 2014 Our three-dimensional reconstruction of the intact nNOS-CaM complex reveals a closed conformation and a cross-monomer arrangement with the FMN domain rotated away from the NADPH-FAD center, toward the oxygenase dimer. NADP 172-177 nitric oxide synthase 1 Homo sapiens 51-55 26923072-5 2016 The electron flow from NADPH to Flavin, and finally to the heme of the paired nNOS subunit within a dimer, is facilitated upon calmodulin (CaM) binding. NADP 23-28 nitric oxide synthase 1 Homo sapiens 78-82 26923072-7 2016 Therefore, it cannot inhibit the rate of NADPH-dependent heme reduction in nNOS, which results in l-Arginine oxidation. NADP 41-46 nitric oxide synthase 1 Homo sapiens 75-79 25921643-9 2015 These ligands have been targeted at four key binding sites of the nNOS enzyme - the tetrahydrobiopterin, calmodulin, nicotinamide adenine dinucleotide phosphate (NADPH) and arginine binding sites. NADP 117-160 nitric oxide synthase 1 Homo sapiens 66-70 25921643-9 2015 These ligands have been targeted at four key binding sites of the nNOS enzyme - the tetrahydrobiopterin, calmodulin, nicotinamide adenine dinucleotide phosphate (NADPH) and arginine binding sites. NADP 162-167 nitric oxide synthase 1 Homo sapiens 66-70 24610812-3 2014 In neuronal NOS (nNOS), 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. NADP 119-124 nitric oxide synthase 1 Homo sapiens 3-15 24610812-3 2014 In neuronal NOS (nNOS), 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. NADP 119-124 nitric oxide synthase 1 Homo sapiens 17-21 22929836-7 2012 Nitric oxide (NO) synthase which comes in three isoforms, as inducible-, neuronal- and endothelial-NOS, or iNOS, nNOS or eNOS, respectively, catalyzes the conversion of L- arginine to L-citrulline, using NADPH to produce NO. NADP 204-209 nitric oxide synthase 1 Homo sapiens 113-117 24129225-10 2013 NADPH-histochemistry revealed nNOS activity only in a part of neurons of that structure. NADP 0-5 nitric oxide synthase 1 Homo sapiens 30-34 23572278-3 2013 We studied in a large sample (763 subjects, age range 19-107 years) the variability of the three human genes (NOS1, -2, -3) coding for the three isoforms of the NADPH-dependent enzymes named NO synthases (NOS) which are responsible of NO synthesis. NADP 161-166 nitric oxide synthase 1 Homo sapiens 110-114 23572278-3 2013 We studied in a large sample (763 subjects, age range 19-107 years) the variability of the three human genes (NOS1, -2, -3) coding for the three isoforms of the NADPH-dependent enzymes named NO synthases (NOS) which are responsible of NO synthesis. NADP 161-166 nitric oxide synthase 1 Homo sapiens 191-203 20950274-4 2011 Mesohaem-nNOS catalysed NO synthesis and retained a coupled NADPH consumption much like the wild-type enzyme. NADP 60-65 nitric oxide synthase 1 Homo sapiens 9-13 18052254-1 2008 Fully coupled nitric oxide synthase (NOS) catalyzes formation of nitric oxide (NO), l-citrulline, NADP+, and water from l-arginine, NADPH, and oxygen. NADP 98-103 nitric oxide synthase 1 Homo sapiens 14-35 24453460-3 2011 NADPH oxidation (NADPH ox ) and acetylated cytochrome-c reduction (AcCyt-cred ) catalyzed by nNOS and the CaM binding sequence-deficient nNOS reductase construct (nNOS-FP) were estimates of total electron flux and [Formula: see text] production, respectively. NADP 0-5 nitric oxide synthase 1 Homo sapiens 93-97 24453460-3 2011 NADPH oxidation (NADPH ox ) and acetylated cytochrome-c reduction (AcCyt-cred ) catalyzed by nNOS and the CaM binding sequence-deficient nNOS reductase construct (nNOS-FP) were estimates of total electron flux and [Formula: see text] production, respectively. NADP 0-5 nitric oxide synthase 1 Homo sapiens 137-141 24453460-3 2011 NADPH oxidation (NADPH ox ) and acetylated cytochrome-c reduction (AcCyt-cred ) catalyzed by nNOS and the CaM binding sequence-deficient nNOS reductase construct (nNOS-FP) were estimates of total electron flux and [Formula: see text] production, respectively. NADP 0-5 nitric oxide synthase 1 Homo sapiens 137-141 24453460-3 2011 NADPH oxidation (NADPH ox ) and acetylated cytochrome-c reduction (AcCyt-cred ) catalyzed by nNOS and the CaM binding sequence-deficient nNOS reductase construct (nNOS-FP) were estimates of total electron flux and [Formula: see text] production, respectively. NADP 17-22 nitric oxide synthase 1 Homo sapiens 93-97 24453460-3 2011 NADPH oxidation (NADPH ox ) and acetylated cytochrome-c reduction (AcCyt-cred ) catalyzed by nNOS and the CaM binding sequence-deficient nNOS reductase construct (nNOS-FP) were estimates of total electron flux and [Formula: see text] production, respectively. NADP 17-22 nitric oxide synthase 1 Homo sapiens 137-141 24453460-3 2011 NADPH oxidation (NADPH ox ) and acetylated cytochrome-c reduction (AcCyt-cred ) catalyzed by nNOS and the CaM binding sequence-deficient nNOS reductase construct (nNOS-FP) were estimates of total electron flux and [Formula: see text] production, respectively. NADP 17-22 nitric oxide synthase 1 Homo sapiens 137-141 24453460-4 2011 All the DNBs (o-, m-, p-) independently stimulated rates of NADPH ox by CaM-free nNOS and by nNOS-FP in isomer- and concentration-dependent manner. NADP 60-65 nitric oxide synthase 1 Homo sapiens 81-85 24453460-4 2011 All the DNBs (o-, m-, p-) independently stimulated rates of NADPH ox by CaM-free nNOS and by nNOS-FP in isomer- and concentration-dependent manner. NADP 60-65 nitric oxide synthase 1 Homo sapiens 93-97 20529840-5 2010 The bridging interaction appeared to control FMN subdomain interactions with both its electron donor (NADPH-FAD subdomain) and electron acceptor (heme domain) partner subdomains in nNOS. NADP 102-107 nitric oxide synthase 1 Homo sapiens 181-185 18370414-7 2008 The reduction of CB1954 catalyzed by the neuronal NOS (nNOS) was inhibited by O 2 and a flavin/NADPH binding inhibitor, diphenyliodonium (DPI), but insensitive to the addition of the heme ligands imidazole and carbon monoxide and of l-arginine analogues. NADP 95-100 nitric oxide synthase 1 Homo sapiens 41-53 18370414-7 2008 The reduction of CB1954 catalyzed by the neuronal NOS (nNOS) was inhibited by O 2 and a flavin/NADPH binding inhibitor, diphenyliodonium (DPI), but insensitive to the addition of the heme ligands imidazole and carbon monoxide and of l-arginine analogues. NADP 95-100 nitric oxide synthase 1 Homo sapiens 55-59 18052254-1 2008 Fully coupled nitric oxide synthase (NOS) catalyzes formation of nitric oxide (NO), l-citrulline, NADP+, and water from l-arginine, NADPH, and oxygen. NADP 132-137 nitric oxide synthase 1 Homo sapiens 14-35 16966328-1 2006 The crystal structure of the neuronal nitric-oxide synthase (nNOS) NADPH/FAD binding domain indicated that Ser-1176 is within hydrogen bonding distance of Asp-1393 and the O4 atom of FAD and is also near the N5 atom of FAD (3.7 A). NADP 67-72 nitric oxide synthase 1 Homo sapiens 29-59 17454123-3 2007 Our results reveal that nNOS is activated by serotonin as both NADPH consumption and oxyhemoglobin (OxyHb) oxidation were enhanced. NADP 63-68 nitric oxide synthase 1 Homo sapiens 24-28 16966328-1 2006 The crystal structure of the neuronal nitric-oxide synthase (nNOS) NADPH/FAD binding domain indicated that Ser-1176 is within hydrogen bonding distance of Asp-1393 and the O4 atom of FAD and is also near the N5 atom of FAD (3.7 A). NADP 67-72 nitric oxide synthase 1 Homo sapiens 61-65 16150731-0 2005 C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase. NADP 40-45 nitric oxide synthase 1 Homo sapiens 79-109 17236649-5 2006 Expression of nNOS in the brain and peripheral nervous system is widely determined by staining with NADPH (reduced nicotinamide adenine dinucleotide phosphate) diaphorase or NOS immunoreactivity, and functional roles of NO formed by nNOS are evidenced in the early phylogenetic stages (invertebrates and fishes). NADP 100-105 nitric oxide synthase 1 Homo sapiens 14-18 17236649-5 2006 Expression of nNOS in the brain and peripheral nervous system is widely determined by staining with NADPH (reduced nicotinamide adenine dinucleotide phosphate) diaphorase or NOS immunoreactivity, and functional roles of NO formed by nNOS are evidenced in the early phylogenetic stages (invertebrates and fishes). NADP 115-158 nitric oxide synthase 1 Homo sapiens 14-18 16085316-8 2006 These results demonstrate that NADPH-d activity in the superficial spinal cord is ascribed to nNOS activity and is dependent on NMDA. NADP 31-36 nitric oxide synthase 1 Homo sapiens 94-98 16085316-9 2006 A combination of isolated intact spinal cord preparations and NADPH-d histochemistry may provide a unique system to elucidate biochemical and molecular mechanisms for nNOS activation in the spinal cord. NADP 62-67 nitric oxide synthase 1 Homo sapiens 167-171 12777376-9 2003 Reduction of the air-stable semiquinone (FAD-FMNH*) of both domains with NADPH showed that the extent of conversion of FADH2/FMNH* to FADH*/FMNH2 in the iNOS flavin domain was greater than that of the nNOS flavin domain. NADP 73-78 nitric oxide synthase 1 Homo sapiens 201-205 15748708-6 2005 As the concentration of L-arginine and N(omega)-hydroxyl-L-arginine increases, the rate of NADPH consumption for H(4)B-bound NOS1 decreased resulting in lower rates of both O(2)(*-) and H(2)O(2) generation, while increasing the rate of nitric oxide (*NO) production. NADP 91-96 nitric oxide synthase 1 Homo sapiens 125-129 15323562-2 2004 Here we report the preparation of the isolated flavin mononucleotide (FMN)-binding domain of nNOS with bound CaM and the electrochemical analysis of this and the isolated flavin adenine dinucleotide (FAD)-binding domain in the presence and absence of NADP(+) and ADP (an inhibitor). NADP 251-255 nitric oxide synthase 1 Homo sapiens 93-97 15180983-0 2004 The FAD-shielding residue Phe1395 regulates neuronal nitric-oxide synthase catalysis by controlling NADP+ affinity and a conformational equilibrium within the flavoprotein domain. NADP 100-105 nitric oxide synthase 1 Homo sapiens 44-74 15180983-3 2004 Here we characterized the F1395S mutant of the nNOS flavoprotein domain (nNOSr) regarding its physical properties, NADP(+) binding characteristics, flavin reduction kinetics, steady-state and pre-steady-state cytochrome c reduction kinetics, and ability to shield its FMN cofactor in response to CaM or NADP(H) binding. NADP 115-122 nitric oxide synthase 1 Homo sapiens 47-51 15180983-3 2004 Here we characterized the F1395S mutant of the nNOS flavoprotein domain (nNOSr) regarding its physical properties, NADP(+) binding characteristics, flavin reduction kinetics, steady-state and pre-steady-state cytochrome c reduction kinetics, and ability to shield its FMN cofactor in response to CaM or NADP(H) binding. NADP 303-310 nitric oxide synthase 1 Homo sapiens 47-51 14966111-11 2004 1) The presence and positioning of the Asp-1393 carboxylate side chain are critical to enable NADPH-dependent reduction of the nNOS flavoprotein. NADP 94-99 nitric oxide synthase 1 Homo sapiens 127-131 14681230-5 2004 CaV1p1 inhibited NO formation activity and NADPH oxidation of wild-type nNOS in a dose-dependent manner with an IC(50) value of 1.8 microM. NADP 43-48 nitric oxide synthase 1 Homo sapiens 72-76 14769337-0 2004 Application of the measurement of oxidized pyridine dinucleotides with high-performance liquid chromatography-fluorescence detection to assay the uncoupled oxidation of NADPH by neuronal nitric oxide synthase. NADP 169-174 nitric oxide synthase 1 Homo sapiens 178-208 14769337-7 2004 As an example, the activity of neuronal nitric oxide synthase (nNOS), a NADPH-requiring enzyme, has been assessed by measuring the products NADP+ and l-citrulline at various substrate (l-arginine) concentrations. NADP 72-77 nitric oxide synthase 1 Homo sapiens 31-61 14769337-7 2004 As an example, the activity of neuronal nitric oxide synthase (nNOS), a NADPH-requiring enzyme, has been assessed by measuring the products NADP+ and l-citrulline at various substrate (l-arginine) concentrations. NADP 72-77 nitric oxide synthase 1 Homo sapiens 63-67 14769337-7 2004 As an example, the activity of neuronal nitric oxide synthase (nNOS), a NADPH-requiring enzyme, has been assessed by measuring the products NADP+ and l-citrulline at various substrate (l-arginine) concentrations. NADP 140-145 nitric oxide synthase 1 Homo sapiens 31-61 14769337-7 2004 As an example, the activity of neuronal nitric oxide synthase (nNOS), a NADPH-requiring enzyme, has been assessed by measuring the products NADP+ and l-citrulline at various substrate (l-arginine) concentrations. NADP 140-145 nitric oxide synthase 1 Homo sapiens 63-67 14769337-8 2004 The rate of the uncoupled NADPH oxidation by nNOS can be estimated from the ratio of NADP+/l-citrulline produced. NADP 26-31 nitric oxide synthase 1 Homo sapiens 45-49 14769337-8 2004 The rate of the uncoupled NADPH oxidation by nNOS can be estimated from the ratio of NADP+/l-citrulline produced. NADP 85-90 nitric oxide synthase 1 Homo sapiens 45-49 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). NADP 200-205 nitric oxide synthase 1 Homo sapiens 123-127 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). NADP 200-205 nitric oxide synthase 1 Homo sapiens 91-121 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). NADP 232-237 nitric oxide synthase 1 Homo sapiens 91-121 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). NADP 232-237 nitric oxide synthase 1 Homo sapiens 123-127 11038356-5 2001 Computer simulations of the model precisely described both pre-steady and steady-state features of nNOS catalysis, including NADPH consumption and NO production, buildup of a heme-NO complex, changes between pre-steady and steady-state rates, and the change in enzyme K(m,O(2)) in the presence or absence of NO synthesis. NADP 125-130 nitric oxide synthase 1 Homo sapiens 99-103 11772017-3 2002 nNOS was found to abstract the pro-R (A-side) hydrogen from NADPH. NADP 60-65 nitric oxide synthase 1 Homo sapiens 0-4 12089147-4 2002 Pre-steady state reduction and oxidation time courses for the nNOS reductase domain indicate that CaM binding triggers NADP(+) release, which may exert control over steady-state turnover. NADP 119-126 nitric oxide synthase 1 Homo sapiens 62-66 11125020-3 2001 In the current study, we have discovered that agmatine, at concentrations much lower than the reported Ki value, leads to a time-, concentration-, NADPH-, and calmodulin-dependent irreversible inactivation of nNOS. NADP 147-152 nitric oxide synthase 1 Homo sapiens 209-213 11150917-1 2001 Nitric oxide synthase (NOS) catalyzes nitric oxide (NO) formation from L-arginine in the presence of molecular oxygen and NADPH. NADP 122-127 nitric oxide synthase 1 Homo sapiens 0-21 10799481-1 2000 Cu(2+) and Zn(2+) inhibit all of the NADPH-dependent reactions catalyzed by neuronal nitric-oxide synthase (nNOS) including ferricytochrome c reduction, NADPH oxidation, and citrulline formation. NADP 37-42 nitric oxide synthase 1 Homo sapiens 76-106 10924903-2 2000 The recombinant neuronal nitric oxide synthase (nNOS) reductase domain, which contains the FAD-FMN prosthetic group pair and calmodulin-binding site, catalyzed aerobic NADPH-oxidation in the presence of the model quinone compound menadione (MD), including antitumor mitomycin C (Mit C) and adriamycin (Adr). NADP 168-173 nitric oxide synthase 1 Homo sapiens 16-46 10924903-2 2000 The recombinant neuronal nitric oxide synthase (nNOS) reductase domain, which contains the FAD-FMN prosthetic group pair and calmodulin-binding site, catalyzed aerobic NADPH-oxidation in the presence of the model quinone compound menadione (MD), including antitumor mitomycin C (Mit C) and adriamycin (Adr). NADP 168-173 nitric oxide synthase 1 Homo sapiens 48-52 10945985-3 2000 H4B-free nNOS catalyzed Arg oxidation to N(omega)-hydroxy-l-Arg (NOHA) and citrulline in both NADPH- and H(2)O(2)-driven reactions. NADP 94-99 nitric oxide synthase 1 Homo sapiens 9-13 10799481-1 2000 Cu(2+) and Zn(2+) inhibit all of the NADPH-dependent reactions catalyzed by neuronal nitric-oxide synthase (nNOS) including ferricytochrome c reduction, NADPH oxidation, and citrulline formation. NADP 37-42 nitric oxide synthase 1 Homo sapiens 108-112 10799481-1 2000 Cu(2+) and Zn(2+) inhibit all of the NADPH-dependent reactions catalyzed by neuronal nitric-oxide synthase (nNOS) including ferricytochrome c reduction, NADPH oxidation, and citrulline formation. NADP 153-158 nitric oxide synthase 1 Homo sapiens 76-106 10799481-4 2000 Citrulline formation and NADPH oxidation by the full-length nNOS and ferricytochrome c reduction by the reductase domain are affected similarly by Cu(2+), with estimated IC(50) values ranging from 6 to 33 microm. NADP 25-30 nitric oxide synthase 1 Homo sapiens 60-64 10681501-9 2000 Steady-state absorbance spectra of nNOS recorded during uncoupled NADPH oxidation showed that the heme remained oxidized in the presence of the synthetic peptide consisting of amino acids 310-329 of the B2R, whereas the reduced oxyferrous heme complex was accumulated in its absence. NADP 66-71 nitric oxide synthase 1 Homo sapiens 35-39 10594372-1 1999 The neuronal NO synthase (nNOS) flavin domain, which has similar redox properties to those of NADPH-cytochrome P450 reductase (P450R), contains binding sites for calmodulin, FAD, FMN, and NADPH. NADP 94-99 nitric oxide synthase 1 Homo sapiens 26-30 10521442-8 1999 Reduction of nNOS heme by NADPH under rigorous anaerobic conditions was found to occur in the wild type enzyme only in the presence of Ca(2+)/CaM. NADP 26-31 nitric oxide synthase 1 Homo sapiens 13-17 10417510-11 1999 NADPH activity was present in all nNOS + naevi, but in two malignant cases, NADPH activity was not accompanied by nNOS expression. NADP 0-5 nitric oxide synthase 1 Homo sapiens 34-38 10417510-12 1999 We conclude that nNOS expression is induced de novo in benign and malignant pigment cell lesions which have all the requirements (NADPH, PIN) necessary for the production and modulation of NO. NADP 130-135 nitric oxide synthase 1 Homo sapiens 17-21 10428800-5 1999 Characterization of the FMN-depleted mutants showed that bound FMN was essential for reduction of the nNOS heme or cytochrome c, but not for ferricyanide or dichlorophenolindolphenol, and established that the electron transfer path in nNOS is NADPH to FAD to FMN to heme. NADP 243-248 nitric oxide synthase 1 Homo sapiens 102-106