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Drug-Target Interaction

Drug

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PubChem ID:10638
Structure:
Synonyms:
1,2-Benzenedicarboxylic acid, 3-amino-, cyclic hydrazide
1,4-Phthalazinedione, 5-amino-2,3-dihydro-
123072_ALDRICH
20666-12-0
20666-12-0 (MONOSODIUM SALT)
3-Aminophthalhydrazide
3-Aminophthalic acid hydrazide
3-Aminophthalic hydrazide
3-Aminophthaloylhydrazine
3-Aminophthalylhydrazide
5-Amino-1,2,3,4-tetrahydrophthalazine-1,4-dione
5-Amino-2,3-dihydro-1,4-phthalazinedione
5-Amino-2,3-dihydro-1,4-phthalazinedone
5-amino-2,3-dihydrophthalazine-1,4-dione
5-aminophthalazine-1,4-diol
521-31-3
521-31-3 (FREE ACID)
A5301
A8511_SIGMA
AB1008411
AC-13306
AC1L1VMP
AC1Q1H95
AC1Q51AX
AI3-52555
AIDS-009151
AIDS009151
AKOS000111313
AKOS002945870
BBL002758
BB_SC-2667
Bio-0419
CCRIS 5962
CHEBI:114906
CHEMBL442329
EINECS 208-309-4
EU-0066798
I06-0694
L-8600
L-8610
LS-177
Luminol
MLS002637790
MolPort-001-759-850
NCGC00091452-01
NCGC00091452-02
NSC 5064
NSC5064
NSC5064 (FREE ACID)
o-aminophthalylhydrazide
Oprea1_698774
Oprea1_819727
SBB057600
SDCCGMLS-0065581.P001
SMR001547307
ST5447781
STK138069
TL80090829
ZINC12405253

Target

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Uniprot ID:NOS3_HUMAN
Synonyms:
cNOS
Constitutive NOS
EC-NOS
Endothelial NOS
eNOS
Nitric oxide synthase, endothelial
NOS type III
NOSIII
EC-Numbers:1.14.13.39
Organism:Homo sapiens
Human
PDB IDs:1M9J 1M9K 1M9M 1M9Q 1M9R 3EAH 3NOS
Structure:
3NOS

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

8582646
Nitric oxide synthase inhibitors decrease human polymorphonuclear leukocyte luminol-dependent chemiluminescence.. S D Catz; M C Carreras; J J Poderoso (1995) Free radical biology & medicine display abstract
Nitric oxide synthase (NOS) inhibitors have been reported to modulate luminol-dependent chemiluminescence (CL) in rat macrophages, whereas the potent oxidant peroxynitrite (ONOO-) was shown to react with luminol to yield CL in a cell-free system. We evaluated the role of the L-arginine/NOS pathway in luminol CL by phorbol ester-activated human polymorphonuclear (PMN) leukocytes using the NOS inhibitors NG-monomethyl-L-arginine (L-NMMA) and N-iminoethyl-L-ornithine (L-NIO). Nitric oxide (.NO) release was determined by oxidation of oxymyoglobin. In addition, the effect of NOS inhibitors on superoxide anion O2.-) production was measured. Luminol CL was notably diminished by L-NMMA in a dose-dependent manner. Superoxide dismutase (SOD) also decreased luminol CL and L-NMMA potentiated light emission decrease produced by SOD. Nitric oxide and O2.- production was significantly decreased by L-NMMA; moreover, luminol-dependent CL but not O2.- production was attenuated by L-NIO. These data suggest that products of catalytic activity of both .NO synthase and NADPH oxidase are required to elicit maximal luminol CL in this system. These studies demonstrate that the NOS synthase pathway is involved in luminol CL by human PMN, and they suggest that ONOO- would be an unrecognized mediator in this phenomenon.