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NADPH oxidase

Current Opinion in Immunology, 2004
NADPH oxidase is an enzyme that catalyzes the production of superoxide from oxygen and NADPH. It is a complex enzyme consisting of two membrane-bound components and three components in the cytosol, plus rac 1 or rac 2. Activation of the oxidase involves the phosphorylation of one of the cytosolic components.
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Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase

Biochemistry, 1988
The binding of the substrate NADPH as well as a number of fragments and derivatives of NADPH to glutathione reductase from human erythrocytes has been investigated by using X-ray crystallography. Crystals of the enzyme were soaked with the compounds of interest, and then the diffraction intensities were collected out to a resolution of 3 A.
Pai, E., Karplus, P., Schulz, G.
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The Neutrophil NADPH Oxidase

Archives of Biochemistry and Biophysics, 2002
The NADPH oxidase of phagocytes catalyzes the conversion of oxygen to O2(-). This multicomponent enzyme complex contains five essential protein components, two in the membrane and three in the cytosol. Unassembled and inactive in resting phagocytes, the oxidase becomes active after translocation of cytosolic components to the membrane to assemble a ...
B M, Babior, J D, Lambeth, W, Nauseef
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NADPH oxidases and cancer

Clinical Science, 2015
The mechanism by which reactive oxygen species (ROS) are produced by tumour cells remained incompletely understood until the discovery over the last 15 years of the family of NADPH oxidases (NOXs 1–5 and dual oxidases DUOX1/2) which are structural homologues of gp91phox, the major membrane-bound component of the respiratory burst oxidase of leucocytes.
Krishnendu, Roy   +8 more
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Cyanobacterial NADPH dehydrogenase complexes

Photosynthesis Research, 2007
Cyanobacteria possess functionally distinct multiple NADPH dehydrogenase (NDH-1) complexes that are essential to CO(2) uptake, photosystem-1 cyclic electron transport and respiration. The unique nature of cyanobacterial NDH-1 complexes is the presence of subunits involved in CO(2) uptake.
Teruo, Ogawa, Hualing, Mi
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NADPH-cytochrome P450 reductase

Archives of Biochemistry and Biophysics, 1976
Abstract The rate of reduction of cytochrome P450 in hepatic microsomes in the presence of NADPH has been measured with a dual wavelength stopped-flow spectrophotometer. The results obtained, with microsomes prepared from phenobarbital-pretreated rats, indicate that the reduction process is biphasic and most probably composed of two concurrent first ...
T, Matsubara   +3 more
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Paraquat and Iron-Dependent Lipid Peroxidation : NADPH Versus NADPH-Generating Systems

Biological Trace Element Research, 2000
The aim of this work was to study the effect of paraquat (P2+) on NADPH iron-dependent lipid peroxidation (basal peroxidation) either in the presence of NADPH or in the presence of NADPH-generating systems. When NADPH is present, P2+ potentiates NADPH iron-dependent lipid peroxidation, but use of NADPH-generating systems cancels this effect.
Y, Fernandez, F, Anglade, S, Mitjavila
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NADPH Oxidase: An Update

Blood, 1999
T HE NADPH OXIDASES are a group of plasma membrane–associated enzymes found in a variety of cells of mesodermal origin. The most thoroughly studied of these is the leukocyte NADPH oxidase, which is found in professional phagocytes and B lymphocytes.
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