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Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system

Lassegue, B.; San Martin, A.; Griendling, K.K.; Circ. Res. 110, 1364-1390 (2012)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
angiotensin II
stimulates Nox1
Homo sapiens
betaPix
a Rac1 guanine nucleotide exchange factor, appears to be constitutively bound to Nox1 and essential for its activity
Homo sapiens
H2O2
Nox5 can be upregulated and activated by minute concentrations of hydrogen peroxide
Homo sapiens
heat shock protein 90
binding of heat shock protein 90 to the C-terminus of Nox5 appears to stabilize the protein and enhance expression and activity
Homo sapiens
interleukin-1beta
stimulates Nox1
Homo sapiens
additional information
agonists appear to stimulate Nox1 in specific locations, thus determining where superoxide is produced: extracellularly by muscarinic agonists and thrombin, in endosomes by IL-1beta and TNF-alpha, both inside and outside cells by angiotensin II. Nox activators comprise p67phox and the structurally similar Noxa1. In colon the cytosolic subunits p47phox and p67phox are not expressed and are replaced by Noxo1 and Noxa1. Besides p47phox, other possible organizers include Tks4 and Tks5, two Src substrates with a PX domain and multiple SH3 domains capable of binding p22phox and Noxa1, but not p67phox. Cdc42 cannot activate Nox1
Homo sapiens
NOXA1
in contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Noxa1 contains four Rac-binding TPR motifs, a Nox activation domain and an SH3 domain that interacts with the prolinerich region of an organizer subunit, But the p40phox-binding PB1 domain is not well conserved and the SH3 domain in the middle of the molecule is missing. Phosphorylation of Noxa1 by protein kinase A favors binding to 14-3-3 and dissociation from Nox1, whereas other kinases appear to decrease Noxa1 affinity for Rac1 and Nox1. In contrast, phosphorylation of Noxa1 by Src on tyrosine 110 increases Nox1 activity
Homo sapiens
NOXO1
In contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Unlike p47phox, because Noxo1 lacks an autoinhibitory domain, it is thought to constitutively bind the cytochrome, but similar to p47phox, Noxo1 facilitates oxidase assembly by binding both an activator subunit and p22phox. The proline-rich region of Noxo1 binds to an SH3 domain of the activator, whereas the tandem SH3 domains of Noxo1 bind to the proline-rich region of p22phox. Noxo1 also binds to the dehydrogenase domain of Nox1. The PX domain of Noxo1 provides an essential affinity for membrane phosphoinositides
Homo sapiens
p67phox
activation domain of p67phox triggers FAD reduction by Nox2. P40phox appears to increase oxidase activity in cooperation with p47phox not by inducing translocation to the membrane, but by retaining the oxidase at the phagosome
Homo sapiens
Poldip2
reactive oxygen species production is enhanced by the multifunctional Poldip2, which also interacts with p22phox, presumably at the beginning of the cytosolic C-terminus, upstream of the region dispensable for Nox4 activity
Homo sapiens
Rac1
in addition to cytosolic organizers and activators, Nox1 also requires Rac1 for activity. Rac1 interacts directly with the C-terminus of Nox1, even in the absence of Noxa1. Nox1 is stimulated by constitutively active Rac1 and inhibited by Rac1 knockdown. Rac1 provides a crucial mechanism for activation by agonists, particularly in cells that exclusively express Nox1/Noxo1/Noxal. Rac1 does not activate Nox4 in transfected cells. Rac1 may participate in Nox5 activation
Homo sapiens
thrombin
stimulates Nox1 extracellularly
Homo sapiens
TNF-alpha
stimulates Nox1
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
additional information
Nox5 is unaffected by expression or knockdown p22phox intransfected cells. The cytosolic N-terminal segment, containing 4 calcium binding EF-hands is missing in Nox5S, a short calcium-insensitive variant, which is the dominant isoform in carcinoma cells, and expressed together with the long Nox5L in endothelial cells. Replacing the first transmembrane domain of Nox4 by that of Nox1, or altering the last extracellular loop of Nox4, makes it produce superoxide, rather than peroxide. Deletion of the NADPH binding domain produces a dominant-negative Nox4. Nox1-Nox4 and Nox2-Nox4 chimeras are active without transfection of cytosolic subunits, whereas the opposite Nox4-Nox2 chimera requires activation. Mutation of the proline-rich domain of p22phox required for docking organizers does not affect Nox4 activity
Homo sapiens
P437H
the mutation in the canonical NADPH binding motif of Nox4, analogous to the Nox2 mutation of a CGD patient, abolishes activity
Homo sapiens
R96E
Nox4 is inhibited by an R96E mutation in the cytosolic B loop, a region of the amino-terminal domain that interacts with the NADPH binding site
Homo sapiens
General Stability
General Stability
Organism
association with p22phox is required for Nox4 activity, the 2 proteins stabilize each other
Homo sapiens
Nox1 activity is dependent on chaperones Hsp90 and PDI, which appear to be necessary not only for protein folding after synthesis, but also to maintain enzyme stability
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
apocynin
inhibition of NOX1 and NOX2
Homo sapiens
Cdc42
a small monomeric GTPase, competitive inhibitor of Nox2, might also be a competitive inhibitor of Nox1
Homo sapiens
GK-136901
inhibition of NOX1 and NOX4
Homo sapiens
ML171
inhibition NOX1
Homo sapiens
additional information
V204A mutant is a competitive inhibitor of wild-type p67phox
Homo sapiens
Nox2ds-tat
inhibition of NAOX1 and NOX2
Homo sapiens
Plumbagin
inhibition of NOX4
Homo sapiens
VAS2870
inhibition of NOX2 and NOX4
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
caveola
NOX1
Homo sapiens
5901
-
cytoplasm
NOX4
Homo sapiens
5737
-
endoplasmic reticulum
NOX4
Homo sapiens
5783
-
endosome
; NOX1, Nox1 stimulation in endosomes is dependent on ClC-3, where this ion exchanger is required to balance the electrogenic activity of the enzyme
Homo sapiens
5768
-
focal adhesion
NOX4
Homo sapiens
5925
-
membrane
Nox1, like Nox2, associates with p22phox to form a membrane-bound cytochrome
Homo sapiens
16020
-
mitochondrion
NOX4
Homo sapiens
5739
-
additional information
Nox4 location varies according to cell type, different Nox4 isoforms may be present in specific subcellular locations
Homo sapiens
-
-
nuclear pore complex
NOX2
Homo sapiens
-
-
nucleus
NOX4
Homo sapiens
5634
-
plasma membrane
NOX1, NOX5, NOX2, and NOX4. The signal peptide at the N-terminus of Nox1 is important for localization at the plasma membrane, as it is prevented by replacement with the N-terminus of Nox4. A polybasic region in Nox5 with affinity for phosphoinositides may favor translocation to the plasma membrane and extracellular superoxide release
Homo sapiens
5886
-
stress fiber
NOX4
Homo sapiens
1725
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
an increase in cytosolic calcium concentration triggers high superoxide production by Nox5. Calcium induces binding of the N-terminal domain of Nox5 to the dehydrogenase domain, thus relieving autoinhibition. Two mechanisms may increase Nox5 sensitivity, allowing activation by resting calcium concentrations: (1) calcium-dependent binding of calmodulin to another site in the dehydrogenase domain157 and (2) phosphorylation of serine and threonine residues by protein kinase C and calcium/calmodulin-dependent kinase II
Homo sapiens
Fe2+
heme iron
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. NOX2-produced superoxide can be released outside the cell when Nox2 is located at the plasma membrane, thus allowing it to intercept, e.g., with endothelial-derived nitric oxide before it reaches the adjacent smooth muscle cell layer in vessels
?
-
-
-
NADH + H+ + O2
Homo sapiens
2 electrons are transferred from cytosolic NADPH to FAD and in succession across the membrane, via redox changes in heme irons. Finally, each electron reduces a molecule of oxygen to a superoxide radical, which is subsequently released outside the cell or in a topologically equivalent compartment, such as a vesicle lumen
NAD+ + H2O2
-
-
?
NADPH + H+ + O2
Homo sapiens
-
NADP+ + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
3 loops of Nox2 are extracellular and include consensus asparagine glycosylation sites. Phosphorylation of p67phox, mediated by PKCdelta, ERK2 and p38 MAPK, increases superoxide production by Nox2
Homo sapiens
phosphoprotein
phosphorylation of serine 461 by protein kinase A, serine 282 by ERK1/2 or p38 MAPK, or serine 172 by PKA or PKC, decreases ROS production by Nox1. Phosphorylation of p40phox on serine and threonine by PKC is increased during stimulation, particularly at threonine 154
Homo sapiens
Reaction
Reaction
Commentary
Organism
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2
a cytosolic C-terminal dehydrogenase domain includes an FAD cofactor and an NADPH substrate binding site. On activation, electrons are transferred from NADPH to FAD and across the membrane, via heme irons, to molecular oxygen, thus producing superoxide anion, which can be dismutated into hydrogen peroxide
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
blood vessel
-
Homo sapiens
-
carcinoma cell
the cytosolic N-terminal segment, containing 4 calcium binding EF-hands is missing in Nox5S, a short calcium-insensitive variant, which is the dominant isoform in carcinoma cells, and expressed together with the long Nox5L in endothelial cells. Nox5S may be constitutively active or be a competitive inhibitor of calcium-dependent activation when present in the same tetrameric complex as Nox5L
Homo sapiens
-
cardiomyocyte
in ischemic cardiomyocytes, Nox2 is upregulated in the cytosol and targeted to the nuclear pore complex
Homo sapiens
-
cardiovascular system
-
Homo sapiens
-
colon
Nox1 is most highly expressed in colon epithelium. In colon the cytosolic subunits p47phox and p67phox are not expressed and are replaced by Noxo1 and Noxa1
Homo sapiens
-
endothelial cell
-
Homo sapiens
-
epithelium
-
Homo sapiens
-
fibroblast
adventitial and cardial
Homo sapiens
-
lung
five splice variants of Nox4, named Nox4A through E, are found in lung epithelial cells
Homo sapiens
-
additional information
Nox5 expression is restricted to fewer tissues. Nox4 activity is constitutive, addition of cytosol to membrane fractions in transfected cells does not increase Nox4 activity, also transfection of organizer and activator subunits does not increase reactive oxygen species production
Homo sapiens
-
phagocyte
high expression level of Nox2
Homo sapiens
-
vascular smooth muscle cell
-
Homo sapiens
-
vascular wall
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. NOX2-produced superoxide can be released outside the cell when Nox2 is located at the plasma membrane, thus allowing it to intercept, e.g., with endothelial-derived nitric oxide before it reaches the adjacent smooth muscle cell layer in vessels
724778
Homo sapiens
?
-
-
-
-
NADH + H+ + O2
-
724778
Homo sapiens
NAD+ + H2O2
-
-
-
?
NADH + H+ + O2
2 electrons are transferred from cytosolic NADPH to FAD and in succession across the membrane, via redox changes in heme irons. Finally, each electron reduces a molecule of oxygen to a superoxide radical, which is subsequently released outside the cell or in a topologically equivalent compartment, such as a vesicle lumen
724778
Homo sapiens
NAD+ + H2O2
-
-
-
?
NADPH + H+ + O2
-
724778
Homo sapiens
NADP+ + H2O2
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
Nox2 structure homology modeling, and structure and activation mechanism of NOX proteins, overview. Nox2 is composed of two main domains of equal sizes with very different properties. The amino-terminal moiety includes six transmembrane alpha-helices I-VI connected by 5 loops A-E. The cytosolic carboxy-terminal moiety of Nox2 constitutes a dehydrogenase domain that includes consensus binding sites for its NADPH substrate and FAD cofactor. NOX2 p40phox is composed of an N-terminal PX domain, a central SH3 domain and a C-terminal PB1 domain. The C-terminal PB1 domain of p40phox interacts with the PB1 domain of p67phox
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
a dehydrogenase domain is binding FAD and NADPH, Nox1, Nox2, and Nox4 requires FAD and NADPH. Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites
Homo sapiens
heme
4 conserved histidine residues in transmembrane helices III and V, thought to coordinate 2 heme molecules, mutation of these histidines abolishes binding to p22phox
Homo sapiens
NADH
-
Homo sapiens
NADPH
a dehydrogenase domain is binding FAD and NADPH, Nox1, Nox2, and Nox4 requires FAD and NADPH. Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites
Homo sapiens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
angiotensin II
stimulates Nox1
Homo sapiens
betaPix
a Rac1 guanine nucleotide exchange factor, appears to be constitutively bound to Nox1 and essential for its activity
Homo sapiens
H2O2
Nox5 can be upregulated and activated by minute concentrations of hydrogen peroxide
Homo sapiens
heat shock protein 90
binding of heat shock protein 90 to the C-terminus of Nox5 appears to stabilize the protein and enhance expression and activity
Homo sapiens
interleukin-1beta
stimulates Nox1
Homo sapiens
additional information
agonists appear to stimulate Nox1 in specific locations, thus determining where superoxide is produced: extracellularly by muscarinic agonists and thrombin, in endosomes by IL-1beta and TNF-alpha, both inside and outside cells by angiotensin II. Nox activators comprise p67phox and the structurally similar Noxa1. In colon the cytosolic subunits p47phox and p67phox are not expressed and are replaced by Noxo1 and Noxa1. Besides p47phox, other possible organizers include Tks4 and Tks5, two Src substrates with a PX domain and multiple SH3 domains capable of binding p22phox and Noxa1, but not p67phox. Cdc42 cannot activate Nox1
Homo sapiens
NOXA1
in contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Noxa1 contains four Rac-binding TPR motifs, a Nox activation domain and an SH3 domain that interacts with the prolinerich region of an organizer subunit, But the p40phox-binding PB1 domain is not well conserved and the SH3 domain in the middle of the molecule is missing. Phosphorylation of Noxa1 by protein kinase A favors binding to 14-3-3 and dissociation from Nox1, whereas other kinases appear to decrease Noxa1 affinity for Rac1 and Nox1. In contrast, phosphorylation of Noxa1 by Src on tyrosine 110 increases Nox1 activity
Homo sapiens
NOXO1
In contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Unlike p47phox, because Noxo1 lacks an autoinhibitory domain, it is thought to constitutively bind the cytochrome, but similar to p47phox, Noxo1 facilitates oxidase assembly by binding both an activator subunit and p22phox. The proline-rich region of Noxo1 binds to an SH3 domain of the activator, whereas the tandem SH3 domains of Noxo1 bind to the proline-rich region of p22phox. Noxo1 also binds to the dehydrogenase domain of Nox1. The PX domain of Noxo1 provides an essential affinity for membrane phosphoinositides
Homo sapiens
p67phox
activation domain of p67phox triggers FAD reduction by Nox2. P40phox appears to increase oxidase activity in cooperation with p47phox not by inducing translocation to the membrane, but by retaining the oxidase at the phagosome
Homo sapiens
Poldip2
reactive oxygen species production is enhanced by the multifunctional Poldip2, which also interacts with p22phox, presumably at the beginning of the cytosolic C-terminus, upstream of the region dispensable for Nox4 activity
Homo sapiens
Rac1
in addition to cytosolic organizers and activators, Nox1 also requires Rac1 for activity. Rac1 interacts directly with the C-terminus of Nox1, even in the absence of Noxa1. Nox1 is stimulated by constitutively active Rac1 and inhibited by Rac1 knockdown. Rac1 provides a crucial mechanism for activation by agonists, particularly in cells that exclusively express Nox1/Noxo1/Noxal. Rac1 does not activate Nox4 in transfected cells. Rac1 may participate in Nox5 activation
Homo sapiens
thrombin
stimulates Nox1 extracellularly
Homo sapiens
TNF-alpha
stimulates Nox1
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
a dehydrogenase domain is binding FAD and NADPH, Nox1, Nox2, and Nox4 requires FAD and NADPH. Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites
Homo sapiens
heme
4 conserved histidine residues in transmembrane helices III and V, thought to coordinate 2 heme molecules, mutation of these histidines abolishes binding to p22phox
Homo sapiens
NADH
-
Homo sapiens
NADPH
a dehydrogenase domain is binding FAD and NADPH, Nox1, Nox2, and Nox4 requires FAD and NADPH. Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
Nox5 is unaffected by expression or knockdown p22phox intransfected cells. The cytosolic N-terminal segment, containing 4 calcium binding EF-hands is missing in Nox5S, a short calcium-insensitive variant, which is the dominant isoform in carcinoma cells, and expressed together with the long Nox5L in endothelial cells. Replacing the first transmembrane domain of Nox4 by that of Nox1, or altering the last extracellular loop of Nox4, makes it produce superoxide, rather than peroxide. Deletion of the NADPH binding domain produces a dominant-negative Nox4. Nox1-Nox4 and Nox2-Nox4 chimeras are active without transfection of cytosolic subunits, whereas the opposite Nox4-Nox2 chimera requires activation. Mutation of the proline-rich domain of p22phox required for docking organizers does not affect Nox4 activity
Homo sapiens
P437H
the mutation in the canonical NADPH binding motif of Nox4, analogous to the Nox2 mutation of a CGD patient, abolishes activity
Homo sapiens
R96E
Nox4 is inhibited by an R96E mutation in the cytosolic B loop, a region of the amino-terminal domain that interacts with the NADPH binding site
Homo sapiens
General Stability (protein specific)
General Stability
Organism
association with p22phox is required for Nox4 activity, the 2 proteins stabilize each other
Homo sapiens
Nox1 activity is dependent on chaperones Hsp90 and PDI, which appear to be necessary not only for protein folding after synthesis, but also to maintain enzyme stability
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
apocynin
inhibition of NOX1 and NOX2
Homo sapiens
Cdc42
a small monomeric GTPase, competitive inhibitor of Nox2, might also be a competitive inhibitor of Nox1
Homo sapiens
GK-136901
inhibition of NOX1 and NOX4
Homo sapiens
ML171
inhibition NOX1
Homo sapiens
additional information
V204A mutant is a competitive inhibitor of wild-type p67phox
Homo sapiens
Nox2ds-tat
inhibition of NAOX1 and NOX2
Homo sapiens
Plumbagin
inhibition of NOX4
Homo sapiens
VAS2870
inhibition of NOX2 and NOX4
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
caveola
NOX1
Homo sapiens
5901
-
cytoplasm
NOX4
Homo sapiens
5737
-
endoplasmic reticulum
NOX4
Homo sapiens
5783
-
endosome
; NOX1, Nox1 stimulation in endosomes is dependent on ClC-3, where this ion exchanger is required to balance the electrogenic activity of the enzyme
Homo sapiens
5768
-
focal adhesion
NOX4
Homo sapiens
5925
-
membrane
Nox1, like Nox2, associates with p22phox to form a membrane-bound cytochrome
Homo sapiens
16020
-
mitochondrion
NOX4
Homo sapiens
5739
-
additional information
Nox4 location varies according to cell type, different Nox4 isoforms may be present in specific subcellular locations
Homo sapiens
-
-
nuclear pore complex
NOX2
Homo sapiens
-
-
nucleus
NOX4
Homo sapiens
5634
-
plasma membrane
NOX1, NOX5, NOX2, and NOX4. The signal peptide at the N-terminus of Nox1 is important for localization at the plasma membrane, as it is prevented by replacement with the N-terminus of Nox4. A polybasic region in Nox5 with affinity for phosphoinositides may favor translocation to the plasma membrane and extracellular superoxide release
Homo sapiens
5886
-
stress fiber
NOX4
Homo sapiens
1725
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
an increase in cytosolic calcium concentration triggers high superoxide production by Nox5. Calcium induces binding of the N-terminal domain of Nox5 to the dehydrogenase domain, thus relieving autoinhibition. Two mechanisms may increase Nox5 sensitivity, allowing activation by resting calcium concentrations: (1) calcium-dependent binding of calmodulin to another site in the dehydrogenase domain157 and (2) phosphorylation of serine and threonine residues by protein kinase C and calcium/calmodulin-dependent kinase II
Homo sapiens
Fe2+
heme iron
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. NOX2-produced superoxide can be released outside the cell when Nox2 is located at the plasma membrane, thus allowing it to intercept, e.g., with endothelial-derived nitric oxide before it reaches the adjacent smooth muscle cell layer in vessels
?
-
-
-
NADH + H+ + O2
Homo sapiens
2 electrons are transferred from cytosolic NADPH to FAD and in succession across the membrane, via redox changes in heme irons. Finally, each electron reduces a molecule of oxygen to a superoxide radical, which is subsequently released outside the cell or in a topologically equivalent compartment, such as a vesicle lumen
NAD+ + H2O2
-
-
?
NADPH + H+ + O2
Homo sapiens
-
NADP+ + H2O2
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
3 loops of Nox2 are extracellular and include consensus asparagine glycosylation sites. Phosphorylation of p67phox, mediated by PKCdelta, ERK2 and p38 MAPK, increases superoxide production by Nox2
Homo sapiens
phosphoprotein
phosphorylation of serine 461 by protein kinase A, serine 282 by ERK1/2 or p38 MAPK, or serine 172 by PKA or PKC, decreases ROS production by Nox1. Phosphorylation of p40phox on serine and threonine by PKC is increased during stimulation, particularly at threonine 154
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
blood vessel
-
Homo sapiens
-
carcinoma cell
the cytosolic N-terminal segment, containing 4 calcium binding EF-hands is missing in Nox5S, a short calcium-insensitive variant, which is the dominant isoform in carcinoma cells, and expressed together with the long Nox5L in endothelial cells. Nox5S may be constitutively active or be a competitive inhibitor of calcium-dependent activation when present in the same tetrameric complex as Nox5L
Homo sapiens
-
cardiomyocyte
in ischemic cardiomyocytes, Nox2 is upregulated in the cytosol and targeted to the nuclear pore complex
Homo sapiens
-
cardiovascular system
-
Homo sapiens
-
colon
Nox1 is most highly expressed in colon epithelium. In colon the cytosolic subunits p47phox and p67phox are not expressed and are replaced by Noxo1 and Noxa1
Homo sapiens
-
endothelial cell
-
Homo sapiens
-
epithelium
-
Homo sapiens
-
fibroblast
adventitial and cardial
Homo sapiens
-
lung
five splice variants of Nox4, named Nox4A through E, are found in lung epithelial cells
Homo sapiens
-
additional information
Nox5 expression is restricted to fewer tissues. Nox4 activity is constitutive, addition of cytosol to membrane fractions in transfected cells does not increase Nox4 activity, also transfection of organizer and activator subunits does not increase reactive oxygen species production
Homo sapiens
-
phagocyte
high expression level of Nox2
Homo sapiens
-
vascular smooth muscle cell
-
Homo sapiens
-
vascular wall
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. NOX2-produced superoxide can be released outside the cell when Nox2 is located at the plasma membrane, thus allowing it to intercept, e.g., with endothelial-derived nitric oxide before it reaches the adjacent smooth muscle cell layer in vessels
724778
Homo sapiens
?
-
-
-
-
NADH + H+ + O2
-
724778
Homo sapiens
NAD+ + H2O2
-
-
-
?
NADH + H+ + O2
2 electrons are transferred from cytosolic NADPH to FAD and in succession across the membrane, via redox changes in heme irons. Finally, each electron reduces a molecule of oxygen to a superoxide radical, which is subsequently released outside the cell or in a topologically equivalent compartment, such as a vesicle lumen
724778
Homo sapiens
NAD+ + H2O2
-
-
-
?
NADPH + H+ + O2
-
724778
Homo sapiens
NADP+ + H2O2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
Nox2 structure homology modeling, and structure and activation mechanism of NOX proteins, overview. Nox2 is composed of two main domains of equal sizes with very different properties. The amino-terminal moiety includes six transmembrane alpha-helices I-VI connected by 5 loops A-E. The cytosolic carboxy-terminal moiety of Nox2 constitutes a dehydrogenase domain that includes consensus binding sites for its NADPH substrate and FAD cofactor. NOX2 p40phox is composed of an N-terminal PX domain, a central SH3 domain and a C-terminal PB1 domain. The C-terminal PB1 domain of p40phox interacts with the PB1 domain of p67phox
Homo sapiens
Expression
Organism
Commentary
Expression
Homo sapiens
NOX1 is upregulated by angiotensin II, PDGF, PGF, LDL, TNF-alpha, oscillatory shear stress BMP4, aldosterone plus salt, IFN-gamma, ET-1, T3, urokinase8, oxidized LDL, and vascular injury. NOX2 is upregulated by angiotensin II, ET-1, TGF-beta, IFN-gamma, oxidized LDL oscillatory shear stress, aldosterone plus salt, Ischemia, and vascular injury.NOX4 is upregulated by TGF-beta, thromboxane, TNF-alpha. IFN-gamma, urotensin, urokinase, oscillatory shear stress, hypoxia, hyperoxia vascular injury. NOX5 iss upregulated by angiotensin II, ET-1, thromboxane A2, TNF-alpha, atherosclerosis. Nox5 can be upregulated and activated by minute concentrations of hydrogen peroxide. In ischemic cardiomyocytes, Nox2 is upregulated in the cytosol and targeted to the nuclear pore complex
up
General Information
General Information
Commentary
Organism
malfunction
in pathological circumstances, excess Nox2 can lead to oxidative stress and disease development. NOX2 V204A mutant is a competitive inhibitor of wild-type p67phox. Binding of the PB1 domain of NOX2 to p40phox is abolished by a K355A mutation in NOX2. Depletion or mutation of p40phox impairs reactive oxygen species production in neutrophils and endothelial cells. Upregulation of Nox1 can lead to oxidative stress in the cardiovascular system
Homo sapiens
metabolism
tight regulation, critical to avoid excessive production of deleterious superoxide, is evident from the large number of proteins involved in oxidase assembly. These include Nox2 itself, p22phox, p47phox, p67phox, and p40phox, all essential subunits whose mutations can cause CGD Also crucial is Rac GTPase, which binds p67phox and the dehydrogenase domain of Nox2. In the resting state, Nox2 and p22phox form an inactive membrane complex known as cytochrome b558. Product superoxide is the first reactive oxygen species in a cascade of metabolites including hydrogen peroxide and peroxynitrite
Homo sapiens
additional information
Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites, but neither Nox5 isoform appears to require cytosolic subunits or p22phox. Presence of an additional cytosolic N-terminal segment, containing 4 calcium binding EF-hands in Nox5. Nox4 activity is constitutive, isozyme Nox4D appears to be fully active, although it lacks most of the transmembrane domain, it might retain activity by coupling to electron acceptors, such as cytochrome c in mitochondria, which might also be an alternative route of hydrogen peroxide formation by full-length Nox4. Nox4, Nox1 and Nox2 bind to p22phox, the interaction is abolished by mutation of heme-binding histidine 115. Nox2 is composed of two main domains of equal sizes with very different properties. The amino-terminal moiety includes six transmembrane alpha-helices I-VI connected by 5 loops A-E. Because both N- and C-termini are cytosolic, 3 loops are extracellular and include consensus asparagine glycosylation sites, whereas the other 2 are intracellular and accessible to cytosolic regulators. The cytosolic carboxy-terminal moiety of Nox2 constitutes a dehydrogenase domain that includes consensus binding sites for its NADPH substrate and FAD cofactor, activation domain of p67phox triggers FAD reduction by Nox2. A charge compensation mechanism, required to balance electron transport by Nox2 and sustain its activity, is provided by a voltage-gated proton channel8 and the chloride/proton antiporter ClC-3. The first SH3 domain of NOX2 increases oxidase activity, the NOX2 PB1 domain allows binding to p40phox. The C-terminal SH3 domain of p67phox of NOX2 is responsible for binding the proline-rich region of p47phox and therefore allows p67phox translocation to the membrane after activation. The C-terminal PB1 domain of p40phox interacts with the PB1 domain of p67phox. Nox1, like Nox2, associates with p22phox to form a membrane-bound cytochrome
Homo sapiens
physiological function
NADPH oxidase enzymes are critical mediators of cardiovascular physiology and pathophysiology. They are expressed in virtually all cardiovascular cells, and regulate such diverse functions as differentiation, proliferation, apoptosis, senescence, inflammatory responses and oxygen sensing. They target a number of important signaling molecules, including kinases, phosphatases, transcription factors, ion channels, and proteins that regulate the cytoskeleton. On activation, Nox2 uses NADPH to reduce molecular oxygen to superoxide anion, which, in concert with its metabolites, is used by phagocytes to destroy invading microorganisms. Nox organizers include both p47phox and its homologue, Noxo1, whereas Nox activators comprise p67phox and the structurally similar Noxa1. Because Nox2 and Nox1 are closely related, both enzymes can be activated in transfected cells by various organizer and activator pairs. Nox1 plays a host defensive role in colon epithelium. primary biochemical function of vascular Nox1 is superoxide production, which is then rapidly converted to hydrogen peroxide. The moderate physiological activity of Nox1, compared with the phagocytic Nox2, can be attributed to its low expression as well as specific regulatory subunits and signaling cascades. Nox4 is a constitutively active enzyme mostly regulated by transcription. Role of enzyme complex component p22phox, detailed overview. Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. Isozyme Nox5S may be constitutively active or be a competitive inhibitor of calcium-dependent activation when present in the same tetrameric complex as Nox5L
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
in pathological circumstances, excess Nox2 can lead to oxidative stress and disease development. NOX2 V204A mutant is a competitive inhibitor of wild-type p67phox. Binding of the PB1 domain of NOX2 to p40phox is abolished by a K355A mutation in NOX2. Depletion or mutation of p40phox impairs reactive oxygen species production in neutrophils and endothelial cells. Upregulation of Nox1 can lead to oxidative stress in the cardiovascular system
Homo sapiens
metabolism
tight regulation, critical to avoid excessive production of deleterious superoxide, is evident from the large number of proteins involved in oxidase assembly. These include Nox2 itself, p22phox, p47phox, p67phox, and p40phox, all essential subunits whose mutations can cause CGD Also crucial is Rac GTPase, which binds p67phox and the dehydrogenase domain of Nox2. In the resting state, Nox2 and p22phox form an inactive membrane complex known as cytochrome b558. Product superoxide is the first reactive oxygen species in a cascade of metabolites including hydrogen peroxide and peroxynitrite
Homo sapiens
additional information
Nox5 is similar to other Nox enzymes, with 6 transmembrane helices expected to bind 2 hemes and a cytosolic dehydrogenase domain including FAD and NADPH binding sites, but neither Nox5 isoform appears to require cytosolic subunits or p22phox. Presence of an additional cytosolic N-terminal segment, containing 4 calcium binding EF-hands in Nox5. Nox4 activity is constitutive, isozyme Nox4D appears to be fully active, although it lacks most of the transmembrane domain, it might retain activity by coupling to electron acceptors, such as cytochrome c in mitochondria, which might also be an alternative route of hydrogen peroxide formation by full-length Nox4. Nox4, Nox1 and Nox2 bind to p22phox, the interaction is abolished by mutation of heme-binding histidine 115. Nox2 is composed of two main domains of equal sizes with very different properties. The amino-terminal moiety includes six transmembrane alpha-helices I-VI connected by 5 loops A-E. Because both N- and C-termini are cytosolic, 3 loops are extracellular and include consensus asparagine glycosylation sites, whereas the other 2 are intracellular and accessible to cytosolic regulators. The cytosolic carboxy-terminal moiety of Nox2 constitutes a dehydrogenase domain that includes consensus binding sites for its NADPH substrate and FAD cofactor, activation domain of p67phox triggers FAD reduction by Nox2. A charge compensation mechanism, required to balance electron transport by Nox2 and sustain its activity, is provided by a voltage-gated proton channel8 and the chloride/proton antiporter ClC-3. The first SH3 domain of NOX2 increases oxidase activity, the NOX2 PB1 domain allows binding to p40phox. The C-terminal SH3 domain of p67phox of NOX2 is responsible for binding the proline-rich region of p47phox and therefore allows p67phox translocation to the membrane after activation. The C-terminal PB1 domain of p40phox interacts with the PB1 domain of p67phox. Nox1, like Nox2, associates with p22phox to form a membrane-bound cytochrome
Homo sapiens
physiological function
NADPH oxidase enzymes are critical mediators of cardiovascular physiology and pathophysiology. They are expressed in virtually all cardiovascular cells, and regulate such diverse functions as differentiation, proliferation, apoptosis, senescence, inflammatory responses and oxygen sensing. They target a number of important signaling molecules, including kinases, phosphatases, transcription factors, ion channels, and proteins that regulate the cytoskeleton. On activation, Nox2 uses NADPH to reduce molecular oxygen to superoxide anion, which, in concert with its metabolites, is used by phagocytes to destroy invading microorganisms. Nox organizers include both p47phox and its homologue, Noxo1, whereas Nox activators comprise p67phox and the structurally similar Noxa1. Because Nox2 and Nox1 are closely related, both enzymes can be activated in transfected cells by various organizer and activator pairs. Nox1 plays a host defensive role in colon epithelium. primary biochemical function of vascular Nox1 is superoxide production, which is then rapidly converted to hydrogen peroxide. The moderate physiological activity of Nox1, compared with the phagocytic Nox2, can be attributed to its low expression as well as specific regulatory subunits and signaling cascades. Nox4 is a constitutively active enzyme mostly regulated by transcription. Role of enzyme complex component p22phox, detailed overview. Nox4 can produce a higher hydrogen peroxide to superoxide ratio than Nox1 and Nox2. Isozyme Nox5S may be constitutively active or be a competitive inhibitor of calcium-dependent activation when present in the same tetrameric complex as Nox5L
Homo sapiens
Expression (protein specific)
Organism
Commentary
Expression
Homo sapiens
NOX1 is upregulated by angiotensin II, PDGF, PGF, LDL, TNF-alpha, oscillatory shear stress BMP4, aldosterone plus salt, IFN-gamma, ET-1, T3, urokinase8, oxidized LDL, and vascular injury. NOX2 is upregulated by angiotensin II, ET-1, TGF-beta, IFN-gamma, oxidized LDL oscillatory shear stress, aldosterone plus salt, Ischemia, and vascular injury.NOX4 is upregulated by TGF-beta, thromboxane, TNF-alpha. IFN-gamma, urotensin, urokinase, oscillatory shear stress, hypoxia, hyperoxia vascular injury. NOX5 iss upregulated by angiotensin II, ET-1, thromboxane A2, TNF-alpha, atherosclerosis. Nox5 can be upregulated and activated by minute concentrations of hydrogen peroxide. In ischemic cardiomyocytes, Nox2 is upregulated in the cytosol and targeted to the nuclear pore complex
up
Other publictions for EC 1.6.3.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741619
Azouzi
NADPH oxidase NOX4 is a criti ...
Homo sapiens
Antioxid. Redox Signal.
26
864-877
2017
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741996
Souabni
The physicochemical propertie ...
Komagataella pastoris
Biochim. Biophys. Acta
1861
3520-3530
2017
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742197
Gandara
Evolutionary origin and funct ...
Aedes aegypti
BMC Evol. Biol.
17
92
2017
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742452
De Blasio
The superoxide dismutase mime ...
Rattus norvegicus
Eur. J. Pharmacol.
807
12-20
2017
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1
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743694
Magnani
Crystal structures and atomic ...
Cylindrospermum stagnale, Cylindrospermum stagnale PCC 7417
Proc. Natl. Acad. Sci. USA
114
6764-6769
2017
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1
1
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745080
Al-Harbi
Psoriasis-like inflammation l ...
Mus musculus
Int. Immunopharmacol.
46
1-8
2017
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742586
Chen
Cloning, characteristics, and ...
Oryctolagus cuniculus
Front. Physiol.
7
284
2016
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1
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6
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743287
Bermudez
NADPH oxidase isoform express ...
Mus musculus
Mol. Cell. Neurosci.
77
53-64
2016
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744948
Li
Molecular characterization of ...
Portunus trituberculatus
Fish Shellfish Immunol.
52
263-277
2016
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1
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2
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742310
Cachat
Phagocyte NADPH oxidase and s ...
Homo sapiens
Clin. Sci.
128
635-648
2015
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743573
van der Hoeven
Localization of the dual oxid ...
Caenorhabditis elegans
PLoS ONE
10
e0124091
2015
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743686
Ameziane-El-Hassani
NADPH oxidase DUOX1 promotes ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
112
5051-5056
2015
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743770
Libik-Konieczny
The localization of NADPH oxi ...
Mesembryanthemum crystallinum
Protoplasma
252
477-487
2015
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1
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727447
Harnvoravongchai
Characterization and gene dele ...
Thermococcus kodakarensis
Extremophiles
18
603-616
2014
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1
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1
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8
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10
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742557
Matsumoto
Characterization of N-glycosy ...
Homo sapiens, Mus musculus, Rattus norvegicus
Free Radic. Biol. Med.
68
196-204
2014
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3
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3
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742560
Donko
Hypothyroidism-associated mis ...
Mus musculus
Free Radic. Biol. Med.
73
190-200
2014
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1
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742567
Cooney
Characterization of the expre ...
Rattus norvegicus
Free Radic. Res.
48
929-939
2014
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743468
Nestler
Roothairless5, which function ...
Zea mays
Plant J.
79
729-740
2014
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High-cholesterol diet augments ...
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Clin. Exp. Pharmacol. Physiol.
36
764-769
2009
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697953
Sirichandra
Phosphorylation of the Arabido ...
Arabidopsis thaliana
FEBS Lett.
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698160
Aram
Deficiency of nicotinamide ade ...
Mus musculus
Hepatology
49
911-919
2009
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699108
Luxen
Heterodimerization controls lo ...
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J. Cell Sci.
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2
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699176
Bakri
First report of clinical, func ...
Homo sapiens
J. Clin. Immunol.
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699287
Kamizato
Interleukin 10 inhibits interf ...
Homo sapiens
J. Gastroenterol.
44
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2009
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700052
Keith
Delayed association of the NAD ...
Homo sapiens
Microbiology
155
1004-1015
2009
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700073
Zhang
Dependence of cathepsin L-indu ...
Bos taurus
Microvasc. Res.
78
45-50
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1
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700427
Jensen
Involvement of oxidative pathw ...
Rattus norvegicus
Neurochem. Int.
55
362-368
2009
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701019
Haruta
Depleting Rac1 in mouse rod ph ...
Mus musculus
Proc. Natl. Acad. Sci. USA
106
9397-9402
2009
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710816
Matsushima
Increased myocardial NAD(P)H o ...
Mus musculus
Am. J. Physiol. Heart Circ. Physiol.
297
H409-H416
2009
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2
1
1
2
-
-
710897
Muller
Nitric oxide, NAD(P)H oxidase, ...
Homo sapiens
Antioxid. Redox Signal.
11
1711-1731
2009
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1
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711645
Pan
Angiotensin II stimulates MCP- ...
Rattus norvegicus
Braz. J. Med. Biol. Res.
42
531-536
2009
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1
1
1
1
-
-
711688
Gao
Vascular NAD(P)H oxidase activ ...
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Cardiovasc. Res.
82
9-20
2009
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106
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106
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4
4
4
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711828
Saitoh
Telmisartan attenuates fatty-a ...
Mus musculus
Diabetes Metab.
35
392-397
2009
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1
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711856
Morgan
Association of NAD(P)H oxidase ...
Rattus norvegicus
Endocrinology
150
2197-2201
2009
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711969
Olekhnovich
Characterization of the NAD(P) ...
Helicobacter pylori, Helicobacter pylori G27 and SS1
FEBS J.
276
3354-3364
2009
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1
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1
1
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712062
Feillet-Coudray
Oxidative stress in rats fed a ...
Rattus norvegicus
Free Radic. Biol. Med.
46
624-632
2009
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-
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1
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4
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4
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1
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1
1
1
1
-
-
712075
Maraldi
NAD(P)H oxidase isoform Nox2 p ...
Homo sapiens
Free Radic. Res.
43
1111-1121
2009
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-
-
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2
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1
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1
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-
1
-
-
1
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-
712136
Zhang
Isoforms and functions of NAD( ...
Rattus norvegicus
Hypertension
53
556-563
2009
-
-
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1
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1
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1
1
1
1
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712573
Bhandarkar
Fulvene-5 potently inhibits NA ...
Mus musculus
J. Clin. Invest.
119
2359-2365
2009
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2
2
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712826
Zhang
Estrogen attenuates ischemic o ...
Rattus norvegicus
J. Neurosci.
29
13823-13836
2009
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1
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1
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-
713491
Polizio
Losartan exerts renoprotection ...
Rattus norvegicus
Regul. Pept.
156
28-33
2009
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2
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2
-
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713521
Zia
Oxidative-nitrosative stress i ...
Oryctolagus cuniculus
Stroke
40
2191-2198
2009
-
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1
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1
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1
2
2
1
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-
684278
Marcal
Up-regulation of NADPH oxidase ...
Homo sapiens
Am. J. Hematol.
83
41-45
2008
-
1
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684311
Chandramohan
Effects of dietary salt on int ...
Rattus norvegicus
Am. J. Nephrol.
28
158-167
2008
-
1
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684312
Benter
Angiotensin-(1-7) prevents act ...
Rattus norvegicus
Am. J. Nephrol.
28
25-33
2008
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1
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1
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2
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2
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-
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-
-
-
-
-
-
-
-
684351
Wolfort
CD4+ T lymphocytes mediate hyp ...
Mus musculus
Am. J. Physiol. Heart Circ. Physiol.
294
H2619-H2626
2008
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1
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1
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2
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-
-
-
-
-
-
-
684361
Chitano
Airway smooth muscle relaxatio ...
Mus musculus
Am. J. Physiol. Lung Cell. Mol. Physiol.
294
L139-L148
2008
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1
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1
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-
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-
-
-
-
-
-
684500
Turchan-Cholewo
NADPH oxidase drives cytokine ...
Mus musculus
Antioxid. Redox Signal.
11
193-204
2008
1
1
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1
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1
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1
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684695
Steffen
Mono-O-methylated flavanols an ...
Homo sapiens
Arch. Biochem. Biophys.
469
209-219
2008
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20
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20
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1
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684904
Ahluwalia
Characterisation of electron c ...
Homo sapiens
Biochem. Biophys. Res. Commun.
368
656-661
2008
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-
685016
Nisimoto
Activation of NADPH oxidase 1 ...
Homo sapiens
Biochem. J.
415
57-65
2008
1
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-
685277
Shen
Mutations in the PX-SH3A linke ...
Homo sapiens
Biochemistry
47
8855-8865
2008
-
-
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1
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685384
Inoue
Reactive oxygen species produc ...
Mus musculus
Biochim. Biophys. Acta
1783
789-802
2008
2
1
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685793
Tian
Fc{gamma}R-stimulated activati ...
Homo sapiens
Blood
112
3867-3877
2008
-
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1
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685888
Li
The NADPH oxidase is involved ...
Rattus norvegicus
Brain Res.
1226
199-208
2008
1
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685971
Zhao
Cardiac oxidative stress and r ...
Mus musculus
Cardiovasc. Pathol.
18
156-166
2008
-
1
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1
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685977
Sanchez
Exercise and tachycardia incre ...
Canis lupus familiaris
Cardiovasc. Res.
77
380-386
2008
-
1
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1
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685978
Ren
Regulation of swelling-activat ...
Oryctolagus cuniculus
Cardiovasc. Res.
77
73-80
2008
-
1
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1
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685982
Schlueter
Apocynin-induced vasodilation ...
Mus musculus, Rattus norvegicus
Cardiovasc. Res.
80
271-279
2008
-
-
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1
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685992
Owayed
Nitric oxide-mediated activati ...
Homo sapiens
Cell Biochem. Funct.
26
603-608
2008
1
1
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685998
Brechard
Store-operated Ca(2+) channels ...
Homo sapiens
Cell Calcium
44
492-506
2008
1
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686035
Zhang
Local production of O2- by NAD ...
Bos taurus
Cell. Signal.
20
637-644
2008
-
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2
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686306
Thallas-Bonke
Inhibition of NADPH oxidase pr ...
Rattus norvegicus
Diabetes
57
460-469
2008
-
1
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686418
Dammanahalli
Endothelin-1 inhibits NADPH ox ...
Homo sapiens
Endocrinology
149
4979-4987
2008
-
-
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686472
Cano-Dominguez
NADPH oxidases NOX-1 and NOX-2 ...
Neurospora crassa
Eukaryot. Cell
7
1352-1361
2008
-
-
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686562
Matthiesen
Inhibition of NADPH oxidase by ...
Rattus norvegicus
Eur. J. Pharmacol.
579
403-410
2008
-
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686616
Siragy
Renal (pro)renin receptor upre ...
Rattus norvegicus
Exp. Physiol.
93
709-714
2008
-
1
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686878
Ribe
Adenosine A2A receptor signali ...
Mus musculus
Free Radic. Biol. Med.
44
1433-1442
2008
-
-
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1
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1
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1
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1
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-
686879
Sheu
Inhibition of NADPH oxidase-re ...
Homo sapiens
Free Radic. Biol. Med.
44
2043-2050
2008
-
-
-
-
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1
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1
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1
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1
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-
-
-
-
686880
Benavente
Niacin restriction upregulates ...
Homo sapiens
Free Radic. Biol. Med.
44
527-537
2008
-
1
-
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1
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2
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2
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-
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-
686883
Coyoy
Role of NADPH oxidase in the a ...
Rattus norvegicus
Free Radic. Biol. Med.
45
1056-1064
2008
-
-
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2
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1
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-
687053
Jackson
Alpha2-adrenoceptors enhance a ...
Rattus norvegicus
Hypertension
51
719-726
2008
-
1
-
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-
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1
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1
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1
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-
-
-
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-
-
687099
Izakovicova Holla
Haplotype analysis of the NADP ...
Homo sapiens
Int. Arch. Allergy Immunol.
148
73-80
2008
-
1
-
-
1
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-
-
-
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1
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-
-
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-
-
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-
-
687150
Shono
Enhanced expression of NADPH o ...
Homo sapiens
Int. J. Cancer
123
787-792
2008
-
1
-
-
1
-
-
-
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1
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2
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-
-
687451
Nakashima
A prodigiosin analogue inactiv ...
Mus musculus
J. Biochem.
143
107-115
2008
-
-
-
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1
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3
-
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1
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1
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-
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-
687742
Bissonnette
Phosphatidylinositol 3-phospha ...
Homo sapiens
J. Biol. Chem.
283
2108-2119
2008
1
-
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1
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2
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1
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1
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1
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1
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1
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1
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1
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-
687798
Roepstorff
Stimulus-dependent regulation ...
Mus musculus
J. Biol. Chem.
283
7983-7993
2008
2
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1
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1
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1
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1
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1
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687806
Ogasawara
Synergistic activation of the ...
Arabidopsis thaliana
J. Biol. Chem.
283
8885-8892
2008
2
-
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4
-
1
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1
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1
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-
687932
Wakisaka
Oxidative stress through activ ...
Mus musculus
J. Cereb. Blood Flow Metab.
28
1175-1185
2008
-
1
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4
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1
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688219
Paul
Myeloid Src kinases regulate p ...
Mus musculus
J. Leukoc. Biol.
84
1141-1150
2008
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1
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688531
Zhang
Squamosamide derivative FLZ pr ...
Mus musculus, Rattus norvegicus
J. Neuroinflammation
5
21
2008
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1
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2
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688550
Park
Thrombin-induced oxidative str ...
Rattus norvegicus
J. Neurosci. Res.
86
1053-1063
2008
1
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688585
Schaeppi
Branched fungal beta-glucan ca ...
Mus musculus
J. Pathol.
214
434-444
2008
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1
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6
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688605
Li
Cyclooxygenase 2-selective and ...
Homo sapiens, Rattus norvegicus
J. Pharmacol. Exp. Ther.
326
745-753
2008
8
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688627
Zhou
Melatonin impairs NADPH oxidas ...
Rattus norvegicus
J. Pineal Res.
45
157-165
2008
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1
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688711
Hachisuka
Role of NADPH oxidase in tissu ...
Rattus norvegicus
J. Tissue Eng. Regen. Med.
2
430-435
2008
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1
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688753
Wang
NADPH oxidase-derived reactive ...
Homo sapiens
Leuk. Res.
32
429-436
2008
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1
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4
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1
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689034
Mayumi
Characterization of teleost ph ...
Cyprinus carpio
Mol. Immunol.
45
1720-1731
2008
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1
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7
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689225
Jang
Taxol induces oxidative neuron ...
Mus musculus
Neurosci. Lett.
443
17-22
2008
-
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1
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-
689471
Asai
MAPK signaling regulates nitri ...
Nicotiana benthamiana
Plant Cell
20
1390-1406
2008
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1
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4
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689682
Macpherson
NADPH oxidase involvement in c ...
Arabidopsis thaliana
Planta
227
1415-1418
2008
-
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1
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1
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-
690131
Riganti
The NADPH oxidase inhibitor ap ...
Mus musculus
Toxicol. Appl. Pharmacol.
228
277-285
2008
-
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1
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-
690132
Shvedova
Increased accumulation of neut ...
Mus musculus
Toxicol. Appl. Pharmacol.
231
235-240
2008
-
2
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1
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-
684269
Wong
Tetramethylpyrazine inhibits a ...
Rattus norvegicus
Am. J. Chin. Med.
35
1021-1035
2007
-
-
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1
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684310
Whaley-Connell
Albumin activation of NAD(P)H ...
Didelphis sp.
Am. J. Nephrol.
27
15-23
2007
1
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-
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-
684343
Orosz
Cigarette smoke-induced proinf ...
Rattus norvegicus
Am. J. Physiol. Heart Circ. Physiol.
292
H130-H139
2007
-
1
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2
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2
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2
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-
-
-
-
684345
Chen
NADPH oxidase modulates myocar ...
Mus musculus, Sus scrofa
Am. J. Physiol. Heart Circ. Physiol.
292
H1664-H1674
2007
-
2
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1
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2
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2
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2
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-
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684347
Fukatsu
Possible usefulness of apocyni ...
Bos taurus
Am. J. Physiol. Heart Circ. Physiol.
293
H790-H797
2007
-
1
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1
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1
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1
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1
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-
-
-
-
684358
Abdala-Valencia
Nonhematopoietic NADPH oxidase ...
Mus musculus
Am. J. Physiol. Lung Cell. Mol. Physiol.
292
L1111-L1125
2007
-
1
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1
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1
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-
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684364
Chen
Role of NADPH oxidase and ANG ...
Rattus norvegicus
Am. J. Physiol. Regul. Integr. Comp. Physiol.
293
R1619-R1629
2007
-
1
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1
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2
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1
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-
-
-
-
-
684368
Liu
Depolarization of the macula d ...
Oryctolagus cuniculus
Am. J. Physiol. Renal Physiol.
292
F1867-F1872
2007
1
1
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1
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-
684771
Choi
Mechanism of apoptosis induced ...
Homo sapiens
Arch. Pharm. Res.
30
1328-1335
2007
1
-
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-
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3
-
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1
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1
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-
-
684779
Datla
Important role of Nox4 type NA ...
Homo sapiens
Arterioscler. Thromb. Vasc. Biol.
27
2319-2324
2007
-
1
1
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1
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1
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3
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3
-
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-
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-
-
-
-
684781
Ceolotto
Rosiglitazone reduces glucose- ...
Homo sapiens
Arterioscler. Thromb. Vasc. Biol.
27
2627-2633
2007
-
1
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-
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1
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1
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1
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-
-
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-
-
-
-
684839
Ostanin
NADPH oxidase but not myeloper ...
Mus musculus
Biochem. Biophys. Res. Commun.
355
801-806
2007
-
1
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1
-
-
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-
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1
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-
-
-
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-
-
-
-
684859
Steffen
(-)-Epicatechin elevates nitri ...
Homo sapiens
Biochem. Biophys. Res. Commun.
359
828-833
2007
-
-
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2
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1
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-
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-
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684866
Verchier
Concerted activities of nitric ...
Homo sapiens
Biochem. Biophys. Res. Commun.
361
493-498
2007
-
-
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1
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1
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1
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-
-
684872
Nishikawa
Inhibition of NADPH oxidase su ...
Canis lupus familiaris, Homo sapiens
Biochem. Biophys. Res. Commun.
362
504-509
2007
-
-
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3
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-
684970
Pacquelet
Cross-talk between IRAK-4 and ...
Homo sapiens
Biochem. J.
403
451-461
2007
-
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1
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684977
Murillo
Activation of NADPH oxidase by ...
Rattus norvegicus
Biochem. J.
405
251-259
2007
1
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685335
Catarzi
Sphingosine 1-phosphate stimul ...
Mus musculus
Biochim. Biophys. Acta
1770
872-883
2007
2
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685345
Mouche
Reduced expression of the NADP ...
Mus musculus
Biochim. Biophys. Acta
1773
1015-1027
2007
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1
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685410
Miyano
Role of the small GTPase Rac i ...
Homo sapiens
Biochimie
89
1133-1144
2007
1
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1
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685865
Sicard
Influence of rosuvastatin on t ...
Rattus norvegicus
Br. J. Pharmacol.
151
979-986
2007
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1
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1
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685873
Campese
Regional expression of NO synt ...
Rattus norvegicus
Brain Res.
1134
27-32
2007
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685878
Miller
Cytotoxicity of paraquat in mi ...
Mus musculus
Brain Res.
1167
129-139
2007
1
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2
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685975
An
NADPH oxidase mediates angiote ...
Mus musculus
Cardiovasc. Res.
75
702-709
2007
-
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1
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2
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1
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685976
Chan
Adventitial application of the ...
Oryctolagus cuniculus
Cardiovasc. Res.
75
710-718
2007
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1
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1
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1
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1
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-
686030
Becker
Hydrophobic bile salts induce ...
Mus musculus
Cell. Physiol. Biochem.
19
89-98
2007
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1
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1
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1
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-
686113
Doerries
Critical role of the NAD(P)H o ...
Mus musculus
Circ. Res.
100
894-903
2007
-
1
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3
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1
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1
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686115
Mittal
Hypoxia-dependent regulation o ...
Homo sapiens, Mus musculus
Circ. Res.
101
258-267
2007
-
2
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5
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2
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-
-
686126
Silver
Overweight and obese humans de ...
Homo sapiens
Circulation
115
627-637
2007
-
1
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-
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1
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-
686520
Donini
NADPH oxidase of human dendrit ...
Homo sapiens
Eur. J. Immunol.
37
1194-1203
2007
2
1
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1
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1
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1
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1
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1
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-
686552
Ding
Increased oxidative stress in ...
Mus musculus
Eur. J. Pharmacol.
561
121-128
2007
-
1
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3
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1
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-
686556
Borges de Oliveira-Junior
Effects of BAY 41-2272, an act ...
Homo sapiens
Eur. J. Pharmacol.
567
43-49
2007
1
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1
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1
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-
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-
-
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-
686602
Glass
Changes in the subcellular dis ...
Rattus norvegicus
Exp. Neurol.
205
383-395
2007
-
1
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-
-
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4
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3
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4
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2
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-
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-
-
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-
686848
Chen
Isoobtusilactone A-induced apo ...
Homo sapiens, Rattus norvegicus
Food Chem. Toxicol.
45
1268-1276
2007
2
2
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-
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1
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2
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5
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2
2
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1
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5
-
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-
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-
-
-
-
-
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-
686859
Sheh
NADPH oxidase- and mitochondri ...
Rattus norvegicus
Free Radic. Biol. Med.
42
1610-1623
2007
-
1
-
-
-
-
-
-
-
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1
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1
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1
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1
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-
-
-
-
-
-
-
-
-
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-
686861
Deng
Gp91phox-containing NAD(P)H ox ...
Mus musculus
Free Radic. Biol. Med.
42
466-473
2007
2
1
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-
-
-
-
-
-
-
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3
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1
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2
1
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1
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-
-
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-
-
-
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-
-
-
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-
-
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-
686862
Liu
Glucose down-regulation of cGM ...
Rattus norvegicus
Free Radic. Biol. Med.
42
852-863
2007
-
1
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-
-
-
-
-
-
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1
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3
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1
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1
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1
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
686869
Stokes
Platelet-associated NAD(P)H ox ...
Mus musculus
Free Radic. Biol. Med.
43
22-30
2007
-
1
-
-
-
-
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1
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2
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2
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1
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1
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2
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-
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-
-
-
-
-
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-
686870
Qin
Inhibition of NADPH oxidase re ...
Oryctolagus cuniculus
Free Radic. Biol. Med.
43
271-281
2007
-
1
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-
-
-
1
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3
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1
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1
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1
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1
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-
-
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-
-
-
-
-
-
-
-
-
-
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-
686934
Riazi
Sex differences in renal nitri ...
Rattus norvegicus
Gend. Med.
4
214-229
2007
-
1
-
-
-
-
-
-
-
-
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2
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-
2
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1
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2
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-
-
-
-
-
-
-
-
-
-
-
-
687049
Wei
NADPH oxidase contributes to v ...
Rattus norvegicus
Hypertension
50
384-391
2007
-
1
-
-
-
-
-
-
-
-
-
-
-
1
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1
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1
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1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
687050
Datla
Induction of heme oxygenase-1 ...
Homo sapiens, Mus musculus, Rattus norvegicus
Hypertension
50
636-642
2007
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
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4
-
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3
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4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687051
Cao
Differential regulation of NAD ...
Rattus norvegicus
Hypertension
50
663-671
2007
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
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-
-
1
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1
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687314
Babilonia
Role of gp91phox -containing N ...
Mus musculus
J. Am. Soc. Nephrol.
18
2037-2045
2007
-
-
-
-
1
-
1
-
-
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1
-
2
-
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-
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-
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1
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1
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1
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1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687553
Si
NADPH oxidase NOX5-S mediates ...
Homo sapiens
J. Biol. Chem.
282
16244-16255
2007
-
-
-
-
1
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-
-
-
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-
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1
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-
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2
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1
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2
-
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-
-
-
-
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-
-
-
-
-
-
-
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-
687587
Usatyuk
Regulation of hyperoxia-induce ...
Homo sapiens
J. Biol. Chem.
282
23284-23295
2007
2
-
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1
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1
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-
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3
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2
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1
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3
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687620
Chen
Characterization of a mutation ...
Homo sapiens
J. Biol. Chem.
282
30273-30284
2007
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687649
Abid
NADPH oxidase activity selecti ...
Homo sapiens
J. Biol. Chem.
282
35373-35385
2007
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687674
Block
NAD(P)H oxidases regulate HIF- ...
Homo sapiens, Mus musculus
J. Biol. Chem.
282
8019-8026
2007
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687930
Ding
Oxidative stress and increased ...
Mus musculus
J. Cell. Physiol.
212
682-689
2007
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688150
Fan
Hemorrhagic shock induces NAD( ...
Mus musculus
J. Immunol.
178
6573-6580
2007
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688206
Benedyk
HaCaT keratinocytes overexpres ...
Homo sapiens
J. Invest. Dermatol.
127
2001-2011
2007
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688216
Gauss
Role of NF-kappaB in transcrip ...
Homo sapiens
J. Leukoc. Biol.
82
729-741
2007
1
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688446
Szoecs
Increased superoxide productio ...
Rattus norvegicus
J. Mol. Cell. Cardiol.
42
1111-1118
2007
1
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688530
Qian
Sinomenine, a natural dextroro ...
Rattus norvegicus
J. Neuroinflammation
4
23
2007
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688583
Chiriac
NADPH oxidase is required for ...
Homo sapiens, Mus musculus
J. Pathol.
212
56-65
2007
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688597
Teixeira
Effects of 5-cyclopropyl-2-[1- ...
Mus musculus
J. Pharmacol. Exp. Ther.
322
1093-1102
2007
1
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688599
Steinkamp-Fenske
Reciprocal regulation of endot ...
Homo sapiens
J. Pharmacol. Exp. Ther.
322
836-842
2007
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688636
Yang
NADPH oxidase-dependent hydrog ...
Triticum aestivum
J. Plant Physiol.
164
1429-1435
2007
1
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688739
Terashima
Relationship between coronary ...
Homo sapiens
Kobe J. Med. Sci.
53
107-117
2007
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688937
Kim
TNF-induced activation of the ...
Mus musculus
Mol. Cell
26
675-687
2007
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688991
Grasberger
Missense mutations of dual oxi ...
Homo sapiens
Mol. Endocrinol.
21
1408-1421
2007
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688992
Johnson
Congenital hypothyroidism, dwa ...
Mus musculus
Mol. Endocrinol.
21
1593-1602
2007
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1
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1
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4
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689097
Saito
Inhibition of NAD(P)H oxidase ...
Rattus norvegicus
Mol. Vis.
13
840-853
2007
-
1
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1
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689213
Nitti
PKC delta and NADPH oxidase in ...
Homo sapiens
Neurosci. Lett.
416
261-265
2007
-
1
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689235
Anantharam
Pharmacological inhibition of ...
Rattus norvegicus
Neurotoxicology
28
988-997
2007
-
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3
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1
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689238
Potocky
Reactive oxygen species produc ...
Nicotiana tabacum
New Phytol.
174
742-751
2007
-
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1
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1
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1
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1
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-
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-
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-
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-
689371
Stef
Inhibition of NAD(P)H oxidase ...
Homo sapiens
Pharmacol. Rep.
59
428-436
2007
-
1
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2
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689459
Kobayashi
Calcium-dependent protein kina ...
Solanum tuberosum
Plant Cell
19
1065-1080
2007
-
-
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2
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1
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4
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1
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1
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689468
Wong
Regulation of rice NADPH oxida ...
Oryza sativa
Plant Cell
19
4022-4034
2007
-
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1
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1
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5
-
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1
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1
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689683
Kumar
Strboh A homologue of NADPH ox ...
Solanum tuberosum
Planta
227
25-36
2007
-
-
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1
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1
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1
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1
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-
-
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-
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-
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-
689749
Egan
Generation of reactive oxygen ...
Magnaporthe grisea
Proc. Natl. Acad. Sci. USA
104
11772-11777
2007
-
1
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1
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1
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690006
Sabeur
Characterization of NADPH oxid ...
Equus caballus
Reproduction
134
263-270
2007
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4
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690084
Kahles
NADPH oxidase plays a central ...
Mus musculus, Sus scrofa
Stroke
38
3000-3006
2007
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2
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1
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1
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5
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2
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690180
Hwang
The PPARgamma ligand, rosiglit ...
Mus musculus
Vascul. Pharmacol.
46
456-462
2007
-
1
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1
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1
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1
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671217
Cheranov
TNF-alpha dilates cerebral art ...
Rattus norvegicus
Am. J. Physiol.
290
C964-C971
2006
1
1
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1
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1
1
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1
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671246
Biswas
Insulin-induced activation of ...
Homo sapiens
Am. J. Physiol. Heart Circ. Physiol.
292
758-766
2006
-
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1
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2
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1
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1
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Molecular interaction of NADPH ...
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1
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672212
Lountos
The crystal structure of NAD(P ...
Lactobacillus sanfranciscensis, Lactococcus lactis
Biochemistry
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Hiruta
Restricted expression of NADPH ...
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673137
Pfarr
Congenital hypothyroidism caus ...
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673469
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Grasberger
Identification of the maturati ...
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Hidalgo
A transverse tubule NADPH oxid ...
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675531
Jekabsone
Fibrillar beta-amyloid peptide ...
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J. Neuroinflammation
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676665
Hao
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Involvement of plasma-membrane ...
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677049
Hritz
Cofactor assisted gating mecha ...
Thermus thermophilus
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Activation of the phagocyte NA ...
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671214
El Hassani
Dual oxidase2 is expressed all ...
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671829
Petheo
Voltage- and NADPH-dependence ...
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672959
Liu
NADPH oxidase produces reactiv ...
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673106
Miller
NADPH oxidase activity and fun ...
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3
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1
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Harper
Differential regulation of dua ...
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673788
Djordjevic
The expression of the NADPH ox ...
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616-630
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673806
Maia
NADH oxidase activity of rat l ...
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674426
Li
Crucial role of two potential ...
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J. Biol. Chem.
280
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11
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Ameziane-El-Hassani
Dual oxidase-2 has an intrinsi ...
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280
30046-30054
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Fu
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Mechanism of Ca2+ activation o ...
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659408
Banfi
NOX3, a superoxide-generating ...
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Park
Direct interaction of TLR4 wit ...
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3589-3593
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Ambruso
NADPH oxidase activity of neut ...
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Mol. Genet. Metab.
81
313-321
2004
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Ferreira
Thyroid Ca2+/NADPH-dependent H ...
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270
2363-2368
2003
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Banfi
Two novel proteins activate su ...
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Moreno
Inactivating mutations in the ...
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Characterization of ThOX prote ...
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Matsushita
NADH dehydrogenase of Coryneba ...
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1
1
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Expression of reduced nicotina ...
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2001
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3
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636491
De Deken
Cloning of two human thyroid c ...
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8
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6
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2
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4
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6
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8
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719803
Arcari
A NAD(P)H oxidase isolated fro ...
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
J. Biol. Chem.
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2000
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4
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1
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3
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1
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4
1
2
1
4
1
1
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1
1
636492
Dupuy
Purification of a novel flavop ...
Caenorhabditis elegans, Homo sapiens, Sus scrofa
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1999
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1
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4
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6
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4
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3
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4
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6
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636493
Leseney
Biochemical characterization o ...
Homo sapiens, Sus scrofa
Biochimie
81
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1999
4
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2
4
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2
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3
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2
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2
1
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7
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6
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6
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1
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7
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636499
Gorin
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Regulation of the thyroid NADP ...
Sus scrofa
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1997
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2
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1
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636498
Carvalho
The Ca2+- and reduced nicotina ...
Sus scrofa
Endocrinology
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1996
4
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1
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4
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1
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394274
Umeki
Prostaglandin E1 and analogs o ...
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1
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1
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1
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394275
Umeki
Mechanisms for the activation/ ...
Bos taurus, Cavia porcellus, Homo sapiens, Sus scrofa
Ann. Hematol.
68
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1994
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4
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1
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1
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5
2
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636497
Ohayon
Inhibition of thyroid NADPH-ox ...
Sus scrofa
Mol. Cell. Endocrinol.
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133-141
1994
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11
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11
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394273
Capuozzo
Polyene antibiotics inhibit su ...
Bos taurus
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1993
2
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1
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1
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636494
Dupuy
Mechanism of hydrogen peroxide ...
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636496
Nakamura
Activation by ATP of calcium-d ...
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4
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Dupuy
Solubilization and characteris ...
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1986
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