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1 tion pathways draw on reducing power held by NADPH-cytochrome P450 reductase.
2 two electrons delivered by the FMN domain of NADPH-cytochrome P450 reductase.
3 site conformations that cannot be reduced by NADPH-cytochrome P450 reductase.
4 1 is also mutually exclusive with binding of NADPH-cytochrome P450 reductase.
5 cytochrome b5 and a 10-fold molar excess of NADPH-cytochrome P450 reductase.
6 the presence of molecular oxygen, NADPH, and NADPH-cytochrome P450 reductase.
7 nditions by the one-electron reducing enzyme NADPH:cytochrome P450 reductase.
8 nd FMN-containing flavoprotein homologous to NADPH: cytochrome P450 reductase.
9 of an enzymatic assay specific for FMN-bound NADPH cytochrome P450 reductase activity in the absence
10 This treatment also results in increases in NADPH cytochrome P450 reductase and P-glycoprotein (the
11 reduction of oxygen by flavoenzymes such as NADPH-cytochrome P450 reductase and mitochondrial NADH d
12 s establish that reduction of the mutants by NADPH-cytochrome P450 reductase, as observed, is thermod
13 utathione synthetase, glutathione reductase, NADPH-cytochrome P450 reductase, biliverdin reductase, a
14 interactions were altered, and the putative NADPH-cytochrome P450 reductase binding site was reforme
18 -pong mechanism previously described for the NADPH-cytochrome P450 reductase-catalyzed reduction of c
19 enine dinucleotide phosphate (reduced form) (NADPH)-cytochrome P450 reductase cDNAs is also reported.
20 bolic resistance to insecticides and require NADPH cytochrome P450 reductase (CPR) to transfer electr
21 ecessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free ir
23 se model with liver-specific deletion of the NADPH-cytochrome P450 reductase (Cpr) gene (designated A
29 conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomai
30 NOS) flavin domains closely resemble that of NADPH-cytochrome P450 reductase (CPR), with the exceptio
33 d for mixed reconstituted systems containing NADPH-cytochrome P450 reductase, CYP2B4, and CYP1A2, whe
36 Heme oxygenase (HO) catalyzes the O(2)- and NADPH-cytochrome P450 reductase-dependent conversion of
37 Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of h
38 tants investigated, only G139A catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of h
39 ndividually does not significantly alter the NADPH-cytochrome P450 reductase-dependent reaction regio
40 HT in transgenic mice carrying a hypomorphic NADPH-cytochrome P450 reductase gene (Cpr-low mice).
41 esoheme by human truncated HO-1 supported by NADPH-cytochrome P450 reductase, H2O2, or ascorbate have
42 ) form of the reductase, the T491V mutant of NADPH-cytochrome P450 reductase has been reconstituted w
45 ion of HO-1, biliverdin reductase (BVR), and NADPH:cytochrome P450 reductase (NPR) in pulmonary arter
46 pressing NADH:cytochrome b5 reductase (NBR), NADPH:cytochrome P450 reductase (NPR), or NADPH: quinone
48 xidize heme in reactions supported by either NADPH-cytochrome P450 reductase or ascorbic acid has bee
50 chrome P450 monooxygenase system consists of NADPH-cytochrome P450 reductase (P450 reductase) and cyt
51 omes P450 requires the membrane-bound enzyme NADPH-cytochrome P450 reductase (P450 reductase), which
52 NADPH/FAD binding domains, respectively) of NADPH-cytochrome P450 reductases (P450 reductases), thes
53 [triiodothyronine (T3)] positively regulates NADPH cytochrome P450 reductase (P450R) mRNA expression
54 man CYP2B6) is delivered in combination with NADPH-cytochrome P450 reductase (P450R), which encodes t
57 me circumstances, also accept electrons from NADPH:cytochrome P450 reductase, potentially allowing fo
58 ) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron,
60 cted RNAi knock-down of Drosophila CYP4G1 or NADPH-cytochrome P450 reductase results in flies deficie
62 In the presence of ascorbate or the human NADPH cytochrome P450 reductase system, the heme-HemO co
64 n of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for
65 ol ring structure of heme in the presence of NADPH cytochrome P450 reductase, thereby releasing iron.
66 nstituted enzyme system containing NADPH and NADPH-cytochrome P450 reductase under aerobic conditions
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