Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution
about
Tricyclic [1,2,4]triazine 1,4-dioxides as hypoxia selective cytotoxinsPseudosymmetry, high copy number and twinning complicate the structure determination ofDesulfovibrio desulfuricans(ATCC 29577) flavodoxinMolecular view of an electron transfer process essential for iron-sulfur protein biogenesisCrystal Structure of Cindoxin, the P450cin Redox PartnerCytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMRInvolvement of the flavin si-face tyrosine on the structure and function of ferredoxin-NADP+ reductases.Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c.NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Human cytochrome P450 oxidoreductase deficiency caused by the Y181D mutation: molecular consequences and rescue of defect.Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks.Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization.Electron supply and catalytic oxidation of nitrogen by cytochrome P450 and nitric oxide synthase.New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme.Inhibition of NADPH cytochrome P450 reductase by the model sulfur mustard vesicant 2-chloroethyl ethyl sulfide is associated with increased production of reactive oxygen species.Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.Impeded electron transfer from a pathogenic FMN domain mutant of methionine synthase reductase and its responsiveness to flavin supplementationFunctional characterization of the re-face loop spanning residues 536-541 and its interactions with the cofactor in the flavin mononucleotide-binding domain of flavocytochrome P450 from Bacillus megaterium.Flavin-containing reductase: new perspective on the detoxification of nitrobenzodiazepine.Dynamic control of electron transfers in diflavin reductases.The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases.Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme.The catalytic function of cytochrome P450 is entwined with its membrane-bound nature.Altered CYP19A1 and CYP3A4 Activities Due to Mutations A115V, T142A, Q153R and P284L in the Human P450 Oxidoreductase.Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering.Molecular dynamics simulations give insight into the conformational change, complex formation, and electron transfer pathway for cytochrome P450 reductase.Fusion of Ferredoxin and Cytochrome P450 Enables Direct Light-Driven Biosynthesis.Functional analysis of CYP2D6.31 variant: homology modeling suggests possible disruption of redox partner interaction by Arg440His substitution.Rice P450 reductases differentially affect P450-mediated metabolism in bacterial expression systems.Outer membrane cytochromes/flavin interactions in Shewanella spp.-A molecular perspective.Association of cytochrome P450 enzymes is a determining factor in their catalytic activity.High warfarin sensitivity in carriers of CYP2C9*35 is determined by the impaired interaction with P450 oxidoreductase.Solution structure of the cytochrome P450 reductase-cytochrome c complex determined by neutron scattering.Metabolons involving plant cytochrome P450sEffects of polymorphic variation on the thermostability of heterogenous populations of CYP3A4 and CYP2C9 enzymes in solution
P2860
Q24651122-DDCBDE68-5972-4B81-8AFF-81137B0C26EAQ27655590-EB41D81C-4574-480F-A98A-4DDEF4EE2581Q27677438-5921CE98-891D-4DCB-BCD9-149132320660Q27681780-12F51A91-03E8-4BBF-9484-F20BCB8EB6B5Q28271636-67594202-832B-433E-A523-1152836DF300Q30167900-A7E99F73-ED51-4B5F-95AB-6FCA800E17E4Q30369811-8DB380DA-37E1-4BDA-913F-B461A9340806Q30537968-C6C3A7F2-14AF-43C4-B74B-2C1F78B97AD4Q33613333-61C777ED-8A21-4F9D-930B-C9460861EED0Q34067351-F3480182-2901-4309-88DC-D27CB3925210Q34128999-28C9F48E-3187-473B-ABE7-D2184143BC3FQ34818959-62C1288D-276E-44DB-9414-868AE00CF422Q34994964-57F5FCDE-C28D-4EAE-95CD-6425C9FE5A67Q35967421-5A8334D8-CB20-4059-8D95-025C6DA98B28Q36744200-D295A272-43DE-4F7F-952A-3DDBCA95C3EBQ37104912-AFE4D666-2621-4B8B-AEDF-D30CF5B71125Q37424835-B4D03BE3-D5E5-42B9-9909-DB44C4CCC486Q37760940-FF8EF607-80FB-404B-86D4-63F7D5310B5DQ38064332-574BA9C9-5A51-4EA1-A324-E463E307CBCEQ38696686-DD2FD97B-A441-48E9-BB6E-207FDC833EA1Q39313060-B560AD70-96EB-411A-A60C-B411D3492F78Q39321457-5BF19E40-EACD-40DB-BAD9-97A6A624044AQ41808460-23F3BD88-5FC1-476C-8423-B5A7B35BA4D1Q41808959-3871A05D-77B8-46A2-BBD7-648194538239Q41897409-F3E50166-A3F9-4E5D-AF2A-67A865AB2644Q42072181-36E8F6CB-4471-4668-834E-AA961547CC42Q42414347-C577AD58-5C5F-4D9D-9758-043B21B3980CQ45279397-6B19CC9B-CB12-49CC-93C1-3308667DDFDBQ45881703-94D884F8-381B-4C4A-A025-32AFC9BB1B14Q46402829-EB13FECC-92D2-4EF1-BC28-69C03E75784FQ46703807-6BC3F50A-5287-4530-889A-6C650A9B1F95Q48336005-E0D4C274-21C2-49C1-BC67-FD352486BE54Q52373725-E981B014-1A76-4863-804F-F1970A6EED17Q57357493-2FEEA110-B6A9-4D96-B2EB-23EA6C9095F9Q58796074-16299D4A-D70C-4D90-B339-634823296B07
P2860
Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@ast
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en-gb
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@nl
type
label
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@ast
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en-gb
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@nl
altLabel
Crystal structure of the FMN-b ...... reductase at 1.93 Å resolution
@en
prefLabel
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@ast
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en-gb
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@nl
P2093
P2860
P921
P3181
P356
P1433
P1476
Crystal structure of the FMN-b ...... reductase at 1.93 A resolution
@en
P2093
Driessen HP
McDonagh PD
P2860
P304
P3181
P356
10.1110/PS.8.2.298
P407
P577
1999-02-01T00:00:00Z