FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific

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Dynamic control of electron transfers in diflavin reductases.Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome P450 reductase (POR) in nanodiscs

P2860

Q38064332-115211CF-2C93-4C94-8955-1A369D84B028 Q42519476-4635B6FA-29A8-4864-BAFD-72D8C28F9FEF

P2860

FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific

Item

http://www.wikidata.org/entity/Q42261122

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2010 nî lūn-bûn

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2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

FMN binding site of yeast NADP ...... the surface is highly specific

@en

FMN binding site of yeast NADP ...... the surface is highly specific

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type

Item

label

FMN binding site of yeast NADP ...... the surface is highly specific

@en

FMN binding site of yeast NADP ...... the surface is highly specific

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prefLabel

FMN binding site of yeast NADP ...... the surface is highly specific

@en

FMN binding site of yeast NADP ...... the surface is highly specific

@nl

P1476

FMN binding site of yeast NADP ...... the surface is highly specific

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P2093

Alexander I Archakov

http://www.w3.org/2001/XMLSchema#string

Andrey A Molnar

http://www.w3.org/2001/XMLSchema#string

Larissa M Podust

http://www.w3.org/2001/XMLSchema#string

Oksana V Gnedenko

http://www.w3.org/2001/XMLSchema#string

P2860

Cloning and characterization of a novel human dual flavin reductase

Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria

Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes

NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer

Structure and Function of an NADPH-Cytochrome P450 Oxidoreductase in an Open Conformation Capable of Reducing Cytochrome P450

Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase

VMD: visual molecular dynamics

UCSF Chimera--a visualization system for exploratory research and analysis

The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity.

Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase

P304

767-776

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P31

scholarly article

P356

10.1021/CB100055V

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Alexis Ivanov

P577

2010-08-01T00:00:00Z

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P5875

44681822

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20557022

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P932

2924936

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FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific

about

P2860

P2860

FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932