Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 34, 2010, Pages 15027-15032

  Schulman, Sol ^a   Wang, Belinda ^a   Li, Weikai ^a   Rapoport, Tom A ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

Blood coagulation; Disulfide bond formation; Electron transfer; Quinone; Warfarin

Indexed keywords

MENADIONE EPOXIDE; THIOREDOXIN; UNCLASSIFIED DRUG; VITAMIN K EPOXIDE REDUCTASE; BACTERIAL PROTEIN; MENADIONE EPOXIDASE; MIXED FUNCTION OXIDASE; RECOMBINANT PROTEIN;

ARTICLE; DISULFIDE BOND; ELECTRON TRANSPORT; ENDOPLASMIC RETICULUM; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IMMUNOBLOTTING; MEMBRANE STRUCTURE; MOLECULAR CLONING; MOLECULAR WEIGHT; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; SYNECHOCOCCUS; ANIMAL; CELL STRAIN COS1; CERCOPITHECUS; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; IN VITRO STUDY; METABOLISM; SITE DIRECTED MUTAGENESIS; SPECIES DIFFERENCE; STRUCTURAL HOMOLOGY; SYNECHOCYSTIS;

BACTERIA (MICROORGANISMS); MAMMALIA; SYNECHOCOCCUS SP.;

ANIMALS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CERCOPITHECUS AETHIOPS; COS CELLS; ELECTRON TRANSPORT; ENDOPLASMIC RETICULUM; HUMANS; MIXED FUNCTION OXYGENASES; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; RECOMBINANT PROTEINS; SPECIES SPECIFICITY; STRUCTURAL HOMOLOGY, PROTEIN; SYNECHOCYSTIS; THIOREDOXINS;

EID: 77957007036     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1009972107     Document Type: Article

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