Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation.
about
Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylationConserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regenerationStructural Modeling Insights into Human VKORC1 PhenotypesStructure of a bacterial homologue of vitamin K epoxide reductaseStructural and functional insights into enzymes of the vitamin K cycleThe vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylationNovel mutations in the VKORC1 gene of wild rats and mice--a response to 50 years of selection pressure by warfarin?More than 1,001 problems with protein domain databases: transmembrane regions, signal peptides and the issue of sequence homology.Disulfide bond formation in prokaryotes: history, diversity and designVitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase.A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.Quantum Chemical Study of the Mechanism of Action of Vitamin K Carboxylase in Solvent.Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells.Human herpesvirus 8 viral interleukin-6 interacts with splice variant 2 of vitamin K epoxide reductase complex subunit 1.Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanismsAltered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase.Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cells.Recent trends in the metabolism and cell biology of vitamin K with special reference to vitamin K cycling and MK-4 biosynthesis.Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1.Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer.Detecting species-site dependencies in large multiple sequence alignments.Thirteen novel VKORC1 mutations associated with oral anticoagulant resistance: insights into improved patient diagnosis and treatment.Dietary reference values for vitamin KVitamin K epoxide reductase and its paralogous enzyme have different structures and functions.Intramembrane Thiol Oxidoreductases: Evolutionary Convergence and Structural Controversy.A protein oxidase catalysing disulfide bond formation is localized to the chloroplast thylakoids.VKORC1 sequence variants associated with resistance to anticoagulant rodenticides in Irish populations of Rattus norvegicus and Mus musculus domesticus.Warfarin and vitamin K epoxide reductase: a molecular accounting for observed inhibition.
P2860
Q24304387-BE83B319-97A1-4914-9425-89DBB32FA8E4Q24337424-017165C3-E280-4B4B-95B9-A9C3EE87FC6CQ26796613-B83EC62A-5769-4B72-886A-E148CDE11AF8Q27659264-53286E7A-393A-48F9-A722-C1903B1DCF44Q28086880-522DEF6C-4634-4B74-87F4-08B71C3BC8AFQ28115117-E4BD5999-6B92-4F11-8599-7009BE0F7582Q33406630-B1DE34C1-AB2E-4284-9524-0D7734CB7559Q33649790-EC5FCD38-ACE4-4894-97CD-4AB8FFEB99D6Q33723782-C21DEA3A-6F5B-47D1-A3DB-0CBB425144ABQ34093937-4B0F42F6-F964-4643-BD44-000CCF34E47BQ34700221-94BDC9B0-CC05-4F71-AAEB-DF8F6390EFC4Q35025482-5390B2D2-01BE-4364-A6EB-176C36ADF7D1Q35189822-C66E5444-CF7C-450D-B354-F1868F1DFAE0Q35221146-96BFA042-28BC-43AB-AB61-6B3867FD62A8Q35635177-9276F81D-8E0A-447F-A78C-32BD693C382EQ35689626-8FDC8E1C-7242-4837-B099-238111D67CF1Q36298281-509493A9-1DBB-48D0-AF45-AF965B06566AQ36371403-CC732DAC-87B0-4262-9052-A96B221F0B15Q37100171-6EA69CDA-C9E3-46A3-8FFD-EAD692E149F0Q37603199-02210FF7-D2CD-48C4-92CC-280B618F651EQ38103055-92944378-A8CB-4CEB-BF2E-2DB83A3E0971Q41168727-E576FE24-3117-47C9-B101-9742BE592269Q41984591-73CC1F76-C251-4B55-A874-B9060A1F2992Q44460442-2BB4EE57-D781-4BA9-997A-17645DA3088DQ47159417-138E163B-C2F9-49A6-8410-456D31DEDB92Q47287209-CC37BCE6-C842-4952-B8BF-C66BEEF80FAEQ47610685-B33DE41A-BF60-4881-B49D-7C09BF59DE47Q50515989-BAF9FC48-7557-4BA3-A83C-496E5CB21D82Q53079086-47E3BF29-9B10-45F9-BE34-8E8FF4AE6542Q53823783-C87AF6C7-30C9-447D-B158-B368A4CADC9A
P2860
Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Membrane topology mapping of v ...... o translation/cotranslocation.
@en
Membrane topology mapping of v ...... o translation/cotranslocation.
@nl
type
label
Membrane topology mapping of v ...... o translation/cotranslocation.
@en
Membrane topology mapping of v ...... o translation/cotranslocation.
@nl
prefLabel
Membrane topology mapping of v ...... o translation/cotranslocation.
@en
Membrane topology mapping of v ...... o translation/cotranslocation.
@nl
P2093
P2860
P356
P1476
Membrane topology mapping of v ...... o translation/cotranslocation.
@en
P2093
Christopher Nicchitta
Darrel W Stafford
Jian-Ke Tie
P2860
P304
16410-16416
P356
10.1074/JBC.M500765200
P407
P577
2005-02-16T00:00:00Z