Zebrafish vitamin K epoxide reductases: expression in vivo, along extracellular matrix mineralization and under phylloquinone and warfarin in vitro exposure.

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VKORC1 and VKORC1L1: Why do Vertebrates Have Two Vitamin K 2,3-Epoxide Reductases?

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Zebrafish vitamin K epoxide reductases: expression in vivo, along extracellular matrix mineralization and under phylloquinone and warfarin in vitro exposure.

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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Zebrafish vitamin K epoxide re ...... nd warfarin in vitro exposure.

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Zebrafish vitamin K epoxide re ...... nd warfarin in vitro exposure.

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Zebrafish vitamin K epoxide re ...... nd warfarin in vitro exposure.

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P1476

Zebrafish vitamin K epoxide re ...... and warfarin in vitro exposure

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P2093

Carlos Marques

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Parameswaran Vijayakumar

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

P2860

Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant function

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 carboxylation

Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension

Unexpected novel relational links uncovered by extensive developmental profiling of nuclear receptor expression

VKORC1L1, an enzyme rescuing the vitamin K 2,3-epoxide reductase activity in some extrahepatic tissues during anticoagulation therapy

The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylation

Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2

Vitamin K epoxide reductase: homology, active site and catalytic mechanism

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s10695-015-0043-z

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745-759

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scholarly article

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10.1007/S10695-015-0043-Z

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1006692039

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25792234

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P921

Danio rerio

vitamin K

extracellular matrix

Zebrafish vitamin K epoxide reductases: expression in vivo, along extracellular matrix mineralization and under phylloquinone and warfarin in vitro exposure.

about

P2860

P2860

Zebrafish vitamin K epoxide reductases: expression in vivo, along extracellular matrix mineralization and under phylloquinone and warfarin in vitro exposure.

description

name

type

label

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P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P5875

P6179

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P921

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

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P5875

P6179

P698

P921