Substrate positioning by Gln(239) stimulates turnover in factor inhibiting HIF, an αKG-dependent hydroxylase.

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Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O2 activation.

P2860

Q36691958-730A50B2-07B2-4073-B32A-4DC17C6A850D Q39213151-414852C8-9FDB-46A8-BFA4-635258772A1D

P2860

Substrate positioning by Gln(239) stimulates turnover in factor inhibiting HIF, an αKG-dependent hydroxylase.

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http://www.wikidata.org/entity/Q41903057

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2014 nî lūn-bûn

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2014年の論文

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2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

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@zh-tw

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@wuu

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@zh-cn

name

Substrate positioning by Gln(2 ...... an αKG-dependent hydroxylase.

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type

Item

label

Substrate positioning by Gln(2 ...... an αKG-dependent hydroxylase.

@en

prefLabel

Substrate positioning by Gln(2 ...... an αKG-dependent hydroxylase.

@en

P1476

Substrate positioning by Gln(2 ...... an αKG-dependent hydroxylase.

@en

P2093

Michael J Knapp

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

P2860

N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO

Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility

Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor

Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha

Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains

Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway.

P304

5750-5758

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P31

scholarly article

P356

10.1021/BI500703S

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P407

English

P433

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

P478

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

P50

Geoffrey Ivison

John A Hangasky

P577

2014-08-29T00:00:00Z

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P5875

264745106

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25119663

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P932

4165446

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Substrate positioning by Gln(239) stimulates turnover in factor inhibiting HIF, an αKG-dependent hydroxylase.

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P2860

P2860

Substrate positioning by Gln(239) stimulates turnover in factor inhibiting HIF, an αKG-dependent hydroxylase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932