Molecular response and association analysis of Megalobrama amblycephala fih-1 with hypoxia.

about

Sequence and functional characterization of hypoxia-inducible factors, HIF1α, HIF2αa, and HIF3α, from the estuarine fish, Fundulus heteroclitus.

P2860

Q39048994-55FED7BC-0AEA-4892-BC32-90C2B8EA7BFB

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Molecular response and association analysis of Megalobrama amblycephala fih-1 with hypoxia.

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http://www.wikidata.org/entity/Q50517911

description

2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

@wuu

2016年学术文章

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2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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name

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@en

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@nl

type

Item

label

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@en

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@nl

prefLabel

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@en

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@nl

P1476

Molecular response and associa ...... blycephala fih-1 with hypoxia.

@en

P2093

Bao Zhang

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

Boxiang Chen

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

Chunxiao Huang

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

Cuihong Huang

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

Hong Liu

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

Huanling Wang

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

Nan Chen

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

Weimin Wang

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

Yasmeen Gul

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

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FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

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

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

Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways

Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha

Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway

Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau

Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases

Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

Notch signaling: from the outside in

P2888

s00438-016-1208-x

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1615-1624

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

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scholarly article

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10.1007/S00438-016-1208-X

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

P478

291

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

P577

2016-04-25T00:00:00Z

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

P698

27112926

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

Molecular response and association analysis of Megalobrama amblycephala fih-1 with hypoxia.

about

P2860

P2860

Molecular response and association analysis of Megalobrama amblycephala fih-1 with hypoxia.

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P1476

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P698