Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

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New Insights into Protein Hydroxylation and Its Important Role in Human Diseases.VHL and Hypoxia Signaling: Beyond HIF in Cancer.HIF-2α-pVHL complex reveals broad genotype-phenotype correlations in HIF-2α-driven disease

P2860

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P2860

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

Item

http://www.wikidata.org/entity/Q39770199

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh

2016年學術文章

@zh-hant

name

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@en

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@nl

type

Item

label

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@en

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@nl

prefLabel

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@en

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@nl

P1476

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

@en

P2093

Betty P Poon

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

Brian Raught

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

George Bikopoulos

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

Jeffrey E Lee

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

Michael Ohh

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

Pardeep Heir

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

Severa Bunda

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

Tharan Srikumar

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

P2860

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

A conserved family of prolyl-4-hydroxylases that modify HIF

Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline

Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL

Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor.

von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2

The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor

P304

7357-7372

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P31

scholarly article

P356

10.1074/JBC.M115.694562

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P407

English

P433

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

P478

291

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P577

2016-02-04T00:00:00Z

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

P698

26846855

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

P921

Erythropoietin

P932

4817168

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

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

about

P2860

P2860

Oxygen-dependent Regulation of Erythropoietin Receptor Turnover and Signaling.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932