(Q27860876)

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

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title

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

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main subject

HIF [nucleoplasm]

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HIF-alpha [nucleoplasm]

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1 reference

P Jaakkola

1

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Peter J. Ratcliffe

series ordinal

13

object named as

P J Ratcliffe

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author name string

D R Mole

series ordinal

2

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Y M Tian

series ordinal

3

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M I Wilson

series ordinal

4

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J Gielbert

series ordinal

5

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S J Gaskell

series ordinal

6

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A von Kriegsheim

series ordinal

7

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H F Hebestreit

series ordinal

8

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M Mukherji

series ordinal

9

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C J Schofield

series ordinal

10

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P H Maxwell

series ordinal

11

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C W Pugh

series ordinal

12

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language of work or name

English

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publication date

20 April 2001

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published in

Science

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volume

292

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issue

5516

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page(s)

468-72

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cites work

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Cobalt and desferrioxamine reveal crucial members of the oxygen sensing pathway in HepG2 cells

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Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

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Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analogue N-oxaloglycine and its derivatives

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

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1059796

Combinatorial control in ubiquitin-dependent proteolysis: don't Skp the F-box hypothesis

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Activation of Hypoxia-inducible Factor-1; Definition of Regulatory Domains within the α Subunit

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1059796

Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1059796

Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein

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Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

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

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Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1059796

Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1α

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p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1.

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Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein

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10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes

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F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

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Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein

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The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity

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Perspectives on oxygen sensing

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EPAS1 trans-activation during hypoxia requires p42/p44 MAPK

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(Q27860876)

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

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