Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein (Q29615931)

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Ratcliffe PJ

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Cockman ME

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Masson N

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Mole DR

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Jaakkola P

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Chang GW

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Clifford SC

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Maher ER

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Pugh CW

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Maxwell PH

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language of work or name

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publication date

18 August 2000

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Journal of Biological Chemistry

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published in

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volume

275

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page(s)

25733-41

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issue

33

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The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

30 April 2017

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Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: implications for degradation of oxidized proteins

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Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2

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12 October 2022

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Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C

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Activation of Sp1-mediated vascular permeability factor/vascular endothelial growth factor transcription requires specific interaction with protein kinase C zeta

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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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Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc.

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Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex

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Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein

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Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit

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12 October 2022

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A second major native von Hippel-Lindau gene product, initiated from an internal translation start site, functions as a tumor suppressor.

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12 October 2022

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Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase

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12 October 2022

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Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1alpha.

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pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation

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12 October 2022

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Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1

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The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins

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12 October 2022

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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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12 October 2022

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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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12 October 2022

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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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12 October 2022

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Post-transcriptional regulation of vascular endothelial growth factor mRNA by the product of the VHL tumor suppressor gene

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12 October 2022

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Software and database for the analysis of mutations in the VHL gene

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12 October 2022

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Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function

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12 October 2022

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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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12 October 2022

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Inhibition of transcription elongation by the VHL tumor suppressor protein

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Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein

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Hypoxia post-translationally activates iron-regulatory protein 2.

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The VHL tumour-suppressor gene paradigm

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12 October 2022

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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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12 October 2022

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The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix

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12 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1074/JBC.M002740200

Identifiers

DOI

10.1074/JBC.M002740200

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=10823831

30 April 2017

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4184925

OpenCitations bibliographic resource ID

4184925

1 reference