(Q28203647)

1

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Dakun Wang

2

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Xi Na

3

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Susan R Schoen

4

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Edward M Messing

5

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Guan Wu

Biochemical and Biophysical Research Communications

6

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language of work or name

English

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publication date

14 June 2002

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published in

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volume

294

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page(s)

700-9

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issue

3

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cites work

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Ubiquitin, proteasomes, and the regulation of intracellular protein degradation

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Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome

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Deubiquitinating enzymes: a new class of biological regulators

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Deubiquitinating enzymes: their diversity and emerging roles

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von Hippel-Lindau disease

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Identification of the von Hippel-Lindau disease tumor suppressor gene

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The von Hippel-Lindau tumor suppressor gene

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Mutations of the VHL tumour suppressor gene in renal carcinoma

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Somatic mutations of the von Hippel-Lindau disease tumour suppressor gene in non-familial clear cell renal carcinoma

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

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Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1.

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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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VHL: a very hip ligase

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

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

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

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

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Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

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

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

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

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

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Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein

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Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro

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Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products

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10.1016/S0006-291X(02)00534-X

7 January 2021

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

4912600

4912600

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference