Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1alpha interactions. (Q53352910)

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8 January 2020

title

Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1alpha interactions (English)

1 reference

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von Hippel-Lindau disease

8 January 2020

main subject

1 reference

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4

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8 January 2020

author name string

K Knauth

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16261165%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

C Bex

series ordinal

2

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8 January 2020

P Jemth

series ordinal

3

1 reference

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8 January 2020

language of work or name

English

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publication date

1 January 2006

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8 January 2020

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8 January 2020

volume

25

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8 January 2020

issue

3

1 reference

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8 January 2020

page(s)

370-377

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Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth

8 January 2020

cites work

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Two distinct phenotypes caused by two different missense mutations in the same codon of the VHL gene

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Von Hippel-Lindau (VHL) disease with pheochromocytoma in the Black Forest region of Germany: evidence for a founder effect

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

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Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.

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Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: correlations with phenotype

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Genotype-phenotype correlation in von Hippel-Lindau disease: identification of a mutation associated with VHL type 2A

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Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation

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Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease.

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

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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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Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding

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Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.

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Mutations of the VHL tumour suppressor gene in renal carcinoma

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Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity

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Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL.

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von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF.

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7 January 2021

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

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

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

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VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases

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Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase

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Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein

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7 January 2021

The VHL protein recruits a novel KRAB-A domain protein to repress HIF-1alpha transcriptional activity

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7 January 2021

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

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von Hippel-Lindau disease

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von Hippel-Lindau disease

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The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma

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7 January 2021

Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation

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

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7 January 2021

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

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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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7 January 2021

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

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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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Gene array of VHL mutation and hypoxia shows novel hypoxia-induced genes and that cyclin D1 is a VHL target gene

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