Molecular basis of the VHL hereditary cancer syndrome

By W. Kaelin. Nature Reviews. Cancer, 2002

880 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6b13bcf0623256d5dceb071144a84d45b84f9a99

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Citations in the corpus

The hypoxia-inducible factor alpha pathway couples angiogenesis to osteogenesis during skeletal development. (2007, background): “The E3 ligase von Hippel–Lindau protein (pVHL) binds directly to hydroxylated HIFα subunits and regulates their polyubiquitination and destruction by the proteasome (5).”
Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2 (2004, background): “The transcriptional activity of Hif-1 is thus repressed during normoxia (11).”
Pathways of apoptotic and non-apoptotic death in tumour cells (2004, background): “The ubiquitin-ligase complex that contains the von Hippel–Lindau (VHL) protein targets and inactivates the hypoxia-inducible transcription factor HIF1&alpha”
Cancer's molecular sweet tooth and the Warburg effect. (2006, background): “In renal cell carcinoma, mutations in the VHL tumor suppressor disrupt its function, which is necessary for the oxygen-dependent prolyl hydroxylation and proteasomal degradation of HIF-1 (11).”
The genetic basis of kidney cancer: a metabolic disease (2010, background): “(21;23) (Figure 2) Similarly, when the VHL gene is mutated, mutant pVHL can no longer bind to HIF- α resulting in HIF over accumulation.”
Contrasting Properties of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-Associated Renal Cell Carcinoma (2005, background): “…have been proposed for VHL, the best understood is in the regulation of HIF, where VHL acts as the recognition component of an E3 ubiquitin ligase complex that targets HIF-(cid:2) subunits to the ubiquitin/proteasome degradation pathway following oxygen-dependent prolyl hydroxylation (16).”
Regulation of angiogenesis by hypoxia: role of the HIF system (2003, background): “Furthermore, the disease manifests a clear genotype-phenotype correlation, with functional studies of different mutations being consistent with a role of HIF upregulation in the predisposition to renal cell carcinoma (RCC) and hemangioblastoma but not pheochromocytoma (reviewed in ref”
Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. (2005, background): “Since pVHL binding to the ODD domain is dependent on PHD activity (Kaelin, 2002; Safran and Kaelin, 2003), these results indicate that inhibiting SDH activity in cells results in decreased PHD activity. puriﬁed HA-pVHL protein and GFP-ODD/HA-pVHL complexes were detected by an anti-HA antibody…”
Chemokine receptor CXCR4 downregulated by von Hippel–Lindau tumour suppressor pVHL (2003, background): “Inactivation of the VHL tumour suppressor gene is linked to the development of several different tumour types in humans, including hereditary and sporadic clear cell carcinoma of the kidne”
Oxygen, oxidative stress, hypoxia, and heart failure. (2005, background): “Molecular basis of the VHL hereditary cancer syndrome.”
Inhibition of HIF2α Is Sufficient to Suppress pVHL-Defective Tumor Growth (2003, background): “Enzymatic hydroxylation of conserved prolyl residues within these proteins by members of the egg-laying-defective nine (EGLN) family is required for their recognition by pVHL (Kaelin 2002).”
Differential Roles of Hypoxia-Inducible Factor 1α (HIF-1α) and HIF-2α in Hypoxic Gene Regulation (2003, neutral): “clear cell phenotype in VHL-defective renal carcinoma (49).”