Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

18 Mar 1997

Abstract excerpt

The inactivation of the von Hippel-Lindau (VHL) gene predisposes affected individuals to VHL syndrome and is an early genetic event associated with sporadic renal cell carcinoma and CNS hemangioblastomas. The VHL protein (pVHL) has been shown to form a stable complex with elongin B and elongin C, two factors that stabilize and activate the transcription elongation factor elongin A. Here, Hs-CUL-2, a member of the...

Source

Identifiers

PMID: 9122164
DOI: 10.1073/pnas.94.6.2156

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteinsPMID 9122164Read ↗

Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function.Semantic proximity Read ↗

Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex.Semantic proximity Read ↗

Recent advances in etiology and treatment of von Hippel-Lindau Disease (VHLD).Semantic proximity Read ↗

The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity.Semantic proximity Read ↗

von Hippel-Lindau DiseaseSemantic proximity Read ↗

VHL mutations linked to type 2C von Hippel-Lindau disease cause extensive structural perturbations in pVHL.Semantic proximity Read ↗

VHL type 2B mutations retain VBC complex form and function.Semantic proximity Read ↗

Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein.Semantic proximity Read ↗

Genomic organization and chromosomal localization of the human CUL2 gene and the role of von Hippel-Lindau tumor suppressor-binding protein (CUL2 and VBP1) mutation and loss in renal-cell carcinoma development.Semantic proximity Read ↗

Insights into Cullin-RING E3 Ubiquitin Ligase Recruitment: Structure of the VHL-EloBC-Cul2 ComplexSemantic proximity Read ↗

Ubiquitin Pathway in VHL Cancer SyndromeSemantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.