Discover Community Create You

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

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

The Journal of clinical investigation - 1 Dec 1999

Ohh M, Takagi Y, Aso T, Stebbins C E, Pavletich N P, Zbar B, Conaway R C, Conaway J W, Kaelin W G

Abstract excerpt

The von Hippel-Lindau tumor suppressor protein (pVHL) negatively regulates hypoxia-inducible mRNAs such as the mRNA encoding vascular endothelial growth factor (VEGF). This activity has been linked to its ability to form multimeric complexes that contain elongin C, elongin B, and Cul2. To understand this process in greater detail, we performed a series of in vitro binding assays using pVHL, elongin B, and elongin...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Hypoxia
Share to Ligases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Peptide Fragments

Share to Proteins

Share to Tumor Suppressor Proteins

Share to Ubiquitin-Protein Ligases

Share to von Hippel-Lindau Disease

Share to Von Hippel-Lindau Tumor Suppressor Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 10587522
DOI: 10.1172/JCI8161
PMCID: PMC481054

Genes

VHL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein.PMID 10587522Read ↗

Binding of the von Hippel-Lindau Tumor Suppressor Protein to Elongin B and CSemantic proximity Read ↗

Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.Semantic proximity Read ↗

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling.Semantic proximity Read ↗

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

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

Inhibition of transcription elongation by the VHL tumor suppressor protein.Semantic proximity Read ↗

The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families.Semantic proximity Read ↗

pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation.Semantic proximity Read ↗

Post-transcriptional regulation of vascular endothelial growth factor mRNA by the product of the VHL tumor suppressor gene.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila.Semantic proximity Read ↗

Identification of Elongin C and Skp1 sequences that determine Cullin selection.Semantic proximity Read ↗

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