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

Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta.

1 Jan 1994

Abstract excerpt

Human endoglin is a dimeric protein that binds transforming growth factor-beta (TGF-beta). A porcine cDNA clone for endoglin was obtained from a porcine uterus cDNA library. The deduced sequence of the primary translated product of endoglin consists of 643 amino acids with a high sequence identity (96%) to human endoglin in the transmembrane and intracellular domains, but with a lower sequence similarity (66%) in...

Read the complete abstract on PubMed

Topics

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

Share to Caveolin-1 and cellular processes
Share to Cell Adhesion Molecules Research
Share to TGF-β signaling in diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 8294451
DOI: 10.1016/s0021-9258(17)42126-0

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta.PMID 8294451Read ↗

Endoglin Expression Is Regulated by Transcriptional Cooperation between the Hypoxia and Transforming Growth Factor-β PathwaysSemantic proximity Read ↗

Endoglin: a critical mediator of cardiovascular healthSemantic proximity Read ↗

Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor GrowthSemantic proximity Read ↗

Novel biochemical pathways of endoglin in vascular cell physiologySemantic proximity Read ↗

Cloning and expression of a cDNA encoding mouse endoglin, an endothelial cell TGF-β ligandSemantic proximity Read ↗

Endoglin as an Adhesion Molecule in Mature and Progenitor Endothelial Cells: A Function Beyond TGF-βSemantic proximity Read ↗

Endoglin: An accessory component of the TGF‐β‐binding receptor‐complex with diagnostic, prognostic, and bioimmunotherapeutic potential in human malignanciesSemantic proximity Read ↗

Interaction and functional interplay between endoglin and ALK‐1, two components of the endothelial transforming growth factor‐β receptor complexSemantic proximity Read ↗

Endoglin Requirement for BMP9 Signaling in Endothelial Cells Reveals New Mechanism of Action for Selective Anti-Endoglin AntibodiesSemantic proximity Read ↗

Identification of Tctex2β, a Novel Dynein Light Chain Family Member That Interacts with Different Transforming Growth Factor-β ReceptorsSemantic proximity Read ↗

Cellular signaling by peptides of the endothelin gene familySemantic proximity Read ↗

Characterization of murine S-endoglin isoform and its effects on tumor development.Semantic proximity Read ↗

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