Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Expression analysis of four endoglin missense mutations suggests that haploinsufficiency is the predominant mechanism for hereditary hemorrhagic telangiectasia type 1.
Endoglin: An accessory component of the TGF-beta-binding receptor-complex with diagnostic, prognostic, and bioimmunotherapeutic potential in human malignancies.
Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II.
Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells.
Regulated expression on human macrophages of endoglin, an Arg-Gly-Asp-containing surface antigen.
Interaction and functional interplay between endoglin and ALK-1, two components of the endothelial transforming growth factor-beta receptor complex.
Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells.
Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells.
The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells.
S-endoglin expression is induced in senescent endothelial cells and contributes to vascular pathology.
Endoglin (CD105) as a urinary and serum marker of prostate cancer.
Endoglin phosphorylation by ALK2 contributes to the regulation of prostate cancer cell migration.
Critical role of endoglin in tumor cell plasticity of Ewing sarcoma and melanoma.
Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation.
Endoglin mediates fibronectin/α5β1 integrin and TGF-β pathway crosstalk in endothelial cells.
LRG1 promotes angiogenesis by modulating endothelial TGF-β signalling.
miR-342-5p Is a Notch Downstream Molecule and Regulates Multiple Angiogenic Pathways Including Notch, Vascular Endothelial Growth Factor and Transforming Growth Factor β Signaling.
Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1.
Endoglin Protein Interactome Profiling Identifies TRIM21 and Galectin-3 as New Binding Partners.
Biochemical characterization of the 44G4 antigen from the HOON pre-B leukemic cell line.
Endoglin, a TGF-beta binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1.
Molecular characterization and in situ localization of murine endoglin reveal that it is a transforming growth factor-beta binding protein of endothelial and stromal cells.
Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta.
Identification and expression of two forms of the human transforming growth factor-beta-binding protein endoglin with distinct cytoplasmic regions.
Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily.
Defective angiogenesis in mice lacking endoglin.
A murine model of hereditary hemorrhagic telangiectasia.
Loss of distinct arterial and venous boundaries in mice lacking endoglin, a vascular-specific TGFbeta coreceptor.
Endoglin is required for myogenic differentiation potential of neural crest stem cells.
Endoglin is dispensable for angiogenesis, but required for endocardial cushion formation in the midgestation mouse embryo.
CD36 participates in a signaling pathway that regulates ROS formation in murine VSMCs.
Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10 via its orphan domain, inhibits blood vessel formation, and suppresses tumor growth.
Structural and functional insights into endoglin ligand recognition and binding.
Endoglin requirement for BMP9 signaling in endothelial cells reveals new mechanism of action for selective anti-endoglin antibodies.
ENG source and assay guide
ENG reproducible source-context analysis