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

EphrinA1 is released in three forms from cancer cells by matrix metalloproteases.

Molecular and cellular biology - 1 Aug 2012

Beauchamp Amanda, Lively Mark O, Mintz Akiva, Gibo Denise, Wykosky Jill, Debinski Waldemar

Abstract excerpt

EphrinA1 is a glycosylphosphatidylinositol (GPI)-linked ligand for the EphA2 receptor, which is overexpressed in glioblastoma (GBM), among other cancers. Activation of the receptor by ephrinA1 leads to a suppression of oncogenic properties of GBM cells. We documented that a monomeric functional form of ephrinA1 is released from cancer cells and thus explored the mechanism of ephrinA1 release and the primary...

Read the complete abstract on PubMed

Topics

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

Share to Culture Media, Conditioned
Share to Gene Expression Regulation, Enzymologic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Mass Spectrometry

Share to Matrix Metalloproteinases

Share to Peptides

Share to Phosphoinositide Phospholipase C

Share to Proteolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 22688511
DOI: 10.1128/MCB.06791-11
PMCID: PMC3434542

Genes

GPI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

EphrinA1 is released in three forms from cancer cells by matrix metalloproteases.PMID 22688511Read ↗

Proteolysis of EphA2 Converts It from a Tumor Suppressor to an Oncoprotein.Semantic proximity Read ↗

Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.Semantic proximity Read ↗

Signal Peptide Peptidase, Encoded by HM13, Contributes to Tumor Progression by Affecting EGFRvIII Secretion Profiles in Glioblastoma.Semantic proximity Read ↗

Dissociation of the intramolecularly cleaved N- and C-terminal fragments of the adhesion G protein-coupled receptor GPR133 (ADGRD1) increases canonical signalingSemantic proximity Read ↗

Proteolytic Shedding of Human Colony-Stimulating Factor 1 Receptor and its implication.Semantic proximity Read ↗

EphrinA/EphA-induced ectodomain shedding of neural cell adhesion molecule regulates growth cone repulsion through ADAM10 metalloprotease.Semantic proximity Read ↗

Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor.Semantic proximity Read ↗

The N-terminus of GPR37L1 is proteolytically processed by matrix metalloproteasesSemantic proximity Read ↗

Missense mutations of the ephrin receptor EPHA1 associated with Alzheimer’s disease disrupt receptor signaling functionsSemantic proximity Read ↗

Regulated cleavage of a contact-mediated axon repellent.Semantic proximity Read ↗

Eph Receptors and Ephrins: Therapeutic OpportunitiesSemantic proximity Read ↗

Ephrin-B1 transduces signals to activate integrin-mediated migration, attachment and angiogenesis.Semantic proximity Read ↗

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