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

Regulation of ADAM10 by the TspanC8 Family of Tetraspanins and Their Therapeutic Potential

23 Jun 2021

Abstract excerpt

The ubiquitously expressed transmembrane protein a disintegrin and metalloproteinase 10 (ADAM10) functions as a "molecular scissor", by cleaving the extracellular regions from its membrane protein substrates in a process termed ectodomain shedding. ADAM10 is known to have over 100 substrates including Notch, amyloid precursor protein, cadherins, and growth factors, and is important in health and implicated in...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules Research
Share to Glycosylation and Glycoproteins Research
Share to HER2/EGFR in Cancer Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34201472
DOI: 10.3390/ijms22136707

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of ADAM10 by the TspanC8 Family of Tetraspanins and Their Therapeutic PotentialPMID 34201472Read ↗

Regulation of the trafficking and the function of the metalloprotease ADAM10 by tetraspanins.Semantic proximity Read ↗

Tetraspanin Tspan15 is an essential subunit of an ADAM10 scissor complexSemantic proximity Read ↗

TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammals.Semantic proximity Read ↗

An Overview of ADAM9: Structure, Activation, and Regulation in Human DiseasesSemantic proximity Read ↗

Molecular switch in human diseases-disintegrin and metalloproteinases, ADAM17Semantic proximity Read ↗

The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) familySemantic proximity Read ↗

Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein.Semantic proximity Read ↗

The “A Disintegrin And Metalloproteases” ADAM10 and ADAM17: Novel drug targets with therapeutic potential?Semantic proximity Read ↗

ADAMTS6: Emerging roles in cardiovascular, musculoskeletal and cancer biologySemantic proximity Read ↗

Adamalysins in biology and diseaseSemantic proximity Read ↗

Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domainsSemantic proximity Read ↗

ADAM-TS5, ADAM-TS6, and ADAM-TS7, Novel Members of a New Family of Zinc MetalloproteasesSemantic proximity Read ↗

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