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

A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10.

Journal of neurochemistry - 1 Mar 2009

Parkin Edward, Harris Benjamin

Abstract excerpt

A disintegrin and metalloproteinase (ADAM) 10 is a type I transmembrane glycoprotein responsible for the ectodomain shedding of a range of proteins including the amyloid precursor protein implicated in Alzheimer's disease. In this study we demonstrate that ADAM10 itself is subject to shedding by one or more ADAMs. Expression of epitope-tagged wild-type ADAM10 in SH-SY5Y cells enabled the detection of a soluble...

Read the complete abstract on PubMed

Topics

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

Share to ADAM Proteins
Share to Amyloid beta-Protein Precursor
Share to Amyloid Precursor Protein Secretases

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

Share to Arginine

Share to Metalloproteases

Share to Neuroblastoma

Share to Phosphoinositide Phospholipase C

Share to Tetradecanoylphorbol Acetate

Source

Identifiers

PMID: 19183255
DOI: 10.1111/j.1471-4159.2009.05907.x

Genes

ADAM10
ADAM9

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

A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10.PMID 19183255Read ↗

Part-Time &#945;-Secretases: The Functional Biology of ADAM 9, 10 and 17Semantic proximity Read ↗

Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivoSemantic proximity Read ↗

Effects of ADAM10 deletion on APP shedding, synapse and synaptic plasticity in adult miceSemantic proximity Read ↗

Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity.Semantic proximity Read ↗

Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein.Semantic proximity Read ↗

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

Active Metalloproteases of the A Disintegrin And Metalloprotease (ADAM) Family: Biological Function and StructureSemantic proximity Read ↗

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands.Semantic proximity Read ↗

Regulation of ADAM10 by miR-140-5p and potential relevance for Alzheimer's diseaseSemantic proximity Read ↗

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

The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.Semantic proximity Read ↗

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

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