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

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

The Biochemical journal - 15 Apr 2008

Rapti Magdalini, Atkinson Susan J, Lee Meng-Huee, Trim Andrew, Moss Marcia, Murphy Gillian

Abstract excerpt

ADAM (a disintegrin and metalloproteinase) 10 is a key member of the ADAM family of disintegrin and metalloproteinases which process membrane-associated proteins to soluble forms in a process known as 'shedding'. Among the major targets of ADAM10 are Notch, EphrinA2 and CD44. In many cell-based studies of shedding, the activity of ADAM10 appears to overlap with that of ADAM17, which has a similar active-site...

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 ADAM17 Protein
Share to Amyloid Precursor Protein Secretases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hyaluronan Receptors

Share to Protease Inhibitors

Share to Solubility

Share to Tissue Inhibitor of Metalloproteinase-1

Share to Tissue Inhibitor of Metalloproteinase-3

Source

Identifiers

PMID: 18215140
DOI: 10.1042/BJ20071430

Genes

ADAM10
ADAM17

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.PMID 18215140Read ↗

Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).Semantic proximity Read ↗

Strategies to Target ADAM17 in Disease: From Its Discovery to the iRhom RevolutionSemantic proximity Read ↗

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

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

The TIMP protein family: diverse roles in pathophysiologySemantic proximity Read ↗

Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme.Semantic proximity Read ↗

Delineating the molecular basis of the inactivity of tissue inhibitor of metalloproteinase-2 against tumor necrosis factor-alpha-converting enzyme.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 the TspanC8 Family of Tetraspanins and Their Therapeutic PotentialSemantic proximity Read ↗

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

Threonine 98, the pivotal residue of tissue inhibitor of metalloproteinases (TIMP)-1 in metalloproteinase recognition.Semantic proximity Read ↗

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