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

ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan.

The Journal of biological chemistry - 30 Jul 2004

Hashimoto Gakuji, Shimoda Masayuki, Okada Yasunori

Abstract excerpt

ADAMTS4 (aggrecanase-1), a secreted enzyme belonging to the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) gene family, is considered to play a key role in the degradation of cartilage proteoglycan (aggrecan) in osteoarthritis and rheumatoid arthritis. To clone molecules that bind to ADAMTS4, we screened a human chondrocyte cDNA library by the yeast two-hybrid system using the ADAMTS4...

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 Cartilage
Share to Chondrocytes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cross-Linking Reagents

Share to Fibronectins

Share to Gene Library

Share to Inhibitory Concentration 50

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 15161923
DOI: 10.1074/jbc.M314216200

Genes

ADAMTS4

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan.PMID 15161923Read ↗

Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing.Semantic proximity Read ↗

Cloning and Characterization of ADAMTS11 , an Aggrecanase from the ADAMTS FamilySemantic proximity Read ↗

Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4.Semantic proximity Read ↗

ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan.Semantic proximity Read ↗

The role of ADAMTSs in arthritisSemantic proximity Read ↗

Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity.Semantic proximity Read ↗

Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1.Semantic proximity Read ↗

Alternative splicing of the metalloprotease ADAMTS17 spacer regulates secretion and modulates autoproteolytic activity.Semantic proximity Read ↗

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.Semantic proximity Read ↗

Characterization of the human ADAMTS-5 (aggrecanase-2) gene promoterSemantic proximity Read ↗

Evidence of a novel aggrecan‐degrading activity in cartilage: Studies of mice deficient in both ADAMTS‐4 and ADAMTS‐5Semantic proximity Read ↗

ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1.Semantic proximity Read ↗

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