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 metalloproteinase-proteoglycans ADAMTS7 and ADAMTS12 provide an innate, tendon-specific protective mechanism against heterotopic ossification

4 Apr 2018

Abstract excerpt

Heterotopic ossification (HO) is a significant clinical problem with incompletely resolved mechanisms. Here, the secreted metalloproteinases ADAMTS7 and ADAMTS12 are shown to comprise a unique proteoglycan class that protects against a tendency toward HO in mouse hindlimb tendons, menisci, and ligaments. Adamts7 and Adamts12 mRNAs were sparsely expressed in murine forelimbs but strongly coexpressed in hindlimb...

Read the complete abstract on PubMed

Topics

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

Share to Cervical and Thoracic Myelopathy
Share to Heterotopic Ossification and Related Conditions
Share to Tendon Structure and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 29618652
DOI: 10.1172/jci.insight.92941

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The metalloproteinase-proteoglycans ADAMTS7 and ADAMTS12 provide an innate, tendon-specific protective mechanism against heterotopic ossificationPMID 29618652Read ↗

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

The role of ADAMTSs in arthritisSemantic proximity Read ↗

Insights on ADAMTS proteases and ADAMTS-like proteins from mammalian genetics.Semantic proximity Read ↗

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

Catabolism of Fibromodulin in Developmental Rudiment and Pathologic Articular Cartilage Demonstrate Novel Roles for MMP-13 and ADAMTS-4 in C-Terminal Processing of SLRPsSemantic proximity Read ↗

The ADAMTS metalloproteinasesSemantic proximity Read ↗

Combined ADAMTS10 and ADAMTS17 inactivation exacerbates bone shortening and compromises extracellular matrix formationSemantic proximity Read ↗

ADAMTS proteins in human disorders.Semantic proximity Read ↗

ADAMTS-18: a metalloproteinase with multiple functions.Semantic proximity Read ↗

Update of human and mouse matrix metalloproteinase familiesSemantic proximity Read ↗

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

Combined ADAMTS10 and ADAMTS17 inactivation exacerbates bone shortening and skin phenotypes.Semantic proximity Read ↗

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