Evidence map›Paper›PMID 26025392›Full record

ReviewGenome biology2015

The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family.

Richard Kelwick, Ines Desanlis, Grant N Wheeler, Dylan R Edwards

Open access · hybridAbstract readReview
In one paragraph

Review in Genome biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 351 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
351citing papers in PubMed, 3 pooled it
16.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

351 citing papers in PubMed, 3 syntheses or guidelines pooled it, 633 citations in OpenAlex.

  1. Pooled it
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  4. Physiology (Bethesda, Md.) · 2026
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291 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Richard KelwickSchool of Biological Sciences, Biomedical Research Centre, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK. r.kelwick@imperial.ac.uk.
Ines DesanlisSchool of Biological Sciences, Biomedical Research Centre, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK. i.desanlis@uea.ac.uk.
Grant N WheelerSchool of Biological Sciences, Biomedical Research Centre, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK. grant.wheeler@uea.ac.uk.
Dylan R EdwardsSchool of Biological Sciences, Biomedical Research Centre, University of East Anglia, Norwich Research Park, Norwich, NR4 7TJ, UK. dylan.edwards@uea.ac.uk.
University of East Anglia · GBNorwich Research Park · GB

Funding

Cancer Research UK
6 · The paper itself

Abstract

The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) enzymes are secreted, multi-domain matrix-associated zinc metalloendopeptidases that have diverse roles in tissue morphogenesis and patho-physiological remodeling, in inflammation and in vascular biology. The human family includes 19 members that can be sub-grouped on the basis of their known substrates, namely the aggrecanases or proteoglycanases (ADAMTS1, 4, 5, 8, 9, 15 and 20), the procollagen N-propeptidases (ADAMTS2, 3 and 14), the cartilage oligomeric matrix protein-cleaving enzymes (ADAMTS7 and 12), the von-Willebrand Factor proteinase (ADAMTS13) and a group of orphan enzymes (ADAMTS6, 10, 16, 17, 18 and 19). Control of the structure and function of the extracellular matrix (ECM) is a central theme of the biology of the ADAMTS, as exemplified by the actions of the procollagen-N-propeptidases in collagen fibril assembly and of the aggrecanases in the cleavage or modification of ECM proteoglycans. Defects in certain family members give rise to inherited genetic disorders, while the aberrant expression or function of others is associated with arthritis, cancer and cardiovascular disease. In particular, ADAMTS4 and 5 have emerged as therapeutic targets in arthritis. Multiple ADAMTSs from different sub-groupings exert either positive or negative effects on tumorigenesis and metastasis, with both metalloproteinase-dependent and -independent actions known to occur. The basic ADAMTS structure comprises a metalloproteinase catalytic domain and a carboxy-terminal ancillary domain, the latter determining substrate specificity and the localization of the protease and its interaction partners; ancillary domains probably also have independent biological functions. Focusing primarily on the aggrecanases and proteoglycanases, this review provides a perspective on the evolution of the ADAMTS family, their links with developmental and disease mechanisms, and key questions for the future.

Indexed as

Multigene FamilyADAM ProteinsAnimalsArthritisCardiovascular DiseasesCatalytic DomainDisease Models, AnimalDisintegrinsEndopeptidasesEvolution, MolecularExtracellular MatrixGene Expression RegulationHumansNeoplasmsSubstrate SpecificityThrombospondinsADAM ProteinsaggrecanaseDisintegrinsEndopeptidasesThrombospondins

Identifiers

PMID26025392
PMCPMC4448532
OpenAlexW2162977739

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.