Evidence map›Paper›PMID 41917349›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2026

An Overview of ADAMTS Proteases.

Suneel S Apte

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Suneel S ApteDepartment of Biomedical Engineering, Cleveland Clinic Research, Cleveland Clinic, Cleveland, OH, USA. aptes@ccf.org.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ADAMTS superfamily comprises 19 secreted metalloproteases (ADAMTS proteases) and seven structurally related secreted proteins without catalytic activity (ADAMTS-like proteins). Members of both families participate in diverse and numerous processes in a variety of tissues and organs during embryo development and in connective tissue maintenance and hemostasis in the adult. The functional relationships between the two families are unclear, although most ADAMTS roles can be attributed to proteolytic actions and most ADAMTS-like roles to their functions as matricellular proteins. ADAMTS proteases are implicated in human and animal Mendelian disorders and are key participants in acquired disease pathways, including inflammatory and degenerative conditions. Several spontaneous mutations and genetically engineered invertebrate and mammalian (mostly mouse) models have been used to uncover ADAMTS biological roles in organogenesis and to define their cellular impact and underlying mechanisms. Despite their profound biological and medical importance, detailed knowledge about ADAMTS molecular structures, substrates, or binding partners and biochemical mechanisms is still limited. ADAMTS2, ADAMTS5, and ADAMTS13 have previously been extensively investigated because of their obvious clinical relevance, but much less is known about other ADAMTS proteases and most ADAMTS-like proteins. Here, the essential background and concepts relevant to this superfamily of proteins are discussed.

Indexed as

ADAMTS ProteinsAnimalsHumansProteolysisSubstrate SpecificityADAMTS ProteinsDegradomeExtracellular matrixMetalloproteaseMetalloproteinaseProteaseProteolysis

Identifiers

What OpenQuestion holds

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Registered trials

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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.