Evidence map›Paper›PMID 41920022›Full record

ReviewOpen biology2026

The biology and pathophysiology of the proatherogenic metalloprotease ADAMTS7.

Shiwali Goyal, James Muniu, Mohd Akbar Bhat, Eli Oldham, Derrick W Pruitt, Luis Frias Perez, Frida Z Miranda, Joshua Muia

Abstract readReview
PubMed Publisher
In one paragraph

Review in Open biology, 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

8 authors.

Shiwali GoyalNational Institute of Health, National Eye Institute , Bethesda, MD,USA.
James MuniuOklahoma State University College of Osteopathic Medicine , Tulsa, OK, USA.
Mohd Akbar BhatDepartment of Ophthalmology, Georgetown University Medical Center, Washington, DC, USA.
Eli OldhamOklahoma State University College of Osteopathic Medicine , Tulsa, OK, USA.
Derrick W PruittOklahoma State University College of Osteopathic Medicine , Tulsa, OK, USA.ORCID 0009-0003-3053-7183
Luis Frias PerezOklahoma State University College of Osteopathic Medicine , Tulsa, OK, USA.
Frida Z MirandaOklahoma State University College of Osteopathic Medicine , Tulsa, OK, USA.
Joshua MuiaDepartment of Biochemistry and Microbiology, Oklahoma State University Center for Health Sciences, Tulsa, OK, USA.ORCID 0000-0001-5011-2420

Funding

Investigating the regulation and substrate processing of ADAMTS13 and ADAMTS7 metalloproteases.R35GM142926 · NIGMS · VERSITI WISCONSIN, INC. · PI MUIA, JOSHUA MUTAMBUKI · 2021 to 2025
$2.0M
NIGMS NIH HHS R35 GM142926The National Institutes of Health
6 · The paper itself

Abstract

The ADAMTS (a disintegrin and metalloproteinase with thrombospondin type-1 motifs) metalloprotease family comprises 19 members, and they play critical roles in development, angiogenesis and coagulation. These enzymes are also pivotal in the turnover of extracellular matrix proteins in various tissues, and their dysregulation has been linked to diseases such as arthritis, atherosclerosis, cancer and inflammation. These secreted zinc metalloproteases are composed of multiple domains and are localized to the extracellular matrix and present in circulation. The metalloprotease member 7 of this family or ADAMTS7 was cloned in 2004. However, in 2011, it gained significant attention when its gene locus was associated with an increased risk of atherosclerosis and coronary artery disease. Despite its strong association with human diseases, the biological functions, substrate targets and processing of ADAMTS7 remain poorly understood, limiting our comprehension of its roles in both health and disease. This review highlights the structural organization of ADAMTS7, its expression and regulation, known substrates, and its involvement in various pathophysiological processes. Additionally, perspectives on future research directions and priorities are presented. ADAMTS7 remains a compelling target for drug and biomarker discovery, though much about this metalloprotease remains to be uncovered.

Indexed as

ADAMTS7 ProteinAtherosclerosisAnimalsHumansADAMTS7 ProteinADAMTS7 protein, humanADAMTS7ADAMTS metalloproteasesatherosclerosiscoronary artery diseaseGWAS

Identifiers

PMID41920022

What OpenQuestion holds

Textmetadata
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.