Evidence map›Paper›PMID 23680494›Full record

ReviewBiochimica et biophysica acta2013

A disintegrin and metalloproteinase-12 (ADAM12): function, roles in disease progression, and clinical implications.

Erin K Nyren-Erickson, Justin M Jones, D K Srivastava, Sanku Mallik

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  10. Review
  11. Alternatively Spliced Isoforms ofJournal of personalized medicine · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Adamalysins in COVID-19 - Potential mechanisms behind exacerbating the disease.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 1 institution in 1 country.

Erin K Nyren-EricksonDepartment of Pharmaceutical Sciences, North Dakota State University, Fargo, ND 58108-6050, USA.
Justin M Jones
D K Srivastava
Sanku Mallik
North Dakota State University · US

Funding

Lipid Nanoparticle Mediated Inhibition and Detection of Matrix MetalloproteinasesR01CA132034 · NCI · NORTH DAKOTA STATE UNIVERSITY · PI MALLIK, SANKU · 2008 to 2012
$1.4M
NCI NIH HHS 1R01 CA132034NCI NIH HHS R01 CA132034
6 · The paper itself

Abstract

backgroundA disintegrin and metalloproteinase-12 (ADAM12) is a member of the greater ADAM family of enzymes: these are multifunctional, generally membrane-bound, zinc proteases for which there are forty genes known (21 of these appearing in humans). ADAM12 has been implicated in the pathogenesis of various cancers, liver fibrogenesis, hypertension, and asthma, and its elevation or decrease in human serum has been linked to these and other physiological/pathological conditions. SCOPE: In this review, we begin with a brief overview of the ADAM family of enzymes and protein structure. We then discuss the role of ADAM12 in the progression and/or diagnosis of various disease conditions, and we will conclude with an exploration of currently known natural and synthetic inhibitors. MAJOR

conclusionADAM12 has potential to emerge as a successful drug target, although targeting the metalloproteinase domain with any specificity will be difficult to achieve due to structural similarity between the members of the ADAM and MMP family of enzymes. Overall, more research is required to establish ADAM12 being as a highly desirable biomarker and drug target of different diseases, and their selective inhibitors as potential therapeutic agents. GENERAL SIGNIFICANCE: Given the appearance of elevated levels of ADAM12 in various diseases, particularly breast cancer, our understanding of this enzyme both as a biomarker and a potential drug target could help make significant inroads into both early diagnosis and treatment of disease.

Indexed as

ADAM12 ProteinADAM ProteinsBiocatalysisDiseaseDisease ProgressionGenes, erbB-2HumansMembrane ProteinsModels, MolecularADAM12 ProteinADAM12 protein, humanADAM ProteinsMembrane ProteinsADAM12Disintegrin and metalloproteinaseFunctionInhibitorsStructure

Identifiers

PMID23680494
PMCPMC3740046
OpenAlexW2020396793

What OpenQuestion holds

Textmetadata
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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.