Evidence map›Paper›PMID 20184396›Full record

ReviewCritical reviews in biochemistry and molecular biology2010

ADAM-17: the enzyme that does it all.

Monika Gooz

Registry-linked trialAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT06392425 (Role of Serum ADAM 17), which is not on this map. Cited by 225 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed, 1 pooled it
9.5field-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.

NCT06392425 not yet recruitingnot on this mapstarted 2024, after this paper: background citation

Role of Serum ADAM 17 (A Disintegrin And Metalloprotease 17) and Caspase 3 in Patients With Chronic Kidney Disease

TypeobservationalSponsorAssiut UniversityRan2024 to 2027Enrolled90ConditionsChronic Kidney DiseasesArmscaspase 3 and ADAM 17 biomarkers
3 · Its place in the literature

Who cites it

225 citing papers in PubMed, 1 synthesis or guideline pooled it, 407 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. A genome-scale drug discovery pipeline uncovers therapeutic targets and a unique p97 allosteric binding site inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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  14. Review
  15. A Valuable Target for Therapy: The Metalloproteinase ADAM10.Current protein & peptide science · 2025
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

165 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

1 author at 1 institution in 1 country.

Monika GoozDepartment of Medicine, Medical University of South Carolina, Charleston, SC 29425, USA. beckm@musc.edu
Medical University of South Carolina · US

Funding

Crosstalk among Growth Factors, ADAMs and IntegrinsK01DK070054 · NIDDK · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI GOOZ, MONIKA · 2005 to 2010
$587k
NIDDK NIH HHS 3K01DK070054-05S1NIDDK NIH HHS K01 DK070054
6 · The paper itself

Abstract

This review focuses on the role of ADAM-17 in disease. Since its debut as the tumor necrosis factor converting enzyme (TACE), ADAM-17 has been reported to be an indispensible regulator of almost every cellular event from proliferation to migration. The central role of ADAM-17 in cell regulation is rooted in its diverse array of substrates: cytokines, growth factors, and their receptors as well as adhesion molecules are activated or inactivated by their cleavage with ADAM-17. It is therefore not surprising that ADAM-17 is implicated in numerous human diseases including cancer, heart disease, diabetes, rheumatoid arthritis, kidney fibrosis, Alzheimer's disease, and is a promising target for future treatments. The specific role of ADAM-17 in the pathophysiology of these diseases is very complex and depends on the cellular context. To exploit the therapeutic potential of ADAM-17, it is important to understand how its activity is regulated and how specific organs and cells can be targeted to inactivate or activate the enzyme.

Indexed as

ADAM17 ProteinADAM ProteinsAnimalsDiseaseEnzyme ActivationEnzyme InhibitorsHumansInflammationSubstrate SpecificityTumor Necrosis Factor-alphaADAM17 ProteinADAM17 protein, humanADAM ProteinsEnzyme InhibitorsTumor Necrosis Factor-alpha

Identifiers

PMID20184396
PMCPMC2841225
OpenAlexW2038578669

What OpenQuestion holds

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Registered trials

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.