Evidence map›Paper›PMID 28456643›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2017

Matrix metalloproteinase collagenolysis in health and disease.

Sabrina Amar, Lyndsay Smith, Gregg B Fields

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed, 1 pooled it
8.1field-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

114 citing papers in PubMed, 1 synthesis or guideline pooled it, 235 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
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  5. Article
  6. Article
  7. The Impact of Ageing on Fibrillar Collagens.Sub-cellular biochemistry · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Plants (Basel, Switzerland) · 2025
    Review
  18. Review
  19. Review
  20. Review

54 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

3 authors at 2 institutions in 1 country.

Sabrina AmarDepartment of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA. Electronic address: samar@fau.edu.
Lyndsay SmithDepartment of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA. Electronic address: lyndsaysmith2015@fau.edu.
Gregg B FieldsDepartment of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA; Department of Chemistry, The Scripps Research Institute/Scripps Florida, Jupiter, FL 33458, USA. Electronic address: fieldsg@fau.edu.
Florida Atlantic University · USScripps Research Institute · US

Funding

Mechanism &Inhibition of Collagenolytic ActivityR01CA098799 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2003 to 2017
$4.5M
New probes for matrix metalloproteinase 13R01AR063795 · NIAMS · TORREY PINES INST FOR MOLECULAR STUDIES · PI FIELDS, GREGG B · 2013 to 2015
$1.5M
NCI NIH HHS R01 CA098799NIAMS NIH HHS R01 AR063795NIH HHS MH078948
6 · The paper itself

Abstract

The proteolytic processing of collagen (collagenolysis) is critical in development and homeostasis, but also contributes to numerous pathologies. Mammalian interstitial collagenolytic enzymes include members of the matrix metalloproteinase (MMP) family and cathepsin K. While MMPs have long been recognized for their ability to catalyze the hydrolysis of collagen, the roles of individual MMPs in physiological and pathological collagenolysis are less defined. The use of knockout and mutant animal models, which reflect human diseases, has revealed distinct collagenolytic roles for MT1-MMP and MMP-13. A better understanding of temporal and spatial collagen processing, along with the knowledge of the specific MMP involved, will ultimately lead to more effective treatments for cancer, arthritis, cardiovascular conditions, and infectious diseases. This article is part of a Special Issue entitled: Matrix Metalloproteinases edited by Rafael Fridman.

Indexed as

AnimalsArthritisCathepsin KHumansInfectionsMatrix Metalloproteinase 13Matrix Metalloproteinase 14Neoplasm ProteinsNeoplasmsCathepsin KCTSK protein, humanMatrix Metalloproteinase 13Matrix Metalloproteinase 14MMP13 protein, humanMMP14 protein, humanNeoplasm ProteinsArthritisCollagenMatrix metalloproteinaseMetastasisSkeletal defectsWound healing

Identifiers

PMID28456643
PMCPMC5605394
OpenAlexW2607704951

What OpenQuestion holds

Textmetadata
LicenceTDM
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.