Evidence map›Paper›PMID 23430258›Full record

ReviewThe Journal of biological chemistry2013

Interstitial collagen catabolism.

Gregg B Fields

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed, 1 pooled it
9.4field-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

102 citing papers in PubMed, 1 synthesis or guideline pooled it, 203 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Amoeboid-mesenchymal transition and the proteolytic control of cancer invasion plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Application of collagen in bone regeneration.Journal of orthopaedic translation · 2025
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. A conserved strategy to attack collagen: The activator domain in bacterial collagenases unwinds triple-helical collagen.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. Inhibitory effects of bioactive compounds on UVB-induced photodamage in human keratinocytes: modulation of MMP1 and Wnt signaling pathways.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024
    Article

42 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.

Gregg B FieldsTorrey Pines Institute for Molecular Studies, Port St. Lucie, FL 34987, USA. gfields@tpims.org
Torrey Pines Institute For Molecular Studies · US

Funding

Mechanism &Inhibition of Collagenolytic ActivityR01CA098799 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2003 to 2017
$4.5M
NCI NIH HHS CA98799NCI NIH HHS R01 CA098799NIMH NIH HHS MH78948PHS HHS 268201000036C
6 · The paper itself

Abstract

Interstitial collagen mechanical and biological properties are altered by proteases that catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in development and homeostasis but also contributes to numerous pathologies. Mammalian collagenolytic enzymes include matrix metalloproteinases, cathepsin K, and neutrophil elastase, and a variety of invertebrates and pathogens possess collagenolytic enzymes. Components of the mechanism of action for the collagenolytic enzyme MMP-1 have been defined experimentally, and insights into other collagenolytic mechanisms have been provided. Ancillary biomolecules may modulate the action of collagenolytic enzymes.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsArthritisBinding SitesCatalysisCathepsin KCollagenHumansLeukocyte ElastaseMatrix Metalloproteinase 1Matrix MetalloproteinasesMetabolismMolecular ConformationNeoplasmsProtein BindingProtein Structure, TertiaryCathepsin KCollagenLeukocyte ElastaseMatrix Metalloproteinase 1Matrix MetalloproteinasesSerine

Identifiers

PMID23430258
PMCPMC3610953
OpenAlexW2037060384

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.