Evidence map›Paper›PMID 30828429›Full record

ReviewF1000Research2019

Recent advances in understanding the regulation of metalloproteinases.

David A Young, Matt J Barter, David J Wilkinson

Open access · goldAbstract readReview
In one paragraph

Review in F1000Research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. RNA 5-Methylcytosine Modification in Myocardial Fibrosis.Reviews in cardiovascular medicine · 2025
    Review
  4. Article
  5. Amelogenin Null Mice Develop Osteoarthritis, While Its Application Mitigates Disease Phenotypes in a Rat Model.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Role of macrophage polarization in osteoarthritis (Review).Experimental and therapeutic medicine · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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 1 institution in 1 country.

David A YoungSkeletal Research Group, Institute of Genetic Medicine, Central Parkway, Newcastle University, Newcastle upon Tyne, NE1 3BZ, UK.ORCID 0000-0002-7078-6745
Matt J BarterSkeletal Research Group, Institute of Genetic Medicine, Central Parkway, Newcastle University, Newcastle upon Tyne, NE1 3BZ, UK.
David J WilkinsonSkeletal Research Group, Institute of Genetic Medicine, Central Parkway, Newcastle University, Newcastle upon Tyne, NE1 3BZ, UK.
Newcastle University · GB

Funding

Arthritis Research UK 20199Medical Research Council MR/P020941/1The Dunhill Medical Trust R476/0516
6 · The paper itself

Abstract

Metalloproteinases remain important players in arthritic disease, in part because members of this large enzymatic family, namely matrix metalloproteinase-1 (MMP-1) and MMP-13, are responsible for the irreversible degradation of articular cartilage collagen. Although direct inhibition of MMPs fell out of vogue with the initial clinical disappointment of the first generation of compounds, interest in other mechanisms that control these important enzymes has always been maintained. Since these enzymes are critically important for tissue homeostasis, their expression and activity are tightly regulated at many levels, not just by direct inhibition by their endogenous inhibitors the tissue inhibitors of metalloproteinases (TIMPs). Focussing on MMP-13, we discuss recent work that highlights new discoveries in the transcriptional regulation of this enzyme, from defined promoter functional analysis to how more global technologies can provide insight into the enzyme's regulation, especially by epigenetic mechanisms, including non-coding RNAs. In terms of protein regulation, we highlight recent findings into enzymatic cascades involved in MMP-13 regulation and activation. Importantly, we highlight a series of recent studies that describe how MMP-13 activity, and in fact that of other metalloproteinases, is in part controlled by receptor-mediated endocytosis. Together, these new discoveries provide a plethora of novel regulatory mechanisms, besides direct inhibition, which with renewed vigour could provide further therapeutic opportunities for regulating the activity of this class of important enzymes.

Indexed as

CollagenEndocytosisGene Expression RegulationHumansMatrix Metalloproteinase 13Tissue Inhibitor of MetalloproteinasesCollagenMatrix Metalloproteinase 13MMP13 protein, humanTissue Inhibitor of Metalloproteinasescartilagemetalloproteinaseosteoarthritisregulationtranscription

Identifiers

PMID30828429
PMCPMC6381797
OpenAlexW2911438365

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.