Evidence map›Paper›PMID 25595836›Full record

ReviewMatrix biology : journal of the International Society for Matrix Biology

New strategies for targeting matrix metalloproteinases.

Gregg B Fields

Open access · hybridAbstract readReview
In one paragraph

Review in Matrix biology : journal of the International Society for Matrix Biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 106 citations in OpenAlex.

  1. High-Resolution Relaxometry for Fragment Screening.Journal of medicinal chemistry · 2026
    Article
  2. Matrix Metalloproteinases in Inflammatory Dermatoses.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. TheFoods (Basel, Switzerland) · 2023
    Article
  7. Review
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  20. Venlafaxine Stimulates an MMP-9-Dependent Increase in Excitatory/Inhibitory Balance in a Stress Model of Depression.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    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

1 author at 1 institution in 1 country.

Gregg B FieldsFlorida Atlantic University, Department of Chemistry & Biochemistry, 5353 Parkside Drive, Building MC17, Jupiter, FL 33458, United States; The Scripps Research Institute/Scripps Florida, Department of Chemistry, 130 Scripps Way, Jupiter, FL 33458, United States; Torrey Pines Institute for Molecular Studies, Department of Chemistry, 11350 SW Village Parkway, Port St. Lucie, FL 34987, United States; Torrey Pines Institute for Molecular Studies, Department of Biology, 11350 SW Village Parkway, Port St. Lucie, FL 34987, United States. Electronic address: fieldsg@fau.edu.
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
New probes for matrix metalloproteinase 13R01AR063795 · NIAMS · TORREY PINES INST FOR MOLECULAR STUDIES · PI FIELDS, GREGG B · 2013 to 2015
$1.5M
ADSC Isolation by MMPsR43GM106469 · NIGMS · AKRON BIOTECHNOLOGY, LLC · PI ZYLBERBERG, CLAUDIA · 2014 to 2014
$154k
NCI NIH HHS CA98799NCI NIH HHS R01 CA098799NIAMS NIH HHS AR063795NIAMS NIH HHS R01 AR063795NIGMS NIH HHS GM106469NIGMS NIH HHS R43 GM106469
6 · The paper itself

Abstract

The development of matrix metalloproteinase (MMP) inhibitors has often been frustrated by a lack of specificity and subsequent off-target effects. More recently, inhibitor design has considered secondary binding sites (exosites) to improve specificity. Small molecules and peptides have been developed that bind exosites in the catalytic (CAT) domain of MMP-13, the CAT or hemopexin-like (HPX) domain of MT1-MMP, and the collagen binding domain (CBD) of MMP-2 and MMP-9. Antibody-based approaches have resulted in selective inhibitors for MMP-9 and MT1-MMP that target CAT domain exosites. Triple-helical "mini-proteins" have taken advantage of collagen binding exosites, producing a family of novel probes. A variety of non-traditional approaches that incorporate exosite binding into the design process has yielded inhibitors with desirable selectivities within the MMP family.

Indexed as

Binding SitesEnzyme InhibitorsHumansMaleMatrix MetalloproteinasesPeptidesSmall Molecule LibrariesSubstrate SpecificityEnzyme InhibitorsMatrix MetalloproteinasesPeptidesSmall Molecule LibrariesCollagenExositeInhibitorMatrix metalloproteinase (MMP)Triple-helical peptide

Identifiers

PMID25595836
PMCPMC4466128
OpenAlexW2084323667

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.