Evidence map›Paper›PMID 20640864›Full record

ReviewAmino acids2011

Physiology and pathophysiology of matrix metalloproteases.

T Klein, R Bischoff

Registry-linked trialOpen access · hybridAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Amino acids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT06701058 (Active MMP-8 in Oral Fluid for the Detection of Oral and Oropharyngeal Cancer), which is not on this map. Cited by 401 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
401citing papers in PubMed, 4 pooled it
9.3field-weighted citation impact, top 2% 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.

NCT06701058 completednot on this mapstarted 2022, after this paper: background citation

Active MMP-8 in Oral Fluid for the Detection of Oral and Oropharyngeal Cancer

Typeobservational_patient_registrySponsorHelsinki University Central HospitalRan2022 to 2024Enrolled107ConditionsOropharyngeal Cancers, Biomarker in Early Diagnosis, Oral Cancer , Oral Squamous Cell Carcinoma, Oral Cavity Cancer, Periodontal Diseases
3 · Its place in the literature

Who cites it

401 citing papers in PubMed, 4 syntheses or guidelines pooled it, 809 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  4. Pooled it
  5. Trial
  6. Article
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  9. Can nanozymes achieve more than enzymes?Nature reviews. Materials · 2026
    Article
  10. Article
  11. Protective Effects ofInternational journal of molecular sciences · 2026
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  15. Article
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341 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

2 authors at 1 institution in 1 country.

T KleinDepartment of Pharmacy, Analytical Biochemistry, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, The Netherlands.
R Bischoff
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix metalloproteases (MMPs) comprise a family of enzymes that cleave protein substrates based on a conserved mechanism involving activation of an active site-bound water molecule by a Zn(2+) ion. Although the catalytic domain of MMPs is structurally highly similar, there are many differences with respect to substrate specificity, cellular and tissue localization, membrane binding and regulation that make this a very versatile family of enzymes with a multitude of physiological functions, many of which are still not fully understood. Essentially, all members of the MMP family have been linked to disease development, notably to cancer metastasis, chronic inflammation and the ensuing tissue damage as well as to neurological disorders. This has stimulated a flurry of studies into MMP inhibitors as therapeutic agents, as well as into measuring MMP levels as diagnostic or prognostic markers. As with most protein families, deciphering the function(s) of MMPs is difficult, as they can modify many proteins. Which of these reactions are physiologically or pathophysiologically relevant is often not clear, although studies on knockout animals, human genetic and epigenetic, as well as biochemical studies using natural or synthetic inhibitors have provided insight to a great extent. In this review, we will give an overview of 23 members of the human MMP family and describe functions, linkages to disease and structural and mechanistic features. MMPs can be grouped into soluble (including matrilysins) and membrane-anchored species. We adhere to the 'MMP nomenclature' and provide the reader with reference to the many, often diverse, names for this enzyme family in the introduction.

Indexed as

Protein Processing, Post-TranslationalAnimalsCollagenFibronectinsGelatinHumansMatrix MetalloproteinasesNeoplasm MetastasisNeoplasmsProtein Structure, TertiaryProteoglycansSubstrate SpecificityCollagenFibronectinsGelatinMatrix MetalloproteinasesProteoglycans

Identifiers

PMID20640864
PMCPMC3102199
OpenAlexW2012162957

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.