Evidence map›Paper›PMID 41914222›Full record

ReviewThe FEBS journal2026

Membrane-type I metalloproteinase (MT1-MMP): A key modifier of extracellular matrix microenvironment.

Yoshifumi Itoh, Masaki Inada

Abstract readReview
In one paragraph

Review in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. In Vitro Anti-Aging Properties of aMolecules (Basel, Switzerland) · 2026
    Article
  2. Review
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.

Yoshifumi ItohKennedy Institute of Rheumatology, University of Oxford, UK.ORCID https://orcid.org/0000-0002-2128-2823
Masaki InadaInstitute of Global Innovation Research, Tokyo University of Agriculture and Technology, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular matrix (ECM) is a major component of the cellular microenvironment. It holds cells, directly sends signals to the cells, pools growth factors and cytokines, and guides cell migration and differentiation. A type I transmembrane proteinase, membrane-type I matrix metalloproteinase (MT1-MMP/MMP14), degrades ECM at the cell surface and cleaves cell surface receptors, thereby modifying cellular behavior. It is a major promoter of cell invasion and tissue destruction in diseases, such as cancer and arthritis, and is a crucial enzyme that maintains fibrillar collagen homeostasis in stromal tissue. This review discusses the current understanding of the function and regulation of this important cell surface proteinase in health and disease.

Indexed as

Cellular MicroenvironmentExtracellular MatrixMatrix Metalloproteinase 14AnimalsHumansNeoplasmsMatrix Metalloproteinase 14collagenECMmicroenvironment signalMT1‐MMP

Identifiers

PMID41914222
PMCPMC13326503

What OpenQuestion holds

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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.