Evidence map›Paper›PMID 36076910›Full record

ReviewInternational journal of molecular sciences2022

Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.

Deanna V Maybee, Nicole L Ink, Mohammad A M Ali

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.1field-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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Matrix Metalloproteinase 14 in Corneal Neovascularization.International journal of molecular sciences · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. 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.

Deanna V MaybeeDepartment of Pharmaceutical Sciences, SUNY Binghamton University School of Pharmacy and Pharmaceutical Sciences, Binghamton, NY 13902-6000, USA.
Nicole L InkDepartment of Pharmaceutical Sciences, SUNY Binghamton University School of Pharmacy and Pharmaceutical Sciences, Binghamton, NY 13902-6000, USA.
Mohammad A M AliDepartment of Pharmaceutical Sciences, SUNY Binghamton University School of Pharmacy and Pharmaceutical Sciences, Binghamton, NY 13902-6000, USA.ORCID 0000-0002-6404-4198
Binghamton University · US

Funding

State University of New York 910252-50
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are critical enzymes involved in a variety of cellular processes. MMPs are well known for their ability to degrade the extracellular matrix (ECM) and their extracellular role in cell migration. Recently, more research has been conducted on investigating novel subcellular localizations of MMPs and their intracellular roles at their respective locations. In this review article, we focus on the subcellular localization and novel intracellular roles of two closely related MMPs: membrane-type-1 matrix metalloproteinase (MT1-MMP) and matrix metalloproteinase-2 (MMP-2). Although MT1-MMP is commonly known to localize on the cell surface, the protease also localizes to the cytoplasm, caveolae, Golgi, cytoskeleton, centrosome, and nucleus. At these subcellular locations, MT1-MMP functions in cell migration, macrophage metabolism, invadopodia development, spindle formation and gene expression, respectively. Similar to MT1-MMP, MMP-2 localizes to the caveolae, mitochondria, cytoskeleton, nucleus and nucleolus and functions in calcium regulation, contractile dysfunction, gene expression and ribosomal RNA transcription. Our particular interest lies in the roles MMP-2 and MT1-MMP serve within the nucleus, as they may provide critical insights into cancer epigenetics and tumor migration and invasion. We suggest that targeting nuclear MT1-MMP or MMP-2 to reduce or halt cell proliferation and migration may lead to the development of new therapies for cancer and other diseases.

Indexed as

Extracellular MatrixMatrix Metalloproteinase 14Matrix Metalloproteinase 2NeoplasmsHumansMatrix MetalloproteinasesMetalloendopeptidasesMatrix Metalloproteinase 14Matrix Metalloproteinase 2Matrix MetalloproteinasesMetalloendopeptidasesintracellular rolesmatrix metalloproteinases (MMPs)MMP-2MT1-MMPsubcellular localization

Identifiers

PMID36076910
PMCPMC9455801
OpenAlexW4293030847

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.