Evidence map›Paper›PMID 29079818›Full record

ArticleScientific reports2017

MMP proteolytic activity regulates cancer invasiveness by modulating integrins.

Alakesh Das, Melissa Monteiro, Amlan Barai, Sandeep Kumar, Shamik Sen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 4% 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

71 citing papers in PubMed, 1 synthesis or guideline pooled it, 157 citations in OpenAlex.

  1. Pooled it
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  12. FAPNature communications · 2025
    Article
  13. Article
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  15. Article
  16. Matrix degradation enhances stress relaxation, regulating cell adhesion and spreading.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Review
  19. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  20. Review

11 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

5 authors at 1 institution in 1 country.

Alakesh DasDepartment of Biosciences & Bioengineering, IIT Bombay, Mumbai, 400 076, India.
Melissa MonteiroDepartment of Biosciences & Bioengineering, IIT Bombay, Mumbai, 400 076, India.
Amlan BaraiDepartment of Biosciences & Bioengineering, IIT Bombay, Mumbai, 400 076, India.
Sandeep KumarDepartment of Biosciences & Bioengineering, IIT Bombay, Mumbai, 400 076, India.ORCID 0000-0001-9525-4836
Shamik SenDepartment of Biosciences & Bioengineering, IIT Bombay, Mumbai, 400 076, India. shamiks@iitb.ac.in.
Indian Institute of Technology Bombay · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cancer invasion through dense extracellular matrices (ECMs) is mediated by matrix metalloproteinases (MMPs) which degrade the ECM thereby creating paths for migration. However, how this degradation influences the phenotype of cancer cells is not fully clear. Here we address this question by probing the function of MMPs in regulating biophysical properties of cancer cells relevant to invasion. We show that MMP catalytic activity regulates cell spreading, motility, contractility and cortical stiffness by stabilizing integrins at the membrane and activating focal adhesion kinase. Interestingly, cell rounding and cell softening on stiff gels induced by MMP inhibition is attenuated on MMP pre-conditioned surfaces. Together, our results suggest that MMP catalytic activity regulates invasiveness of cancer cells by modulating integrins.

Indexed as

ProteolysisBiomechanical PhenomenaCell AdhesionCell Line, TumorCell MembraneCell MovementExtracellular MatrixHumansIntegrin beta1IntegrinsMatrix MetalloproteinasesNeoplasm InvasivenessProtein TransportIntegrin beta1IntegrinsMatrix Metalloproteinases

Identifiers

PMID29079818
PMCPMC5660204
OpenAlexW2766048879

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.