Evidence map›Paper›PMID 20837483›Full record

ArticleThe Journal of biological chemistry2010

Role of matrix metalloproteinase-9 dimers in cell migration: design of inhibitory peptides.

Antoine Dufour, Stanley Zucker, Nicole S Sampson, Cem Kuscu, Jian Cao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

83 citing papers in PubMed, 138 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Integrating Single-Cell Profiling with Generative AI forMolecules (Basel, Switzerland) · 2026
    Article
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Metal Complexes as Promising Matrix Metalloproteinases Regulators.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Review

23 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 2 institutions in 1 country.

Antoine DufourDepartment of Chemistry, Stony Brook University, Stony Brook, New York 11794, USA.
Stanley Zucker
Nicole S Sampson
Cem Kuscu
Jian Cao
Stony Brook University · USNorthport VA Medical Center · US

Funding

Targeting the PEX Domain of MT1-MMP: Novel Cancer TherapyR01CA113553 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI CAO, JIAN · 2006 to 2010
$1.7M
NCI NIH HHS 5R01CA11355301A1NCI NIH HHS R01 CA113553
6 · The paper itself

Abstract

Non-proteolytic activities of matrix metalloproteinases (MMPs) have recently been shown to impact cell migration, but the precise mechanism remains to be understood. We previously demonstrated that the hemopexin (PEX) domain of MMP-9 is a prerequisite for enhanced cell migration. Using a biochemical approach, we now report that dimerization of MMP-9 through the PEX domain appears necessary for MMP-9-enhanced cell migration. Following a series of substitution mutations within the MMP-9 PEX domain, blade IV was shown to be critical for homodimerization, whereas blade I was required for heterodimerization with CD44. Blade I and IV mutants showed diminished enhancement of cell migration compared with wild type MMP-9-transfected cells. Peptides mimicking motifs in the outermost strands of the first and fourth blades of the MMP-9 PEX domain were designed. These peptides efficiently blocked MMP-9 dimer formation and inhibited motility of COS-1 cells overexpressing MMP-9, HT-1080, and MDA-MB-435 cells. Using a shRNA approach, CD44 was found to be a critical molecule in MMP-9-mediated cell migration. Furthermore, an axis involving a MMP-9-CD44-EGFR signaling pathway in cell migration was identified using antibody array and specific receptor tyrosine kinase inhibitors. In conclusion, we dissected the mechanism of pro-MMP-9-enhanced cell migration and developed structure-based inhibitory peptides targeting MMP-9-mediated cell migration.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCell Line, TumorCell MovementChlorocebus aethiopsCOS CellsEnzyme InhibitorsErbB ReceptorsHumansHyaluronan ReceptorsMatrix Metalloproteinase 9Models, MolecularMutationOligopeptidesProtein BindingEnzyme InhibitorsErbB ReceptorsHyaluronan ReceptorsMatrix Metalloproteinase 9OligopeptidesQuinazolinesRTKI cpdTissue Inhibitor of Metalloproteinase-1Tyrphostins

Identifiers

PMID20837483
PMCPMC2975217
OpenAlexW2054506084

What OpenQuestion holds

Textmetadata
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.