Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 12 Nov 2010

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chlorocebus aethiops
Share to Hyaluronan Receptors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Matrix Metalloproteinase 9

Share to Oligopeptides

Share to Protein Multimerization

Share to Quinazolines

Share to Tissue Inhibitor of Metalloproteinase-1

Share to Tyrphostins

Source

Open in PubMed Open full text

Identifiers

PMID: 20837483
DOI: 10.1074/jbc.M109.091769
PMCID: PMC2975217

Genes

EGFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of matrix metalloproteinase-9 dimers in cell migration: design of inhibitory peptides.PMID 20837483Read ↗

Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and inflammatory diseasesSemantic proximity Read ↗

Tetraspanin CD9 promotes the invasive phenotype of human fibrosarcoma cells via upregulation of matrix metalloproteinase-9.Semantic proximity Read ↗

Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.Semantic proximity Read ↗

Discovery of potent and specific inhibitors targeting the active site of MMP-9 from the engineered SPINK2 library.Semantic proximity Read ↗

Functional Roles of N-Linked Glycosylation of Human Matrix Metalloproteinase 9.Semantic proximity Read ↗

Emerging Features in the Regulation of MMP-9 Gene Expression for the Development of Novel Molecular Targets and Therapeutic StrategiesSemantic proximity Read ↗

Alpha4beta1 integrin and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not in normal B cells.Semantic proximity Read ↗

Secreted and membrane-bound isoforms of protease ADAM9 have opposing effects on breast cancer cell migration.Semantic proximity Read ↗

An MMP-9 mutant without gelatinolytic activity as a novel TIMP-1-antagonist.Semantic proximity Read ↗

ADAM9 silencing inhibits breast tumor cell invasion in vitroSemantic proximity Read ↗

Identification of a novel anti-angiogenic regulatory sequence within the syndecan-3 extracellular core proteinSemantic proximity Read ↗

Targeting NEDD9-SH3 with a Covalent Peptide Controls Endothelial PhenotypeSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.