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

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

Cancer research - 15 Oct 2010

Fry Jessica L, Toker Alex

Abstract excerpt

Tumor cell migration is mediated by cell-autonomous signaling mechanisms as well as paracrine and autocrine factors secreted by activated stromal cells in the tumor microenvironment. Like other members of the ADAM (a disintegrin and metalloproteinase) family, the integrin-binding metalloproteinase ADAM9 modulates cell-cell and cell-matrix interactions as well as ectodomain shedding of cell surface receptors and...

Read the complete abstract on PubMed

Topics

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

Share to ADAM Proteins
Share to Cell Membrane
Share to Cell Movement

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cross Reactions

Share to Gene Expression Regulation, Enzymologic

Share to Immunoblotting

Share to Isoenzymes

Share to RNA, Small Interfering

Source

Open in PubMed Open full text

Identifiers

PMID: 20736367
DOI: 10.1158/0008-5472.CAN-09-4231
PMCID: PMC2955804

Genes

ADAM9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Secreted and membrane-bound isoforms of protease ADAM9 have opposing effects on breast cancer cell migration.PMID 20736367Read ↗

ADAM8 in invasive cancers: links to tumor progression, metastasis, and chemoresistanceSemantic proximity Read ↗

ADAM8 expression in invasive breast cancer promotes tumor dissemination and metastasis.Semantic proximity Read ↗

ADAM9 as a Potential Target Molecule in CancerSemantic proximity Read ↗

An Overview of ADAM9: Structure, Activation, and Regulation in Human DiseasesSemantic proximity Read ↗

The ADAMs family of proteases: new biomarkers and therapeutic targets for cancer?Semantic proximity Read ↗

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

ADAMs and ADAMTSs in cancerSemantic proximity Read ↗

Emerging roles of ADAM and ADAMTS metalloproteinases in cancerSemantic proximity Read ↗

The roles of ADAMTS metalloproteinases in tumorigenesis and metastasisSemantic proximity Read ↗

Expression of ADAM‐9 mRNA and protein in human breast cancerSemantic proximity Read ↗

Breast cancer-associated mutations in metalloprotease disintegrin ADAM12 interfere with the intracellular trafficking and processing of the protein.Semantic proximity Read ↗

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands.Semantic proximity Read ↗

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