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

FAPalpha, a surface peptidase expressed during wound healing, is a tumor suppressor.

Oncogene - 15 Jul 2004

Ramirez-Montagut Teresa, Blachere Nathalie E, Sviderskaya Elena V, Bennett Dorothy C, Rettig Wolfgang J, Garin-Chesa Pilar, Houghton Alan N

Abstract excerpt

Fibroblast activation protein-alpha (FAP) is a cell surface serine protease expressed at sites of tissue remodeling in embryonic development. FAP is not expressed by mature somatic tissues except activated melanocytes and fibroblasts in wound healing or tumor stroma. FAP expression is specifically silenced in proliferating melanocytic cells during malignant transformation. To study the role of FAP as a tumor...

Read the complete abstract on PubMed

Topics

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

Share to Dipeptidyl Peptidase 4
Share to Endopeptidases

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

Share to Gelatinases

Share to Melanocytes

Share to Melanoma

Share to Serine

Share to Serine Endopeptidases

Share to Wound Healing

Source

Identifiers

PMID: 15133496
DOI: 10.1038/sj.onc.1207730

Genes

FAP
RAG1

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

FAPalpha, a surface peptidase expressed during wound healing, is a tumor suppressor.PMID 15133496Read ↗

Fibroblast activation protein is dispensable in the anti-influenza immune response in mice.Semantic proximity Read ↗

Targeted Disruption of Mouse Fibroblast Activation ProteinSemantic proximity Read ↗

Mouse fibroblast‐activation proteinSemantic proximity Read ↗

Mouse fibroblast activation protein: Molecular cloning, alternative splicing and expression in the reactive stroma of epithelial cancersSemantic proximity Read ↗

Understanding fibroblast activation protein (FAP): Substrates, activities, expression and targeting for cancer therapySemantic proximity Read ↗

Fibroblast activation protein-α in fibrogenic disorders and cancer: more than a prolyl-specific peptidase?Semantic proximity Read ↗

Fibroblast activation protein‐α, a stromal cell surface protease, shapes key features of cancer associated fibroblasts through proteome and degradome alterationsSemantic proximity Read ↗

Expression of the fibroblast activation protein during mouse embryo development.Semantic proximity Read ↗

Targeting Inhibition of Fibroblast Activation Protein-α and Prolyl Oligopeptidase Activities on Cells Common to Metastatic Tumor MicroenvironmentsSemantic proximity Read ↗

Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development.Semantic proximity Read ↗

Molecular cloning of seprase: a serine integral membrane protease from human melanomaSemantic proximity Read ↗

A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells.Semantic proximity Read ↗

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