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

Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand.

Archives of biochemistry and biophysics - 15 Dec 2002

Vargo-Gogola Tracy, Crawford Howard C, Fingleton Barbara, Matrisian Lynn M

Abstract excerpt

Soluble Fas ligand (sFasL) is released from the cell surface by matrix metalloproteinases (MMPs), one of which is MMP-7. We have reported that MMP-7-generated sFasL is pro-apoptotic in both in vitro and in vivo systems. However, there are contradictory reports that the soluble form of FasL is ina...

Read the complete abstract on PubMed

Topics

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

Share to Fas Ligand Protein
Share to Leucine
Share to Matrix Metalloproteinase 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Matrix Metalloproteinase 3

Share to Matrix Metalloproteinase 7

Share to Peptide Fragments

Share to Solubility

Share to Substrate Specificity

Source

Identifiers

PMID: 12464266
DOI: 10.1016/s0003-9861(02)00525-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-12464266-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand.PMID 12464266Read ↗

Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.Semantic proximity Read ↗

Differential expression of human Fas mRNA species upon peripheral blood mononuclear cell activation.Semantic proximity Read ↗

A new alternative splice variant of the mouse Fas antigen with a deletion in the N-terminal portion of the extracellular domain.Semantic proximity Read ↗

Signal transduction. FasL binds preassembled Fas.Semantic proximity Read ↗

Human caspase-7 activity and regulation by its N-terminal peptide.Semantic proximity Read ↗

N-terminal cleavage and release of the ectodomain of Flt1 is mediated via ADAM10 and ADAM 17 and regulated by VEGFR2 and the Flt1 intracellular domain.Semantic proximity Read ↗

A non-cleavable mutant of Fas ligand does not prevent neutrophilic destruction of islet transplants.Semantic proximity Read ↗

Expression of the functional soluble form of human fas ligand in activated lymphocytes.Semantic proximity Read ↗

The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability.Semantic proximity Read ↗

The activity of a type II transmembrane serine protease, matriptase, is dependent solely on the catalytic domain.Semantic proximity Read ↗

Engineered hybrid dimers: tracking the activation pathway of caspase-7.Semantic proximity Read ↗

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