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Article

The Notch1 receptor is cleaved constitutively by a furin-like convertase.

Proceedings of the National Academy of Sciences of the United States of America - 7 Jul 1998

Logeat F, Bessia C, Brou C, LeBail O, Jarriault S, Seidah N G, Israël A

Abstract excerpt

The Notch receptor, which is involved in numerous cell fate decisions in invertebrates and vertebrates, is synthesized as a 300-kDa precursor molecule (p300). We show here that proteolytic processing of p300 is an essential step in the formation of the biologically active receptor because only the cleaved fragments are present at the cell surface. Our results confirm and extend recent reports indicating that the...

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Identifiers

PMID: 9653148
DOI: 10.1073/pnas.95.14.8108
PMCID: PMC20937

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

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The Notch1 receptor is cleaved constitutively by a furin-like convertase.PMID 9653148Read ↗

Proteolytic cleavage of Notch: "HIT and RUN".Semantic proximity Read ↗

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Human NOTCH2 Is Resistant to Ligand-independent Activation by Metalloprotease Adam17.Semantic proximity Read ↗

Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2.Semantic proximity Read ↗

Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme.Semantic proximity Read ↗

Notch receptor cleavage depends on but is not directly executed by presenilins.Semantic proximity Read ↗

The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site.Semantic proximity Read ↗

Nuclear access and action of notch in vivo.Semantic proximity Read ↗

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