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Article

Molecular genetic analysis of the glycosyltransferase Fringe in Drosophila.

Proceedings of the National Academy of Sciences of the United States of America - 27 May 2003

Correia Trudy, Papayannopoulos Venizelos, Panin Vladislav, Woronoff Pamela, Jiang Jin, Vogt Thomas F, Irvine Kenneth D

Abstract excerpt

Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modulate signaling through Notch receptors by modifying O-linked fucose on epidermal growth factor domains. Fringe is highly conserved, and comparison among 18 different Fringe proteins from 11 different species identifies a core set of 84 amino acids that are identical among all Fringes. Fringe is only distantly related to other...

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Identifiers

PMID: 12743367
DOI: 10.1073/pnas.1131007100
PMCID: PMC164459

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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.

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Molecular genetic analysis of the glycosyltransferase Fringe in Drosophila.PMID 12743367Read ↗

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A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.Semantic proximity Read ↗

In vitro reconstitution of the modulation of Drosophila Notch-ligand binding by Fringe.Semantic proximity Read ↗

The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signaling.Semantic proximity Read ↗

Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster.Semantic proximity Read ↗

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Fringe forms a complex with Notch.Semantic proximity Read ↗

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