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

Functional analysis of Drosophila beta1,4-N-acetlygalactosaminyltransferases.

Glycobiology - 1 Apr 2005

Haines Nicola, Irvine Kenneth D

Abstract excerpt

Members of the mammalian beta1,4-galactosyltransferase family are among the best studied glycosyltransferases, but the requirements for all members of this family within an animal have not previously been determined. Here, we describe analysis of two Drosophila genes, beta4GalNAcTA (CG8536) and beta4GalNAcTB (CG14517), that are homologous to mammalian beta1,4-galactosyltransferases. Like their mammalian homologs,...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Animals, Genetically Modified
Share to Drosophila melanogaster

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

Share to Drosophila Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to N-Acetylgalactosaminyltransferases

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 15563714
DOI: 10.1093/glycob/cwi017

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of Drosophila beta1,4-N-acetlygalactosaminyltransferases.PMID 15563714Read ↗

Null mutations in Drosophila N-acetylglucosaminyltransferase I produce defects in locomotion and a reduced life span.Semantic proximity Read ↗

Requirement for a core 1 galactosyltransferase in the Drosophila nervous system.Semantic proximity Read ↗

Functional analysis of glycosylation using Drosophila melanogaster.Semantic proximity Read ↗

Multiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila.Semantic proximity Read ↗

Functional roles for beta1,4-N-acetlygalactosaminyltransferase-A in Drosophila larval neurons and muscles.Semantic proximity Read ↗

Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila.Semantic proximity Read ↗

Sialyltransferase regulates nervous system function in Drosophila.Semantic proximity Read ↗

Distinct contributions of beta 4GalNAcTA and beta 4GalNAcTB to Drosophila glycosphingolipid biosynthesis.Semantic proximity Read ↗

Functional analysis of proteoglycan galactosyltransferase II RNA interference mutant flies.Semantic proximity Read ↗

Glucuronylated core 1 glycans are required for precise localization of neuromuscular junctions and normal formation of basement membranes on Drosophila muscles.Semantic proximity Read ↗

A sweet spot in the FGFR signal transduction pathway.Semantic proximity Read ↗

Intellectual disability-associated disruption of O-GlcNAcylation impairs neuronal development and cognitive function in <i>Drosophila</i>Semantic proximity Read ↗

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