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

Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes.

Cells - 27 Apr 2021

Akan Ilhan, Halim Adnan, Vakhrushev Sergey Y, Clausen Henrik, Hanover John A

Abstract excerpt

The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes, with O-GlcNAc transferase (OGT) adding O-GlcNAc and with O-GlcNAcase (OGA) removing it in a manner that's protein-...

Read the complete abstract on PubMed

Topics

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

Share to beta-N-Acetylhexosaminidases
Share to Body Size
Share to Gene Ontology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycoproteins

Share to Histone-Lysine N-Methyltransferase

Share to Longevity

Share to Proteome

Share to Wings, Animal

Source

Open in PubMed Open full text

Identifiers

PMID: 33925313
DOI: 10.3390/cells10051026
PMCID: PMC8145559

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes.PMID 33925313Read ↗

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

A mutant O-GlcNAcase enriches Drosophila developmental regulators.Semantic proximity Read ↗

Protein O-GlcNAcylation is required for fibroblast growth factor signaling in Drosophila.Semantic proximity Read ↗

Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.Semantic proximity Read ↗

The hexosamine signaling pathway: deciphering the "O-GlcNAc code".Semantic proximity Read ↗

Rescuable sleep and synaptogenesis phenotypes in a <i>Drosophila</i> model of O-GlcNAc transferase intellectual disabilitySemantic proximity Read ↗

Effects of hypo-O-GlcNAcylation on Drosophila development.Semantic proximity Read ↗

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

Rescuable sleep and synaptogenesis phenotypes in a Drosophila model of O-GlcNAc transferase intellectual disability.Semantic proximity Read ↗

O-GlcNAcylation modulates expression and abundance of N-glycosylation machinery in an inherited glycosylation disorder.Semantic proximity Read ↗

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

Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc).Semantic proximity Read ↗

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