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Article

Human OGA binds substrates in a conserved peptide recognition groove.

The Biochemical journal - 15 Nov 2010

Schimpl Marianne, Schüttelkopf Alexander W, Borodkin Vladimir S, van Aalten Daan M F

Abstract excerpt

Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes. O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms. In the present study, we uncovered the first...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20863279
DOI: 10.1042/BJ20101338
PMCID: PMC2973230

Genes

OGA
TAB1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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