Evidence map›Paper›PMID 19666537›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

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

Donald A R Sinclair, Monika Syrzycka, Matthew S Macauley, Tara Rastgardani, Ivana Komljenovic, David J Vocadlo, Hugh W Brock, Barry M Honda

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed, 1 pooled it
7.4field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

157 citing papers in PubMed, 1 synthesis or guideline pooled it, 228 citations in OpenAlex.

  1. Pooled it
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  3. Article
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  8. HumanResearch square · 2025
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  16. The role of O-GlcNAcylation in development.Development (Cambridge, England) · 2023
    Article
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  18. Review
  19. Review
  20. Review

97 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Donald A R SinclairDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, Canada V5A 1S6. dsinclai@sfu.ca or honda@sfu.ca
Monika Syrzycka
Matthew S Macauley
Tara Rastgardani
Ivana Komljenovic
David J Vocadlo
Hugh W Brock
Barry M Honda
Simon Fraser University · CAUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-linked N-acetylglucosamine transferase (OGT) reversibly modifies serine and threonine residues of many intracellular proteins with a single beta-O-linked N-acetylglucosamine residue (O-GlcNAc), and has been implicated in insulin signaling, neurodegenerative disease, cellular stress response, and other important processes in mammals. OGT also glycosylates RNA polymerase II and various transcription factors, which suggests that it might be directly involved in transcriptional regulation. We report here that the Drosophila OGT is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). Furthermore, major sites of O-GlcNAc modification on polytene chromosomes correspond to PcG protein binding sites. Our results thus suggest a direct role for O-linked glycosylation by OGT in PcG-mediated epigenetic gene silencing, which is important in developmental regulation, stem cell maintenance, genomic imprinting, and cancer. In addition, we observe rescue of sxc lethality by a human Ogt cDNA transgene; thus Drosophila may provide an ideal model to study important functional roles of OGT in mammals.

Indexed as

Genes, InsectAnimalsBinding SitesChromatin ImmunoprecipitationChromosome MappingChromosomesDrosophila melanogasterDrosophila ProteinsHumansMutationN-AcetylglucosaminyltransferasesPolycomb-Group ProteinsProtein BindingProtein Processing, Post-TranslationalProtein TransportRepressor ProteinsDrosophila ProteinsN-AcetylglucosaminyltransferasesO-GlcNAc transferasePolycomb-Group ProteinsRepressor ProteinsUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase

Identifiers

PMID19666537
PMCPMC2726349
OpenAlexW2099766227

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.