Evidence map›Paper›PMID 28604694›Full record

ArticleNature chemical biology2017

A mutant O-GlcNAcase enriches Drosophila developmental regulators.

Nithya Selvan, Ritchie Williamson, Daniel Mariappa, David G Campbell, Robert Gourlay, Andrew T Ferenbach, Tonia Aristotelous, Iva Hopkins-Navratilova, Matthias Trost, Daan M F van Aalten

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

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  8. Tissue-specificeLife · 2024
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  9. Molecular Mechanisms Linking Diabetes with Increased Risk of Thrombosis.International journal of molecular sciences · 2023
    Review
  10. Article
  11. The role of O-GlcNAcylation in development.Development (Cambridge, England) · 2023
    Article
  12. Review
  13. Article
  14. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022
    Article
  15. The citron homology domain as a scaffold for Rho1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  17. Review
  18. DrosophilaCells · 2021
    Article
  19. Role ofPhysiological reviews · 2021
    Review
  20. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
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

10 authors at 1 institution in 1 country.

Nithya SelvanMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Ritchie WilliamsonMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0003-4278-0909
Daniel MariappaMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
David G CampbellMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0003-2278-2149
Robert GourlayMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Andrew T FerenbachMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Tonia AristotelousDivision of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee, UK.
Iva Hopkins-NavratilovaDivision of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee, UK.
Matthias TrostMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-5732-700X
Daan M F van AaltenMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0002-1499-6908
University of Dundee · GB

Funding

Medical Research Council MC_UP_A500_1020Medical Research Council MC_UU_12016/5Wellcome Trust 110061
6 · The paper itself

Abstract

Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA). Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis. The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage. However, the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development are poorly understood. Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools. Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.

Indexed as

MutationAnimalsbeta-N-AcetylhexosaminidasesDrosophila melanogasterbeta-N-Acetylhexosaminidaseshexosaminidase C

Identifiers

PMID28604694
PMCPMC7611224
OpenAlexW2623401869

What OpenQuestion holds

Textmetadata
LicenceTDM
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.