Evidence map›Paper›PMID 26348912›Full record

ArticleThe Biochemical journal2015

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

Daniel Mariappa, Nithya Selvan, Vladimir Borodkin, Jana Alonso, Andrew T Ferenbach, Claire Shepherd, Iva Hopkins Navratilova, Daan M F vanAalten

Abstract read
In one paragraph

Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Tissue-specificeLife · 2024
    Article
  6. Molecular Mechanisms Linking Diabetes with Increased Risk of Thrombosis.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  9. Role ofPhysiological reviews · 2021
    Review
  10. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  11. Review
  12. Review
  13. Native detection of proteinThe Analyst · 2020
    Article
  14. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  15. The Journal of biological chemistry · 2020
    Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Structural studies of a surface-entropy reduction mutant of O-GlcNAcase.Acta crystallographica. Section D, Structural biology · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Daniel Mariappa *MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Nithya Selvan *Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Vladimir BorodkinMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Jana AlonsoMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Andrew T FerenbachMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Claire ShepherdDivision of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Iva Hopkins NavratilovaDivision of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.
Daan M F vanAaltenMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom.

Funding

Wellcome Trust 087590Wellcome Trust WT087590MA
6 · The paper itself

Abstract

O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-N-acetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

Indexed as

AcylationAdaptor Proteins, Signal TransducingAnimalsBacterial Proteinsbeta-N-AcetylhexosaminidasesBlotting, Far-WesternClostridium perfringensDrosophilaEmbryonic DevelopmentEmbryo, NonmammalianHEK293 CellsHumansMutationAdaptor Proteins, Signal TransducingBacterial Proteinsbeta-N-Acetylhexosaminidaseshexosaminidase CTAB1 protein, humanDrosophilaembryonic developmentFluorescence polarizationO-GlcNAcase (OGA)O-GlcNAc probe

Identifiers

PMID26348912
PMCPMC4941924

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Registered trials

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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.