Evidence map›Paper›PMID 28346405›Full record

ArticleNature chemical biology2017

Structural and functional insight into human O-GlcNAcase.

Christian Roth, Sherry Chan, Wendy A Offen, Glyn R Hemsworth, Lianne I Willems, Dustin T King, Vimal Varghese, Robert Britton, David J Vocadlo, Gideon J Davies

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 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. A Scalable Design for Proximity-Inducing Molecules.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. HumanResearch square · 2025
    Article
  8. Insights into O-GlcNAcylation and programmed cell death in cancer.Frontiers in cell and developmental biology · 2025
    Review
  9. Review
  10. Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. HumanACS catalysis · 2023
    Article
  20. spJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
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 2 institutions in 2 countries.

Christian RothYork Structural Biology Laboratory, Department of Chemistry University of York, York, UK.ORCID 0000-0001-5806-0987
Sherry ChanYork Structural Biology Laboratory, Department of Chemistry University of York, York, UK.
Wendy A OffenYork Structural Biology Laboratory, Department of Chemistry University of York, York, UK.
Glyn R HemsworthYork Structural Biology Laboratory, Department of Chemistry University of York, York, UK.ORCID 0000-0002-8226-1380
Lianne I WillemsDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Dustin T KingDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Vimal VargheseDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Robert BrittonDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
David J VocadloDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.ORCID 0000-0001-6897-5558
Gideon J DaviesYork Structural Biology Laboratory, Department of Chemistry University of York, York, UK.ORCID 0000-0002-7343-776X
Simon Fraser University · CAUniversity of York · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K003836/1CIHR MOP-123341
6 · The paper itself

Abstract

O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value.

Indexed as

Models, MolecularAcetylglucosaminebeta-N-AcetylhexosaminidasesBinding SitesEnzyme ActivationEnzyme InhibitorsHEK293 CellsHumansLigandsProtein BindingProtein IsoformsProtein Structure, TertiaryAcetylglucosaminebeta-N-AcetylhexosaminidasesEnzyme Inhibitorshexosaminidase CLigandsProtein Isoforms

Identifiers

PMID28346405
PMCPMC5438047
OpenAlexW2603194836

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.