Evidence map›Paper›PMID 31695185›Full record

ArticleNature structural & molecular biology2019

Genetic recoding to dissect the roles of site-specific protein O-GlcNAcylation.

Andrii Gorelik, Sergio Galan Bartual, Vladimir S Borodkin, Joby Varghese, Andrew T Ferenbach, Daan M F van Aalten

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules.Journal of the American Chemical Society · 2024
    Article
  11. Article
  12. Article
  13. HumanACS catalysis · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Cancers · 2022
    Review
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Andrii GorelikCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK.ORCID http://orcid.org/0000-0001-5354-4042
Sergio Galan BartualCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK.
Vladimir S BorodkinCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK.
Joby VargheseMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Andrew T FerenbachCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK.
Daan M F van AaltenCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, UK. dmfvanaalten@dundee.ac.uk.ORCID http://orcid.org/0000-0002-1499-6908
University of Dundee · GB

Funding

Wellcome Trust 105310Wellcome Trust 110061Wellcome Trust 200208Wellcome Trust 200208/Z/15/Z
6 · The paper itself

Abstract

Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an abundant posttranslational event essential for proper animal development and is dysregulated in various diseases. Due to the rapid concurrent removal by the single O-GlcNAcase (OGA), precise functional dissection of site-specific O-GlcNAc modification in vivo is currently not possible without affecting the entire O-GlcNAc proteome. Exploiting the fortuitous promiscuity of OGT, we show that S-GlcNAc is a hydrolytically stable and accurate structural mimic of O-GlcNAc that can be encoded in mammalian systems with CRISPR-Cas9 in an otherwise unperturbed O-GlcNAcome. Using this approach, we target an elusive Ser 405 O-GlcNAc site on OGA, showing that this site-specific modification affects OGA stability.

Indexed as

AcetylglucosamineAnimalsbeta-N-AcetylhexosaminidasesCRISPR-Cas SystemsGlycosylationHEK293 CellsHumansMiceModels, MolecularN-AcetylglucosaminyltransferasesProtein Processing, Post-TranslationalSubstrate SpecificityAcetylglucosaminebeta-N-Acetylhexosaminidaseshexosaminidase CN-AcetylglucosaminyltransferasesO-GlcNAc transferase

Identifiers

PMID31695185
PMCPMC6858883
OpenAlexW2989464372

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.