Evidence map›Paper›PMID 24256146›Full record

ArticleThe Biochemical journal2014

Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.

Vladimir S Borodkin, Marianne Schimpl, Mehmet Gundogdu, Karim Rafie, Helge C Dorfmueller, David A Robinson, Daan M F van Aalten

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

34 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  12. Review
  13. Overview of the Assays to ProbeMolecules (Basel, Switzerland) · 2021
    Review
  14. Article
  15. Article
  16. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  17. Intracellular Hydrolysis of Small-MoleculeMolecules (Basel, Switzerland) · 2020
    Article
  18. Review
  19. Targeted covalent inhibition of O-GlcNAc transferase in cells.Chemical communications (Cambridge, England) · 2019
    Article
  20. O-GlcNAcylation in immunity and inflammation: An intricate system (Review).International journal of molecular medicine · 2019
    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

7 authors at 2 institutions in 1 country.

Vladimir S Borodkin*MRC Protein Phosphorylation und Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Marianne Schimpl*MRC Protein Phosphorylation und Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Mehmet Gundogdu*MRC Protein Phosphorylation und Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Karim Rafie*MRC Protein Phosphorylation und Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Helge C Dorfmueller
David A Robinson‡Drug Discovery Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Daan M F van Aalten
MRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Medical Research Council G0900138Wellcome Trust 087590Wellcome Trust WT087590MA
6 · The paper itself

Abstract

Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation. We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring. Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.

Indexed as

Drug DesignModels, MolecularAdaptor Proteins, Signal TransducingBinding SitesCrystallography, X-RayEnzyme InhibitorsGlycosylationHumansInterferometryKineticsN-AcetylglucosaminyltransferasesOligopeptidesPeptide FragmentsProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsAdaptor Proteins, Signal TransducingEnzyme InhibitorsN-AcetylglucosaminyltransferasesOligopeptidesPeptide FragmentsRecombinant ProteinsSerineTAB1 protein, humanUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferaseUridine Diphosphate

Identifiers

PMID24256146
PMCPMC3927924
OpenAlexW2144619812

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.