Evidence map›Paper›PMID 31626249›Full record

ArticleChemical communications (Cambridge, England)2019

Targeted covalent inhibition of O-GlcNAc transferase in cells.

Matthew Worth, Chia-Wei Hu, Hao Li, Dacheng Fan, Arielis Estevez, Dongsheng Zhu, Ao Wang, Jiaoyang Jiang

Open access · greenAbstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  9. Article
  10. Functional Analysis ofFrontiers in oncology · 2020
    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

8 authors at 1 institution in 1 country.

Matthew WorthDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA.
Chia-Wei HuPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.
Hao LiPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.
Dacheng FanPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.
Arielis EstevezPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.ORCID http://orcid.org/0000-0001-7588-2691
Dongsheng ZhuPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.
Ao WangPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.
Jiaoyang JiangPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA. jiaoyang.jiang@wisc.edu.ORCID http://orcid.org/0000-0001-8445-9924
University of Wisconsin–Madison · US

Funding

Chemical Probes to Characterize the Functional States of O-GlcNAc TransferaseR01GM121718 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Jiaoyang Jiang · 2017 to 2026
$3.3M
NIGMS NIH HHS R01 GM121718
6 · The paper itself

Abstract

O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases. To date, most OGT inhibitors lack either sufficient potency or characterized specificity in cells. We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes. This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.

Indexed as

Enzyme InhibitorsHEK293 CellsHumansMCF-7 CellsModels, MolecularN-AcetylglucosaminyltransferasesEnzyme InhibitorsN-AcetylglucosaminyltransferasesO-GlcNAc transferase

Identifiers

PMID31626249
PMCPMC6823131
OpenAlexW2979778107

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.