Evidence map›Paper›PMID 32207184›Full record

ReviewChemistry (Weinheim an der Bergstrasse, Germany)2020

Molecular Interrogation to Crack the Case of O-GlcNAc.

Arielis Estevez, Dongsheng Zhu, Connor Blankenship, Jiaoyang Jiang

Abstract readReview
In one paragraph

Review in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Glycosylation in aging and neurodegenerative diseases.Acta biochimica et biophysica Sinica · 2024
    Review
  6. Identification of RESP18 Gene Mutations Linked to Hereditary Non-Syndromic Cleft Lip and Palate in a Southern Chinese Family.Medical science monitor : international medical journal of experimental and clinical research · 2024
    Article
  7. Tissue-specificeLife · 2024
    Article
  8. Article
  9. Article
  10. O-GlcNAcylation regulates epidermal growth factor receptor intracellular trafficking and signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  13. Article
  14. Article
  15. The Metabolic Chemical Reporter AcFrontiers in chemistry · 2021
    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

4 authors.

Arielis EstevezPharmaceutical Sciences Division, University of Wisconsin-Madison, Madison, WI, 53705, USA.
Dongsheng ZhuPharmaceutical Sciences Division, University of Wisconsin-Madison, Madison, WI, 53705, USA.
Connor BlankenshipPharmaceutical Sciences Division, University of Wisconsin-Madison, Madison, WI, 53705, USA.
Jiaoyang JiangPharmaceutical Sciences Division, University of Wisconsin-Madison, Madison, WI, 53705, USA.ORCID http://orcid.org/0000-0001-8445-9924

Funding

Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Chemical Probes to Characterize the Functional States of O-GlcNAc TransferaseR01GM121718 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Jiaoyang Jiang · 2017 to 2026
$3.3M
Structure, Function and Regulation of Human O-GlcNAcaseR01GM126300 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI JIANG, JIAOYANG · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM121718NIGMS NIH HHS R01 GM126300NIGMS NIH HHS T32 GM008505
6 · The paper itself

Abstract

The O-linked β-N-acetylglucosamine (O-GlcNAc) modification, termed O-GlcNAcylation, is an essential and dynamic post-translational modification in cells. O-GlcNAc transferase (OGT) installs this modification on serine and threonine residues, whereas O-GlcNAcase (OGA) hydrolyzes it. O-GlcNAc modifications are found on thousands of intracellular proteins involved in diverse biological processes. Dysregulation of O-GlcNAcylation and O-GlcNAc cycling enzymes has been detected in many diseases, including cancer, diabetes, cardiovascular and neurodegenerative diseases. Here, recent advances in the development of molecular tools to investigate OGT and OGA functions and substrate recognition are discussed. New chemical approaches to study O-GlcNAc dynamics and its potential roles in the immune system are also highlighted. It is hoped that this minireview will encourage more research in these areas to advance the understanding of O-GlcNAc in biology and diseases.

Indexed as

beta-N-AcetylhexosaminidasesN-AcetylglucosaminyltransferasesAcetylglucosamineProtein Processing, Post-TranslationalSerineThreonineAcetylglucosaminebeta-N-AcetylhexosaminidasesN-AcetylglucosaminyltransferasesSerineThreoninechemical toolsglycosylationinhibitorsO-GlcNAcsubstrate recognition

Identifiers

PMID32207184
PMCPMC7724648

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.