Evidence map›Paper›PMID 34800629›Full record

ReviewCellular signalling2022

O-GlcNAcylation regulation of cellular signaling in cancer.

Lorela Ciraku, Emily M Esquea, Mauricio J Reginato

Open access · greenAbstract readReview
In one paragraph

Review in Cellular signalling, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Insights into O-GlcNAcylation and programmed cell death in cancer.Frontiers in cell and developmental biology · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Phage display uncovers a sequence motif that drives polypeptide binding to a conserved regulatory exosite of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  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

3 authors at 2 institutions in 1 country.

Lorela CirakuDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, USA.
Emily M EsqueaDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, USA.
Mauricio J ReginatoDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, USA; Sidney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA. Electronic address: mjr53@drexel.edu.
Drexel University · USThomas Jefferson University · US

Funding

Role of O-GlcNAcome on Breast Cancer Initiating CellsU01CA244303 · NCI · DREXEL UNIVERSITY · PI BALL, LAUREN ELIZABETH, REGINATO, MAURICIO J. · 2020 to 2024
$3.0M
NCI NIH HHS U01 CA244303
6 · The paper itself

Abstract

O-GlcNAcylation is a post-translational modification occurring on serine/threonine residues of nuclear and cytoplasmic proteins, mediated by the enzymes OGT and OGA which catalyze the addition or removal of the UDP-GlcNAc moieties, respectively. Structural changes brought by this modification lead to alternations of protein stability, protein-protein interactions, and phosphorylation. Importantly, O-GlcNAcylation is a nutrient sensor by coupling nutrient sensing with cellular signaling. Elevated levels of OGT and O-GlcNAc have been reported in a variety of cancers and has been linked to regulation of multiple cancer signaling pathways. In this review, we discuss the most recent findings on the role of O-GlcNAcylation as a metabolic sensor in signaling pathways and immune response in cancer.

Indexed as

AcetylglucosamineNeoplasmsHumansN-AcetylglucosaminyltransferasesPhosphorylationProtein Processing, Post-TranslationalAcetylglucosamineN-AcetylglucosaminyltransferasescancerMetabolismO-GlcNAcOGTSignalingTranscription

Identifiers

PMID34800629
PMCPMC8712408
OpenAlexW3213800887

What Socratic 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 Socratic graph.