Evidence map›Paper›PMID 33916244›Full record

ReviewCancers2021

O-GlcNAcylation and O-GlcNAc Cycling Regulate Gene Transcription: Emerging Roles in Cancer.

Matthew P Parker, Kenneth R Peterson, Chad Slawson

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

64 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. NSUN7-mediated mJournal of translational medicine · 2025
    Article
  8. Article
  9. Review
  10. Glycosylation in kidney diseases.Precision clinical medicine · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Application and mechanisms of targeting BRD4 in osteosarcoma.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2025
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

4 more citing papers are in PubMed but not listed here.

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.

Matthew P ParkerDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA.
Kenneth R PetersonDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA.ORCID 0000-0002-8598-9334
Chad SlawsonDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA.ORCID 0000-0002-6886-4847
The University of Kansas Cancer Center · USUniversity of Kansas Medical Center · US

Funding

Regulation of Globin Gene Switching by O-GlcNAc Post-Translational ModificationR01DK100595 · NIDDK · UNIVERSITY OF KANSAS MEDICAL CENTER · PI PETERSON, KENNETH R, SLAWSON, CHAD ERIC · 2014 to 2016
$788k
NIH HHS R01DK100595
6 · The paper itself

Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc) is a single sugar post-translational modification (PTM) of intracellular proteins linking nutrient flux through the Hexosamine Biosynthetic Pathway (HBP) to the control of cis-regulatory elements in the genome. Aberrant O-GlcNAcylation is associated with the development, progression, and alterations in gene expression in cancer. O-GlcNAc cycling is defined as the addition and subsequent removal of the modification by O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) provides a novel method for cells to regulate various aspects of gene expression, including RNA polymerase function, epigenetic dynamics, and transcription factor activity. We will focus on the complex relationship between phosphorylation and O-GlcNAcylation in the regulation of the RNA Polymerase II (RNAP II) pre-initiation complex and the regulation of the carboxyl-terminal domain of RNAP II via the synchronous actions of OGT, OGA, and kinases. Additionally, we discuss how O-GlcNAcylation of TATA-box binding protein (TBP) alters cellular metabolism. Next, in a non-exhaustive manner, we will discuss the current literature on how O-GlcNAcylation drives gene transcription in cancer through changes in transcription factor or chromatin remodeling complex functions. We conclude with a discussion of the challenges associated with studying O-GlcNAcylation and present several new approaches for studying O-GlcNAc regulated transcription that will advance our understanding of the role of O-GlcNAc in cancer.

Indexed as

O-GlcNAcO-GlcNAcaseO-GlcNAc transferasetranscription

Identifiers

PMID33916244
PMCPMC8037238
OpenAlexW3142553327

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.