Evidence map›Paper›PMID 25141978›Full record

ReviewCellular & molecular biology letters2014

The potential role of O-GlcNAc modification in cancer epigenetics.

Ewa Forma, Paweł Jóźwiak, Magdalena Bryś, Anna Krześlak

Open access · goldAbstract readReview
In one paragraph

Review in Cellular & molecular biology letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. ProteinMetabolites · 2022
    Review
  5. Article
  6. Article
  7. Review
  8. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Nutrient regulation of signaling and transcription.The Journal of biological chemistry · 2019
    Review
  16. Review
  17. Review
  18. Review
  19. An integrative view on sex differences in brain tumors.Cellular and molecular life sciences : CMLS · 2015
    Review
  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

4 authors at 1 institution in 1 country.

Ewa FormaDepartment of Cytobiochemistry, Faculty of Biology and Environmental Protection, University of Łódź, Pomorska 141/143, 90-237, Łódź, Poland.
Paweł Jóźwiak
Magdalena Bryś
Anna Krześlak
University of Łódź · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is no doubt that cancer is not only a genetic disease but that it can also occur due to epigenetic abnormalities. Diet and environmental factors can alter the scope of epigenetic regulation. The results of recent studies suggest that O-GlcNAcylation, which involves the addition of N-acetylglucosamine on the serine or threonine residues of proteins, may play a key role in the regulation of the epigenome in response to the metabolic status of the cell. Two enzymes are responsible for cyclic O-GlcNAcylation: O-GlcNAc transferase (OGT), which catalyzes the addition of the GlcNAc moiety to target proteins; and O-GlcNAcase (OGA), which removes the sugar moiety from proteins. Aberrant expression of O-GlcNAc cycling enzymes, especially OGT, has been found in all studied human cancers. OGT can link the cellular metabolic state and the epigenetic status of cancer cells by interacting with and modifying many epigenetic factors, such as HCF-1, TET, mSin3A, HDAC, and BAP1. A growing body of evidence from animal model systems also suggests an important role for OGT in polycomb-dependent repression of genes activity. Moreover, O-GlcNAcylation may be a part of the histone code: O-GlcNAc residues are found on all core histones.

Indexed as

Epigenesis, GeneticAcetylglucosamineAcylationAnimalsbeta-N-AcetylhexosaminidasesHistonesHumansModels, GeneticN-AcetylglucosaminyltransferasesNeoplasmsAcetylglucosaminebeta-N-Acetylhexosaminidaseshexosaminidase CHistonesN-AcetylglucosaminyltransferasesO-GlcNAc transferase

Identifiers

PMID25141978
PMCPMC6275943
OpenAlexW2053564705

What OpenQuestion holds

Textmetadata
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.