Evidence map›Paper›PMID 33240407›Full record

ReviewOncology letters2021

Roles of ten-eleven translocation family proteins and their O-linked β-N-acetylglucosaminylated forms in cancer development.

Hong-Jiao Li, Yi Wang, Bing-Xin Li, Yang Yang, Feng Guan, Xing-Chen Pang, Xiang Li

Open access · diamondAbstract readReview
In one paragraph

Review in Oncology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Mesenchymal Stem Cells in Cancer Therapy.Advances in experimental medicine and biology · 2025
    Review
  9. Review
  10. Exploring the Therapeutic Potential ofCurrent pharmaceutical design · 2025
    Article
  11. Review
  12. Review
  13. Review
  14. Mechanisms that regulate the activities of TET proteins.Cellular and molecular life sciences : CMLS · 2022
    Review
  15. New Insights into TETs in Psychiatric Disorders.International journal of molecular sciences · 2022
    Review
  16. Article
  17. Structure and Function of TET Enzymes.Advances in experimental medicine and biology · 2022
    Article
  18. Review
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Hong-Jiao LiKey Laboratory of Resource Biology and Biotechnology Western China, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Yi WangDepartment of Hematology, Provincial People's Hospital, Xi'an, Shaanxi 710069, P.R. China.
Bing-Xin LiKey Laboratory of Resource Biology and Biotechnology Western China, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Yang YangKey Laboratory of Resource Biology and Biotechnology Western China, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Feng GuanKey Laboratory of Resource Biology and Biotechnology Western China, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Xing-Chen PangKey Laboratory of Resource Biology and Biotechnology Western China, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Xiang LiKey Laboratory of Resource Biology and Biotechnology Western China, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, P.R. China.
Northwest University · CNShaanxi Provincial People's Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the ten-eleven translocation (TET) protein family of which three mammalian TET proteins have been discovered so far, catalyze the sequential oxidation of 5-methylcytosine to 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine which serve an important role in embryonic development and tumor progression. O-GlcNAcylation (O-linked β-N-acetylglucosaminylation) is a reversible post-translational modification known to serve important roles in tumorigenesis and metastasis especially in hematopoietic malignancies such as myelodysplastic syndromes, chronic myelomonocytic leukemia and acute myeloid leukemia. O-GlcNAcylation activity requires only two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). OGT catalyzes attachment of GlcNAc sugar to serine, threonine and cytosine residues in proteins, while OGA hydrolyzes O-GlcNAc attached to proteins. Numerous recent studies have demonstrated that TETs can be O-GlcNAcylated by OGT, with consequent alteration of TET activity and stability. The present review focuses on the cellular, biological and biochemical functions of TET and its O-GlcNAcylated form and proposes a model of the role of TET/OGT complex in regulation of target proteins during cancer development. In addition, the present review provides directions for future research in this area.

Indexed as

O-GlcNAcylationTET

Identifiers

PMID33240407
PMCPMC7681232
OpenAlexW3095515966

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.