Evidence map›Paper›PMID 32855658›Full record

ReviewExperimental and therapeutic medicine2020

Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review).

Can Xia, Yu Tao, Mingshan Li, Tuanjie Che, Jing Qu

Open access · diamondAbstract readReview
In one paragraph

Review in Experimental and therapeutic medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

93 citing papers in PubMed, 131 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Adaptation of White Adipocytes to Cooler Temperatures: Impacts on Energy Metabolism and Protein Acetylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

33 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

5 authors at 2 institutions in 1 country.

Can XiaDepartment of Cell Biology, Medical College of Soochow University, Suzhou, Jiangsu 215123, P.R. China.
Yu TaoDepartment of Cell Biology, Medical College of Soochow University, Suzhou, Jiangsu 215123, P.R. China.
Mingshan LiDepartment of Cell Biology, Medical College of Soochow University, Suzhou, Jiangsu 215123, P.R. China.
Tuanjie CheLaboratory of Precision Medicine and Translational Medicine, Suzhou Hospital Affiliated to Nanjing Medical University, Suzhou Science and Technology Town Hospital, Suzhou, Jiangsu 215153, P.R. China.
Jing QuDepartment of Cell Biology, Medical College of Soochow University, Suzhou, Jiangsu 215123, P.R. China.
Soochow University · CNNanjing Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells primarily rely on proteins to perform the majority of their physiological functions, and the function of proteins is regulated by post-translational modifications (PTMs). The acetylation of proteins is a dynamic and highly specific PTM, which has an important influence on the functions of proteins, such as gene transcription and signal transduction. The acetylation of proteins is primarily dependent on lysine acetyltransferases and lysine deacetylases. In recent years, due to the widespread use of mass spectrometry and the emergence of new technologies, such as protein chips, studies on protein acetylation have been further developed. Compared with histone acetylation, acetylation of non-histone proteins has gradually become the focus of research due to its important regulatory mechanisms and wide range of applications. The discovery of specific protein acetylation sites using bioinformatic tools can greatly aid the understanding of the underlying mechanisms of protein acetylation involved in related physiological and pathological processes.

Indexed as

acetylationdeacetylationlysine acetyltransferaselysine deacetylasesnon-histone protein acetylation

Identifiers

PMID32855658
PMCPMC7444376
OpenAlexW3045982661

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.