Evidence map›Paper›PMID 37554202›Full record

ReviewGenes & diseases2023

Functions and mechanisms of protein lysine butyrylation (Kbu): Therapeutic implications in human diseases.

Qianqian Xue, Yanyan Yang, Hong Li, Xiaoxin Li, Lu Zou, Tianxiang Li, Huibo Ma, Hongzhao Qi, Jianxun Wang, Tao Yu

Abstract readReview
In one paragraph

Review in Genes & diseases, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Review
  2. Review
  3. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  4. Incorporation of Butyryl-Lysine into Phage-Displayed Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. 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

10 authors.

Qianqian XueInstitute for Translational Medicine, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Yanyan YangDepartment of Immunology, School of Basic Medicine, Qingdao University, Qingdao, Shandong 266021, China.
Hong LiClinical Laboratory, Central Laboratory. The Affiliated Qingdao Hiser Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Xiaoxin LiInstitute for Translational Medicine, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Lu ZouInstitute for Translational Medicine, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Tianxiang LiInstitute for Translational Medicine, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Huibo MaDepartment of Vascular Surgery, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Hongzhao QiInstitute for Translational Medicine, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.
Jianxun WangDepartment of Immunology, School of Basic Medicine, Qingdao University, Qingdao, Shandong 266021, China.
Tao YuInstitute for Translational Medicine, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications (PTM) are covalent modifications of proteins or peptides caused by proteolytic cleavage or the attachment of moieties to one or more amino acids. PTMs play essential roles in biological function and regulation and have been linked with several diseases. Modifications of protein acylation (Kac), a type of PTM, are known to induce epigenetic regulatory processes that promote various diseases. Thus, an increasing number of studies focusing on acylation modifications are being undertaken. Butyrylation (Kbu) is a new acylation process found in animals and plants. Kbu has been recently linked to the onset and progression of several diseases, such as cancer, cardiovascular diseases, diabetes, and vascular dementia. Moreover, the mode of action of certain drugs used in the treatment of lymphoma and colon cancer is based on the regulation of butyrylation levels, suggesting that butyrylation may play a therapeutic role in these diseases. In addition, butyrylation is also commonly involved in rice gene expression and thus plays an important role in the growth, development, and metabolism of rice. The tools and analytical methods that could be utilized for the prediction and detection of lysine butyrylation have also been investigated. This study reviews the potential role of histone Kbu, as well as the mechanisms underlying this process. It also summarizes various enzymes and analytical methods associated with Kbu, with the goal of providing new insights into the role of Kbu in gene regulation and diseases.

Indexed as

ButyrylationGene regulationHistonePost-translational modificationTarget treatment

Identifiers

PMID37554202
PMCPMC10404885

What Socratic 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 Socratic graph.