Evidence map›Paper›PMID 36388951›Full record

ArticleiScience2022

HBO1 catalyzes lysine benzoylation in mammalian cells.

Doudou Tan, Wei Wei, Zhen Han, Xuelian Ren, Cong Yan, Shankang Qi, Xiaohan Song, Y George Zheng, Jiemin Wong, He Huang

Open access · goldAbstract read
In one paragraph

Article in iScience, 2022. 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
2.5field-weighted citation impact, top 8% 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, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. HBO1, a MYSTerious KAT and its links to cancer.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  13. Proteomics of the heart.Physiological reviews · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  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

10 authors at 3 institutions in 2 countries.

Doudou TanShanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Wei WeiShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China.
Zhen HanDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, USA.
Xuelian RenShanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Cong YanShanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Shankang QiShanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Xiaohan SongShanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Y George ZhengDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, USA.
Jiemin WongShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China.
He HuangShanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Chinese Academy of Sciences · CNEast China Normal University · CNUniversity of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine benzoylation (Kbz) is a newly discovered protein post-translational modification (PTM). This PTM can be stimulated by benzoate and contributes to gene expression. However, its regulatory enzymes and substrate proteins remain largely unknown, hindering further functional studies. Here we identified and validated the lysine acetyltransferase (KAT) HBO1 as a "writer" of Kbz in mammalian cells. In addition, we report the benzoylome in mammalian cells, identifying 1747 Kbz sites; among them at least 77 are the HBO1-targeted Kbz substrates. Bioinformatics analysis showed that HBO1-targeted Kbz sites were involved in multiple processes, including chromatin remodeling, transcription regulation, immune regulation, and tumor growth. Our results thus identify the regulatory elements of the Kbz pathway and reveal the non-canonical enzymatic activity and functions of HBO1 in cellular physiology.

Indexed as

Biological sciencesCell biologyMolecular biology

Identifiers

PMID36388951
PMCPMC9647509
OpenAlexW4308150964

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.