Evidence map›Paper›PMID 37720100›Full record

ArticleiScience2023

Identification of SIRT3 as an eraser of H4K16la.

Zhuming Fan, Zhiyang Liu, Nan Zhang, Wenyu Wei, Ke Cheng, Hongyan Sun, Quan Hao

Abstract read
In one paragraph

Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing 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

90 citing papers in PubMed.

  1. Review
  2. Lactate Signal: Modulator of Cellular Energy Production and Anabolism.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Review
  4. Lactate-Mediated Lysine Lactylation in Renal Fibrosis: Current Progress and Challenges.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  5. Review
  6. Review
  7. Review
  8. Unveiling Lactylation: A Novel Frontier in Cancer Stemness and Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Lactylation: a novel post-translational modification for cGAS-STING pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
  19. Review
  20. Review

30 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

7 authors.

Zhuming FanInstitute of High Energy Physics, CAS, Beijing 100000, China.
Zhiyang LiuDepartment of Chemistry and COSDAF (Centre of Super-Diamond and Advanced Films), City University of Hong Kong, Hong Kong, China.
Nan ZhangSchool of Biomedical Sciences, The University of Hong Kong, Hong Kong, China.
Wenyu WeiDepartment of Chemistry and COSDAF (Centre of Super-Diamond and Advanced Films), City University of Hong Kong, Hong Kong, China.
Ke ChengDepartment of Chemistry and COSDAF (Centre of Super-Diamond and Advanced Films), City University of Hong Kong, Hong Kong, China.
Hongyan SunDepartment of Chemistry and COSDAF (Centre of Super-Diamond and Advanced Films), City University of Hong Kong, Hong Kong, China.
Quan HaoInstitute of High Energy Physics, CAS, Beijing 100000, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine lactylation (Kla) is a novel histone post-translational modification discovered in late 2019. Later, HDAC1-3, were identified as the robust Kla erasers. While the Sirtuin family proteins showed weak eraser activities toward Kla, as reported. However, the catalytic mechanisms and physiological functions of HDACs and Sirtuins are not identical. In this study, we observed that SIRT3 exhibits a higher eraser activity against the H4K16la site than the other human Sirtuins. Crystal structures revealed the detailed binding mechanisms between lactyl-lysine peptides and SIRT3. Furthermore, a chemical probe, p-H4K16laAlk, was developed to capture potential Kla erasers from cell lysates. SIRT3 was captured by this probe and detected via proteomic analysis. And another chemical probe, p-H4K16la-NBD, was developed to detect the eraser-Kla delactylation processes directly via fluorescence indication. Our findings and chemical probes provide new directions for further investigating Kla and its roles in gene transcription regulation.

Indexed as

EnzymologyMolecular interactionProteinStructural biology

Identifiers

PMID37720100
PMCPMC10504495

What OpenQuestion holds

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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.