Evidence map›Paper›PMID 37098732›Full record

ArticleCurrent protocols2023

New Histone Lysine Acylation Biomarkers and Their Roles in Epigenetic Regulation.

Qianyun Fu, Amber Cat, Y George Zheng

Open access · hybridAbstract read
In one paragraph

Article in Current protocols, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Lactylation and antitumor immunity.Frontiers in immunology · 2025
    Review
  12. Review
  13. Review
  14. Review
  15. Epigenetic meets metabolism: novel vulnerabilities to fight cancer.Cell communication and signaling : CCS · 2023
    Review
  16. 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

3 authors at 1 institution in 1 country.

Qianyun FuDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, Georgia.
Amber CatDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, Georgia.
Y George ZhengDepartment of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, Georgia.
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein posttranslational modification (PTM) is a biochemical mechanism benefitting cellular adaptation to dynamic intracellular and environmental conditions. Recently, several acylation marks have been identified as new protein PTMs occurring on specific lysine residues in mammalian cells: isobutyrylation, methacrylation, benzoylation, isonicotinylation, and lactylation. These acylation marks were initially discovered to occur on nucleosomal histones, but they potentially occur as prevalent biomarkers on non-histone proteins as well. The existence of these PTMs is a downstream consequence of metabolism and demonstrates the intimate crosstalk between active cellular metabolites and regulation of protein function. Emerging evidence indicates that these acylation marks on histones affect DNA transcription and are functionally distinct from the well-studied lysine acetylation. Herein, we discuss enzymatic regulation and metabolic etiology of these acylations, 'reader' proteins that recognize different acylations, and their possible physiological and pathological functions. Several of these modifications correlate with other well-studied acylations and fine-tune the regulation of gene expression. Overall, findings of these acylation marks reveal new molecular links between metabolism and epigenetics and open up many questions for future investigation. © 2023 The Authors. Current Protocols published by Wiley Periodicals LLC.

Indexed as

HistonesLysineAcylationAnimalsBiomarkersEpigenesis, GeneticMammalsBiomarkersHistonesLysineacetylationepigeneticshistonelysine acylationmetabolism

Identifiers

PMID37098732
PMCPMC13528283
OpenAlexW4367047805

What OpenQuestion holds

Textmetadata
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.