Evidence map›Paper›PMID 32698016›Full record

ReviewCell chemical biology2020

The Chemical Biology of Reversible Lysine Post-translational Modifications.

Zhipeng A Wang, Philip A Cole

Abstract readReview
In one paragraph

Review in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing 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

106 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Lactylation Modification and Esophageal Cancer: Research Progress From Hypoxia-Induced Metabolic Reprogramming to Immune Escape.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Photoredox-Catalyzed Lysine C(spJournal of the American Chemical Society · 2026
    Article
  10. Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Mining lysine post-translational modification sites by integrating protein language model representations with structural context.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Review
  20. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review

46 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

2 authors.

Zhipeng A WangDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 77 Avenue Louis Pasteur NRB, Boston, MA 02115, USA.
Philip A ColeDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 77 Avenue Louis Pasteur NRB, Boston, MA 02115, USA. Electronic address: pacole@bwh.harvard.edu.

Funding

Protein Acylation and Methylation Mechanisms_Administrative SupplementR37GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2013 to 2022
$4.1M
Mechanisms &Inhibition of Histone AcetyltransferasesR01GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2001 to 2012
$3.8M
Biochemistry of the lysine beta-hydroxybutyrylation pathwayR01DK118266 · NIDDK · UNIVERSITY OF CHICAGO · PI COLE, PHILIP A, ZHAO, YINGMING · 2018 to 2021
$2.1M
NIDDK NIH HHS R01 DK118266NIGMS NIH HHS R01 GM062437NIGMS NIH HHS R37 GM062437
6 · The paper itself

Abstract

Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the "writers," "erasers," and "readers" of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.

Indexed as

AcetylationLysineLysine AcetyltransferasesMethylationProtein MethyltransferasesSmall Molecule LibrariesUbiquitinationUbiquitin-Specific ProteasesLysineLysine AcetyltransferasesProtein MethyltransferasesSmall Molecule LibrariesUbiquitin-Specific Proteasesacetylationacetyltransferasebromodomaindeacetylaseenzymemethylationubiquitination

Identifiers

PMID32698016
PMCPMC7487139

What OpenQuestion holds

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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.