Evidence map›Paper›PMID 30894531›Full record

ArticleNature communications2019

Reversible histone glycation is associated with disease-related changes in chromatin architecture.

Qingfei Zheng, Nathaniel D Omans, Rachel Leicher, Adewola Osunsade, Albert S Agustinus, Efrat Finkin-Groner, Hannah D'Ambrosio, Bo Liu, Sarat Chandarlapaty, Shixin Liu and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed, 1 pooled it
8.6field-weighted citation impact, top 2% 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

118 citing papers in PubMed, 1 synthesis or guideline pooled it, 183 citations in OpenAlex.

  1. Interplay Between Glucose Metabolism and Chromatin Modifications in Cancer.Frontiers in cell and developmental biology · 2021
    Pooled it
  2. Article
  3. Review
  4. Review
  5. Non-Enzymatic MGO-Glycation of SRSF2 Drives RNA Mis-Splicing.Journal of the American Chemical Society · 2026
    Article
  6. Article
  7. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. A Chemical Mechanistic Path Leads the Way to Cellular Argpyrimidine.Journal of the American Chemical Society · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. The chemical language of protein glycation.Nature chemical biology · 2025
    Review
  17. Article
  18. Review
  19. Review
  20. Genesis and regulation of C-terminal cyclic imides from protein damage.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

58 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

11 authors at 3 institutions in 1 country.

Qingfei ZhengChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.ORCID http://orcid.org/0000-0002-8397-3507
Nathaniel D OmansChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.
Rachel LeicherLaboratory of Nanoscale Biophysics and Biochemistry, Rockefeller University, New York, NY, 10065, USA.
Adewola OsunsadeChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.ORCID http://orcid.org/0000-0001-6340-8765
Albert S AgustinusChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.ORCID http://orcid.org/0000-0002-2700-6475
Efrat Finkin-GronerChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.
Hannah D'AmbrosioChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.
Bo LiuHuman Oncology & Pathogenesis Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
Sarat ChandarlapatyHuman Oncology & Pathogenesis Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.ORCID http://orcid.org/0000-0003-4532-8053
Shixin LiuLaboratory of Nanoscale Biophysics and Biochemistry, Rockefeller University, New York, NY, 10065, USA.
Yael DavidChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA. davidshy@mskcc.org.
Memorial Sloan Kettering Cancer Center · USRockefeller University · USTri-Institutional PhD Program in Chemical Biology · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Elisa de Stanchina · 1985 to 2026
$347.4M
Translating Stress Response Targeted Therapy for B-Cell LymphomasP50CA192937 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI BRENTJENS, RENIER JOSEPH · 2016 to 2020
$10.9M
Tri-Institutional Training Program in Computational Biology & MedicineT32GM083937 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI CHRISTINI, DAVID J. · 2009 to 2018
$3.1M
Tri-Institutional PhD Program in Chemical BiologyT32GM115327 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI TAN, DEREK S · 2015 to 2019
$741k
NCI NIH HHS P30 CA008748NCI NIH HHS P50 CA192937NIGMS NIH HHS T32 GM083937NIGMS NIH HHS T32 GM115327NIH HHS P30 CA008748NIH HHS P50-CA192937
6 · The paper itself

Abstract

Cellular proteins continuously undergo non-enzymatic covalent modifications (NECMs) that accumulate under normal physiological conditions and are stimulated by changes in the cellular microenvironment. Glycation, the hallmark of diabetes, is a prevalent NECM associated with an array of pathologies. Histone proteins are particularly susceptible to NECMs due to their long half-lives and nucleophilic disordered tails that undergo extensive regulatory modifications; however, histone NECMs remain poorly understood. Here we perform a detailed analysis of histone glycation in vitro and in vivo and find it has global ramifications on histone enzymatic PTMs, the assembly and stability of nucleosomes, and chromatin architecture. Importantly, we identify a physiologic regulation mechanism, the enzyme DJ-1, which functions as a potent histone deglycase. Finally, we detect intense histone glycation and DJ-1 overexpression in breast cancer tumors. Collectively, our results suggest an additional mechanism for cellular metabolic damage through epigenetic perturbation, with implications in pathogenesis.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAcetylationAnimalsBreast NeoplasmsCell Line, TumorFemaleGlycation End Products, AdvancedGlycosylationHeterograftsHistonesHumansMiceNucleosomesProtein Deglycase DJ-1PyruvaldehydeGlycation End Products, AdvancedHistonesNucleosomesPARK7 protein, humanProtein Deglycase DJ-1Pyruvaldehyde

Identifiers

PMID30894531
PMCPMC6426841
OpenAlexW2924725909

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.