Evidence map›Paper›PMID 40192571›Full record

ArticleAngewandte Chemie (International ed. in English)2025

A Method for Constructing Nucleosome Arrays with Spatially Defined Histone PTMs and DNA Damage.

Ziyun Liu, Siqi Xi, Lauren A McGregor, Kenzo Yamatsugu, Shigehiro A Kawashima, Jonathan T Sczepanski, Motomu Kanai

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
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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.

Ziyun LiuGraduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Siqi XiGraduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Lauren A McGregorDepartment of Chemistry, Texas A&M University, College Station, Texas, 77843, USA.
Kenzo YamatsuguGraduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Shigehiro A KawashimaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Jonathan T SczepanskiDepartment of Chemistry, Texas A&M University, College Station, Texas, 77843, USA.
Motomu KanaiGraduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan.

Funding

Japan Society for the Promotion of Science JP19KK0179Japan Society for the Promotion of Science JP21H02074Japan Society for the Promotion of Science JP23H05466Mochida Memorial Foundation for Medical and Pharmaceutical ResearchNational Science Foundation 2126416Takeda Science Foundation
6 · The paper itself

Abstract

DNA damage repair mechanisms, such as base excision repair (BER), safeguard cells against genotoxic agents that cause genetic instability and diseases, including cancer. In eukaryotic nuclei, DNA within nucleosome arrays is less accessible to repair factors than naked DNA owing to the structural constraints of chromatin. Histone acetylation is crucial for loosening the chromatin structure and facilitating access to damaged DNA, yet its effects-particularly in histone globular domains-on BER in nucleosome arrays remain unexplored. Herein, we employ an abiotic/enzymatic hybrid catalyst system (ABEHCS) and a plug-and-play strategy to regioselectively introduce histone acetylation and deoxycytidine-to-deoxyuridine DNA damage. This approach enables the construction of nucleosome arrays with diverse spatial configurations of histone acetylation and DNA lesions, similar to those found in living organisms. Our findings reveal that H3K56 acetylation in the histone globular domain enhances BER efficiency mediated by UDG and APE1 in nucleosome arrays, contingent upon the spatial relationship between H3K56Ac and the DNA damage site.

Indexed as

DNA DamageHistonesNucleosomesAcetylationDNADNA RepairHumansProtein Processing, Post-TranslationalDNAHistonesNucleosomesAbiotic catalystsBase excision repairChromatinDNA damageHistone acetylation

Identifiers

PMID40192571
PMCPMC12144863

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Registered trials

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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.