Evidence map›Paper›PMID 42104010›Full record

ArticleNature chemical biology2026

Chemoproteomic profiling reveals histone H4 dopaminylation inhibiting cell growth.

Yinfeng Zhang, Yaqi Yang, Wenyan Wu, Min Zhang, Jianan Rao, Wenting Song, Yi Pan, Nan Shen, Linxue Li, Taishan Min and 8 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

18 authors.

Yinfeng Zhang *Pediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Yaqi Yang *Pediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Wenyan Wu *Pediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Min Zhang *Division of Life Sciences and Medicine, School of Life Sciences, University of Science and Technology of China, Hefei, China.
Jianan RaoPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0009-0006-0936-8196
Wenting SongPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0000-0002-2077-2441
Yi PanPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0000-0001-7724-6322
Nan ShenDepartment of Infectious Diseases, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0000-0003-3923-3488
Linxue LiPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Taishan MinPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0009-0004-3121-5386
Kai LiCenter for Cell and Gene Therapy, Clinical Research Center for Cell-Based Immunotherapy, Shanghai Pudong Hospital, State Key Laboratory of Genetic Engineering, School of Life Sciences, Human Phenome Institute, Fudan University, Shanghai, China.ORCID http://orcid.org/0000-0001-6544-6052
Xiaoqing ZhangPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0000-0002-2106-2994
Xin-Yue QiuState Key Laboratory of Synergistic Chem-Bio Synthesis, School of Chemistry and Chemical Engineering, Shanghai Jiao Tong University, Shanghai, China.
Shu-Yu ZhangState Key Laboratory of Synergistic Chem-Bio Synthesis, School of Chemistry and Chemical Engineering, Shanghai Jiao Tong University, Shanghai, China. zhangsy16@sjtu.edu.cn.ORCID http://orcid.org/0000-0002-1811-4159
Wenjun YangDepartment of Pediatric Orthopedics, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. wjyang@sibcb.ac.cn.ORCID http://orcid.org/0000-0002-0324-1649
Jianye ZangDivision of Life Sciences and Medicine, School of Life Sciences, University of Science and Technology of China, Hefei, China. zangjy@ustc.edu.cn.ORCID http://orcid.org/0000-0003-2648-9783
Yu LiuPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China. yu.liu@sjtu.edu.cn.ORCID http://orcid.org/0000-0001-8928-2558
Xi MoPediatric Translational Medicine Institute, Shanghai Children's Medical Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China. xi.mo@shsmu.edu.cn.ORCID http://orcid.org/0000-0001-7035-6182

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32401008National Natural Science Foundation of China (National Science Foundation of China) 32570695National Natural Science Foundation of China (National Science Foundation of China) 82002662National Natural Science Foundation of China (National Science Foundation of China) 82372340National Natural Science Foundation of China (National Science Foundation of China) 82572664
6 · The paper itself

Abstract

Dopaminylation, the covalent attachment of dopamine to the side chain of glutamine in proteins, represents a newly characterized class of posttranslational modifications. Because of the limited identification of substrates, the functions and molecular mechanisms associated with dopaminylation remain largely uncharacterized. Using an alkyne-functionalized dopamine probe, we developed a method for selectively enriching dopaminylated proteins in whole-cell systems. This approach provided a comprehensive resource of 4,133 dopamine-enriched protein candidates and peptide-level analysis with acid-cleavable tags identified 1,181 putative dopaminylated proteins, including histone H4 dopaminylation at Q27 (H4Q27dop), which we further validated. Functionally, H4Q27dop acts as a transcriptional repressor in a neuroblastoma model, where it blocks CEBPD binding at the CCND1 promoter, leading to transcriptional downregulation of CCND1 and subsequent suppression of cell proliferation. Our findings provide both a valuable resource of dopaminylated substrate proteins and a distinct mechanistic insight into how dopamine regulates neuroblastoma cell growth.

Identifiers

PMID42104010

What Socratic 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 Socratic graph.