Mass spectrometry-based characterization of histone post-translational modification
文献类型：期刊论文
| 作者 | Zhao, Wensi6; Zhang, Jun1; Chen, Kaifeng1,2; Yuan, Jian3,4; Zhai, Linhui6; Tan, Minjia1,2,5,6 |
| 刊名 | CURRENT OPINION IN CHEMICAL BIOLOGY
 |
| 出版日期 | 2025-10-01 |
| 卷号 | 88页码:10 |
| ISSN号 | 1367-5931 |
| DOI | 10.1016/j.cbpa.2025.102622 |
| 英文摘要 | Histone post-translational modifications (PTMs) play critical roles in regulating chromatin dynamics and gene expression. Increasing evidence demonstrates that the dysregulation of histone PTMs is closely associated with the pathogenesis of various diseases. Traditional methods for detecting histone PTMs, such as western blot (WB) and chromatin immunoprecipitation sequencing (ChIP-seq), are often limited by their dependence on specific antibodies and relatively low analytical throughput. Mass spectrometry (MS)-based proteomics offers a powerful and unbiased approach for comprehensive characterization of histone PTMs. This review focuses on the advanced development of MS-based strategies for characterizing histone PTMs. These strategies include histone extraction, enzymatic digestion, labeling, enrichment, and MS based detection. These techniques not only enable comprehensive identification and quantitative analysis of classical modifications, such as acetylation and methylation, but also substantially facilitate the discovery of less-characterized histone PTMs, including succinylation, lactylation, crotonylation, and monoaminylation. Consequently, these findings significantly enhance the complexity of histone code. Collectively, MS-based approaches have profoundly advanced our understanding of histone PTM landscapes and their potential epigenetic regulatory mechanisms in both physiology and pathology contexts. |
| WOS关键词 | QUANTITATIVE PROTEOMICS ; METABOLIC-REGULATION ; GENE-EXPRESSION ; LYSINE ; PROPIONYLATION ; CELLS |
| 资助项目 | Natural Science Foundation of China[22225702] ; Natural Science Foundation of China[T2488301] ; Natural Science Foundation of China[32171434] ; Natural Science Foundation of China[32090032] ; Zhongshan Science and Technology Bureau[CXTD2023009] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:001548856400001 |
| 出版者 | ELSEVIER SCI LTD |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/321249]  |
| 专题 | 国家级研究中心_原创新药研究全国重点实验室 |
| 通讯作者 | Zhai, Linhui; Tan, Minjia |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China 2.Univ Chinese Acad Sci, Beijing 101408, Peoples R China 3.Tongji Univ, Shanghai East Hosp, Res Ctr Translat Med, State Key Lab Cardiol,Sch Med, Shanghai 200120, Peoples R China 4.Tongji Univ, Sch Med, Shanghai East Hosp, Res Ctr Translat Med, Shanghai 200120, Peoples R China 5.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Zhongshan 528400, Peoples R China 6.Tongji Univ, Shanghai Peoples Hosp 4, Translat Res Inst Brain & Brain Like Intelligence, Sch Med, Shanghai 200434, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhao, Wensi,Zhang, Jun,Chen, Kaifeng,et al. Mass spectrometry-based characterization of histone post-translational modification[J]. CURRENT OPINION IN CHEMICAL BIOLOGY,2025,88:10. |
| APA | Zhao, Wensi,Zhang, Jun,Chen, Kaifeng,Yuan, Jian,Zhai, Linhui,&Tan, Minjia.(2025).Mass spectrometry-based characterization of histone post-translational modification.CURRENT OPINION IN CHEMICAL BIOLOGY,88,10. |
| MLA | Zhao, Wensi,et al."Mass spectrometry-based characterization of histone post-translational modification".CURRENT OPINION IN CHEMICAL BIOLOGY 88(2025):10. |
入库方式： OAI收割
来源：上海药物研究所
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