Z
Zhongyi Cheng
Researcher at University of Chicago
Publications - 25
Citations - 4050
Zhongyi Cheng is an academic researcher from University of Chicago. The author has contributed to research in topics: Lysine & Acetylation. The author has an hindex of 16, co-authored 22 publications receiving 3365 citations. Previous affiliations of Zhongyi Cheng include University of Texas Southwestern Medical Center & Tongji University.
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Journal ArticleDOI
Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification
Minjia Tan,Hao Luo,Sangkyu Lee,Fulai Jin,Jeong Soo Yang,Emilie Montellier,Thierry Buchou,Zhongyi Cheng,Sophie Rousseaux,Nisha Rajagopal,Zhike Lu,Zhen Ye,Qin Zhu,Joanna Wysocka,Yang Ye,Saadi Khochbin,Bing Ren,Yingming Zhao +17 more
TL;DR: The identification of 67 previously undescribed histone modifications is reported, increasing the current number of known histone marks by about 70%, and lysine crotonylation (Kcr) is investigated, confirming that it represents an evolutionarily-conserved histone posttranslational modification.
Journal ArticleDOI
The first identification of lysine malonylation substrates and its regulatory enzyme
Chao Peng,Zhike Lu,Zhongyu Xie,Zhongyi Cheng,Yue Chen,Minjia Tan,Hao Luo,Yi Zhang,Wendy He,Ke Yang,Bernadette M. M. Zwaans,Daniel X. Tishkoff,Linh Ho,David B. Lombard,Tong-Chuan He,Junbiao Dai,Eric Verdin,Yang Ye,Yingming Zhao +18 more
TL;DR: The results reveal a new type of PTM pathway and identify the first enzyme that can regulate lysine malonylation and lysines succinylation status, and suggest the possibility of nondeacetylation activity of other class IIIlysine deacetylases, especially those without obvious acetylation protein substrates.
Journal ArticleDOI
Lysine Succinylation and Lysine Malonylation in Histones
Zhongyu Xie,Junbiao Dai,Junbiao Dai,Lunzhi Dai,Minjia Tan,Zhongyi Cheng,Yeming Wu,Jef D. Boeke,Yingming Zhao +8 more
TL;DR: The identification and validation of a new type of PTM in histones, lysine succinylation, and it is demonstrated that this histone PTM is present in all eukaryotic cells the authors examined.
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SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability
Lei Li,Lan Shi,Shangda Yang,Ruorong Yan,Di Zhang,Jianguo Yang,Lin He,Wanjin Li,Xia Yi,Luyang Sun,Jing Liang,Zhongyi Cheng,Lei Shi,Yongfeng Shang,Yongfeng Shang,Wenhua Yu +15 more
TL;DR: It is shown that SIRT7 is recruited to DNA double-strand breaks (DSBs) in a PARP1-dependent manner and catalyses desuccinylation of H3K122 therein, thereby promoting chromatin condensation and DSB repair.
Journal ArticleDOI
Comprehensive Profiling of Protein Lysine Acetylation in Escherichia coli
TL;DR: This study has demonstrated that the combined approach is powerful for identification and characterization of protein lysine acetylation on a large scale and provides a series of important information including localization, networks and characterize of acetylome.