发表论文
[1] Xiao, Shumin, Wang, Yajing, Shan, Shan, Zhou, Zheng. The interplay between viral molecular mimicry and host chromatin dynamics. NUCLEUS[J]. 2023, 14(1): http://dx.doi.org/10.1080/19491034.2023.2216560.[2] Li Huang, Youwang Wang, Haizhen Long, Haoqiang Zhu, Zengqi Wen, Liwei Zhang, Wenhao Zhang, Zhenqian Guo, Longge Wang, Fangyi Tang, Jie Hu, Keyan Bao, Ping Zhu, Guohong Li, Zheng Zhou. Structural insight into H4K20 methylation on H2A.Z-nucleosome by SUV420H1. MOLECULAR CELL[J]. 2023, 83(16): 2884-2895.e7, http://dx.doi.org/10.1016/j.molcel.2023.07.001.[3] 周政. 周政:因材施教 因地制宜 寓研于乐. 中国科技教育[J]. 2022, 34-35, http://lib.cqvip.com/Qikan/Article/Detail?id=7106845778.[4] Shi, Liuxin, Huang, Li, Long, Haizhen, Song, Aoqun, Zhou, Zheng. Structural basis of nucleosomal H4K20 methylation by methyltransferase SET8. FASEB JOURNAL[J]. 2022, 36(6): http://dx.doi.org/10.1096/fj.202101821R.[5] Jiao Chen, Zheng. Epstein-Barr virus protein BKRF4 restricts nucleosome assembly to suppress host antiviral responses. Proceedings of the National Academy of Sciences of the United States of America[J]. 2022, [6] Dai, Linchang, Xiao, Xue, Pan, Lu, Shi, Liuxin, Xu, Ning, Zhang, Zhuqiang, Feng, Xiaoli, Ma, Lu, Dou, Shuoxing, Wang, Pengye, Zhu, Bing, Li, Wei, Zhou, Zheng. Recognition of the inherently unstable H2A nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange. CELL REPORTS[J]. 2021, 35(8): http://dx.doi.org/10.1016/j.celrep.2021.109183.[7] Zhou, Ning, Shi, Liuxin, Shan, Shan, Zhou, Zheng. Molecular basis for the selective recognition and ubiquitination of centromeric histone H3 by yeast E3 ligase Psh1. JOURNAL OF GENETICS AND GENOMICS[J]. 2021, 48(6): 463-472, http://dx.doi.org/10.1016/j.jgg.2021.04.007.[8] Zhou, Min, Dai, Linchang, Li, Chengmin, Shi, Liuxin, Huang, Yan, Guo, Zhenqian, Wu, Fei, Zhu, Ping, Zhou, Zheng. Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2AZ2.2. EMBO JOURNAL[J]. 2021, 40(1): http://dx.doi.org/10.15252/embj.2020105907.[9] Dai, Linchang, Dai, Yaxin, Han, Jinhua, Huang, Yan, Wang, Longge, Huang, Jun, Zhou, Zheng. Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin. MOLECULAR CELL[J]. 2021, 81(13): 2765-+, http://dx.doi.org/10.1016/j.molcel.2021.05.010.[10] Huang, Yan, Sun, Lu, Pierrakeas, Leonidas, Dai, Linchang, Pan, Lu, Luk, Ed, Zhou, Zheng. Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2020, 117(7): 3543-3550, https://www.webofscience.com/wos/woscc/full-record/WOS:000514096400035.[11] Huang, Yan, Dai, Yaxin, Zhou, Zheng. Mechanistic and structural insights into histone H2A-H2B chaperone in chromatin regulation. BIOCHEMICAL JOURNALnull. 2020, 477(17): 3367-3386, https://www.webofscience.com/wos/woscc/full-record/WOS:000582386500016.[12] Dai, Yaxin, Zhang, Fan, Wang, Longge, Shan, Shan, Gong, Zihua, Zhou, Zheng. Structural basis for shieldin complex subunit 3?mediated recruitment of the checkpoint protein REV7 during DNA double-strand break repair. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2020, 295(1): 250-262, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6952594/.[13] Gao, Ying, Ren, RuJing, Zhong, ZiLin, Dammer, Eric, Zhao, QianHua, Shan, Shan, Zhou, Zheng, Li, Xia, Zhang, YueQi, Cui, HaiLun, Hu, YongBo, Chen, ShengDi, Chen, JianJun, Guo, QiHao, Wang, Gang. Mutation profile of APP, PSEN1, and PSEN2 in Chinese familial Alzheimer's disease. NEUROBIOLOGY OF AGING[J]. 2019, 77: 154-157, http://dx.doi.org/10.1016/j.neurobiolaging.2019.01.018.[14] Wang, Yunyun, Liu, Sheng, Sun, Lu, Xu, Ning, Shan, Shan, Wu, Fei, Liang, Xiaoping, Huang, Yingzi, Luk, Ed, Wu, Carl, Zhou, Zheng. Structural insights into histone chaperone Chz1-mediated H2A.Z recognition and histone replacement. PLOS BIOLOGY[J]. 2019, 17(5): http://dx.doi.org/10.1371/journal.pbio.3000277.[15] Yaxin Dai, Fan Zhang, Longge Wang, Shan Shan, Zihua Gong, Zheng Zhou. Structural basis for shieldin complex subunit 3–mediated recruitment of the checkpoint protein REV7 during DNA double-strand break repair. THE JOURNAL OF BIOLOGICAL CHEMISTRY. 2019, 295(1): 250-262, http://dx.doi.org/10.1074/jbc.RA119.011464.[16] Dai, Linchang, Xu, Ning, Zhou, Zheng. NMR investigations on H2A-H2B heterodimer dynamics conferred by histone variant H2A.Z. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS[J]. 2019, 518(4): 752-758, http://dx.doi.org/10.1016/j.bbrc.2019.08.127.[17] Sun, Wan, Shen, Yanjie, Shan, Shan, Han, Liyun, Li, Yang, Zhou, Zheng, Zhong, Zilin, Chen, Jianjun. Identification of TYR mutations in patients with oculocutaneous albinism. MOLECULAR MEDICINE REPORTS[J]. 2018, 17(6): 8409-8413, https://www.webofscience.com/wos/woscc/full-record/WOS:000435394000118.[18] Huang Yan, Zhou Zheng. Recent Progress in Histone Chaperones Associated With H2A-H2B Type Histones. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2018, 45(9): 971-980, https://www.webofscience.com/wos/woscc/full-record/WOS:000445847600010.[19] Dai, Linchang, Xie, Xiaoyan, Zhou, Zheng. Crystal structure of the histone heterodimer containing histone variant H2A.Bbd. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS[J]. 2018, 503(3): 1786-1791, http://dx.doi.org/10.1016/j.bbrc.2018.07.114.[20] Yaxin Dai, Aili Zhang, Shan Shan, Zihua Gong, Zheng Zhou. Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR. NATURE COMMUNICATIONS[J]. 2018, 9(1): https://doaj.org/article/a2d88984045941a58372fc19fffd5812.[21] Huang Yan, Zhou Zheng. Recent Progress in Histone Chaperones Associated With H2A-H2B Type Histones. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2018, 45(9): 971-980, https://www.webofscience.com/wos/woscc/full-record/WOS:000445847600010.[22] Liang, Xiaoping, Shan, Shan, Pan, Lu, Zhao, Jicheng, Ranjan, Anand, Wang, Feng, Zhang, Zhuqiang, Huang, Yingzi, Feng, Hanqiao, Wei, Debbie, Huang, Li, Liu, Xuehui, Zhong, Qiang, Lou, Jizhong, Li, Guohong, Wu, Carl, Zhou, Zheng. Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2016, 23(4): 317-323, http://dx.doi.org/10.1038/nsmb.3190.[23] Zhong, Zilin, Yan, Min, Sun, Wan, Wu, Zehua, Han, Liyun, Zhou, Zheng, Zheng, Fang, Chen, Jianjun. Two novel mutations in PRPF3 causing autosomal dominant retinitis pigmentosa. SCIENTIFIC REPORTS[J]. 2016, 6: http://dx.doi.org/10.1038/srep37840.[24] Zhou JuJun, Feng XiaoLi, Zhou Zheng. Chromatin Assembly of Histone Variants. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2015, 42(11): 1003-1008, https://www.webofscience.com/wos/woscc/full-record/WOS:000365558600004.[25] Mao, Zhuo, Pan, Lu, Wang, Weixiang, Sun, Jian, Shan, Shan, Dong, Qiang, Liang, Xiaoping, Dai, Linchang, Ding, Xiaojun, Chen, She, Zhang, Zhuqiang, Zhu, Bing, Zhou, Zheng. Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. CELL RESEARCH[J]. 2014, 24(4): 389-399, http://dx.doi.org/10.1038/cr.2014.30.[26] Hong, Jingjun, Feng, Hanqiao, Zhou, Zheng, Ghirlando, Rodolfo, Bai, Yawen. Identification of Functionally Conserved Regions in the Structure of the Chaperone/CenH3/H4 Complex. JOURNAL OF MOLECULAR BIOLOGY[J]. 2013, 425(3): 536-545, http://dx.doi.org/10.1016/j.jmb.2012.11.021.[27] Zhou, Zheng, Feng, Hanqiao, Zhou, BingRui, Ghirlando, Rodolfo, Hu, Kaifeng, Zwolak, Adam, Jenkins, Lisa M Miller, Xiao, Hua, Tjandra, Nico, Wu, Carl, Bai, Yawen. Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3. NATURE[J]. 2011, 472(7342): 234-237, https://www.webofscience.com/wos/woscc/full-record/WOS:000289469100046.[28] Hansen, D Flemming, Zhou, Zheng, Fen, Haniqiao, Jenkins, Lisa M Miller, Bai, Yawen, Kay, Lewis E. Binding Kinetics of Histone Chaperone Chz1 and Variant Histone H2A.Z-H2B by Relaxation Dispersion NMR Spectroscopy. JOURNAL OF MOLECULAR BIOLOGY[J]. 2009, 387(1): 1-9, http://dx.doi.org/10.1016/j.jmb.2009.01.009.[29] Zhou, Zheng, Feng, Hanqiao, Ghirlando, Rodolfo, Bai, Yawen. The High-Resolution NMR Structure of the Early Folding Intermediate of the Thermus thermophilus Ribonuclease H. JOURNAL OF MOLECULAR BIOLOGY[J]. 2008, 384(2): 531-539, http://dx.doi.org/10.1016/j.jmb.2008.09.044.[30] Zhou, Zheng, Feng, Hanqiao, Hansen, D Flemming, Kato, Hidenori, Luk, Ed, Freedberg, Daron I, Kay, Lewis E, Wu, Carl, Bai, Yawen. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2008, 15(8): 868-869, https://www.webofscience.com/wos/woscc/full-record/WOS:000258191100023.[31] Zheng Zhou, Hanqiao Feng, Yawen Bai. Detection of a hidden folding intermediate in the focal adhesion target domain: Implications for its function and folding. PROTEINS. 2006, [32] Feng, HQ, Zhou, Z, Bai, YW. A protein folding pathway with multiple folding intermediates at atomic resolution. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2005, 102(14): 5026-5031, https://www.webofscience.com/wos/woscc/full-record/WOS:000228195800021.[33] Zheng Zhou. Structure determination and folding pathway characterization of an engineered multi-domain protein: kinetic versus equilibrium intermediates. Biochemistry-US. 2005, [34] Zheng Zhou. The folding pathway of Rd-apocyt b562: Demonstration of the on-pathway nature of a hidden intermediate and characterization of the rate-limiting transition state by protein. J. Mol. Biol.. 2005,