071010-生物化学与分子生物学
071011-生物物理学

基因转录的表观遗传调控和RNA转录后加工
表观遗传学，结构生物学

1985-06--1989-08   美国Brandeis大学物理系   理学博士学位
1984-09--1985-05   美国Brandeis大学物理系   理学硕士学位
1980-09--1984-07   浙江大学物理系   获理学学士学位

   

2015-12~现在, 中国科学院生物物理研究所, 副所长
2013-05~2015-12,中国科学院前沿科学与教育局, 局长
2012-11~2013-05,中国科学院生物科学与生物技术局, 局长
2010-01~2012-11,中国科学院生物物理研究所, 副所长
2009-01~现在, 中国科学院生物物理研究所, 研究员
2006-01~2008-12,美国纽约大学医学院, 教授（终身）
2005-01~2005-12,美国冷泉港实验室, 教授
2000-01~2004-12,美国冷泉港实验室, 副教授
1996-06~2000-01,美国冷泉港实验室, 助理教授
1993-03~1996-05,美国冷泉港实验室, 访问学者、研究助理
1991-09~1993-03,美国纽约州立大学石溪分校物理系, 博士后
1989-09~1991-09,美国德克萨斯大学奥斯汀分校物理系, 博士后

2015-10-01-今,《Epigenetics & Chromatin》杂志, 编委会成员
2015-03-01-今,《Structure》杂志, 编委会成员
2014-08-01-今,中国生物化学与分子生物学学会, 副理事长
2013-11-01-今,中国生物物理学会, 副理事长
2013-01-01-今,《中国科学：生命科学》英文版, 编委会成员
2011-06-01-今,《BBA‐Gene Regulatory Mechanisms》杂志, 编委会成员
2010-01-01-今,《Protein & Cell》杂志, 副主编
2007-01-01-今,《Genes & Development》杂志, 编委会成员

   

（1） 全国优秀科技工作者, 国家级, 2016
（2） 中国科学院优秀研究生指导教师奖, , 部委级, 2012
（3） 中国侨界（创新人才）贡献奖, , 其他, 2010
（4） 中国科学院－诺和诺德长城教授奖, , 部委级, 2009
（5） 国家“杰出青年”基金, , 部委级, 2009
（6） 首批****专家, , 国家级, 2008
（7） 中美联合招收物理研究生考试 (CUSPEA) 入选者, , 其他, 1984
（8） 浙江大学优秀毕业论文奖, , 研究所（学校）, 1984

[1] 许瑞明, 倪龙麒, 杨文思, 金文星. 一种蛋白质核酸纳米颗粒的设计以及组装方法. 202211593512.4, 2022-12-13.

   

[1] Liu, Fei, Pang, Ningning, Xu, RuiMing, Yang, Na. Mechanism and design of allosteric activators of SIRT1. PROTEIN & CELLnull. 2023, 14(5): 387-392, http://dx.doi.org/10.1093/procel/pwac039.
[2] Chao-Pei Liu, Zhenyu Yu, Jun Xiong, Jie Hu, Aoqun Song, Dongbo Ding, Cong Yu, Na Yang, Mingzhu Wang, Juan Yu, Peini Hou, Kangning Zeng, Zhenyu Li, Xinzheng Zhang, Wei Li, Zhiguo Zhang, Bing Zhu, Guohong Li, Ruiming Xu. Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1. Science[J]. 2023, 381: eadd8673-, [3] Ge, Weiran, Yu, Cong, Li, Jingjing, Yu, Zhenyu, Li, Xiaorong, Zhang, Yan, Liu, ChaoPei, Li, Yingfeng, Tian, Changlin, Zhang, Xinzheng, Li, Guohong, Zhu, Bing, Xu, RuiMing. Basis of the H2AK119 specificity of the Polycomb repressive deubiquitinase. NATURE. 2023, http://dx.doi.org/10.1038/s41586-023-05841-y.
[4] 许瑞明. Topography of histone H3–H4 interaction with the Hat1–Hat2 acetyltransferase complex. Genes & Dev.[J]. 2022, [5] Yue, Ye, Yang, WenSi, Zhang, Lin, Liu, ChaoPei, Xu, RuiMing. Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex. GENES & DEVELOPMENT[J]. 2022, 36(7-8): 408-413, http://dx.doi.org/10.1101/gad.349099.121.
[6] Jing Zhang, Yan Zhang, Qinglong You, Chang Huang, Tiantian Zhang, Mingzhu Wang, Tianwei Zhang, Xiaocheng Yang, Jun Xiong, Yingfeng Li, Chao-Pei Liu, Zhuqiang Zhang, rui-ming xu, Bing Zhu. Highly enriched BEND3 prevents the premature activation of bivalent genes during differentiation. Science[J]. 2022, 1053-1058, [7] Liu, ChaoPei, Jin, Wenxing, Hu, Jie, Wang, Mingzhu, Chen, Jingjing, Li, Guohong, Xu, RuiMing. Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones. GENES & DEVELOPMENT[J]. 2021, 35(23-24): 1610-1624, http://dx.doi.org/10.1101/gad.349100.121.
[8] 许瑞明. Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones. Genes & Dev[J]. 2021, [9] Xu, Xiang, Wang, Mingzhu, Sun, Jixue, Yu, Zhenyu, Li, Guohong, Yang, Na, Xu, RuiMing. Structure specific DNA recognition by the SLX1-SLX4 endonuclease complex. NUCLEIC ACIDS RESEARCH[J]. 2021, 49(13): 7740-7752, http://dx.doi.org/10.1093/nar/gkab542.
[10] Gou, LanTao, Lim, DoHwan, Ma, Wubin, Aubol, Brandon E, Hao, Yajing, Wang, Xin, Zhao, Jun, Liang, Zhengyu, Shao, Changwei, Zhang, Xuan, Meng, Fan, Li, Hairi, Zhang, Xiaorong, Xu, Ruiming, Li, Dangsheng, Rosenfeld, Michael G, Mellon, Pamela L, Adams, Joseph A, Liu, MoFang, Fu, XiangDong. Initiation of Parental Genome Reprogramming in Fertilized Oocyte by Splicing Kinase SRPK1-Catalyzed Protamine Phosphorylation. CELL[J]. 2020, 180(6): 1212-+, http://dx.doi.org/10.1016/j.cell.2020.02.020.
[11] Gao, Yujing, Chen, Lijia, Han, Yali, Wu, Fangrui, Yang, WenSi, Zhang, Zheng, Huo, Tong, Zhu, Yingmin, Yu, Chengtai, Kim, Hong, Lee, Mark, Tang, Zhen, Phillips, Kevin, He, Bin, Jung, Sung Yun, Song, Yongcheng, Zhu, Bokai, Xu, RuiMing, Feng, Qin. Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha. COMMUNICATIONS BIOLOGY[J]. 2020, 3(1): http://dx.doi.org/10.1038/s42003-020-0898-0.
[12] Li, Zhiming, Hua, Xu, SerraCardona, Albert, Xu, Xiaowei, Gan, Songlin, Zhou, Hui, Yang, WenSi, Chen, Chunlong, Xu, RuiMing, Zhang, Zhiguo. DNA polymerase alpha interacts with H3-H4 and facilitates the transfer of parental histones to lagging strands. SCIENCE ADVANCES[J]. 2020, 6(35): http://dx.doi.org/10.1126/sciadv.abb5820.
[13] Jin, Wenxing, Wang, Jia, Liu, ChaoPei, Wang, HongWei, Xu, RuiMing. Structural Basis for pri-miRNA Recognition by Drosha. MOLECULAR CELL[J]. 2020, 78(3): 423-+, http://dx.doi.org/10.1016/j.molcel.2020.02.024.
[14] Cao, Duanfang, Han, Xiaonan, Fan, Xiaoyi, Xu, RuiMing, Zhang, Xinzheng. Structural basis for nucleosome-mediated inhibition of cGAS activity. CELL RESEARCH[J]. 2020, 30(12): 1088-1097, http://lib.cqvip.com/Qikan/Article/Detail?id=7104154142.
[15] Hou, Peini, Huang, Chang, Liu, ChaoPei, Yang, Na, Yu, Tianshu, Yin, Yuxin, Zhu, Bing, Xu, RuiMing. Structural Insights into Stimulation of Ash1L's H3K36 Methyltransferase Activity through Mrg15 Binding. STRUCTURE[J]. 2019, 27(5): 837-+, http://dx.doi.org/10.1016/j.str.2019.01.015.
[16] 张林, Albert, SerraCardona, Hui, Zhou, Mingzhu, Wang, Na, Yang, 张志国, 许瑞明. Rtt109催化组蛋白H3K56的Asf1依赖性乙酰化中的多位点底物识别. 科学新闻[J]. 2019, 56-56, http://lib.cqvip.com/Qikan/Article/Detail?id=75888869504849574850485153.
[17] Du, Wenlong, Dong, Qiang, Zhang, Zhuqiang, Liu, Baodong, Zhou, Ting, Xu, Ruiming, Wang, Hailin, Zhu, Bing, Li, Yingfeng. Stella protein facilitates DNA demethylation by disrupting the chromatin association of the RING finger-type E3 ubiquitin ligase UHRF1. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2019, 294(22): 8907-8917, http://dx.doi.org/10.1074/jbc.RA119.008008.
[18] Song, Xiaosheng, Yang, Liuliu, Wang, Mingzhu, Gu, Yue, Ye, Buqing, Fan, Zusen, Xu, RuiMing, Yang, Na. A higher-order configuration of the heterodimeric DOT1L-AF10 coiled-coil domains potentiates their leukemogenenic activity. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2019, 116(40): 19917-19923, http://dx.doi.org/10.1073/pnas.1904672116.
[19] Yu, Chuanhe, Gan, Haiyun, SerraCardona, Albert, Zhang, Lin, Gan, Songlin, Sharma, Sushma, Johansson, Erik, Chabes, Andrei, Xu, RuiMing, Zhang, Zhiguo. A mechanism for preventing asymmetric histone segregation onto replicating DNA strands. SCIENCE[J]. 2018, 361(6409): 1386-+, http://dx.doi.org/10.1126/science.aat8849.
[20] RuimingXu. The road to a first-class research institute: creating an exceptional environment, recruiting outstanding scientists, producing high-impact work,and nurturing a culture of innovation-preface to the 60th anniversary special issue. Biophysics Reports[J]. 2018, 4(4): 167-169, http://www.biophysics-reports.org:80/en/article/doi/10.1007/s41048-018-0069-8.
[21] Xiong, Chaoyang, Wen, Zengqi, Yu, Juan, Chen, Jun, Liu, ChaoPei, Zhang, Xiaodong, Chen, Ping, Xu, RuiMing, Li, Guohong. UBN1/2 of HIRA complex is responsible for recognition and deposition of H3.3 at cis- regulatory elements of genes in mouse ES cells. BMC BIOLOGY[J]. 2018, 16(1): http://dx.doi.org/10.1186/s12915-018-0573-9.
[22] 许瑞明. 筑巢引凤产出高水平成果 凝练文化创建一流研究所. 生物化学与生物物理进展[J]. 2018, 45(9): 885-886, http://lib.cqvip.com/Qikan/Article/Detail?id=676250509.
[23] Zhang, Lin, SerraCardona, Albert, Zhou, Hui, Wang, Mingzhu, Yang, Na, Zhang, Zhiguo, Xu, RuiMing. Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109. CELL[J]. 2018, 174(4): 818-+, http://www.corc.org.cn/handle/1471x/2201300.
[24] 杨娜, 许瑞明. 组蛋白变体的功能与识别机制. 生命科学[J]. 2017, 29(10): 946-954, http://lib.cqvip.com/Qikan/Article/Detail?id=674160591.
[25] Kong, GuiMei, Yu, Min, Gu, Zhongping, Chen, Zhi, Xu, RuiMing, OBryant, Deon, Wang, Zhengxin. Selective small-chemical inhibitors of protein arginine methyltransferase 5 with anti-lung cancer activity. PLOS ONE[J]. 2017, 12(8): https://doaj.org/article/2291e2f5c2114d85b6c51266fea9e97d.
[26] Fang, Qianglin, Chen, Ping, Wang, Mingzhu, Fang, Junnan, Yang, Na, Li, Guohong, Xu, RuiMing. Human cytomegalovirus IE1 protein alters the higher-order chromatin structure by targeting the acidic patch of the nucleosome. ELIFE[J]. 2016, 5: https://doaj.org/article/d5ccb8aae2824d78a5f7299303ab4d35.
[27] Fang, Dong, Gan, Haiyun, Lee, JeongHeon, Han, Jing, Wang, Zhiquan, Riester, Scott M, Jin, Long, Chen, Jianji, Zhou, Hui, Wang, Jinglong, Zhang, Honglian, Yang, Na, Bradley, Elizabeth W, Ho, Thai H, Rubin, Brian P, Bridge, Julia A, Thibodeau, Stephen N, Ordog, Tamas, Chen, Yue, van Wijnen, Andre J, Oliveira, Andre M, Xu, RuiMing, Westendorf, Jennifer J, Zhang, Zhiguo. The histone H3.3K36M mutation reprograms the epigenome of chondroblastomas. SCIENCE[J]. 2016, 352(6291): 1344-1348, [28] Jin, Wenxing, Wang, Yi, Liu, ChaoPei, Yang, Na, Jin, Mingliang, Cong, Yao, Wang, Mingzhu, Xu, RuiMing. Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5. GENES & DEVELOPMENT[J]. 2016, 30(21): 2391-2403, http://dx.doi.org/10.1101/gad.291377.116.
[29] Fu, Weiqi, Liu, Nan, Qiao, Qi, Wang, Mingzhu, Min, Jinrong, Zhu, Bing, Xu, RuiMing, Yang, Na. Structural Basis for Substrate Preference of SMYD3, a SET Domain-containing Protein Lysine Methyltransferase. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2016, 291(17): 9173-9180, http://dx.doi.org/10.1074/jbc.M115.709832.
[30] Wang, Hong, Wang, Mingzhu, Yang, Na, Xu, RuiMing. Structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2. PROTEIN & CELLnull. 2015, 6(9): 693-697, http://dx.doi.org/10.1007/s13238-015-0190-0.
[31] Fang, Junnan, Liu, Yuting, Wei, Yun, Deng, Wenqiang, Yu, Zhouliang, Huang, Li, Teng, Yan, Yao, Ting, You, Qinglong, Ruan, Haihe, Chen, Ping, Xu, RuiMing, Li, Guohong. Structural transitions of centromeric chromatin regulate the cell cycle-dependent recruitment of CENP-N. GENES & DEVELOPMENT[J]. 2015, 29(10): 1058-1073, http://www.corc.org.cn/handle/1471x/2376555.
[32] Yang, Na, Yu, Zhenyu, Hu, Menglong, Wang, Mingzhu, Lehmann, Ruth, Xu, RuiMing. Structure of Drosophila Oskar reveals a novel RNA binding protein. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2015, 112(37): 11541-11546, http://dx.doi.org/10.1073/pnas.1515568112.
[33] 许瑞明. UHRF2的SRA结构域特异识别羟甲基胞嘧啶的机制. 科学新闻[J]. 2015, 73-73, http://lib.cqvip.com/Qikan/Article/Detail?id=663926389.
[34] Gao, GuanNan, Wang, Mingzhu, Yang, Na, Huang, Ying, Xu, RuiMing. Structure of Zeste-DNA Complex Reveals a New Modality of DNA Recognition by Homeodomain-Like Proteins. JOURNAL OF MOLECULAR BIOLOGY[J]. 2015, 427(24): 3824-3833, http://dx.doi.org/10.1016/j.jmb.2015.10.008.
[35] Cao, Duanfang, Wang, Mingzhu, Qiu, Xiayang, Liu, Dongxiang, Jiang, Hualiang, Yang, Na, Xu, RuiMing. Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol. GENES & DEVELOPMENT[J]. 2015, 29(12): 1316-1325, http://www.corc.org.cn/handle/1471x/2376429.
[36] Yu, Zhouliang, Zhou, Xiang, Wang, Wenjing, Deng, Wenqiang, Fang, Junnan, Hu, Hao, Wang, Zichen, Li, Shangze, Cui, Lei, Shen, Jing, Zhai, Linhui, Peng, Shengyi, Wong, Jiemin, Dong, Shuo, Yuan, Zengqiang, Ou, Guangshuo, Zhang, Xiaodong, Xu, Ping, Lou, Jizhong, Yang, Na, Chen, Ping, Xu, RuiMing, Li, Guohong. Dynamic Phosphorylation of CENP-A at Ser68 Orchestrates Its Cell-Cycle-Dependent Deposition at Centromeres. DEVELOPMENTAL CELL[J]. 2015, 32(1): 68-81, http://dx.doi.org/10.1016/j.devcel.2014.11.030.
[37] 王大成, 秦文明, 李娜, 姚德强, 叶盛, 张荣光, 朱平, 施蕴渝, 施一公. 结构生物学研究在中国. 生物化学与生物物理进展[J]. 2014, 41(10): 944-971, https://d.wanfangdata.com.cn/periodical/swhx201410005.
[38] Yang Na, Xu RuiMing. Structural Basis for Methyl DNA Readout by MBD and SRA Domains. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2014, 41(10): 1063-1074, https://www.webofscience.com/wos/woscc/full-record/WOS:000343688600017.
[39] Yang, N, Zhou, T, Xiong, J, Wang, M, Wong, J, Zhu, B, Xu, R. Structural basis for hydroxymethylcytosine recognition by the SRA domain of UHRF2. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCESnull. 2014, 70: C1827-C1827, https://www.webofscience.com/wos/woscc/full-record/WOS:000519606301829.
[40] Zhou, Ting, Xiong, Jun, Wang, Mingzhu, Yang, Na, Wong, Jiemin, Zhu, Bing, Xu, RuiMing. Structural Basis for Hydroxymethylcytosine Recognition by the SRA Domain of UHRF2. MOLECULAR CELL[J]. 2014, 54(5): 879-886, http://dx.doi.org/10.1016/j.molcel.2014.04.003.
[41] Li, Yang, Zhang, Li, Liu, Tingting, Chai, Chengliang, Fang, Qianglin, Wu, Han, Garcia, Paula A Agudelo, Han, Zhifu, Zong, Shuai, Yu, You, Zhang, Xinyue, Parthun, Mark R, Chai, Jijie, Xu, RuiMing, Yang, Maojun. Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex. GENES & DEVELOPMENT[J]. 2014, 28(11): 1217-1227, http://dx.doi.org/10.1101/gad.240531.114.
[42] Yang Na, Xu RuiMing. Structural Basis for Methyl DNA Readout by MBD and SRA Domains. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS[J]. 2014, 41(10): 1063-1074, https://www.webofscience.com/wos/woscc/full-record/WOS:000343688600017.
[43] Ren, Ren, Liu, Haiping, Wang, Wenjia, Wang, Mingzhu, Yang, Na, Dong, YuHui, Gong, Weimin, Lehmann, Ruth, Xu, RuiMing. Structure and domain organization of Drosophila Tudor. CELL RESEARCH[J]. 2014, 24(9): 1146-1149, https://www.webofscience.com/wos/woscc/full-record/WOS:000344992900015.
[44] Song, Feng, Chen, Ping, Sun, Dapeng, Wang, Mingzhu, Dong, Liping, Liang, Dan, Xu, RuiMing, Zhu, Ping, Li, Guohong. Cryo-EM Study of the Chromatin Fiber Reveals a Double Helix Twisted by Tetranucleosomal Units. SCIENCE[J]. 2014, 344(6182): 376-380, https://www.webofscience.com/wos/woscc/full-record/WOS:000334867800032.
[45] 朱平, 李国红, 许瑞明. 利用冷冻电镜技术解析30nm染色质高级结构. 中国科学基金[J]. 2014, 200-203, http://lib.cqvip.com/Qikan/Article/Detail?id=90757474504849524851484950.
[46] Rui-Ming Xu. Na-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. Nat. Struct. Mol. Biol.. 2013, [47] Yang, Na, Xu, RuiMing. Structure and function of the BAH domain in chromatin biology. CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGYnull. 2013, 48(3): 211-221, https://dx.doi.org/10.3109/10409238.2012.742035.
[48] Wang, Min, Xu, RuiMing, Thompson, Paul R. Substrate Specificity, Processivity, and Kinetic Mechanism of Protein Arginine Methyltransferase 5. BIOCHEMISTRY[J]. 2013, 52(32): 5430-5440, https://www.webofscience.com/wos/woscc/full-record/WOS:000323193700013.
[49] Yang, Dongxue, Fang, Qianglin, Wang, Mingzhu, Ren, Ren, Wang, Hong, He, Meng, Sun, Youwei, Yang, Na, Xu, RuiMing. N alpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2013, 20(9): 1116-+, http://dx.doi.org/10.1038/nsmb.2637.
[50] Hsu, HaoChi, Wang, ChiaLin, Wang, Mingzhu, Yang, Na, Chen, Zhi, Sternglanz, Rolf, Xu, RuiMing. Structural basis for allosteric stimulation of Sir2 activity by Sir4 binding. GENES & DEVELOPMENT[J]. 2013, 27(1): 64-73, http://dx.doi.org/10.1101/gad.208140.112.
[51] Rui-Ming Xu. Distinct mode of methyl-H3K4 recognition by tandem tudor-like domains of Spindlin1. Proc. Natl. Acad. Sci .USA. 2012, [52] Lin, PeiChun, Xu, RuiMing. Structure and assembly of the SF3a splicing factor complex of U2 snRNP. EMBO JOURNAL[J]. 2012, 31(6): 1579-1590, http://www.irgrid.ac.cn/handle/1471x/756948.
[53] 杨福愉. A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2012, 19(4): 403-410, http://www.irgrid.ac.cn/handle/1471x/756694.
[54] Rui-Ming Xu. Crystal structure of TDRD3 and methyl-arginine binding characterizations of TDRD3, SMN and SPF30. 2012, [55] Liu, Ke, Guo, Yahong, Liu, Haiping, Bian, Chuanbing, Lam, Robert, Liu, Yongsong, Mackenzie, Farrell, Rojas, Luis Alejandro, Reinberg, Danny, Bedford, Mark T, Xu, RuiMing, Min, Jinrong. Crystal Structure of TDRD3 and Methyl-Arginine Binding Characterization of TDRD3, SMN and SPF30. PLOS ONE[J]. 2012, 7(2): http://www.irgrid.ac.cn/handle/1471x/756755.
[56] Liu, ChaoPei, Xiong, Chaoyang, Wang, Mingzhu, Yu, Zhouliang, Yang, Na, Chen, Ping, Zhang, Zhiguo, Li, Guohong, Xu, RuiMing. Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX. NATURE STRUCTURAL & MOLECULAR BIOLOGY[J]. 2012, 19(12): 1287-+, http://dx.doi.org/10.1038/nsmb.2439.
[57] Yang, Na, Wang, Weixiang, Wang, Yan, Wang, Mingzhu, Zhao, Qiang, Rao, Zihe, Zhu, Bing, Xu, RuiMing. Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2012, 109(44): 17954-17959, http://dx.doi.org/10.1073/pnas.1208517109.
[58] Su, Dan, Hu, Qi, Zhou, Hui, Thompson, James R, Xu, RuiMing, Zhang, Zhiguo, Mer, Georges. Structure and Histone Binding Properties of the Vps75-Rtt109 Chaperone-Lysine Acetyltransferase Complex. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2011, 286(18): 15625-15629, http://dx.doi.org/10.1074/jbc.C111.220715.
[59] Sun, Litao, Wang, Mingzhu, Lv, Zongyang, Yang, Na, Liu, Yingfang, Bao, Shilai, Gong, Weimin, Xu, RuiMing. Structural insights into protein arginine symmetric dimethylation by PRMT5. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA[J]. 2011, 108(51): 20538-20543, http://dx.doi.org/10.1073/pnas.1106946108.
[60] Hu, Hao, Liu, Yang, Wang, Mingzhu, Fang, Junnan, Huang, Hongda, Yang, Na, Li, Yanbo, Wang, Jianyu, Yao, Xuebiao, Shi, Yunyu, Li, Guohong, Xu, RuiMing. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. GENES & DEVELOPMENT[J]. 2011, 25(9): 901-906, http://www.irgrid.ac.cn/handle/1471x/757447.
[61] Xu, RuiMing. Structural Studies of Histone Methylation. FASEB JOURNALnull. 2011, 25: https://www.webofscience.com/wos/woscc/full-record/WOS:000310708402360.
[62] Qiao, Qi, Li, Yan, Chen, Zhi, Wang, Mingzhu, Reinberg, Danny, Xu, RuiMing. The Structure of NSD1 Reveals an Autoregulatory Mechanism Underlying Histone H3K36 Methylation. JOURNAL OF BIOLOGICAL CHEMISTRY[J]. 2011, 286(10): 8361-8368, http://dx.doi.org/10.1074/jbc.M110.204115.
[63] Yang, Na, Hu, Hao, Xu, RuiMing. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCESnull. 2011, 67: C50-C51, https://www.webofscience.com/wos/woscc/full-record/WOS:000484219400117.
[64] Wang, Weixiang, Chen, Zhi, Mao, Zhuo, Zhang, Huihui, Ding, Xiaojun, Chen, She, Zhang, Xiaodong, Xu, Ruiming, Zhu, Bing. Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes. EMBO REPORTS[J]. 2011, 12(11): 1160-1166, http://dx.doi.org/10.1038/embor.2011.184.
[65] Liu, Haiping, Wang, JuYu S, Huang, Ying, Li, Zhizhong, Gong, Weimin, Lehmann, Ruth, Xu, RuiMing. Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. GENES & DEVELOPMENT[J]. 2010, 24(17): 1876-1881, http://dx.doi.org/10.1101/gad.1956010.
[66] Sun, Ming, Xu, RuiMing. Protein science research in China. PROTEIN & CELL[J]. 2010, 1(1): 4-5, https://www.webofscience.com/wos/woscc/full-record/WOS:000208510300003.
[67] XU RuiMing. Editoral: Molecular epigenetics: dawn of a new era of biomedical research. SCIENCE IN CHINA. SERIES C: LIFE SCIENCE[J]. 2009, 52(4): 309-310, http://sciencechina.cn/gw.jsp?action=detail.jsp&internal_id=3590945&detailType=1.
[68] Xu RuiMing. Molecular epigenetics: dawn of a new era of biomedical research. SCIENCE IN CHINA SERIES C-LIFE SCIENCES. 2009, 52(4): 309-310, http://www.irgrid.ac.cn/handle/1471x/757971.
[69] Huang, Y, Fang, J, Bedford, MT, Zhang, Y, Xu, RM. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. SCIENCE[J]. 2006, 312(5774): 748-751, https://www.webofscience.com/wos/woscc/full-record/WOS:000237312100051.
[70] Rui-Ming Xu. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at lysine 27. Genes and Development. 2003, [71] Min, JR, Feng, Q, Li, ZZ, Zhang, Y, Xu, RM. Structure of the catalytic domain of human DOT1L, a Non-SET domain nucleosomal histone methyltransferase. CELL[J]. 2003, 112(5): 711-723, http://dx.doi.org/10.1016/S0092-8674(03)00114-4.
[72] Min, JR, Landry, J, Sternglanz, R, Xu, RM. Crystal structure of a SIR2 homolog-NAD complex. CELL[J]. 2001, 105(2): 269-279, http://dx.doi.org/10.1016/S0092-8674(01)00317-8.
[73] Qianglin Fang, Ping Chen, Mingzhu Wang, Junnan Fang, Na Yang, Guohong Li, RuiMing Xu. Correction: Human cytomegalovirus IE1 alters the higher-order chromatin structure by targeting the acidic patch of the nucleosome. ELIFE[J]. 5: https://doaj.org/article/5178f46736754da39f94c8b11e21651e.

   

（ 1 ） 核小体与蛋白质相互作用的结构机理研究, 主持, 国家级, 2015-01--2019-12
（ 2 ） 染色质结构及其调控, 主持, 国家级, 2016-01--2021-12
（ 3 ） 组蛋白伴侣HIRA特异识别组蛋白变体H3.3-H4的结构研究, 主持, 国家级, 2016-01--2016-12
（ 4 ） PRMT5靶点确认及其候选化合物的结构功能机制研究, 主持, 国家级, 2014-01--2016-12

（1）Alteration of chromatin folding by the binding of a viral protein to the nucleosome   2016-05-09
（2）Structural characterizations of snRNP assembly   国际剪接体学术研讨大会   2016-04-21
（3）Structural Studies of Histone Chaperones and Nucleosome Assembly Factors   2015-06-07
（4）Chromatin structure and dynamics   2014-12-27
（5）Structural basis for stimulation of SIRT1 activity by resveratrol   2014-05-08
（6）Structural Basis for Chaperone-histone Interactions   第八届亚太表观遗传年会   2013-11-08

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