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杨娜 教授 Na Yang
Special Talent:
Address: Room D326, Integrated Laboratories D, Jinnan Campus, Nankai University
Telephone: 022-85358193
Email: yangnaNKU@nankai.edu.cn
Research Group Website: http://pharmacy.nankai.edu.cn/info/1011/1280.htm, https://pharmacy-en.nankai.edu.cn/info/1019/1033.htm (English)

Doctor degree, professor, State laboratory of Chemical Medical Biology, graduated from Peking University

National Science Found for Excellent Young Scholars, Distinguished Young Scholars of Tianjin City



Research Interest

Dr. Yang has been carrying out studies of structural basis of epigenetics, including histone modifications and DNA methylation, as well as RNA-protein interactions. The main research interest of Dr. Yang’s group is on drug target validation of epigenetic factors closely related to human diseases, such as malignant tumor. The lab principally uses structure-based approaches, by solving the three-dimensional structures of these epigenetic factors, to reveal the relationship between their structures and functions. Followed by virtual screening and rational drug design based on these structures. Finally candidate compounds will be evaluated and optimized by iterative Structure-Activity Relationship (SAR) analyses.

Education History

1996-2000School of Life Sciences, Peking UniversityBachelor of Biology

2000-2005Institute of Biophysics, Chinese Academy of SciencesDoctor of Biology

Honors and Awards

2019   15th Science and Technology Award for Youth, Tianjin

2018   Science and Technology Award of Beijing Municipality, Second prize

2017   Distinguished Young Scholars of Tianjin City

2016   National Science Found for Excellent Young Scholars

2015   Excellent Member of the Youth Innovation Promotion Association of CAS

2011   Lu Jiaxi Young Talent Award of Chinese Academy of Sciences, CAS

Scientific Achievements & Selected Publications

Liu, F.#, Pang, N.N.#, Xu, R.M. and Yang, N.* (2023) Mechanism and design of allosteric activators of SIRT1. Protein & Cell, Vol. 14, 387-392.

Sun, J.X., Liu, F., Yuan, L.X., Pang, N.N., Zhu, B. and Yang, N.* (2023) Mechanism studies of the activation of DNA methyltransferase DNMT1 triggered by histone H3 ubiquitination, revealed by multi-scale molecular dynamics simulations. Science China Life Sciences, Vol. 66(2), 313-323.

Liu, C.P.#, Yu, Z.#, Xiong, J.#, Hu, J.#, Song, A.#, Ding, D., Yu, C., Yang, N., Wang, M., Yu, J., Hou, P., Zeng, K., Li, Z., Zhang, Z., Zhang, X., Li, W., Zhang, Z., Zhu, B.*, Li, G.*, Xu, R.M.* (2023) Structural insights into histone binding and nucleosome assembly by chromatin assembly factor-1. Science, Vol. 381, eadd8673.

Pang, N.N.#, Sun, J.X.#, Che, S.Y., and Yang, N.* (2022) Structural study of fungus-specific histone deacetylase Hos3 and insight into developing selective inhibitors with antifungal activity. Journal of Biological Chemistry, Vol. 298, 102068.

Ma, S.#, Zhang, J.Y.#, Guo, Q.S., Cao, C., Bao, K.W., Liu, L., Chen, D.G., Liu, Z., Yang, J., Yang, N.*, Yao, Z.* and Shi, L.* (2022) Disrupting PHF8-TOPBP1 connection elicits a breast tumor-specific vulnerability to chemotherapeutics. Cancer Letters, Vol. 530, 29-44.

Ma, S.#, Cao, C.#, Che, S.Y.#, Wang, Y.J.#, Su, D.X.#, et al., Yao, Z.*, Yang, N.* and Shi, L.* (2021) PHF8-promoted TOPBP1 demethylation drives ATR activation and preserves genome stability. Science Advances, Vol. 7, eabf7684.

Xu, X.#, Wang, M.Z.#, Sun, J.X.#, Yu, Z.Y.#, Li, G.H., Yang, N.* and Xu, R.M.* (2021) Structure specific DNA recognition by the SLX1-SLX4 endonuclease complex. Nucleic Acid Research, Vol. 49, 7740-7752.

Sun, J.X.#, Li, Z.B#. and Yang, N.* (2021) Mechanism of the conformational change of the protein methyltransferase SMYD3: a molecular dynamics simulation study. International Journal of Molecular Sciences, Vol. 22, 7185 (1-21).

Liu, F. and Yang, N.* (2020) Multiscale landscape of molecular mechanism of SIRT1 activation by STACs. Physical Chemistry Chemical Physics, Vol. 22, 826-837.

Song, X.S.#, Yang, L.L.#, Wang, M.Z., Gu, Y., Ye, B.Q., Fan, Z.S., Xu, R.M.* and Yang, N.* (2019) A higher-order configuration of the heterodimeric DOT1L-AF10 coiled-coil domains potentiates their leukemogenenic activity. Proc. Natl. Acad. Sci. USA, Vol. 116, 19917-19923.

Sun, J.X., Shi, F.D. and Yang, N.* (2019) Exploration of the substrate preference of lysine methyltransferase SMYD3 by molecular dynamics simulations. ACS Omega, Vol. 4, 19573-19581.

Li, Y.#, Duan, F.F.#, Zhao, Y.T., Gu, K.L., Liao, L.Q., Su, H.B., Hao, J., Zhang, K., Yang, N. and Wang Y.M.* (2019) A TRIM71 binding long noncoding RNA Trincr1 represses FGF/ERK signaling in embryonic stem cells. Nature Communications, Vol. 10, 1368.

Zhang, L.#, Serra-Cardona, A.#, Zhou, H., Wang, N., Yang, N., Zhang, Z.* and Xu, R.M.* (2018) Multisite substrate recognition in Asf1-dependent acetylation of histone H3 K56 by Rtt109. Cell, Vol. 174, 818-830.

Fu, W.Q.#, Liu, N.#, Qiao, Q.#, Wang, M., Min, J.R., Zhu, B.*, Xu, R.M.* and Yang, N.* (2016) Structural Basis for Substrate Preference of SMYD3, A SET Domain-containing Protein Lysine Methyltransferase. Journal of Biological Chemistry, Vol. 291, 9173-9180.

Fang, D.#, Gan, H.#, Lee, J.H.#, Han, J.#, Wang, Z.#, Riester, S.M., Jin, L., Chen, J., Zhou, H., Wang, J., Zhang, H., Yang, N., Bradley, E.W., Ho, T.H., Rubin, B.P., Bridge, J.A., Thibodeau, S.N., Ordog, T., Chen, Y., van Wijnen, A.J., Oliveira, A.M., Xu, R.M., Westendorf, J.J. and Zhang, Z.* (2016) The histone H3.3K36M mutation reprograms the epigenome of chondroblastomas. Science, Vol. 29, 1316-1325.

Yang, N.#*, Yu, Z.Y.#, Hu, M.L.#, Wang, M., Lehmann, R.* and Xu, R.M.* (2015) Structure of Drosophila Oskar reveals a novel RNA binding protein. Proc. Natl. Acad. Sci. USA, Vol. 112, 11541-11546.

Cao, D.F., Wang, M., Qiu, X.Y., Liu, D.X., Jiang, H.L., Yang, N.* and Xu, R.M.* (2015) Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol. Genes & Development, Vol. 29, 1316-1325.

Wang, H., Wang, M., Yang, N.* and Xu, R.M.* (2015) Structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2. Protein & Cell, Vol. 6, 693-697.

Yang, D.X.#, Fang, Q.L.#, Wang, M.#, Ren, R., Wang, H., He, M., Sun, Y.W., Yang, N.* and Xu, R.M.* (2013) Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. Nature Structural & Molecular Biology, Vol. 20, 1116-1118.

Yang, N.#*, Wang, W.#, Wang, Y. #, Wang, M., Zhao, Q., Rao, Z., Zhu, B.* and Xu, R.M.* (2012) Distinct mode of methyl-H3K4 recognition by tandem tudor-like domains of Spindlin1. Proc. Natl. Acad. Sci. USA, Vol. 109, 17954-17959.