Publications (* corresponding author)
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Li, N., Gao, Y., Zhang, Y., Yu, D., Lin, W., Feng, J., Li, J., Xu, Z., Zhang, Y., Dang, S., Liu, Y., Zhou, K., Tye, B.*, Li, Q.*, Gao, N.*, Zhai, Y.* (2024) Parental histone transfer caught at the replication fork. Nature 627, 890-897 https://doi.org/10.1038/s41586-024-07152-2
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Luo, J., Lam, W.*, Yu, D., Chao, V., Zopfi, M., Khoo, C., Liu, Z., Li, X.D., Zheng, C., Zhai, Y.*, Ti, S.* (2024) Tubulin acetyltransferases access and modify the microtubule luminal K40 residue via anchors in taxine-binding pockets. Nature Structural & Molecular Biology https://doi.org/10.1038/s41594-024-01406-3
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Wu, Y., Zhang, Q., Lin, Y., Lam, W., Zhai, Y.* (2024) Replication licensing regulated by a short linear motif within an intrinsically disordered region of origin recognition complex. Nature Communications 15:8039 https://doi.org/10.1038/s41467-024-52408-0
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Ding D., Pang, M., Deng, M., Nguyen, T., Sun, X., Xu, Z., Zhang, Y., Zhai, Y., Yan Y., & Ishibashi, T. (2024) Testis-specific H2BFWT disrupts nucleosome integrity through reductions of DNA-histone interactions. Nucleic Acids Research 1-14 https://doi.org/10.1093/nar/gkae825​​
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Zhang, Q., Lam, W., Zhai, Y.* (2024) Assembly and activation of replicative helicases at origin DNA for replication initiation. Current Opinion in Structural Biology 88:102876
https://doi.org/10.1016/j.sbi.2024.102876
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Tye, B. & Zhai, Y. (2024) The Origin Recognition Complex: From Origin Selection to Replication Licensing in Yeast and Humans. Biology, 13(1), 13 https://doi.org/10.3390/biology13010013
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Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W., Liu, Z., Jing, Y., Dang, S., Bao, X.*, Wong J.*, Zhai, Y.*, & Li X.*(2023) Menin 'reads' H3K79me2 mark in a nucleosomal context. Science 379, 717-72 https://doi.org/10.1126/science.adc9318
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Li, J., Dong, J., Wang, W., Yu, D., Fan, X., Hui, Y., Lee, C., Lam, H., Alary, N., Yang, Y., Zhang, Y., Zhao, Q., Chen, C.*, Tye, B.*, Dang, S.*, & Zhai, Y.* (2023) The Human Pre-replication Complex is an Open Complex. Cell 186, 98-111 https://doi.org/10.1016/j.cell.2022.12.008
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Li, N., Gao, N.*, & Zhai, Y.* (2023) DDK promotes DNA replication initiation: mechanistic and structural insights. Current Opinion in Structural Biology 78, 102504
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Cheng, J., Li, N., Huo, Y., Dang, S., Tye, B.*, Gao, N.*, and Zhai, Y.* (2022) Structural Insight into the MCM double hexamer activation by Dbf4-Cdc7 kinase. Nature Communications 13:1396
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Ding D., Pang, M., Deng, M., Nguyen, T., Sun, X., Xu, Z., Zhang, Y., Zhai, Y., Yan Y., & Ishibashi, T. (2022) Testis-specific H2BFWT disrupts nucleosome integrity through reductions of DNA-histone interactions. bioRxiv https://doi.org/10.1101/2022.07.20.500751
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Lee, S., Cheung, M., Li, J., Zhao, Y., Lam, W., Ho, V., Rohs, R., Zhai, Y.*, Leung, D. *, Tye, B.* (2021) Humanizing the Yeast Origin Recognition Complex. Nature Communications12, 33
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Deng, L., Chen, C.-L., Zhai, Y., Dong, Y. & Lou, H. (2021) DNA Replication Stress and Cell Fate. Frontiers in Cell and Developmental Biology 9, https://doi.org/10.3389/fcell.2021.778486
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Cheng, J., Li, N., Wang, X., Hu, J., Zhai, Y., and Gao, N. (2020) Structural insight into the assembly and conformational activation of autoinhibited human origin recognition complex. Cell Discovery 6, 88
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Li, N.*, Lam, W.*, Zhai, Y.*#, Cheng, J.*, Cheng, E., Zhao, Y., Gao, N.# & Tye, B.# (2018) Structure of the origin recognition complex bound to DNA replication origin. Nature 559, 217-222, *Co-first authors # co-corresponding authors ​https://www.nature.com/articles/s41586-018-0293-x
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Zhai, Y., and Tye, B. (2017) Structure of the MCM2-7 Double Hexamer and Its Implications for the Mechanistic Functions of the Mcm2-7 Complex. in “DNA replication: From Old Principles to New Discovery” Advances in Experimental Medicine and Biology. Springer publisher.
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Zhao, T., Wang, Y., Zhai, Y., Qu, X., Ai, F., Du, S., and Loy, M. (2015) A user-friendly two-color super-resolution localization microscope. Optics Express 23, 1879-187
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Li, N.*, Zhai, Y.*#, Zhang, Y., Li, W., Yang, M., Lei, J., Tye, B.#, and Gao, N.# (2015) Structure of the Eukaryotic Minichromosome Maintenance Complex at 3.8 Å. Nature 524, 186–191 *Co-first # co-corresponding authors (highlighted in Nature News & Views) https://www.nature.com/articles/nature14685