代表性论文
1. Long, T. #, Li, D. #, Vale, G., Jiang, Y., Schmiege, P., Yang, Z., McDonald, J., Li, X. (2024) Molecular insights into human phosphatidylserine synthase 1 reveal its inhibition promotes LDL uptake. Cell, in press. (#co-first author)
2. Long, T. #, Zhang, Y. #, Donnelly, L., Li, H., Pien, Y.C., Liu, N., Olson, E.N. and Li, X. (2023) Cryo-EM structures of Myomaker reveal a molecular basis for myoblast fusion. Nat Struct Mol Biol, 30, 1746-1754. (#co-first author)
3. Long, T.*, Debler, E.W. and Li, X. * (2022) Structural enzymology of cholesterol biosynthesis and storage. Curr Opin Struct Biol, 74, 102369. (*corresponding author)
4. Long, T., Liu, Y., Li, X. (2021) Molecular structures of human ACAT2 disclose mechanism for selective inhibition. Structure, 29, 1410-1418.e1414.
5. Long, T. #, Liu, Y. #, Qin, Y., DeBose-Boyd, R.A. and Li, X. (2021) Structures of dimeric human NPC1L1 provide insight into mechanisms for cholesterol absorption. Sci Adv, 7. (#co-first author)
6. Sun, Y. #, Wang, J.#*, Long, T. #, Qi, X. #, Donnelly, L., Elghobashi-Meinhardt, N., Esparza, L., Cohen, J.C., Xie, X.S., Hobbs, H.H. et al. (2021) Molecular basis of cholesterol efflux via ABCG subfamily transporters. Proc. Natl. Acad. Sci. U. S. A., 118. (#co-first author)
7. Long, T. #, Sun, Y.#, Hassan, A., Qi, X. and Li, X. (2020) Structure of nevanimibe-bound tetrameric human ACAT1. Nature, 581, 339-343. (#co-first author)
8. Liu, R.J. #, Long, T. #, Li, H., Zhao, J., Li, J., Wang, M., Palencia, A., Lin, J., Cusack, S. and Wang, E.D. (2020) Molecular basis of the multifaceted functions of human leucyl-tRNA synthetase in protein synthesis and beyond. Nucleic Acids Res, 48, 4946-4959. (#co-first author)
9. Long, T., Qi, X., Hassan, A., Liang, Q., De Brabander, J.K. and Li, X. (2020) Structural basis for itraconazole-mediated NPC1 inhibition. Nat Commun, 11, 152.
10. Long, T., Hassan, A., Thompson, B.M., McDonald, J.G., Wang, J. and Li, X. (2019) Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition. Nat Commun, 10, 2452.