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Li, Z., Lu, W., Beyett, T. S., Ficarro, S. B., Jiang, J., Tse, J., Kim, A. Yong- Ju, Marto, J. A., Che, J., Jänne, P. A., Eck, M. J., Zhang, T., and Gray, N. S. (2024) ZNL0325, a Pyrazolopyrimidine-Based Covalent Probe, Demonstrates an Alternative Binding Mode for Kinases. J Med Chem. 67, 2837-2848
Li, W., Schulman, S., Dutton, R. J., Boyd, D., Beckwith, J., and Rapoport, T. A. (2010) Structure of a bacterial homologue of vitamin K epoxide reductase. Nature. 463, 507-12
Li, X., Zhang, R., Draheim, K. M., Liu, W., Calderwood, D. A., and Boggon, T. J. (2012) Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1). J Biol Chem. 287, 22317-27
Li, Y. L., Zee, C. - T., Lin, J. B., Basile, V. M., Muni, M., Flores, M. D., Munárriz, J., Kaner, R. B., Alexandrova, A. N., Houk, K. N., Tolbert, S. H., and Rubin, Y. (2020) Fjord-Edge Graphene Nanoribbons with Site-Specific Nitrogen Substitution. J Am Chem Soc. 142, 18093-18102
Li, J., Bandekar, S. J., and Araç, D. (2023) The structure of fly Teneurin-m reveals an asymmetric self-assembly that allows expansion into zippers. EMBO Rep. 10.15252/embr.202256728
Li, H., Hwang, Y., Perry, K., Bushman, F., and Van Duyne, G. D. (2016) Structure and Metal Binding Properties of a Poxvirus Resolvase. J Biol Chem. 291, 11094-104
Li, J., Ma, X., Banerjee, S., Baruah, S., Schnicker, N. J., Roh, E., Ma, W., Liu, K., Bode, A. M., and Dong, Z. (2020) Structural basis for multifunctional roles of human Ints3 C-terminal domain. J Biol Chem. 10.1074/jbc.RA120.016393
Li, H., Pink, M. D., Murphy, J. G., Stein, A., Dell'Acqua, M. L., and Hogan, P. G. (2012) Balanced interactions of calcineurin with AKAP79 regulate Ca2+-calcineurin-NFAT signaling. Nat Struct Mol Biol. 19, 337-45
Li, J., Ma, X., Banerjee, S., Chen, H., Ma, W., Bode, A. M., and Dong, Z. (2021) Crystal structure of the human PRPK-TPRKB complex. Commun Biol. 4, 167
Li, Z., Wang, S., Nattermann, U., Bera, A. K., Borst, A. J., Yaman, M. Y., Bick, M. J., Yang, E. C., Sheffler, W., Lee, B., Seifert, S., Hura, G. L., Nguyen, H., Kang, A., Dalal, R., Lubner, J. M., Hsia, Y., Haddox, H., Courbet, A., Dowling, Q., Miranda, M., Favor, A., Etemadi, A., Edman, N. I., Yang, W., Weidle, C., Sankaran, B., Negahdari, B., Ross, M. B., Ginger, D. S., and Baker, D. (2023) Accurate computational design of three-dimensional protein crystals. Nat Mater. 10.1038/s41563-023-01683-1
Li, K., Zheng, J., Wirawan, M., Trinh, N. Mai, Fedorova, O., Griffin, P. R., Pyle, A. M., and Luo, D. (2021) Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3). Nucleic Acids Res. 49, 9978-9991
Li, R., Chou, W. K. W., Himmelberger, J. A., Litwin, K. M., Harris, G. G., Cane, D. E., and Christianson, D. W. (2014) Reprogramming the chemodiversity of terpenoid cyclization by remolding the active site contour of epi-isozizaene synthase. Biochemistry. 53, 1155-68
Li, H., Fischle, W., Wang, W., Duncan, E. M., Liang, L., Murakami-Ishibe, S., C Allis, D., and Patel, D. J. (2007) Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger. Mol Cell. 28, 677-91
Li, Y., Zhao, Y., Su, M., Glover, K., Chakravarthy, S., Colbert, C. L., Levine, B., and Sinha, S. C. (2017) Structural insights into the interaction of the conserved mammalian proteins GAPR-1 and Beclin 1, a key autophagy protein. Acta Crystallogr D Struct Biol. 73, 775-792
Lewicka, A., Roman, C., Jones, S., Disare, M., Rice, P. A., and Piccirilli, J. A. (2023) Crystal structure of a cap-independent translation enhancer RNA. Nucleic Acids Res. 10.1093/nar/gkad649
Levsh, O., Chiang, Y. - C., Tung, C. Fai, Noel, J. P., Wang, Y., and Weng, J. - K. (2016) Dynamic Conformational States Dictate Selectivity toward the Native Substrate in a Substrate-Permissive Acyltransferase. Biochemistry. 55, 6314-6326
Levin, E. J., Quick, M., and Zhou, M. (2009) Crystal structure of a bacterial homologue of the kidney urea transporter. Nature. 462, 757-61
Levin, E. J., Cao, Y., Enkavi, G., Quick, M., Pan, Y., Tajkhorshid, E., and Zhou, M. (2012) Structure and permeation mechanism of a mammalian urea transporter. Proc Natl Acad Sci U S A. 109, 11194-9
Levin, E. J., Kondrashov, D. A., Wesenberg, G. E., and Phillips, G. N. (2007) Ensemble refinement of protein crystal structures: validation and application. Structure. 15, 1040-52
Levenson-Palmer, R., Luciano, D. J., Vasilyev, N., Nuthanakanti, A., Serganov, A., and Belasco, J. G. (2022) A distinct RNA recognition mechanism governs Np decapping by RppH. Proc Natl Acad Sci U S A. 10.1073/pnas.2117318119
Levchenko, I., Grant, R. A., Flynn, J. M., Sauer, R. T., and Baker, T. A. (2005) Versatile modes of peptide recognition by the AAA+ adaptor protein SspB. Nat Struct Mol Biol. 12, 520-5
Leung, J. H., Schurig-Briccio, L. A., Yamaguchi, M., Moeller, A., Speir, J. A., Gennis, R. B., and Stout, C. D. (2015) Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer. Science. 347, 178-81
Leroy, E., Dusa, A., Colau, D., Motamedi, A., Cahu, X., Mouton, C., Huang, L. J., Shiau, A. K., and Constantinescu, S. N. (2016) Uncoupling JAK2 V617F activation from cytokine-induced signalling by modulation of JH2 αC helix.. Biochem J. 473, 1579-91
Lepore, R., Kryshtafovych, A., Alahuhta, M., Veraszto, H. A., Bomble, Y. J., Bufton, J. C., Bullock, A. N., Caba, C., Cao, H., Davies, O. R., Desfosses, A., Dunne, M., Fidelis, K., Goulding, C. W., Gurusaran, M., Gutsche, I., Harding, C. J., Hartmann, M. D., Hayes, C. S., Joachimiak, A., Leiman, P. G., Loppnau, P., Lovering, A. L., Lunin, V. V., Michalska, K., Mir-Sanchis, I., Mitra, A. K., Moult, J., Phillips, G. N., Pinkas, D. M., Rice, P. A., Tong, Y., Topf, M., Walton, J. D., and Schwede, T. (2019) Target highlights in CASP13: Experimental target structures through the eyes of their authors. Proteins. 87, 1037-1057
LeNoue-Newton, M., Watkins, G. R., Zou, P., Germane, K. L., McCorvey, L. R., Wadzinski, B. E., and Spiller, B. W. (2011) The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains of the Alpha4 protein are both required for Alpha4 to inhibit PP2A degradation. J Biol Chem. 286, 17665-71

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