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Wang, L., Ferrao, R., Li, Q., Hatcher, J. M., Choi, H. Geun, Buhrlage, S. J., Gray, N. S., and Wu, H. (2019) Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4). J Biol Chem. 10.1074/jbc.RA118.005428
Blankenship, E., Vukoti, K., Miyagi, M., and Lodowski, D. T. (2014) Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state. Acta Crystallogr D Biol Crystallogr. 70, 833-40
Lin, D. Yin-wei, Kueffer, L. E., Juneja, P., and Wales, T. E. (2024) Conformational heterogeneity of the BTK PHTH domain drives multiple regulatory states. Elife. 10.7554/eLife.89489
Zubcevic, L., Le, S., Yang, H., and Lee, S. - Y. (2018) Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat Struct Mol Biol. 25, 405-415
Zubcevic, L., Le, S., Yang, H., and Lee, S. - Y. (2018) Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat Struct Mol Biol. 25, 405-415
Todd, R. C., and Lippard, S. J. (2010) Consequences of cisplatin binding on nucleosome structure and dynamics. Chem Biol. 17, 1334-43
Ostrander, E. L., Larson, J. D., Schuermann, J. P., and Tanner, J. J. (2009) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry. 48, 951-9
West, A. Mv, Rosenberg, S. C., Ur, S. N., Lehmer, M. K., Ye, Q., Hagemann, G., Caballero, I., Usón, I., MacQueen, A. J., Herzog, F., and Corbett, K. D. (2019) A conserved filamentous assembly underlies the structure of the meiotic chromosome axis. Elife. 10.7554/eLife.40372
Lau, R. K., Enustun, E., Gu, Y., Nguyen, J. V., and Corbett, K. D. (2022) A conserved signaling pathway activates bacterial CBASS immune signaling in response to DNA damage. EMBO J. 10.15252/embj.2022111540
Bryson, D. I., Fan, C., Guo, L. - T., Miller, C., Söll, D., and Liu, D. R. (2017) Continuous directed evolution of aminoacyl-tRNA synthetases. Nat Chem Biol. 13, 1253-1260
Li, X., Lee, H., Wu, J., and Breslow, E. (2007) Contributions of the interdomain loop, amino terminus, and subunit interface to the ligand-facilitated dimerization of neurophysin: crystal structures and mutation studies of bovine neurophysin-I. Protein Sci. 16, 52-68
Li, X., Lee, H., Wu, J., and Breslow, E. (2007) Contributions of the interdomain loop, amino terminus, and subunit interface to the ligand-facilitated dimerization of neurophysin: crystal structures and mutation studies of bovine neurophysin-I. Protein Sci. 16, 52-68
Blankenchip, C. L., Nguyen, J. V., Lau, R. K., Ye, Q., Gu, Y., and Corbett, K. D. (2022) Control of bacterial immune signaling by a WYL domain transcription factor. Nucleic Acids Res. 50, 5239-5250
Smith, M. A., Majer, S. H., Vilbert, A. C., and Lancaster, K. M. (2019) Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460. Chem Sci. 10, 3756-3764
Sasaki, E., Zhang, X., Sun, H. G., Lu, M. -yehJade, Liu, T. -lin, Ou, A., Li, J. -yi, Chen, Y. -hsiang, Ealick, S. E., and Liu, H. -wen (2014) Co-opting sulphur-carrier proteins from primary metabolic pathways for 2-thiosugar biosynthesis. Nature. 510, 427-31
Sasaki, E., Zhang, X., Sun, H. G., Lu, M. -yehJade, Liu, T. -lin, Ou, A., Li, J. -yi, Chen, Y. -hsiang, Ealick, S. E., and Liu, H. -wen (2014) Co-opting sulphur-carrier proteins from primary metabolic pathways for 2-thiosugar biosynthesis. Nature. 510, 427-31
Sasaki, E., Zhang, X., Sun, H. G., Lu, M. -yehJade, Liu, T. -lin, Ou, A., Li, J. -yi, Chen, Y. -hsiang, Ealick, S. E., and Liu, H. -wen (2014) Co-opting sulphur-carrier proteins from primary metabolic pathways for 2-thiosugar biosynthesis. Nature. 510, 427-31
Sasaki, E., Zhang, X., Sun, H. G., Lu, M. -yehJade, Liu, T. -lin, Ou, A., Li, J. -yi, Chen, Y. -hsiang, Ealick, S. E., and Liu, H. -wen (2014) Co-opting sulphur-carrier proteins from primary metabolic pathways for 2-thiosugar biosynthesis. Nature. 510, 427-31
Chan, A. H., Lee, W. - G., Spasov, K. A., Cisneros, J. A., Kudalkar, S. N., Petrova, Z. O., Buckingham, A. B., Anderson, K. S., and Jorgensen, W. L. (2017) Covalent inhibitors for eradication of drug-resistant HIV-1 reverse transcriptase: From design to protein crystallography. Proc Natl Acad Sci U S A. 10.1073/pnas.1711463114
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Liu, Y., Pan, J., Jenni, S., Raymond, D. D., Caradonna, T., Do, K. T., Schmidt, A. G., Harrison, S. C., and Grigorieff, N. (2017) CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface. J Mol Biol. 429, 1829-1839
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250
Lu, J., Cao, Q., Hughes, M. P., Sawaya, M. R., Boyer, D. R., Cascio, D., and Eisenberg, D. S. (2020) CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Nat Commun. 11, 4090

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