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Heppner, D. E., Wittlinger, F., Beyett, T. S., Shaurova, T., Urul, D. A., Buckley, B., Pham, C. D., Schaeffner, I. K., Yang, B., Ogboo, B. C., May, E. W., Schaefer, E. M., Eck, M. J., Laufer, S. A., and Hershberger, P. A. (2022) Structural Basis for Inhibition of Mutant EGFR with Lazertinib (YH25448). ACS Med Chem Lett. 13, 1856-1863
Lyu, J., Liu, C., Zhang, T., Schrecke, S., Elam, N. P., Packianathan, C., Hochberg, G. K. A., Russell, D., Zhao, M., and Laganowsky, A. (2022) Structural basis for lipid and copper regulation of the ABC transporter MsbA. Nat Commun. 13, 7291
Krochmal, D., Shao, Y., Li, N. - S., DasGupta, S., Shelke, S. A., Koirala, D., and Piccirilli, J. A. (2022) Structural basis for substrate binding and catalysis by a self-alkylating ribozyme. Nat Chem Biol. 10.1038/s41589-021-00950-z
Syroegin, E. A., Flemmich, L., Klepacki, D., Vázquez-Laslop, N., Micura, R., and Polikanov, Y. S. (2022) Structural basis for the context-specific action of the classic peptidyl transferase inhibitor chloramphenicol. Nat Struct Mol Biol. 29, 152-161
Syroegin, E. A., Aleksandrova, E. V., and Polikanov, Y. S. (2022) Structural basis for the inability of chloramphenicol to inhibit peptide bond formation in the presence of A-site glycine. Nucleic Acids Res. 50, 7669-7679
Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Velilla, J. A., Volpe, M. R., Kenney, G. E., Walsh, R. M., Balskus, E. P., and Gaudet, R. (2022) Structural basis of colibactin activation by the ClbP peptidase. Nat Chem Biol. 10.1038/s41589-022-01142-z
Zhou, W., Richmond-Buccola, D., Wang, Q., and Kranzusch, P. J. (2022) Structural basis of human TREX1 DNA degradation and autoimmune disease. Nat Commun. 13, 4277
Kumar, S., Zavaliev, R., Wu, Q., Zhou, Y., Cheng, J., Dillard, L., Powers, J., Withers, J., Zhao, J., Guan, Z., Borgnia, M. J., Bartesaghi, A., Dong, X., and Zhou, P. (2022) Structural basis of NPR1 in activating plant immunity. Nature. 605, 561-566
Eaton, S. A., Ronnebaum, T. A., Roose, B. W., and Christianson, D. W. (2022) Structural Basis of Substrate Promiscuity and Catalysis by the Reverse Prenyltransferase -Dimethylallyl-l-tryptophan Synthase from . Biochemistry. 10.1021/acs.biochem.2c00350
Luo, M., Zhou, B., Reddem, E. R., Tang, B., Chen, B., Zhou, R., Liu, H., Liu, L., Katsamba, P. S., Au, K. - K., Man, H. - O., To, K. Kai- Wang, Yuen, K. - Y., Shapiro, L., Dang, S., Ho, D. D., and Chen, Z. (2022) Structural insights into broadly neutralizing antibodies against SARS-CoV-2 elicited by hybrid immunity. Emerg Microbes Infect. 10.1080/22221751.2022.2146538
Joseph, D., Nayak, S. Ranjan, and Penmatsa, A. (2022) Structural insights into GABA transport inhibition using an engineered neurotransmitter transporter. EMBO J. 41, e110735
Frey, K. M., Bertoletti, N., Chan, A. H., Ippolito, J. A., Bollini, M., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2022) Structural Studies and Structure Activity Relationships for Novel Computationally Designed Non-nucleoside Inhibitors and Their Interactions With HIV-1 Reverse Transcriptase. Front Mol Biosci. 9, 805187
Lou, X., Ma, B., Zhuang, Y., Xiao, X., Minze, L. J., Xing, J., Zhang, Z., and Li, X. C. (2022) Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex. Comput Struct Biotechnol J. 20, 4921-4929
Liang, Q., Richey, S. T., Ur, S. N., Ye, Q., Lau, R. K., and Corbett, K. D. (2022) Structure and activity of a bacterial defense-associated 3'-5' exonuclease. Protein Sci. 31, e4374
Fraser, B. J., Beldar, S., Seitova, A., Hutchinson, A., Mannar, D., Li, Y., Kwon, D., Tan, R., Wilson, R. P., Leopold, K., Subramaniam, S., Halabelian, L., Arrowsmith, C. H., and Bénard, F. (2022) Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation. Nat Chem Biol. 10.1038/s41589-022-01059-7
Chen, B., Basak, S., Chen, P., Zhang, C., Perry, K., Tian, S., Yu, C., Dong, M., Huang, L., Bowen, M. E., and Jin, R. (2022) Structure and conformational dynamics of toxin A. Life Sci Alliance. 10.26508/lsa.202201383
Moeller, N. H., Shi, K., Demir, Ö., Belica, C., Banerjee, S., Yin, L., Durfee, C., Amaro, R. E., and Aihara, H. (2022) Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN. Proc Natl Acad Sci U S A. 10.1073/pnas.2106379119
Patteson, J. B., Fortinez, C. Marie, Putz, A. T., Rodriguez-Rivas, J., L Bryant, H., Adhikari, K., Weigt, M., T Schmeing, M., and Li, B. (2022) Structure and Function of a Dehydrating Condensation Domain in Nonribosomal Peptide Biosynthesis. J Am Chem Soc. 144, 14057-14070
Guo, X., Schmiege, P., Assafa, T. E., Wang, R., Xu, Y., Donnelly, L., Fine, M., Ni, X., Jiang, J., Millhauser, G., Feng, L., and Li, X. (2022) Structure and mechanism of human cystine exporter cystinosin. Cell. 185, 3739-3752.e18
Swofford, C. A., Nordeen, S. A., Chen, L., Desai, M. M., Chen, J., Springs, S. L., Schwartz, T. U., and Sinskey, A. J. (2022) Structure and Specificity of an Anti-Chloramphenicol Single Domain Antibody for Detection of Amphenicol Residues. Protein Sci. 10.1002/pro.4457
Hall, D., Giaimo, B. Daniele, Park, S. - S., Hemmer, W., Friedrich, T., Ferrante, F., Bartkuhn, M., Yuan, Z., Oswald, F., Borggrefe, T., Rual, J. - F., and Kovall, R. A. (2022) The structure, binding and function of a Notch transcription complex involving RBPJ and the epigenetic reader protein L3MBTL3.. Nucleic Acids Res. 50, 13083-13099
Sharon, I., Grogg, M., Hilvert, D., and T Schmeing, M. (2022) The structure of cyanophycinase in complex with a cyanophycin degradation intermediate. Biochim Biophys Acta Gen Subj. 1866, 130217
Gao, L., Guo, Y., Biswal, M., Lu, J., Yin, J., Fang, J., Chen, X., Shao, Z., Huang, M., Wang, Y., Wang, G. Greg, and Song, J. (2022) Structure of DNMT3B homo-oligomer reveals vulnerability to impairment by ICF mutations. Nat Commun. 13, 4249
Mahoney, B. J., Takayesu, A., Zhou, A., Cascio, D., and Clubb, R. T. (2022) The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins. 10.1002/prot.26326