Found 857 results
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Zeller, M. J., Favorov, O., Li, K., Nuthanakanti, A., Hussein, D., Michaud, A., Lafontaine, D. A., Busan, S., Serganov, A., Aubé, J., and Weeks, K. M. (2022) SHAPE-enabled fragment-based ligand discovery for RNA. Proc Natl Acad Sci U S A. 119, e2122660119
Czajka, T. F., Vance, D. J., Davis, S., Rudolph, M. J., and Mantis, N. J. (2022) Single-domain antibodies neutralize ricin toxin intracellularly by blocking access to ribosomal P-stalk proteins. J Biol Chem. 298, 101742
Adlakha, J., Hong, Z., Li, P. Q., and Reinisch, K. M. (2022) Structural and biochemical insights into lipid transport by VPS13 proteins. J Cell Biol. 10.1083/jcb.202202030
Baranovskiy, A. G., Babayeva, N. D., Lisova, A. E., Morstadt, L. M., and Tahirov, T. H. (2022) Structural and functional insight into mismatch extension by human DNA polymerase α.. Proc Natl Acad Sci U S A. 119, e2111744119
Rees, H. C., Gogacz, W., Li, N. - S., Koirala, D., and Piccirilli, J. A. (2022) Structural Basis for Fluorescence Activation by Pepper RNA. ACS Chem Biol. 17, 1866-1875
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
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
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
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
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
Chen, B., Liu, Z., Perry, K., and Jin, R. (2022) Structure of the glucosyltransferase domain of TcdA in complex with RhoA provides insights into substrate recognition. Sci Rep. 12, 9028
Bogner, A. N., and Tanner, J. J. (2022) Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase. Org Biomol Chem. 10.1039/d1ob02328d
Cui, H., Divakaran, A., Hoell, Z. J., Ellingson, M. O., Scholtz, C. R., Zahid, H., Johnson, J. A., Griffith, E. C., Gee, C. T., Lee, A. L., Khanal, S., Shi, K., Aihara, H., Shah, V. H., Lee, R. E., Harki, D. A., and Pomerantz, W. C. K. (2022) A Structure-based Design Approach for Generating High Affinity BRD4 D1-Selective Chemical Probes. J Med Chem. 10.1021/acs.jmedchem.1c01779
Fortinez, C. Marie, Bloudoff, K., Harrigan, C., Sharon, I., Strauss, M., and T Schmeing, M. (2022) Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module. Nat Commun. 13, 548
Gorelik, A., Illes, K., Bui, K. Huy, and Nagar, B. (2022) Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase. Proc Natl Acad Sci U S A. 119, e2203518119
Zeller, M. J., Nuthanakanti, A., Li, K., Aubé, J., Serganov, A., and Weeks, K. M. (2022) Subsite Ligand Recognition and Cooperativity in the TPP Riboswitch: Implications for Fragment-Linking in RNA Ligand Discovery. ACS Chem Biol. 17, 438-448