Publications

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Journal Article
Bulkley, D., Brandi, L., Polikanov, Y. S., Fabbretti, A., O'Connor, M., Gualerzi, C. O., and Steitz, T. A. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Rep. 6, 357-65
Marathe, N., Nguyen, H. An, Alumasa, J. N., Nagy, A. B. Kuzmishi, Vazquez, M., Dunham, C. M., and Keiler, K. C. (2023) Antibiotic that inhibits -translation blocks binding of EF-Tu to tmRNA but not to tRNA. mBio. 10.1128/mbio.01461-23
Lilic, M., Chen, J., Boyaci, H., Braffman, N., Hubin, E. A., Herrmann, J., Müller, R., Mooney, R., Landick, R., Darst, S. A., and Campbell, E. A. (2020) The antibiotic sorangicin A inhibits promoter DNA unwinding in a rifampicin-resistant RNA polymerase. Proc Natl Acad Sci U S A. 117, 30423-30432
J Y Wu, K., Tresco, B. I. C., Ramkissoon, A., Aleksandrova, E. V., Syroegin, E. A., N Y See, D., Liow, P., Dittemore, G. A., Yu, M., Testolin, G., Mitcheltree, M. J., Liu, R. Y., Svetlov, M. S., Polikanov, Y. S., and Myers, A. G. (2024) An antibiotic preorganized for ribosomal binding overcomes antimicrobial resistance. Science. 383, 721-726
May, J. M., Owens, T. W., Mandler, M. D., Simpson, B. W., Lazarus, M. B., Sherman, D. J., Davis, R. M., Okuda, S., Massefski, W., Ruiz, N., and Kahne, D. (2017) The Antibiotic Novobiocin Binds and Activates the ATPase That Powers Lipopolysaccharide Transport. J Am Chem Soc. 139, 17221-17224
Bosnakovski, D., Toso, E. A., Ener, E. T., Gearhart, M. D., Yin, L., Lüttmann, F. F., Magli, A., Shi, K., Kim, J., Aihara, H., and Kyba, M. (2023) Antagonism among DUX family members evolved from an ancestral toxic single homeodomain protein. iScience. 26, 107823
Kucera, K., Harrison, L. M., Cappello, M., and Modis, Y. (2011) Ancylostoma ceylanicum excretory-secretory protein 2 adopts a netrin-like fold and defines a novel family of nematode proteins. J Mol Biol. 408, 9-17
Murphy, M. W., Lee, J. K., Rojo, S., Gearhart, M. D., Kurahashi, K., Banerjee, S., Loeuille, G. - A., Bashamboo, A., McElreavey, K., Zarkower, D., Aihara, H., and Bardwell, V. J. (2015) An ancient protein-DNA interaction underlying metazoan sex determination. Nat Struct Mol Biol. 22, 442-51
Finkelstein, M. T., Miller, E. Parker, Erdman, M. C., and Fera, D. (2022) Analysis of two cooperating antibodies unveils immune pressure imposed on HIV Env to elicit a V3-glycan supersite broadly neutralizing antibody lineage. Front Immunol. 13, 962939
Tsai, Y., Sawaya, M. R., and Yeates, T. O. (2009) Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C. Acta Crystallogr D Biol Crystallogr. 65, 980-8
Andorfer, M. C., Evans, D., Yang, S., He, C. Qixin, Girlich, A. M., Vergara-Coll, J., Sukumar, N., Houk, K. N., and Lewis, J. C. (2022) Analysis of Laboratory-Evolved Flavin-Dependent Halogenases Affords a Computational Model for Predicting Halogenase Site Selectivity. Chem Catal. 2, 2658-2674
Sui, X., Kiser, P. D., Che, T., Carey, P. R., Golczak, M., Shi, W., von Lintig, J., and Palczewski, K. (2014) Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO). J Biol Chem. 289, 12286-99
Cheng, P. - N., Liu, C., Zhao, M., Eisenberg, D., and Nowick, J. S. (2012) Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.. Nat Chem. 4, 927-33
Polikanov, Y. S., Osterman, I. A., Szal, T., Tashlitsky, V. N., Serebryakova, M. V., Kusochek, P., Bulkley, D., Malanicheva, I. A., Efimenko, T. A., Efremenkova, O. V., Konevega, A. L., Shaw, K. J., Bogdanov, A. A., Rodnina, M. V., Dontsova, O. A., Mankin, A. S., Steitz, T. A., and Sergiev, P. V. (2014) Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Mol Cell. 56, 531-40
Oruganti, S., Zhang, Y., Li, H., Robinson, H., Terns, M. P., Terns, R. M., Yang, W., and Li, H. (2007) Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. J Mol Biol. 371, 1141-50
Clancy-Thompson, E., Devlin, C. A., Tyler, P. M., Servos, M. M., Ali, L. R., Ventre, K. S., M Bhuiyan, A., Bruck, P. T., Birnbaum, M. E., and Dougan, S. K. (2018) Altered Binding of Tumor Antigenic Peptides to MHC Class I Affects CD8 T Cell-Effector Responses. Cancer Immunol Res. 6, 1524-1536
Xia, S., Wood, M., Bradley, M. J., De La Cruz, E. M., and Konigsberg, W. H. (2013) Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Res. 41, 9077-89
Miller, J. E., Agdanowski, M. P., Dolinsky, J. L., Sawaya, M. R., Cascio, D., Rodriguez, J. A., and Yeates, T. O. (2024) AlphaFold-assisted structure determination of a bacterial protein of unknown function using X-ray and electron crystallography. Acta Crystallogr D Struct Biol. 80, 270-278
Patrick, J. W., Boone, C. D., Liu, W., Conover, G. M., Liu, Y., Cong, X., and Laganowsky, A. (2018) Allostery revealed within lipid binding events to membrane proteins. Proc Natl Acad Sci U S A. 115, 2976-2981
Sohn, J., Grant, R. A., and Sauer, R. T. (2010) Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. J Biol Chem. 285, 34039-47
Hobbs, K. F., Propp, J., Vance, N. R., Kalenkiewicz, A., Witkin, K. R., and M Spies, A. (2023) Allosteric Tuning of Caspase-7: Establishing the Nexus of Structure and Catalytic Power. Chemistry. 29, e202300872
Gannam, Z. T. K., Min, K., Shillingford, S. R., Zhang, L., Herrington, J., Abriola, L., Gareiss, P. C., Pantouris, G., Tzouvelekis, A., Kaminski, N., Zhang, X., Yu, J., Jamali, H., Ellman, J. A., Lolis, E., Anderson, K. S., and Bennett, A. M. (2020) An allosteric site on MKP5 reveals a strategy for small-molecule inhibition. Sci Signal. 10.1126/scisignal.aba3043
Yang, M. Hee, Tran, T. H., Hunt, B., Agnor, R., Johnson, C. W., Shui, B., Waybright, T. J., Nowak, J. A., Stephen, A. G., Simanshu, D. K., and Haigis, K. M. (2023) Allosteric Regulation of Switch-II Domain Controls KRAS Oncogenicity. Cancer Res. 83, 3176-3183
Thompson, M. C., Cascio, D., Leibly, D. J., and Yeates, T. O. (2015) An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein. Protein Sci. 24, 956-75
Del Pino, G. L. Gonzalez, Li, K., Park, E., Schmoker, A. M., Ha, B. Hak, and Eck, M. J. (2021) Allosteric MEK inhibitors act on BRAF/MEK complexes to block MEK activation. Proc Natl Acad Sci U S A. 10.1073/pnas.2107207118

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