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Batool, Z., Lomakin, I. B., Polikanov, Y. S., and Bunick, C. G. (2020) Sarecycline interferes with tRNA accommodation and tethers mRNA to the 70S ribosome. Proc Natl Acad Sci U S A. 10.1073/pnas.2008671117
Batool, Z., Pavlova, J. A., Paranjpe, M. N., Tereshchenkov, A. G., Lukianov, D. A., Osterman, I. A., Bogdanov, A. A., Sumbatyan, N. V., and Polikanov, Y. S. (2024) Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity. Structure. 10.1016/j.str.2024.06.013
Battaglia, R. A., Price, I. R., and Ke, A. (2017) Structural basis for guanidine sensing by the ykkC family of riboswitches. RNA. 23, 578-585
Battaglia, R. A., Grigg, J. C., and Ke, A. (2019) Structural basis for tRNA decoding and aminoacylation sensing by T-box riboregulators. Nat Struct Mol Biol. 26, 1106-1113
Bauer, J. A., Bennett, E. M., Begley, T. P., and Ealick, S. E. (2004) Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis. J Biol Chem. 279, 2704-11
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Baytshtok, V., Fei, X., Shih, T. - T., Grant, R. A., Santos, J. C., Baker, T. A., and Sauer, R. T. (2021) Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Rep. 34, 108639
Baytshtok, V., Chen, J., Glynn, S. E., Nager, A. R., Grant, R. A., Baker, T. A., and Sauer, R. T. (2017) Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. J Biol Chem. 292, 5695-5704
Bazzoli, A., Vance, D. J., Rudolph, M. J., Rong, Y., Angalakurthi, S. Krishna, Toth, R. T., C Middaugh, R., Volkin, D. B., Weis, D. D., Karanicolas, J., and Mantis, N. J. (2017) Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies. Proteins. 85, 1994-2008
Becker, A., Kannan, T. R., Taylor, A. B., Pakhomova, O. N., Zhang, Y., Somarajan, S. R., Galaleldeen, A., Holloway, S. P., Baseman, J. B., and P Hart, J. (2015) Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 112, 5165-70
Begley, M. J., Yun, C. -hong, Gewinner, C. A., Asara, J. M., Johnson, J. L., Coyle, A. J., Eck, M. J., Apostolou, I., and Cantley, L. C. (2015) EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with Src. Nat Struct Mol Biol. 22, 983-90
Békés, M., van Noort, G. J. van der, Ekkebus, R., Ovaa, H., Huang, T. T., and Lima, C. D. (2016) Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease. Mol Cell. 62, 572-85
Bellizzi, J. J., Sorger, P. K., and Harrison, S. C. (2007) Crystal structure of the yeast inner kinetochore subunit Cep3p. Structure. 15, 1422-30
Ben-Nun, Y., Seo, H. - S., Harvey, E. P., Hauseman, Z. J., Wales, T. E., Newman, C. E., Cathcart, A. M., Engen, J. R., Dhe-Paganon, S., and Walensky, L. D. (2020) Identification of a Structural Determinant for Selective Targeting of HDMX. Structure. 28, 847-857.e5
Benavides, B. S., Valandro, S., Cioloboc, D., Taylor, A. B., Schanze, K. S., and Kurtz, D. M. (2020) Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. 59, 1618-1629
Benjamin, B., Goldgur, Y., Jork, N., Jessen, H. J., Schwer, B., and Shuman, S. (2022) Structures of Fission Yeast Inositol Pyrophosphate Kinase Asp1 in Ligand-Free, Substrate-Bound, and Product-Bound States. mBio. 10.1128/mbio.03087-22
Benveniste, P. M., Roy, S., Nakatsugawa, M., L Y Chen, E., Nguyen, L., Millar, D. G., Ohashi, P. S., Hirano, N., Adams, E. J., and Zúñiga-Pflücker, J. Carlos (2018) Generation and molecular recognition of melanoma-associated antigen-specific human γδ T cells.. Sci Immunol. 10.1126/sciimmunol.aav4036
Berger, S., Seeger, F., Yu, T. - Y., Aydin, M., Yang, H., Rosenblum, D., Guenin-Macé, L., Glassman, C., Arguinchona, L., Sniezek, C., Blackstone, A., Carter, L., Ravichandran, R., Ahlrichs, M., Murphy, M., Pultz, I. Swanson, Kang, A., Bera, A. K., Stewart, L., K Garcia, C., Naik, S., Spangler, J. B., Beigel, F., Siebeck, M., Gropp, R., and Baker, D. (2024) Preclinical proof of principle for orally delivered Th17 antagonist miniproteins. Cell. 187, 4305-4317.e18
Berk, J. M., Lim, C., Ronau, J. A., Chaudhuri, A., Chen, H., Beckmann, J. F., J Loria, P., Xiong, Y., and Hochstrasser, M. (2020) A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi. Nat Commun. 11, 2343
Berkovitch, F., Behshad, E., Tang, K. - H., Enns, E. A., Frey, P. A., and Drennan, C. L. (2004) A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proc Natl Acad Sci U S A. 101, 15870-5
Berman, A. J., Kamtekar, S., Goodman, J. L., Lázaro, J. M., de Vega, M., Blanco, L., Salas, M., and Steitz, T. A. (2007) Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases. EMBO J. 26, 3494-505
Bertoletti, N., Chan, A. H., Schinazi, R. F., and Anderson, K. S. (2020) Post-Catalytic Complexes with Emtricitabine or Stavudine and HIV-1 Reverse Transcriptase Reveal New Mechanistic Insights for Nucleotide Incorporation and Drug Resistance. Molecules. 10.3390/molecules25204868
Bertoletti, N., Chan, A. H., Schinazi, R. F., Y Yin, W., and Anderson, K. S. (2019) Structural insights into the recognition of nucleoside reverse transcriptase inhibitors by HIV-1 reverse transcriptase: First crystal structures with reverse transcriptase and the active triphosphate forms of lamivudine and emtricitabine. Protein Sci. 28, 1664-1675
Bertram, J. H., Mulliner, K. M., Shi, K., Plunkett, M. H., Nixon, P., Serratore, N. A., Douglas, C. J., Aihara, H., and Barney, B. M. (2017) Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket. Appl Environ Microbiol. 10.1128/AEM.00018-17
Beseiso, D., Chen, E. V., McCarthy, S. E., Martin, K. N., Gallagher, E. P., Miao, J., and Yatsunyk, L. A. (2022) The first crystal structures of hybrid and parallel four-tetrad intramolecular G-quadruplexes. Nucleic Acids Res. 50, 2959-2972

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