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Borovinskaya, M. A., Pai, R. D., Zhang, W., Schuwirth, B. S., Holton, J. M., Hirokawa, G., Kaji, H., Kaji, A., and Cate, J. H. Doudna (2007) Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Nat Struct Mol Biol. 14, 727-32
Bowen, N. E., Temple, J., Shepard, C., Oo, A., Arizaga, F., Kapoor-Vazirani, P., Persaud, M., Yu, C. H., Kim, D. - H., Schinazi, R. F., Ivanov, D. N., Diaz-Griffero, F., Yu, D. S., Xiong, Y., and Kim, B. (2021) Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins. J Biol Chem. 10.1016/j.jbc.2021.101170
Bowman, B. R., Lee, S., Wang, S., and Verdine, G. L. (2010) Structure of Escherichia coli AlkA in complex with undamaged DNA. J Biol Chem. 285, 35783-91
Bowman, B. R., Lee, S., Wang, S., and Verdine, G. L. (2008) Structure of the E. coli DNA glycosylase AlkA bound to the ends of duplex DNA: a system for the structure determination of lesion-containing DNA. Structure. 16, 1166-74
Boys, I. N., Johnson, A. G., Quinlan, M. R., Kranzusch, P. J., and Elde, N. C. (2023) Structural homology screens reveal host-derived poxvirus protein families impacting inflammasome activity. Cell Rep. 42, 112878
Boys, I. N., Johnson, A. G., Quinlan, M., Kranzusch, P. J., and Elde, N. C. (2023) Structural homology screens reveal poxvirus-encoded proteins impacting inflammasome-mediated defenses. bioRxiv. 10.1101/2023.02.26.529821
Bozzi, A. T., Zimanyi, C. M., Nicoludis, J. M., Lee, B. K., Zhang, C. H., and Gaudet, R. (2019) Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter. Elife. 10.7554/eLife.41124
Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54
Braffman, N. R., Piscotta, F. J., Hauver, J., Campbell, E. A., A Link, J., and Darst, S. A. (2019) Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin. Proc Natl Acad Sci U S A. 116, 1273-1278
Brohawn, S. G., Leksa, N. C., Spear, E. D., Rajashankar, K. R., and Schwartz, T. U. (2008) Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Science. 322, 1369-73
Broussard, T. C., Pakhomova, S., Neau, D. B., Bonnot, R., and Waldrop, G. L. (2015) Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase. Biochemistry. 54, 3860-70
Brown, K. L., Banerjee, S., Feigley, A., Abe, H., Blackwell, T. S., Pozzi, A., Hudson, B. G., and Zent, R. (2018) Salt-bridge modulates differential calcium-mediated ligand binding to integrin α1- and α2-I domains.. Sci Rep. 8, 2916
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Brown, J. A., Bulkley, D., Wang, J., Valenstein, M. L., Yario, T. A., Steitz, T. A., and Steitz, J. A. (2014) Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nat Struct Mol Biol. 21, 633-40
Brugger, C., Schwartz, J., Novick, S., Tong, S., Hoskins, J., Majdalani, N., Kim, R., Filipovski, M., Wickner, S., Gottesman, S., Griffin, P., and Deaconescu, A. M. (2023) Structure of Phosphorylated-like RssB, the Adaptor Delivering σ to the ClpXP Proteolytic Machinery, Reveals an Interface Switch for Activation.. J Biol Chem. 10.1016/j.jbc.2023.105440
Bu, W., Settembre, E. C., Kouni, M. H. el, and Ealick, S. E. (2005) Structural basis for inhibition of Escherichia coli uridine phosphorylase by 5-substituted acyclouridines. Acta Crystallogr D Biol Crystallogr. 61, 863-72
Busscher, B. M., Befekadu, H. B., Liu, Z., and Xiao, T. Sam (2023) SARS-CoV-2 ORF3a-Mediated NF-κB Activation Is Not Dependent on TRAF-Binding Sequence.. Viruses. 10.3390/v15112229
Butler, E. B., Xiong, Y., Wang, J., and Strobel, S. A. (2011) Structural basis of cooperative ligand binding by the glycine riboswitch. Chem Biol. 18, 293-8
Buzovetsky, O., Tang, C., Knecht, K. M., Antonucci, J. M., Wu, L., Ji, X., and Xiong, Y. (2018) The SAM domain of mouse SAMHD1 is critical for its activation and regulation. Nat Commun. 9, 411
C
Cabarca, S., de Souza, M. Frazão, de Oliveira, A. Albert, Muniz, G. S. Vignoli, M Lamy, T., Reis, C. Vinicius D., Takarada, J., Effer, B., Souza, L. Santos, de la Torre, L. Iriarte, Couñago, R., Oliveira, C. Luis Pinto, and Balan, A. (2021) Structure of the PknF and conformational changes induced in forkhead-associated regulatory domains. Curr Res Struct Biol. 3, 165-178
Cai, Y., Chin, H. F., Lazarova, D., Menon, S., Fu, C., Cai, H., Sclafani, A., Rodgers, D. W., De La Cruz, E. M., Ferro-Novick, S., and Reinisch, K. M. (2008) The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cell. 133, 1202-13
Cai, Z., Chehab, N. H., and Pavletich, N. P. (2009) Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. Mol Cell. 35, 818-29
Cai, Y., Deng, Y., Horenkamp, F., Reinisch, K. M., and Burd, C. G. (2014) Sac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. J Cell Biol. 206, 485-91
Callahan, S. J., Luyten, Y. A., Gupta, Y. K., Wilson, G. G., Roberts, R. J., Morgan, R. D., and Aggarwal, A. K. (2016) Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities. PLoS Biol. 14, e1002442
Calmettes, C., Alcantara, J., Yu, R. - H., Schryvers, A. B., and Moraes, T. F. (2012) The structural basis of transferrin sequestration by transferrin-binding protein B. Nat Struct Mol Biol. 19, 358-60

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