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Bulkley, D., C Innis, A., Blaha, G., and Steitz, T. A. (2010) Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proc Natl Acad Sci U S A. 107, 17158-63
Bunker, R. D., Mandal, K., Bashiri, G., Chaston, J. J., Pentelute, B. L., J Lott, S., Kent, S. B. H., and Baker, E. N. (2015) A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography. Proc Natl Acad Sci U S A. 112, 4310-5
Burke, H. G., and Heldwein, E. E. (2015) Crystal Structure of the Human Cytomegalovirus Glycoprotein B. PLoS Pathog. 11, e1005227
Buss, J. M., McTamney, P. M., and Rokita, S. E. (2012) Expression of a soluble form of iodotyrosine deiodinase for active site characterization by engineering the native membrane protein from Mus musculus. Protein Sci. 21, 351-61
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
Buzovetsky, O., Kwon, Y., Pham, N. Tuyet, Kim, C., Ira, G., Sung, P., and Xiong, Y. (2017) Role of the Pif1-PCNA Complex in Pol δ-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication.. Cell Rep. 21, 1707-1714
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C Y Jeng, S., Trachman, R. J., Weissenboeck, F., Truong, L., Link, K. A., Jepsen, M. D. E., Knutson, J. R., Andersen, E. S., Ferré-D'Amaré, A. R., and Unrau, P. J. (2021) Fluorogenic aptamers resolve the flexibility of RNA junctions using orientation-dependent FRET. RNA. 27, 433-444
C Y Kuk, A., Mashalidis, E. H., and Lee, S. - Y. (2017) Crystal structure of the MOP flippase MurJ in an inward-facing conformation. Nat Struct Mol Biol. 24, 171-176
C Y Kuk, A., Hao, A., Guan, Z., and Lee, S. - Y. (2019) Visualizing conformation transitions of the Lipid II flippase MurJ. Nat Commun. 10, 1736
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, X. - C., Zhang, T., Kim, E. - J., Jiang, M., Wang, K., Wang, J., Chen, S., Zhang, N., Wu, H., Li, F., Seña, C. C. Dela, Zeng, H., Vivcharuk, V., Niu, X., Zheng, W., Lee, J. P., Chen, Y., Barsyte, D., Szewczyk, M., Hajian, T., Ibáñez, G., Dong, A., Dombrovski, L., Zhang, Z., Deng, H., Min, J., Arrowsmith, C. H., Mazutis, L., Shi, L., Vedadi, M., Brown, P. J., Xiang, J., Qin, L. - X., Xu, W., and Luo, M. (2019) A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion. Elife. 10.7554/eLife.47110
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, R., Price, I. R., Ding, F., Wu, F., Chen, T., Zhang, Y., Liu, G., Jardine, P. J., Lu, C., and Ke, A. (2019) ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor. Nucleic Acids Res. 10.1093/nar/gkz692
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
Calabrese, M. F., Scott, D. C., Duda, D. M., Grace, C. R. R., Kurinov, I., Kriwacki, R. W., and Schulman, B. A. (2011) A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nat Struct Mol Biol. 18, 947-9
Caldwell, J. T., Mermelstein, D. J., Walker, R. C., Bernstein, S. I., and Huxford, T. (2019) X-ray crystallographic and molecular dynamic analyses of Drosophila melanogaster embryonic muscle myosin define domains responsible for isoform-specific properties. J Mol Biol. 10.1016/j.jmb.2019.11.013
Callahan, S. J., Morgan, R. D., Jain, R., Townson, S. A., Wilson, G. G., Roberts, R. J., and Aggarwal, A. K. (2011) Crystallization and preliminary crystallographic analysis of the type IIL restriction enzyme MmeI in complex with DNA. Acta Crystallogr Sect F Struct Biol Cryst Commun. 67, 1262-5
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., Ing, C., Buckwalter, C. M., Bakkouri, M. El, Lai, C. Chieh- Lin, Pogoutse, A., Gray-Owen, S. D., Pomès, R., and Moraes, T. F. (2015) The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. Nat Commun. 6, 7996
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
Campbell, A. C., Becker, D. F., Gates, K. S., and Tanner, J. J. (2020) Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. ACS Chem Biol. 10.1021/acschembio.9b00935
Campbell, A. C., Prater, A. R., Bogner, A. N., Quinn, T. P., Gates, K. S., Becker, D. F., and Tanner, J. J. (2021) Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles. ACS Chem Biol. 10.1021/acschembio.1c00427

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