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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
Sue, A. C. - H., Mannige, R. V., Deng, H., Cao, D., Wang, C., Gándara, F., J Stoddart, F., Whitelam, S., and Yaghi, O. M. (2015) Heterogeneity of functional groups in a metal-organic framework displays magic number ratios. Proc Natl Acad Sci U S A. 112, 5591-6
Sudhamsu, J., Lee, G. In, Klessig, D. F., and Crane, B. R. (2008) The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition. J Biol Chem. 283, 32968-76
Suddala, K. C., Price, I. R., Dandpat, S. S., Janeček, M., Kührová, P., Šponer, J., Banáš, P., Ke, A., and Walter, N. G. (2019) Local-to-global signal transduction at the core of a Mn sensing riboswitch. Nat Commun. 10, 4304
Subramanian, R., Wilson-Kubalek, E. M., Arthur, C. P., Bick, M. J., Campbell, E. A., Darst, S. A., Milligan, R. A., and Kapoor, T. M. (2010) Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. Cell. 142, 433-43
Subramanian, R., Ti, S. - C., Tan, L., Darst, S. A., and Kapoor, T. M. (2013) Marking and measuring single microtubules by PRC1 and kinesin-4. Cell. 154, 377-90
Su, C. - C., Radhakrishnan, A., Kumar, N., Long, F., Bolla, J. Reddy, Lei, H. - T., Delmar, J. A., Do, S. V., Chou, T. - H., Rajashankar, K. R., Zhang, Q., and Yu, E. W. (2014) Crystal structure of the Campylobacter jejuni CmeC outer membrane channel. Protein Sci. 23, 954-61
Su, C. - C., Klenotic, P. A., Bolla, J. Reddy, Purdy, G. E., Robinson, C. V., and Yu, E. W. (2019) MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine. Proc Natl Acad Sci U S A. 10.1073/pnas.1901346116
Su, C. - C., Long, F., McDermott, G., Shafer, W. M., and Yu, E. W. (2008) Crystallization and preliminary X-ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64, 289-92
Su, M., Li, Y., Wyborny, S., Neau, D., Chakravarthy, S., Levine, B., Colbert, C. L., and Sinha, S. C. (2017) BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy. Protein Sci. 26, 972-984
Su, C. - C., Long, F., and Yu, E. W. (2011) The Cus efflux system removes toxic ions via a methionine shuttle. Protein Sci. 20, 6-18
Su, C. - C., Yin, L., Kumar, N., Dai, L., Radhakrishnan, A., Bolla, J. Reddy, Lei, H. - T., Chou, T. - H., Delmar, J. A., Rajashankar, K. R., Zhang, Q., Shin, Y. - K., and Yu, E. W. (2017) Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump. Nat Commun. 8, 171
Su, C. - C., Klenotic, P. A., Cui, M., Lyu, M., Morgan, C. E., and Yu, E. W. (2021) Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol. 19, e3001370
Su, C. - C., Long, F., Zimmermann, M. T., Rajashankar, K. R., Jernigan, R. L., and Yu, E. W. (2011) Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature. 470, 558-62
Su, C. - C., Long, F., Lei, H. - T., Bolla, J. Reddy, Do, S. V., Rajashankar, K. R., and Yu, E. W. (2012) Charged amino acids (R83, E567, D617, E625, R669, and K678) of CusA are required for metal ion transport in the Cus efflux system. J Mol Biol. 422, 429-41
Su, M., Gao, F., Yuan, Q., Mao, Y., Li, D. - L., Guo, Y., Yang, C., Wang, X. - H., Bruni, R., Kloss, B., Zhao, H., Zeng, Y., Ben Zhang, F. -, Marks, A. R., Hendrickson, W. A., and Chen, Y. - H. (2017) Structural basis for conductance through TRIC cation channels. Nat Commun. 8, 15103
Su, C. - C., Bolla, J. Reddy, Kumar, N., Radhakrishnan, A., Long, F., Delmar, J. A., Chou, T. - H., Rajashankar, K. R., Shafer, W. M., and Yu, E. W. (2015) Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps. Cell Rep. 11, 61-70
Su, C. - C., Yang, F., Long, F., Reyon, D., Routh, M. D., Kuo, D. W., Mokhtari, A. K., Van Ornam, J. D., Rabe, K. L., Hoy, J. A., Lee, Y. Jin, Rajashankar, K. R., and Yu, E. W. (2009) Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol. 393, 342-55
Strunk, R. J., Piemonte, K. M., Petersen, N. M., Koutsioulis, D., Bouriotis, V., Perry, K., and Cole, K. E. (2014) Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis. Acta Crystallogr F Struct Biol Commun. 70, 156-9
Strugatsky, D., McNulty, R., Munson, K., Chen, C. - K., S Soltis, M., Sachs, G., and Luecke, H. (2013) Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori. Nature. 493, 255-8
Streich, F. C., and Lima, C. D. (2016) Capturing a substrate in an activated RING E3/E2-SUMO complex. Nature. 536, 304-8
Streeter, O., Shi, K., Vavra, J., Aihara, H., Ervasti, J. M., Evans, R., and Muretta, J. M. (2025) Human dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation. Acta Crystallogr D Struct Biol. 81, 122-129
Stopper, D., Biermann, L., Watson, P. R., Li, J., König, B., Gaynes, M. N., de Carvalho, L. Pessanha, Klose, J., Hanl, M., Hamacher, A., Schäker-Hübner, L., Ramsbeck, D., Held, J., Christianson, D. W., Kassack, M. U., and Hansen, F. K. (2025) Exploring Alternative Zinc-Binding Groups in Histone Deacetylase (HDAC) Inhibitors Uncovers as a Potent Ethylhydrazide-Based HDAC Inhibitor with Chemosensitizing Properties. J Med Chem. 10.1021/acs.jmedchem.4c02373
Stokes-Rees, I., Levesque, I., Murphy, F. V., Yang, W., Deacon, A., and Sliz, P. (2012) Adapting federated cyberinfrastructure for shared data collection facilities in structural biology. J Synchrotron Radiat. 19, 462-7
Stoddard, P. R., Lynch, E. M., Farrell, D. P., Dosey, A. M., DiMaio, F., Williams, T. A., Kollman, J. M., Murray, A. W., and Garner, E. C. (2020) Polymerization in the actin ATPase clan regulates hexokinase activity in yeast. Science. 367, 1039-1042

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