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Cappadocia, L., Kochańczyk, T., and Lima, C. D. (2021) DNA asymmetry promotes SUMO modification of the single-stranded DNA-binding protein RPA. EMBO J. 10.15252/embj.2019103787
Cappadocia, L., Pichler, A., and Lima, C. D. (2015) Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. Nat Struct Mol Biol. 22, 968-75
Capili, A. D., and Lima, C. D. (2007) Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction. J Mol Biol. 369, 608-18
Capel, M. (2021) New endstations at NE-CAT: MD3UP microdiffractometer and 30 puck ALS-style loader. Current and Future Trends in Macromolecular Crystallography Experiments: Focus on Automation, High Data Rate Analysis and User Interfaces
Capel, M. (2022) NE-CAT Upgrades Drive by the APS-U. APS Upgrade Structural Biology Virtual Town Hall Meeting
Cao, Q., Shin, W. Shik, Chan, H., Vuong, C. K., Dubois, B., Li, B., Murray, K. A., Sawaya, M. R., Feigon, J., Black, D. L., Eisenberg, D. S., and Jiang, L. (2018) Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.. Nat Chem. 10.1038/s41557-018-0147-z
Cao, Y., Qiu, T., Kathayat, R. S., Azizi, S. - A., Thorne, A. K., Ahn, D., Fukata, Y., Fukata, M., Rice, P. A., and Dickinson, B. C. (2019) ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5. Nat Chem Biol. 15, 1232-1240
Cao, Y., Pan, Y., Huang, H., Jin, X., Levin, E. J., Kloss, B., and Zhou, M. (2013) Gating of the TrkH ion channel by its associated RCK protein TrkA. Nature. 496, 317-22
Cao, H., Pauff, J. M., and Hille, R. (2010) Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid. J Biol Chem. 285, 28044-53
Cao, L., Coventry, B., Goreshnik, I., Huang, B., Park, J. Sung, Jude, K. M., Marković, I., Kadam, R. U., Verschueren, K. H. G., Verstraete, K., Walsh, S. Thomas Rus, Bennett, N., Phal, A., Yang, A., Kozodoy, L., DeWitt, M., Picton, L., Miller, L., Strauch, E. - M., DeBouver, N. D., Pires, A., Bera, A. K., Halabiya, S., Hammerson, B., Yang, W., Bernard, S., Stewart, L., Wilson, I. A., Ruohola-Baker, H., Schlessinger, J., Lee, S., Savvides, S. N., K Garcia, C., and Baker, D. (2022) Design of protein binding proteins from target structure alone. Nature. 10.1038/s41586-022-04654-9
Cao, Y., Jin, X., Levin, E. J., Huang, H., Zong, Y., Quick, M., Weng, J., Pan, Y., Love, J., Punta, M., Rost, B., Hendrickson, W. A., Javitch, J. A., Rajashankar, K. R., and Zhou, M. (2011) Crystal structure of a phosphorylation-coupled saccharide transporter. Nature. 473, 50-4
Cao, Z., and Bowie, J. U. (2012) Shifting hydrogen bonds may produce flexible transmembrane helices. Proc Natl Acad Sci U S A. 109, 8121-6
Cao, R., Gozlan, O., Airich, A., Tveriakhina, L., Zhou, H., Jiang, H., Cole, P. A., Aster, J. C., Klein, T., Sprinzak, D., and Blacklow, S. C. (2024) Structural requirements for activity of Mind bomb1 in Notch signaling. Structure. 32, 1667-1676.e5
Cao, Y., Jin, X., Huang, H., Derebe, M. Getahun, Levin, E. J., Kabaleeswaran, V., Pan, Y., Punta, M., Love, J., Weng, J., Quick, M., Ye, S., Kloss, B., Bruni, R., Martinez-Hackert, E., Hendrickson, W. A., Rost, B., Javitch, J. A., Rajashankar, K. R., Jiang, Y., and Zhou, M. (2011) Crystal structure of a potassium ion transporter, TrkH. Nature. 471, 336-40
Cantara, W. A., Murphy, F. V., Demirci, H., and Agris, P. F. (2013) Expanded use of sense codons is regulated by modified cytidines in tRNA. Proc Natl Acad Sci U S A. 110, 10964-9
Cannon, K. A., Park, R. U., Boyken, S. E., Nattermann, U., Yi, S., Baker, D., King, N. P., and Yeates, T. O. (2019) Design and structure of two new protein cages illustrate successes and ongoing challenges in protein engineering. Protein Sci. 10.1002/pro.3802
Campiani, G., Cavella, C., Osko, J. D., Brindisi, M., Relitti, N., Brogi, S., A Saraswati, P., Federico, S., Chemi, G., Maramai, S., Carullo, G., Jaeger, B., Carleo, A., Benedetti, R., Sarno, F., Lamponi, S., Rottoli, P., Bargagli, E., Bertucci, C., Tedesco, D., Herp, D., Senger, J., Ruberti, G., Saccoccia, F., Saponara, S., Gorelli, B., Valoti, M., Kennedy, B., Sundaramurthi, H., Butini, S., Jung, M., Roach, K. M., Altucci, L., Bradding, P., Christianson, D. W., Gemma, S., and Prasse, A. (2021) Harnessing the Role of HDAC6 in Idiopathic Pulmonary Fibrosis: Design, Synthesis, Structural Analysis, and Biological Evaluation of Potent Inhibitors. J Med Chem. 64, 9960-9988
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
Campbell, A. C., Stiers, K. M., Del Campo, J. S. Martin, Mehra-Chaudhary, R., Sobrado, P., and Tanner, J. J. (2020) Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. J Biol Chem. 10.1074/jbc.RA120.014750
Campbell, E. A., Kamath, S., Rajashankar, K. R., Wu, M., and Darst, S. A. (2017) Crystal structure of Aquifex aeolicus σ(N) bound to promoter DNA and the structure of σ(N)-holoenzyme.. Proc Natl Acad Sci U S A. 114, E1805-E1814
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
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
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

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