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Found 149 results
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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, 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, 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, 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., 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
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
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
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, 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
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
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., 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
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
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
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
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, 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
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, 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, 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
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
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

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