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Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
Chen, Z., Pelc, L. A., and Di Cera, E. (2010) Crystal structure of prethrombin-1. Proc Natl Acad Sci U S A. 107, 19278-83
Chen, G., Liu, Y., Goetz, R., Fu, L., Jayaraman, S., Hu, M. - C., Moe, O. W., Liang, G., Li, X., and Mohammadi, M. (2018) α-Klotho is a non-enzymatic molecular scaffold for FGF23 hormone signalling.. Nature. 10.1038/nature25451
Chen, S., Oldham, M. L., Davidson, A. L., and Chen, J. (2013) Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography. Nature. 499, 364-8
Chen, P. Yang- Ting, Li, B., Drennan, C. L., and Elliott, S. J. (2019) A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO. Joule. 3, 595-611
Chen, P., Tao, L., Wang, T., Zhang, J., He, A., Lam, K. - H., Liu, Z., He, X., Perry, K., Dong, M., and Jin, R. (2018) Structural basis for recognition of frizzled proteins by toxin B. Science. 360, 664-669
Chen, Y., Bauer, B. W., Rapoport, T. A., and Gumbart, J. C. (2015) Conformational Changes of the Clamp of the Protein Translocation ATPase SecA. J Mol Biol. 427, 2348-59
Chen, M., Drury, J. E., Christianson, D. W., and Penning, T. M. (2012) Conversion of human steroid 5β-reductase (AKR1D1) into 3β-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering.. J Biol Chem. 287, 16609-22
Chen, Y., Seepersaud, R., Bensing, B. A., Sullam, P. M., and Rapoport, T. A. (2016) Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Proc Natl Acad Sci U S A. 113, E1190-9
Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., and Christianson, D. W. (2016) Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase. ACS Chem Biol. 11, 889-99
Chen, P., Lam, K. - H., Liu, Z., Mindlin, F. A., Chen, B., Gutierrez, C. B., Huang, L., Zhang, Y., Hamza, T., Feng, H., Matsui, T., Bowen, M. E., Perry, K., and Jin, R. (2019) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0
Chen, W. - H., Kim, J. H., Bu, W., Board, N. L., Tsybovsky, Y., Wang, Y., Hostal, A., Andrews, S. F., Gillespie, R. A., Choe, M., Stephens, T., Yang, E. Sung, Pegu, A., Peterson, C. E., Fisher, B. E., Mascola, J. R., Pittaluga, S., McDermott, A. B., Kanekiyo, M., M Joyce, G., and Cohen, J. I. (2022) Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition. Immunity. 55, 2135-2148.e6
Chen, B., Liu, Z., Perry, K., and Jin, R. (2022) Structure of the glucosyltransferase domain of TcdA in complex with RhoA provides insights into substrate recognition. Sci Rep. 12, 9028
Cheng, S., Park, Y., Kurleto, J. D., Jeon, M., Zinn, K., Thornton, J. W., and zkan, E. Ö. (2019) Family of neural wiring receptors in bilaterians defined by phylogenetic, biochemical, and structural evidence. Proc Natl Acad Sci U S A. 10.1073/pnas.1818631116
Cheng, P. - N., Liu, C., Zhao, M., Eisenberg, D., and Nowick, J. S. (2012) Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.. Nat Chem. 4, 927-33
Cheng, Z., Cheung, P., Kuo, A. J., Yukl, E. T., Wilmot, C. M., Gozani, O., and Patel, D. J. (2014) A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36. Genes Dev. 28, 1758-71
Cheng, S., Ashley, J., Kurleto, J. D., Lobb-Rabe, M., Park, Y. Jenny, Carrillo, R. A., and zkan, E. Ö. (2019) Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in . Elife. 10.7554/eLife.41028
Cheng, W., and Li, W. (2014) Structural insights into ubiquinone biosynthesis in membranes. Science. 343, 878-81
Chetty, A. K., Sexton, J. A., Ha, B. Hak, Turk, B. E., and Boggon, T. J. (2020) Recognition of physiological phosphorylation sites by p21-activated kinase 4. J Struct Biol. 211, 107553
Cheung, J., Mahmood, A., Kalathur, R., Liu, L., and Carlier, P. R. (2018) Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance. Structure. 26, 130-136.e2
Chevalier, A., Silva, D. - A., Rocklin, G. J., Hicks, D. R., Vergara, R., Murapa, P., Bernard, S. M., Zhang, L., Lam, K. - H., Yao, G., Bahl, C. D., Miyashita, S. - I., Goreshnik, I., Fuller, J. T., Koday, M. T., Jenkins, C. M., Colvin, T., Carter, L., Bohn, A., Bryan, C. M., D Fernández-Velasco, A., Stewart, L., Dong, M., Huang, X., Jin, R., Wilson, I. A., Fuller, D. H., and Baker, D. (2017) Massively parallel de novo protein design for targeted therapeutics. Nature. 550, 74-79
Chiang, Y. - C., Levsh, O., Lam, C. Kei, Weng, J. - K., and Wang, Y. (2018) Structural and dynamic basis of substrate permissiveness in hydroxycinnamoyltransferase (HCT). PLoS Comput Biol. 14, e1006511
Chichili, V. Priyanka R., Chew, T. Weng, Shankar, S., Er, S. Yin, Chin, C. Fei, Jobichen, C., Pan, C. Qiurong, Zhou, Y., Yeong, F. May, Low, B. Chuan, and Sivaraman, J. (2021) Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation. Proc Natl Acad Sci U S A. 10.1073/pnas.2014242118
Chien, P., Grant, R. A., Sauer, R. T., and Baker, T. A. (2007) Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors. Structure. 15, 1296-305
Chinai, J. M., Taylor, A. B., Ryno, L. M., Hargreaves, N. D., Morris, C. A., P Hart, J., and Urbach, A. R. (2011) Molecular recognition of insulin by a synthetic receptor. J Am Chem Soc. 133, 8810-3

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