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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, 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, X., Kim, T. Doohun, Carman, C. V., Mi, L. - Z., Song, G., and Springer, T. A. (2007) Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization. Proc Natl Acad Sci U S A. 104, 15358-63
Chen, H., Coseno, M., Ficarro, S. B., Mansueto, M. Sam, Komazin-Meredith, G., Boissel, S., Filman, D. J., Marto, J. A., Hogle, J. M., and Coen, D. M. (2017) A Small Covalent Allosteric Inhibitor of Human Cytomegalovirus DNA Polymerase Subunit Interactions. ACS Infect Dis. 3, 112-118
Chen, S., Rufiange, A., Huang, H., Rajashankar, K. R., Nourani, A., and Patel, D. J. (2015) Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2. Genes Dev. 29, 1326-40
Chen, E., Trajkovski, M., Lee, H. Kyung, Nyovanie, S., Martin, K. N., Dean, W. L., Tahiliani, M., Plavec, J., and Yatsunyk, L. A. (2024) Structure of native four-repeat satellite III sequence with non-canonical base interactions. Nucleic Acids Res. 52, 3390-3405
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, 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., 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, W., and Li, W. (2014) Structural insights into ubiquinone biosynthesis in membranes. Science. 343, 878-81
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
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
Chitrakar, I., Iuliano, J. N., He, Y. L., Woroniecka, H. A., Collado, J. Tolentino, Wint, J. M., Walker, S. G., Tonge, P. J., and French, J. B. (2020) Structural Basis for the Regulation of Biofilm Formation and Iron Uptake in by the Blue-Light-Using Photoreceptor, BlsA. ACS Infect Dis. 6, 2592-2603
Chitrakar, I., Ahmed, S. Fardin, Torelli, A. T., and French, J. B. (2021) Structure of the E. coli agmatinase, SPEB. PLoS One. 16, e0248991
Cho, U. - S., and Harrison, S. C. (2011) Ndc10 is a platform for inner kinetochore assembly in budding yeast. Nat Struct Mol Biol. 19, 48-55
Cho, U. - S., and Harrison, S. C. (2011) Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Proc Natl Acad Sci U S A. 108, 9367-71
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nature Microbiology. 10.1038/nmicrobiol.2016.154
Cho, J., Lee, M., C Cochrane, S., Webster, C. G., Fenton, B. A., Zhao, J., Hong, J., and Zhou, P. (2020) Structural basis of the UDP-diacylglucosamine pyrophosphohydrolase LpxH inhibition by sulfonyl piperazine antibiotics. Proc Natl Acad Sci U S A. 117, 4109-4116
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol. 1, 16154

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