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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, 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, W., and Li, W. (2014) Structural insights into ubiquinone biosynthesis in membranes. Science. 343, 878-81
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
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, 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, 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
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, 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, 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
Choi, E. H., Suh, S., Sander, C. L., Hernandez, C. J. Ortiz, Bulman, E. R., Khadka, N., Dong, Z., Shi, W., Palczewski, K., and Kiser, P. D. (2018) Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65. Hum Mol Genet. 10.1093/hmg/ddy128
Choi, P. H., Vu, T. Minh Ngoc, Pham, H. Thi, Woodward, J. J., Turner, M. S., and Tong, L. (2017) Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria. Proc Natl Acad Sci U S A. 114, E7226-E7235
Choi, P. H., Jo, J., Lin, Y. - C., Lin, M. - H., Chou, C. - Y., Dietrich, L. E. P., and Tong, L. (2016) A distinct holoenzyme organization for two-subunit pyruvate carboxylase. Nat Commun. 7, 12713
Choi, J. Yong, Fuerst, R., Knapinska, A. M., Taylor, A. B., Smith, L., Cao, X., P Hart, J., Fields, G. B., and Roush, W. R. (2017) Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors. J Med Chem. 60, 5816-5825
Choi, M., Sukumar, N., F Mathews, S., Liu, A., and Davidson, V. L. (2011) Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface. Biochemistry. 50, 1265-73
Choi, M., Sukumar, N., Liu, A., and Davidson, V. L. (2009) Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry. 48, 9174-84

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