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C
Cosmanescu, F., Katsamba, P. S., Sergeeva, A. P., Ahlsen, G., Patel, S. D., Brewer, J. J., Tan, L., Xu, S., Xiao, Q., Nagarkar-Jaiswal, S., Nern, A., Bellen, H. J., S Zipursky, L., Honig, B., and Shapiro, L. (2018) Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins. Neuron. 100, 1385-1400.e6
Cotner-Gohara, E., Kim, I. - K., Hammel, M., Tainer, J. A., Tomkinson, A. E., and Ellenberger, T. (2010) Human DNA ligase III recognizes DNA ends by dynamic switching between two DNA-bound states. Biochemistry. 49, 6165-76
Couzens, A. L., Xiong, S., Knight, J. D. R., Mao, D. Y., Guettler, S., Picaud, S., Kurinov, I., Filippakopoulos, P., Sicheri, F., and Gingras, A. - C. (2017) MOB1 Mediated Phospho-recognition in the Core Mammalian Hippo Pathway. Mol Cell Proteomics. 16, 1098-1110
Cramer, E. R., Starcovic, S. A., Avey, R. M., Kaya, A. I., and Robart, A. R. (2023) Structure of a 10-23 deoxyribozyme exhibiting a homodimer conformation. Commun Chem. 6, 119
Crenshaw, C. M., Nam, K., Oo, K., Kutchukian, P. S., Bowman, B. R., Karplus, M., and Verdine, G. L. (2012) Enforced presentation of an extrahelical guanine to the lesion recognition pocket of human 8-oxoguanine glycosylase, hOGG1. J Biol Chem. 287, 24916-28
Crochet, R. B., Kim, J. - D., Lee, H., Yim, Y. - S., Kim, S. - G., Neau, D., and Lee, Y. - H. (2017) Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding. Proteins. 85, 117-124
Crowley, C. S., Cascio, D., Sawaya, M. R., Kopstein, J. S., Bobik, T. A., and Yeates, T. O. (2010) Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell. J Biol Chem. 285, 37838-46
Cruz, V. E., F Demircioglu, E., and Schwartz, T. U. (2020) Structural analysis of different LINC complexes reveals distinct binding modes. J Mol Biol. 10.1016/j.jmb.2020.09.019
Cuello, L. G., Jogini, V., D Cortes, M., Pan, A. C., Gagnon, D. G., Dalmas, O., Cordero-Morales, J. F., Chakrapani, S., Roux, B., and Perozo, E. (2010) Structural basis for the coupling between activation and inactivation gates in K(+) channels. Nature. 466, 272-5
Cuello, L. G., Jogini, V., D Cortes, M., and Perozo, E. (2010) Structural mechanism of C-type inactivation in K(+) channels. Nature. 466, 203-8
Cui, H., Divakaran, A., Hoell, Z. J., Ellingson, M. O., Scholtz, C. R., Zahid, H., Johnson, J. A., Griffith, E. C., Gee, C. T., Lee, A. L., Khanal, S., Shi, K., Aihara, H., Shah, V. H., Lee, R. E., Harki, D. A., and Pomerantz, W. C. K. (2022) A Structure-based Design Approach for Generating High Affinity BRD4 D1-Selective Chemical Probes. J Med Chem. 10.1021/acs.jmedchem.1c01779
Cui, H., M Ali, Y., Goyal, P., Zhang, K., Loh, J. Ying, Trybus, K. M., and Solmaz, S. R. (2020) Coiled-coil registry shifts in the F684I mutant of Bicaudal D result in cargo-independent activation of dynein motility. Traffic. 10.1111/tra.12734
Cui, H., Carlson, A. S., Schleiff, M. A., Divakaran, A., Johnson, J. A., Buchholz, C. R., Zahid, H., Vail, N. R., Shi, K., Aihara, H., Harki, D. A., Miller, G. P., Topczewski, J. J., and Pomerantz, W. C. K. (2021) 4-Methyl-1,2,3-Triazoles as -Acetyl-Lysine Mimics Afford Potent BET Bromodomain Inhibitors with Improved Selectivity. J Med Chem. 64, 10497-10511
Custodio, J. M., Ayres, C. M., Rosales, T. J., Brambley, C. A., Arbuiso, A. G., Landau, L. M., Keller, G. L. J., Srivastava, P. K., and Baker, B. M. (2023) Structural and physical features that distinguish tumor-controlling from inactive cancer neoepitopes. Proc Natl Acad Sci U S A. 120, e2312057120
Czajka, T. F., Vance, D. J., Davis, S., Rudolph, M. J., and Mantis, N. J. (2022) Single-domain antibodies neutralize ricin toxin intracellularly by blocking access to ribosomal P-stalk proteins. J Biol Chem. 298, 101742
Czyzyk, D. J., Valhondo, M., Jorgensen, W. L., and Anderson, K. S. (2019) Understanding the structural basis of species selective, stereospecific inhibition for Cryptosporidium and human thymidylate synthase. FEBS Lett. 593, 2069-2078
Czyzyk, D. J., Valhondo, M., Deiana, L., Tirado-Rives, J., Jorgensen, W. L., and Anderson, K. S. (2019) Structure activity relationship towards design of cryptosporidium specific thymidylate synthase inhibitors. Eur J Med Chem. 183, 111673
D
D'Antonio, E. L., Deinema, M. S., Kearns, S. P., Frey, T. A., Tanghe, S., Perry, K., Roy, T. A., Gracz, H. S., Rodriguez, A., and D'Antonio, J. (2015) Structure-based approach to the identification of a novel group of selective glucosamine analogue inhibitors of Trypanosoma cruzi glucokinase. Mol Biochem Parasitol. 204, 64-76
Da Fonseca, I., Qureshi, I. A., Mehra-Chaudhary, R., Kizjakina, K., Tanner, J. J., and Sobrado, P. (2014) Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics. Biochemistry. 53, 7794-804
da Rosa, S. Tabares-, Wogulis, L. A., Wogulis, M. D., González-Sapienza, G., and Wilson, D. K. (2019) Structure and specificity of several triclocarban-binding single domain camelid antibody fragments. J Mol Recognit. 32, e2755
Dai, Q., Ren, A., Westholm, J. O., Duan, H., Patel, D. J., and Lai, E. C. (2015) Common and distinct DNA-binding and regulatory activities of the BEN-solo transcription factor family. Genes Dev. 29, 48-62
Dalton, K. M., and Crosson, S. (2010) A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex. Biochemistry. 49, 2205-15
Dalton, K. M., Greisman, J. B., and Hekstra, D. R. (2022) A unifying Bayesian framework for merging X-ray diffraction data. Nat Commun. 13, 7764
Dang, B., Kubota, T., Mandal, K., Correa, A. M., Bezanilla, F., and Kent, S. B. H. (2016) Elucidation of the Covalent and Tertiary Structures of Biologically Active Ts3 Toxin. Angew Chem Int Ed Engl. 55, 8639-42
Dang, B., Shen, R., Kubota, T., Mandal, K., Bezanilla, F., Roux, B., and Kent, S. B. H. (2017) Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 56, 3324-3328

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