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Dayeh, D. M., Kruithoff, B. C., and Nakanishi, K. (2018) Structural and functional analyses reveal the contributions of the C- and N-lobes of Argonaute protein to selectivity of RNA target cleavage. J Biol Chem. 10.1074/jbc.RA117.001051
Day, J. E., Hall, ii, T., Pegg, L. E., Benson, T. E., Hausmann, J., and Kamtekar, S. (2010) Crystallization and preliminary X-ray diffraction analysis of rat autotaxin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 1127-9
Dawson, C. D., Irwin, S. M., Backman, L. R. F., Le, C., Wang, J. X., Vennelakanti, V., Yang, Z., Kulik, H. J., Drennan, C. L., and Balskus, E. P. (2021) Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase. Cell Chem Biol. 10.1016/j.chembiol.2021.03.001
Dawson, T. K., Dziedzic, P., Robertson, M. J., Cisneros, J. A., Krimmer, S. G., Newton, A. S., Tirado-Rives, J., and Jorgensen, W. L. (2017) Adding a Hydrogen Bond May Not Help: Naphthyridinone vs Quinoline Inhibitors of Macrophage Migration Inhibitory Factor. ACS Med Chem Lett. 8, 1287-1291
Davis, M. J., Ha, B. Hak, Holman, E. C., Halaban, R., Schlessinger, J., and Boggon, T. J. (2013) RAC1P29S is a spontaneously activating cancer-associated GTPase. Proc Natl Acad Sci U S A. 110, 912-7
DasGupta, S., Suslov, N. B., and Piccirilli, J. A. (2017) Structural Basis for Substrate Helix Remodeling and Cleavage Loop Activation in the Varkud Satellite Ribozyme. J Am Chem Soc. 139, 9591-9597
Das, A., Hand, T. H., Smith, C. L., Wickline, E., Zawrotny, M., and Li, H. (2020) The molecular basis for recognition of 5'-NNNCC-3' PAM and its methylation state by Acidothermus cellulolyticus Cas9. Nat Commun. 11, 6346
Daruwalla, A., Zhang, J., Lee, H. Jun, Khadka, N., Farquhar, E. R., Shi, W., von Lintig, J., and Kiser, P. D. (2020) Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase. Proc Natl Acad Sci U S A. 117, 19914-19925
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., Kubota, T., Mandal, K., Bezanilla, F., and Kent, S. B. H. (2013) Native chemical ligation at Asx-Cys, Glx-Cys: chemical synthesis and high-resolution X-ray structure of ShK toxin by racemic protein crystallography. J Am Chem Soc. 135, 11911-9
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
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
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
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
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
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

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