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Dharmaiah, S., Tran, T. H., Messing, S., Agamasu, C., Gillette, W. K., Yan, W., Waybright, T., Alexander, P., Esposito, D., Nissley, D. V., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2019) Structures of N-terminally processed KRAS provide insight into the role of N-acetylation. Sci Rep. 9, 10512
Dhakshnamoorthy, B., Rohaim, A., Rui, H., Blachowicz, L., and Roux, B. (2016) Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola. Nat Commun. 7, 12753
Dhakshnamoorthy, B., Ziervogel, B. K., Blachowicz, L., and Roux, B. (2013) A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations. J Am Chem Soc. 135, 16561-8
Devlin, J. R., Alonso, J. A., Ayres, C. M., Keller, G. L. J., Bobisse, S., Kooi, C. W. Vander, Coukos, G., Gfeller, D., Harari, A., and Baker, B. M. (2020) Structural dissimilarity from self drives neoepitope escape from immune tolerance. Nat Chem Biol. 10.1038/s41589-020-0610-1
Dessanti, P., Zhang, Y., Allegrini, S., Tozzi, M. Grazia, Sgarrella, F., and Ealick, S. E. (2012) Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase. Acta Crystallogr D Biol Crystallogr. 68, 239-48
Deshmukh, M. G., Ippolito, J. A., Zhang, C. - H., Stone, E. A., Reilly, R. A., Miller, S. J., Jorgensen, W. L., and Anderson, K. S. (2021) Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease. Structure. 10.1016/j.str.2021.06.002
Deng, S., Magin, R. S., Wei, X., Pan, B., E Petersson, J., and Marmorstein, R. (2019) Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex. Structure. 27, 1057-1070.e4
Dempsey, D. R., Viennet, T., Iwase, R., Park, E., Henriquez, S., Chen, Z., Jeliazkov, J. R., Palanski, B. A., Phan, K. L., Coote, P., Gray, J. J., Eck, M. J., Gabelli, S. B., Arthanari, H., and Cole, P. A. (2021) The structural basis of PTEN regulation by multi-site phosphorylation. Nat Struct Mol Biol. 28, 858-868
F Demircioglu, E., Sosa, B. A., Ingram, J., Ploegh, H. L., and Schwartz, T. U. (2016) Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia. Elife. 10.7554/eLife.17983
Demirci, H., Murphy, F., Murphy, E., Gregory, S. T., Dahlberg, A. E., and Jogl, G. (2013) A structural basis for streptomycin-induced misreading of the genetic code. Nat Commun. 4, 1355
Demirci, H., Murphy, F. V., Murphy, E. L., Connetti, J. L., Dahlberg, A. E., Jogl, G., and Gregory, S. T. (2014) Structural analysis of base substitutions in Thermus thermophilus 16S rRNA conferring streptomycin resistance. Antimicrob Agents Chemother. 58, 4308-17
Delmar, J. A., Chou, T. - H., Wright, C. C., Licon, M. H., Doh, J. K., Radhakrishnan, A., Kumar, N., Lei, H. - T., Bolla, J. Reddy, Rajashankar, K. R., Su, C. - C., Purdy, G. E., and Yu, E. W. (2015) Structural Basis for the Regulation of the MmpL Transporters of Mycobacterium tuberculosis. J Biol Chem. 290, 28559-74
Deaconescu, A. M., Chambers, A. L., Smith, A. J., Nickels, B. E., Hochschild, A., Savery, N. J., and Darst, S. A. (2006) Structural basis for bacterial transcription-coupled DNA repair. Cell. 124, 507-20
De Ioannes, P., Leon, V. A., Kuang, Z., Wang, M., Boeke, J. D., Hochwagen, A., and Armache, K. - J. (2019) Structure and function of the Orc1 BAH-nucleosome complex. Nat Commun. 10, 2894
De Ioannes, P., Malu, S., Cortes, P., and Aggarwal, A. K. (2012) Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining. Cell Rep. 2, 1505-12
de Araujo, E. D., Erdogan, F., Neubauer, H. A., Meneksedag-Erol, D., Manaswiyoungkul, P., Eram, M. S., Seo, H. - S., Qadree, A. K., Israelian, J., Orlova, A., Suske, T., Pham, H. T. T., Boersma, A., Tangermann, S., Kenner, L., Rülicke, T., Dong, A., Ravichandran, M., Brown, P. J., Audette, G. F., Rauscher, S., Dhe-Paganon, S., Moriggl, R., and Gunning, P. T. (2019) Structural and functional consequences of the STAT5B driver mutation. Nat Commun. 10, 2517
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
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
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
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
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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