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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
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
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
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
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
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
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
Dharmaiah, S., Bindu, L., Tran, T. H., Gillette, W. K., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2016) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.. Proc Natl Acad Sci U S A. 113, E6766-E6775
Dhayalan, B., Mandal, K., Rege, N., Weiss, M. A., Eitel, S. H., Meier, T., Schoenleber, R. O., and Kent, S. B. H. (2017) Scope and Limitations of Fmoc Chemistry SPPS-Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin. Chemistry. 23, 1709-1716
Dhindwal, S., Gomez-Gil, L., Neau, D. B., Pham, T. Thanh My, Sylvestre, M., Eltis, L. D., Bolin, J. T., and Kumar, P. (2016) Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase. J Bacteriol. 198, 1499-512
Di Paolo, J. A., Huang, T., Balazs, M., Barbosa, J., Barck, K. H., Bravo, B. J., Carano, R. A. D., Darrow, J., Davies, D. R., DeForge, L. E., Diehl, L., Ferrando, R., Gallion, S. L., Giannetti, A. M., Gribling, P., Hurez, V., Hymowitz, S. G., Jones, R., Kropf, J. E., Lee, W. P., Maciejewski, P. M., Mitchell, S. A., Rong, H., Staker, B. L., J Whitney, A., Yeh, S., Young, W. B., Yu, C., Zhang, J., Reif, K., and Currie, K. S. (2011) Specific Btk inhibition suppresses B cell- and myeloid cell-mediated arthritis. Nat Chem Biol. 7, 41-50
Dickson, V. Kane, Pedi, L., and Long, S. B. (2014) Structure and insights into the function of a Ca(2+)-activated Cl(-) channel. Nature. 516, 213-8
Didovyk, A., and Verdine, G. L. (2012) Structural origins of DNA target selection and nucleobase extrusion by a DNA cytosine methyltransferase. J Biol Chem. 287, 40099-105
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Dimitrova, Y. N., Jenni, S., Valverde, R., Khin, Y., and Harrison, S. C. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell. 167, 1014-1027.e12
Ding, F., Lu, C., Zhao, W., Rajashankar, K. R., Anderson, D. L., Jardine, P. J., Grimes, S., and Ke, A. (2011) Structure and assembly of the essential RNA ring component of a viral DNA packaging motor. Proc Natl Acad Sci U S A. 108, 7357-62
Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60
Donaldson, T. M., Ting, L. - M., Zhan, C., Shi, W., Zheng, R., Almo, S. C., and Kim, K. (2014) Structural determinants of the 5'-methylthioinosine specificity of Plasmodium purine nucleoside phosphorylase. PLoS One. 9, e84384
Dong, G., Hutagalung, A. H., Fu, C., Novick, P., and Reinisch, K. M. (2005) The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol. 12, 1094-100
Dong, N., Zhu, Y., Lu, Q., Hu, L., Zheng, Y., and Shao, F. (2012) Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell. 150, 1029-41
Dong, C., Mao, Y., Tempel, W., Qin, S., Li, L., Loppnau, P., Huang, R., and Min, J. (2015) Structural basis for substrate recognition by the human N-terminal methyltransferase 1. Genes Dev. 29, 2343-8
Dong, C., Liu, Y., Lyu, T. - J., Beldar, S., Lamb, K. N., Tempel, W., Li, Y., Li, Z., James, L. I., Qin, S., Wang, Y., and Min, J. (2020) Structural Basis for the Binding Selectivity of Human CDY Chromodomains. Cell Chem Biol. 10.1016/j.chembiol.2020.05.007
Dove, K. K., Olszewski, J. L., Martino, L., Duda, D. M., Wu, X. S., Miller, D. J., Reiter, K. H., Rittinger, K., Schulman, B. A., and Klevit, R. E. (2017) Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.. Structure. 25, 890-900.e5
Dow, B. A., Sukumar, N., Matos, J. O., Choi, M., Schulte, A., Tatulian, S. A., and Davidson, V. L. (2014) The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Arch Biochem Biophys. 550-551, 20-7

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