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DeAngelo, T. M., Adhikary, U., Korshavn, K. J., Seo, H. - S., Brotzen-Smith, C. R., Camara, C. M., Dhe-Paganon, S., Bird, G. H., Wales, T. E., and Walensky, L. D. (2025) Structural insights into chemoresistance mutants of BCL-2 and their targeting by stapled BAD BH3 helices. Nat Commun. 16, 8623
Debler, E. W., Ma, Y., Seo, H. - S., Hsia, K. - C., Noriega, T. R., Blobel, G., and Hoelz, A. (2008) A fence-like coat for the nuclear pore membrane. Mol Cell. 32, 815-26
Decroos, C., and Christianson, D. W. (2015) Design, Synthesis, and Evaluation of Polyamine Deacetylase Inhibitors, and High-Resolution Crystal Structures of Their Complexes with Acetylpolyamine Amidohydrolase. Biochemistry. 54, 4692-703
Deinema, M. S., Perry, K., Kearns, S. P., D’Antonio, E. L., and D’Antonio, J. (2014) Inhibition of Trypanosoma cruzi Glucokinase with 2,6-Dideoxy-2,6-Diamino-D-Glucose. 66th Southeastern Regional Meeting of the American Chemical Society, October 16-19, 2014
Del Pino, G. L. Gonzalez, Li, K., Park, E., Schmoker, A. M., Ha, B. Hak, and Eck, M. J. (2021) Allosteric MEK inhibitors act on BRAF/MEK complexes to block MEK activation. Proc Natl Acad Sci U S A. 10.1073/pnas.2107207118
Delmar, J. A., and Yu, E. W. (2018) Crystallographic Analysis of the CusBA Heavy-Metal Efflux Complex of Escherichia coli. Methods Mol Biol. 1700, 59-70
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
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., Belardinelli, R., Kelley, A. C., Ramakrishnan, V., Gregory, S. T., Dahlberg, A. E., and Jogl, G. (2010) Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function. RNA. 16, 2319-24
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
Demirci, H., Wang, L., Murphy, F. V., Murphy, E. L., Carr, J. F., Blanchard, S. C., Jogl, G., Dahlberg, A. E., and Gregory, S. T. (2013) The central role of protein S12 in organizing the structure of the decoding site of the ribosome. RNA. 19, 1791-801
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
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, Y., Song, X., Iyamu, I. D., Dong, A., Min, J., and Huang, R. (2023) A unique binding pocket induced by a noncanonical SAH mimic to develop potent and selective PRMT inhibitors. Acta Pharm Sin B. 13, 4893-4905
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
Deng, S., Cai, J., Harrison, S. C., Zhou, H., and Hinshaw, S. M. (2023) Recognition of centromere-specific histone Cse4 by the inner kinetochore Okp1-Ame1 complex. EMBO Rep. 10.15252/embr.202357702
Deng, Z., Paknejad, N., Maksaev, G., Sala-Rabanal, M., Nichols, C. G., Hite, R. K., and Yuan, P. (2018) Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms. Nat Struct Mol Biol. 25, 252-260
Deng, Y., Deng, S., Ho, Y. - H., Gardner, S. M., Huang, Z., Marmorstein, R., and Huang, R. (2021) Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D. J Med Chem. 10.1021/acs.jmedchem.1c00141
Deo, C., Abdelfattah, A. S., Bhargava, H. K., Berro, A. J., Falco, N., Farrants, H., Moeyaert, B., Chupanova, M., Lavis, L. D., and Schreiter, E. R. (2021) The HaloTag as a general scaffold for far-red tunable chemigenetic indicators. Nat Chem Biol. 17, 718-723
Deochand, D. K., Perera, I. C., Crochet, R. B., Gilbert, N. C., Newcomer, M. E., and Grove, A. (2016) Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices. Mol Biosyst. 12, 2417-26
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
Dessau, M., and Modis, Y. (2013) Crystal structure of glycoprotein C from Rift Valley fever virus. Proc Natl Acad Sci U S A. 110, 1696-701
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
DeWeese, D. E., Everett, M. P., Babicz, J. T., Daruwalla, A., Solomon, E. I., and Kiser, P. D. (2025) Spectroscopy and crystallography define carotenoid oxygenases as a new subclass of mononuclear non-heme Fe enzymes. J Biol Chem. 301, 108444

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