Publications

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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
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
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
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
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
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
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
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
Deaconescu, A. M., and Darst, S. A. (2005) Crystallization and preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 61, 1062-4
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-la-Torre, P., Choudhary, D., Araya-Secchi, R., Narui, Y., and Sotomayor, M. (2018) A Mechanically Weak Extracellular Membrane-Adjacent Domain Induces Dimerization of Protocadherin-15. Biophys J. 115, 2368-2385
De Schutter, J. W., Morrison, J. P., Morrison, M. J., Ciulli, A., and Imperiali, B. (2017) Targeting Bacillosamine Biosynthesis in Bacterial Pathogens: Development of Inhibitors to a Bacterial Amino-Sugar Acetyltransferase from Campylobacter jejuni. J Med Chem. 60, 2099-2118
de Miranda, R., Cuthbert, B. J., Klevorn, T., Chao, A., Mendoza, J., Arbing, M., Sieminski, P. J., Papavinasasundaram, K., Abdul-Hafiz, S., Chan, S., Sassetti, C. M., Ehrt, S., and Goulding, C. W. (2023) Differentiating the roles of Mycobacterium tuberculosis substrate binding proteins, FecB and FecB2, in iron uptake. PLoS Pathog. 19, e1011650
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 Haas, R. J., Tas, R. P., van den Broek, D., Zheng, C., Nguyen, H., Kang, A., Bera, A. K., King, N. P., Voets, I. K., and de Vries, R. (2023) De novo designed ice-binding proteins from twist-constrained helices. Proc Natl Acad Sci U S A. 120, e2220380120
De Clercq, D. J. H., Heppner, D. E., To, C., Jang, J., Park, E., Yun, C. -hong, Mushajiang, M., Shin, B. Hee, Gero, T. W., Scott, D. A., Jänne, P. A., Eck, M. J., and Gray, N. S. (2019) Discovery and Optimization of Dibenzodiazepinones as Allosteric Mutant-Selective EGFR Inhibitors. ACS Med Chem Lett. 10, 1549-1553
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., Cantara, W. A., Kitzrow, J. P., Musier-Forsyth, K., and Nakanishi, K. (2018) Argonaute-based programmable RNase as a tool for cleavage of highly-structured RNA. Nucleic Acids Res. 46, e98
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, 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
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
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

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