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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 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 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-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
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
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., 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
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
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
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., 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
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, 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
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

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