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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
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 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
Daudu, O. I., Meeks, K. R., Zhang, L., Seravalli, J., Tanner, J. J., and Becker, D. F. (2023) Functional Impact of a Cancer-Related Variant in Human Δ-Pyrroline-5-Carboxylate Reductase 1.. ACS Omega. 8, 3509-3519
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
Das, N. K., Hollmann, N. M., Vogt, J., Sevdalis, S. E., Banna, H. A., Ojha, M., and Koirala, D. (2023) Crystal structure of a highly conserved enteroviral 5' cloverleaf RNA replication element. Nat Commun. 14, 1955
Das, A., Hand, T. H., Smith, C. L., Wickline, E., Zawrotny, M., and Li, H. (2020) The molecular basis for recognition of 5'-NNNCC-3' PAM and its methylation state by Acidothermus cellulolyticus Cas9. Nat Commun. 11, 6346
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
Darabedian, N., Ji, W., Fan, M., Lin, S., Seo, H. - S., Vinogradova, E. V., Yaron, T. M., Mills, E. L., Xiao, H., Senkane, K., Huntsman, E. M., Johnson, J. L., Che, J., Cantley, L. C., Cravatt, B. F., Dhe-Paganon, S., Stegmaier, K., Zhang, T., Gray, N. S., and Chouchani, E. T. (2023) Depletion of creatine phosphagen energetics with a covalent creatine kinase inhibitor. Nat Chem Biol. 10.1038/s41589-023-01273-x
Danhart, E. M., Bakhtina, M., Cantara, W. A., Kuzmishin, A. B., Ma, X., Sanford, B. L., Vargas-Rodriguez, O., Košutić, M., Goto, Y., Suga, H., Nakanishi, K., Micura, R., Foster, M. P., and Musier-Forsyth, K. (2017) Conformational and chemical selection by a -acting editing domain. Proc Natl Acad Sci U S A. 114, E6774-E6783
Dang, B., Kubota, T., Mandal, K., Correa, A. M., Bezanilla, F., and Kent, S. B. H. (2016) Elucidation of the Covalent and Tertiary Structures of Biologically Active Ts3 Toxin. Angew Chem Int Ed Engl. 55, 8639-42
Dang, B., Kubota, T., Mandal, K., Bezanilla, F., and Kent, S. B. H. (2013) Native chemical ligation at Asx-Cys, Glx-Cys: chemical synthesis and high-resolution X-ray structure of ShK toxin by racemic protein crystallography. J Am Chem Soc. 135, 11911-9