Publications

Found 1711 results
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2018
Gao, A., Vasilyev, N., Luciano, D. J., Levenson-Palmer, R., Richards, J., Marsiglia, W. M., Traaseth, N. J., Belasco, J. G., and Serganov, A. (2018) Structural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF. Nucleic Acids Res. 10.1093/nar/gky327
Nomura, Y., Roston, D., Montemayor, E. J., Cui, Q., and Butcher, S. E. (2018) Structural and mechanistic basis for preferential deadenylation of U6 snRNA by Usb1. Nucleic Acids Res. 10.1093/nar/gky812
Grell, T. A. J., Kincannon, W. M., Bruender, N. A., Blaesi, E. J., Krebs, C., Bandarian, V., and Drennan, C. L. (2018) Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. J Biol Chem. 10.1074/jbc.RA118.005369
Grell, T. A. J., Kincannon, W. M., Bruender, N. A., Blaesi, E. J., Krebs, C., Bandarian, V., and Drennan, C. L. (2018) Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. J Biol Chem. 10.1074/jbc.RA118.005369
Grell, T. A. J., Kincannon, W. M., Bruender, N. A., Blaesi, E. J., Krebs, C., Bandarian, V., and Drennan, C. L. (2018) Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. J Biol Chem. 10.1074/jbc.RA118.005369
Shelke, S. A., Shao, Y., Laski, A., Koirala, D., Weissman, B. P., Fuller, J. R., Tan, X., Constantin, T. P., Waggoner, A. S., Bruchez, M. P., Armitage, B. A., and Piccirilli, J. A. (2018) Structural basis for activation of fluorogenic dyes by an RNA aptamer lacking a G-quadruplex motif. Nat Commun. 9, 4542
Sun, J., Paduch, M., Kim, S. - A., Kramer, R. M., Barrios, A. F., Lu, V., Luke, J., Usatyuk, S., Kossiakoff, A. A., and Tan, S. (2018) Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2. Proc Natl Acad Sci U S A. 10.1073/pnas.1805343115
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Cooper, R. S., Georgieva, E. R., Borbat, P. P., Freed, J. H., and Heldwein, E. E. (2018) Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB. Nat Struct Mol Biol. 25, 416-424
Rechkoblit, O., Choudhury, J. Roy, Buku, A., Prakash, L., Prakash, S., and Aggarwal, A. K. (2018) Structural basis for polymerase η-promoted resistance to the anticancer nucleoside analog cytarabine.. Sci Rep. 8, 12702
Nithianantham, S., Cook, B. D., Beans, M., Guo, F., Chang, F., and Al-Bassam, J. (2018) Structural basis of tubulin recruitment and assembly by microtubule polymerases with Tumor Overexpressed Gene (TOG) domain arrays. Elife. 10.7554/eLife.38922
Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Varland, S., Ree, R., Drazic, A., Bhambra, P., Støve, S. I., Baumann, M., Haug, B. Erik, Marmorstein, R., and Arnesen, T. (2018) Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc Natl Acad Sci U S A. 115, 4405-4410
Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Varland, S., Ree, R., Drazic, A., Bhambra, P., Støve, S. I., Baumann, M., Haug, B. Erik, Marmorstein, R., and Arnesen, T. (2018) Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc Natl Acad Sci U S A. 115, 4405-4410
Banerjee, A., Ghosh, S., Goldgur, Y., and Shuman, S. (2018) Structure and two-metal mechanism of fungal tRNA ligase. Nucleic Acids Res. 10.1093/nar/gky1275
Jobichen, C., Chong, T. Ying, Prabhakar, M. Tirumuru, Nayak, D., Biswas, D., Pannu, N. Singh, Hanski, E., and Sivaraman, J. (2018) Structure of ScpC, a virulence protease from , reveal the functional domains and maturation mechanism. Biochem J. 10.1042/BCJ20180145
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., and McDermott, A. E. (2018) The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell. 173, 1244-1253.e10
Sanghai, Z. Assur, Liu, Q., Clarke, O. B., Belcher-Dufrisne, M., Wiriyasermkul, P., M Giese, H., Leal-Pinto, E., Kloss, B., Tabuso, S., Love, J., Punta, M., Banerjee, S., Rajashankar, K. R., Rost, B., Logothetis, D., Quick, M., Hendrickson, W. A., and Mancia, F. (2018) Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife. 10.7554/eLife.27829
Sanghai, Z. Assur, Liu, Q., Clarke, O. B., Belcher-Dufrisne, M., Wiriyasermkul, P., M Giese, H., Leal-Pinto, E., Kloss, B., Tabuso, S., Love, J., Punta, M., Banerjee, S., Rajashankar, K. R., Rost, B., Logothetis, D., Quick, M., Hendrickson, W. A., and Mancia, F. (2018) Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife. 10.7554/eLife.27829
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Orman, M., Bodea, S., Funk, M. A., Del Campo, A. Martínez-, Bollenbach, M., Drennan, C. L., and Balskus, E. P. (2018) Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. J Am Chem Soc. 10.1021/jacs.8b04883
Orman, M., Bodea, S., Funk, M. A., Del Campo, A. Martínez-, Bollenbach, M., Drennan, C. L., and Balskus, E. P. (2018) Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. J Am Chem Soc. 10.1021/jacs.8b04883

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