Publications

Found 1208 results
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2017
Taylor, A. B., Roberts, K. M., Cao, X., Clark, N. E., Holloway, S. P., Donati, E., Polcaro, C. M., Pica-Mattoccia, L., Tarpley, R. S., McHardy, S. F., Cioli, D., LoVerde, P. T., Fitzpatrick, P. F., and P Hart, J. (2017) Structural and enzymatic insights into species-specific resistance to schistosome parasite drug therapy. J Biol Chem. 292, 11154-11164
Taylor, A. B., Roberts, K. M., Cao, X., Clark, N. E., Holloway, S. P., Donati, E., Polcaro, C. M., Pica-Mattoccia, L., Tarpley, R. S., McHardy, S. F., Cioli, D., LoVerde, P. T., Fitzpatrick, P. F., and P Hart, J. (2017) Structural and enzymatic insights into species-specific resistance to schistosome parasite drug therapy. J Biol Chem. 292, 11154-11164
Choi, P. H., Vu, T. Minh Ngoc, Pham, H. Thi, Woodward, J. J., Turner, M. S., and Tong, L. (2017) Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria. Proc Natl Acad Sci U S A. 114, E7226-E7235
Hoelper, D., Huang, H., Jain, A. Y., Patel, D. J., and Lewis, P. W. (2017) Structural and mechanistic insights into ATRX-dependent and -independent functions of the histone chaperone DAXX. Nat Commun. 8, 1193
Peng, G., Yang, Y., Pasquarella, J. R., Xu, L., Qian, Z., Holmes, K. V., and Li, F. (2017) Structural and Molecular Evidence Suggesting Coronavirus-driven Evolution of Mouse Receptor. J Biol Chem. 292, 2174-2181
Peng, G., Yang, Y., Pasquarella, J. R., Xu, L., Qian, Z., Holmes, K. V., and Li, F. (2017) Structural and Molecular Evidence Suggesting Coronavirus-driven Evolution of Mouse Receptor. J Biol Chem. 292, 2174-2181
Dufrisne, M. Belcher, Petrou, V. I., Clarke, O. B., and Mancia, F. (2017) Structural basis for catalysis at the membrane-water interface. Biochim Biophys Acta Mol Cell Biol Lipids. 1862, 1368-1385
Battaglia, R. A., Price, I. R., and Ke, A. (2017) Structural basis for guanidine sensing by the ykkC family of riboswitches. RNA. 23, 578-585
Trachman, R. J., Demeshkina, N. A., Lau, M. W. L., Panchapakesan, S. Shyam S., C Y Jeng, S., Unrau, P. J., and Ferré-D'Amaré, A. R. (2017) Structural basis for high-affinity fluorophore binding and activation by RNA Mango. Nat Chem Biol. 13, 807-813
Ren, X., Gelinas, A. D., von Carlowitz, I., Janjic, N., and Pyle, A. Marie (2017) Structural basis for IL-1α recognition by a modified DNA aptamer that specifically inhibits IL-1α signaling.. Nat Commun. 8, 810
Born, D. A., Ulrich, E. C., San Ju, K. -, Peck, S. C., van der Donk, W. A., and Drennan, C. L. (2017) Structural basis for methylphosphonate biosynthesis. Science. 358, 1336-1339
Seegar, T. C. M., Killingsworth, L. B., Saha, N., Meyer, P. A., Patra, D., Zimmerman, B., Janes, P. W., Rubinstein, E., Nikolov, D. B., Skiniotis, G., Kruse, A. C., and Blacklow, S. C. (2017) Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.. Cell. 171, 1638-1648.e7
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
Zhao, C., and Pyle, A. Marie (2017) Structural Insights into the Mechanism of Group II Intron Splicing. Trends Biochem Sci. 42, 470-482
Sui, X., Weitz, A. C., Farquhar, E. R., Badiee, M., Banerjee, S., von Lintig, J., Tochtrop, G. P., Palczewski, K., Hendrich, M. P., and Kiser, P. D. (2017) Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Biochemistry. 56, 2836-2852
Lanier, M., Pickens, J., Bigi, S. V., Bradshaw-Pierce, E. L., Chambers, A., Cheruvallath, Z. S., Cole, D., Dougan, D. R., Ermolieff, J., Gibson, T., Halkowycz, P., Hirokawa, A., Ivetac, A., Miura, J., Nunez, E., Sabat, M., Tyhonas, J., Wang, H., Wang, X., and Swann, S. (2017) Structure-Based Design of ASK1 Inhibitors as Potential Agents for Heart Failure. ACS Med Chem Lett. 8, 316-320
Sheng, G., Gogakos, T., Wang, J., Zhao, H., Serganov, A., Juranek, S., Tuschl, T., Patel, D. J., and Wang, Y. (2017) Structure/cleavage-based insights into helical perturbations at bulge sites within T. thermophilus Argonaute silencing complexes. Nucleic Acids Res. 45, 9149-9163
Porter, N. J., Mahendran, A., Breslow, R., and Christianson, D. W. (2017) Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors. Proc Natl Acad Sci U S A. 10.1073/pnas.1718823114
Hanke, L., Schmidt, F. I., Knockenhauer, K. E., Morin, B., Whelan, S. Pj, Schwartz, T. U., and Ploegh, H. L. (2017) Vesicular stomatitis virus N protein-specific single-domain antibody fragments inhibit replication. EMBO Rep. 18, 1027-1037
2016
Hanke, L., Knockenhauer, K. E., R Brewer, C., van Diest, E., Schmidt, F. I., Schwartz, T. U., and Ploegh, H. L. (2016) The Antiviral Mechanism of an Influenza A Virus Nucleoprotein-Specific Single-Domain Antibody Fragment. MBio. 10.1128/mBio.01569-16
Fenwick, M. K., Philmus, B., Begley, T. P., and Ealick, S. E. (2016) Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis. Biochemistry. 55, 2748-59
Truttmann, M. C., Cruz, V. E., Guo, X., Engert, C., Schwartz, T. U., and Ploegh, H. L. (2016) The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones. PLoS Genet. 12, e1006023
Li, X., Saha, P., Li, J., Blobel, G., and Pfeffer, S. R. (2016) Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2. Proc Natl Acad Sci U S A. 113, 10079-84
Handa, S., Paul, B. G., Miller, J. F., Valentine, D. L., and Ghosh, P. (2016) Conservation of the C-type lectin fold for accommodating massive sequence variation in archaeal diversity-generating retroelements. BMC Struct Biol. 16, 13
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250

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