Publications

Found 414 results
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2018
Bohl, T. E., Shi, K., Lee, J. K., and Aihara, H. (2018) Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat Commun. 9, 377
Ji, T., Corbalán-García, S., and Hubbard, S. R. (2018) Crystal structure of the C-terminal four-helix bundle of the potassium channel KCa3.1. PLoS One. 13, e0199942
Lee, J. K., Bosnakovski, D., Toso, E. A., Dinh, T., Banerjee, S., Bohl, T. E., Shi, K., Orellana, K., Kyba, M., and Aihara, H. (2018) Crystal Structure of the Double Homeodomain of DUX4 in Complex with DNA. Cell Rep. 25, 2955-2962.e3
Hosford, C. J., and Chappie, J. S. (2018) The crystal structure of the LlaJI.R1 N-terminal domain provides a model for site-specific DNA binding. J Biol Chem. 293, 11758-11771
Saelices, L., Sievers, S. A., Sawaya, M. R., and Eisenberg, D. S. (2018) Crystal Structures of Amyloidogenic Segments of Human Transthyretin. Protein Sci. 10.1002/pro.3420
Harvey, E. P., Seo, H. - S., Guerra, R. M., Bird, G. H., Dhe-Paganon, S., and Walensky, L. D. (2018) Crystal Structures of Anti-apoptotic BFL-1 and Its Complex with a Covalent Stapled Peptide Inhibitor. Structure. 26, 153-160.e4
Maurici, N., Savidge, N., Lee, B. Uk, Brewer, S. H., and Phillips-Piro, C. M. (2018) Crystal structures of green fluorescent protein with the unnatural amino acid 4-nitro-L-phenylalanine. Acta Crystallogr F Struct Biol Commun. 74, 650-655
Trachman, R. J., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2018) Crystal Structures of the Mango-II RNA Aptamer Reveal Heterogeneous Fluorophore Binding and Guide Engineering of Variants with Improved Selectivity and Brightness. Biochemistry. 57, 3544-3548
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
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Guagnini, F., Antonik, P. M., Rennie, M. L., O'Byrne, P., Khan, A. R., Pinalli, R., Dalcanale, E., and Crowley, P. B. (2018) Cucurbit[7]uril-Dimethyllysine Recognition in a Model Protein. Angew Chem Int Ed Engl. 10.1002/anie.201803232
2017
Yao, G., Lam, K. - H., Weisemann, J., Peng, L., Krez, N., Perry, K., Shoemaker, C. B., Dong, M., Rummel, A., and Jin, R. (2017) A camelid single-domain antibody neutralizes botulinum neurotoxin A by blocking host receptor binding. Sci Rep. 7, 7438
Grintsevich, E. E., Ge, P., Sawaya, M. R., Yesilyurt, H. Gizem, Terman, J. R., Z Zhou, H., and Reisler, E. (2017) Catastrophic disassembly of actin filaments via Mical-mediated oxidation. Nat Commun. 8, 2183
Banerjee, S., Capel, M., Kourinov, I., A. Lynch, E., Murphy, F., Perry, K., Rajashankar, K.  R., Salbego, C., Schuermann, J. P., Sukumar, N., Neau, D., Withrow, J., and Ealick, S. E. (2017) Challenging Structural Biology Research at NE-CAT. BES Trienniel Review of the APS, August 15, 2017
Lynch, M. J., Levenson, R., Kim, E. A., Sircar, R., Blair, D. F., Dahlquist, F. W., and Crane, B. R. (2017) Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor. Structure. 25, 317-328
Fallas, J. A., Ueda, G., Sheffler, W., Nguyen, V., McNamara, D. E., Sankaran, B., Pereira, J. Henrique, Parmeggiani, F., Brunette, T. J., Cascio, D., Yeates, T. R., Zwart, P., and Baker, D. (2017) Computational design of self-assembling cyclic protein homo-oligomers. Nat Chem. 9, 353-360
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
Shi, K., Demir, Ö., Carpenter, M. A., Wagner, J., Kurahashi, K., Harris, R. S., Amaro, R. E., and Aihara, H. (2017) Conformational Switch Regulates the DNA Cytosine Deaminase Activity of Human APOBEC3B. Sci Rep. 7, 17415
Bryson, D. I., Fan, C., Guo, L. - T., Miller, C., Söll, D., and Liu, D. R. (2017) Continuous directed evolution of aminoacyl-tRNA synthetases. Nat Chem Biol. 13, 1253-1260
Fetherolf, M. M., Boyd, S. D., Taylor, A. B., Kim, H. Jong, Wohlschlegel, J. A., Blackburn, N. J., P Hart, J., Winge, D. R., and Winkler, D. D. (2017) Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site. J Biol Chem. 292, 12025-12040
Almutairi, M. M., Svetlov, M. S., Hansen, D. A., Khabibullina, N. F., Klepacki, D., Kang, H. - Y., Sherman, D. H., Vázquez-Laslop, N., Polikanov, Y. S., and Mankin, A. S. (2017) Co-produced natural ketolides methymycin and pikromycin inhibit bacterial growth by preventing synthesis of a limited number of proteins. Nucleic Acids Res. 45, 9573-9582
Chan, A. H., Lee, W. - G., Spasov, K. A., Cisneros, J. A., Kudalkar, S. N., Petrova, Z. O., Buckingham, A. B., Anderson, K. S., and Jorgensen, W. L. (2017) Covalent inhibitors for eradication of drug-resistant HIV-1 reverse transcriptase: From design to protein crystallography. Proc Natl Acad Sci U S A. 10.1073/pnas.1711463114
Baytshtok, V., Chen, J., Glynn, S. E., Nager, A. R., Grant, R. A., Baker, T. A., and Sauer, R. T. (2017) Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. J Biol Chem. 292, 5695-5704
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Liu, Y., Pan, J., Jenni, S., Raymond, D. D., Caradonna, T., Do, K. T., Schmidt, A. G., Harrison, S. C., and Grigorieff, N. (2017) CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface. J Mol Biol. 429, 1829-1839

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