Publications

Found 85 results
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2018
Kono, M., Ochida, A., Oda, T., Imada, T., Banno, Y., Taya, N., Masada, S., Kawamoto, T., Yonemori, K., Nara, Y., Fukase, Y., Yukawa, T., Tokuhara, H., Skene, R., Sang, B. - C., Hoffman, I. D., Snell, G. P., Uga, K., Shibata, A., Igaki, K., Nakamura, Y., Nakagawa, H., Tsuchimori, N., Yamasaki, M., Shirai, J., and Yamamoto, S. (2018) Discovery of [cis-3-({(5 R)-5-[(7-Fluoro-1,1-dimethyl-2,3-dihydro-1H-inden-5-yl)carbamoyl]-2-methoxy-7,8-dihydro-1,6-naphthyridin-6(5H)-yl}carbonyl)cyclobutyl]acetic Acid (TAK-828F) as a Potent Selective and Orally Available Novel Retinoic Acid Receptor-R. J Med Chem. 10.1021/acs.jmedchem.8b00061
Wittenborn, E. C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M. - E., Dementin, S., and Drennan, C. L. (2018) Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife. 10.7554/eLife.39451
Fontán, L., Qiao, Q., Hatcher, J. M., Casalena, G., Us, I., Teater, M., Durant, M., Du, G., Xia, M., Bilchuk, N., Chennamadhavuni, S., Palladino, G., Inghirami, G., Philippar, U., Wu, H., Scott, D. A., Gray, N. S., and Melnick, A. (2018) Specific covalent inhibition of MALT1 paracaspase suppresses B cell lymphoma growth. J Clin Invest. 128, 4397-4412
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
2017
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
Puleo, D. E., Kucera, K., Hammarén, H. M., Ungureanu, D., Newton, A. S., Silvennoinen, O., Jorgensen, W. L., and Schlessinger, J. (2017) Identification and Characterization of JAK2 Pseudokinase Domain Small Molecule Binders. ACS Med Chem Lett. 8, 618-621
Metelev, M., Osterman, I. A., Ghilarov, D., Khabibullina, N. F., Yakimov, A., Shabalin, K., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M., Artamonova, T., Khodorkovskii, M., Konevega, A. L., Sergiev, P. V., Severinov, K., and Polikanov, Y. S. (2017) Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel. Nat Chem Biol. 10.1038/nchembio.2462
Durzynska, I., Xu, X., Adelmant, G., Ficarro, S. B., Marto, J. A., Sliz, P., Uljon, S., and Blacklow, S. C. (2017) STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1.. Structure. 25, 287-294
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
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
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2017) Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD(+)-dependent polynucleotide ligases. Proc Natl Acad Sci U S A. 114, 2592-2597
2016
Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Zhou, Q., Zhao, M., Brewster, A. S., Michels-Clark, T., Holton, J. M., Sauter, N. K., Weis, W. I., and Brunger, A. T. (2016) Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex. Elife. 10.7554/eLife.18740
Uddin, M. Jashim, Crews, B. C., Xu, S., Ghebreselasie, K., Daniel, C. K., Kingsley, P. J., Banerjee, S., and Marnett, L. J. (2016) Antitumor Activity of Cytotoxic Cyclooxygenase-2 Inhibitors. ACS Chem Biol. 11, 3052-3060
Unciuleac, M. - C., Smith, P. C., and Shuman, S. (2016) Crystal Structure and Biochemical Characterization of a Mycobacterium smegmatis AAA-Type Nucleoside Triphosphatase Phosphohydrolase (Msm0858). J Bacteriol. 198, 1521-33
Schormann, N., Ayres, C. A., Fry, A., Green, T. J., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2016) Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes. PLoS One. 11, e0165917
Uppalapati, M., Lee, D. Jun, Mandal, K., Li, H., Miranda, L. P., Lowitz, J., Kenney, J., Adams, J. J., Ault-Riché, D., Kent, S. B. H., and Sidhu, S. S. (2016) A Potent d-Protein Antagonist of VEGF-A is Nonimmunogenic, Metabolically Stable, and Longer-Circulating in Vivo. ACS Chem Biol. 11, 1058-65
Uljon, S., Xu, X., Durzynska, I., Stein, S., Adelmant, G., Marto, J. A., Pear, W. S., and Blacklow, S. C. (2016) Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure. 24, 687-696
Ye, Q., Ur, S. N., Su, T. Y., and Corbett, K. D. (2016) Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. EMBO J. 35, 2139-2151
2015
Zhou, Q., Lai, Y., Bacaj, T., Zhao, M., Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Brewster, A. S., Sauter, N. K., Cohen, A. E., S Soltis, M., Alonso-Mori, R., Chollet, M., Lemke, H. T., Pfuetzner, R. A., Choi, U. B., Weis, W. I., Diao, J., Südhof, T. C., and Brunger, A. T. (2015) Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis. Nature. 525, 62-7
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2015) Structure and two-metal mechanism of a eukaryal nick-sealing RNA ligase. Proc Natl Acad Sci U S A. 112, 13868-73
Jiang, J., Chan, H., Cash, D. D., Miracco, E. J., Loo, R. R. Ogorzale, Upton, H. E., Cascio, D., Johnson, R. O. 'Brien, Collins, K., Loo, J. A., Z Zhou, H., and Feigon, J. (2015) Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions. Science. 350, aab4070
2014
Lee, K. Sing Steph, Liu, J. - Y., Wagner, K. M., Pakhomova, S., Dong, H., Morisseau, C., Fu, S. H., Yang, J., Wang, P., Ulu, A., Mate, C. A., Nguyen, L. V., Hwang, S. Hee, Edin, M. L., Mara, A. A., Wulff, H., Newcomer, M. E., Zeldin, D. C., and Hammock, B. D. (2014) Optimized inhibitors of soluble epoxide hydrolase improve in vitro target residence time and in vivo efficacy. J Med Chem. 57, 7016-30
Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9
2013
Andersen, K. R., Onischenko, E., Tang, J. H., Kumar, P., Chen, J. Z., Ulrich, A., Liphardt, J. T., Weis, K., and Schwartz, T. U. (2013) Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors. Elife. 2, e00745

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