Publications

Found 2797 results
Filters: Shipping is   [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
T
Tu, X., and Palczewski, K. (2014) The macular degeneration-linked C1QTNF5 (S163) mutation causes higher-order structural rearrangements. J Struct Biol. 186, 86-94
Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L., and Eck, M. J. (2012) Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc Natl Acad Sci U S A. 109, E3424-33
Turlington, Z. R., de Macedo, S. Vaz Ferrei, Perry, K., Belsky, S. L., Faust, J. A., Snider, M. J., and Hicks, K. A. (2023) Ligand bound structure of a 6-hydroxynicotinic acid 3-monooxygenase provides mechanistic insights. Arch Biochem Biophys. 752, 109859
Tuukkanen, A. T., Freire, D., Chan, S., Arbing, M. A., Reed, R. W., Evans, T. J., Zenkeviciutė, G., Kim, J., Kahng, S., Sawaya, M. R., Chaton, C. T., Wilmanns, M., Eisenberg, D., Parret, A. H. A., and Korotkov, K. V. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 10.1016/j.jmb.2018.11.003
Tyler, R. C., Bitto, E., Berndsen, C. E., Bingman, C. A., Singh, S., Lee, M. S., Wesenberg, G. E., Denu, J. M., Phillips, G. N., and Markley, J. L. (2006) Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family. Biochemistry. 45, 14325-36
U
Ubah, O. C., Lake, E. W., Gunaratne, G. S., Gallant, J. P., Fernie, M., Robertson, A. J., Marchant, J. S., Bold, T. D., Langlois, R. A., Matchett, W. E., Thiede, J. M., Shi, K., Yin, L., Moeller, N. H., Banerjee, S., Ferguson, L., Kovaleva, M., Porter, A. J., Aihara, H., LeBeau, A. M., and Barelle, C. J. (2021) Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography. Nat Commun. 12, 7325
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
Uddin, M. Jashim, Xu, S., Crews, B. C., Aleem, A. M., Ghebreselasie, K., Banerjee, S., and Marnett, L. J. (2020) Harmaline Analogs as Substrate-Selective Cyclooxygenase-2 Inhibitors. ACS Med Chem Lett. 11, 1881-1885
Uervirojnangkoorn, M., Lyubimov, A. Y., Zhou, Q., Weis, W. I., and Brunger, A. T. (2019) Resolving indexing ambiguities in X-ray free-electron laser diffraction patterns. Acta Crystallogr D Struct Biol. 75, 234-241
Ujwal, R., Cascio, D., Colletier, J. - P., Faham, S., Zhang, J., Toro, L., Ping, P., and Abramson, J. (2008) The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A. 105, 17742-7
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
Ultsch, M., Li, W., Eigenbrot, C., Di Lello, P., Lipari, M. T., Gerhardy, S., AhYoung, A. P., Quinn, J., Franke, Y., Chen, Y., M Beltran, K., Peterson, A., and Kirchhofer, D. (2019) Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. J Mol Biol. 431, 885-903
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2019) Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates. J Biol Chem. 10.1074/jbc.RA119.007445
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
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
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2020) Caveat mutator: alanine substitutions for conserved amino acids in RNA ligase elicit unexpected rearrangements of the active site for lysine adenylylation. Nucleic Acids Res. 10.1093/nar/gkaa238
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
Unger, E. K., Keller, J. P., Altermatt, M., Liang, R., Matsui, A., Dong, C., Hon, O. J., Yao, Z., Sun, J., Banala, S., Flanigan, M. E., Jaffe, D. A., Hartanto, S., Carlen, J., Mizuno, G. O., Borden, P. M., Shivange, A. V., Cameron, L. P., Sinning, S., Underhill, S. M., Olson, D. E., Amara, S. G., Lang, D. Temple, Rudnick, G., Marvin, J. S., Lavis, L. D., Lester, H. A., Alvarez, V. A., Fisher, A. J., Prescher, J. A., Kash, T. L., Yarov-Yarovoy, V., Gradinaru, V., Looger, L. L., and Tian, L. (2020) Directed Evolution of a Selective and Sensitive Serotonin Sensor via Machine Learning. Cell. 183, 1986-2002.e26
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
Uson, M. Loressa, Carl, A., Goldgur, Y., and Shuman, S. (2018) Crystal structure and mutational analysis of Mycobacterium smegmatis FenA highlight active site amino acids and three metal ions essential for flap endonuclease and 5' exonuclease activities. Nucleic Acids Res. 10.1093/nar/gky238
Uysal, S., Cuello, L. G., D Cortes, M., Koide, S., Kossiakoff, A. A., and Perozo, E. (2011) Mechanism of activation gating in the full-length KcsA K+ channel. Proc Natl Acad Sci U S A. 108, 11896-9
V
Vaccaro, F. A., Born, D. A., and Drennan, C. L. (2023) Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery. Proc Natl Acad Sci U S A. 120, e2214085120
Vaidya, A. T., Chen, C. - H., Dunlap, J. C., Loros, J. J., and Crane, B. R. (2011) Structure of a light-activated LOV protein dimer that regulates transcription. Sci Signal. 4, ra50
Vaidya, A. T., Lomakin, I. B., Joseph, N. N., Dmitriev, S. E., and Steitz, T. A. (2017) Crystal Structure of the C-terminal Domain of Human eIF2D and its Implications on Eukaryotic Translation Initiation. J Mol Biol. 10.1016/j.jmb.2017.07.015
Vaisey, G., Miller, A. N., and Long, S. B. (2016) Distinct regions that control ion selectivity and calcium-dependent activation in the bestrophin ion channel. Proc Natl Acad Sci U S A. 113, E7399-E7408

Pages