Found 2727 results
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Travis, S., Green, K. D., Gilbert, N. C., Tsodikov, O. V., Garneau-Tsodikova, S., and Thompson, M. K. (2023) Inhibition of Fosfomycin Resistance Protein FosB from Gram-Positive Pathogens by Phosphonoformate. Biochemistry. 62, 109-117
Tripathi, S., Zhang, D., and Paukstelis, P. J. (2015) An intercalation-locked parallel-stranded DNA tetraplex. Nucleic Acids Res. 43, 1937-44
Tripathi, S., and Paukstelis, P. J. (2016) Structural Implications of Homopyrimidine Base Pairs in the Parallel-Stranded d(YGA) Motif. Chembiochem. 17, 1177-83
Tripathi, A., Mandon, E. C., Gilmore, R., and Rapoport, T. A. (2017) Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins. J Biol Chem. 292, 8007-8018
Truong, L., Kooshapur, H., Dey, S. Kumar, Li, X., Tjandra, N., Jaffrey, S. R., and Ferré-D'Amaré, A. R. (2021) The fluorescent aptamer Squash extensively repurposes the adenine riboswitch fold. Nat Chem Biol. 10.1038/s41589-021-00931-2
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
Tsai, W. - W., Wang, Z., Yiu, T. T., Akdemir, K. C., Xia, W., Winter, S., Tsai, C. - Y., Shi, X., Schwarzer, D., Plunkett, W., Aronow, B., Gozani, O., Fischle, W., Hung, M. - C., Patel, D. J., and Barton, M. Craig (2010) TRIM24 links a non-canonical histone signature to breast cancer. Nature. 468, 927-32
Tsai, W. - C., Gilbert, N. C., Ohler, A., Armstrong, M., Perry, S., Kalyanaraman, C., Yasgar, A., Rai, G., Simeonov, A., Jadhav, A., Standley, M., Lee, H. - W., Crews, P., Iavarone, A. T., Jacobson, M. P., Neau, D. B., Offenbacher, A. R., Newcomer, M., and Holman, T. R. (2021) Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2. Bioorg Med Chem. 46, 116349
Tsai, Y., Sawaya, M. R., and Yeates, T. O. (2009) Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C. Acta Crystallogr D Biol Crystallogr. 65, 980-8
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
Tu, D., Zhu, Z., Zhou, A. Y., Yun, C. -hong, Lee, K. - E., Toms, A. V., Li, Y., Dunn, G. P., Chan, E., Thai, T., Yang, S., Ficarro, S. B., Marto, J. A., Jeon, H., Hahn, W. C., Barbie, D. A., and Eck, M. J. (2013) Structure and ubiquitination-dependent activation of TANK-binding kinase 1. Cell Rep. 3, 747-58
Tu, D., Li, Y., Song, H. Kyu, Toms, A. V., Gould, C. J., Ficarro, S. B., Marto, J. A., Goode, B. L., and Eck, M. J. (2011) Crystal structure of a coiled-coil domain from human ROCK I. PLoS One. 6, e18080
Tu, X., and Palczewski, K. (2012) Crystal structure of the globular domain of C1QTNF5: Implications for late-onset retinal macular degeneration. J Struct Biol. 180, 439-46
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
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. (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