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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
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
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, 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
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., 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. (2014) The macular degeneration-linked C1QTNF5 (S163) mutation causes higher-order structural rearrangements. J Struct Biol. 186, 86-94
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, 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
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
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
Tripathi, S., Zhang, D., and Paukstelis, P. J. (2015) An intercalation-locked parallel-stranded DNA tetraplex. Nucleic Acids Res. 43, 1937-44
Tran, T. H., Christoffersen, S., Allan, P. W., Parker, W. B., Piskur, J., Serra, I., Terreni, M., and Ealick, S. E. (2011) The crystal structure of Streptococcus pyogenes uridine phosphorylase reveals a distinct subfamily of nucleoside phosphorylases. Biochemistry. 50, 6549-58
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
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
Trachman, R. J., Cojocaru, R., Wu, D., Piszczek, G., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2020) Structure-Guided Engineering of the Homodimeric Mango-IV Fluorescence Turn-on Aptamer Yields an RNA FRET Pair. Structure. 10.1016/j.str.2020.04.007
Trachman, R. J., Autour, A., C Y Jeng, S., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Garipov, R., Dolgosheina, E. V., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2019) Structure and functional reselection of the Mango-III fluorogenic RNA aptamer. Nat Chem Biol. 15, 472-479
Torrens-Spence, M. P., Chiang, Y. - C., Smith, T., Vicent, M. A., Wang, Y., and Weng, J. - K. (2020) Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins. Proc Natl Acad Sci U S A. 10.1073/pnas.1920097117
Torrens-Spence, M. Patrick, Liu, C. - T., Pluskal, T., Chung, Y. Kwan, and Weng, J. - K. (2018) Monoamine Biosynthesis via a Noncanonical Calcium-Activatable Aromatic Amino Acid Decarboxylase in Psilocybin Mushroom. ACS Chem Biol. 13, 3343-3353
Tormos, J. R., Taylor, A. B., S Daubner, C., P Hart, J., and Fitzpatrick, P. F. (2010) Identification of a hypothetical protein from Podospora anserina as a nitroalkane oxidase. Biochemistry. 49, 5035-41
Torbeev, V. Yu, Raghuraman, H., Hamelberg, D., Tonelli, M., Westler, W. M., Perozo, E., and Kent, S. B. H. (2011) Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc Natl Acad Sci U S A. 108, 20982-7
Toor, N., Rajashankar, K., Keating, K. S., and Pyle, A. Marie (2008) Structural basis for exon recognition by a group II intron. Nat Struct Mol Biol. 15, 1221-2
Toor, N., Keating, K. S., Fedorova, O., Rajashankar, K., Wang, J., and Pyle, A. Marie (2010) Tertiary architecture of the Oceanobacillus iheyensis group II intron. RNA. 16, 57-69
Toor, N., Keating, K. S., Taylor, S. D., and Pyle, A. Marie (2008) Crystal structure of a self-spliced group II intron. Science. 320, 77-82

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