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Thompson, M. C., Cascio, D., and Yeates, T. O. (2018) Microfocus diffraction from different regions of a protein crystal: structural variations and unit-cell polymorphism. Acta Crystallogr D Struct Biol. 74, 411-421
Thompson, M. C., Cascio, D., Leibly, D. J., and Yeates, T. O. (2015) An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein. Protein Sci. 24, 956-75
Thomaston, J. L., and DeGrado, W. F. (2016) Crystal structure of the drug-resistant S31N influenza M2 proton channel. Protein Sci. 25, 1551-4
Thomas, S. R., Keller, C. A., Szyk, A., Cannon, J. R., and Laronde-Leblanc, N. A. (2011) Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis. Nucleic Acids Res. 39, 2445-57
Thomas, S. R., McTamney, P. M., Adler, J. M., LaRonde-LeBlanc, N., and Rokita, S. E. (2009) Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands. J Biol Chem. 284, 19659-67
Thomä, N. H., Czyzewski, B. K., Alexeev, A. A., Mazin, A. V., Kowalczykowski, S. C., and Pavletich, N. P. (2005) Structure of the SWI2/SNF2 chromatin-remodeling domain of eukaryotic Rad54. Nat Struct Mol Biol. 12, 350-6
Thaler, J., Syroegin, E. A., Breuker, K., Polikanov, Y. S., and Micura, R. (2023) Practical Synthesis of -Formylmethionylated Peptidyl-tRNA Mimics. ACS Chem Biol. 10.1021/acschembio.3c00237
Teyra, J., Singer, A. U., Schmitges, F. W., Jaynes, P., Lui, S. Kit Leng, Polyak, M. J., Fodil, N., Krieger, J. R., Tong, J., Schwerdtfeger, C., Brasher, B. B., Ceccarelli, D. F. J., Moffat, J., Sicheri, F., Moran, M. F., Gros, P., Eichhorn, P. J. A., Lenter, M., Boehmelt, G., and Sidhu, S. S. (2019) Structural and Functional Characterization of Ubiquitin Variant Inhibitors of USP15. Structure. 27, 590-605.e5
Tessier, T. M., Chowdhury, A., Stekel, Z., Fux, J., Sartori, M. Augusta, Teyra, J., Jarvik, N., Chung, J., Kurinov, I., Sicheri, F., Sidhu, S. S., Singer, A. U., and Zhang, W. (2023) Structural and functional validation of a highly specific Smurf2 inhibitor. Protein Sci. 10.1002/pro.4885
Teron, K. I. Negron, and Das, C. (2023) Cocrystallization of ubiquitin-deubiquitinase complexes through disulfide linkage. Acta Crystallogr D Struct Biol. 79, 1044-1055
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Teplova, M., Hafner, M., Teplov, D., Essig, K., Tuschl, T., and Patel, D. J. (2013) Structure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sites. Genes Dev. 27, 928-40
Teplova, M., Song, J., Gaw, H. Yan, Teplov, A., and Patel, D. J. (2010) Structural insights into RNA recognition by the alternate-splicing regulator CUG-binding protein 1. Structure. 18, 1364-77
Teplova, M., and Patel, D. J. (2008) Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1. Nat Struct Mol Biol. 15, 1343-51
Teplova, M., Falschlunger, C., Krasheninina, O., Egger, M., Ren, A., Patel, D. J., and Micura, R. (2019) Crucial Roles of Two Hydrated Mg Ions in Reaction Catalysis of the Pistol Ribozyme. Angew Chem Int Ed Engl. 10.1002/anie.201912522
Teplova, M., Farazi, T. A., Tuschl, T., and Patel, D. J. (2016) Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS. Q Rev Biophys. 49, e1
Teng, M., Jiang, J., Ficarro, S. B., Seo, H. - S., Bae, J. Hyun, Donovan, K. A., Fischer, E. S., Zhang, T., Dhe-Paganon, S., Marto, J. A., and Gray, N. S. (2021) Exploring Ligand-Directed -Acyl--alkylsulfonamide-Based Acylation Chemistry for Potential Targeted Degrader Development. ACS Med Chem Lett. 12, 1302-1307
Teng, P. K., Anderson, N. J., Goldschmidt, L., Sawaya, M. R., Sambashivan, S., and Eisenberg, D. (2012) Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation. Protein Sci. 21, 26-37
Tei, R., Bagde, S. R., J Fromme, C., and Baskin, J. M. (2023) Activity-based directed evolution of a membrane editor in mammalian cells. Nat Chem. 15, 1030-1039
Taylor, A. B., Pica-Mattoccia, L., Polcaro, C. M., Donati, E., Cao, X., Basso, A., Guidi, A., Rugel, A. R., Holloway, S. P., Anderson, T. J. C., P Hart, J., Cioli, D., and LoVerde, P. T. (2015) Structural and Functional Characterization of the Enantiomers of the Antischistosomal Drug Oxamniquine. PLoS Negl Trop Dis. 9, e0004132
Taylor, A. B., Roberts, K. M., Cao, X., Clark, N. E., Holloway, S. P., Donati, E., Polcaro, C. M., Pica-Mattoccia, L., Tarpley, R. S., McHardy, S. F., Cioli, D., LoVerde, P. T., Fitzpatrick, P. F., and P Hart, J. (2017) Structural and enzymatic insights into species-specific resistance to schistosome parasite drug therapy. J Biol Chem. 292, 11154-11164
Taylor, S. K., Tran, T. H., Liu, M. Z., Harris, P. E., Sun, Y., Jambawalikar, S. R., Tong, L., and Stojanovic, M. N. (2018) Insulin Hexamer-Caged Gadolinium Ion as MRI Contrast-o-phore. Chemistry. 24, 10646-10652
Taylor, N. D., Garruss, A. S., Moretti, R., Chan, S., Arbing, M. A., Cascio, D., Rogers, J. K., Isaacs, F. J., Kosuri, S., Baker, D., Fields, S., Church, G. M., and Raman, S. (2016) Engineering an allosteric transcription factor to respond to new ligands. Nat Methods. 13, 177-83
Tayeb-Fligelman, E., Bowler, J. T., Tai, C. E., Sawaya, M. R., Jiang, Y. Xiao, Garcia, G., Griner, S. L., Cheng, X., Salwinski, L., Lutter, L., Seidler, P. M., Lu, J., Rosenberg, G. M., Hou, K., Abskharon, R., Pan, H., Zee, C. - T., Boyer, D. R., Li, Y., Anderson, D. H., Murray, K. A., Falcon, G., Cascio, D., Saelices, L., Damoiseaux, R., Arumugaswami, V., Guo, F., and Eisenberg, D. S. (2023) Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils. Nat Commun. 14, 2379
Tayeb-Fligelman, E., Cheng, X., Tai, C., Bowler, J. T., Griner, S., Sawaya, M. R., Seidler, P. M., Jiang, Y. Xiao, Lu, J., Rosenberg, G. M., Salwinski, L., Abskharon, R., Zee, C. - T., Hou, K., Li, Y., Boyer, D. R., Murray, K. A., Falcon, G., Anderson, D. H., Cascio, D., Saelices, L., Damoiseaux, R., Guo, F., and Eisenberg, D. S. (2021) Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 10.1101/2021.03.05.434000