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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
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
Thomaston, J. L., and DeGrado, W. F. (2016) Crystal structure of the drug-resistant S31N influenza M2 proton channel. Protein Sci. 25, 1551-4
Thompson, M. C., Wheatley, N. M., Jorda, J., Sawaya, M. R., Gidaniyan, S. D., Ahmed, H., Yang, Z., McCarty, K. N., Whitelegge, J. P., and Yeates, T. O. (2014) Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein. J Mol Biol. 426, 3287-304
Thompson, M. C., Crowley, C. S., Kopstein, J., Bobik, T. A., and Yeates, T. O. (2014) Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 70, 1584-90
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
Thorsen, M. K., Draganova, E. B., and Heldwein, E. E. (2022) The nuclear egress complex of Epstein-Barr virus buds membranes through an oligomerization-driven mechanism. PLoS Pathog. 18, e1010623
Tian, Y., Simanshu, D. K., Ma, J. - B., and Patel, D. J. (2011) Structural basis for piRNA 2'-O-methylated 3'-end recognition by Piwi PAZ (Piwi/Argonaute/Zwille) domains. Proc Natl Acad Sci U S A. 108, 903-10
Tian, Y., Simanshu, D. K., Ma, J. - B., Park, J. - E., Heo, I., V Kim, N., and Patel, D. J. (2014) A phosphate-binding pocket within the platform-PAZ-connector helix cassette of human Dicer. Mol Cell. 53, 606-16
Tian, Y., Simanshu, D. K., Ascano, M., Diaz-Avalos, R., Park, A. Young, Juranek, S. A., Rice, W. J., Yin, Q., Robinson, C. V., Tuschl, T., and Patel, D. J. (2011) Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex. Nat Struct Mol Biol. 18, 658-64
Tkacik, E., Li, K., Del Pino, G. Gonzalez-, Ha, B. Hak, Vinals, J., Park, E., Beyett, T. S., and Eck, M. J. (2023) Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib. J Biol Chem. 299, 104634
To, C., Jang, J., Chen, T., Park, E., Mushajiang, M., De Clercq, D. J. H., Xu, M., Wang, S., Cameron, M. D., Heppner, D. E., Shin, B. Hee, Gero, T. W., Yang, A., Dahlberg, S. E., Wong, K. - K., Eck, M. J., Gray, N. S., and Jänne, P. A. (2019) Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor. Cancer Discov. 9, 926-943
To, C., Beyett, T. S., Jang, J., Feng, W. W., Bahcall, M., Haikala, H. M., Shin, B. H., Heppner, D. E., Rana, J. K., Leeper, B. A., Soroko, K. M., Poitras, M. J., Gokhale, P. C., Kobayashi, Y., Wahid, K., Kurppa, K. J., Gero, T. W., Cameron, M. D., Ogino, A., Mushajiang, M., Xu, C., Zhang, Y., Scott, D. A., Eck, M. J., Gray, N. S., and Jänne, P. A. (2022) An allosteric inhibitor against the therapy-resistant mutant forms of EGFR in non-small cell lung cancer. Nat Cancer. 3, 402-417
Todd, R. C., and Lippard, S. J. (2010) Consequences of cisplatin binding on nucleosome structure and dynamics. Chem Biol. 17, 1334-43
W Tolbert, D., Graham, D. E., White, R. H., and Ealick, S. E. (2003) Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms. Structure. 11, 285-94
Tomasic, I. B., Metcalf, M. C., Guce, A. I., Clark, N. E., and Garman, S. C. (2010) Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases. J Biol Chem. 285, 21560-6
Tompkins, K. J., Houtti, M., Litzau, L. A., Aird, E. J., Everett, B. A., Nelson, A. T., Pornschloegl, L., Limón-Swanson, L. K., Evans, R. L., Evans, K., Shi, K., Aihara, H., and Gordon, W. R. (2021) Molecular underpinnings of ssDNA specificity by Rep HUH-endonucleases and implications for HUH-tag multiplexing and engineering. Nucleic Acids Res. 49, 1046-1064
Toms, A. V., Kinsland, C., McCloskey, D. E., Pegg, A. E., and Ealick, S. E. (2004) Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase. J Biol Chem. 279, 33837-46
Toms, A. V., Deshpande, A., McNally, R., Jeong, Y., Rogers, J. M., Kim, C. Un, Gruner, S. M., Ficarro, S. B., Marto, J. A., Sattler, M., Griffin, J. D., and Eck, M. J. (2013) Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases. Nat Struct Mol Biol. 20, 1221-3
Toms, A. V., Haas, A. L., Park, J. - H., Begley, T. P., and Ealick, S. E. (2005) Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II. Biochemistry. 44, 2319-29
Tookmanian, E. M., Phillips-Piro, C. M., Fenlon, E. E., and Brewer, S. H. (2015) Azidoethoxyphenylalanine as a Vibrational Reporter and Click Chemistry Partner in Proteins. Chemistry. 21, 19096-103
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

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