Publications

Found 2924 results
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Teron, K. I. Negron, and Das, C. (2023) Cocrystallization of ubiquitin-deubiquitinase complexes through disulfide linkage. Acta Crystallogr D Struct Biol. 79, 1044-1055
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
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
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
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., 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
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
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., 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
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., 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., 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
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., 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
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
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., 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
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
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., 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

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