Publications

Found 15 results
Filters: Author is Tuschl, Thomas  [Clear All Filters]
Journal Article
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
Gao, P., Ascano, M., Zillinger, T., Wang, W., Dai, P., Serganov, A. A., Gaffney, B. L., Shuman, S., Jones, R. A., Deng, L., Hartmann, G., Barchet, W., Tuschl, T., and Patel, D. J. (2013) Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA. Cell. 154, 748-62
Sheng, G., Gogakos, T., Wang, J., Zhao, H., Serganov, A., Juranek, S., Tuschl, T., Patel, D. J., and Wang, Y. (2017) Structure/cleavage-based insights into helical perturbations at bulge sites within T. thermophilus Argonaute silencing complexes. Nucleic Acids Res. 45, 9149-9163
Wang, Y., Sheng, G., Juranek, S., Tuschl, T., and Patel, D. J. (2008) Structure of the guide-strand-containing argonaute silencing complex. Nature. 456, 209-13
Wang, Y., Juranek, S., Li, H., Sheng, G., Tuschl, T., and Patel, D. J. (2008) Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex. Nature. 456, 921-6
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
Vincent, J., Adura, C., Gao, P., Luz, A., Lama, L., Asano, Y., Okamoto, R., Imaeda, T., Aida, J., Rothamel, K., Gogakos, T., Steinberg, J., Reasoner, S., Aso, K., Tuschl, T., Patel, D. J., J Glickman, F., and Ascano, M. (2017) Small molecule inhibition of cGAS reduces interferon expression in primary macrophages from autoimmune mice. Nat Commun. 8, 750
Wang, Y., Juranek, S., Li, H., Sheng, G., Wardle, G. S., Tuschl, T., and Patel, D. J. (2009) Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes. Nature. 461, 754-61
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
Xie, W., Lama, L., Adura, C., Tomita, D., J Glickman, F., Tuschl, T., and Patel, D. J. (2019) Human cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation. Proc Natl Acad Sci U S A. 116, 11946-11955
Nakanishi, K., Ascano, M., Gogakos, T., Ishibe-Murakami, S., Serganov, A. A., Briskin, D., Morozov, P., Tuschl, T., and Patel, D. J. (2013) Eukaryote-specific insertion elements control human ARGONAUTE slicer activity. Cell Rep. 3, 1893-900
Lama, L., Adura, C., Xie, W., Tomita, D., Kamei, T., Kuryavyi, V., Gogakos, T., Steinberg, J. I., Miller, M., Ramos-Espiritu, L., Asano, Y., Hashizume, S., Aida, J., Imaeda, T., Okamoto, R., Jennings, A. J., Michino, M., Kuroita, T., Stamford, A., Gao, P., Meinke, P., J Glickman, F., Patel, D. J., and Tuschl, T. (2019) Development of human cGAS-specific small-molecule inhibitors for repression of dsDNA-triggered interferon expression. Nat Commun. 10, 2261
Gao, P., Ascano, M., Wu, Y., Barchet, W., Gaffney, B. L., Zillinger, T., Serganov, A. A., Liu, Y., Jones, R. A., Hartmann, G., Tuschl, T., and Patel, D. J. (2013) Cyclic [G(2',5')pA(3',5')p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase. Cell. 153, 1094-107
Gao, P., Zillinger, T., Wang, W., Ascano, M., Dai, P., Hartmann, G., Tuschl, T., Deng, L., Barchet, W., and Patel, D. J. (2014) Binding-pocket and lid-region substitutions render human STING sensitive to the species-specific drug DMXAA. Cell Rep. 8, 1668-1676
Xie, W., Lama, L., Yang, X., Kuryavyi, V., Bhattacharya, S., Nudelman, I., Yang, G., Ouerfelli, O., J Glickman, F., Jones, R. A., Tuschl, T., and Patel, D. J. (2023) Arabinose- and xylose-modified analogs of 2',3'-cGAMP act as STING agonists. Cell Chem Biol. 10.1016/j.chembiol.2023.07.002