Publications

Found 8 results
Filters: Author is Micura, Ronald  [Clear All Filters]
Journal Article
Danhart, E. M., Bakhtina, M., Cantara, W. A., Kuzmishin, A. B., Ma, X., Sanford, B. L., Vargas-Rodriguez, O., Košutić, M., Goto, Y., Suga, H., Nakanishi, K., Micura, R., Foster, M. P., and Musier-Forsyth, K. (2017) Conformational and chemical selection by a -acting editing domain. Proc Natl Acad Sci U S A. 114, E6774-E6783
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
Zheng, L., Falschlunger, C., Huang, K., Mairhofer, E., Yuan, S., Wang, J., Patel, D. J., Micura, R., and Ren, A. (2019) Hatchet ribozyme structure and implications for cleavage mechanism. Proc Natl Acad Sci U S A. 10.1073/pnas.1902413116
Ren, A., Košutić, M., Rajashankar, K. R., Frener, M., Santner, T., Westhof, E., Micura, R., and Patel, D. J. (2014) In-line alignment and Mg²⁺ coordination at the cleavage site of the env22 twister ribozyme.. Nat Commun. 5, 5534
Melnikov, S. V., Khabibullina, N. F., Mairhofer, E., Vargas-Rodriguez, O., Reynolds, N. M., Micura, R., Söll, D., and Polikanov, Y. S. (2018) Mechanistic insights into the slow peptide bond formation with D-amino acids in the ribosomal active site. Nucleic Acids Res. 10.1093/nar/gky1211
Košutić, M., Neuner, S., Ren, A., Flür, S., Wunderlich, C., Mairhofer, E., Vušurović, N., Seikowski, J., Breuker, K., Höbartner, C., Patel, D. J., Kreutz, C., and Micura, R. (2015) A Mini-Twister Variant and Impact of Residues/Cations on the Phosphodiester Cleavage of this Ribozyme Class. Angew Chem Int Ed Engl. 54, 15128-15133
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
Syroegin, E. A., Flemmich, L., Klepacki, D., Vázquez-Laslop, N., Micura, R., and Polikanov, Y. S. (2022) Structural basis for the context-specific action of the classic peptidyl transferase inhibitor chloramphenicol. Nat Struct Mol Biol. 29, 152-161