Publikace
Researcher ID: B-7142-2012 |
2014
Kosek, D., Kylarova, S., Psenakova, K., Rezabkova, L., Herman, P., Vecer, J., Obsilova, V., Obsil, T. (2014). Biophysical and Structural Characterization of the Thioredoxin-Binding Domain of Protein Kinase ASK1 and its Interaction with Reduced Thioredoxin.
J. Biol. Chem. 289, 24463-24474. Abstract
Kopecka, M., Kosek, D., Kukacka, Z., Rezabkova, L., Man, P., Novak, P., Obsil, T., Obsilova, V. (2014). Role of the EF-hand like motif in the 14-3-3 protein-mediated activation of yeast neutral trehalase Nth1.
J. Biol. Chem. 289, 13948-13961. Abstract
Obsilova, V., Kopecka, M., Kosek, D., Kacirova, M., Kylarova, S., Rezabkova, L., Obsil, T. (2014). Mechanisms of the 14-3-3 protein function: regulation of protein function through conformational modulation.
Physiol. Res. 63 Suppl. 1, 155-164. Abstract
2013
Vacha, P., Zuskova, I., Bumba, L., Herman, P., Vecer, J., Obsilova, V., Obsil, T. (2013). Detailed kinetic analysis of the interaction between the FOXO4-DNA-binding domain and DNA.
Biophys. Chem. 184C, 68-78. Abstract
Macakova, E., Kopecka, M., Kukacka, Z., Veisova, D., Novak, P., Man, P., Obsil, T., Obsilova, V. (2013). Structural basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Biochim. Biophys. Acta 1830(10), 4491-4499. Abstract
2012
Veisova, D. Macakova, E., Rezabkova, L., Sulc, M., Vacha, P., Sychrova, H., Obsil, T., Obsilova, V. (2012). Role of individual phosphorylation sites for the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Biochem. J. 443(3), 663-670. Abstract
Rezabkova, L., Kacirova, M. Sulc, M., Herman, P., Vecer, J., Stepanek, M., Obsilova, V., Obsil, T. (2012). Role of individual phosphorylation sites for the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Biophys. J. 103(9), 1960-1969 Abstract
2011
Rezabkova, L., Man, P., Novak, P., Herman, P., Vecer, J., Obsilova, V., Obsil, T. (2011). Structural basis for the 14-3-3 protein-dependent inhibition of the regulator of G-Protein signaling 3 (RGS3) function.
J. Biol. Chem. 286(50), 43527-43536. Abstract
Obsil, T., Obsilova, V. (2011). Structural basis of 14-3-3 protein functions.
Semin. Cell. Dev. Biol. 22, 663-672. Abstract
Obsil, T., Obsilova, V. (2011). Structural basis for DNA recognition by FOXO proteins.
Biochim. Biophys. Acta 1813(11), 1946-1953. Abstract
Coddou, C., Yan, Z., Obsil, T., Huidobro-Toro, J.P., Stojilkovic, S.S. (2011).Activation and regulation of purinergic P2X receptor channels.
Pharmacol. Rev. 63(3), 641-683. Abstract
Valis, K., Prochazka, L., Boura, E., Chladova, J., Obsil, T., Rohlena, J., Truksa, J., Dong, L.F., Ralph, S.J., Neuzil, J. (2011). Hippo/Mst1 stimulates transcription of the proapoptotic mediator NOXA in a FoxO1-dependent manner.
Cancer Res. 71(3), 946-954. Abstract
2010
Veisova, D., Rezabkova, L., Stepanek, M., Novotna, P., Herman, P., Vecer, J., Obsil, T., Obsilova, V. (2010). C-terminal segment of yeast BMH proteins exhibits different structure compared to other 14-3-3 protein isoforms.
Biochemistry 49(18), 3853-3861. Abstract
Rezabkova, L., Boura, E., Herman, P., Vecer, J., Bourova, L., Sulc, M., Svoboda, P., Obsilova, V., Obsil, T. (2010). 14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G-protein signaling 3 (RGS3).
J. Struct. Biol. 170(3), 451-461. Abstract
Boura, E., Rezabkova, L., Brynda, J., Obsilova, V., Obsil, T. (2010). Structure of the human FOXO4-DBD-DNA complex at 1.9 A resolution reveals new details of FOXO binding to the DNA.
Acta Cryst. D66, 1351-1357. Abstract
2009
Silhan, J., Vacha, P., Strnadova, P., Vecer, J., Herman, P., Sulc, M., Teisinger, J., Obsilova, V., Obsil, T. (2009). 14-3-3 Protein Masks the DNA Binding Interface of Forkhead Transcription Factor FOXO4.
J. Biol. Chem. 284(29), 19349-60. Abstract
Jindrichova, M., Vavra, V., Obsil, T., Stojilkovic, S.S., Zemkova, H. (2009). Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors.
J. Neurochem. 109(3), 923-934. Abstract
2008
Obsil, T., Obsilova, V. (2008). Structure/function relationships underlying regulation of FOXO transcription factors.
Oncogene 27, 2263-2275. Abstract
Obsilova, V., Nedbalkova, E., Silhan, J., Boura, E., Herman, P., Vecer, J., Sulc, M., Teisinger, J., Dyda, F., Obsil,T. (2008). The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase.
Biochemistry 47, 1168-1777. Abstract
Jelinkova, I., Vavra, V., Jindrichova, M., Obsil, T., Zemkova, H.W., Zemkova, H., Stojilkovic, S.S. (2008). Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin.
Pflugers Arch. 456,939-950. Abstract
Mazna, P., Grycova, L., Balik, A., Zamkova, H., Friedlova, E., Obsilova, V., Obsil, T., Teisinger, J. (2008). The role of proline residues in the structure and function of human MT2 melatonin receptor.
J. Pineal Res. 45(4) ,361-372. Abstract
2007
Boura, E., Silhan, J., Herman, P., Vecer, J., Sulc, M., Teisinger, J., Obsilova, V., Obsil,T. (2007). Both N-terminal loop and wing W2 of forkhead domain of transcription factor FoxO4 are important for DNA binding.
J. Biol. Chem. 282(11) , 8265-75. Abstract
Grycova, L., Lansky, Z., Friedlova, E., Vlachova, V., Kubala, M., Obsilova, V., Obsil,T., Teisinger, J. (2007). ATP binding site on the C-terminus of the vanilloid receptor.
Arch. Biochem. Biophys. 465(2) , 389-98. Abstract
2006
Yan, Z., Liang, Z., Obsil,T., Stojilkovic, S.S. (2006). Participation of the lys313-ile333 sequence of the P2X4 receptor in agonist binding and transduction of signals to the channel gate.
J. Biol. Chem. 281(43) , 32649-59. Abstract
2005
Obsilova, V., Vecer, V., Herman, P., Pabianova, A., Sulc, M., Teisinger, J., Boura, E., Obsil,T. (2005). 14-3-3 protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4.
Biochemistry 44, 11608-11617. Abstract
Yan, Z., Liang, Z., Tomic, M., Obsil,T., Stojilkovic, S.S. (2005). Molecular determinants of the agonist binding domain of a P2X receptor channel.
Mol. Pharmacol. 67, 1078-1088. Abstract
Mazna, P., Berka, K., Jelinkova, I., Balik, A., Svoboda, P., Obsilova, V., Obsil,T., Teisinger, J. (2005). Ligand binding to the human MT2 melatonin receptor: The role of residues in transmembrane domains 3, 6, and 7.
Biochem. Biophys. Res. Commun. 332, 726-734. Abstract
2004
Silhan, J., Obsilova, V., Vecer, J., Herman, P., Sulc, M., Teisinger, J., Obsil, T. (2004). 14-3-3 Protein C-terminal Stretch Occupies Ligand Binding Groove and Is Displaced by Phosphopeptide Binding.
J. Biol. Chem. 279, 49113-49119. Abstract
Obsilova, V., Herman, P., Vecer, J., Sulc, M., Teisinger, J., Obsil, T. (2004). 14-3-3 C-Terminal Stretch Changes its Conformation upon Ligand Binding and Phosphorylation at Thr232.
J. Biol. Chem. 279, 4531-4540. Abstract
Mazna, P., Obsilova, V., Jelinkova, I., Balik, A., Berka, K., Sovova, Z., Ettrich , R., Svoboda, P., Obsil, T., Teisinger, J. (2004). Molecular modeling of human MT2 melatonin receptor: the role of Val204, Leu272 and Tyr298 in ligand binding.
J. Neurochem. 91, 836-842. Abstract
2003
Obsil, T., Ghirlando, R., Anderson, D.E., Hickman, A.B., Dyda, F. (2003). Two 14-3-3 Binding Motifs Are Required for Stable Association of Forkhead Transcription Factor FOXO4 with 14-3-3 Proteins and Inhibition of DNA Binding.
Biochemistry 42, 15264-15272. Abstract
2002
Klein D.C., Ganguly S., Coon S., Weller J.L., Obsil T., Hickman A., Dyda F. (2002). 14-3-3 Proteins and photoneuroendocrine transduction: role in controlling the daily rhythm in melatonin.
Biochem. Soc. Trans. 30, 365-373. Abstract
2001
Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F. (2001). Crystal Structure of the 14-3-3:Serotonin N-Acetyltransferase Complex: A Role of Scaffolding in Enzyme Regulation.
Cell 105, 257-267. Abstract
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., Beauverger P., Ferry G., Boutin J.A., Klein D.C. (2001) Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis.
Proc. Natl. Acad. Sci. U S A 98, 8083-8088. Abstract
Akce dokumentů