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doc. RNDr. Tomáš Obšil, Ph.D.
Researcher ID: B-7142-2012


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


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


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


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


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


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


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


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


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


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


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


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


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


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

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