OBSIL GROUP
Biophysical Chemistry of Protein Complexes

Author: Year: Journal:


Selected publications
Honzejkova, K., Kosek, D., Obsilova, V., Obsil, T.
The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1.
Elife . 2024 Mar 27:13:RP95199. doi: 10.7554/eLife.95199.
IF = 7.7
Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T.
14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices.
Protein Sci. 2023 Oct 10:e4805. doi: 10.1002/pro.4805
IF = 8
Obsilova V and Obsil T
Structural insights into the functional roles of 14-3-3 proteins
Front. Mol. Biosci., 16 September 2022 Sec. Structural Biology https://doi.org/10.3389/fmolb.2022.1016071
IF = 6.113
Mandal R, Kohoutova K, Petrvalska O, Horvath M, Srb P, Veverka V, Obsilova V, Obsil T
FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA.
Protein Sci. 2022 May;31(5):e4287. doi: 10.1002/pro.4287.
IF = 6.725
Publications by year

2024

Honzejkova, K., Kosek, D., Obsilova, V., Obsil, T.
The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1.
Elife . 2024 Mar 27:13:RP95199. doi: 10.7554/eLife.95199.
IF = 7.7
Obsilova V, Obsil T
The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways
Front. Mol. Biosci. 11 | https://doi.org/10.3389/fmolb.2024.1327014
IF = 5

2023

Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T.
14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices.
Protein Sci. 2023 Oct 10:e4805. doi: 10.1002/pro.4805
IF = 8
Somsen BA, Sijbesma E, Leysen S, Honzejkova K, Visser EJ, Cossar PJ, Obsil T, Brunsveld L, Ottmann C.
Molecular basis and dual ligand regulation of tetrameric estrogen receptor alpha/14-3-3z protein complex
J Biol Chem. 2023 Jul; 299(7): 104855.
IF = 4.8

2022

Obsilova V and Obsil T
Structural insights into the functional roles of 14-3-3 proteins
Front. Mol. Biosci., 16 September 2022 Sec. Structural Biology https://doi.org/10.3389/fmolb.2022.1016071
IF = 6.113
Kohoutova K, Docekal V, Ausserlechner MJ, Kaiser N, Tekel A, Mandal R, Horvath M, Obsilova V, Vesely J, Hagenbuchner J and Obsil T
Lengthening the Guanidine–Aryl Linker of Phenylpyrimidinylguanidines Increases Their Potency as Inhibitors of FOXO3-Induced Gene Transcription
ACS Omega 2022, 7, 38, 34632–34646
IF = 4.132
Mandal R, Kohoutova K, Petrvalska O, Horvath M, Srb P, Veverka V, Obsilova V, Obsil T
FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA.
Protein Sci. 2022 May;31(5):e4287. doi: 10.1002/pro.4287.
IF = 6.725
Joshi R, Pohl P, Strachotova D, Herman P, Obsil T, Obsilova V.
Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains.
Biophys J . 2022 Apr 5;121(7):1299-1311. doi: 10.1016/j.bpj.2022.02.025
IF = 4.033

2021

Leysen S, Burnley RJ, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Zoghbi HY, Ottmann C, Davis JM
A Structural Study of the Cytoplasmic Chaperone Effect of 14-3-3 Proteins on Ataxin-1.
J Mol Biol . 2021 Jul 21;433(19):167174. doi: 10.1016/j.jmb.2021.167174
IF = 5.469
Horvath M, Petrvalska O, Herman P, Obsilova V, Obsil T
14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites.
Commun Biol . 2021 Aug 19;4(1):986. doi: 10.1038/s42003-021-02518-y
IF = 6.268
Pohl P, Joshi R, Petrvalska O, Obsil T, Obsilova V
14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains.
Commun. Biol. (2021) 4:899, DOI : 10.1038/s42003-021-02419-0
IF = 6.268
Neves JF, Petrvalska O, Bosica F, Cantrelle FX, Merzougui H, Obsil T, Landrieu I
Phosphorylated full-length Tau interacts with 14-3-3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14-3-3 dimer.
FEBS J . 2021 Mar;288(6):1918-1934.
IF = 5.542

2020

Obsilova V, Obsil T.
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases.
Int J Mol Sci.
IF = 4.556
Lentini Santo D, Petrvalska O, Obsilova V, Ottmann C, Obsil T
Stabilization of Protein-Protein Interactions between CaMKK2 and 14-3-3 by Fusicoccins
ACS Chem. Biol. 2020 Nov 4. doi: 10.1021/acschembio.0c00821.
IF = 4.434
Wolter M, Santo DL, Herman P, Ballone A, Centorrino F, Obsil T, Ottmann C
Interaction of an IκBα Peptide with 14-3-3
ACS Omega
IF = 2.584
Kalabova D, Filandr F, Alblova M, Petrvalska O, Horvath M, Man P, Obsil T, Obsilova V.
14-3-3 protein binding blocks the dimerization interface of caspase-2
FEBS J. 2020 Jan 21. doi: 10.1111/febs.15215.
IF = 4.739
Psenakova K, Hexnerova R, Srb P, Obsilova V, Veverka V, Obsil T
The redox active site of thioredoxin is directly involved in apoptosis signal‐regulating kinase 1 binding that is modulated by oxidative stress
FEBS J. 2020 Apr;287(8):1626-1644.
IF = 4.739

2019

Hagenbuchner J, Obsilova V, Kaserer T, Kaiser N, Rass B, Psenakova K, Docekal V, Alblova M, Kohoutova K, Schuster D, Aneichyk T, Vesely J, Obexer P, Obsil T, Ausserlechner MJ
Modulating FOXO3 transcriptional activity by small, DBD-binding molecules
eLife 2019;8:e48876 DOI: 10.7554/eLife.48876
IF = 7.55
Valenti D, Neves JF, Cantrelle FX, Hristeva S, Lentini Santo D, Obsil T, Hanoulle X, Levy LM, Tzalis D, Landrieu I, Ottmann C
Set-up and screening of a fragment library targeting the 14-3-3 protein interface
Med. Chem. Commun., 2019, doi: 10.1039/c9md00215d
IF = 2.394
Psenakova K, Kohoutova K, Obsilova V, Ausserlechner MJ, Veverka V, Obsil T
Forkhead Domains of FOXO Transcription Factors Differ in both Overall Conformation and Dynamics
Cells 2019, 8(9), 966; https://doi.org/10.3390/cells8090966
IF = 5.656
Alblova M, Smidova A, Kalabova D, Lentini Santo D, Obsil T, Obsilova V
Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein
Physiol Res. 2019 Apr 30;68(2):147-160.
IF = 1.324
Smidova A, Stankova K, Petrvalska O, Lazar J, Sychrova H, Obsil T, Zimmermannova O, Obsilova V
The activity of Saccharomyces cerevisiae Na+, K+/H+ antiporter Nha1 is negatively regulated by 14-3-3 protein binding at serine 481
Biochim Biophys Acta Mol Cell Res. 2019 Aug 22;1866(12):118534. doi: 10.1016/j.bbamcr.2019.118534.
IF = 4.739

2018

Smidova A, Alblova M, Kalabova D, Psenakova K, Rosulek M, Herman P, Obsil T, Obsilova V
14-3-3 protein masks the nuclear localization sequence of caspase-2
FEBS J. 2018 Nov;285(22):4196-4213.
IF = 4.53
Kylarova S, Psenakova K, Herman P, Obsilova V, Obsil T.
CaMKK2 kinase domain interacts with the autoinhibitory region through the N-terminal lobe including the RP insert.
Biochim Biophys Acta-General Subjects 2018 Jul 24;1862(10):2304-2313.
IF = 3.679
Psenakova K, Petrvalska O, Kylarova S, Santo DL, Kalabova D, Herman P, Obsilova V, Obsil T.
14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2).
Biochim Biophys Acta-General Subjects. 2018, 1862(7):1612-1625
IF = 3.679

2017

Alblova M, Smidova A, Docekal V, Vesely J, Herman P, Obsilova V, Obsil T
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Proc Natl Acad Sci U S A. 2017 Nov 14;114(46):E9811-E9820.
IF = 9.66
Obsil T, Obsilova V
Structural aspects of protein kinase ASK1 regulation.
Adv Biol Regul. 2017 Oct 16. pii: S2212-4926(17)30163-X.
IF = 0
Stevers LM, Sijbesma E, Botta M, MacKintosh C, Obsil T, Landrieu I, Cau Y, Wilson AJ, Karawajczyk A, Eickhoff J, Davis J, Hann MM, O
Modulators of 14-3-3 Protein-Protein Interactions.
J Med Chem. 2017 Oct 19. doi: 10.1021/acs.jmedchem.7b00574.
IF = 6.259
Kalabova D, Smidova A, Petrvalska O, Alblova M, Kosek D, Man P, Obsil T, Obsilova V
Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding.
Biochem Biophys Res Commun. 2017 Nov 18;493(2):940-945.
IF = 2.466
Kacirova M, Novacek J, Man P, Obsilova V, Obsil T
Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function.
Biophys J. 2017 Apr 11;112(7):1339-1349
IF = 3.632

2016

Kylarova S, Kosek D, Petrvalska O, Psenakova K, Man P, Vecer J, Herman P, Obsilova V, Obsil T
Cysteine residues mediate high-affinity binding of thioredoxin to ASK1.
FEBS J. 2016 Oct;283(20):3821-3838
IF = 4.237
Petrvalska O, Kosek D, Kukacka Z, Tosner Z, Man P, Vecer J, Herman P, Obsilova V and Obsil T
Structural Insight into the 14-3-3 Protein-Dependent Inhibition of Protein Kinase ASK1
J Biol Chem 2016 Sep 23;291(39):20753-65
IF = 4.258

2015

Zhao H, Ghirlando R, ..., Kosek D, ..., Obsil T, ..., Schuck P
A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.
PLoS One. 2015 May 21;10(5):e0126420
IF = 3.057
Kacirova M, Kosek D, Kadek A, Man P, Vecer J, Herman P, Obsilova V, Obsil T
Structural Characterization of Phosducin and its Complex with the 14-3-3 Protein
J Biol Chem 2015 Jun 26;290(26):16246-60.
IF = 4.573

2014

Kosek D, Kylarova S, PsenakovaK, Rezabkova L, Herman P, Vecer J, Obsilova V, Obsil T
Biophysical and Structural Characterization of the Thioredoxin-Binding Domain of Protein Kinase ASK1 and its Interaction with Reduced Thioredoxin
J Biol Chem 2014 Aug 29; 289(35):24463-24474
IF = 4.6
Kopecka M, Kosek D, Kukacka Z, Rezabkova L, Man P, Novak P, Obsil T, Obsilova V
Role of the EF-hand like motif in the 14-3-3 protein-mediated activation of yeast neutral trehalase Nth1
J Biol Chem 2014 May 16; 289(20):13948-13961
IF = 4.6
Obsilova V, Kopecka M, Kosek D, Kacirova M, Kylarova S, Rezabkova L, Obsil T.
Mechanisms of the 14-3-3 protein function: regulation of protein function through conformational modulation.
Physiol Res. 2014 Feb 24;63 Suppl 1:S155-64.
IF = 1.531

2013

Vacha P, Zuskova I, Bumba L, Herman P, Vecer J, Obsilova V, Obsil T.
Detailed kinetic analysis of the interaction between the FOXO4–DNA-binding domain and DNA.
Biophysical Chemistry 2013 Sep 15;184:68-78.
IF = 2.283
Macakova E, Kopecka M, Kukacka Z, Veisova D, Novak P, Man P, Obsil T, Obsilova V
Structural basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1
Biochimica Et Biophysica Acta-General Subjects 2013 May;1830(10):4491-4499.
IF = 3.848

2012

Rezabkova L, Kacirova M, Sulc M, Herman P, Vecer J, Stepanek M, Obsilova V, Obsil T
Structural modulation of phosducin by the phosphorylation and the 14-3-3 protein binding
Biophysical Journal 2012 Nov;103(9):1960–1969.
IF = 3.668
Haladova K, Mrazek H, Jecmen T, Halada P, Man P, Novak P, Chmelik J, Obsil T, Sulc M.
The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: mapping of human 14-3-3ζ homodimer interface.
J Struct Biol. 2012 Jul;179(1):10-7
IF = 3.361
Veisova D, Macakova E, Rezabkova L, Sulc M, Vacha P, Sychrova H, Obsil T, Obsilova V.
Role of individual phosphorylation sites for the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.
Biochem J. 2012 May 1;443(3):663-70.
IF = 4.654

2011

Rezabkova L, Man P, Novak P, Herman P, Vecer J, Obsilova V, Obsil T.
Structural basis for the 14-3-3 protein-dependent inhibition of the regulator of G-Protein signaling 3 (RGS3) function.
J Biol Chem. 2011 Dec 16;286(50):43527-36.
IF = 5.328
Obsil T, Obsilova V.
Structural basis of 14-3-3 protein functions.
Semin Cell Dev Biol. 2011 Sep;22(7):663-72.
IF = 6.342
Obsil T, Obsilova V.
Structural basis for DNA recognition by FOXO proteins.
Biochim Biophys Acta. 2011 Nov;1813(11):1946-53.
IF = 4.374
Coddou C, Yan Z, Obsil T, Huidobro-Toro JP, Stojilkovic SS.
Activation and regulation of purinergic P2X receptor channels.
Pharmacol Rev. 2011 Sep;63(3):641-83.
IF = 18.861
Valis K, Prochazka L, Boura E, Chladova J, Obsil T, Rohlena J, Truksa J, Dong LF, Ralph SJ, Neuzil J.
Hippo/Mst1 stimulates transcription of the proapoptotic mediator NOXA in a FoxO1-dependent manner.
Cancer Res. 2011 Feb 1;71(3):946-54.
IF = 7.543

2010

Stojilkovic SS, Yan Z, Obsil T, Zemkova H.
Structural insights into the function of P2X4: an ATP-gated cation channel of neuroendocrine cells.
Cell Mol Neurobiol. 2010 Nov;30(8):1251-8.
IF = 3.226
Veisova, D., Rezabkova, L., Stepanek, M., Novotna, P., Herman, P., Vecer, J., Obsil, T., Obsilova, V.
C-terminal segment of yeast BMH proteins exhibits different structure compared to other 14-3-3 protein isoforms.
Biochemistry 49(18), 3853-3861, 2010
IF = 3.226
Rezabkova, L., Boura, E., Herman, P., Vecer, J., Bourova, L., Sulc, M., Svoboda, P., Obsilova, V., Obsil
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, 2010
IF = 3.673
Boura E, Rezabkova L, Brynda J, Obsilova V, Obsil T.
Crystal structure of human FOXO4-DBD/DNA complex at 1.9 A resolution reveals new details on FOXO binding to the DNA
Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1351-7.
IF = 14.103
Friedlova E, Grycova L, Holakovska B, Silhan J, Janouskova H, Sulc M, Obsilova V, Obsil T, Teisinger J.
The interactions of the C-terminal region of the TRPC6 channel with calmodulin.
Neurochem Int. 2010 Jan;56(2):363-6.
IF = 3.541

2009

Silhan J. - Vacha P. - Strnadova P. - Vecer J. - Herman P. - Sulc M. - Teisinger J. - Obsilova V. - Obsil T.
14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.
Journal of Biological Chemistry, 284(29), 19349-19360, 2009
IF = 5.52
Jindrichova M. - Vavra V. - Obsil T. - Stojilkovic S. S. - Zemkova H.
Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors.
Journal of Neurochemistry, 109(3), 923-934, 2009
IF = 4.5

2008

Grycova L. - Lansky Z. - Friedlova E. - Obsilova V. - Janouskova H. - Obsil T. - Teisinger J.
Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin.
Biochemical and Biophysical Research Communications, 375(4), 680-683, 2008
IF = 2.648
Obsilova V. - Nedbalkova E. - Silhan J. - Boura E. - Herman P. - Vecer J. - Sulc M. - Teisinger J. - Dyda F. - Obsil T.
The 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylase.
Biochemistry, 47(6), 1768-1777, 2008
IF = 3.379
Mazna P. - Grycova L. - Balik A. - Zemkova H. - Friedlova E. - Obsilova V. - Obsil T. - Teisinger J.
The role of proline residues in the structure and function of human MT2 melatonin receptor
Journal of Pineal Research, 45(4), 361-372, 2008
IF = 5.056
Obsil T. - Obsilova V.
Structure/function relationships underlying regulation of FOXO transcription factors.
Oncogene, 27(16), 2263-2275, 2008
IF = 7.216
Jelinkova I. - Vavra V. - Jindrichova M. - Obsil T. - Zemkova H.W. - Zemkova H. - Stojilkovic S. S.
Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin.
Pflügers Archiv, 465(5), 939-950, 2008
IF = 3.526
Obsilova V, Silhan J, Boura E, Teisinger J, Obsil T.
14-3-3 proteins: a family of versatile molecular regulators.
Physiol Res. 57 Suppl 3:S11-21, 2008. Review.
IF = 1.653

2007

Grycova L. - Lansky Z. - Friedlova E. - Vlachova V. - Kubala M. - Obsilova V. - Obsil T. - Teisinger J.
ATP binding site on the C-terminus of the vanilloid receptor.
Archives of Biochemistry and Biophysics, 465(2), 389-398, 2007
IF = 2.578
Boura E. - Silhan J. - Herman P. - Vecer J. - Teisinger J. - Obsilova V. - Obsil T.
Both the N-terminal loop and wing W2 of the forkhead domain of transcription factor Foxo4 are important for DNA binding.
Journal of Biological Chemistry, 282(11), 8265-8275, 2007
IF = 5.581

2005

Mazna P. - Berka K. - Jelinkova I. - Balik A. - Svoboda P. - Obsilova V. - Obsil T. - Teisinger J.
Ligand binding to the human MT2 melatonin receptor: the role of residues in transmembrane domains 3, 6, and 7.
Biochemical and Biophysical Research Communications, 332(3), 726-734, 2005
IF = 3
Obsilova V. - Vecer J. - Herman P. - Pabianova A. - Sulc M. - Teisinger J. - Boura E. - Obsil T.
14-3-3 Protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4.
Biochemistry, 44(34), 11608-11617, 2005
IF = 3.848

2004

Obsilova V. - Herman P. - Vecer J. - Sulc M. - Teisinger J. - Obsil T.
14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232.
Journal of Biological Chemistry, 279(6), 4531-4540, 2004
IF = 6.355
Silhan J. - Obsilova V. - Vecer J. - Herman P. - Sulc M. - Teisinger J. - Obsil T.
14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding.
Journal of Biological Chemistry, 279(47), 49113-49119, 2004
IF = 6.355
Mazna P. - Obsilova V. - Jelinkova I. - Balik A. - Berka K. - Sovova Z. - Ettrich R. - Svoboda P. - Obsil T. - Teisinger J.
Molecular modeling of human MT2 melatonin receptor: the role of Val204, Leu272 and Tyr298 in ligand binding.
Journal of Neurochemistry, 91(4), 836-842, 2004
IF = 4.824
Kubala M. - Obsil T. - Obsilova V. - Lansky Z. - Amler E.
Protein modeling combined with spectroscopic techniques: an attractive quick alternative to obtain structural information.
Physiological Research, 53(Suppl. 1), S187-S197, 2004
IF = 1.14
© 2017 Cenek Albl