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Recent publications

Articles

1.   Merényi G, Kovári J, Tóth J, Takács E, Zagyva I, Erdei A and Vértessy BG (2011) [21780905]
  Cellular Response to Efficient dUTPase RNAi Silencing in Stable HeLa Cell Lines Perturbs Expression Levels of Genes Involved in Thymidylate Metabolism.
  Nucleos Nucleot Nucl 30, 369-90
2.   Takács E, Nagy G, Leveles I, Harmat V, Lopata A, Tóth J and Vértessy BG (2010) [20493855]
  Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases.
  FEBS Lett 584, 3047-54
3.   Varga B, Migliardo F, Takacs E, Vertessy B, Magazù S and Telling MT (2010) [19795216]
  Study of solvent-protein coupling effects by neutron scattering.
  J Biol Phys 36, 207-20
4.   Takács E, Barabás O, Petoukhov MV, Svergun DI and Vértessy BG (2009) [19302784]
  Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers.
  FEBS Lett 583, 865-71
5.   Varga B, Barabás O, Takács E, Nagy N, Nagy P and Vértessy BG (2008) [18519027]
  Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor.
  Biochem Bioph Res Co 373, 8-13
6.   Varga B, Migliardo F, Takács E, Vértessy BG and Magazu S (2008) [-100017974]
  Experimental study on dUTPase-inhibitor candidate and dUTPase/disaccharide mixtures by PCS and ENS
  J Mol Struct 886, 128-135
7.   Varga B , Migliardo F , Takacs E , Vertessy B , Magazu S and Mondelli C (2008) [-100031082]
  Neutron scattering studies on dUTPase complex in the presence of bioprotectant systems
  Chem Phys 345, 250-258
8.   Takács E, Grolmusz VK and Vértessy BG (2004) [15147867]
  A tradeoff between protein stability and conformational mobility in homotrimeric dUTPases.
  FEBS Lett 566, 48-54
9.   Kovári J, Barabás O, Takács E, Békési A, Dubrovay Z, Pongrácz V, Zagyva I, Imre T, Szabó P and Vértessy BG (2004) [14724274]
  Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme.
  J Biol Chem 279, 17932-44