Vertessy BG - Search Results

1

Differential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.

Hirmondo R, Lopata A, Suranyi EV, Vertessy BG, Toth J. Hirmondo R, et al. Among authors: vertessy bg. Sci Rep. 2017 Jul 20;7(1):6043. doi: 10.1038/s41598-017-06206-y. Sci Rep. 2017. PMID: 28729658 Free PMC article.

2

Multidimensional NMR identifies the conformational shift essential for catalytic competence in the 60-kDa Drosophila melanogaster dUTPase trimer.

Dubrovay Z, Gáspári Z, Hunyadi-Gulyás E, Medzihradszky KF, Perczel A, Vértessy BG. Dubrovay Z, et al. Among authors: vertessy bg. J Biol Chem. 2004 Apr 23;279(17):17945-50. doi: 10.1074/jbc.M313644200. Epub 2004 Jan 14. J Biol Chem. 2004. PMID: 14724273 Free article.

3

Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase.

Barabás O, Pongrácz V, Kovári J, Wilmanns M, Vértessy BG. Barabás O, et al. Among authors: vertessy bg. J Biol Chem. 2004 Oct 8;279(41):42907-15. doi: 10.1074/jbc.M406135200. Epub 2004 Jun 17. J Biol Chem. 2004. PMID: 15208312 Free article.

4

Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme.

Tóth J, Varga B, Kovács M, Málnási-Csizmadia A, Vértessy BG. Tóth J, et al. Among authors: vertessy bg. J Biol Chem. 2007 Nov 16;282(46):33572-33582. doi: 10.1074/jbc.M706230200. Epub 2007 Sep 11. J Biol Chem. 2007. PMID: 17848562 Free article.

5

Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase.

Varga B, Barabás O, Kovári J, Tóth J, Hunyadi-Gulyás E, Klement E, Medzihradszky KF, Tölgyesi F, Fidy J, Vértessy BG. Varga B, et al. Among authors: vertessy bg. FEBS Lett. 2007 Oct 2;581(24):4783-8. doi: 10.1016/j.febslet.2007.09.005. Epub 2007 Sep 12. FEBS Lett. 2007. PMID: 17880943 Free article.

6

Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor.

Varga B, Barabás O, Takács E, Nagy N, Nagy P, Vértessy BG. Varga B, et al. Among authors: vertessy bg. Biochem Biophys Res Commun. 2008 Aug 15;373(1):8-13. doi: 10.1016/j.bbrc.2008.05.130. Epub 2008 Jun 2. Biochem Biophys Res Commun. 2008. PMID: 18519027

7

Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases.

Vértessy BG, Tóth J. Vértessy BG, et al. Acc Chem Res. 2009 Jan 20;42(1):97-106. doi: 10.1021/ar800114w. Acc Chem Res. 2009. PMID: 18837522 Free PMC article.

8

Dissociation of calmodulin-target peptide complexes by the lipid mediator sphingosylphosphorylcholine: implications in calcium signaling.

Kovacs E, Tóth J, Vértessy BG, Liliom K. Kovacs E, et al. Among authors: vertessy bg. J Biol Chem. 2010 Jan 15;285(3):1799-808. doi: 10.1074/jbc.M109.053116. Epub 2009 Nov 12. J Biol Chem. 2010. PMID: 19910470 Free PMC article.

9

Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases.

Takács E, Nagy G, Leveles I, Harmat V, Lopata A, Tóth J, Vértessy BG. Takács E, et al. Among authors: vertessy bg. FEBS Lett. 2010 Jul 16;584(14):3047-54. doi: 10.1016/j.febslet.2010.05.018. Epub 2010 May 21. FEBS Lett. 2010. PMID: 20493855 Free PMC article.

10

Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions.

Kovacs E, Harmat V, Tóth J, Vértessy BG, Módos K, Kardos J, Liliom K. Kovacs E, et al. Among authors: vertessy bg. FASEB J. 2010 Oct;24(10):3829-39. doi: 10.1096/fj.10-155614. Epub 2010 Jun 3. FASEB J. 2010. PMID: 20522785 Free PMC article.

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