Vértessy BG - Search Results

1

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.

2

Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site.

Vertessy BG, Persson R, Rosengren AM, Zeppezauer M, Nyman PO. Vertessy BG, et al. Biochem Biophys Res Commun. 1996 Feb 15;219(2):294-300. doi: 10.1006/bbrc.1996.0226. Biochem Biophys Res Commun. 1996. PMID: 8604980

3

Specific characteristics of phosphofructokinase-microtubule interaction.

Vértessy BG, Kovács J, Ovádi J. Vértessy BG, et al. FEBS Lett. 1996 Jan 29;379(2):191-5. doi: 10.1016/0014-5793(95)01510-8. FEBS Lett. 1996. PMID: 8635590 Free article.

4

Flexible glycine rich motif of Escherichia coli deoxyuridine triphosphate nucleotidohydrolase is important for functional but not for structural integrity of the enzyme.

Vertessy BG. Vertessy BG. Proteins. 1997 Aug;28(4):568-79. Proteins. 1997. PMID: 9261872

5

The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase.

Vertessy BG, Larsson G, Persson T, Bergman AC, Persson R, Nyman PO. Vertessy BG, et al. FEBS Lett. 1998 Jan 2;421(1):83-8. doi: 10.1016/s0014-5793(97)01545-7. FEBS Lett. 1998. PMID: 9462846 Free article.

6

Simultaneous binding of drugs with different chemical structures to Ca2+-calmodulin: crystallographic and spectroscopic studies.

Vertessy BG, Harmat V, Böcskei Z, Náray-Szabó G, Orosz F, Ovádi J. Vertessy BG, et al. Biochemistry. 1998 Nov 3;37(44):15300-10. doi: 10.1021/bi980795a. Biochemistry. 1998. PMID: 9799490

7

A new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studies.

Harmat V, Böcskei Z, Náray-Szabó G, Bata I, Csutor AS, Hermecz I, Arányi P, Szabó B, Liliom K, Vértessy BG, Ovádi J. Harmat V, et al. Among authors: vertessy bg. J Mol Biol. 2000 Mar 31;297(3):747-55. doi: 10.1006/jmbi.2000.3607. J Mol Biol. 2000. PMID: 10731425

8

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.

9

Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme.

Kovári J, Barabás O, Takács E, Békési A, Dubrovay Z, Pongrácz V, Zagyva I, Imre T, Szabó P, Vértessy BG. Kovári J, et al. Among authors: vertessy bg. J Biol Chem. 2004 Apr 23;279(17):17932-44. doi: 10.1074/jbc.M313643200. Epub 2004 Jan 14. J Biol Chem. 2004. PMID: 14724274 Free article.

10

A tradeoff between protein stability and conformational mobility in homotrimeric dUTPases.

Takács E, Grolmusz VK, Vértessy BG. Takács E, et al. Among authors: vertessy bg. FEBS Lett. 2004 May 21;566(1-3):48-54. doi: 10.1016/j.febslet.2004.04.039. FEBS Lett. 2004. PMID: 15147867 Free article.

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