J. Szabó

发表

Trading in cooperativity for specificity to maintain uracil-free DNA

J. Szabó, E. Takács, G. Merényi, 2016, Scientific Reports.

Investigation of the traditional enzymatic role and the emerging regulatory function of dUTPases

J. Szabó, 2015 .

Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis.

Matthew W Bowler, N. J. Baxter, A. Hounslow, 2010, Journal of the American Chemical Society.

Structural model of human dUTPase in complex with a novel proteinaceous inhibitor

D. Svergun, J. Szabó, B. Vértessy, 2018, Scientific Reports.

Unshielding multidrug resistant cancer through selective iron depletion of P-glycoprotein expressing cells.

Veronika F. S. Pape, G. Szakács, J. Szabó, 2019, Cancer research.

Nucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination

I. Simon, J. Sellers, J. Szabó, 2011, Proceedings of the National Academy of Sciences.

Role of PCNA and TLS polymerases in D-loop extension during homologous recombination in humans☆

Szilvia Juhász, J. Szabó, Marietta Y. W. T. Lee, 2013, DNA repair.

Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability

J. Szabó, B. Vértessy, K. Nyíri, 2021, Scientific Reports.

dNTPpoolDB: a manually curated database of experimentally determined dNTP pools and pool changes in biological samples

J. Szabó, J. Tóth, R. Pancsa, 2021, Nucleic Acids Res..

Student abstracts P1 IN VITRO CHARACTERISATION OF STAPHYLOCOCCAL PATHOGENICITY ISLAND REGULATORY ELEMENTS

J. Szabó, B. Vértessy, I. Zagyva, 2012 .

A user-friendly, high-throughput tool for the precise fluorescent quantification of deoxyribonucleoside triphosphates from biological samples

J. Szabó, J. Tóth, É. Surányi, 2020, Nucleic acids research.

Life without dUTPase

J. Szabó, B. Vértessy, D. Szabo, 2015, Front. Microbiol..

Structure and enzymatic mechanism of a moonlighting dUTPase.

J. Szabó, B. Vértessy, J. Tóth, 2013, Acta crystallographica. Section D, Biological crystallography.

Thermodynamic analysis of substrate induced domain closure of 3‐phosphoglycerate kinase

J. Szabó, P. Závodszky, M. Vas, 2009, FEBS letters.

Communication between the nucleotide site and the main molecular hinge of 3-phosphoglycerate kinase.

Beáta Flachner, Dmitri I Svergun, Péter Závodszky, 2008, Biochemistry.

Insight into the mechanism of domain movements and its role in functioning of 3-phosphoglycerate kinase

D. Svergun, J. Szabó, P. Konarev, 2008 .

Substrate‐induced double sided H‐bond network as a means of domain closure in 3‐phosphoglycerate kinase

Beáta Flachner, Dmitri Svergun, Péter Závodszky, 2006, FEBS letters.

In Vitro Analysis of Predicted DNA-Binding Sites for the Stl Repressor of the Staphylococcus aureus SaPIBov1 Pathogenicity Island

J. Szabó, B. Vértessy, K. Nyíri, 2016, PloS one.

Cross-species inhibition of dUTPase via the Staphylococcal Stl protein perturbs dNTP pool and colony formation in Mycobacterium.

J. Szabó, B. Vértessy, J. Tóth, 2015, DNA repair.

Exploring the role of the phage-specific insert of bacteriophage Φ11 dUTPase

J. Szabó, B. Vértessy, K. Nyíri, 2015, Structural Chemistry.

Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control

J. Szabó, B. Vértessy, J. Tóth, 2014, Nucleic acids research.

Role of side‐chains in the operation of the main molecular hinge of 3‐phosphoglycerate kinase

Beáta Flachner, Dmitri I Svergun, Péter Závodszky, 2008, FEBS letters.

The Role of a Key Amino Acid Position in Species-Specific Proteinaceous dUTPase Inhibition

J. Szabó, B. Vértessy, A. Benedek, 2019, Biomolecules.

Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase.

Beáta Flachner, Gergely Gyimesi, Péter Závodszky, 2005, Biochemistry.

Direct kinetic evidence that lysine 215 is involved in the phospho-transfer step of human 3-phosphoglycerate kinase.

J. Szabó, M. Vas, C. Lionne, 2009, Biochemistry.

Interaction of human 3-phosphoglycerate kinase with L-ADP, the mirror image of D-ADP.

Beáta Flachner, Dmitri Svergun, Péter Závodszky, 2008, Biochemical and biophysical research communications.

Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis.

N. J. Baxter, A. Hounslow, J. Waltho, 2010, Journal of the American Chemical Society.