Center of Excellence of the European Union
 
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Selected publications

Articles

1.   Varga A, Gráczer E, Chaloin L, Liliom K, Závodszky P, Lionne C and Vas M (2013) [23201309]
  Selectivity of kinases on the activation of tenofovir, an anti-HIV agent.
  Eur J Pharm Sci 48, 307-15
2.   Varga A, Marcus AP, Himoto M, Iwai S and Szüts D (2012) [23272247]
  Analysis of CPD Ultraviolet Lesion Bypass in Chicken DT40 Cells: Polymerase η and PCNA Ubiquitylation Play Identical Roles.
  PLoS ONE 7, e52472
3.   Varga A, Palmai Z, Gugolya Z, Gráczer E, Vonderviszt F, Závodszky P, Balog E and Vas M (2012) [23231058]
  Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase.
  Biochemistry-us 51, 10197-207
4.   Zerrad L, Merli A, Schröder GF, Varga A, Gráczer É, Pernot P, Round A, Vas M and Bowler MW (2011) [21349853]
  A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase.
  J Biol Chem 286, 14040-8
5.   Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C and Vas M (2011) [21505655]
  Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues.
  Mol Biosyst 7, 1863-73
6.   Vas M, Varga A and Gráczer E (2010) [20088776]
  Insight into the mechanism of domain movements and their role in enzyme function: example of 3-phosphoglycerate kinase.
  Curr Protein Pept Sc 11, 118-47
7.   Agócs G, Solymosi K, Varga A, Módos K, Kellermayer M, Závodszky P, Fidy J and Osváth S (2010) [20132817]
  Recovery of functional enzyme from amyloid fibrils.
  FEBS Lett 584, 1139-42
8.   Cliff MJ, Bowler MW, Varga A, Marston JP, Szabó J, Hounslow AM, Baxter NJ, Blackburn GM, Vas M and Waltho JP (2010) [20397725]
  Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis.
  J Am Chem Soc 132, 6507-16
9.   Varga A, Lionne C, Lallemand P, Szabó J, Adamek N, Valentin C, Vas M, Barman T and Chaloin L (2009) [19530648]
  Direct kinetic evidence that lysine 215 is involved in the phospho-transfer step of human 3-phosphoglycerate kinase.
  Biochemistry-us 48, 6998-7008
10.   Varga A, Szabó J, Flachner B, Gugolya Z, Vonderviszt F, Závodszky P and Vas M (2009) [19854185]
  Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
  FEBS Lett 583, 3660-4
11.   Szabó J, Varga A, Flachner B, Konarev PV, Svergun DI, Závodszky P and Vas M (2008) [18540639]
  Communication between the nucleotide site and the main molecular hinge of 3-phosphoglycerate kinase.
  Biochemistry-us 47, 6735-44
12.   Gondeau C, Chaloin L, Varga A, Roy B, Lallemand P, Périgaud C, Barman T, Vas M and Lionne C (2008) [18288812]
  Differences in the transient kinetics of the binding of D-ADP and its mirror image L-ADP to human 3-phosphoglycerate kinase revealed by the presence of 3-phosphoglycerate.
  Biochemistry-us 47, 3462-73
13.   Varga A, Szabó J, Flachner B, Roy B, Konarev P, Svergun D, Závodszky P, Périgaud C, Barman T, Lionne C and Vas M (2008) [18096512]
  Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP.
  Biochem Bioph Res Co 366, 994-1000
14.   Gondeau C, Chaloin L, Lallemand P, Roy B, Périgaud C, Barman T, Varga A, Vas M, Lionne C and Arold ST (2008) [18463139]
  Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase.
  Nucleic Acids Res 36, 3620-9
15.   Szabó J, Varga A, Flachner B, Konarev PV, Svergun DI, Závodszky P and Vas M (2008) [18358841]
  Role of side-chains in the operation of the main molecular hinge of 3-phosphoglycerate kinase.
  FEBS Lett 582, 1335-40
16.   Portöro I, Kocsis L, Hermán P, Caccia D, Perrella M, Ronda L, Bruno S, Bettati S, Micalella C, Mozzarelli A, Varga A, Vas M, Lowe KC and Eke A (2008) [18405674]
  Towards a novel haemoglobin-based oxygen carrier: Euro-PEG-Hb, physico-chemical properties, vasoactivity and renal filtration.
  Bba-proteins Proteom 1784, 1402-9
17.   Gráczer É, Varga A, Hajdú I, Melnik B, Szilágyi A, Semisotnov G, Závodszky P and Vas M (2007) [17887729]
  Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.
  Biochemistry-us 46, 11536-49
18.   Varga A, Flachner B, Konarev P, Gráczer É, Szabó J, Svergun D, Závodszky P and Vas M (2006) [16647059]
  Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase.
  FEBS Lett 580, 2698-706
19.   Varga A, Flachner B, Gráczer É, Osváth S, Szilágyi AN and Vas M (2005) [15819882]
  Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase.
  FEBS J 272, 1867-85
20.   Flachner B, Varga A, Szabó J, Barna L, Hajdú I, Gyimesi G, Závodszky P and Vas M (2005) [16363799]
  Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase.
  Biochemistry-us 44, 16853-65
21.   Flachner B, Kovári Z, Varga A, Gugolya Z, Vonderviszt F, Náray-Szabó G and Vas M (2004) [15035615]
  Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP.
  Biochemistry-us 43, 3436-49