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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.   Gráczer É, Lionne C, Závodszky P, Chaloin L and Vas M (2013) [23421786]
  Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase.
  FEBS J 280, 1764-72
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.   Gráczer É, Merli A, Singh RK, Karuppasamy M, Závodszky P, Weiss MS and Vas M (2011) [21387033]
  Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase.
  Mol Biosyst 7, 1646-59
6.   Gráczer E, Konarev PV, Szimler T, Bacsó A, Bodonyi A, Svergun DI, Závodszky P and Vas M (2011) [21939659]
  Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.
  FEBS Lett 585, 3297-302
7.   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
8.   Merli A, Manikandan K, Gráczer E, Schuldt L, Singh RK, Závodszky P, Vas M and Weiss MS (2010) [20516614]
  Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.
  Acta Crystallogr F 66, 738-43
9.   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
10.   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
11.   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
12.   Portörő I. , Kocsis L. , Hermán P. , Caccia D. , Perrella M. , Varga A. , Vas M. and Eke A. (2009) [-100085120]
  PEG-Hb-based oxygen carriers: vasoactvity and renal filtration
  Acta Physiol Hung 96, 114-115
13.   Gráczer É., Varga A., Melnik B., Semisotnov G., Závodszky P. and Vas M. (2009) [-100076773]
  Symmetrical refolding of protein domains and subunits: example of the dimeric two-domain 3-Isopropylmalate dehydrogenases.
  Biochemistry-us 48, 1123-1134
14.   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
15.   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
16.   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
17.   Vas M., Varga A., Szabó J., Gráczer É., Flachner B., Závodszky P., Konarev P.V. and Svergun D.I. (2008) [-100047371]
  Insight into the Mechanism of Domain Movement and Its Role in Functioning of 3-Phosphoglycerate Kinase
  Moscow University Chemistry Bulletin 63, 114-119
18.   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
19.   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
20.   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
21.   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
22.   Moniot S, Bruno S, Vonrhein C, Didierjean C, Boschi-Muller S, Vas M, Bricogne G, Branlant G, Mozzarelli A and Corbier C (2008) [18480053]
  Trapping of the Thioacylglyceraldehyde-3-phosphate Dehydrogenase Intermediate from Bacillus stearothermophilus: DIRECT EVIDENCE FOR A FLIP-FLOP MECHANISM.
  J Biol Chem 283, 21693-702
23.   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
24.   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
25.   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
26.   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
27.   Kovári Z and Vas M (2004) [14997553]
  Protein conformer selection by sequence-dependent packing contacts in crystals of 3-phosphoglycerate kinase.
  Proteins 55, 198-209
28.   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
29.   Kovári Z, Flachner B, Náray-Szabó G and Vas M (2002) [12102622]
  Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility.
  Biochemistry-us 41, 8796-806
30.   Merli A, Szilágyi AN, Flachner B, Rossi GL and Vas M (2002) [11772008]
  Nucleotide binding to pig muscle 3-phosphoglycerate kinase in the crystal and in solution: relationship between substrate antagonism and interdomain communication.
  Biochemistry-us 41, 111-9
31.   Szilágyi AN, Ghosh M, Garman E and Vas M (2001) [11178909]
  A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure.
  J Mol Biol 306, 499-511
32.   Szilágyi AN, Kotova NV, Semisotnov GV and Vas M (2001) [11248706]
  Incomplete refolding of a fragment of the N-terminal domain of pig muscle 3-phosphoglycerate kinase that lacks a subdomain. Comparison with refolding of the complementary C-terminal fragment.
  Eur J Biochem 268, 1851-60
33.   Szilágyi AN and Vas M (1998) [9622507]
  Anion activation of 3-phosphoglycerate kinase requires domain closure.
  Biochemistry-us 37, 8551-63
34.   Szilágyi AN and Vas M (1998) [9889168]
  Sequential domain refolding of pig muscle 3-phosphoglycerate kinase: kinetic analysis of reactivation.
  Fold Des 3, 565-75
35.   May A, Vas M, Harlos K and Blake C (1996) [8778776]
  2.0 A resolution structure of a ternary complex of pig muscle phosphoglycerate kinase containing 3-phospho-D-glycerate and the nucleotide Mn adenylylimidodiphosphate.
  Proteins 24, 292-303
36.   Vas M, Merli A and Rossi GL (1994) [8053912]
  Antagonistic binding of substrates to 3-phosphoglycerate kinase monitored by the fluorescent analogue 2\'(3\')-O-(2,4,6-trinitrophenyl)adenosine 5\'-triphosphate.
  Biochem J 301 (Pt 3), 885-91
37.   Molnár M and Vas M (1993) [8343139]
  Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium dialysis binding and enzyme kinetic data.
  Biochem J 293 (Pt 2), 595-9
38.   Harlos K, Vas M and Blake CF (1992) [1603803]
  Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate.
  Proteins 12, 133-44
39.   Vértessy BG and Vas M (1992) [1417758]
  Metabolite channeling versus free diffusion: reinterpretation of aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase.
  Biochem J 286 (Pt 3), 977-9
40.   Semisotnov GV, Vas M, Chemeris VV, Kashparova NJ, Kotova NV, Razgulyaev OI and Sinev MA (1991) [1765069]
  Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments.
  Eur J Biochem 202, 1083-9
41.   Vas M and Batke J (1990) [-100005161]
  Kinetic Misinterpretation of a Coupled Enzyme Reaction Can Lead to the Assumption of An Enzyme Enzyme Interaction - the Example of 3-phospho-d-glycerate Kinase And Glyceraldehyde-3-phosphate Dehydrogenase Couple
  Eur J Biochem 191, 679-83
42.   Vas M (1990) [2269289]
  Modelling of substrate binding to 3-phosphoglycerate kinase with analogues of 3-phosphoglycerate.
  Eur J Biochem 194, 639-45
43.   Vas M, Sinev MA, Kotova NV and Semisotnov GV (1990) [2351137]
  Reactivation of 3-phosphoglycerate kinase from its unfolded proteolytic fragments.
  Eur J Biochem 189, 575-9
44.   Sinev MA, Razgulyaev OI, Vas M, Timchenko AA and Ptitsyn OB (1989) [2707265]
  Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase.
  Eur J Biochem 180, 61-6
45.   Keleti T, Berni R, Vas M, Mozzarelli A and Rossi GL (1989) [2514536]
  Coupled enzymatic reactions measured in a single protein crystal from myogen A.
  Acta Biochim Biophys Acad Sci Hung 24, 15-23
46.   Vas M, Berni R, Batke J, Keleti T and Rossi GL (1988) [3369857]
  Kinetic evidence for a reversible isomerization of pig muscle glyceraldehyde-3-phosphate dehydrogenase in its crystallization medium.
  Arch Biochem Biophys 263, 121-9
47.   Jiang SX and Vas M (1988) [3360118]
  Limited proteolysis of 3-phosphoglycerate kinase without loss of enzymic activity.
  FEBS Lett 231, 151-4
48.   Vas M and Csanády G (1987) [3816810]
  The two fast-reacting thiols of 3-phosphoglycerate kinase are structurally juxtaposed. Chemical modification with bifunctional reagents.
  Eur J Biochem 163, 365-8
49.   Vértessy B, Vas M and Keleti T (1986) [3789735]
  Microenvironment of the enzyme-bound NADH is different in lobster and pig muscle glyceraldehyde-3-phosphate dehydrogenase microcrystals.
  Arch Biochem Biophys 251, 299-305
50.   Tompa P, Hong PT and Vas M (1986) [3948871]
  The phosphate group of 3-phosphoglycerate accounts for conformational changes occurring on binding to 3-phosphoglycerate kinase. Enzyme inhibition and thiol reactivity studies.
  Eur J Biochem 154, 643-9
51.   Hung ND, Vas M, Cseke E and Szabolcsi G (1985) [-100002775]
  Tápfehérjék tripszines emésztési sebességének összehasonlító vizsgálata.
  Magyar Kémiai folyóirat 91, 506-515
52.   Vas M and Batke J (1984) [6607835]
  Adenine nucleotides affect the binding of 3-phosphoglycerate to pig muscle 3-phosphoglycerate kinase.
  Eur J Biochem 139, 115-23
53.   Dékány K and Vas M (1984) [6697999]
  Inactivation of pig muscle 3-phosphoglycerate kinase by thiol modification depends on reagent size.
  Eur J Biochem 139, 125-30
54.   Hung ND, Cseke E, Vas M and Szabolcsi G (1984) [-100002774]
  Processed protein foods characterized by in vitro digestion rates.
  J. Food Science 49, 1543-1546
55.   Hung ND, Vas M, Cseke E and Szabolcsi G (1984) [-100002773]
  Tryptic digestion rates of food proteins.
  J. Food Science 49, 1535-1542
56.   Cserpán I and Vas M (1983) [6832138]
  Effects of substrates on the heat stability and on the reactivities of thiol groups of 3-phosphoglycerate kinase.
  Eur J Biochem 131, 157-62
57.   Vas M and Batke j (1982) [-100064896]
  Effects of substrates on the fluorimetric properties of ANS-labelled 3-phosphoglycerate kinase
  Acta Biochim Biophys Acad Sci Hung 17, 96-96
58.   Mozzarelli A, Berni R, Rossi GL, Vas M, Bartha F and Keleti T (1982) [7085599]
  Protein isomerization in the NAD+-dependent activation of beta-(2-furyl)acryloyl-glyceraldehyde-3-phosphate dehydrogenase in the crystal.
  J Biol Chem 257, 6739-44
59.   Vas M and Batke J (1981) [-100005170]
  Evidence for Absence of An Interaction Between Purified 3-phosphoglycerate Kinase And Glyceraldehyde-3-phosphate Dehydrogenase
  Biochim Biophys Acta 660, 193-8
60.   Vas M, Lakatos S, Hajdu J and Friedrich P (1981) [-100005171]
  Kinetic-behavior And Oligomeric State of 3-phosphoglyceroyl-d-glyceraldehyde-3-phosphate Dehydrogenase
  Biochimie 63, 89-96
61.   Vas M, Berni R, Mozzarelli A, Tegoni M and Rossi GL (1979) [224055]
  Kinetic studies of crystalline enzymes by single crystal microspectrophotometry: Analysis of a single turnorver in glyceraldehyde-3-phosphate dehydrogenase crystal
  J Biol Chem 254, 8480-8486
62.   Patthy L and Vas M (1978) [740028]
  Aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase.
  Nature 276, 94-5
63.   Vas M and Batke J (1978) [-100088609]
  Concentration-dependent differences in the kinetic properties of 3-phosphoglycerate kinase and glyceraldehyde-dehydrogenase enzyme system
  Acta Phys Acad Sci Hung 52, 296-297
64.   Vas M (1976) [188292]
  Conformational motility in D-glyceraldehyde-3-phosphate dehydrogenase influenced by subunit interactions.
  Acta Biochim Biophys Acad Sci Hung 11, 105-12
65.   Vas M and Bartha F (1976) [188295]
  Effect of modification of SH-groups in D-glyceraldehyde-3-phosphate dehydrogenase on the properties of enzyme--coenzyme complex.
  Acta Biochim Biophys Acad Sci Hung 11, 95-104
66.   Vas M and Boross L (1975) [238353]
  Charge-transfer absorption spectrum of the complex of NAD and D-glyceraldehyde-3-phosphate dehydrogenase modified with N-ethylmaleimide.
  Acta Biochim Biophys Acad Sci Hung 10, 1-5
67.   Vas M and Boross L (1974) [4838979]
  An approach for the determination of equilibrium constant of structural motility. Characterization of the fluctuational motion around residue Cys-153 of D-glyceraldehyde-3-phosphate dehydrogenase.
  Eur J Biochem 43, 237-44
68.   Vas M and Boross L (1972) [4677681]
  Heat inactivation of D-glyceraldehyde-3-phosphate dehydrogenase apoenzyme.
  Acta Biochim Biophys Acad Sci Hung 7, 105-14
69.   Vas M and Boross L (1970) [5531275]
  Characterization of the less-reactive SH groups of D-glyceraldehyde-3-phosphate dehydrogenase. I. Kinetic analysis of mercaptide formation.
  Acta Biochim Biophys Acad Sci Hung 5, 203-13
70.   Vas M and Boross L (1970) [4321951]
  Characterization of the less-reactive SH groups of D-glyceraldehyde-3-phosphate dehydrogenase. II. Effect of coenzyme, anions and pH on the reactivity.
  Acta Biochim Biophys Acad Sci Hung 5, 215-23
71.   Boross L, Cseke E and Vas M (1969) [5367478]
  Characterization of the SH-groups of D-glyceraldehyde-3-phosphate dehydrogenase.
  Acta Biochim Biophys Acad Sci Hung 4, 301-4

Books or book chapters

1.   Kazinczné Vas Mária (1991)
  Glicerát-3-foszfát kináz
  ENZIMES ANALÍZIS , 251-256
2.   Kazinczyné Vas Mária (1991)
  Az enzimek mennyiségi meghatározását zavaró tényezők
  ENZIMES ANALÍZIS , 61-85
3.   Kazinczyné Vas Mária (1991)
  Glicerinaldehid-3-foszfát dehidrogenáz
  ENZIMES ANALÍZIS , 158-165