Mária Vas

University of British Columbia — Canada

Materials Science · Physical Sciences

21h-index1.4kcitations89works0.02yr avg
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Research Topics

Enzyme Structure and Function(49), Protein Structure and Dynamics(25), Biochemical and Molecular Research(19), Amino Acid Enzymes and Metabolism(18), Metabolism, Diabetes, and Cancer(17)

Publications89 total

Asian-White Health Inequalities in Canada: Intersections with Immigration
Journal of Immigrant and Minority Health·2019· 13 cited
New type of interaction between the SARAH domain of the tumour suppressor RASSF1A and its mitotic kinase Aurora A
Scientific Reports·2019· 4 citedOpen Access
[Experience with cabazitaxel therapy for patients with metastatic castrate resistant prostate cancer in Hungary].
PubMed·2017· 1 cited
Dual Role of the Active Site Residues of <i>Thermus thermophilus</i> 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure
Biochemistry·2016· 2 cited
Glutamate 270 plays an essential role in K<sup>+</sup>‐activation and domain closure of <i>Thermus thermophilus</i> isopropylmalate dehydrogenase
FEBS Letters·2014· 5 citedOpen Access
Drugs Against Mycobacterium tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed Using Homologous Enzymes as Surrogate Targets
Protein and Peptide Letters·2014· 2 cited
Structure of the E270A Mutant Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH
2014
Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis
FEBS Journal·2014· 20 citedOpen Access
Transient kinetic studies reveal isomerization steps along the kinetic pathway of <i><scp>T</scp>hermus thermophilus</i> 3‐isopropylmalate dehydrogenase
FEBS Journal·2013· 6 cited
Architecture of the active site and the importance of charge balance in catalysis
Research Explorer (The University of Manchester)·2013
Fehérjék konformációs dinamikája mint a biomolekuláris felismerés és jelátvitel meghatározó eleme = Protein conformational dynamics as a key determinant in biomolecular recognition and signal transmission
Repository of the Academy's Library (Library of the Hungarian Academy of Sciences)·2013Open Access
Importance of Aspartate Residues in Balancing the Flexibility and Fine-Tuning the Catalysis of Human 3-Phosphoglycerate Kinase
Biochemistry·2012· 3 cited
Selectivity of kinases on the activation of tenofovir, an anti-HIV agent
European Journal of Pharmaceutical Sciences·2012· 15 cited
Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase
FEBS Letters·2011· 5 citedOpen Access
Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues
Molecular BioSystems·2011· 13 cited
Atomic level description of the domain closure in a dimeric enzyme: <i>Thermus thermophilus</i> 3-isopropylmalate dehydrogenase
Molecular BioSystems·2011· 13 cited
A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase
Journal of Biological Chemistry·2011· 65 citedOpen Access
Crystallization and preliminary X-ray diffraction analysis of various enzyme–substrate complexes of isopropylmalate dehydrogenase from<i>Thermus thermophilus</i>
Acta Crystallographica Section F Structural Biology and Crystallization Communications·2010· 1 citedOpen Access
The complete reaction cycle of human phosphoglycerate kinase: The open binary complex with 3PG
2010
The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and ADP
2010
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Frequent Co-authors

Andrea Varga(19), Péter Závodszky(13), Éva Gráczer(11), Beáta Flachner(10), J. Szabó(8), Corinne Lionne(7), Laurent Chaloin(6), Angelo Merli(5), Andrea N. Szilágyi(4), Andrea Mozzarelli(4), Petr V. Konarev(4), Dmitri I. Svergun(4), Gian Luigi Rossi(4), Gennady V. Semisotnov(4), Michael A. Sinev(3), Zoltán Kovári(3), Perrine Lallemand(3), Béatrice Roy(3), Christian Périgaud(3), József Batke(3)