Publications by authors named "Eva Graczer"

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BRAF Modulates the Interplay Between Cell-Cell and Cell-Extracellular Matrix Adhesions in PECAM-1-Mediated Mechanotransduction.
Éva Gráczer, Katalin Pászty, Laura Harsányi, Csilla Lehoczky, Antónia Fülöp

Int J Mol Sci· October 2024

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Ligand-induced conformational rearrangements regulate the switch between membrane-proximal and distal functions of Rho kinase 2.
István Hajdú, András Szilágyi, Barbara M Végh, András Wacha, Dániel Györffy

Commun Biol· November 2020

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A versatile modular vector set for optimizing protein expression among bacterial, yeast, insect and mammalian hosts.
Márk Somogyi, Tamás Szimler, Attila Baksa, Barbara M Végh, Tamás Bakos

PLoS One· April 2020

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Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.
Éva Gráczer, Tamás Szimler, Anita Garamszegi, Petr V Konarev, Anikó Lábas

Biochemistry· January 2016

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Drugs against Mycobacterium tuberculosis 3-isopropylmalate dehydrogenase can be developed using homologous enzymes as surrogate targets.
Eva Graczer, Andras Bacso, Denes Konya, Adrian Kazi, Tibor Soos

Protein Pept Lett· July 2015

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Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.
Éva Gráczer, Anna Palló, Julianna Oláh, Tamás Szimler, Petr V Konarev

FEBS Lett· January 2015

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Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis.
Anna Palló, Julianna Oláh, Eva Gráczer, Angelo Merli, Péter Závodszky

FEBS J· November 2014

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Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase.
Éva Gráczer, Corinne Lionne, Péter Závodszky, Laurent Chaloin, Mária Vas

FEBS J· April 2013

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Selectivity of kinases on the activation of tenofovir, an anti-HIV agent.
Andrea Varga, Eva Gráczer, Laurent Chaloin, Károly Liliom, Péter Závodszky

Eur J Pharm Sci· January 2013

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Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase.
Andrea Varga, Zoltan Palmai, Zoltán Gugolya, Éva Gráczer, Ferenc Vonderviszt

Biochemistry· December 2012

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Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.
Eva Gráczer, Peter V Konarev, Tamás Szimler, András Bacsó, Adrienn Bodonyi

FEBS Lett· October 2011

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Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues.
Andrea Varga, Laurent Chaloin, Gyula Sági, Róbert Sendula, Eva Gráczer

Mol Biosyst· June 2011

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Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase.
Éva Gráczer, Angelo Merli, Rajesh Kumar Singh, Manikandan Karuppasamy, Péter Závodszky

Mol Biosyst· May 2011

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A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase.
Louiza Zerrad, Angelo Merli, Gunnar F Schröder, Andrea Varga, Éva Gráczer

J Biol Chem· April 2011

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Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.
Angelo Merli, Karuppasamy Manikandan, Eva Gráczer, Linda Schuldt, Rajesh Kumar Singh

Acta Crystallogr Sect F Struct Biol Cryst Commun· June 2010

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Symmetrical refolding of protein domains and subunits: example of the dimeric two-domain 3-isopropylmalate dehydrogenases.
Eva Gráczer, Andrea Varga, Bogdan Melnik, Gennady Semisotnov, Péter Závodszky

Biochemistry· February 2009

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Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.
Eva Gráczer, Andrea Varga, István Hajdú, Bogdan Melnik, András Szilágyi

Biochemistry· October 2007

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Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase.
Andrea Varga, Beáta Flachner, Peter Konarev, Eva Gráczer, Judit Szabó

FEBS Lett· May 2006

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Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase.
Andrea Varga, Beáta Flachner, Eva Gráczer, Szabolcs Osváth, Andrea N Szilágyi

FEBS J· April 2005

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