Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Mária, Vas"'
Autor:
András Szilágyi, Dániel Györffy, Mária Vas, Éva Gráczer, Tamás Szimler, István Hajdú, Péter Závodszky, Barbara M. Végh
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Scientific Reports
Scientific Reports
The tumour suppressor protein RASSF1A is phosphorylated by Aurora A kinase, thereby impairing its tumour suppressor function. Consequently, inhibiting the interaction between Aurora A and RASSF1A may be used for anti-tumour therapy. We used recombina
Autor:
Anna Palló, Petr V. Konarev, Tamás Szimler, Julianna Oláh, Anita Garamszegi, Éva Gráczer, Mária Vas, Angelo Merli, Anikó Lábas, Manfred S. Weiss, Dmitri I. Svergun, Péter Závodszky
Publikováno v:
Biochemistry. 55:560-574
The key active site residues K185, Y139, D217, D241, D245, and N102 of Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) have been replaced, one by one, with Ala. A drastic decrease in the kcat value (0.06% compared to that of the wild-
Autor:
Manfred S. Weiss, Dmitri I. Svergun, Petr V. Konarev, Anna Palló, Mária Vas, Angelo Merli, Éva Gráczer, Julianna Oláh, Péter Závodszky, Tamás Szimler
Publikováno v:
FEBS Letters. 589:240-245
The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the c
Autor:
András Bacsó, László Beinrohr, Tamás Szimler, Mária Vas, Adrian Kazi, András Szilágyi, Éva Gráczer, Laura Molnár, Denes Konya, Péter Závodszky, Tibor Soós
Publikováno v:
Andras Szilagyi
Scopus-Elsevier
ResearcherID
Scopus-Elsevier
ResearcherID
3-Isopropylmalate dehydrogenase (IPMDH) from Mycobacterium tuberculosis (Mtb) may be a target for specific drugs against this pathogenic bacterium. We have expressed and purified Mtb IPMDH and determined its physicalchemical and enzymological propert
Autor:
Anikó, Maráz, Katalin, Boér, Zsófia, Dankovics, Magdolna, Dank, Erika, Lahm, Ágota, Petrányi, János, Révész, Ágnes, Ruzsa, Miklós, Szûcs, Anikó, Valikovics, Mária, Vas, Zsófia, Küronya
Publikováno v:
Magyar onkologia. 61(4)
Our aim was to assess the efficacy and adverse effects of cabazitaxel (CBZ), a chemotherapeutic agent that can be administered to patients with metastatic castrate resistant prostate cancer (mCRPC) after docetaxel (DOC) therapy. We retrospectively an
Autor:
Anna Palló, Manfred S. Weiss, Éva Gráczer, Julianna Oláh, Angelo Merli, Mária Vas, Péter Závodszky
Publikováno v:
FEBS Journal. 281:5063-5076
The three-dimensional structure of the enzyme 3-isopropylmalate dehydrogenase from the bacterium Thermus thermophilus in complex with Mn2+, its substrate isopropylmalate and its co-factor product NADH at 2.0 A resolution features a fully closed confo
Autor:
Éva Gráczer, Péter Závodszky, Andrea Varga, Zoltán Gugolya, Ferenc Vonderviszt, Mária Vas, Zoltan Palmai, Erika Balog
Publikováno v:
Biochemistry. 51:10197-10207
The exact role of the metal ion, usually Mg(2+), in the catalysis of human 3-phosphoglycerate kinase, a well-studied two-domain enzyme, has not been clarified. Here we have prepared single and double alanine mutants of the potential metal-binding res
Autor:
Karuppasamy Manikandan, Linda Schuldt, Manfred S. Weiss, Péter Závodszky, Angelo Merli, Rajesh Kumar Singh, Mária Vas, Éva Gráczer
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:738-743
The Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) enzyme catalyses the penultimate step of the leucine-biosynthesis pathway. It converts (2R,3S)-3-isopropylmalate to (2S)-2-isopropyl-3-oxosuccinate in the presence of divalent Mg(2+)
Autor:
Andrea Varga, Nicola J. Baxter, Andrea M. Hounslow, James P Marston, Jonathan P. Waltho, G. Michael Blackburn, Matthew W. Bowler, Mária Vas, Judit Szabó, Matthew J. Cliff
Publikováno v:
Journal of the American Chemical Society. 132:6507-6516
Transition state analogue (TSA) complexes formed by phosphoglycerate kinase (PGK) have been used to test the hypothesis that balancing of charge within the transition state dominates enzyme-catalyzed phosphoryl transfer. High-resolution structures of
Autor:
Tom Barman, Perrine Lallemand, Nancy Adamek, Christian Valentin, Andrea Varga, Laurent Chaloin, Mária Vas, Judit Szabó, Corinne Lionne
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2009, 48 (29), pp.6998-7008. ⟨10.1021/bi900396h⟩
Biochemistry, American Chemical Society, 2009, 48 (29), pp.6998-7008. ⟨10.1021/bi900396h⟩
International audience; 3-Phosphoglycerate kinase (PGK) is a promising candidate for the activation of nucleotide analogues used in antiviral and anticancer therapies. PGK is a key enzyme in glycolysis; it catalyzes the reversible reaction 1,3-bispho