Search Results - "Vertessy, B. G."

Malaria pigment crystals as magnetic micro-rotors: key for high-sensitivity diagnosis by Butykai, A., Orbán, A., Kocsis, V., Szaller, D., Bordács, S., Tátrai-Szekeres, E., Kiss, L. F., Bóta, A., Vértessy, B. G., Zelles, T., Kézsmárki, I.

“…The need to develop new methods for the high-sensitivity diagnosis of malaria has initiated a global activity in medical and interdisciplinary sciences. Most…”
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The interaction of a new anti‐tumour drug, KAR‐2 with calmodulin by Orosz, F, Vértessy, B G, Salerno, C, Crifo, C, Capuozzo, E, Ovádi, J

“…KAR‐2 (3′′‐(β‐chloroethyl)‐2′′,4′′‐dioxo‐3,5′′‐spiro‐oxazolidino‐4‐deacetoxy‐vinblastine) is a semisynthetic bis‐indol derivative, with high anti‐microtubular…”
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A new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studies by Harmat, Veronika, Böcskei, Zsolt, Náray-Szabó, Gábor, Bata, Imre, Csutor, Andrea S., Hermecz, István, Arányi, Péter, Szabó, Beáta, Liliom, Károly, Vértessy, Beáta G., Ovádi, Judit

“…An arylalkylamine-type calmodulin antagonist, N-(3,3-diphenylpropyl)- N′-[1-R-(3,4-bis-butoxyphenyl)ethyl]-propylene-diamine (AAA) is presented and its…”
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Interaction of a new bis‐indol derivative, KAR‐2 with tubulin and its antimitotic activity by Orosz, Ferenc, Kovács, János, Löw, Péter, Vértessy, Beáta G, Urbányi, Zoltán, Ács, Tibor, Keve, Tibor, Ovádi, Judit

“…KAR‐2 (3″‐(β‐chloroethyl)‐2″,4″‐dioxo‐3,5″‐spiro‐oxazolidino‐4‐deacetoxy‐vinblastine), is a bis‐indol derivative; catharantine is coupled with the vindoline…”
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Elasticity of the human red cell membrane skeleton. Effects of temperature and denaturants by Vertessy, B.G., Steck, T.L.

“…The molecular basis for the elasticity of the human erythrocyte membrane was explored. Skeletons were released from ghosts in Triton X-100 and their dimensions…”
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Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme by Kovári, Júlia, Barabás, Orsolya, Takács, Enikõ, Békési, Angéla, Dubrovay, Zsófia, Pongrácz, Veronika, Zagyva, Imre, Imre, Timea, Szabó, Pál, Vértessy, Beáta G

“…dUTPase is responsible for preventive DNA repair via exclusion of uracil. Developmental regulation of the Drosophila enzyme is suggested to be involved in…”
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Catalytic and Structural Role of the Metal Ion in dUTP Pyrophosphatase by Mustafi, Devkumar, Bekesi, Angela, Vertessy, Beata G., Makinen, Marvin W.

“…The metal ion dependence of the catalytic activity of recombinant Escherichia coli dUTP pyrophosphatase (dUTPase), an essential enzyme preventing incorporation…”
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Developmental Regulation of dUTPase in Drosophila melanogaster by Békési, Angéla, Zagyva, Imre, Hunyadi-Gulyás, Eva, Pongrácz, Veronika, Kovári, Júlia, Nagy, Agnes O, Erdei, Anna, Medzihradszky, Katalin F, Vértessy, Beáta G

“…dUTPase prevents uracil incorporation into DNA by strict regulation of the cellular dUTP:dTTP ratio. Lack of the enzyme initiates thymineless cell death,…”
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dUTPase and Nucleocapsid Polypeptides of the Mason-Pfizer Monkey Virus Form a Fusion Protein in the Virion with Homotrimeric Organization and Low Catalytic Efficiency by Barabás, Orsolya, Rumlová, Michaela, Erdei, Anna, Pongrácz, Veronika, Pichová, Iva, Vértessy, Beáta G.

“…Betaretroviruses encode dUTPase, an essential factor in DNA metabolism and repair, in the pro open reading frame located between gag and pol. Ribosomal…”
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Investigations of homologous disaccharides by elastic incoherent neutron scattering and wavelet multiresolution analysis by Magazù, S., Migliardo, F., Vertessy, B.G., Caccamo, M.T.

“…[Display omitted] •Innovative multiresolution wavelet analysis of elastic incoherent neutron scattering.•Elastic Incoherent Neutron Scattering measurements on…”
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Mechanistic Studies of dUTPases by Kovári, J., Imre, T., Szabó, P., Vértessy, B. G.

“…The essential enzyme dUTPase is responsible for preventive DNA repair via exclusion of uracil. Lack or inhibition of the enzyme induces thymine-less cell death…”
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Identification of tyrosine as a functional residue in the active site of Escherichia coli dUTPase by Vertessy, B G, Zalud, P, Nyman, P O, Zeppezauer, M

“…dUTP nucleotidohydrolase (dUTPase, EC 3.6.1.23) from E. coli contains a total of six tyrosine residues per trimer. About half of them were found to be…”
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Interacting Partners of M-PMV Nucleocapsid-DUTPase by Németh-Pongrácz, V., Snasel, J., Rumlova, M., Pichova, I., Vértessy, B. G.

“…The nucleocapsid-dUTPase protein of Mason-Pfizer monkey virus is a truly bifunctional fusion enzyme. The exact role of this fusion protein in the viral life…”
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Multidimensional NMR Identifies the Conformational Shift Essential for Catalytic Competence in the 60-kDa Drosophila melanogaster dUTPase Trimer by Dubrovay, Zsófia, Gáspári, Zoltán, Hunyadi-Gulyás, Éva, Medzihradszky, Katalin F., Perczel, András, Vértessy, Beáta G.

“…The catalytic mechanism of dUTP pyrophosphatase (dUTPase), responsible for the prevention of uracil incorporation into DNA, involves ordering of the flexible C…”
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Pyruvate kinase as a microtubule destabilizing factor in vitro by Vértessy, B G, Bánkfalvi, D, Kovács, J, Löw, P, Lehotzky, A, Ovádi, J

“…Endogenous control of microtubule dynamism is essential in many cell types. Numerous microtubule-adhering proteins stabilize the polymer status, while very few…”
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The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase by Vertessy, Beata G, Larsson, Gunilla, Persson, Tina, Bergman, Anna-Carin, Persson, Rebecca, Nyman, Per Olof

“…The molecular mechanism of substrate analogue interaction with Escherichia coli dUTPase was investigated, using the non-hydrolyzable 2′-deoxyuridine…”
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Characterization of conformational properties of protein/trehalose/water system by neutron scattering by Brandt, A., Magazu', S., Mangione, A., Migliardo, F., Vertessy, B.G.

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Shared developmental roles and transcriptional control of autophagy and apoptosis in Caenorhabditis elegans by Erdélyi, P., Borsos, É., Takács-Vellai, K., Kovács, T., Kovács, A. L., Sigmond, T., Hargitai, B., Pásztor, L., SenGupta, T., Dengg, M., Pécsi, I., Tóth, J., Nilsen, H., Vértessy, B. G., Vellai, T.

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Specific Derivatization of the Active Site Tyrosine in dUTPase Perturbs Ligand Binding to the Active Site by Vertessy, Beata G., Persson, Rebecca, Rosengren, Anna-Maria, Zeppezauer, Michael, Nyman, Per Olof

“…Selective modification of one (of three) tyrosine residue per enzyme monomer leads to inactivation of dUTPase of the retrovirus equine infectious anemia virus…”
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Characterization of Microtubule−Phosphofructokinase Complex:  Specific Effects of MgATP and Vinblastine by Vértessy, Beáta G, Kovács, János, Löw, Péter, Lehotzky, Attila, Molnár, Attila, Orosz, Ferenc, Ovádi, Judit

“…Phosphofructokinase interacts with both microtubules and microtubules containing microtubule-associated proteins to produce bundling and periodical…”
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