Search Results - "Jancsó, Attila"

Inducing α‐Helicity in Peptides by Silver Coordination to Cysteine by Fischer, Niklas, Tóth, Annamária, Jancsó, Attila, Thulstrup, Peter, Diness, Frederik

“…Short peptide sequences consisting of two cysteine residues separated by three other amino acids display complete change from random coil to α‐helical…”
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Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS3 Coordination Environment Imitating Metalloid Binding Sites in Proteins by Szekeres, Levente I., Maldivi, Pascale, Lebrun, Colette, Gateau, Christelle, Mesterházy, Edit, Delangle, Pascale, Jancsó, Attila

“…The AsIII binding of two NTA-based tripodal pseudopeptides, possessing three cysteine (ligand L1 ) or d-penicillamine residues (ligand L2 ) as potential…”
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A Constrained Tetrapeptide as a Model of Cu(I) Binding Sites Involving Cu4S6 Clusters in Proteins by Mesterházy, Edit, Lebrun, Colette, Jancsó, Attila, Delangle, Pascale

“…Peptide design is an efficient strategy to create relevant models of natural metal binding sites found in proteins. The two short tetrapeptides…”
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AsIII Selectively Induces a Disorder-to-Order Transition in the Metalloid Binding Region of the AfArsR Protein by Tóth, Annamária, Sajdik, Kadosa, Gyurcsik, Béla, Nafaee, Zeyad H., Wéber, Edit, Kele, Zoltan, Christensen, Niels Johan, Schell, Juliana, Correia, Joao Guilherme, Sigfridsson Clauss, Kajsa G. V., Pittkowski, Rebecca K., Thulstrup, Peter Waaben, Hemmingsen, Lars, Jancsó, Attila

“…Arsenic is highly toxic and a significant threat to human health, but certain bacteria have developed defense mechanisms initiated by AsIII binding to…”
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Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study by May, Nóra V., Jancsó, Attila, Enyedy, Éva A.

“…Copper(II) complexes of thiosemicarbazones (TSCs) often exhibit anticancer properties, and their pharmacokinetic behavior can be affected by their interaction…”
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A study on the secondary structure of the metalloregulatory protein CueR: effect of pH, metal ions and DNA by Balogh, Ria K., Németh, Eszter, Jones, Nykola C., Hoffmann, Søren Vrønning, Jancsó, Attila, Gyurcsik, Béla

“…The response of CueR towards environmental changes in solution was investigated. CueR is a bacterial metal ion selective transcriptional metalloregulator…”
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Synthesis and Fluorescence Mechanism of the Aminoimidazolone Analogues of the Green Fluorescent Protein: Towards Advanced Dyes with Enhanced Stokes Shift, Quantum Yield and Two‐Photon Absorption by Kovács, Ervin, Cseri, Levente, Jancsó, Attila, Terényi, Ferenc, Fülöp, Anna, Rózsa, Balázs, Galbács, Gábor, Mucsi, Zoltán

“…Novel small‐molecular analogues the green fluorescence protein (GFP) chromophore were synthesised to expand and improve this fluorophore family and to deepen…”
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Interaction of Arsenous Acid with the Dithiol-Type Chelator British Anti-Lewisite (BAL): Structure and Stability of Species Formed in an Unexpectedly Complex System by Szekeres, Levente I, Gyurcsik, Béla, Kiss, Tamás, Kele, Zoltán, Jancsó, Attila

“…British anti-Lewisite (2,3-dimerkaptopropan-1-ol, dimercaprol, BAL) is one of the best-known chelator-type therapeutic agents against toxic metal ions and…”
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A Comprehensive Study of the Ca2+ Ion Binding of Fluorescently Labelled BAPTA Analogues by Csomos, Attila, Kontra, Bence, Jancsó, Attila, Galbács, Gábor, Deme, Ruth, Kele, Zoltán, Rózsa, Balázs József, Kovács, Ervin, Mucsi, Zoltán

“…Since its development, the ionophore BAPTA (1,2‐bis(2‐aminophenoxy)‐ethane‐N,N,N’,N’‐tetraacetic acid) has been used unchanged in calcium sensing applications…”
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Specificity of the Metalloregulator CueR for Monovalent Metal Ions: Possible Functional Role of a Coordinated Thiol? by Szunyogh, Dániel, Szokolai, Hajnalka, Thulstrup, Peter W., Larsen, Flemming H., Gyurcsik, Béla, Christensen, Niels Johan, Stachura, Monika, Hemmingsen, Lars, Jancsó, Attila

“…Metal‐ion‐responsive transcriptional regulators within the MerR family effectively discriminate between mono‐ and divalent metal ions. Herein we address the…”
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Revisiting the hydrolysis of ampicillin catalyzed by Temoneira‐1 β‐lactamase, and the effect of Ni(II), Cd(II) and Hg(II) by Nafaee, Zeyad H., Egyed, Viktória, Jancsó, Attila, Tóth, Annamária, Gerami, Adeleh Mokhles, Dang, Thanh Thien, Heiniger‐Schell, Juliana, Hemmingsen, Lars, Hunyadi‐Gulyás, Éva, Peintler, Gábor, Gyurcsik, Béla

“…β‐Lactamases grant resistance to bacteria against β‐lactam antibiotics. The active center of TEM‐1 β‐lactamase accommodates a Ser‐Xaa‐Xaa‐Lys motif. TEM‐1…”
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Short oligopeptides with three cysteine residues as models of sulphur-rich Cu(i)- and Hg(ii)-binding sites in proteins by Mesterházy, Edit, Lebrun, Colette, Crouzy, Serge, Jancsó, Attila, Delangle, Pascale

“…The essential Cu(i) and the toxic Hg(ii) ions possess similar coordination properties, and therefore, similar cysteine rich proteins participate in the control…”
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C-terminal Cysteines of CueR Act as Auxiliary Metal Site Ligands upon Hg II Binding-A Mechanism To Prevent Transcriptional Activation by Divalent Metal Ions? by Balogh, Ria K, Gyurcsik, Béla, Hunyadi-Gulyás, Éva, Schell, Juliana, Thulstrup, Peter W, Hemmingsen, Lars, Jancsó, Attila

“…Intracellular Cu is controlled by the transcriptional regulator CueR, which effectively discriminates between monovalent and divalent metal ions. It is…”
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Oligopeptide models of the metal binding loop of the bacterial copper efflux regulator protein CueR as potential Cu(I) chelators by Mesterházy, Edit, Boff, Bastien, Lebrun, Colette, Delangle, Pascale, Jancsó, Attila

“…Copper(I) binding features of oligopeptides, mimicking the metal binding loops (MBL) of the bacterial copper efflux regulator protein CueR, were investigated…”
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Tying Up a Loose End: On the Role of the C‐Terminal CCHHRAG Fragment of the Metalloregulator CueR by Balogh, Ria K., Gyurcsik, Béla, Jensen, Mikael, Thulstrup, Peter W., Köster, Ulli, Christensen, Niels Johan, Jensen, Marianne L., Hunyadi‐Gulyás, Éva, Hemmingsen, Lars, Jancsó, Attila

“…The transcriptional regulator CueR is activated by the binding of CuI, AgI, or AuI to two cysteinates in a near‐linear fashion. The C‐terminal CCHHRAG sequence…”
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Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from Ag I to Cd II by Balogh, Ria K, Gyurcsik, Béla, Jensen, Mikael, Thulstrup, Peter W, Köster, Ulli, Christensen, Niels Johan, Mørch, Frederik J, Jensen, Marianne L, Jancsó, Attila, Hemmingsen, Lars

“…Selectivity for monovalent metal ions is an important facet of the function of the metalloregulatory protein CueR. Ag perturbed angular correlation of γ-rays…”
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Modulation of the catalytic activity of a metallonuclease by tagging with oligohistidine by Abd Elhameed, Heba A.H., Hajdu, Bálint, Jancsó, Attila, Kéri, Albert, Galbács, Gábor, Hunyadi-Gulyás, Éva, Gyurcsik, Béla

“…Peptide tags are extensively used for affinity purification of proteins. In an optimal case, these tags can be completely removed from the purified protein by…”
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Synthesis and spectroscopic characterization of novel GFP chromophore analogues based on aminoimidazolone derivatives by Jancsó, Attila, Kovács, Ervin, Cseri, Levente, Rózsa, Balázs J., Galbács, Gábor, Csizmadia, Imre G., Mucsi, Zoltán

“…In order to improve the fluorescence properties of the green fluorescent protein chromophore, p‑HOBDI…”
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Magnesium(II)‐ATP Complexes in 1‐Ethyl‐3‐Methylimidazolium Acetate Solutions Characterized by 31Mg β‐Radiation‐Detected NMR Spectroscopy by McFadden, Ryan M. L., Szunyogh, Dániel, Bravo‐Frank, Nicholas, Chatzichristos, Aris, Dehn, Martin H., Fujimoto, Derek, Jancsó, Attila, Johannsen, Silke, Kálomista, Ildikó, Karner, Victoria L., Kiefl, Robert F., Larsen, Flemming H., Lassen, Jens, Levy, C. D. Philip, Li, Ruohong, McKenzie, Iain, McPhee, Hannah, Morris, Gerald D., Pearson, Matthew R., Sauer, Stephan P. A., Sigel, Roland K. O., Thulstrup, Peter W., MacFarlane, W. Andrew, Hemmingsen, Lars, Stachura, Monika

“…The complexation of MgII with adenosine 5′‐triphosphate (ATP) is omnipresent in biochemical energy conversion, but is difficult to interrogate directly. Here…”
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C‐terminal Cysteines of CueR Act as Auxiliary Metal Site Ligands upon HgII Binding—A Mechanism To Prevent Transcriptional Activation by Divalent Metal Ions? by Balogh, Ria K., Gyurcsik, Béla, Hunyadi‐Gulyás, Éva, Schell, Juliana, Thulstrup, Peter W., Hemmingsen, Lars, Jancsó, Attila

“…Intracellular CuI is controlled by the transcriptional regulator CueR, which effectively discriminates between monovalent and divalent metal ions. It is…”
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