Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Béla, Gyurcsik"'
Publikováno v:
Inorganics, Vol 11, Iss 8, p 334 (2023)
The chirality of the polyether ionophore monensic acid A can be successfully used to study its coordination ability in solution. A complementary approach to gain new insights into the complexation chemistry of the antibiotic (studied previously by ci
Externí odkaz:
https://doaj.org/article/c45e57f04a5b45668bb358c41bd2ef81
Publikováno v:
Molecules, Vol 28, Iss 14, p 5511 (2023)
The nuclease domain of colicin E7 cleaves double-strand DNA non-specifically. Zn2+ ion was shown to be coordinated by the purified NColE7 as its native metal ion. Here, we study the structural and catalytic aspects of the interaction with Ni2+, Cu2+
Externí odkaz:
https://doaj.org/article/6fb3678e14a746ac91e45d087c0e3d56
Publikováno v:
Inorganics, Vol 11, Iss 2, p 64 (2023)
Cys2His2 zinc finger proteins are important for living organisms, as they—among other functions—specifically recognise DNA when Zn(II) is coordinated to the proteins, stabilising their ββα secondary structure. Therefore, competition with other
Externí odkaz:
https://doaj.org/article/62aa7cedfbc74730a1674b05577b0c1d
Autor:
Tatsiana V. Petrasheuskaya, Ferenc Kovács, Nóra Igaz, Andrea Rónavári, Bálint Hajdu, Laura Bereczki, Nóra V. May, Gabriella Spengler, Béla Gyurcsik, Mónika Kiricsi, Éva Frank, Éva A. Enyedy
Publikováno v:
Molecules, Vol 28, Iss 1, p 54 (2022)
A series of novel estradiol-based salicylaldehyde (thio)semicarbazones ((T)SCs) bearing (O,N,S) and (O,N,O) donor sets and their Cu(II) complexes were developed and characterized in detail by 1H and ¹³C nuclear magnetic resonance spectroscopy, UV
Externí odkaz:
https://doaj.org/article/8955a198063c498eaca85577a98baf1a
Publikováno v:
Protein expression and purification. 201
β-lactamases protect bacteria from β-lactam antibiotics. Temoneira (TEM) is a class A serine β-lactamase and its coding sequence is designed into DNA vectors, such as pET-21a (+), to provide antibiotic resistance. TEM-1 β-lactamase was overexpres
Autor:
Ria K. Balogh, Béla Gyurcsik, Mikael Jensen, Peter W. Thulstrup, Ulli Köster, Niels Johan Christensen, Marianne L. Jensen, Éva Hunyadi‐Gulyás, Lars Hemmingsen, Attila Jancsó
Publikováno v:
Balogh, R K, Gyurcsik, B, Jensen, M, Thulstrup, P W, Köster, U, Christensen, N J, Jensen, M L, Hunyadi-Gulyás, É, Hemmingsen, L & Jancsó, A 2022, ' Tying Up a Loose End : On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR ', ChemBioChem, vol. 23, no. 16, e202200290 . https://doi.org/10.1002/cbic.202200290
Balogh, R K, Gyurcsik, B, Jensen, M, Thulstrup, P W, Koester, U, Christensen, N J, Jensen, M L, Hunyadi-Gulyas, E, Hemmingsen, L & Jancso, A 2022, ' Tying Up a Loose End : On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR ', ChemBioChem, vol. 23, no. 16, 202200290 . https://doi.org/10.1002/cbic.202200290
Balogh, R K, Gyurcsik, B, Jensen, M, Thulstrup, P W, Koester, U, Christensen, N J, Jensen, M L, Hunyadi-Gulyas, E, Hemmingsen, L & Jancso, A 2022, ' Tying Up a Loose End : On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR ', ChemBioChem, vol. 23, no. 16, 202200290 . https://doi.org/10.1002/cbic.202200290
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 in Escherichia coli CueR present potential additional metal binding ligands and here we ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e6e74408ddfdb1383338cefccbfcb8c
https://orbit.dtu.dk/en/publications/6368e5c3-04de-46e9-b93c-38c71b9f0688
https://orbit.dtu.dk/en/publications/6368e5c3-04de-46e9-b93c-38c71b9f0688
Autor:
Vivien Pósa, Bálint Hajdu, Gábor Tóth, Orsolya Dömötör, Christian R. Kowol, Bernhard K. Keppler, Gabriella Spengler, Béla Gyurcsik, Éva A. Enyedy
Publikováno v:
SSRN Electronic Journal.
Thiosemicarbazones are promising candidates for anticancer therapy and their mechanism of action is often linked to their metal chelating ability. In this study, five (thio)semicarbazones with different donor sets (NNS, NNO, ONS, ONO) were selected a
Autor:
Søren Vrønning Hoffmann, Ria K. Balogh, Eszter Németh, Attila Jancsó, Béla Gyurcsik, Nykola C. Jones
Publikováno v:
Balogh, R K, Németh, E, Jones, N C, Hoffmann, S V, Jansco, A & Gyurcsik, B 2021, ' A study on the secondary structure of the metalloregulatory protein CueR : effect of pH, metal ions and DNA ', European Biophysics Journal, vol. 50, pp. 491-500 . https://doi.org/10.1007/s00249-021-01539-z
The response of CueR towards environmental changes in solution was investigated. CueR is a bacterial metal ion selective transcriptional metalloregulator protein, which controls the concentration of copper ions in the cell. Although several articles
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d74f3a9d6aae79664aedfc6bb8ae8c4
https://pure.au.dk/ws/files/305738714/A_study_on_the_secondary_structure_of_the_metalloregulatory_protein_CueR_effect_of_pH_metal_ions_and_DNA.pdf
https://pure.au.dk/ws/files/305738714/A_study_on_the_secondary_structure_of_the_metalloregulatory_protein_CueR_effect_of_pH_metal_ions_and_DNA.pdf
Autor:
Peter W. Thulstrup, Mikael Jensen, Ria K. Balogh, Frederik J. Mørch, Marianne L. Jensen, Niels Johan Christensen, Lars Hemmingsen, Attila Jancsó, Béla Gyurcsik, Ulli Köster
Publikováno v:
Balogh, R K, Gyurcsik, B, Jensen, M, Thulstrup, P W, Köster, U, Christensen, N J, Mørch, F J, Jensen, M L, Jancsó, A & Hemmingsen, L 2020, ' Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from Ag I to Cd II ', Chemistry: A European Journal, vol. 26, no. 33, pp. 7451-7457 . https://doi.org/10.1002/chem.202000132
Balogh, R K, Gyurcsik, B, Jensen, M, Thulstrup, P W, Köster, U, Christensen, N J, Mørch, F J, Jensen, M L, Jancso, A & Hemmingsen, L 2020, ' Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from Ag I to Cd II ', Chemistry-A European Journal, vol. 26, no. 33, pp. 7451-7457 . https://doi.org/10.1002/chem.202000132
Chemistry (Weinheim an Der Bergstrasse, Germany)
'Chemistry-A European Journal ', vol: 26, pages: 7451-7457 (2020)
Balogh, R K, Gyurcsik, B, Jensen, M, Thulstrup, P W, Köster, U, Christensen, N J, Mørch, F J, Jensen, M L, Jancso, A & Hemmingsen, L 2020, ' Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from Ag I to Cd II ', Chemistry-A European Journal, vol. 26, no. 33, pp. 7451-7457 . https://doi.org/10.1002/chem.202000132
Chemistry (Weinheim an Der Bergstrasse, Germany)
'Chemistry-A European Journal ', vol: 26, pages: 7451-7457 (2020)
Selectivity for monovalent metal ions is an important facet of the function of the metalloregulatory protein CueR. 111Ag perturbed angular correlation of γ‐rays (PAC) spectroscopy probes the metal site structure and the relaxation accompanying the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed2e8885dded3f35982e72607b8ebba6
https://curis.ku.dk/ws/files/242842319/chem.202000132.pdf
https://curis.ku.dk/ws/files/242842319/chem.202000132.pdf
Autor:
Bálint Hajdu, Kyosuke Nagata, Wojciech Bal, Agnieszka Belczyk-Ciesielska, Béla Gyurcsik, Aleksandra Sparavier, Masamitsu N. Asaka, Brigitta Csipak
Publikováno v:
Metallomics. 10:1089-1098
In this work we demonstrate that the previously described reaction of sequence specific Ni(ii)-dependent hydrolytic peptide bond cleavage can be performed in complex metalloprotein molecules, such as the Cys2His2 zinc finger proteins. The cleavage wi