Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Anikó Czene"'
Publikováno v:
Protein Science. 25:1977-1988
X-ray diffractometry dominates protein studies, as it can provide 3D structures of these diverse macromolecules or their molecular complexes with interacting partners: substrates, inhibitors, and/or cofactors. Here, we show that under cocrystallizati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52bcd73e4e49bb3c56cb2e0ba454ac2e
https://doi.org/10.1002/pro.3010
https://doi.org/10.1002/pro.3010
Autor:
Hans Erik Mølager Christensen, Béla Gyurcsik, Milan Kožíšek, Kyosuke Nagata, Peter W. Thulstrup, Anikó Czene, Tamás Körtvélyesi, Eszter Németh
Publikováno v:
Protein Science. 23:1113-1122
The nuclease domain of colicin E7 (NColE7) promotes the nonspecific cleavage of nucleic acids at its C-terminal HNH motif. Interestingly, the deletion of four N-terminal residues (446–449 NColE7 = KRNK) resulted in complete loss of the enzyme activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::efa5ff6ea74de49cbb1a38e19a8b9898
https://doi.org/10.1002/pro.2497
https://doi.org/10.1002/pro.2497
Autor:
Leila Lo Leggio, Harm Otten, Jens-Christian N. Poulsen, Anikó Czene, Hans Erik Mølager Christensen, Kyosuke Nagata, Sine Larsen, Eszter Tóth, Béla Gyurcsik
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:551-554
The metallonuclease colicin E7 is a member of the HNH family of endonucleases. It serves as a bacterial toxin in Escherichia coli, protecting the host cell from other related bacteria and bacteriophages by degradation of their chromosomal DNA under e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d03e64da7d0573936628e6aac208fd2f
https://doi.org/10.1107/s1744309113008233
https://doi.org/10.1107/s1744309113008233
Autor:
Eszter, Németh, Tamás, Körtvélyesi, Peter W, Thulstrup, Hans E M, Christensen, Milan, Kožíšek, Kyosuke, Nagata, Anikó, Czene, Béla, Gyurcsik
Publikováno v:
Protein science : a publication of the Protein Society. 23(8)
The nuclease domain of colicin E7 (NColE7) promotes the nonspecific cleavage of nucleic acids at its C-terminal HNH motif. Interestingly, the deletion of four N-terminal residues (446–449 NColE7 = KRNK) resulted in complete loss of the enzyme activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4e43fac10ebf76a8cd7c09a3208784d6
https://pubmed.ncbi.nlm.nih.gov/24895333
https://pubmed.ncbi.nlm.nih.gov/24895333
Autor:
Lubomír Rulíšek, Harm Otten, Kyosuke Nagata, Eszter Németh, Hans Erik Mølager Christensen, Eszter Tóth, Béla Gyurcsik, Jens-Christian N. Poulsen, Anikó Czene, Sine Larsen
Publikováno v:
Czene, A, Tóth, E, Németh, E, Otten, H, Poulsen, J-C N, Christensen, H E M, Rulíšek, L, Nagata, K, Larsen, S & Gyurcsik, B 2014, ' A new insight into the zinc-dependent DNA-cleavage by the colicin E7 nuclease: a crystallographic and computational study. ', Metallomics, vol. 6, no. 11, pp. 2090-2099 . https://doi.org/10.1039/c4mt00195h
Czene, A, Tóth, E, Németh, E, Otten, H, Poulsen, J-C N, Christensen, H E M, Rulíšek, L, Nagata, K, Larsen, S & Gyurcsik, B 2014, ' A new insight into the zinc-dependent DNA-cleavage by the colicin E7 nuclease : a crystallographic and computational study ', Metallomics, vol. 6, no. 11, pp. 2090-2099 . https://doi.org/10.1039/c4mt00195h
Czene, A, Tóth, E, Németh, E, Otten, H, Poulsen, J-C N, Christensen, H E M, Rulíšek, L, Nagata, K, Larsen, S & Gyurcsik, B 2014, ' A new insight into the zinc-dependent DNA-cleavage by the colicin E7 nuclease : a crystallographic and computational study ', Metallomics, vol. 6, no. 11, pp. 2090-2099 . https://doi.org/10.1039/c4mt00195h
The nuclease domain of colicin E7 metallonuclease (NColE7) contains its active centre at the C-terminus. The mutant ΔN4-NColE7-C∗-where the four N-terminal residues including the positively charged K446, R447 and K449 are replaced with eight resid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad12182f52b56357922de9ba6bfb6c85
https://orbit.dtu.dk/en/publications/0084af8c-2e00-43de-b8b3-c612c7b5587f
https://orbit.dtu.dk/en/publications/0084af8c-2e00-43de-b8b3-c612c7b5587f
Autor:
Zoltán Kele, Krystyna Ślaska-Kiss, Antal Kiss, Anikó Czene, Béla Gyurcsik, Noémi I. Jakab-Simon, Hajnalka Jankovics
Publikováno v:
Protein expression and purification. 89(2)
The HNH family of endonucleases is characterized by a ββα metal-finger structural motif. Colicin E7 is a representative member of this family containing the strictly conserved HNH motif at its C-terminus. Structural and biochemical studies suggest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1ac04f960ef52b7da726b4376182232
https://pubmed.ncbi.nlm.nih.gov/23563167
https://pubmed.ncbi.nlm.nih.gov/23563167
Autor:
István G. Zóka, Béla Gyurcsik, Eszter Németh, Kyosuke Nagata, Anikó Czene, Tamás Körtvélyesi, Hans Erik Mølager Christensen, Noémi I. Jakab-Simon
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 18(3)
Colicin E7 (ColE7) is a metallonuclease toxin of Escherichia coli belonging to the HNH superfamily of nucleases. It contains highly conserved amino acids in its HHX(14)NX(8)HX(3)H ββα-type metal ion binding C-terminal active centre. However, the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef02fda5eac68abf69b271da49d5c811
https://pubmed.ncbi.nlm.nih.gov/23334162
https://pubmed.ncbi.nlm.nih.gov/23334162
Autor:
Béla Gyurcsik, Anikó Czene
Publikováno v:
Future medicinal chemistry. 3(15)
The process of DNA targeting or repair of mutated genes within the cell, induced by specifically positioned double-strand cleavage of DNA near the mutated sequence, can be applied for gene therapy of monogenic diseases. For this purpose, highly speci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d6a1f5a37d962f24ce7b2eb5a56ad92
https://pubmed.ncbi.nlm.nih.gov/22023035
https://pubmed.ncbi.nlm.nih.gov/22023035