Výsledky vyhledávání

Chemical Rescue of Active Site Mutants of S. pneumoniae Surface Endonuclease EndA and Other Nucleases of the HNH Family by Imidazole

Autor: Midon M., Gimadutdinow O., Meiss G., Friedhoff P., Pingoud A.

Publikováno v: SCOPUS14394227-2012-13-5-SID84858304940

The His-Asn-His (HNH) motif characterizes the active sites of a large number of different nucleases such as homing endonucleases, restriction endonucleases, structure-specific nucleases and, in particular, nonspecific nucleases. Several biochemical s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::148680eddb7ead57e510bddb6e58ea10
https://openrepository.ru/article?id=715760

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Production and characterization of recombinant protein preparations of Endonuclease G-homologs from yeast, C. elegans and humans

Autor: Kieper J., Lauber C., Gimadutdinow O., Urbaǹska A., Cymerman I., Ghosh M., Szczesny B., Meiss G.

Publikováno v: SCOPUS10465928-2010-73-1-SID77955365267

Nuc1p, CPS-6, EndoG and EXOG are evolutionary conserved mitochondrial nucleases from yeast, Caenorhabditis elegans and humans, respectively. These enzymes play an important role in programmed cell death as well as mitochondrial DNA-repair and recombi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::21866ab1d672ac13f3959bbaa30d3b03
https://openrepository.ru/article?id=669524

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Interaction of DNA Fragmentation Factor (DFF) with DNA reveals an unprecedented mechanism for nuclease inhibition and suggests that DFF can be activated in a DNA-bound state

Autor: Korn C., Scholz S., Gimadutdinow O., Lurz R., Pingoud A., Meiss G.

Publikováno v: SCOPUS00219258-2005-280-7-SID14044274338

DNA fragmentation factor (DFF) is a complex of the DNase DFF40 (CAD) and its chaperone/inhibitor DFF45 (ICAD-L) that can be activated during apoptosis to induce DNA fragmentation. Here, we demonstrate that DFF directly binds to DNA in vitro without p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::1865fbbc97aec95e36d0f939be8214f6
https://openrepository.ru/article?id=709244

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Structural basis for stable DNA complex formation by the caspase-activated DNase

Autor: Reh S., Korn C., Gimadutdinow O., Meiss G.

Publikováno v: SCOPUS00219258-2005-280-50-SID29244462831

We describe a structural model for DNA binding by the caspase-activated DNase (CAD). Results of a mutational analysis and computational modeling suggest that DNA is bound via a positively charged surface with two functionally distinct regions, one be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::42b83a71fe4e4ce67f9d4374aab68706
https://openrepository.ru/article?id=709243

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Structural and functional characterization of mitochondrial EndoG, a sugar non-specific nuclease which plays an important role during apoptosis

Autor: Schäfer P., Scholz S., Gimadutdinow O., Cymerman I., Bujnicki J., Ruiz-Carrillo A., Pingoud A., Meiss G.

Publikováno v: SCOPUS00222836-2004-338-2-SID1842452746

Combining sequence analysis, structure prediction, and site-directed mutagenesis, we have investigated the mechanism of catalysis and substrate binding by the apoptotic mitochondrial nuclease EndoG, which belongs to the large family of DNA/RNA non-sp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::5064220b3e88781bb3aaa1ffe25dfa4e
https://openrepository.ru/article?id=39716

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Experimental evidence for a ββα-Me-finger nuclease motif to represent the active site of the caspase-activated DNase

Autor: Scholz S., Korn C., Bujnicki J., Gimadutdinow O., Pingoud A., Meiss G.

Publikováno v: SCOPUS00062960-2003-42-31-SID0042573738

The caspase-activated DNase (CAD) is an important nuclease involved in apoptotic DNA degradation. Results of a sequence comparison of CAD proteins with ββα-Me-finger nucleases in conjunction with a mutational and chemical modification analysis sug

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::43d75dca1ed7615611208771ae5a6658
https://openrepository.ru/article?id=198955

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Involvement of conserved histidine, lysine and tyrosine residues in the mechanism of DNA cleavage by the caspase-3 activated DNase CAD

Autor: Korn C., Scholz S., Gimadutdinow O., Pingoud A., Meiss G.

Publikováno v: SCOPUS03051048-2002-30-6-SID0037085733

The caspase-activated DNase (CAD) is involved in DNA degradation during apoptosis. Chemical modification of murine CAD with the lysine-specific reagent 2,4,6-trinitrobenzenesulphonic acid and the tyrosine-specific reagent N-acetylimidazole leads to i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::18f7774c803ab643d56bb560f08b5c13
https://dspace.kpfu.ru/xmlui/handle/net/133859

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The effect of ICAD-S on the formation and intracellular distribution of a nucleolytically active caspase-activated DNase

Autor: Scholz S., Korn C., Gimadutdinow O., Knoblauch M., Pingoud A., Meiss G.

Publikováno v: SCOPUS03051048-2002-30-14-SID0037100613

We show here that co-expression of murine CAD with either ICAD-L or ICAD-S in Escherichia coli as well as mammalian cells leads to a functional DFF complex, which after caspase-3 activation releases a nucleolytically active DNase. The chaperone activ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::47f525445326565cf9780cdb8fae1305
https://openrepository.ru/article?id=668089

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