http://www.cnr.it/ontology/cnr/individuo/prodotto/ID16040
Histamine modified 2'-deoxyriboadenosine - Potential copper binding site in DNAzymes. (Articolo in rivista)
- Type
- Label
- Histamine modified 2'-deoxyriboadenosine - Potential copper binding site in DNAzymes. (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.jinorgbio.2010.01.009 (literal)
- Alternative label
E. Lodyga-Chruscinska, E. Sochacka, D. Smuga, L. Chruscinski, G. Micera, D. Sanna, M. Turek, M. Gasiorkiewicz (2010)
Histamine modified 2'-deoxyriboadenosine - Potential copper binding site in DNAzymes.
in Journal of inorganic biochemistry
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- E. Lodyga-Chruscinska, E. Sochacka, D. Smuga, L. Chruscinski, G. Micera, D. Sanna, M. Turek, M. Gasiorkiewicz (literal)
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- http://www.sciencedirect.com/science/article/pii/S0162013410000279 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Institute of General Food Chemistry, Technical University of ?ód?, ul. Stefanowskiego 4/10, 90-924 ?ód?, Poland
Institute of Organic Chemistry, Technical University of ?ód?, ul. ?eromskiego 176, 90-924 ?ód?, Poland
Faculty of Process and Environmental Engineering, Technical University of ?ód? ul. Wólcza?ska 213, 90-924 ?ód?, Poland
Department of Chemistry, University of Sassari, via Vienna 2, I-07100 Sassari, Italy
Istituto C.N.R. Chimica Biomolecolare, Trav. La Crucca 3, reg. Baldinca, 07040 Sassari, Italy (literal)
- Titolo
- Histamine modified 2'-deoxyriboadenosine - Potential copper binding site in DNAzymes. (literal)
- Abstract
- Copper(II) complexes of histamine modified 2?-deoxyriboadenosine (N-[(9-?-D-2?-deoxyribofuranosylpurin-6-yl)-carbamoyl]histamine) ligand were studied by potentiometric, UV-visible and EPR techniques. The imidazole residue of the ligand was described as the main binding site forming mono-, bis-(ligand) and dimer complexes, but the interactions between adenosine nitrogen N(1) and carbamoyl nitrogen atoms and the copper(II) ion also were detected. This is the first report evaluating the coordinating ability of such a modified adenosine ligand towards copper(II) ion. Our findings suggest that histamine modified 2?-deoxyriboadenosine could chelate efficiently copper(II) ions if it were incorporated into DNAzyme sequence. (literal)
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