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The Catalytic Redox Activity of Prion Protein–Cu<sup>II</sup> is Controlled by Metal Exchange with the Zn<sup>II</sup>–Thiolate Clusters of Zn<sub>7</sub>Metallothionein-3

The Catalytic Redox Activity of Prion Protein–CuII is Controlled by Metal Exchange with the ZnII–Thiolate Clusters of Zn7Metallothionein-3

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MELONI, Gabriele, Andrea CRAMERI, Günter FRITZ, Paul DAVIES, David R. BROWN, Peter KRONECK, Milan VAŠÁK, 2012. The Catalytic Redox Activity of Prion Protein–CuII is Controlled by Metal Exchange with the ZnII–Thiolate Clusters of Zn7Metallothionein-3. In: ChemBioChem. 13(9), pp. 1261-1265. ISSN 1439-4227. eISSN 1439-7633

@article{Meloni2012-06-18Catal-23613, title={The Catalytic Redox Activity of Prion Protein–CuII is Controlled by Metal Exchange with the ZnII–Thiolate Clusters of Zn7Metallothionein-3}, year={2012}, doi={10.1002/cbic.201200198}, number={9}, volume={13}, issn={1439-4227}, journal={ChemBioChem}, pages={1261--1265}, author={Meloni, Gabriele and Crameri, Andrea and Fritz, Günter and Davies, Paul and Brown, David R. and Kroneck, Peter and Vašák, Milan} }

Fritz, Günter deposit-license Davies, Paul Silencing prion: Copper-catalyzed transformations of prion protein (PrP) lead to the production of reactive oxygen species (ROS), PrP oxidation, and cleavage and aggregation in transmissible spongiphorm encephalopathies. Zn(7) MT-3 efficiently targets Cu(II) bound in different coordination modes to PrP-Cu(II) . By an unusual redox-dependent metal-swap reaction, MT-3 modulates the catalytic redox properties of PrP-Cu(II) . Vašák, Milan Brown, David R. Crameri, Andrea Brown, David R. Crameri, Andrea 2012-06-18 eng Fritz, Günter The Catalytic Redox Activity of Prion Protein–Cu<sup>II</sup> is Controlled by Metal Exchange with the Zn<sup>II</sup>–Thiolate Clusters of Zn<sub>7</sub>Metallothionein-3 Meloni, Gabriele Meloni, Gabriele ChemBioChem ; 13 (2012), 9. - S. 1261-1265 Kroneck, Peter Kroneck, Peter Vašák, Milan Davies, Paul 2013-06-17T14:39:23Z 2013-06-17T14:39:23Z

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