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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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2012

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Meloni, Gabriele
Crameri, Andrea
Davies, Paul
Brown, David R.
Vašák, Milan

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ChemBioChem. 2012, 13(9), pp. 1261-1265. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201200198

Zusammenfassung

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) .

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Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Copper, metallothionein-3, prion proteins, reactive oxygen species, zinc

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ISO 690MELONI, Gabriele, Andrea CRAMERI, Günter FRITZ, Paul DAVIES, David R. BROWN, Peter M. H. 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. 2012, 13(9), pp. 1261-1265. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201200198
BibTex
@article{Meloni2012-06-18Catal-23613,
  year={2012},
  doi={10.1002/cbic.201200198},
  title={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},
  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 M. H. and Vašák, Milan}
}
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