Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-65051
Meloni, Gabriele; Crameri, Andrea; Fritz, Günter; Davies, Paul; Brown, David R; Kroneck, Peter M H; Vašák, Milan (2012). The catalytic redox activity of prion protein-Cu(II) is controlled by metal exchange with the Zn(II) -thiolate clusters of Zn(7) metallothionein-3. ChemBioChem, 13(9):1261-1265.
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Abstract
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).
| Item Type: | Journal Article, refereed, original work |
|---|---|
| Communities & Collections: | 04 Faculty of Medicine > Institute of Biochemistry 07 Faculty of Science > Institute of Biochemistry |
| DDC: | 570 Life sciences; biology |
| Language: | English |
| Date: | 2012 |
| Deposited On: | 09 Oct 2012 14:42 |
| Last Modified: | 26 Nov 2012 04:46 |
| Publisher: | Wiley-Blackwell |
| ISSN: | 1439-4227 |
| Publisher DOI: | 10.1002/cbic.201200198 |
| PubMed ID: | 22615124 |
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