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Copper Alters Aggregation Behavior of Prion Protein and Induces Novel Interactions between Its N- and C-terminal Regions
Copper is reported to promote and prevent aggregation of prion protein. Conformational and functional consequences of Cu(2+)-binding to prion protein (PrP) are not well understood largely because most of the Cu(2+)-binding studies have been performed on fragments and truncated variants of the prion...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2011
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3207452/ https://ncbi.nlm.nih.gov/pubmed/21900252 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.265645 |
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