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...

وصف كامل

محفوظ في:
التفاصيل البيبلوغرافية
المؤلفون الرئيسيون: Thakur, Abhay Kumar, Srivastava, Atul Kumar, Srinivas, Volety, Chary, Kandala Venkata Ramana, Rao, Chintalagiri Mohan
التنسيق: Artigo
اللغة:Inglês
منشور في: American Society for Biochemistry and Molecular Biology 2011
الموضوعات:
Protein Structure and Folding
الوصول للمادة أونلاين: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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