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- W2949412650 abstract "A conformational change of the prion protein is responsible for a class of neurodegenerative diseases called the transmissible spongiform encephalopathies that include mad cow disease and the human afflictions kuru and Creutzfeldt−Jakob disease. Despite the attention given to these diseases, the normal function of the prion protein in healthy tissue is unknown. Research over the past few years, however, demonstrates that the prion protein is a copper binding protein with high selectivity for Cu2+. The structural features of the Cu2+ binding sites have now been characterized and are providing important clues about the normal function of the prion protein and perhaps how metals or loss of protein function play a role in disease. The link between prion protein and copper may provide insight into the general, and recently appreciated, role of metals in neurodegenerative disease." @default.
- W2949412650 created "2019-06-27" @default.
- W2949412650 creator A5075994602 @default.
- W2949412650 date "2004-05-11" @default.
- W2949412650 modified "2023-09-27" @default.
- W2949412650 title "Copper Binding in the Prion Protein" @default.
- W2949412650 cites W2164960448 @default.
- W2949412650 doi "https://doi.org/10.1002/chin.200419283" @default.
- W2949412650 hasPublicationYear "2004" @default.
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