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- W2045261923 endingPage "1907" @default.
- W2045261923 startingPage "1907" @default.
- W2045261923 abstract "A change of the prion protein conformation results in a class of neurodegenerative diseases called the transmissible spongiform encephalopathies (like mad cow and Creutzfeld-Jakob diseases). The function of the normal prion protein is unknown, although much of recent research demonstrates the it may be a copper binding protein selective for Cu(II). Amyloid precursor protein (APP) releases the 39-42 amino acid peptide, a major constituent of the deposit in plaques of Alzheimer disease brain. Also APP is a metal binding protein, including copper ions. The link between copper and both proteins may provide insight into the role of metals in neurodegenerative pathologies." @default.
- W2045261923 created "2016-06-24" @default.
- W2045261923 creator A5050708434 @default.
- W2045261923 creator A5091019722 @default.
- W2045261923 date "2004-01-01" @default.
- W2045261923 modified "2023-10-10" @default.
- W2045261923 title "Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases" @default.
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