Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

D R Brown, H Kozlowski

Research output: Contribution to journalArticlepeer-review

296 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)1907-1917
Number of pages11
JournalDalton Transactions
Volume2004
DOIs
Publication statusPublished - 2004

Fingerprint Dive into the research topics of 'Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases'. Together they form a unique fingerprint.

Cite this