
Most gene mutations associated with Alzheimer's disease point to the metabolism of amyloid precursor protein as potential cause. The beta- and gamma-secretases are two executioners of amyloid precursor protein processing resulting in amyloid beta. Significant progress has been made in the selective inhibition of both proteases, regardless of structural information for gamma-secretase. Several peptidic and non-peptidic leads were identified and first drug candidates are in clinical trials. This review focuses on the developments since 2003.
Models, Molecular, Alzheimer Disease, Endopeptidases, Animals, Aspartic Acid Endopeptidases, Humans, Amino Acid Sequence, Amyloid Precursor Protein Secretases, Enzyme Inhibitors, Cell Line
Models, Molecular, Alzheimer Disease, Endopeptidases, Animals, Aspartic Acid Endopeptidases, Humans, Amino Acid Sequence, Amyloid Precursor Protein Secretases, Enzyme Inhibitors, Cell Line
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