
doi: 10.1042/bst0260491
pmid: 9765902
The discovery of the PS proteins, the complexities of their biochemistry and their potential involvement in signalling pathways and in apoptosis have galvanized research into AD. To date, the aspect of the functionality of the PSs most relevant to the pathology of AD is the effect of PS FAD mutants to increase the proportion of A beta 42 produced from cells. This, coupled to the observation that gamma-secretase cleavage is considerably reduced in neurons derived from PS-1 knockout mice, argues strongly that PS plays a very direct role in the proteolytic processing of APP.
Mice, Knockout, Models, Molecular, Neurons, 570, Protein Conformation, Cell Membrane, Molecular Sequence Data, 500, Membrane Proteins, Mice, Alzheimer Disease, Presenilin-2, Presenilin-1, Animals, Humans, Point Mutation, Amino Acid Sequence, Signal Transduction
Mice, Knockout, Models, Molecular, Neurons, 570, Protein Conformation, Cell Membrane, Molecular Sequence Data, 500, Membrane Proteins, Mice, Alzheimer Disease, Presenilin-2, Presenilin-1, Animals, Humans, Point Mutation, Amino Acid Sequence, Signal Transduction
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