Karran, E H and Allsop, D and Christie, G and Davis, J and Gray, C and Mansfield, F and Ward, R V (1998) Presenilins:in search of functionality. Biochemical Society Transactions, 26 (3). pp. 491-496. ISSN 0300-5127Full text not available from this repository.
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.
|Journal or Publication Title:||Biochemical Society Transactions|
|Uncontrolled Keywords:||Alzheimer Disease ; Amino Acid Sequence ; Animals ; Cell Membrane ; Humans ; Membrane Proteins ; Mice ; Mice, Knockout ; Models, Molecular ; Molecular Sequence Data ; Neurons ; Point Mutation ; Presenilin-1 ; Presenilin-2 ; Protein Conformation ; Signal Transduction|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited On:||07 Nov 2011 12:11|
|Last Modified:||24 Jan 2016 01:18|
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