Lancaster EPrints

Presenilins:in search of functionality

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 0300-5127

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Abstract

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.

Item Type: Article
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
Subjects: UNSPECIFIED
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 50829
Deposited By: ep_importer_pure
Deposited On: 07 Nov 2011 12:11
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 19:43
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/50829

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