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dc.contributor.authorVerdile, Giuseppe
dc.contributor.authorGandy, S.
dc.contributor.authorMartins, R.
dc.date.accessioned2017-01-30T11:41:49Z
dc.date.available2017-01-30T11:41:49Z
dc.date.created2015-09-29T01:51:53Z
dc.date.issued2007
dc.identifier.citationVerdile, G. and Gandy, S. and Martins, R. 2007. The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid. Neurochemical Research. 32 (4-5): pp. 609-623.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/14145
dc.identifier.doi10.1007/s11064-006-9131-x
dc.description.abstract

The biogenesis and accumulation of the beta amyloid protein (Aß) is a key event in the cascade of oxidative and inflammatory processes that characterises Alzheimer’s disease. The presenilins and its interacting proteins play a pivotal role in the generation of Aß from the amyloid precursor protein (APP). In particular, three proteins (nicastrin, aph-1 and pen-2) interact with presenilins to form a large multi-subunit enzymatic complex (?-secretase) that cleaves APP to generate Aß. Reconstitution studies in yeast and insect cells have provided strong evidence that these four proteins are the major components of the ?-secretase enzyme. Current research is directed at elucidating the roles that each of these protein play in the function of this enzyme. In addition, a number of presenilin interacting proteins that are not components of ?-secretase play important roles in modulating Aß production. This review will discuss the components of the ?-secretase complex and the role of presenilin interacting proteins on ?-secretase activity.

dc.publisherKluwer Academic Publishers-Plenum Publishers
dc.titleThe Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
dc.typeJournal Article
dcterms.source.volume32
dcterms.source.number4-5
dcterms.source.startPage609
dcterms.source.endPage623
dcterms.source.issn0364-3190
dcterms.source.titleNeurochemical Research
curtin.accessStatusOpen access via publisher


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