(Q28249607)

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H H Slunt

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G Thinakaran

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D L Price

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S S Sisodia

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D R Borchelt

Journal of Biological Chemistry

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language of work or name

English

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publication date

26 September 1997

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published in

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volume

272

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issue

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page(s)

24536-41

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cites work

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

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Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene

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Candidate gene for the chromosome 1 familial Alzheimer's disease locus

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Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene

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Assessment of normal and mutant human presenilin function in Caenorhabditis elegans

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Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins.

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Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo

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Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice

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A vector for expressing foreign genes in the brains and hearts of transgenic mice

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Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1

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Hyperaccumulation of FAD-linked presenilin 1 variants in vivo

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Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing

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Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo

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Evidence for phosphorylation and oligomeric assembly of presenilin 1.

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Presenilin Proteins Undergo Heterogeneous Endoproteolysis between Thr291and Ala299and Occur as Stable N- and C-Terminal Fragments in Normal and Alzheimer Brain Tissue

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