Results 201 to 210 of about 25,523 (241)
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Presenilins – in search of functionality

Biochemical Society Transactions, 1998
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 ...
Karran, E H   +6 more
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Presenilin immunoreactivity in Alzheimer's disease

European Journal of Neurology, 2005
The role of presenilin (PS) mutations in familial Alzheimer's disease (AD) may be as a toxic gain of function, but in sporadic disease their contribution is more difficult to understand. In this study, we investigated PS proteins in sporadic AD by comparing the immunocytochemical profiles in sporadic AD with control brains using a quantitative ...
P K, Panegyres, K, Toufexis
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Amyloid, Presenilins, and Alzheimer’s Disease

The Neuroscientist, 2003
The regulated intramembrane proteolysis of the amyloid precursor protein (APP) that results in the generation of a toxic 40 to 42 amino acid fragment, Aβ, and a C-terminal intracellular fragment stands central in the pathogenesis of Alzheimer’s disease.
Geert, Van Gassen, Wim, Annaert
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Presenilin mutations in Alzheimer's disease

Human Mutation, 1998
The presenilins (PS-1 and PS-2) are 2 members of a novel family of genes encoding integral membrane proteins recently implicated in Alzheimer's disease (AD) pathology. To date, 43 mutations have been identified in PS-1 and 2 in PS-2 that lead to familial presenile AD (onset before age 65 years). The normal and pathological functions of the PS proteins (
Cruts, Marc, Van Broeckhoven, Christine
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Presenile because of presenilin

Current Opinion in Neurology, 1996
Alzheimer's disease is a neurodegenerative disorder characterized by the massive and invariant accumulation of amyloid plaques in the brains of affected patients. In many cases Alzheimer's disease occurs in the absence of a prior history of the disease in other family members and is designated as sporadic, whereas in approximately 10% of patients ...
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Presenilin Function in APP Processing

Annals of the New York Academy of Sciences, 2000
Abstract: Familial Alzheimer's disease (FAD) is now linked to at least three genes encoding the amyloid precursor protein (APP) on chromosome 21, and presenilin 1 and 2 on chromosome 14 and 1, respectively. FAD cases in whom presenilin mutations occur are more frequent than those with APP mutations.
W, Annaert   +3 more
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Peering into proteolysis with presenilins

Journal of Alzheimer's Disease, 2001
Presenilins were originally identified because they cause a neurodegenerative disease, but the impact of these proteins on the neuron appears to extend beyond neurodegeneration and into fundamental concepts of cell biology and development. Presenilins were identified as a result of the steady march of molecular genetics which first lead to ...
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The Phosphorylation of Presenilin Proteins

2003
The phosphorylation of presenilin (PS) proteins was initially analyzed in cultured cells overexpressing the respective proteins. These studies revealed that the homologous PS proteins are differentially phosphorylated in vivo. Fulllength PS2 was found to be constitutively phosphorylated on serine residues (1,2). In contrast, very little if any (1) or a
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Metabolism of presenilins.

Journal of molecular neuroscience : MN, 2002
Understanding mechanisms involved in the production of Abeta has long been the central focus of cell biologists engaged in molecular AD research. The discovery of two genes that encode homologous polytopic membrane proteins termed Presenilins (PS), has lead to several exciting recent findings on the proteolytic processes responsible for generating the ...
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Presenilin genes and Alzheimer's disease

1999
Abstract n.223 pag ...
Sorbi S.   +15 more
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