Results 191 to 200 of about 40,397 (225)

Presenilin-1 in late-onset depressive disorder

Psychiatry Research, 2000
Late-onset depressive disorder (LOD) is thought to be associated with dementia. Allele 1 in the presenilin-1 (PS-1) gene is a risk factor for Alzheimer's disease. An association study on this polymorphism was performed in depressive patients and control subjects. The patients were subdivided into those with early onset and late onset, using 50 years as
K, Ohara, Y, Suzuki, D, Ohta, K, Ohara
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Presenilin 1: more than just γ-secretase

Biochemical Society Transactions, 2005
Presenilin 1 plays a central catalytic role in the γ-secretase processing of amyloid precursor protein, Notch and many other substrates. However, this core component clearly mediates independently several other physiological roles in the cell/neuron. Besides its involvement in β-catenin degradation, we discuss here the recent implication of presenilin ...
T, Raemaekers, C, Esselens, W, Annaert
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Presenilin-1 regulates neuronal differentiation during neurogenesis

Development, 2000
ABSTRACT Mutations in Presenilin-1 (PSP) are a major cause of familial Alzheimer’s disease. Our previous studies showed that PS1 is required for murine neural development. Here we report that lack of PS1 leads to premature differentiation of neural progenitor cells, indicating a role for PS1 in a cell fate decision between postmitotic ...
M, Handler, X, Yang, J, Shen
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Presenilin-1 is located in rat mitochondria

Biochemical and Biophysical Research Communications, 2002
Presenilins are mutated in most cases of autosomal dominant inherited forms of early onset Alzheimer's disease and such mutations are known to sensitize cells to apoptotic stimuli in vitro. Previous studies show that presenilins are primarily located in the endoplasmatic reticulum and cell membranes.
Maria, Ankarcrona, Kjell, Hultenby
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Mutation of conserved aspartates affect maturation of presenilin 1 and presenilin 2 complexes.

Acta neurologica Scandinavica. Supplementum, 2001
Presenilin (PS1 and PS2) holoproteins are transiently incorporated into low molecular weight (MW) complexes. During subsequent incorporation into a higher MW complex, they undergo endoproteolysis to generate stable N- and C-terminal fragments (NTF/CTF).
Tandon, A, Holmes, E, Rogaeva, E, Arawaka, S, Supala, A, St GeorgeHyslop, P, Haass, C, Fraser, P, Milman, P, Zhang, DM, Kawarai, T, Chen, F, Yu, G, Steiner, H, Nishimura, M, Song, YQ   +15 more
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Biochemical properties of endogenous presenilin 1 and presenilin 2 in cultured human B-lymphocytes

Clinical Chemical Laboratory Medicine, 2007
AbstractClin Chem Lab Med 2007;45:1273–6.
Lukasz, Bojarski, Andrzej, Lewandowicz, Magdalena, Blazejczyk, Adam, Sobczak, Jacek, Kuznicki, Urszula, Wojda   +5 more
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[Biochemistry of presenilin 1].

Rinsho shinkeigaku = Clinical neurology, 1998
The majority of cases of early-onset familial Alzheimer disease are caused by mutations in the recently identified presenilin 1 (PS 1) gene, located on chromosome 14. PS1, a 467 amino acid protein, is predicted to be an integral membrane protein containing seven putative transmembrane domains and a large hydrophilic loop between the sixth and seventh ...
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Metabolism and Function of Presenilin 1

1998
Neither the normal functions of presenilins nor the mechanism(s) by which familial Alzheimer’s disease (FAD)-linked mutations cause AD have been defined. Presenilin 1 (PS1) is a polytopic membrane protein that is subject to endoproteolytic processing in vivo; PS1 derivatives accumulate to saturable levels and to ~ 1:1 stoichiometry by mechanism(s) that
S. S. Sisodia, G. Thinakaran, P. C. Wong, D. R. Borchelt, M. K. Lee, A. Doan, J. Regard, H. Chen, H. Zheng, C. Eckman, H. H. Slunt, T. Ratovitsky, F. Davenport, C. Harris, L. H. T. Van der Ploeg, S. G. Younkin, N. A. Jenkins, N. G. Copeland, D. L. Price   +18 more
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Neuronal Regulation of Presenilin-1 Processing

1998
Presenilin 1 (PS1) is ubiquitously expressed but causes pathology only in the brain. The basis of this neuropathogenic specificity is unknown. In non-neuronal cells, PS1 is localized predominantly in the endoplasmic reticulum, where it co- localizes with the resident endoplasmic reticulum protein BiP.
H. Hartmann, J. Busciglio, B. A. Yankner
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Molecular consequences of presenilin-1 mutation

Nature, 2001
C. RUSSO, SCHETTINI, GENNARO, TC SAIDO, C. HULETTE, C. LIPPA, L. LANNFELT, B. GHETTI, P. GAMBETTI, TABATON, MASSIMO, JK TELLER   +9 more
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