Results 141 to 150 of about 22,628 (189)

Generation and deposition of Aβ43 by the virtually inactive presenilin‐1 L435F mutant contradicts the presenilin loss‐of‐function hypothesis of Alzheimer's disease

EMBO Molecular Medicine, 2016
As stated by the prevailing amyloid cascade hypothesis, Alzheimer's disease (AD) is caused by the aggregation and cerebral deposition of long amyloid‐β peptide (Aβ) species, which are released from a C‐terminal amyloid precursor protein fragment by γ ...
Johannes Trambauer, Akio Fukumori, Elisabeth Kremmer   +2 more
exaly   +2 more sources

Toward the structure of presenilin/γ-secretase and presenilin homologs

Biochimica Et Biophysica Acta - Biomembranes, 2013
Presenilin is the catalytic component of the γ-secretase complex, a membrane-embedded aspartyl protease that plays a central role in biology and in the pathogenesis of Alzheimer's disease. Upon assembly with its three protein cofactors (nicastrin, Aph-1 and Pen-2), presenilin undergoes autoproteolysis into two subunits, each of which contributes one of
exaly   +3 more sources

Some of the next articles are maybe not open access.

Related searches:

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, Allsop, D, Christie, G, Davis, J, Gray, C, Mansfield, F, Ward, R V   +6 more
openaire   +2 more sources

Intramembrane proteolysis by presenilins

Nature Reviews Molecular Cell Biology, 2000
Many neurodegenerative diseases involve the deposition of insoluble amyloid molecules. In Alzheimer's disease, for example, the amyloid beta-peptide (A beta) is the main component of the characteristic senile plaques. Proteolytic enzymes called secretases are involved in generating A beta, and one of these may have been identified as presenilin--a ...
H, Steiner, C, Haass
openaire   +2 more sources

Presenilins and Alzheimer's disease

Current Opinion in Neurobiology, 1997
Mutations in the genes encoding the presenilins cause the majority of early-onset cases of Alzheimer's disease (AD). The identification of the presenilin genes has provided new opportunities for elucidating the molecular mechanisms underlying the etiology and pathogenesis of AD.
T W, Kim, R E, Tanzi
openaire   +2 more sources

Presenilins

2007
Abstract Alzheimer‘s disease (AD) is the leading cause of dementia in the elderly. While the vast majority of AD occurs as an age-associated disorder, autosomal dominant inheritance of mutant genes APP, PSENl, or PSEN2, which encode the amyloid precursor protein (APP), presenilin 1 (PSl), or presenilin 2 (PS2), respectively, cause ...
Kulandaivelu S Vetrivel, Gopal Thinakaran   +1 more
openaire   +1 more source

Presenilin-interacting proteins

Expert Reviews in Molecular Medicine, 2002
Familial Alzheimer's disease (FAD) accounts for 5–10% of deaths from Alzheimer's disease (AD), and approximately 50% of these cases have been definitely linked to missense mutations in three genes, encoding the amyloid precursor protein (APP), presenilin 1 (PS1) and presenilin 2 (PS2). Of these, the vast majority of FAD-linked mutations are within PS1.
Qi, Chen, David, Schubert
openaire   +2 more sources

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 ...
openaire   +2 more sources