Associated Papers
Aβ profiles generated by Alzheimer's disease causing PSEN1 variants determine the pathogenicity of the mutation and predict age at disease onset.
Petit D et al.
Molecular Psychiatry, 2022
Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.
Fernandez MA et al.
The Journal of Biological Chemistry, 2014
Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.
Wanngren J et al.
Febs Open Bio, 2014
Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's disease.
Weggen S et al.
Alzheimer's Research & Therapy, 2012
Familial Alzheimer's disease mutations in presenilin 1 do not alter levels of the secreted amyloid-beta protein precursor generated by beta-secretase cleavage.
Zhang C et al.
Current Alzheimer Research, 2010
Familial Alzheimer disease-linked mutations specifically disrupt Ca2+ leak function of presenilin 1.
Nelson O et al.
The Journal of Clinical Investigation, 2007
Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms.
Bentahir M et al.
Journal of Neurochemistry, 2006
Amyloid precursor protein gene mutations responsible for early-onset autosomal dominant Alzheimer's disease.
Kowalska A
Folia Neuropathologica, 2003
The role of beta-catenin stability in mutant PS1-associated apoptosis.
Weihl CC et al.
Neuroreport, 1999
Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing.
Baumeister R et al.
Genes and Function, 1997
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