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
Suppressor Mutations for Presenilin 1 Familial Alzheimer Disease Mutants Modulate γ-Secretase Activities.
Futai E et al.
The Journal of Biological Chemistry, 2016
Decrease in catalytic capacity of γ-secretase can facilitate pathogenesis in sporadic and Familial Alzheimer's disease.
Svedružić ŽM et al.
Molecular and Cellular Neurosciences, 2015
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
The mechanism of γ-Secretase dysfunction in familial Alzheimer disease.
Chávez-Gutiérrez L et al.
The Embo Journal, 2012
Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's disease.
Weggen S et al.
Alzheimer's Research & Therapy, 2012
Insensitivity to Abeta42-lowering nonsteroidal anti-inflammatory drugs and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations.
Czirr E et al.
The Journal of Biological Chemistry, 2007
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
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