Associated Papers
Two novel presenilin-1 mutations (I249L and P433S) in early onset Chinese Alzheimer's pedigrees and their functional characterization.
Shen L et al.
Biochemical and Biophysical Research Communications, 2019
Mutational re-modeling of di-aspartyl intramembrane proteases: uncoupling physiologically-relevant activities from those associated with Alzheimer's disease.
Grigorenko AP et al.
Oncotarget, 2017
Exploratory data from complete genomes of familial alzheimer disease age-at-onset outliers.
Lalli MA et al.
Human Mutation, 2012
Presenilins as endoplasmic reticulum calcium leak channels and Alzheimer's disease pathogenesis.
Supnet C et al.
Science China. Life Sciences, 2011
Mutagenesis mapping of the presenilin 1 calcium leak conductance pore.
Nelson O et al.
The Journal of Biological Chemistry, 2011
A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activity.
Heilig EA et al.
The Journal of Biological Chemistry, 2010
Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of gamma-secretase.
Tolia A et al.
The Journal of Biological Chemistry, 2008
Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.
Fraering PC
Current Genomics, 2007
C-terminal fragment of presenilin is the molecular target of a dipeptidic gamma-secretase-specific inhibitor DAPT (N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester).
Morohashi Y et al.
The Journal of Biological Chemistry, 2006
C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation.
Wang J et al.
Journal of Neurochemistry, 2006
Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid beta-peptides.
Nakaya Y et al.
The Journal of Biological Chemistry, 2005
Presenilin endoproteolysis is an intramolecular cleavage.
Brunkan AL et al.
Molecular and Cellular Neurosciences, 2005
Conserved "PAL" sequence in presenilins is essential for gamma-secretase activity, but not required for formation or stabilization of gamma-secretase complexes.
Wang J et al.
Neurobiology of Disease, 2004
The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and gamma-secretase activities of presenilins.
Tomita T et al.
The Journal of Biological Chemistry, 2001
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