Associated Papers
Identification of Structural Calcium Binding Sites in Membrane-Bound Presenilin 1 and 2.
Mehra R et al.
The Journal of Physical Chemistry. B, 2020
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
Mutagenesis mapping of the presenilin 1 calcium leak conductance pore.
Nelson O et al.
The Journal of Biological Chemistry, 2011
Attenuated Abeta42 responses to low potency gamma-secretase modulators can be overcome for many pathogenic presenilin mutants by second-generation compounds.
Kretner B et al.
The Journal of Biological Chemistry, 2011
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
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
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