Varaico: Literature-Extracted Genetic Variants

Gene:PSEN1
Variant:p.D385N
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PSEN1

NM_000021.4:p.D385N

Associated Papers

Molecular mechanism of substrate recognition and cleavage by human γ-secretase.

Guo X et al.

Science (new York, N.y.), 2024

Pathogenic Aβ production by heterozygous PSEN1 mutations is intrinsic to the mutant protein and not mediated by conformational hindrance of wild-type PSEN1.

Kurth V et al.

The Journal of Biological Chemistry, 2023

Using human induced pluripotent stem cells (hiPSCs) to investigate the mechanisms by which Apolipoprotein E (APOE) contributes to Alzheimer's disease (AD) risk.

Raman S et al.

Neurobiology of Disease, 2020

Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases.

Fleck D et al.

The Journal of Biological Chemistry, 2016

Identification of tetrahydrocarbazoles as novel multifactorial drug candidates for treatment of Alzheimer's disease.

Honarnejad K et al.

Translational Psychiatry, 2014

Podoplanin is a substrate of presenilin-1/γ-secretase.

Yurrita MM et al.

The International Journal of Biochemistry & Cell Biology, 2014

Involvement of presenilin holoprotein upregulation in calcium dyshomeostasis of Alzheimer's disease.

Honarnejad K et al.

Journal of Cellular and Molecular Medicine, 2013

Generation of amyloid-β is reduced by the interaction of calreticulin with amyloid precursor protein, presenilin and nicastrin.

Stemmer N et al.

Plos One, 2013

Presenilin-1 L166P mutant human pluripotent stem cell-derived neurons exhibit partial loss of γ-secretase activity in endogenous amyloid-β generation.

Koch P et al.

The American Journal of Pathology, 2012

Rapid and direct transport of cell surface APP to the lysosome defines a novel selective pathway.

Lorenzen A et al.

Molecular Brain, 2010

Nuclear translocation and signalling of L1-CAM in human carcinoma cells requires ADAM10 and presenilin/gamma-secretase activity.

Riedle S et al.

The Biochemical Journal, 2009

Presenilin-mediated signal transduction.

Cowburn RF et al.

Physiology & Behavior, 2007

Effect of valine on the efficiency and precision at S4 cleavage of the Notch-1 transmembrane domain.

Tanii H et al.

Journal of Neuroscience Research, 2006

SorLA signaling by regulated intramembrane proteolysis.

Böhm C et al.

The Journal of Biological Chemistry, 2006

Gamma-secretase activity of presenilin 1 regulates acetylcholine muscarinic receptor-mediated signal transduction.

Popescu BO et al.

The Journal of Biological Chemistry, 2004

Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation.

Fluhrer R et al.

The Journal of Biological Chemistry, 2003

Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide.

Lammich S et al.

The Journal of Biological Chemistry, 2002

Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.

Kaether C et al.

The Journal of Cell Biology, 2002

Endoproteolysis of the ER stress transducer ATF6 in the presence of functionally inactive presenilins.

Steiner H et al.

Neurobiology of Disease, 2001

Presenilin-1 differentially facilitates endoproteolysis of the beta-amyloid precursor protein and Notch.

Capell A et al.

Nature Cell Biology, 2000

The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on abeta42 amyloid peptide formation.

Jacobsen H et al.

The Journal of Biological Chemistry, 1999

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.

Steiner H et al.

Biochemistry, 1999

Zebrafish (Danio rerio) presenilin promotes aberrant amyloid beta-peptide production and requires a critical aspartate residue for its function in amyloidogenesis.

Leimer U et al.

Biochemistry, 1999

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."