Abstract 1701 The human RAP1 protein increases gamma-secretase activity in an oxidative environment

Background: Alzheimer's disease (AD) is an age-related disorder that results in progressive cognitive impairment and memory loss. Deposition of amyloid β (Aβ) peptides in senile plaques is a hallmark of AD. γ-secretase produces Aβ peptides mostly as the soluble Aβ40 with fewer insoluble Aβ42 peptides. Rare, early-onset AD (EOAD) occurs in individuals under 60 years of age. Most EOAD cases are due to unknown genetic causes, but a subset is due to mutations in the genes encoding the amyloid precursor protein (APP) that is processed into Aβ peptides or the presenilins (PS1 and PS2) that process APP.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109696
Primary Topic
RNA regulation and disease
Type
article
Field-Weighted Citation Impact
0.00
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article

Abstract 1701 The human RAP1 protein increases gamma-secretase activity in an oxidative environment

Mark E. Swanson, Kelsey Lewis, Alexis Whetzel, Nancy Bae
Journal of Biological Chemistry
RNA regulation and disease
article

Abstract 1701 The human RAP1 protein increases gamma-secretase activity in an oxidative environment

Mark E. Swanson, Kelsey Lewis, Alexis Whetzel, Nancy Bae
article en

Abstract

Background: Alzheimer's disease (AD) is an age-related disorder that results in progressive cognitive impairment and memory loss. Deposition of amyloid β (Aβ) peptides in senile plaques is a hallmark of AD. γ-secretase produces Aβ peptides mostly as the soluble Aβ40 with fewer insoluble Aβ42 peptides. Rare, early-onset AD (EOAD) occurs in individuals under 60 years of age. Most EOAD cases are due to unknown genetic causes, but a subset is due to mutations in the genes encoding the amyloid precursor protein (APP) that is processed into Aβ peptides or the presenilins (PS1 and PS2) that process APP.

Journal of Biological ChemistryVol. 301(5)
Midwestern University (US)
Openalex Percentile: Top 88%
RNA regulation and disease
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