Article

Dissecting Conformational Changes in APP’s Transmembrane Domain Linked to ε-Efficiency in Familial Alzheimer’s Disease

2018-02-21

Abstract excerpt

The mechanism by which familial Alzheimer’s disease (FAD) mutations within the transmembrane domain (TMD) of the Amyloid Precursor Protein (APP) affect å-endoproteolysis is only poorly understood. Thereby, mutations in the cleavage domain reduce å-efficiency of ã-secretase cleavage and some even shift entry into production lines. Since cleavage occurs within the TMD, a relationship between processing and TMD struc...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: a650a7db-ffff-5434-a820-3ecdbc0b8ccc
DOI: 10.1101/269084

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Dissecting Conformational Changes in APP’s Transmembrane Domain Linked to ε-Efficiency in Familial Alzheimer’s DiseaseDOI 10.1101/269084Read

Dissecting conformational changes in APP's transmembrane domain linked to ε-efficiency in familial Alzheimer's disease.Semantic proximity Read

Increased H-Bond Stability Relates to Altered ε-Cleavage Efficiency and Aβ Levels in the I45T Familial Alzheimer’s Disease Mutant of APPSemantic proximity Read

Altered Hinge Conformations in APP Transmembrane Helix Mutants May Affect Enzyme-Substrate Interactions of γ-Secretase.Semantic proximity Read

Familial Alzheimer's mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site.Semantic proximity Read

Alzheimer's disease mutations in APP but not γ-secretase modulators affect epsilon-cleavage-dependent AICD production.Semantic proximity Read

Effects of Presenilin-1 Familial Alzheimer’s Disease Mutations on γ-Secretase Activation for Cleavage of Amyloid Precursor ProteinSemantic proximity Read

Specific Mutations near the Amyloid Precursor Protein Cleavage Site Increase γ-Secretase Sensitivity and Modulate Amyloid-β Production.Semantic proximity Read

Conformational Models of APP Processing by Gamma Secretase Based on Analysis of Pathogenic Mutations.Semantic proximity Read

Mechanisms of γ-Secretase Activation and Substrate ProcessingSemantic proximity Read

A computer-simulated mechanism of familial Alzheimer's disease: Mutations enhance thermal dynamics and favor looser substrate-binding to γ-secretase.Semantic proximity Read

Effects of presenilin-1 familial Alzheimer's disease mutations on γ-secretase activation for cleavage of amyloid precursor protein.Semantic proximity Read

Mechanism of Tripeptide Trimming by γ-SecretaseSemantic proximity Read