The amyloid precursor protein shows a pH-dependent conformational switch in its E1 domain.

doi:10.1016/j.jmb.2014.12.005

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Article

The amyloid precursor protein shows a pH-dependent conformational switch in its E1 domain.

Journal of molecular biology - 30 Jan 2015

Hoefgen Sandra, Dahms Sven O, Oertwig Kathrin, Than Manuel E

Abstract excerpt

The amyloid precursor protein (APP) and its proteolytic cleavage product Aβ are widely believed to be central to the etiology of Alzheimer's disease (AD). APP and its family members are also essential for proper neuronal development and homeostasis. APP is located at the cell surface and within intracellular compartments, cellular regions that exhibit different pH values. The AD-associated amyloidogenic...

Topics

Alzheimer Disease
Amyloid beta-Protein Precursor
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli
Humans
Hydrogen-Ion Concentration
Molecular Structure
Molecular Weight
Mutation
Protein Conformation
Protein Interaction Domains and Motifs
Proteolysis

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Identifiers

PMID: 25528641
DOI: 10.1016/j.jmb.2014.12.005

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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