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Article

The Effects of N-terminal Mutations on β-amyloid Peptide Aggregation and Toxicity.

Neuroscience - 21 May 2018

Foroutanpay B V, Kumar J, Kang S G, Danaei N, Westaway D, Sim V L, Kar S

Abstract excerpt

Human amyloid β1-42 (hAβ1-42) peptides are known to self-aggregate into oligomers that contribute to the degeneration of neurons and development of Alzheimer's disease (AD) pathology. Unlike humans, rodents do not develop AD, possibly due to differences in three amino acids (R5G, Y10F and H13R) within the hydrophilic N-terminal domain of Aβ1-42. This is partly supported by evidence that hAβ1-42 is more prone to...

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Share to Amyloid beta-Peptides
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 29572166
DOI: 10.1016/j.neuroscience.2018.03.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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