Ultrastructural studies in APP/PS1 mice expressing human ApoE isoforms: implications for Alzheimer's disease.

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Article

Ultrastructural studies in APP/PS1 mice expressing human ApoE isoforms: implications for Alzheimer's disease.

International journal of clinical and experimental pathology - 1 Jan 2012

Dikranian Krikor, Kim Jungsu, Stewart Floy R, Levy Marilyn A, Holtzman David M

Abstract excerpt

Alzheimer's disease is characterized in part by extracellular aggregation of the amyloid-β peptide in the form of diffuse and fibrillar plaques in the brain. Electron microscopy (EM) has made an important contribution in understanding of the structure of amyloid plaques in humans. Classical EM studies have revealed the architecture of the fibrillar core, characterized the progression of neuritic changes, and have...

Topics

Alzheimer Disease
Amyloid beta-Protein Precursor
Amyloidosis
Animals
Apolipoproteins E
Disease Models, Animal
Female
Humans
Male
Mice
Mice, Inbred C57BL

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice, Transgenic

Microscopy, Electron, Transmission

Mutation

Neurons

Plaque, Amyloid

Presenilin-1

Protein Isoforms

Source

Open in PubMed Open full text

Identifiers

PMID: 22949930
PMCID: PMC3430100

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-22949930-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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