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Article

Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins.

Glycoconjugate journal - 1 Nov 2008

Akasaka-Manya Keiko, Manya Hiroshi, Sakurai Yoko, Wojczyk Boguslaw S, Spitalnik Steven L, Endo Tamao

Abstract excerpt

Alteration of glycoprotein glycans often changes various properties of the glycoprotein. To understand the significance of N-glycosylation in the pathogenesis of early-onset familial Alzheimer's disease (AD) and in beta-amyloid (Abeta) production, we examined whether the mutations in the amyloid precursor protein (APP) gene found in familial AD affect the N-glycans on APP. We purified the secreted forms of...

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Share to Alzheimer Disease
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 18521746
DOI: 10.1007/s10719-008-9140-x

Genes

APP

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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