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Article

The two-hydrophobic domain tertiary structure of reticulon proteins is critical for modulation of beta-secretase BACE1.

Journal of neuroscience research - 1 Oct 2009

Kume Hideaki, Murayama Kiyoko S, Araki Wataru

Abstract excerpt

beta-Site amyloid precursor protein (APP) cleaving enzyme 1 (BACE1) is a membrane-bound protease that is essential for the production of beta-amyloid protein (Abeta). Given the crucial role of Abeta accumulation in Alzheimer's disease (AD), inhibition of BACE1 activity may represent a feasible therapeutic strategy in the treatment of AD. Recently, we and others identified reticulon 3 (RTN3) and reticulon 4-B/C...

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Source

Identifiers

PMID: 19405102
DOI: 10.1002/jnr.22112

Genes

BACE1
RTN3
RTN4
APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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The two-hydrophobic domain tertiary structure of reticulon proteins is critical for modulation of beta-secretase BACE1.PMID 19405102Read ↗

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