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Article

Amyloid beta inhibits ectodomain shedding of N-cadherin via down-regulation of cell-surface NMDA receptor.

Neuroscience - 2 Mar 2007

Uemura K, Kuzuya A, Aoyagi N, Ando K, Shimozono Y, Ninomiya H, Shimohama S, Kinoshita A

Abstract excerpt

Dysfunction in the synapse is recognized as an early and the primary pathological process in Alzheimer's disease (AD). N-cadherin, an essential adhesion molecule for excitatory synaptic contact, forms a complex with presenilin 1 (PS1) and beta-catenin in the synaptic membrane. N-cadherin is sequentially cleaved by ADAM10 and PS1/gamma-secretase, producing a cytoplasmic fragment, N-cadherin C-terminal fragment...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17257767
DOI: 10.1016/j.neuroscience.2006.12.022

Genes

ADAM10

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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Amyloid beta inhibits ectodomain shedding of N-cadherin via down-regulation of cell-surface NMDA receptor.PMID 17257767Read ↗

Characterization of sequential N-cadherin cleavage by ADAM10 and PS1.Semantic proximity Read ↗

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Familial Alzheimer's disease presenilin 1 mutation M146V increases gamma secretase cutting of p75NTR in vitro.Semantic proximity Read ↗

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