{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jean L"],"funding":["Synaptica Ltd."],"pagination":["6253-6272"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6484111"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["294(16)"],"pubmed_abstract":["Many neurodegenerative diseases are characterized by amyloid deposition. In Alzheimer's disease (AD), β-amyloid (Aβ) peptides accumulate extracellularly in senile plaques. The AD amyloid cascade hypothesis proposes that Aβ production or reduced clearance leads to toxicity. In contrast, the cholinergic hypothesis argues for a specific pathology of brain cholinergic pathways. However, neither hypothesis in isolation explains the pattern of AD pathogenesis. Evidence suggests that a connection exists between these two scenarios: the synaptic form of human acetylcholinesterase (hAChE-S) associates with plaques in AD brains; among hAChE variants, only hAChE-S enhances Aβ fibrillization <i>in vitro</i> and Aβ deposition and toxicity <i>in vivo</i> Only hAChE-S contains an amphiphilic C-terminal d"],"journal":["The Journal of biological chemistry"],"pubmed_title":["<i>In vivo</i> localization of human acetylcholinesterase-derived species in a β-sheet conformation at the core of senile plaques in Alzheimer's disease."],"pmcid":["PMC6484111"],"funding_grant_id":["AChE peptide"],"pubmed_authors":["Jean L","Brimijoin S","Vaux DJ"],"additional_accession":[]},"is_claimable":false,"name":"<i>In vivo</i> localization of human acetylcholinesterase-derived species in a β-sheet conformation at the core of senile plaques in Alzheimer's disease.","description":"Many neurodegenerative diseases are characterized by amyloid deposition. In Alzheimer's disease (AD), β-amyloid (Aβ) peptides accumulate extracellularly in senile plaques. The AD amyloid cascade hypothesis proposes that Aβ production or reduced clearance leads to toxicity. In contrast, the cholinergic hypothesis argues for a specific pathology of brain cholinergic pathways. However, neither hypothesis in isolation explains the pattern of AD pathogenesis. Evidence suggests that a connection exists between these two scenarios: the synaptic form of human acetylcholinesterase (hAChE-S) associates with plaques in AD brains; among hAChE variants, only hAChE-S enhances Aβ fibrillization <i>in vitro</i> and Aβ deposition and toxicity <i>in vivo</i> Only hAChE-S contains an amphiphilic C-terminal d","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Apr","modification":"2025-05-29T20:47:44.393Z","creation":"2025-05-29T20:47:44.393Z"},"accession":"S-EPMC6484111","cross_references":{"pubmed":["30787102"],"doi":["10.1074/jbc.ra118.006230","10.1074/jbc.RA118.006230"]}}