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Depositordc.contributorSpires-Jones, Tara
Funderdc.contributor.otherWellcome Trusten_UK
Data Creatordc.creatorPickett, Eleanor K
Data Creatordc.creatorKoffie, Robert M
Data Creatordc.creatorWegmann, Susanne
Data Creatordc.creatorHenstridge, Christopher M
Data Creatordc.creatorHerrmann, Abigail G
Data Creatordc.creatorColom-Cadena, Marti
Data Creatordc.creatorLleo, Alberto
Data Creatordc.creatorKay, Kevin R
Data Creatordc.creatorVaught, Melissa
Data Creatordc.creatorSoberman, Roy
Data Creatordc.creatorWalsh, Dominic M
Data Creatordc.creatorHyman, Bradley T
Data Creatordc.creatorSpires-Jones, Tara L
Citationdc.identifier.citationPickett, Eleanor K.; Koffie, Robert M.; Wegmann, Susanne; Henstridge, Christopher M.; Herrmann, Abigail G.; Colom-Cadena, Marti; Lleo, Alberto; Kay, Kevin R.; Vaught, Melissa; Soberman, Roy; Walsh, Dominic M.; Hyman, Bradley T.; Spires-Jones, Tara L. (2016). Non-fibrillar oligomeric amyloid-β within synapses: Data set from publication Pickett et al 2016 J Alz Dis, [dataset]. University of Edinburgh. School of Biomedical Sciences.
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Persistent Identifierdc.identifier.uri
Dataset Description (abstract)dc.description.abstractAlzheimer’s disease (AD) is characterized by memory loss, insidious cognitive decline, profound neurodegeneration and the extracellular accumulation of amyloid-beta (Ab) peptide in senile plaques and intracellular accumulation of tau in neurofibrillary tangles. Loss and dysfunction of synapses are believed to underlie the devastating cognitive decline in AD. A large amount of evidence suggests that oligomeric forms of Ab associated with senile plaques are toxic to synapses, but the precise sub-synaptic localization of Ab and which forms are synaptotoxic remain unknown. Here, we characterize the sub-synaptic localization of Ab oligomers using three high-resolution imaging techniques, stochastic optical reconstruction microscopy, immunogold electron microscopy and Förster resonance energy transfer in a plaque-bearing mouse model of Alzheimer’s disease. With all three techniques, we observe oligomeric Ab inside synaptic terminals. Further, we tested a panel of Ab antibodies using the relatively high-throughput array tomography technique to determine which forms are present in synapses. Our results show that different oligomeric Ab species are present in synapses and highlight the potential of array tomography for rapid testing of aggregation state specific Ab antibodies in brain tissue.en_UK
Publisherdc.publisherUniversity of Edinburgh. School of Biomedical Sciencesen_UK
Relation (Is Referenced By)dc.relation.isreferencedby
Relation (Is Referenced By)dc.relation.isreferencedbyPickett, E, Koffie, R, Wegmann, S, Henstridge, C, Herrmann, A, Colom-Cadena, M, Lleo, A, Kay, K, Vaught, M, Soberman, R, Walsh, D, Hyman, B & Spires-Jones, T 2016, 'Non-fibrillar oligomeric amyloid-β within synapses' Journal of Alzheimer's Disease. DOI: 10.3233/JAD-160007en_UK
Subjectdc.subjectarray tomographyen_UK
Subject Classificationdc.subject.classificationSubjects allied to Medicine::Neuroscienceen_UK
Titledc.titleNon-fibrillar oligomeric amyloid-β within synapses: Data set from publication Pickett et al 2016 J Alz Disen_UK

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