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The APP intracellular domain is required for normal synaptic morphology, synaptic plasticity, and hippocampus-dependent behavior

The amyloid precursor protein family (APP/APLPs) has essential roles for neuromuscular synapse development and for the formation and plasticity of synapses within the CNS. Despite this, it has remained unclear whether APP mediates its functions primarily as a cell surface adhesion and signaling mole...

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Bibliographic Details
Main Authors: Klevanski, Maja (Author) , Herrmann, Ulrike (Author) , Weyer, Sascha W. (Author) , Fol, Romain (Author) , Cartier, Nathalie (Author) , Wolfer, David P. (Author) , Caldwell, John H. (Author) , Korte, Martin (Author) , Müller, Ulrike C. (Author)
Format: Article (Journal)
Language:English
Published: December 9, 2015
In: The journal of neuroscience
Year: 2015, Volume: 35, Issue: 49, Pages: 16018-16033
ISSN:1529-2401
DOI:10.1523/JNEUROSCI.2009-15.2015
Online Access:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1523/JNEUROSCI.2009-15.2015
Verlag, lizenzpflichtig, Volltext: https://www.jneurosci.org/content/35/49/16018
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Author Notes:Maja Klevanski, Ulrike Herrmann, Sascha W. Weyer, Romain Fol, Nathalie Cartier, David P. Wolfer, John H. Caldwell, Martin Korte, and Ulrike C. Müller
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Summary:The amyloid precursor protein family (APP/APLPs) has essential roles for neuromuscular synapse development and for the formation and plasticity of synapses within the CNS. Despite this, it has remained unclear whether APP mediates its functions primarily as a cell surface adhesion and signaling molecule or via its numerous proteolytic cleavage products. To address these questions, we followed a genetic approach and used APPΔCT15 knockin mice lacking the last 15 amino acids of APP, including the highly conserved YENPTY protein interaction motif.
Item Description:Gesehen am 08.07.2020
Physical Description:Online Resource
ISSN:1529-2401
DOI:10.1523/JNEUROSCI.2009-15.2015

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