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Status: Bibliographieeintrag

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Verfasst von:Caldwell, John [VerfasserIn]   i
 Klevanski, Maja [VerfasserIn]   i
 Saar, Martina [VerfasserIn]   i
 Müller, Ulrike C. [VerfasserIn]   i
Titel:Roles of the amyloid precursor protein family in the peripheral nervous system
Verf.angabe:John H. Caldwell, Maja Klevanski, Martina Saar, Ulrike C. Müller
Jahr:2013
Jahr des Originals:2012
Umfang:14 S.
Fussnoten:Available online: 29 November 2012 ; Gesehen am 08.02.2021
Titel Quelle:Enthalten in: Mechanisms of development
Ort Quelle:Shannon : Elsevier, 1990
Jahr Quelle:2013
Band/Heft Quelle:130(2013), 6, Seite 433-446
ISSN Quelle:1872-6356
Abstract:Compelling evidence from in vivo model systems within the past decade shows that the APP family of proteins is important for synaptic development and function in the central and peripheral nervous systems. The synaptic role promises to be complex and multifaceted for several reasons. The three family members have overlapping and redundant functions in mammals. They have both adhesive and signaling properties and may, in principle, act as both ligands and receptors. Moreover, they bind a multitude of synapse-specific proteins, and we predict that additional interacting protein partners will be discovered. Transgenic mice with modified or abolished expression of APP and APLPs have synaptic defects that are readily apparent. Studies of the neuromuscular junction (NMJ) in these transgenic mice have revealed molecular and functional deficits in neurotransmitter release, in organization of the postsynaptic receptors, and in coordinated intercellular development. The results summarized here from invertebrate and vertebrate systems confirm that the NMJ with its accessibility, large size, and homogeneity provides a model synapse for identifying and analyzing molecular pathways of APP actions.
DOI:doi:10.1016/j.mod.2012.11.001
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1016/j.mod.2012.11.001
 Volltext: https://www.sciencedirect.com/science/article/pii/S0925477312001128
 DOI: https://doi.org/10.1016/j.mod.2012.11.001
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Alzheimer’s disease
 Amyloid precursor protein
 Neuromuscular junction
 Synaptogenesis
 Transgenic mouse
K10plus-PPN:1747750352
Verknüpfungen:→ Zeitschrift

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