New insights into alzheimers disease pathogenesis: the involvement of neurologins in synaptic malfunction

Sindi, Ikhlas A. and Dodd, Peter R. (2015) New insights into alzheimers disease pathogenesis: the involvement of neurologins in synaptic malfunction. Neurodegenerative Disease Management, 5 2: 137-145.

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Author Sindi, Ikhlas A.
Dodd, Peter R.
Title New insights into alzheimers disease pathogenesis: the involvement of neurologins in synaptic malfunction
Journal name Neurodegenerative Disease Management   Check publisher's open access policy
ISSN 1758-2024
1758-2032
Publication date 2015-04
Year available 2015
Sub-type Article (original research)
Open Access Status
Volume 5
Issue 2
Start page 137
End page 145
Total pages 9
Place of publication London, United Kingdom
Publisher Future Medicine
Collection year 2016
Language eng
Formatted abstract
Synaptic damage is a key hallmark of Alzheimer’s disease and the best correlate with cognitive decline ante mortem. Signature protein combinations arrayed at tightly apposed pre- and post-synaptic sites characterize different types of synapse.  Neuroligins are postsynaptic cell adhesion molecules that interact with neurexins across the synaptic cleft. These pairings recruit receptors, channels and signal transduction molecules to the synapse, and help mediate trans-synaptic transmission. Dysfunction in the neuroligin family can disrupt neuronal networks and leads to neurodegeneration and other diseases.  The extracellular domain of neuroligins is homologous with acetylcholinesterase but lacks residues required for enzymatic activity. This domain may interact pathogenically with β-amyloid. Here we summarize research over the last decade on the potential involvement of neuroligins in Alzheimer’s disease.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Tue, 02 Jun 2015, 15:01:10 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences