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Rationale: Presynaptic NPR directly binds to the GluA1-N terminal extracellular domain and stimulates assembly of both excitatory and inhibitory postsynaptic sites. Loss of NPR suppressed surface GluA1 levels, and impaired excitatory synaptic transmission, without affecting synapse numbers. Figs.1 and 5 support that NPR is involved in formation of postsynaptic specializations. Fig.2 shows that NPR binds the GluA1-NTD. Figs.10 and 11 show that global NPR knockdown in pre- and post-synaptic neurons impairs excitatory postsynaptic scaffold assembly and the strength of excitatory transmission.. Experimental description: Mouse hippocampal neurons were prepared. 23/6/2017 Pim -All overexpression constructs are of human species: "The constructs encoding cDNAs of hNPR (HsCD00083063), hNP1 (HsCD00296108), and hNARP (HsCD00040444) were obtained from PlasmID (http://plasmid.med.harvard.edu/PLASMID/)." - Species of GluA1-NTD overexpressed protein is not mentioned.

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  • Rationale: Presynaptic NPR directly binds to the GluA1-N terminal extracellular domain and stimulates assembly of both excitatory and inhibitory postsynaptic sites. Loss of NPR suppressed surface GluA1 levels, and impaired excitatory synaptic transmission, without affecting synapse numbers. Figs.1 and 5 support that NPR is involved in formation of postsynaptic specializations. Fig.2 shows that NPR binds the GluA1-NTD. Figs.10 and 11 show that global NPR knockdown in pre- and post-synaptic neurons impairs excitatory postsynaptic scaffold assembly and the strength of excitatory transmission.. Experimental description: Mouse hippocampal neurons were prepared. 23/6/2017 Pim -All overexpression constructs are of human species: "The constructs encoding cDNAs of hNPR (HsCD00083063), hNP1 (HsCD00296108), and hNARP (HsCD00040444) were obtained from PlasmID (http://plasmid.med.harvard.edu/PLASMID/)." - Species of GluA1-NTD overexpressed protein is not mentioned.
Title
  • Nptxr_BP_849
Date
  • 2017-11-06
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