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Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex

NMDA receptor (NMDAR) composition and synaptic retention represent pivotal features in the physiology and pathology of excitatory synapses. Here, we identify Rabphilin 3A (Rph3A) as a new GluN2A subunit-binding partner. Rph3A is known as a synaptic vesicle-associated protein involved in the regulati...

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Bibliografische gegevens
Gepubliceerd in:Nat Commun
Hoofdauteurs: Stanic, Jennifer, Carta, Mario, Eberini, Ivano, Pelucchi, Silvia, Marcello, Elena, Genazzani, Armando A., Racca, Claudia, Mulle, Christophe, Di Luca, Monica, Gardoni, Fabrizio
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Nature Publishing Group 2015
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC4703873/
https://ncbi.nlm.nih.gov/pubmed/26679993
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/ncomms10181
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