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http://purl.uniprot.org/citations/32413698http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32413698http://www.w3.org/2000/01/rdf-schema#comment"Excitatory amino acid transporter-2 (EAAT-2) protein localized in the membrane of glial cells are responsible for the clearance of glutamate in synapse and it plays a key role among the five glutamate transporters (EAATs) in regulating synaptic transmission and preventing excitotoxicity in neurons. EAAT-2 dysfunction has been associated with the neuropathology of Alzheimer's disease (AD). Impairment of EAAT-2 transporter function results excess accumulation of glutamate in synaptic cleft that acts on post-synaptic glutaminergic receptors excessively resulting in influx of Na+ and Ca2+ ions into the neurons. This triggers excitotoxicity in post-synaptic neurons by activating apoptotic or necrotic pathways causing neurodegeneration in AD. The compounds that increase the EAAT-2 activity may have therapeutic potential for neuroprotection in AD. The positive allosteric site activation of EAAT-2 represents a promising entry point for the identification of novel pharmacological compounds for the management of neurodegenerative conditions involving glutamate-mediated excitotoxicity. We hypothesize, therefore, that the positive allosteric activators may enhance glutamate clearance from the synaptic cleft by promoting orthosteric binding of glutamate ligand in EAAT-2 transporter protein and attenuate the excitotoxicity in neurons and prevent the disease progression of AD."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.org/dc/terms/identifier"doi:10.1016/j.mehy.2020.109794"xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Manisha C."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Selvaraj A."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Justin A."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Clement J.P."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Jubie S."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Moola Joghee N."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/author"Moola Joghee Nanjan C."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/name"Med Hypotheses"xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/pages"109794"xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/title"Positive allosteric activation of glial EAAT-2 transporter protein: A novel strategy for Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/32413698http://purl.uniprot.org/core/volume"142"xsd:string
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http://purl.uniprot.org/citations/32413698http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32413698
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