Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability a...
Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability and Mg2+block
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Publisher
England: BioMed Central
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Language
English
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Publisher
England: BioMed Central
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Contents
Members of the complex N-methyl-D-aspartate receptor (NMDAR) subfamily of ionotropic glutamate receptors (iGluRs) conventionally assemble from NR1 and NR2 subunits, the composition of which determines receptor properties. Hallmark features of conventional NMDARs include the requirement for a coagonist, voltage-dependent block by Mg2+, and high perm...
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Full title
Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability and Mg2+block
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TN_cdi_doaj_primary_oai_doaj_org_article_edfe017d03ba4529ac8e931d0ce0aed1
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_edfe017d03ba4529ac8e931d0ce0aed1
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ISSN
1471-2202
E-ISSN
1471-2202
DOI
10.1186/1471-2202-11-133
