Delta glutamate receptors are functional glycine- and ᴅ-serine–gated cation channels in situ | Zendy

Elisa Carrillo | Zendy; Cuauhtémoc U. Gonzalez | Zendy; Vladimír Berka | Zendy; Vasanthi Jayaraman | Zendy

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Delta glutamate receptors are functional glycine- and ᴅ-serine–gated cation channels in situ

Author(s) -

Elisa Carrillo,

Cuauhtémoc U. Gonzalez,

Vladimír Berka,

Vasanthi Jayaraman

Publication year - 2021

Publication title -

science advances

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.928

H-Index - 146

ISSN - 2375-2548

DOI - 10.1126/sciadv.abk2200

Subject(s) - kainate receptor , neurexin , ionotropic effect , glutamate receptor , ion channel , neurotransmitter receptor , metabotropic glutamate receptor 1 , receptor , class c gpcr , ionotropic glutamate receptor , metabotropic glutamate receptor 6 , glycine receptor , biophysics , biochemistry , excitatory postsynaptic potential , extracellular , biology , metabotropic receptor , metabotropic glutamate receptor , ampa receptor , glycine , amino acid , postsynaptic potential

The synaptic proteins cerebellin-1 and neurexin-1β permit ion channel activity in delta subtype of ionotropic glutamate receptors.

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