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Cloned glutamate receptors.
The application of molecular cloning technology to the study of the glutamate receptor system has led to an explosion of knowledge about the structure, expression, and function of this most important
Ca2+ permeability of KA-AMPA--gated glutamate receptor channels depends on subunit composition
TLDR
In neurons expressing certain KA-AMPA receptor subunits, glutamate may trigger calcium-dependent intracellular events by activating non-NMDA receptors.
Molecular cloning and functional expression of glutamate receptor subunit genes.
Three closely related genes, GluR1, GluR2, and GluR3, encode receptor subunits for the excitatory neurotransmitter glutamate. The proteins encoded by the individual genes form homomeric ion channels
P2X4: an ATP-activated ionotropic receptor cloned from rat brain.
TLDR
Cl cloning and characterization of complementary DNA from rat brain are reported, encoding an additional member (P2X4) of the emerging multigenic family of ligand-gated ATP channels, the P2X receptors, which suggests that the P1X4 receptor might mediate not only ATP-dependent synaptic transmission in the central nervous system but also a wide repertoire of biological responses in diverse tissues.
Cloning by functional expression of a member of the glutamate receptor family
TLDR
A complementary DNA clone is isolated by screening a rat brain cDNA library for expression of kainate-gated ion channels in Xenopus oocytes which on expression in oocytes forms a functional ion channel possessing the electrophysiological and pharmacological properties of the kainates subtype of the glutamate receptor family in the mammalian central nervous system.
Electrophysiological Properties of AMPA Receptors Are Differentially Modulated Depending on the Associated Member of the TARP Family
TLDR
It is demonstrated that the splice variant of the AMPA receptor plays a key role in determining the modulation of electrophysiological properties by associated TARPs, and evidence that individual TARP–AMPA receptor interactions control the degree of desensitization of AMPA receptors is presented.
A single amino acid determines the subunit-specific spider toxin block of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate receptor channels.
TLDR
Investigating the molecular basis of the JSTX action on the recombinant AMPA/KA receptors GluR1-GluR4 and GLUR6 expressed in Xenopus oocytes found that submicromolar concentrations of J STX exert a subunit-specific block, suggesting that JSTx binds close to the central pore region of the channel.
N-Glycosylation is not a prerequisite for glutamate receptor function but Is essential for lectin modulation.
TLDR
It is determined that in neither case is N-glycosylation required for ion channel function, although for NMDA receptors, functional expression in the absence of N- Glycosylated subunits is very low.
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