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Developmental and regional expression in the rat brain and functional properties of four NMDA receptors
Recombinant binary NR1-NR2 channels show comparable Ca2+ permeabilities, but marked differences in voltage-dependent Mg2+ block and in offset decay time constants, which provide a basis for NMDA channel heterogeneity in the brain. Expand
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95, which may affect the plasticity of excitatory synapses. Expand
Heteromeric NMDA Receptors: Molecular and Functional Distinction of Subtypes
Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% ientical in sequence, and these are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor sub Units. Expand
Relative abundance of subunit mRNAs determines gating and Ca2+ permeability of AMPA receptors in principal neurons and interneurons in rat CNS
Analysis of AMPARs in principal neurons and interneurons of hippocampus and neocortex and in auditory relay neurons and Bergmann glial cells indicates that the GluR-B subunit in its flip version determines formation of receptors with relatively slow gating, whereas the GLUR-D subunit promotes assembly of more rapidly gated receptors. Expand
Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
The complete 1,210-amino acid sequence of the human epidermal growth factor (EGF) receptor precursor, deduced from cDNA clones derived from placental and A431 carcinoma cells, reveals closeExpand
A molecular determinant for submillisecond desensitization in glutamate receptors.
These findings suggest that rapid desensitization of AMPA receptors can be regulated by the expression and alternative splicing of GluR-D gene transcripts. Expand
Importance of AMPA receptors for hippocampal synaptic plasticity but not for spatial learning.
The results suggest that CA1 hippocampal LTP is controlled by the number or subunit composition of AMPA receptors and show a dichotomy between LTP in CA1 and acquisition of spatial memory. Expand
Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2
It is concluded that this transcript is the physiologically most important substrate of ADAR2, as it specifies an ion channel determinant, the Q/R site, in AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionate) receptor GluR-B pre-messenger RNA. Expand
Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.
These results identify a switch in the molecular and functional properties of glutamate receptors operated by alternative splicing. Expand
Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit
Mutational analysis revealed that both the positive charge and the size of the amino acid side chain located at the Q/R site control the divalent permeability of homomeric channels. Expand