Molecular cloning and characterization of the rat NMDA receptor
@article{Moriyoshi1991MolecularCA, title={Molecular cloning and characterization of the rat NMDA receptor}, author={Koki Moriyoshi and Masayuki Masu and Takahiro M. Ishii and Ryuichi Shigemoto and Noboru Mizuno and Shigetada Nakanishi}, journal={Nature}, year={1991}, volume={354}, pages={31-37} }
A complementary DNA encoding the rat NMDA receptor has been cloned and characterized. The single protein encoded by the cDNA forms a receptor-channel complex that has electrophysiological and pharmacological properties characteristic of the NMDA receptor. This protein has a significant sequence similarity to the AMPA/kainate receptors and contains four putative transmembrane segments following a large extracellular domain. The NMDA receptor messenger RNA is expressed in neuronal cells…
1,755 Citations
Molecular cloning of a cDNA encoding a novel member of the mouse glutamate receptor channel family.
- BiologyBiochemical and biophysical research communications
- 1992
Cloning and expression of a glycine transporter reveal colocalization with NMDA receptors
- BiologyNeuron
- 1992
Molecular cloning and chromosomal localization of the key subunit of the human N-methyl-D-aspartate receptor.
- BiologyThe Journal of biological chemistry
- 1993
Functional characterization of a heteromeric NMDA receptor channel expressed from cloned cDNAs
- BiologyNature
- 1992
The identification and primary structure of a novel mouse NMDA receptor channel subunit, designated as ɛl, is reported, which shows 11-18% amino-acid sequence identity with rodent GluR channel subunits that have been characterized so far and has structural features common to neurotransmitter-gated ion channels.
Cloning of the long intracellular loop of the AMPA-selective glutamate receptor for phosphorylation studies.
- Biology, ChemistryJournal of receptor research
- 1993
Antibodies are raised against several consensus phosphorylation sites for Ca(2+)-calmodulin-dependent protein kinase type II and protein kinases C to study the possible function of these sites in the glutamate receptor.
Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1993
The cDNA clone hNR1 codes for a human brain NMDA receptor subunit cognate to the rodent and murine brain NR1 subunits, which exhibits the high Ca2+ permeability characteristic of neuronal NMDA receptors.
Characterization of a presynaptic glutamate receptor.
- BiologyScience
- 1993
In vivo GR33 may be a presynaptic glutamate receptor and form glutamate-activated ion channels that are pharmacologically similar to those of N-methyl-D-aspartate receptors but with different electrophysiological properties.
Molecular diversity of the NMDA receptor channel
- BiologyNature
- 1992
Findings suggest that the molecular diversity of the ɛ subunit family underlies the functional heterogeneity of the NMDA receptor channel.
Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing.
- BiologyBiochemical and biophysical research communications
- 1992
Cloning of the cDNA for the human NMDA receptor NR2C subunit and its expression in the central nervous system and periphery.
- BiologyBrain research. Molecular brain research
- 1996
References
SHOWING 1-10 OF 42 REFERENCES
Cloning by functional expression of a member of the glutamate receptor family
- BiologyNature
- 1989
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.
Sequence and expression of a metabotropic glutamate receptor
- BiologyNature
- 1991
The complementary DNA of a metabotropic glutamate receptor coupled to inositol phosphate/Ca2+ signal transduction has been cloned and characterized and abundant expression of this messenger RNA is observed in neuronal cells in hippocampal dentate gyrus and CA2−3 and in Cerebellar Purkinje cells, suggesting the importance of this receptor in specific hippocampal and cerebellar functions.
A family of AMPA-selective glutamate receptors.
- BiologyScience
- 1990
Four cloned cDNAs encoding 900-amino acid putative glutamate receptors with approximately 70 percent sequence identity were isolated from a rat brain cDNA library. In situ hybridization revealed…
Cloning, expression, and gene structure of a G protein-coupled glutamate receptor from rat brain.
- BiologyScience
- 1991
A complementary DNA encoding a G protein-coupled glutamate receptor from rat brain, GluGR, was cloned by functional expression in Xenopus oocytes, suggesting that it may be a member of a new subfamily.
Sequence and expression of a frog brain complementary DNA encoding a kainate-binding protein
- BiologyNature
- 1989
These results provide the first molecular characterization of an EAA-binding site and raise the possibility that the KBP cDNA encodes a ligand-binding subunit of a kainate receptor–ionophore complex.
Rat brain N-methyl-D-aspartate receptors expressed in Xenopus oocytes.
- BiologyScience
- 1987
Xenopus oocytes injected with messenger RNA isolated from primary cultures of rat brain have been used to study NMDA receptors and should facilitate the quantitative study of the regulation of NMDA receptor activation and serve as a tool for purification of the encoding messenger RNA.
Molecular structure of the chick cerebellar kainate-binding subunit of a putative glutamate receptor
- BiologyNature
- 1989
An oligomeric protein is isolated that displays a pharmacological profile similar to that of a kainate receptor, and the predicted structure of the mature protein has four putative transmembrane domains with a topology analogous to that found in the superfamily of ligand-gated ion channels, raising the possibility, that kainates binding protein may form part of an ion channel and may be a subunit of akainate subtype of glutamate receptor.
Cloning of a putative high-affinity kainate receptor expressed predominantly in hippocampal CA3 cells
- BiologyNature
- 1991
A new member of the rat excitatory amino-acid receptor gene family, KA-1, that has a 30% sequence similarity with the previously characterized α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptor subunits GluR-A to -D3–5 is described.
Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA
- BiologyNature
- 1991
The cloning and expression of a functional rat glutamate receptor subunit cDNA, GluR6, which has a very different pharmacology from that of the GluLl–GluR4 class and exhibits an outwardly rectifying current–voltage relationship.
Molecular cloning and functional expression of glutamate receptor subunit genes.
- BiologyScience
- 1990
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…