GRIN2A

From Wikipedia, the free encyclopedia


Glutamate receptor, ionotropic, N-methyl D-aspartate 2A
PDB rendering based on 2a5s.
Available structures: 2a5s, 2a5t
Identifiers
Symbol(s) GRIN2A; NMDAR2A; NR2A
External IDs OMIM: 138253 MGI95820 HomoloGene645
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 2903 14811
Ensembl ENSG00000183454 ENSMUSG00000059003
Uniprot Q12879 P35436
Refseq NM_000833 (mRNA)
NP_000824 (protein)
XM_988553 (mRNA)
XP_993647 (protein)
Location Chr 16: 9.76 - 10.18 Mb Chr 16: 9.49 - 9.91 Mb
Pubmed search [1] [2]

Glutamate receptor, ionotropic, N-methyl D-aspartate 2A, also known as GRIN2A, is a human gene.

N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C), and NMDAR2D (GRIN2D).[1]

[edit] See also

[edit] References

[edit] Further reading

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  • Monyer H, Sprengel R, Schoepfer R, et al. (1992). "Heteromeric NMDA receptors: molecular and functional distinction of subtypes.". Science 256 (5060): 1217–21. PMID 1350383. 
  • Kornau HC, Schenker LT, Kennedy MB, Seeburg PH (1995). "Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.". Science 269 (5231): 1737–40. PMID 7569905. 
  • Magnuson DS, Knudsen BE, Geiger JD, et al. (1995). "Human immunodeficiency virus type 1 tat activates non-N-methyl-D-aspartate excitatory amino acid receptors and causes neurotoxicity.". Ann. Neurol. 37 (3): 373–80. doi:10.1002/ana.410370314. PMID 7695237. 
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  • Foldes RL, Adams SL, Fantaske RP, Kamboj RK (1994). "Human N-methyl-D-aspartate receptor modulatory subunit hNR2A: cloning and sequencing of the cDNA and primary structure of the protein.". Biochim. Biophys. Acta 1223 (1): 155–9. PMID 8061049. 
  • Sheng M, Cummings J, Roldan LA, et al. (1994). "Changing subunit composition of heteromeric NMDA receptors during development of rat cortex.". Nature 368 (6467): 144–7. doi:10.1038/368144a0. PMID 8139656. 
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  • Takano H, Onodera O, Tanaka H, et al. (1994). "Chromosomal localization of the epsilon 1, epsilon 3 and zeta 1 subunit genes of the human NMDA receptor channel.". Biochem. Biophys. Res. Commun. 197 (2): 922–6. PMID 8267632. 
  • Lannuzel A, Lledo PM, Lamghitnia HO, et al. (1996). "HIV-1 envelope proteins gp120 and gp160 potentiate NMDA-induced [Ca2+]i increase, alter [Ca2+]i homeostasis and induce neurotoxicity in human embryonic neurons.". Eur. J. Neurosci. 7 (11): 2285–93. PMID 8563977. 
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  • Hess SD, Daggett LP, Crona J, et al. (1996). "Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors.". J. Pharmacol. Exp. Ther. 278 (2): 808–16. PMID 8768735. 
  • Wu P, Price P, Du B, et al. (1996). "Direct cytotoxicity of HIV-1 envelope protein gp120 on human NT neurons.". Neuroreport 7 (5): 1045–9. PMID 8804048. 
  • Bennett BA, Rusyniak DE, Hollingsworth CK (1996). "HIV-1 gp120-induced neurotoxicity to midbrain dopamine cultures.". Brain Res. 705 (1-2): 168–76. PMID 8821747. 
  • Toggas SM, Masliah E, Mucke L (1996). "Prevention of HIV-1 gp120-induced neuronal damage in the central nervous system of transgenic mice by the NMDA receptor antagonist memantine.". Brain Res. 706 (2): 303–7. PMID 8822372. 
  • Dreyer EB, Lipton SA (1996). "The coat protein gp120 of HIV-1 inhibits astrocyte uptake of excitatory amino acids via macrophage arachidonic acid.". Eur. J. Neurosci. 7 (12): 2502–7. PMID 8845955. 
  • Raber J, Toggas SM, Lee S, et al. (1997). "Central nervous system expression of HIV-1 Gp120 activates the hypothalamic-pituitary-adrenal axis: evidence for involvement of NMDA receptors and nitric oxide synthase.". Virology 226 (2): 362–73. doi:10.1006/viro.1996.0664. PMID 8955056. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.