Glycine receptor subunit alpha-2 is a protein that in humans is encoded by the GLRA2 gene.[1]
See also
References
Further reading
- Grenningloh G, Schmieden V, Schofield PR, et al. (1990). "Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes.". Embo J. 9 (3): 771–6. PMID 2155780.
- Monani U, Burghes AH (1997). "Structure of the human alpha 2 subunit gene of the glycine receptor--use of vectorette and Alu-exon PCR.". Genome Res. 6 (12): 1200–6. doi:10.1101/gr.6.12.1200. PMID 8973915.
- Cummings CJ, Dahle EJ, Zoghbi HY (1998). "Analysis of the genomic structure of the human glycine receptor alpha2 subunit gene and exclusion of this gene as a candidate for Rett syndrome.". Am. J. Med. Genet. 78 (2): 176–8. doi:10.1002/(SICI)1096-8628(19980630)78:2<176::AID-AJMG16>3.0.CO;2-K. PMID 9674912.
- Feng J, Craddock N, Jones IR, et al. (2001). "Systematic screening for mutations in the glycine receptor alpha2 subunit gene (GLRA2) in patients with schizophrenia and other psychiatric diseases.". Psychiatr. Genet. 11 (1): 45–8. doi:10.1097/00041444-200103000-00009. PMID 11409700.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Davies DL, Crawford DK, Trudell JR, et al. (2004). "Multiple sites of ethanol action in alpha1 and alpha2 glycine receptors suggested by sensitivity to pressure antagonism.". J. Neurochem. 89 (5): 1175–85. doi:10.1111/j.1471-4159.2004.02390.x. PMID 15147510.
- Miller PS, Harvey RJ, Smart TG (2005). "Differential agonist sensitivity of glycine receptor alpha2 subunit splice variants.". Br. J. Pharmacol. 143 (1): 19–26. doi:10.1038/sj.bjp.0705875. PMID 15302677.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- Miller PS, Da Silva HM, Smart TG (2006). "Molecular basis for zinc potentiation at strychnine-sensitive glycine receptors.". J. Biol. Chem. 280 (45): 37877–84. doi:10.1074/jbc.M508303200. PMID 16144831.
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
|
Ion channel, receptor: ligand-gated ion channels |
|
| Cys-loop receptors |
|
|
|
|
|
|
GABAA ( α1, α2, α3, α4, α5, α6, β1, β2, β3, γ1, γ2, γ3, δ, ε, π, θ) · GABAA-ρ ( ρ1, ρ2, ρ3)
|
|
|
|
|
|
|
|
|
|
|
Zinc
|
|
|
|
| Ionotropic glutamates |
|
Ligand-gated only
|
|
|
|
Voltage- and ligand-gated
|
|
|
|
| ATP-gated channels |
|
|
This entry is from Wikipedia, the leading user-contributed encyclopedia. It may not have been reviewed by professional editors (see full disclaimer)
