These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
179 related articles for article (PubMed ID: 9662556)
1. Separate domains for desensitization of GABA rho 1 and beta 2 subunits expressed in Xenopus oocytes. Lu L; Huang Y J Membr Biol; 1998 Jul; 164(2):115-24. PubMed ID: 9662556 [TBL] [Abstract][Full Text] [Related]
2. Modulation of recombinant GABA receptor/channel subunits by domain-specific antibodies in Xenopus oocytes. Ekema GM; Zheng W; Wang L; Lu L J Membr Biol; 2001 Oct; 183(3):205-13. PubMed ID: 11696862 [TBL] [Abstract][Full Text] [Related]
3. A single amino acid change within the ion-channel domain of the gamma-aminobutyric acid rho1 receptor accelerates desensitization and increases taurine agonism. Martínez-Torres A; Miledi R Arch Med Res; 2004; 35(3):194-8. PubMed ID: 15163459 [TBL] [Abstract][Full Text] [Related]
4. Evidence for coassembly of mutant GABAC rho1 with GABAA gamma2S, glycine alpha1 and glycine alpha2 receptor subunits in vitro. Pan ZH; Zhang D; Zhang X; Lipton SA Eur J Neurosci; 2000 Sep; 12(9):3137-45. PubMed ID: 10998097 [TBL] [Abstract][Full Text] [Related]
5. GABArho 1/GABAAalpha 1 receptor chimeras to study receptor desensitization. Martínez-Torres A; Demuro A; Miledi R Proc Natl Acad Sci U S A; 2000 Mar; 97(7):3562-6. PubMed ID: 10725369 [TBL] [Abstract][Full Text] [Related]
6. A single amino acid in the second transmembrane domain of GABA rho subunits is a determinant of the response kinetics of GABAC receptors. Qian H; Dowling JE; Ripps H J Neurobiol; 1999 Jul; 40(1):67-76. PubMed ID: 10398072 [TBL] [Abstract][Full Text] [Related]
7. Sequences in the amino termini of GABA rho and GABA(A) subunits specify their selective interaction in vitro. Hackam AS; Wang TL; Guggino WB; Cutting GR J Neurochem; 1998 Jan; 70(1):40-6. PubMed ID: 9422345 [TBL] [Abstract][Full Text] [Related]
8. Structural determinants for antagonist pharmacology that distinguish the rho1 GABAC receptor from GABAA receptors. Zhang J; Xue F; Chang Y Mol Pharmacol; 2008 Oct; 74(4):941-51. PubMed ID: 18599601 [TBL] [Abstract][Full Text] [Related]
9. Modular design of Cys-loop ligand-gated ion channels: functional 5-HT3 and GABA rho1 receptors lacking the large cytoplasmic M3M4 loop. Jansen M; Bali M; Akabas MH J Gen Physiol; 2008 Feb; 131(2):137-46. PubMed ID: 18227272 [TBL] [Abstract][Full Text] [Related]
10. Functional characterization and visualization of a GABAA receptor-GFP chimera expressed in Xenopus oocytes. Bueno OF; Robinson LC; Alvarez-Hernandez X; Leidenheimer NJ Brain Res Mol Brain Res; 1998 Aug; 59(2):165-77. PubMed ID: 9729362 [TBL] [Abstract][Full Text] [Related]
11. Co-assembly of GABA rho subunits with the GABA(A) receptor gamma(2) subunit cloned from white perch retina. Qian H; Pan Y Brain Res Mol Brain Res; 2002 Jun; 103(1-2):62-70. PubMed ID: 12106692 [TBL] [Abstract][Full Text] [Related]
12. A chimeric prokaryotic-eukaryotic pentameric ligand gated ion channel reveals interactions between the extracellular and transmembrane domains shape neurosteroid modulation. Ghosh B; Tsao TW; Czajkowski C Neuropharmacology; 2017 Oct; 125():343-352. PubMed ID: 28803966 [TBL] [Abstract][Full Text] [Related]
13. The agonist binding site of the gamma-aminobutyric acid type A channel is not formed by the extracellular cysteine loop. Amin J; Dickerson IM; Weiss DS Mol Pharmacol; 1994 Feb; 45(2):317-23. PubMed ID: 7509443 [TBL] [Abstract][Full Text] [Related]
14. A single M1 residue in the beta2 subunit alters channel gating of GABAA receptor in anesthetic modulation and direct activation. Chang CS; Olcese R; Olsen RW J Biol Chem; 2003 Oct; 278(44):42821-8. PubMed ID: 12939268 [TBL] [Abstract][Full Text] [Related]
15. Functional asymmetry of the conserved cystine loops in alphabetagamma GABA A receptors revealed by the response to GABA activation and drug potentiation. Tierney ML; Luu T; Gage PW Int J Biochem Cell Biol; 2008; 40(5):968-79. PubMed ID: 18083058 [TBL] [Abstract][Full Text] [Related]