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295 related items for PubMed ID: 9788926
1. Interaction of Ba2+ with the pores of the cloned inward rectifier K+ channels Kir2.1 expressed in Xenopus oocytes. Shieh RC, Chang JC, Arreola J. Biophys J; 1998 Nov; 75(5):2313-22. PubMed ID: 9788926 [Abstract] [Full Text] [Related]
2. Effect of extracellular cations on the inward rectifying K+ channels Kir2.1 and Kir3.1/Kir3.4. Owen JM, Quinn CC, Leach R, Findlay JB, Boyett MR. Exp Physiol; 1999 May; 84(3):471-88. PubMed ID: 10362846 [Abstract] [Full Text] [Related]
3. [Barium ion blockade on an inward rectifying potassium current in oocytes of the frog Xenopus laevis]. Gamboa R, Martínez M, Cumming E. Arch Inst Cardiol Mex; 1998 May; 68(3):206-13. PubMed ID: 9810341 [Abstract] [Full Text] [Related]
4. Tamoxifen inhibits inward rectifier K+ 2.x family of inward rectifier channels by interfering with phosphatidylinositol 4,5-bisphosphate-channel interactions. Ponce-Balbuena D, López-Izquierdo A, Ferrer T, Rodríguez-Menchaca AA, Aréchiga-Figueroa IA, Sánchez-Chapula JA. J Pharmacol Exp Ther; 2009 Nov; 331(2):563-73. PubMed ID: 19654266 [Abstract] [Full Text] [Related]
5. Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1. Fujiwara Y, Kubo Y. J Gen Physiol; 2006 Apr; 127(4):401-19. PubMed ID: 16533896 [Abstract] [Full Text] [Related]
8. Mechanisms for the time-dependent decay of inward currents through cloned Kir2.1 channels expressed in Xenopus oocytes. Shieh RC. J Physiol; 2000 Jul 15; 526 Pt 2(Pt 2):241-52. PubMed ID: 10896715 [Abstract] [Full Text] [Related]
9. Identification of Kir2.1 channel activity in cultured trabecular meshwork cells. Llobet A, Gasull X, Palés J, Martí E, Gual A. Invest Ophthalmol Vis Sci; 2001 Sep 15; 42(10):2371-9. PubMed ID: 11527952 [Abstract] [Full Text] [Related]
10. Electrostatics in the cytoplasmic pore produce intrinsic inward rectification in kir2.1 channels. Yeh SH, Chang HK, Shieh RC. J Gen Physiol; 2005 Dec 15; 126(6):551-62. PubMed ID: 16316974 [Abstract] [Full Text] [Related]
11. Regulation of inward rectifier K+ channels by shift of intracellular pH dependence. Collins A, Larson M. J Cell Physiol; 2005 Jan 15; 202(1):76-86. PubMed ID: 15389543 [Abstract] [Full Text] [Related]
12. Barium blockade of a clonal potassium channel and its regulation by a critical pore residue. Taglialatela M, Drewe JA, Brown AM. Mol Pharmacol; 1993 Jul 15; 44(1):180-90. PubMed ID: 8341271 [Abstract] [Full Text] [Related]
14. Inward rectification of the IRK1 channel expressed in Xenopus oocytes: effects of intracellular pH reveal an intrinsic gating mechanism. Shieh RC, John SA, Lee JK, Weiss JN. J Physiol; 1996 Jul 15; 494 ( Pt 2)(Pt 2):363-76. PubMed ID: 8841997 [Abstract] [Full Text] [Related]
15. Direct block of inward rectifier potassium channels by nicotine. Wang H, Yang B, Zhang L, Xu D, Wang Z. Toxicol Appl Pharmacol; 2000 Apr 01; 164(1):97-101. PubMed ID: 10739749 [Abstract] [Full Text] [Related]
16. Voltage-dependent gating and block by internal spermine of the murine inwardly rectifying K+ channel, Kir2.1. Matsuda H, Oishi K, Omori K. J Physiol; 2003 Apr 15; 548(Pt 2):361-71. PubMed ID: 12640008 [Abstract] [Full Text] [Related]
17. Electrostatic tuning of Mg2+ affinity in an inward-rectifier K+ channel. Lu Z, MacKinnon R. Nature; 1994 Sep 15; 371(6494):243-6. PubMed ID: 7915826 [Abstract] [Full Text] [Related]
18. Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification. Lopatin AN, Makhina EN, Nichols CG. Nature; 1994 Nov 24; 372(6504):366-9. PubMed ID: 7969496 [Abstract] [Full Text] [Related]
19. Molecular characterization of an inwardly rectifying K+ channel from HeLa cells. Klein H, Garneau L, Coady M, Lemay G, Lapointe JY, Sauvé R. J Membr Biol; 1999 Jan 01; 167(1):43-52. PubMed ID: 9878074 [Abstract] [Full Text] [Related]
20. The mechanism of inward rectification of potassium channels: "long-pore plugging" by cytoplasmic polyamines. Lopatin AN, Makhina EN, Nichols CG. J Gen Physiol; 1995 Nov 01; 106(5):923-55. PubMed ID: 8648298 [Abstract] [Full Text] [Related] Page: [Next] [New Search]