메뉴 건너뛰기




Volumn 86, Issue 4, 2004, Pages 2238-2250

The External K+ Concentration and Mutations in the Outer Pore Mouth Affect the Inhibition of Kv1.5 Current by Ni2+

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; HISTIDINE; MANGANESE; METAL ION; NICKEL; POTASSIUM CHANNEL; POTASSIUM ION; TRANSITION ELEMENT;

EID: 1942487651     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74282-4     Document Type: Article
Times cited : (6)

References (40)
  • 1
    • 15844371854 scopus 로고    scopus 로고
    • Expression and function of voltage-dependent potassium channel genes in human airway smooth muscle
    • Adda, S., B. K. Fleischmann, B. D. Freedman, M. Yu, D. W. Hay, and M. I. Kotlikoff. 1996. Expression and function of voltage-dependent potassium channel genes in human airway smooth muscle. J. Biol. Chem. 271:13239-13243.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13239-13243
    • Adda, S.1    Fleischmann, B.K.2    Freedman, B.D.3    Yu, M.4    Hay, D.W.5    Kotlikoff, M.I.6
  • 3
    • 0030854945 scopus 로고    scopus 로고
    • Allosteric effects of permeating cations on gating currents during K+ channel deactivation
    • Chen, F. S. P., D. Steele, and D. Fedida. 1997. Allosteric effects of permeating cations on gating currents during K+ channel deactivation. J. Gen. Physiol. 110:87-100.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 87-100
    • Chen, F.S.P.1    Steele, D.2    Fedida, D.3
  • 7
    • 0029798467 scopus 로고    scopus 로고
    • Slow gating charge immobilization in the human potassium chanel Kv1.5 and its prevention by 4-aminopyridine
    • Fedida, D., R. Bouchard, and F. S. P. Chen. 1996. Slow gating charge immobilization in the human potassium chanel Kv1.5 and its prevention by 4-aminopyridine. J. Physiol. 494:377-387.
    • (1996) J. Physiol. , vol.494 , pp. 377-387
    • Fedida, D.1    Bouchard, R.2    Chen, F.S.P.3
  • 8
    • 0033106231 scopus 로고    scopus 로고
    • Modulation of slow inactivation in human cardiac Kv1.5 channels by extra- and intracellular permeant cations
    • Fedida, D., N. D. Maruoka, and S. Lin. 1999. Modulation of slow inactivation in human cardiac Kv1.5 channels by extra- and intracellular permeant cations. J. Physiol. 515:315-329.
    • (1999) J. Physiol. , vol.515 , pp. 315-329
    • Fedida, D.1    Maruoka, N.D.2    Lin, S.3
  • 10
    • 0019995491 scopus 로고
    • Divalent cations and the activation kinetics of potassium channels in squid giant axons
    • Gilly, W. F., and C. M. Armstrong. 1982. Divalent cations and the activation kinetics of potassium channels in squid giant axons. J. Gen. Physiol. 79:965-996.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 965-996
    • Gilly, W.F.1    Armstrong, C.M.2
  • 11
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J. P. 1991. Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42:1-76.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 13
    • 0032714399 scopus 로고    scopus 로고
    • + channel incorporates Q1 and Q2 charge components
    • + channel incorporates Q1 and Q2 charge components. Am. J. Physiol. 277:H1956-H1966.
    • (1999) Am. J. Physiol. , vol.277
    • Hesketh, J.C.1    Fedida, D.2
  • 14
    • 0026049511 scopus 로고
    • + channels: Effects of alterations in the carboxy-terminal region
    • + channels: effects of alterations in the carboxy-terminal region. Neuron. 7:547-556.
    • (1991) Neuron , vol.7 , pp. 547-556
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 15
    • 0035846854 scopus 로고    scopus 로고
    • Regulation of a mammalian Shaker-related potassium channel, hKv1.5, by extracellular potassium and pH
    • Jäger, H., and S. Grissmer. 2001. Regulation of a mammalian Shaker-related potassium channel, hKv1.5, by extracellular potassium and pH. FEBS Lett. 488:45-50.
    • (2001) FEBS Lett. , vol.488 , pp. 45-50
    • Jäger, H.1    Grissmer, S.2
  • 17
    • 85030874570 scopus 로고    scopus 로고
    • Single channel analysis of the inhibition of hKv1.5 current by extracellular protons
    • Abstr.
    • Kwan, D. C. H., D. Fedida, and S. J. Kehl. 2003. Single channel analysis of the inhibition of hKv1.5 current by extracellular protons. Biophys. J. 84:74a. (Abstr.)
    • (2003) Biophys. J. , vol.84
    • Kwan, D.C.H.1    Fedida, D.2    Kehl, S.J.3
  • 19
    • 0036845677 scopus 로고    scopus 로고
    • Structural and functional role of the extracellular S5-P linker in the HERG potassium channel
    • Liu, J., M. Zhang, M. Jiang, and G. N. Tseng. 2002. Structural and functional role of the extracellular S5-P linker in the HERG potassium channel. J. Gen. Physiol. 120:723-737.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 723-737
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.N.4
  • 20
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • Lopez-Barneo, J., T. Hoshi, S. H. Heinemann, and R. W. Aldrich. 1993. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels. 1:61-71.
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • Lopez-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 21
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon, R. 1991. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature. 350:232-235.
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 23
    • 0031886490 scopus 로고    scopus 로고
    • Effects of divalent cations on the E-4031-sensitive repolarization current, I(Kr), in rabbit ventricular myocytes
    • Paquette, T., J. R. Clay, A. Ogbaghebriel, and A. Shrier. 1998. Effects of divalent cations on the E-4031-sensitive repolarization current, I(Kr), in rabbit ventricular myocytes. Biophys. J. 74:1278-1285.
    • (1998) Biophys. J. , vol.74 , pp. 1278-1285
    • Paquette, T.1    Clay, J.R.2    Ogbaghebriel, A.3    Shrier, A.4
  • 24
    • 0035449645 scopus 로고    scopus 로고
    • External nickel blocks human Kv1.5 channels stably expressed in CHO cells
    • Perchenet, L., and O. Clement-Chomienne. 2001. External nickel blocks human Kv1.5 channels stably expressed in CHO cells. J. Membr. Biol. 183:51-60.
    • (2001) J. Membr. Biol. , vol.183 , pp. 51-60
    • Perchenet, L.1    Clement-Chomienne, O.2
  • 27
    • 0028063407 scopus 로고
    • Modulation of potassium channel gating by external divalent cations
    • Spires, S., and T. Begenisich. 1994. Modulation of potassium channel gating by external divalent cations. J. Gen. Physiol. 104:675-692.
    • (1994) J. Gen. Physiol. , vol.104 , pp. 675-692
    • Spires, S.1    Begenisich, T.2
  • 29
    • 0842309099 scopus 로고    scopus 로고
    • Mechanisms of the inhibition of Shaker potassium channels by protons
    • Starkus, J. G., Z. Varga, R. Schonherr, and S. H. Heinemann. 2003. Mechanisms of the inhibition of Shaker potassium channels by protons. Pflugers Arch. 447:44-54.
    • (2003) Pflugers Arch. , vol.447 , pp. 44-54
    • Starkus, J.G.1    Varga, Z.2    Schonherr, R.3    Heinemann, S.H.4
  • 30
    • 0032946237 scopus 로고    scopus 로고
    • Differential sensitivity of voltage-gated potassium channels Kv1.5 and Kv1.2 to acidic pH and molecular identification of pH sensor
    • Steidl, J. V., and A. J. Yool. 1999. Differential sensitivity of voltage-gated potassium channels Kv1.5 and Kv1.2 to acidic pH and molecular identification of pH sensor. Mol. Pharmacol. 55:812-820.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 812-820
    • Steidl, J.V.1    Yool, A.J.2
  • 32
    • 0037214493 scopus 로고    scopus 로고
    • Effect of external pH on activation of the Kv1.5 potassium channel
    • Trapani, J. G., and S. J. Korn. 2003. Effect of external pH on activation of the Kv1.5 potassium channel. Biophys. J. 84:195-204.
    • (2003) Biophys. J. , vol.84 , pp. 195-204
    • Trapani, J.G.1    Korn, S.J.2
  • 36
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in Shaker potassium channels?
    • Yang, Y., Y. Yan, and F. J. Sigworth. 1997. How does the W434F mutation block current in Shaker potassium channels? J. Gen. Physiol. 109: 779-789.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 37
    • 0029930662 scopus 로고    scopus 로고
    • Nickel block of a family of neuronal calcium channels: Subtype- and subunit-dependent action at multiple sites
    • Zamponi, G. W., E. Bourinet, and T. P. Snutch. 1996. Nickel block of a family of neuronal calcium channels: subtype- and subunit-dependent action at multiple sites. J. Membr. Biol. 151:77-90.
    • (1996) J. Membr. Biol. , vol.151 , pp. 77-90
    • Zamponi, G.W.1    Bourinet, E.2    Snutch, T.P.3
  • 39
    • 0034961291 scopus 로고    scopus 로고
    • Modulation of Kv1.5 potassium channel gating by extracellular zinc
    • Zhang, S., S. J. Kehl, and D. Fedida. 2001b. Modulation of Kv1.5 potassium channel gating by extracellular zinc. Biophys. J. 81:125-136.
    • (2001) Biophys. J. , vol.81 , pp. 125-136
    • Zhang, S.1    Kehl, S.J.2    Fedida, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.