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Volumn 85, Issue 1, 2003, Pages 300-312

The pore helix is involved in stabilizing the open state of inwardly rectifying K+ channels

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; MEMBRANE PROTEIN; POTASSIUM CHANNEL; POTASSIUM ION; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 0038579261     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74475-0     Document Type: Article
Times cited : (39)

References (58)
  • 1
    • 0035878639 scopus 로고    scopus 로고
    • Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: Differential contribution by two discrete residues
    • Alagem, N., M. Dvir, and E. Reuveny. 2001. Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 534:381-393.
    • (2001) J Physiol. , vol.534 , pp. 381-393
    • Alagem, N.1    Dvir, M.2    Reuveny, E.3
  • 2
    • 0031022168 scopus 로고    scopus 로고
    • Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating
    • Chapman, M. L., H. M. VanDongen, and A. M. VanDongen. 1997. Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating. Biophys. J. 72:708-719.
    • (1997) Biophys. J. , vol.72 , pp. 708-719
    • Chapman, M.L.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 3
    • 0033058271 scopus 로고    scopus 로고
    • Structural determinants of gating in inward-rectifier K+ channels
    • Choe, H., L. G. Palmer, and H. Sackin. 1999. Structural determinants of gating in inward-rectifier K+ channels. Biophys. J. 76:1988-2003.
    • (1999) Biophys. J. , vol.76 , pp. 1988-2003
    • Choe, H.1    Palmer, L.G.2    Sackin, H.3
  • 4
    • 0031688597 scopus 로고    scopus 로고
    • Permeation and gating of an inwardly rectifying potassium channel. Evidence for a variable energy well
    • Choe, H., H. Sackin, and L. G. Palmer. 1998. Permeation and gating of an inwardly rectifying potassium channel. Evidence for a variable energy well. J. Gen. Physiol. 112:433-446.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 433-446
    • Choe, H.1    Sackin, H.2    Palmer, L.G.3
  • 5
    • 0035498636 scopus 로고    scopus 로고
    • Gating properties of inward-rectifier potassium channels: Effects of permeant ions
    • Choe, H., H. Sackin, and L. G. Palmer. 2001. Gating properties of inward-rectifier potassium channels: effects of permeant ions. J. Membr. Biol. 184:81-89.
    • (2001) J. Membr. Biol. , vol.184 , pp. 81-89
    • Choe, H.1    Sackin, H.2    Palmer, L.G.3
  • 6
    • 0030664037 scopus 로고    scopus 로고
    • A conserved cytoplasmic region of ROMK modulates pH sensitivity, conductance, and gating
    • Choe, H., H. Zhou, L. G. Palmer, and H. Sackin. 1997. A conserved cytoplasmic region of ROMK modulates pH sensitivity, conductance, and gating. Am. J. Physiol. 273:F516-F529.
    • (1997) Am. J. Physiol. , vol.273
    • Choe, H.1    Zhou, H.2    Palmer, L.G.3    Sackin, H.4
  • 7
    • 0022272338 scopus 로고
    • Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate
    • Colquhoun, D., and B. Sakmann. 1985. Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate. J Physiol. 369:501-557.
    • (1985) J Physiol. , vol.369 , pp. 501-557
    • Colquhoun, D.1    Sakmann, B.2
  • 8
    • 0032538623 scopus 로고    scopus 로고
    • Identification of native atrial G-protein-regulated inwardly rectifying K+ (GIRK4) channel homomultimers
    • Corey, S., and D. E. Clapham. 1998. Identification of native atrial G-protein-regulated inwardly rectifying K+ (GIRK4) channel homomultimers. J. Biol. Chem. 273:27499-27504.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27499-27504
    • Corey, S.1    Clapham, D.E.2
  • 9
    • 85031145558 scopus 로고    scopus 로고
    • Discerning the closed size of the rod cyclic nucleotide-gated channel smokehole
    • Craven, K. B., and W. N. Zagotta. 2002. Discerning the closed size of the rod cyclic nucleotide-gated channel smokehole. Biophys. J. 82:274a.
    • (2002) Biophys. J. , vol.82
    • Craven, K.B.1    Zagotta, W.N.2
  • 10
    • 4243961394 scopus 로고    scopus 로고
    • Fast gating transitions determined by dynamic rearrangements in the selectivity filter of KcsA
    • Cuello, L. G., and E. Perozo. 2002. Fast gating transitions determined by dynamic rearrangements in the selectivity filter of KcsA. Biophys. J. 82:174a.
    • (2002) Biophys. J. , vol.82
    • Cuello, L.G.1    Perozo, E.2
  • 11
    • 0032528923 scopus 로고    scopus 로고
    • The selectivity filter of a potassium channel, murine kir2.1, investigated using scanning cysteine mutagenesis
    • Dart, C., M. L. Leyland, P. J. Spencer, P. R. Stanfield, and M. J. Sutcliffe. 1998. The selectivity filter of a potassium channel, murine kir2.1, investigated using scanning cysteine mutagenesis. J Physiol. 511:25-32.
    • (1998) J. Physiol. , vol.511 , pp. 25-32
    • Dart, C.1    Leyland, M.L.2    Spencer, P.J.3    Stanfield, P.R.4    Sutcliffe, M.J.5
  • 12
    • 0035923745 scopus 로고    scopus 로고
    • Tight steric closure at the intracellular activation gate of a voltage-gated K(+) channel
    • del Camino, D., and G. Yellen. 2001. Tight steric closure at the intracellular activation gate of a voltage-gated K(+) channel. Neuron. 32:649-656.
    • (2001) Neuron , vol.32 , pp. 649-656
    • Del Camino, D.1    Yellen, G.2
  • 14
    • 0032505868 scopus 로고    scopus 로고
    • KATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit
    • Drain, P., L. Li, and J. Wang. 1998. KATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit. Proc. Natl. Acad. Sci. USA. 95:13953-13958.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13953-13958
    • Drain, P.1    Li, L.2    Wang, J.3
  • 15
    • 0034889859 scopus 로고    scopus 로고
    • Dynamic interaction of S5 and S6 during voltage-controlled gating in a potassium channel
    • Espinosa, F., R. Fleischhauer, A. McMahon, and R. H. Joho. 2001. Dynamic interaction of S5 and S6 during voltage-controlled gating in a potassium channel. J. Gen. Physiol. 118:157-170.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 157-170
    • Espinosa, F.1    Fleischhauer, R.2    McMahon, A.3    Joho, R.H.4
  • 16
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels
    • Flynn, G. E., and W. N. Zagotta. 2001. Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron. 30:689-698.
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 17
    • 0031849619 scopus 로고    scopus 로고
    • Comparison of the open-close kinetics of the cloned inward rectifier K+ channel IRK1 and its point mutant (Q140E) in the pore region
    • Guo, L., and Y. Kubo. 1998. Comparison of the open-close kinetics of the cloned inward rectifier K+ channel IRK1 and its point mutant (Q140E) in the pore region. Receptors Channels. 5:273-289.
    • (1998) Receptors Channels , vol.5 , pp. 273-289
    • Guo, L.1    Kubo, Y.2
  • 18
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., A. Marty, E. Neher, B. Sakmann, and F. J. Sigworth. 1981. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 391:85-100.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 19
    • 0032168179 scopus 로고    scopus 로고
    • The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge
    • Holmgren, M., K. S. Shin, and G. Yellen. 1998. The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge. Neuron. 21:617-621.
    • (1998) Neuron , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 20
    • 0025126043 scopus 로고
    • Strategy for analysing the cooperativity of intramolecular interactions in peptides and proteins
    • Horovitz, A., and A. R. Fersht. 1990. Strategy for analysing the cooperativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214:613-617.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 21
    • 0031058470 scopus 로고    scopus 로고
    • Effector contributions to G beta gamma-mediated signaling as revealed by muscarinic potassium channel gating
    • Ivanova-Nikolova, T. T., and G. E. Breitwieser. 1997. Effector contributions to G beta gamma-mediated signaling as revealed by muscarinic potassium channel gating. J. Gen. Physiol. 109:245-253.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 245-253
    • Ivanova-Nikolova, T.T.1    Breitwieser, G.E.2
  • 23
    • 0036753545 scopus 로고    scopus 로고
    • The subunits of G proteins gate a K+ channel by pivoted bending of a transmembrane segment
    • Jin, T., L. Peng, T. Mirshahi, T. Rohacs, K. W. Chan, R. Sanchez, and D. E. Logothetis. 2002. The subunits of G proteins gate a K+ channel by pivoted bending of a transmembrane segment. Mol. Cell. 10:469-481.
    • (2002) Mol. Cell , vol.10 , pp. 469-481
    • Jin, T.1    Peng, L.2    Mirshahi, T.3    Rohacs, T.4    Chan, K.W.5    Sanchez, R.6    Logothetis, D.E.7
  • 24
    • 0035974844 scopus 로고    scopus 로고
    • Rotational movement during cyclic nucleotide-gated channel opening
    • Johnson, J. P., Jr., and W. N. Zagotta. 2001. Rotational movement during cyclic nucleotide-gated channel opening. Nature. 412:917-921.
    • (2001) Nature , vol.412 , pp. 917-921
    • Johnson J.P., Jr.1    Zagotta, W.N.2
  • 25
    • 0027403280 scopus 로고
    • Primary structure and functional expression of a mouse inward rectifier potassium channel
    • Kubo, Y., T. J. Baldwin, Y. N. Jan, and L. Y. Jan. 1993. Primary structure and functional expression of a mouse inward rectifier potassium channel. Nature. 362:127-133.
    • (1993) Nature , vol.362 , pp. 127-133
    • Kubo, Y.1    Baldwin, T.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 26
    • 0034680907 scopus 로고    scopus 로고
    • Residues and mechanisms for slow activation and Ba2+ block of the cardiac muscarinic K+ channel, Kir3.1/Kir3.4
    • Lancaster, M. K., K. M. Dibb, C. C. Quinn, R. Leach, J. K. Lee, J. B. Findlay, and M. R. Boyett. 2000. Residues and mechanisms for slow activation and Ba2+ block of the cardiac muscarinic K+ channel, Kir3.1/Kir3.4. J. Biol. Chem. 275:35831-35839.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35831-35839
    • Lancaster, M.K.1    Dibb, K.M.2    Quinn, C.C.3    Leach, R.4    Lee, J.K.5    Findlay, J.B.6    Boyett, M.R.7
  • 27
    • 0036142013 scopus 로고    scopus 로고
    • Open state destabilization by ATP occupancy is mechanism speeding burst exit underlying KATP channel inhibition by ATP
    • Li, L., X. Geng, and P. Drain. 2002. Open state destabilization by ATP occupancy is mechanism speeding burst exit underlying KATP channel inhibition by ATP. J. Gen. Physiol. 119:105-116.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 105-116
    • Li, L.1    Geng, X.2    Drain, P.3
  • 28
    • 0034520641 scopus 로고    scopus 로고
    • Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels
    • Liu, J., and S. A. Siegelbaum. 2000. Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels. Neuron. 28:899-909.
    • (2000) Neuron , vol.28 , pp. 899-909
    • Liu, J.1    Siegelbaum, S.A.2
  • 29
    • 0030795112 scopus 로고    scopus 로고
    • Gated access to the pore of a voltage-dependent K+ channel
    • Liu, Y., M. Holmgren, M. E. Jurman, and G. Yellen. 1997. Gated access to the pore of a voltage-dependent K+ channel. Neuron. 19:175-184.
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 30
    • 0033958664 scopus 로고    scopus 로고
    • Structure and dynamics of the pore of inwardly rectifying K(ATP) channels
    • Loussouarn, G., E. N. Makhina, T. Rose, and C. G. Nichols. 2000. Structure and dynamics of the pore of inwardly rectifying K(ATP) channels. J. Biol. Chem. 275:1137-1144.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1137-1144
    • Loussouarn, G.1    Makhina, E.N.2    Rose, T.3    Nichols, C.G.4
  • 31
    • 0035119276 scopus 로고    scopus 로고
    • Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter
    • Lu, T., A. Y. Ting, J. Mainland, L. Y. Jan, P. G. Schultz, and J. Yang. 2001a. Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter. Nat. Neurosci. 4:239-246.
    • (2001) Nat. Neurosci. , vol.4 , pp. 239-246
    • Lu, T.1    Ting, A.Y.2    Mainland, J.3    Jan, L.Y.4    Schultz, P.G.5    Yang, J.6
  • 32
    • 0035165533 scopus 로고    scopus 로고
    • Permeant ion-dependent changes in gating of Kir2.1 inward rectifier potassium channels
    • Lu, T., L. Wu, J. Xiao, and J. Yang. 2001b. Permeant ion-dependent changes in gating of Kir2.1 inward rectifier potassium channels. J. Gen. Physiol. 118:509-522.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 509-522
    • Lu, T.1    Wu, L.2    Xiao, J.3    Yang, J.4
  • 33
    • 0020973067 scopus 로고
    • Burst kinetics of single calcium-activated potassium channels in cultured rat muscle
    • Magleby, K. L., and B. S. Pallotta. 1983. Burst kinetics of single calcium-activated potassium channels in cultured rat muscle. J Physiol. 344:605-623.
    • (1983) J. Physiol. , vol.344 , pp. 605-623
    • Magleby, K.L.1    Pallotta, B.S.2
  • 34
    • 0032606702 scopus 로고    scopus 로고
    • Gβγ binding increases the open time of IKACh: Kinetic evidence for multiple Gβγ binding sites
    • Nemec, J., K. Wickman, and D. E. Clapham. 1999. Gβγ binding increases the open time of IKACh: kinetic evidence for multiple Gβγ binding sites. Biophys. J. 76:246-252.
    • (1999) Biophys. J. , vol.76 , pp. 246-252
    • Nemec, J.1    Wickman, K.2    Clapham, D.E.3
  • 35
    • 0033516494 scopus 로고    scopus 로고
    • Structural rearrangements underlying K+-channel activation gating
    • Perozo, E., D. M. Cortes, and L. G. Cuello. 1999. Structural rearrangements underlying K+-channel activation gating. Science. 285:73-78.
    • (1999) Science , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 36
    • 0035870848 scopus 로고    scopus 로고
    • Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1
    • Pessia, M., P. Imbrici, M. C. D'Adamo, L. Salvatore, and S. J. Tucker. 2001. Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1. J Physiol. 532:359-367.
    • (2001) J. Physiol. , vol.532 , pp. 359-367
    • Pessia, M.1    Imbrici, P.2    D'Adamo, M.C.3    Salvatore, L.4    Tucker, S.J.5
  • 38
    • 4243815854 scopus 로고    scopus 로고
    • Cold draft through the teepee: MTSEA access to the inner vestibule of ATP closed Kir6.2 channels implies gating does not occur at the smokehole
    • Philips, L. R., G. Loussouarn, and C. G. Nichols. 2002. Cold draft through the teepee: MTSEA access to the inner vestibule of ATP closed Kir6.2 channels implies gating does not occur at the smokehole. Biophys. J. 82:590a.
    • (2002) Biophys. J. , vol.82
    • Philips, L.R.1    Loussouarn, G.2    Nichols, C.G.3
  • 39
    • 0034774587 scopus 로고    scopus 로고
    • Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel
    • Proks, P., C. E. Capener, P. Jones, and F. M. Ashcroft. 2001. Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel. J. Gen. Physiol. 118:341-353.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 341-353
    • Proks, P.1    Capener, C.E.2    Jones, P.3    Ashcroft, F.M.4
  • 40
    • 9044225529 scopus 로고    scopus 로고
    • Contributions of a negatively charged residue in the hydrophobic domain of the IRK1 inwardly rectifying K+ channel to K(+)-selective permeation
    • Reuveny, E., Y. N. Jan, and L. Y. Jan. 1996. Contributions of a negatively charged residue in the hydrophobic domain of the IRK1 inwardly rectifying K+ channel to K(+)-selective permeation. Biophys. J. 70:754-761.
    • (1996) Biophys. J. , vol.70 , pp. 754-761
    • Reuveny, E.1    Jan, Y.N.2    Jan, L.Y.3
  • 42
    • 0036143456 scopus 로고    scopus 로고
    • Voltage-controlled gating at the intracellular entrance to a hyperpolarization-activated cation channel
    • Rothberg, B. S., K. S. Shin, P. S. Phale, and G. Yellen. 2002. Voltage-controlled gating at the intracellular entrance to a hyperpolarization-activated cation channel. J. Gen. Physiol. 119:83-91.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 83-91
    • Rothberg, B.S.1    Shin, K.S.2    Phale, P.S.3    Yellen, G.4
  • 43
    • 0034744617 scopus 로고    scopus 로고
    • Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels
    • Sadja, R., K. Smadja, N. Alagem, and E. Reuveny. 2001. Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels. Neuron. 29:669-680.
    • (2001) Neuron , vol.29 , pp. 669-680
    • Sadja, R.1    Smadja, K.2    Alagem, N.3    Reuveny, E.4
  • 44
    • 0020575547 scopus 로고
    • Acetylcholine activation of single muscarinic K+ channels in isolated pacemaker cells of the mammalian heart
    • Sakmann, B., A. Noma, and W. Trautwein. 1983. Acetylcholine activation of single muscarinic K+ channels in isolated pacemaker cells of the mammalian heart. Nature. 303:250-253.
    • (1983) Nature , vol.303 , pp. 250-253
    • Sakmann, B.1    Noma, A.2    Trautwein, W.3
  • 45
    • 0023478292 scopus 로고
    • Data transformations for improved display and fitting of single-channel dwell time histograms
    • Sigworth, F. J., and S. M. Sine. 1987. Data transformations for improved display and fitting of single-channel dwell time histograms. Biophys. J. 52:1047-1054.
    • (1987) Biophys. J. , vol.52 , pp. 1047-1054
    • Sigworth, F.J.1    Sine, S.M.2
  • 46
    • 0031684419 scopus 로고    scopus 로고
    • Asymmetrical contributions of subunit pore regions to ion selectivity in an inward rectifier K+ channel
    • Silverman, S. K., H. A. Lester, and D. A. Dougherty. 1998. Asymmetrical contributions of subunit pore regions to ion selectivity in an inward rectifier K+ channel. Biophys. J. 75:1330-1339.
    • (1998) Biophys. J. , vol.75 , pp. 1330-1339
    • Silverman, S.K.1    Lester, H.A.2    Dougherty, D.A.3
  • 47
    • 0028792376 scopus 로고
    • Identification of structural elements involved in G protein gating of the GIRK1 potassium channel
    • Slesinger, P. A., E. Reuveny, Y. N. Jan, and L. Y. Jan. 1995. Identification of structural elements involved in G protein gating of the GIRK1 potassium channel. Neuron. 15:1145-1156.
    • (1995) Neuron , vol.15 , pp. 1145-1156
    • Slesinger, P.A.1    Reuveny, E.2    Jan, Y.N.3    Jan, L.Y.4
  • 48
    • 0036053724 scopus 로고    scopus 로고
    • Constitutively active and G-protein coupled inward rectifier K+ channels: Kir2.0 and Kir3.0
    • Stanfield, P. R., S. Nakajima, and Y. Nakajima. 2002. Constitutively active and G-protein coupled inward rectifier K+ channels: Kir2.0 and Kir3.0. Rev. Physiol. Biochem. Pharmacol. 145:47-179.
    • (2002) Rev. Physiol. Biochem. Pharmacol. , vol.145 , pp. 47-179
    • Stanfield, P.R.1    Nakajima, S.2    Nakajima, Y.3
  • 50
    • 0003341858 scopus 로고    scopus 로고
    • Where is the activation gate for PIP2 gating of Kir2.1 channels?
    • Xiao, J., and J. Yang. 2002. Where is the activation gate for PIP2 gating of Kir2.1 channels? Biophys. J. 82:180a.
    • (2002) Biophys. J. , vol.82
    • Xiao, J.1    Yang, J.2
  • 51
    • 0034194410 scopus 로고    scopus 로고
    • Slow modal gating of single G protein-activated K+ channels expressed in Xenopus oocytes
    • Yakubovich, D., V. Pastushenko, A. Bitler, C. W. Dessauer, and N. Dascal. 2000. Slow modal gating of single G protein-activated K+ channels expressed in Xenopus oocytes. J Physiol 524:737-755.
    • (2000) J. Physiol. , vol.524 , pp. 737-755
    • Yakubovich, D.1    Pastushenko, V.2    Bitler, A.3    Dessauer, C.W.4    Dascal, N.5
  • 52
    • 0024539514 scopus 로고
    • Block of stretch-activated ion channels in Xenopus oocytes by gadolinium and calcium ions
    • Yang, X. C., and F. Sachs. 1989. Block of stretch-activated ion channels in Xenopus oocytes by gadolinium and calcium ions. Science. 243:1068-1071.
    • (1989) Science , vol.243 , pp. 1068-1071
    • Yang, X.C.1    Sachs, F.2
  • 53
    • 0035049090 scopus 로고    scopus 로고
    • Yeast screen for constitutively active mutant G protein-activated potassium channels
    • Yi, B. A., Y. F. Lin, Y. N. Jan, and L. Y. Jan. 2001. Yeast screen for constitutively active mutant G protein-activated potassium channels. Neuron. 29:657-667.
    • (2001) Neuron , vol.29 , pp. 657-667
    • Yi, B.A.1    Lin, Y.F.2    Jan, Y.N.3    Jan, L.Y.4
  • 54
    • 0037131520 scopus 로고    scopus 로고
    • Energetics of pore opening in a voltage-gated K(+) channel
    • Yifrach, O., and R. MacKinnon. 2002. Energetics of pore opening in a voltage-gated K(+) channel. Cell. 111:231-239.
    • (2002) Cell , vol.111 , pp. 231-239
    • Yifrach, O.1    MacKinnon, R.2
  • 55
    • 0030818830 scopus 로고    scopus 로고
    • Selectivity changes during activation of mutant Shaker potassium channels
    • Zheng, J., and F. J. Sigworth. 1997. Selectivity changes during activation of mutant Shaker potassium channels. J. Gen. Physiol. 110:101-117.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 101-117
    • Zheng, J.1    Sigworth, F.J.2
  • 56
    • 0031718345 scopus 로고    scopus 로고
    • Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels
    • Zheng, J., and F. J. Sigworth. 1998. Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels. J. Gen. Physiol. 112:457-474.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 457-474
    • Zheng, J.1    Sigworth, F.J.2
  • 58
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • Zhou, Y., J. H. Morais-Cabral, A. Kaufman, and R. MacKinnon. 2001. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature. 414:43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.