메뉴 건너뛰기




Volumn 137, Issue 6, 2011, Pages 533-548

Low resistance, large dimension entrance to the inner cavity of BK channels determined by changing side-chain volume

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; MUB PROTEIN, ENTEROBACTERIA PHAGE MU; POTASSIUM; VIRUS PROTEIN;

EID: 79958032674     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201110616     Document Type: Article
Times cited : (27)

References (54)
  • 3
    • 0020630896 scopus 로고
    • Ion movement through gramicidin A channels. Studies on the diffusion-controlled association step
    • Andersen, O.S. 1983. Ion movement through gramicidin A channels. Studies on the diffusion-controlled association step. Biophys. J. 41:147-165
    • (1983) Biophys. J. , vol.41 , pp. 147-165
    • Andersen, O.S.1
  • 4
    • 0020000206 scopus 로고
    • Properties of single calcium-activated potassium channels in cultured rat muscle
    • Barrett, J.N., K.L. Magleby, and B.S. Pallotta. 1982. Properties of single calcium-activated potassium channels in cultured rat muscle. J. Physiol. 331:211-230.
    • (1982) J. Physiol. , vol.331 , pp. 211-230
    • Barrett, J.N.1    Magleby, K.L.2    Pallotta, B.S.3
  • 6
    • 0021266783 scopus 로고
    • Ion conductance and selectivity of single calcium-activated potassium channels in cultured rat muscle
    • Blatz, A.L., and K.L. Magleby. 1984. Ion conductance and selectivity of single calcium-activated potassium channels in cultured rat muscle. J. Gen. Physiol. 84:1-23
    • (1984) J. Gen. Physiol. , vol.84 , pp. 1-23
    • Blatz, A.L.1    Magleby, K.L.2
  • 7
    • 1442285221 scopus 로고    scopus 로고
    • + and contribute to the limits of unitary currents at high voltages
    • + and contribute to the limits of unitary currents at high voltages. J. Gen. Physiol. 123:305-319
    • (2004) J. Gen. Physiol. , vol.123 , pp. 305-319
    • Brelidze, T.I.1    Magleby, K.L.2
  • 8
    • 23744472418 scopus 로고    scopus 로고
    • Probing the geometry of the inner vestibule of BK channels with sugars
    • Brelidze, T.I., and K.L. Magleby. 2005. Probing the geometry of the inner vestibule of BK channels with sugars. J. Gen. Physiol. 126:105- 121
    • (2005) J. Gen. Physiol. , vol.126 , pp. 105-121
    • Brelidze, T.I.1    Magleby, K.L.2
  • 9
    • 0041806510 scopus 로고    scopus 로고
    • A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification
    • Brelidze, T.I., X. Niu, and K.L. Magleby. 2003. A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification. Proc. Natl. Acad. Sci. USA. 100:9017-9022
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 9017-9022
    • Brelidze, T.I.1    Niu, X.2    Magleby, K.L.3
  • 11
    • 0027161159 scopus 로고
    • mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels
    • Butler, A., S. Tsunoda, D.P. McCobb, A. Wei, and L. Salkoff. 1993. mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels. Science. 261:221-224
    • (1993) Science , vol.261 , pp. 221-224
    • Butler, A.1    Tsunoda, S.2    McCobb, D.P.3    Wei, A.4    Salkoff, L.5
  • 17
    • 0001193210 scopus 로고
    • Ion solvation via neutron-scattering
    • Enderby, J.E. 1995. Ion solvation via neutron-scattering. Chem. Soc. Rev. 24:159-168
    • (1995) Chem. Soc. Rev. , vol.24 , pp. 159-168
    • Enderby, J.E.1
  • 18
    • 38149012053 scopus 로고    scopus 로고
    • Role of the intracellular cavity in potassium channel conductivity
    • Furini, S., F. Zerbetto, and S. Cavalcanti. 2007. Role of the intracellular cavity in potassium channel conductivity. J. Phys. Chem. B. 111: 13993-14000
    • (2007) J. Phys. Chem. B. , vol.111 , pp. 13993-14000
    • Furini, S.1    Zerbetto, F.2    Cavalcanti, S.3
  • 19
    • 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
  • 22
    • 0003443746 scopus 로고    scopus 로고
    • Third edition. Sinauer Associates, Inc., Sunderland, MA
    • Hille, B. 2001. Ion Channels of Excitable Membranes. Third edition. Sinauer Associates, Inc., Sunderland, MA. 730
    • (2001) Ion Channels of Excitable Membranes , pp. 730
    • Hille, B.1
  • 23
    • 77956762744 scopus 로고    scopus 로고
    • BK channels mediate a novel ionic mechanism that regulates glucose-dependent electrical activity and insulin secretion in mouse pancreatic β-cells
    • Houamed, K.M., I.R. Sweet, and L.S. Satin. 2010. BK channels mediate a novel ionic mechanism that regulates glucose-dependent electrical activity and insulin secretion in mouse pancreatic β-cells. J. Physiol. 588:3511-3523
    • (2010) J. Physiol. , vol.588 , pp. 3511-3523
    • Houamed, K.M.1    Sweet, I.R.2    Satin, L.S.3
  • 24
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon. 2002a. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 27
    • 0014009204 scopus 로고
    • Effects of blocking sulfhydryl groups and of reducing disulfide bonds on the acetylcholine-activated permeability system of the electroplax
    • Karlin, A., and E. Bartels. 1966. Effects of blocking sulfhydryl groups and of reducing disulfide bonds on the acetylcholine-activated permeability system of the electroplax. Biochim. Biophys. Acta. 126: 525-535
    • (1966) Biochim. Biophys. Acta. , vol.126 , pp. 525-535
    • Karlin, A.1    Bartels, E.2
  • 28
    • 0037120735 scopus 로고    scopus 로고
    • Dynamic hydration numbers for biologically important ions
    • Kiriukhin, M.Y., and K.D. Collins. 2002. Dynamic hydration numbers for biologically important ions. Biophys. Chem. 99:155-168
    • (2002) Biophys. Chem. , vol.99 , pp. 155-168
    • Kiriukhin, M.Y.1    Collins, K.D.2
  • 31
  • 33
    • 77956012236 scopus 로고    scopus 로고
    • BK channel activation: structural and functional insights
    • Lee, U.S., and J. Cui. 2010. BK channel activation: structural and functional insights. Trends Neurosci. 33:415-423
    • (2010) Trends Neurosci , vol.33 , pp. 415-423
    • Lee, U.S.1    Cui, J.2
  • 34
    • 3142682254 scopus 로고    scopus 로고
    • Unique inner pore properties of BK channels revealed by quaternary ammonium block
    • Li, W., and R.W. Aldrich. 2004. Unique inner pore properties of BK channels revealed by quaternary ammonium block. J. Gen. Physiol. 124:43-57
    • (2004) J. Gen. Physiol. , vol.124 , pp. 43-57
    • Li, W.1    Aldrich, R.W.2
  • 38
    • 0037324895 scopus 로고    scopus 로고
    • Gating mechanism of BK (Slo1) channels: so near, yet so far
    • Magleby, K.L. 2003. Gating mechanism of BK (Slo1) channels: so near, yet so far. J. Gen. Physiol. 121:81-96
    • (2003) J. Gen. Physiol. , vol.121 , pp. 81-96
    • Magleby, K.L.1
  • 39
    • 75649097134 scopus 로고    scopus 로고
    • Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales
    • Mant, C.T., J.M. Kovacs, H.M. Kim, D.D. Pollock, and R.S. Hodges. 2009. Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales. Biopolymers. 92:573-595
    • (2009) Biopolymers , vol.92 , pp. 573-595
    • Mant, C.T.1    Kovacs, J.M.2    Kim, H.M.3    Pollock, D.D.4    Hodges, R.S.5
  • 40
    • 0019827872 scopus 로고
    • Ca-dependent K channels with large unitary conductance in chromaffin cell membranes
    • Marty, A. 1981. Ca-dependent K channels with large unitary conductance in chromaffin cell membranes. Nature. 291:497-500
    • (1981) Nature , vol.291 , pp. 497-500
    • Marty, A.1
  • 41
    • 0031457570 scopus 로고    scopus 로고
    • + channel, a distinct member of voltage-dependent ion channels with seven N-terminaltransmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus
    • + channel, a distinct member of voltage-dependent ion channels with seven N-terminaltransmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus. Proc. Natl. Acad. Sci. USA. 94:14066-14071
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 14066-14071
    • Meera, P.1    Wallner, M.2    Song, M.3    Toro, L.4
  • 42
    • 0043074453 scopus 로고    scopus 로고
    • Electrostatic tuning of ion conductance in potassium channels
    • Nimigean, C.M., J.S. Chappie, and C. Miller. 2003. Electrostatic tuning of ion conductance in potassium channels. Biochemistry. 42:9263-9268
    • (2003) Biochemistry , vol.42 , pp. 9263-9268
    • Nimigean, C.M.1    Chappie, J.S.2    Miller, C.3
  • 43
    • 0027956518 scopus 로고
    • Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke
    • Pallanck, L., and B. Ganetzky. 1994. Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke. Hum. Mol. Genet. 3:1239-1243
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1239-1243
    • Pallanck, L.1    Ganetzky, B.2
  • 45
    • 0027365126 scopus 로고
    • Functional colocalization of calcium and calcium-gated potassium channels in control of transmitter release
    • Robitaille, R., M.L. Garcia, G.J. Kaczorowski, and M.P. Charlton. 1993. Functional colocalization of calcium and calcium-gated potassium channels in control of transmitter release. Neuron. 11:645-655
    • (1993) Neuron , vol.11 , pp. 645-655
    • Robitaille, R.1    Garcia, M.L.2    Kaczorowski, G.J.3    Charlton, M.P.4
  • 49
    • 70249124205 scopus 로고    scopus 로고
    • Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
    • Wang, L., and F.J. Sigworth. 2009. Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature. 461:292-295
    • (2009) Nature , vol.461 , pp. 292-295
    • Wang, L.1    Sigworth, F.J.2
  • 53
    • 64549088411 scopus 로고    scopus 로고
    • N-terminal inactivation domains of ? subunits are protected from trypsin digestion by binding within the antechamber of BK channels
    • Zhang, Z., X.H. Zeng, X.M. Xia, and C.J. Lingle. 2009. N-terminal inactivation domains of ? subunits are protected from trypsin digestion by binding within the antechamber of BK channels. J. Gen. Physiol. 133:263-282
    • (2009) J. Gen. Physiol. , vol.133 , pp. 263-282
    • Zhang, Z.1    Zeng, X.H.2    Xia, X.M.3    Lingle, C.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.