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Volumn 73, Issue 3, 1997, Pages 1355-1363

A novel calcium-sensing domain in the BK channel

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL;

EID: 0030852701     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78168-2     Document Type: Article
Times cited : (356)

References (53)
  • 2
    • 0026413976 scopus 로고
    • A component of calcium-activated potassium channels encoded by the Drosophila slo locus
    • Atkinson, N. S., G. A. Robertson, and B. Ganetzky. 1991. A component of calcium-activated potassium channels encoded by the Drosophila slo locus. Science. 253:551-555.
    • (1991) Science , vol.253 , pp. 551-555
    • Atkinson, N.S.1    Robertson, G.A.2    Ganetzky, B.3
  • 3
    • 0024959484 scopus 로고
    • Long-range structural changes in proteinase K triggered by calcium ion removal
    • Bajorath, J., S. Raghunathan, W. Hinrichs, and W. Saenger. 1989. Long-range structural changes in proteinase K triggered by calcium ion removal. Nature. 337:481-484.
    • (1989) Nature , vol.337 , pp. 481-484
    • Bajorath, J.1    Raghunathan, S.2    Hinrichs, W.3    Saenger, W.4
  • 4
    • 0020000206 scopus 로고
    • Properties of single calcium-activated potassium channels in cultured rat muscle
    • Barrett, J. N., K. Magleby, and B. S. Pallotta. 1982. Properties of single calcium-activated potassium channels in cultured rat muscle. J. Physiol. (Lond.). 331:211-230.
    • (1982) J. Physiol. (Lond.) , vol.331 , pp. 211-230
    • Barrett, J.N.1    Magleby, K.2    Pallotta, B.S.3
  • 5
    • 0000418311 scopus 로고
    • Calcium-activated potassium channels
    • Blatz, A. L., and K. L. Magleby. 1987. Calcium-activated potassium channels. Trends Neurosci. 10:463-467.
    • (1987) Trends Neurosci. , vol.10 , pp. 463-467
    • Blatz, A.L.1    Magleby, K.L.2
  • 6
    • 0026575435 scopus 로고
    • Regulation of arterial tone by activation of calcium-dependent potassium channels
    • Brayden, J. E., and M. T. Nelson. 1992. Regulation of arterial tone by activation of calcium-dependent potassium channels. Science. 256: 532-535.
    • (1992) Science , vol.256 , pp. 532-535
    • Brayden, J.E.1    Nelson, M.T.2
  • 7
    • 0002818018 scopus 로고
    • Calcium binding by thermitase
    • Briedigkeit, L., and C. Frommel. 1989. Calcium binding by thermitase. FEBS Lett. 253:83-87.
    • (1989) FEBS Lett. , vol.253 , pp. 83-87
    • Briedigkeit, L.1    Frommel, C.2
  • 8
    • 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
  • 10
    • 0028126679 scopus 로고
    • Cloning and expression of a human large-conductance calcium-activated potassium channel
    • Dworetzky, S. I., J. T. Trojnack, and V. K. Gribkoff. 1994. Cloning and expression of a human large-conductance calcium-activated potassium channel. Brain Res. Mol. Brain Res. 27:189-193.
    • (1994) Brain Res. Mol. Brain Res. , vol.27 , pp. 189-193
    • Dworetzky, S.I.1    Trojnack, J.T.2    Gribkoff, V.K.3
  • 11
    • 0026905554 scopus 로고
    • Development of frequency tuning in the auditory periphery
    • Fuchs, P. A. 1992. Development of frequency tuning in the auditory periphery. Curr. Opin. Neurobiol. 2:457-461.
    • (1992) Curr. Opin. Neurobiol. , vol.2 , pp. 457-461
    • Fuchs, P.A.1
  • 15
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., H. Hunt, S. N. Ho, J. K. Pullen, and L. R. Pease. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene. 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0028136565 scopus 로고
    • Subunit composition of the high-conductance calcium-activated potassium channel from smooth muscle, a representative of the mSlo and slowpoke family of potassium channels
    • Knaus, H. G., M. Garcia-Calvo, G. J. Kaczorowski, and M. L. Garcia. 1994. Subunit composition of the high-conductance calcium-activated potassium channel from smooth muscle, a representative of the mSlo and slowpoke family of potassium channels. J. Biol. Chem. 269:3921-3924.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3921-3924
    • Knaus, H.G.1    Garcia-Calvo, M.2    Kaczorowski, G.J.3    Garcia, M.L.4
  • 18
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 19
    • 0020973066 scopus 로고
    • Calcium dependence of open and shut interval distributions from calcium-activated potassium channels in cultured rat muscle
    • Magleby, K. L., and B. S. Pallotta. 1983. Calcium dependence of open and shut interval distributions from calcium-activated potassium channels in cultured rat muscle. J. Physiol. (Lond.). 344:585-604.
    • (1983) J. Physiol. (Lond.) , vol.344 , pp. 585-604
    • Magleby, K.L.1    Pallotta, B.S.2
  • 21
    • 0019827872 scopus 로고
    • + channels with large unitary conductance in chromaffin cell membranes
    • + channels with large unitary conductance in chromaffin cell membranes. Nature. 231:497-500.
    • (1981) Nature , vol.231 , pp. 497-500
    • Marty, A.1
  • 23
    • 0025864473 scopus 로고
    • Calcium-activated potassium channels: Regulation by calcium
    • McManus, O. B. 1991. Calcium-activated potassium channels: regulation by calcium. J. Bioenerg. Biomembr. 23:537-560.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 537-560
    • McManus, O.B.1
  • 24
    • 0023734971 scopus 로고
    • Kinetic states and modes of single large-conductance calcium-activated potassium channels in cultured rat muscle
    • McManus, O. B., and K. L. Magleby. 1988. Kinetic states and modes of single large-conductance calcium-activated potassium channels in cultured rat muscle. J. Physiol. (Lond.). 402:79-120.
    • (1988) J. Physiol. (Lond.) , vol.402 , pp. 79-120
    • McManus, O.B.1    Magleby, K.L.2
  • 27
    • 0026409654 scopus 로고
    • Calcium-binding sites in proteins: A structural perspective
    • McPhalen, C. A., N. C. J. Strynadka, and M. N. G. James. 1991. Calcium-binding sites in proteins: a structural perspective. Adv. Protein Chem. 42:77-144.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 77-144
    • McPhalen, C.A.1    Strynadka, N.C.J.2    James, M.N.G.3
  • 28
    • 0021770917 scopus 로고
    • Efficient in vitro synthesis of biologically active RNA and DNA hybridization probes from plasmids containing a bacteriophage SP promoter
    • Melton, D., P. Krieg, M. Rebagliati, T. Maniatis, K. Zinn, and M. Green. 1984. Efficient in vitro synthesis of biologically active RNA and DNA hybridization probes from plasmids containing a bacteriophage SP promoter. Nucleic Acids Res. 12:7035-7056.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7035-7056
    • Melton, D.1    Krieg, P.2    Rebagliati, M.3    Maniatis, T.4    Zinn, K.5    Green, M.6
  • 30
    • 0020643557 scopus 로고
    • + channels from rat muscle incorporated into planar lipid bilayers
    • + channels from rat muscle incorporated into planar lipid bilayers. J. Gen. Physiol. 82:511-543.
    • (1983) J. Gen. Physiol. , vol.82 , pp. 511-543
    • Moczydlowski, E.1    Latorre, R.2
  • 31
    • 0030466438 scopus 로고    scopus 로고
    • Hypothesis for a serine protease-like domain at the C-terminus of slowpoke calcium-activated potassium channels
    • Moss, G. W. J., J. Marshall, and E. Moczydlowski. 1996a. Hypothesis for a serine protease-like domain at the C-terminus of slowpoke calcium-activated potassium channels. J. Gen. Physiol. 108:473-484.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 473-484
    • Moss, G.W.J.1    Marshall, J.2    Moczydlowski, E.3
  • 32
    • 0030299989 scopus 로고    scopus 로고
    • An evolutionarily conserved binding site for serine protease inhibitors in large conductance calcium-activated potassium channels
    • Moss, G. W. J., J. Marshall, M. Morabito, J. R. Howe, and E. Moczydlowski. 1996b. An evolutionarily conserved binding site for serine protease inhibitors in large conductance calcium-activated potassium channels. Biochemistry. 35:16024-16035.
    • (1996) Biochemistry , vol.35 , pp. 16024-16035
    • Moss, G.W.J.1    Marshall, J.2    Morabito, M.3    Howe, J.R.4    Moczydlowski, E.5
  • 34
    • 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
  • 36
    • 0026032209 scopus 로고
    • Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence
    • Papazian, D. M., L. C. Timpe, Y. N. Jan, and L. Y. Jan. 1991. Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence. Nature. 349:305-310.
    • (1991) Nature , vol.349 , pp. 305-310
    • Papazian, D.M.1    Timpe, L.C.2    Jan, Y.N.3    Jan, L.Y.4
  • 37
    • 0004148869 scopus 로고
    • Cornell University Press, Ithaca, NY
    • Pauling, L. 1967. The Chemical Bond. Cornell University Press, Ithaca, NY.
    • (1967) The Chemical Bond
    • Pauling, L.1
  • 38
    • 0028178457 scopus 로고
    • Reconstitution of expressed KCa channels from Xenopus oocytes to lipid bilayers
    • Perez, G., A. Lagrutta, J. P. Adelman, and L. Toro. 1994. Reconstitution of expressed KCa channels from Xenopus oocytes to lipid bilayers. Biophys. J. 66:1022-1027.
    • (1994) Biophys. J. , vol.66 , pp. 1022-1027
    • Perez, G.1    Lagrutta, A.2    Adelman, J.P.3    Toro, L.4
  • 39
    • 0027537139 scopus 로고
    • Characterization of large-conductance, calcium-activated potassium channels from human myometrium
    • Perez, G. J., L. Toro, S. D. Erulkar, and E. Stefani. 1993. Characterization of large-conductance, calcium-activated potassium channels from human myometrium. Am. J. Obstet. Gynecol. 168:652-660.
    • (1993) Am. J. Obstet. Gynecol. , vol.168 , pp. 652-660
    • Perez, G.J.1    Toro, L.2    Erulkar, S.D.3    Stefani, E.4
  • 41
    • 0021269612 scopus 로고
    • Calcium-activated potassium channels and their role in secretion
    • Petersen, O. H., and Y. Maruyama. 1984. Calcium-activated potassium channels and their role in secretion. Nature. 307:693-696.
    • (1984) Nature , vol.307 , pp. 693-696
    • Petersen, O.H.1    Maruyama, Y.2
  • 42
    • 0024401693 scopus 로고
    • A family of calcium-dependent potassium channels from rat brain
    • Reinhart, P. H., S. Chung, and I. B. Levitan. 1989. A family of calcium-dependent potassium channels from rat brain. Neuron. 2:1031-1041.
    • (1989) Neuron , vol.2 , pp. 1031-1041
    • Reinhart, P.H.1    Chung, S.2    Levitan, I.B.3
  • 43
    • 0026596694 scopus 로고
    • Presynaptic calcium signals and transmitter release are modulated by calcium-activated potassium channels
    • Robitaille, R., and M. P. Charlton. 1992. Presynaptic calcium signals and transmitter release are modulated by calcium-activated potassium channels. J. Neurosci. 12:297-305.
    • (1992) J. Neurosci. , vol.12 , pp. 297-305
    • Robitaille, R.1    Charlton, M.P.2
  • 44
    • 0342456714 scopus 로고    scopus 로고
    • Gating of BK channels can be independent of calcium or voltage
    • Rothberg, B. S., and K. Magleby. 1996. Gating of BK channels can be independent of calcium or voltage. Soc. Neurosci. Abstr. 22:1443.
    • (1996) Soc. Neurosci. Abstr. , vol.22 , pp. 1443
    • Rothberg, B.S.1    Magleby, K.2
  • 46
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka, N. C. J., and M. N. G. James. 1989. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 59: 951-998.
    • (1989) Annu. Rev. Biochem. , vol.59 , pp. 951-998
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 47
    • 0024382461 scopus 로고
    • + channel in rat pancreatic islet B cells: Permeation, gating, and blockade by cations
    • + channel in rat pancreatic islet B cells: permeation, gating, and blockade by cations. Biochim. Biophys. Acta. 982:62-72.
    • (1989) Biochim. Biophys. Acta. , vol.982 , pp. 62-72
    • Tabcharani, J.A.1    Misler, S.2
  • 50
    • 0029861307 scopus 로고    scopus 로고
    • Conserved classes of potassium channel genes identified from the Caenorhabditis elegans genome
    • Wei, A., T. Jegla, and L. Salkoff. 1996. Conserved classes of potassium channel genes identified from the Caenorhabditis elegans genome. Neuropharmacology. 35:805-829.
    • (1996) Neuropharmacology , vol.35 , pp. 805-829
    • Wei, A.1    Jegla, T.2    Salkoff, L.3
  • 52
    • 0029108205 scopus 로고
    • A kinetic description of the calcium-activated potassium channel and its application to electrical tuning of hair cells
    • Wu, Y. C., J. J. Art, M. R. Goodman, and R. Fettiplace. 1995. A kinetic description of the calcium-activated potassium channel and its application to electrical tuning of hair cells. Prog. Biophys. Mol. Biol. 63: 131-158.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 131-158
    • Wu, Y.C.1    Art, J.J.2    Goodman, M.R.3    Fettiplace, R.4
  • 53
    • 0026058182 scopus 로고
    • + channel by mutation of the H5 region
    • + channel by mutation of the H5 region. Nature. 349:700-704.
    • (1991) Nature , vol.349 , pp. 700-704
    • Yool, A.J.1    Schwarz, T.L.2


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