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Volumn 73, Issue 4, 1997, Pages 1885-1895

Interaction between the sodium channel inactivation linker and domain III S4-S5

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; DOCKING PROTEIN; LINK PROTEIN; SODIUM CHANNEL; SODIUM ION;

EID: 0030855929     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78219-5     Document Type: Article
Times cited : (151)

References (36)
  • 1
    • 0021086246 scopus 로고
    • A reinterpretation of mammalian sodium channel gating based on single channel recording
    • Aldrich, R. W., D. P. Corey, and C. F. Stevens. 1983. A reinterpretation of mammalian sodium channel gating based on single channel recording. Nature. 306:436-441.
    • (1983) Nature , vol.306 , pp. 436-441
    • Aldrich, R.W.1    Corey, D.P.2    Stevens, C.F.3
  • 2
    • 0017743723 scopus 로고
    • Inactivation of the sodium channel. II. Gating current experiments
    • Armstrong, C. M., and F. Bezanilla. 1977. Inactivation of the sodium channel. II. Gating current experiments. J. Gen. Physiol. 70:567-590.
    • (1977) J. Gen. Physiol. , vol.70 , pp. 567-590
    • Armstrong, C.M.1    Bezanilla, F.2
  • 3
    • 0025044555 scopus 로고
    • A neutral amino acid change in segment IIS4 dramatically alters the gating properties of the voltage-dependent sodium channel
    • Auld, V. J., A. L. Goldin, D. S. Krafte, W. A. Catterall, H. A. Lester, N. Davidson, and R. J. Dunn. 1990. A neutral amino acid change in segment IIS4 dramatically alters the gating properties of the voltage-dependent sodium channel. Proc. Natl. Acad. Sci. USA. 87:323-327.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 323-327
    • Auld, V.J.1    Goldin, A.L.2    Krafte, D.S.3    Catterall, W.A.4    Lester, H.A.5    Davidson, N.6    Dunn, R.J.7
  • 4
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    • Carter, P. J., G. Winter, A. J. Wilkinson, and A. R. Fersht. 1984. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell. 38: 835-840.
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 5
    • 0026490286 scopus 로고
    • Cellular and molecular biology of voltage-gated sodium channels
    • Catterall, W. A. 1992. Cellular and molecular biology of voltage-gated sodium channels. Physiol. Rev. 72:S15-S48.
    • (1992) Physiol. Rev. , vol.72
    • Catterall, W.A.1
  • 6
    • 0030453610 scopus 로고    scopus 로고
    • A unique role for the S4 segment of domain 4 in the inactivation of sodium channels
    • Chen, L.-Q., V. Santarelli, R. Horn, and R. Kallen. 1996. A unique role for the S4 segment of domain 4 in the inactivation of sodium channels. J. Gen. Physiol. 108:549-556.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 549-556
    • Chen, L.-Q.1    Santarelli, V.2    Horn, R.3    Kallen, R.4
  • 7
    • 0028363484 scopus 로고
    • Restoration of inactivation and block of open sodium channels by an inactivation gate peptide
    • Eaholtz, G., T. Scheuer, and W. A. Catterall. 1994. Restoration of inactivation and block of open sodium channels by an inactivation gate peptide. Neuron. 12:1041-1048.
    • (1994) Neuron , vol.12 , pp. 1041-1048
    • Eaholtz, G.1    Scheuer, T.2    Catterall, W.A.3
  • 8
    • 0026298725 scopus 로고
    • Expression of ion channels by injection of mRNA into Xenopus oocytes
    • Goldin, A. L. 1991. Expression of ion channels by injection of mRNA into Xenopus oocytes. Methods Cell Biol. 36:487-509.
    • (1991) Methods Cell Biol. , vol.36 , pp. 487-509
    • Goldin, A.L.1
  • 9
    • 0002785854 scopus 로고
    • Voltage-gated sodium channels
    • R. A. North, editor. CRC Press, Boca Raton, FL
    • Goldin, A. L. 1995. Voltage-gated sodium channels. In Ligand- and Voltage-Gated Ion Channels. R. A. North, editor. CRC Press, Boca Raton, FL. 73-112.
    • (1995) Ligand- and Voltage-Gated Ion Channels , pp. 73-112
    • Goldin, A.L.1
  • 10
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., W. N. Zagotta, and R. W. Aldrich. 1990. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 16
    • 0027413853 scopus 로고
    • Site-directed mutagenesis of the putative pore region of the rat IIA sodium channel
    • Kontis, K. J., and A. L. Goldin. 1993. Site-directed mutagenesis of the putative pore region of the rat IIA sodium channel. Mol. Pharmacol. 43:635-644.
    • (1993) Mol. Pharmacol. , vol.43 , pp. 635-644
    • Kontis, K.J.1    Goldin, A.L.2
  • 17
    • 0028258554 scopus 로고
    • + channels must deactivate to recover from inactivation
    • + channels must deactivate to recover from inactivation. Neuron. 12:819-829.
    • (1994) Neuron , vol.12 , pp. 819-829
    • Kuo, C.-C.1    Bean, B.P.2
  • 20
    • 0029044707 scopus 로고
    • A critical role for transmembrane segment IVS6 of the sodium channel α subunit in fast inactivation
    • McPhee, J. C., D. S. Ragsdale, T. Scheuer, and W. A. Catterall. 1995. A critical role for transmembrane segment IVS6 of the sodium channel α subunit in fast inactivation. J. Biol. Chem. 270:12025-12034.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12025-12034
    • McPhee, J.C.1    Ragsdale, D.S.2    Scheuer, T.3    Catterall, W.A.4
  • 21
    • 0025226105 scopus 로고
    • Changes in sodium channel gating produced by point mutations in a cytoplasmic linker
    • Moorman, J. R., G. E. Kirsch, A. M. Brown, and R. H. Joho. 1990. Changes in sodium channel gating produced by point mutations in a cytoplasmic linker. Science. 250:688-691.
    • (1990) Science , vol.250 , pp. 688-691
    • Moorman, J.R.1    Kirsch, G.E.2    Brown, A.M.3    Joho, R.H.4
  • 22
    • 0027724707 scopus 로고
    • Interactions of amino terminal domains of Shaker K channels with a pore blocking site studied with synthetic peptides
    • Murrell-Lagnado, R. D., and R. W. Aldrich. 1993a. Interactions of amino terminal domains of Shaker K channels with a pore blocking site studied with synthetic peptides. J. Gen. Physiol. 102:949-975.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 949-975
    • Murrell-Lagnado, R.D.1    Aldrich, R.W.2
  • 23
    • 0027753950 scopus 로고
    • Energetics of Shaker K channels block by inactivation peptides
    • Murrell-Lagnado, R. D., and R. W. Aldrich. 1993b. Energetics of Shaker K channels block by inactivation peptides. J. Gen. Physiol. 102: 977-1003.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 977-1003
    • Murrell-Lagnado, R.D.1    Aldrich, R.W.2
  • 24
    • 0026055174 scopus 로고
    • A voltage-dependent gating transition induces use-dependent block by tetrodotoxin of rat IIA sodium channels expressed in Xenopus oocytes
    • Patton, D. E., and A. L. Goldin. 1991. A voltage-dependent gating transition induces use-dependent block by tetrodotoxin of rat IIA sodium channels expressed in Xenopus oocytes. Neuron. 7:637-647.
    • (1991) Neuron , vol.7 , pp. 637-647
    • Patton, D.E.1    Goldin, A.L.2
  • 25
    • 0026439086 scopus 로고
    • Amino acid residues required for fast sodium channel inactivation. Charge neutralizations and deletions in the III-IV linker
    • Patton, D. E., J. W. West, W. A. Catterall, and A. L. Goldin. 1992. Amino acid residues required for fast sodium channel inactivation. Charge neutralizations and deletions in the III-IV linker. Proc. Natl. Acad. Sci. USA. 89:10905-10909.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10905-10909
    • Patton, D.E.1    West, J.W.2    Catterall, W.A.3    Goldin, A.L.4
  • 26
    • 0027379450 scopus 로고
    • A peptide segment critical for sodium channel inactivation functions as an inactivation gate in a potassium channel
    • Patton, D. E., J. W. West, W. A. Catterall, and A. L. Goldin. 1993. A peptide segment critical for sodium channel inactivation functions as an inactivation gate in a potassium channel. Neuron. 11:967-974.
    • (1993) Neuron , vol.11 , pp. 967-974
    • Patton, D.E.1    West, J.W.2    Catterall, W.A.3    Goldin, A.L.4
  • 28
    • 0029963312 scopus 로고    scopus 로고
    • Phosphorylation of brain sodium channels in the I-II linker modulates channel function in Xenopus oocytes
    • Smith, R. D., and A. L. Goldin. 1996. Phosphorylation of brain sodium channels in the I-II linker modulates channel function in Xenopus oocytes. J. Neurosci. 16:1965-1974.
    • (1996) J. Neurosci. , vol.16 , pp. 1965-1974
    • Smith, R.D.1    Goldin, A.L.2
  • 29
    • 0024368695 scopus 로고
    • Structural parts involved in activation and inactivation of the sodium channel
    • Stühmer, W., F. Conti, H. Suzuki, X. Wang, M. Noda, N. Yahagi, H. Kubo, and S. Numa. 1989. Structural parts involved in activation and inactivation of the sodium channel. Nature. 339:597-603.
    • (1989) Nature , vol.339 , pp. 597-603
    • Stühmer, W.1    Conti, F.2    Suzuki, H.3    Wang, X.4    Noda, M.5    Yahagi, N.6    Kubo, H.7    Numa, S.8
  • 30
    • 0029814358 scopus 로고    scopus 로고
    • Role of an S4-S5 linker in sodium channel inactivation probed by mutagenesis and a peptide blocker
    • Tang, L., R. G. Kallen, and R. Horn. 1996. Role of an S4-S5 linker in sodium channel inactivation probed by mutagenesis and a peptide blocker. J. Gen. Physiol. 108:89-104.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 89-104
    • Tang, L.1    Kallen, R.G.2    Horn, R.3
  • 31
    • 0008453646 scopus 로고
    • Inhibition of inactivation of single sodium channels by a site-directed antibody
    • Vassilev, P., T. Scheuer, and W. A. Catterall. 1989. Inhibition of inactivation of single sodium channels by a site-directed antibody. Proc. Natl. Acad. Sci. USA. 86:8147-8151.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8147-8151
    • Vassilev, P.1    Scheuer, T.2    Catterall, W.A.3
  • 35
    • 0028589331 scopus 로고
    • Sodium channel mutations in paramyotonia congenita exhibit similar biophysical phenotypes in vitro
    • Yang, N., S. Ji, M. Zhou, L. J. Ptacek, R. L. Barchi, R. Horn, and A. L. George, Jr. 1994. Sodium channel mutations in paramyotonia congenita exhibit similar biophysical phenotypes in vitro. Proc. Natl. Acad. Sci. USA. 91:12785-12789.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12785-12789
    • Yang, N.1    Ji, S.2    Zhou, M.3    Ptacek, L.J.4    Barchi, R.L.5    Horn, R.6    George A.L., Jr.7
  • 36
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta, W. N., T. Hoshi, and R. W. Aldrich. 1990. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science. 250:568-571.
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.