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Volumn 99, Issue 1, 2014, Pages 35-51

Structure and function of voltage-gated sodium channels at atomic resolution

Author keywords

[No Author keywords available]

Indexed keywords

SODIUM; SODIUM CHANNEL; VOLTAGE GATED SODIUM CHANNEL;

EID: 84892438148     PISSN: 09580670     EISSN: 1469445X     Source Type: Journal    
DOI: 10.1113/expphysiol.2013.071969     Document Type: Article
Times cited : (165)

References (109)
  • 1
    • 0014608851 scopus 로고
    • The effects of external potassium and long duration voltage conditioning on the amplitude of sodium currents in the giant axon of the squid, Loligo pealei
    • Adelman WJ Jr & Palti Y (1969). The effects of external potassium and long duration voltage conditioning on the amplitude of sodium currents in the giant axon of the squid, Loligo pealei. J Gen Physiol 54, 589-606.
    • (1969) J Gen Physiol , vol.54 , pp. 589-606
    • Adelman Jr., W.J.1    Palti, Y.2
  • 2
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axon
    • Armstrong CM (1971). Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axon. J Gen Physiol 58, 413-437.
    • (1971) J Gen Physiol , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 3
    • 0019596088 scopus 로고
    • Sodium channels and gating currents
    • Armstrong CM (1981). Sodium channels and gating currents. Physiol Rev 61, 644-682.
    • (1981) Physiol Rev , vol.61 , pp. 644-682
    • Armstrong, C.M.1
  • 4
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • Armstrong CM & Bezanilla F (1973). Currents related to movement of the gating particles of the sodium channels. Nature 242, 459-461.
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 5
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • Armstrong CM & Benzanilla F (1974). Charge movement associated with the opening and closing of the activation gates of the Na channels. J Gen Physiol 63, 533-552.
    • (1974) J Gen Physiol , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Benzanilla, F.2
  • 6
    • 0017743723 scopus 로고
    • Inactivation of the sodium channel. II. Gating current experiments
    • Armstrong CM & Bezanilla F (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
  • 7
    • 0015902531 scopus 로고
    • Destruction of sodium conductance inactivation in squid axons perfused with pronase
    • Armstrong CM, Bezanilla F & Rojas E (1973). Destruction of sodium conductance inactivation in squid axons perfused with pronase. J Gen Physiol 62, 375-391.
    • (1973) J Gen Physiol , vol.62 , pp. 375-391
    • Armstrong, C.M.1    Bezanilla, F.2    Rojas, E.3
  • 9
    • 0005769753 scopus 로고
    • Covalent labeling of protein components of the sodium channel with a photoactivable derivative of scorpion toxin
    • Beneski DA & Catterall WA (1980). Covalent labeling of protein components of the sodium channel with a photoactivable derivative of scorpion toxin. Proc Natl Acad Sci U S A 77, 639-643.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 639-643
    • Beneski, D.A.1    Catterall, W.A.2
  • 10
    • 0017697163 scopus 로고
    • Inactivation of the sodium channel. I. Sodium current experiments
    • Bezanilla F & Armstrong CM (1977). Inactivation of the sodium channel. I. Sodium current experiments. J Gen Physiol 70, 549-566.
    • (1977) J Gen Physiol , vol.70 , pp. 549-566
    • Bezanilla, F.1    Armstrong, C.M.2
  • 11
    • 84857211318 scopus 로고    scopus 로고
    • Na channel β subunits: overachievers of the ion channel family
    • Brackenbury WJ & Isom LL (2011). Na channel β subunits: overachievers of the ion channel family. Front Pharmacol 2, 53.
    • (2011) Front Pharmacol , vol.2 , pp. 53
    • Brackenbury, W.J.1    Isom, L.L.2
  • 12
    • 50849086415 scopus 로고    scopus 로고
    • Large-scale movement within the voltage-sensor paddle of a potassium channel-support for a helical-screw motion
    • Broomand A & Elinder F (2008). Large-scale movement within the voltage-sensor paddle of a potassium channel-support for a helical-screw motion. Neuron 59, 770-777.
    • (2008) Neuron , vol.59 , pp. 770-777
    • Broomand, A.1    Elinder, F.2
  • 13
    • 34249946312 scopus 로고    scopus 로고
    • Two atomic constraints unambiguously position the S4 segment relative to S1 and S2 segments in the closed state of Shaker K channel
    • Campos FV, Chanda B, Roux B & Bezanilla F (2007). Two atomic constraints unambiguously position the S4 segment relative to S1 and S2 segments in the closed state of Shaker K channel. Proc Natl Acad Sci U S A 104, 7904-7909.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7904-7909
    • Campos, F.V.1    Chanda, B.2    Roux, B.3    Bezanilla, F.4
  • 14
    • 84883277214 scopus 로고    scopus 로고
    • Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels
    • Capes DL, Goldschen-Ohm MP, Arcisio-Miranda M, Bezanilla F & Chanda B (2013). Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels. J Gen Physiol 142, 101-112.
    • (2013) J Gen Physiol , vol.142 , pp. 101-112
    • Capes, D.L.1    Goldschen-Ohm, M.P.2    Arcisio-Miranda, M.3    Bezanilla, F.4    Chanda, B.5
  • 15
    • 0018582440 scopus 로고
    • Binding of scorpion toxin to receptor sites associated with sodium channels in frog muscle. Correlation of voltage-dependent binding with activation
    • Catterall WA (1979). Binding of scorpion toxin to receptor sites associated with sodium channels in frog muscle. Correlation of voltage-dependent binding with activation. J Gen Physiol 74, 375-391.
    • (1979) J Gen Physiol , vol.74 , pp. 375-391
    • Catterall, W.A.1
  • 16
    • 0018873513 scopus 로고
    • Neurotoxins that act on voltage-sensitive sodium channels in excitable membranes
    • Catterall WA (1980). Neurotoxins that act on voltage-sensitive sodium channels in excitable membranes. Annu Rev Pharmacol Toxicol 20, 15-43.
    • (1980) Annu Rev Pharmacol Toxicol , vol.20 , pp. 15-43
    • Catterall, W.A.1
  • 17
    • 0022555877 scopus 로고
    • Molecular properties of voltage-sensitive sodium channels
    • Catterall WA (1986a). Molecular properties of voltage-sensitive sodium channels. Annu Rev Biochem 55, 953-985.
    • (1986) Annu Rev Biochem , vol.55 , pp. 953-985
    • Catterall, W.A.1
  • 18
    • 0022658001 scopus 로고
    • Voltage-dependent gating of sodium channels: correlating structure and function
    • Catterall WA (1986b). Voltage-dependent gating of sodium channels: correlating structure and function. Trends Neurosci 9, 7-10.
    • (1986) Trends Neurosci , vol.9 , pp. 7-10
    • Catterall, W.A.1
  • 19
    • 0033694833 scopus 로고    scopus 로고
    • From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels
    • Catterall WA (2000). From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels. Neuron 26, 13-25.
    • (2000) Neuron , vol.26 , pp. 13-25
    • Catterall, W.A.1
  • 20
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: structure, function, and pathophysiology
    • Catterall WA (2010). Ion channel voltage sensors: structure, function, and pathophysiology. Neuron 67, 915-928.
    • (2010) Neuron , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 22
    • 0032191111 scopus 로고    scopus 로고
    • Voltage sensor-trapping: enhanced activation of sodium channels by β-scorpion toxin bound to the S3-S4 loop in domain II
    • Cestèle S, Qu Y, Rogers JC, Rochat H, Scheuer T & Catterall WA (1998). Voltage sensor-trapping: enhanced activation of sodium channels by β-scorpion toxin bound to the S3-S4 loop in domain II. Neuron 21, 919-931.
    • (1998) Neuron , vol.21 , pp. 919-931
    • Cestèle, S.1    Qu, Y.2    Rogers, J.C.3    Rochat, H.4    Scheuer, T.5    Catterall, W.A.6
  • 23
    • 33746369777 scopus 로고    scopus 로고
    • Structure and function of the voltage sensor of sodium channels probed by a β-scorpion toxin
    • Cestèle S, Yarov-Yarovoy V, Qu Y, Sampieri F, Scheuer T & Catterall WA (2006). Structure and function of the voltage sensor of sodium channels probed by a β-scorpion toxin. J Biol Chem 281, 21332-21344.
    • (2006) J Biol Chem , vol.281 , pp. 21332-21344
    • Cestèle, S.1    Yarov-Yarovoy, V.2    Qu, Y.3    Sampieri, F.4    Scheuer, T.5    Catterall, W.A.6
  • 25
    • 23844459909 scopus 로고    scopus 로고
    • Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement
    • Chanda B, Asamoah OK, Blunck R, Roux B & Bezanilla F (2005). Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement. Nature 436, 852-856.
    • (2005) Nature , vol.436 , pp. 852-856
    • Chanda, B.1    Asamoah, O.K.2    Blunck, R.3    Roux, B.4    Bezanilla, F.5
  • 26
    • 0036846886 scopus 로고    scopus 로고
    • Tracking voltage-dependent conformational changes in skeletal muscle sodium channel during activation
    • Chanda B & Bezanilla F (2002). Tracking voltage-dependent conformational changes in skeletal muscle sodium channel during activation. J Gen Physiol 120, 629-645.
    • (2002) J Gen Physiol , vol.120 , pp. 629-645
    • Chanda, B.1    Bezanilla, F.2
  • 30
    • 54449100445 scopus 로고    scopus 로고
    • Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation
    • DeCaen PG, Yarov-Yarovoy V, Zhao Y, Scheuer T & Catterall WA (2008). Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation. Proc Natl Acad Sci U S A 105, 15142-15147.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15142-15147
    • DeCaen, P.G.1    Yarov-Yarovoy, V.2    Zhao, Y.3    Scheuer, T.4    Catterall, W.A.5
  • 31
    • 84892441461 scopus 로고    scopus 로고
    • The mechanism of voltage dependent gating of he NaChBac prokaryotic sodium channel
    • University of Washington, Seattle, WA.
    • DeCaen PG (2010). The mechanism of voltage dependent gating of he NaChBac prokaryotic sodium channel. Unpublished doctoral dissertation. University of Washington, Seattle, WA.
    • (2010) Unpublished doctoral dissertation
    • DeCaen, P.G.1
  • 32
    • 0028363484 scopus 로고
    • Restoration of inactivation and block of open sodium channels by an inactivation gate peptide
    • Eaholtz G, Scheuer T & Catterall WA (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
  • 35
    • 0000882125 scopus 로고
    • Molecular model of the action potential sodium channel
    • Guy HR & Seetharamulu P (1986). Molecular model of the action potential sodium channel. Proc Natl Acad Sci U S A 508, 508-512.
    • (1986) Proc Natl Acad Sci U S A , vol.508 , pp. 508-512
    • Guy, H.R.1    Seetharamulu, P.2
  • 36
    • 0012616825 scopus 로고
    • Purification of the saxitoxin receptor of the sodium channel from rat brain
    • Hartshorne RP & Catterall WA (1981). Purification of the saxitoxin receptor of the sodium channel from rat brain. Proc Natl Acad Sci U S A 78, 4620-4624.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 4620-4624
    • Hartshorne, R.P.1    Catterall, W.A.2
  • 37
    • 0021360647 scopus 로고
    • The sodium channel from rat brain. Purification and subunit composition
    • Hartshorne RP & Catterall WA (1984). The sodium channel from rat brain. Purification and subunit composition. J Biol Chem 259, 1667-1675.
    • (1984) J Biol Chem , vol.259 , pp. 1667-1675
    • Hartshorne, R.P.1    Catterall, W.A.2
  • 39
    • 0020464124 scopus 로고
    • The saxitoxin receptor of the sodium channel from rat brain. Evidence for two nonidentical β subunits
    • Hartshorne RP, Messner DJ, Coppersmith JC & Catterall WA (1982). The saxitoxin receptor of the sodium channel from rat brain. Evidence for two nonidentical β subunits. J Biol Chem 257, 13888-13891.
    • (1982) J Biol Chem , vol.257 , pp. 13888-13891
    • Hartshorne, R.P.1    Messner, D.J.2    Coppersmith, J.C.3    Catterall, W.A.4
  • 40
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • Heinemann SH, Terlau H, Stühmer W, Imoto K & Numa S (1992). Calcium channel characteristics conferred on the sodium channel by single mutations. Nature 356, 441-443.
    • (1992) Nature , vol.356 , pp. 441-443
    • Heinemann, S.H.1    Terlau, H.2    Stühmer, W.3    Imoto, K.4    Numa, S.5
  • 41
    • 27144438639 scopus 로고    scopus 로고
    • Selectivity filter residues contribute unequally to pore stabilization in voltage-gated sodium channels
    • Hilber K, Sandtner W, Zarrabi T, Zebedin E, Kudlacek O, Fozzard HA & Todt H (2005). Selectivity filter residues contribute unequally to pore stabilization in voltage-gated sodium channels. Biochemistry 44, 13874-13882.
    • (2005) Biochemistry , vol.44 , pp. 13874-13882
    • Hilber, K.1    Sandtner, W.2    Zarrabi, T.3    Zebedin, E.4    Kudlacek, O.5    Fozzard, H.A.6    Todt, H.7
  • 42
    • 0015166645 scopus 로고
    • The permeability of the sodium channel to organic cations in myelinated nerve
    • Hille B (1971). The permeability of the sodium channel to organic cations in myelinated nerve. J Gen Physiol 59, 599-619.
    • (1971) J Gen Physiol , vol.59 , pp. 599-619
    • Hille, B.1
  • 43
    • 0015357133 scopus 로고
    • The permeability of the sodium channel to metal cations in myelinated nerve
    • Hille B (1972). The permeability of the sodium channel to metal cations in myelinated nerve. J Gen Physiol 59, 637-658.
    • (1972) J Gen Physiol , vol.59 , pp. 637-658
    • Hille, B.1
  • 44
    • 0016710436 scopus 로고
    • Ionic selectivity, saturation, and block in sodium channels. A four-barrier model
    • Hille B (1975a). Ionic selectivity, saturation, and block in sodium channels. A four-barrier model. J Gen Physiol 66, 535-560.
    • (1975) J Gen Physiol , vol.66 , pp. 535-560
    • Hille, B.1
  • 45
    • 0016782794 scopus 로고
    • The receptor for tetrodotoxin and saxitoxin: a structural hypothesis
    • Hille B (1975b). The receptor for tetrodotoxin and saxitoxin: a structural hypothesis. Biophys J 15, 615-619.
    • (1975) Biophys J , vol.15 , pp. 615-619
    • Hille, B.1
  • 46
    • 0017332486 scopus 로고
    • Local anesthetics: hydrophilic and hydrophobic pathways for the drug-receptor reaction
    • Hille B (1977). Local anesthetics: hydrophilic and hydrophobic pathways for the drug-receptor reaction. J Gen Physiol 69, 497-515.
    • (1977) J Gen Physiol , vol.69 , pp. 497-515
    • Hille, B.1
  • 47
    • 0003443746 scopus 로고    scopus 로고
    • 3rd edition. Sinauer Associates Inc., Sunderland, MA, USA.
    • Hille B (2001). Ionic Channels of Excitable Membranes, 3rd edition. Sinauer Associates Inc., Sunderland, MA, USA.
    • (2001) Ionic Channels of Excitable Membranes
    • Hille, B.1
  • 48
    • 77956707015 scopus 로고
    • Currents carried by sodium and potassium ions through the membrane of the giant axon of Loligo
    • Hodgkin AL & Huxley AF (1952a). Currents carried by sodium and potassium ions through the membrane of the giant axon of Loligo. J Physiol 116, 449-472.
    • (1952) J Physiol , vol.116 , pp. 449-472
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 49
    • 76949125485 scopus 로고
    • The components of membrane conductance in the giant axon of Loligo
    • Hodgkin AL & Huxley AF (1952b). The components of membrane conductance in the giant axon of Loligo. J Physiol 116, 473-496.
    • (1952) J Physiol , vol.116 , pp. 473-496
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 50
    • 77956677051 scopus 로고
    • The dual effect of membrane potential on sodium conductance in the giant axon of Loligo
    • Hodgkin AL & Huxley AF (1952c). The dual effect of membrane potential on sodium conductance in the giant axon of Loligo. J Physiol 116, 497-506.
    • (1952) J Physiol , vol.116 , pp. 497-506
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 51
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin AL & Huxley AF (1952d). A quantitative description of membrane current and its application to conduction and excitation in nerve. J Physiol 117, 500-544.
    • (1952) J Physiol , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 53
  • 58
    • 0016196463 scopus 로고
    • Kinetics and steady-state properties of the charged system controlling sodium conductance in the squid giant axon
    • Keynes RD & Rojas E (1974). Kinetics and steady-state properties of the charged system controlling sodium conductance in the squid giant axon. J Physiol 239, 393-434.
    • (1974) J Physiol , vol.239 , pp. 393-434
    • Keynes, R.D.1    Rojas, E.2
  • 60
    • 0030963793 scopus 로고    scopus 로고
    • Sodium channel activation gating is affected by substitutions of voltage sensor positive charges in all four domains
    • Kontis KJ, Rounaghi A & Goldin AL (1997). Sodium channel activation gating is affected by substitutions of voltage sensor positive charges in all four domains. J Gen Physiol 110, 391-401.
    • (1997) J Gen Physiol , vol.110 , pp. 391-401
    • Kontis, K.J.1    Rounaghi, A.2    Goldin, A.L.3
  • 61
    • 79961124704 scopus 로고    scopus 로고
    • R1 in the Shaker S4 occupies the gating charge transfer center in the resting state
    • Lin MC, Hsieh JY, Mock AF & Papazian DM (2011). R1 in the Shaker S4 occupies the gating charge transfer center in the resting state. J Gen Physiol 138, 155-163.
    • (2011) J Gen Physiol , vol.138 , pp. 155-163
    • Lin, M.C.1    Hsieh, J.Y.2    Mock, A.F.3    Papazian, D.M.4
  • 63
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: structural basis of electromechanical coupling
    • Long SB, Campbell EB & Mackinnon R (2005b). Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 65
    • 0034646634 scopus 로고    scopus 로고
    • Sodium channel β subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact
    • Malhotra JD, Kazen-Gillespie K, Hortsch M & Isom LL (2000). Sodium channel β subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact. J Biol Chem 275, 11383-11388.
    • (2000) J Biol Chem , vol.275 , pp. 11383-11388
    • Malhotra, J.D.1    Kazen-Gillespie, K.2    Hortsch, M.3    Isom, L.L.4
  • 68
    • 0024811092 scopus 로고
    • A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II
    • Noda M, Suzuki H, Numa S & Stühmer W (1989). A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II. FEBS Lett 259, 213-216.
    • (1989) FEBS Lett , vol.259 , pp. 213-216
    • Noda, M.1    Suzuki, H.2    Numa, S.3    Stühmer, W.4
  • 69
    • 23244467740 scopus 로고    scopus 로고
    • The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel
    • Pavlov E, Bladen C, Winkfein R, Diao C, Dhaliwal P & French RJ (2005). The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel. Biophys J 89, 232-242.
    • (2005) Biophys J , vol.89 , pp. 232-242
    • Pavlov, E.1    Bladen, C.2    Winkfein, R.3    Diao, C.4    Dhaliwal, P.5    French, R.J.6
  • 70
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh J, Gamal El-Din TM, Scheuer T, Zheng N & Catterall WA (2012). Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 486, 135-139.
    • (2012) Nature , vol.486 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 71
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh J, Scheuer T, Zheng N & Catterall WA (2011). The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358.
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 73
    • 0027944683 scopus 로고
    • Molecular determinants of state-dependent block of sodium channels by local anesthetics
    • Ragsdale DS, McPhee JC, Scheuer T & Catterall WA (1994). Molecular determinants of state-dependent block of sodium channels by local anesthetics. Science 265, 1724-1728.
    • (1994) Science , vol.265 , pp. 1724-1728
    • Ragsdale, D.S.1    McPhee, J.C.2    Scheuer, T.3    Catterall, W.A.4
  • 76
    • 0035939078 scopus 로고    scopus 로고
    • Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain
    • Ratcliffe CF, Westenbroek RE, Curtis R & Catterall WA (2001). Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain. J Cell Biol 154, 427-434.
    • (2001) J Cell Biol , vol.154 , pp. 427-434
    • Ratcliffe, C.F.1    Westenbroek, R.E.2    Curtis, R.3    Catterall, W.A.4
  • 80
    • 0018196425 scopus 로고
    • Slow inactivation of the sodium conductance in squid giant axons. Pronase resistance
    • Rudy B (1978). Slow inactivation of the sodium conductance in squid giant axons. Pronase resistance. J Physiol 283, 1-21.
    • (1978) J Physiol , vol.283 , pp. 1-21
    • Rudy, B.1
  • 81
    • 56049083760 scopus 로고    scopus 로고
    • Models of voltage-dependent conformational changes in NaChBac channels
    • Shafrir Y, Durell SR & Guy HR (2008). Models of voltage-dependent conformational changes in NaChBac channels. Biophys J 95, 3663-3676.
    • (2008) Biophys J , vol.95 , pp. 3663-3676
    • Shafrir, Y.1    Durell, S.R.2    Guy, H.R.3
  • 82
    • 0032418740 scopus 로고    scopus 로고
    • Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R
    • Srinivasan J, Schachner M & Catterall WA (1998). Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R. Proc Natl Acad Sci U S A 95, 15753-15757.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15753-15757
    • Srinivasan, J.1    Schachner, M.2    Catterall, W.A.3
  • 83
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • Starace DM & Bezanilla F (2004). A proton pore in a potassium channel voltage sensor reveals a focused electric field. Nature 427, 548-553.
    • (2004) Nature , vol.427 , pp. 548-553
    • Starace, D.M.1    Bezanilla, F.2
  • 85
    • 0020353060 scopus 로고
    • Reconstitution of neurotoxin-stimulated sodium transport by the voltage-sensitive sodium channel purified from rat brain
    • Talvenheimo JA, Tamkun MM & Catterall WA (1982). Reconstitution of neurotoxin-stimulated sodium transport by the voltage-sensitive sodium channel purified from rat brain. J Biol Chem 257, 11868-11871.
    • (1982) J Biol Chem , vol.257 , pp. 11868-11871
    • Talvenheimo, J.A.1    Tamkun, M.M.2    Catterall, W.A.3
  • 86
    • 0021329353 scopus 로고
    • The sodium channel from rat brain. Reconstitution of neurotoxin-activated ion flux and scorpion toxin binding from purified components
    • Tamkun MM, Talvenheimo JA & Catterall WA (1984). The sodium channel from rat brain. Reconstitution of neurotoxin-activated ion flux and scorpion toxin binding from purified components. J Biol Chem 259, 1676-1688.
    • (1984) J Biol Chem , vol.259 , pp. 1676-1688
    • Tamkun, M.M.1    Talvenheimo, J.A.2    Catterall, W.A.3
  • 92
    • 0023784649 scopus 로고
    • Identification of an intracellular peptide segment involved in sodium channel inactivation
    • Vassilev PM, Scheuer T & Catterall WA (1988). Identification of an intracellular peptide segment involved in sodium channel inactivation. Science 241, 1658-1661.
    • (1988) Science , vol.241 , pp. 1658-1661
    • Vassilev, P.M.1    Scheuer, T.2    Catterall, W.A.3
  • 93
    • 0008453646 scopus 로고
    • Inhibition of inactivation of single sodium channels by a site-directed antibody
    • Vassilev P, Scheuer T & Catterall WA (1989). Inhibition of inactivation of single sodium channels by a site-directed antibody. Proc Natl Acad Sci U S A 86, 8147-8151.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 8147-8151
    • Vassilev, P.1    Scheuer, T.2    Catterall, W.A.3
  • 98
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • Yang N, George AL Jr & Horn R (1996). Molecular basis of charge movement in voltage-gated sodium channels. Neuron 16, 113-122.
    • (1996) Neuron , vol.16 , pp. 113-122
    • Yang, N.1    George Jr., A.L.2    Horn, R.3
  • 99
    • 0029084477 scopus 로고
    • Evidence for voltage-dependent S4 movement in sodium channel
    • Yang N & Horn R (1995). Evidence for voltage-dependent S4 movement in sodium channel. Neuron 15, 213-218.
    • (1995) Neuron , vol.15 , pp. 213-218
    • Yang, N.1    Horn, R.2
  • 103
    • 0037144493 scopus 로고    scopus 로고
    • Role of amino acid residues in transmembrane segments IS6 and IIS6 of the sodium channel α subunit in voltage-dependent gating and drug block
    • Yarov-Yarovoy V, McPhee JC, Idsvoog D, Pate C, Scheuer T & Catterall WA (2002). Role of amino acid residues in transmembrane segments IS6 and IIS6 of the sodium channel α subunit in voltage-dependent gating and drug block. J Biol Chem 277, 35393-35401.
    • (2002) J Biol Chem , vol.277 , pp. 35393-35401
    • Yarov-Yarovoy, V.1    McPhee, J.C.2    Idsvoog, D.3    Pate, C.4    Scheuer, T.5    Catterall, W.A.6
  • 104
    • 15244344363 scopus 로고    scopus 로고
    • The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis
    • Yu FH & Catterall WA (2004). The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis. Sci STKE 2004, re15.
    • (2004) Sci STKE , vol.2004
    • Yu, F.H.1    Catterall, W.A.2
  • 107
    • 11144221751 scopus 로고    scopus 로고
    • Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment
    • Zhao Y, Scheuer T & Catterall WA (2004a). Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment. Proc Natl Acad Sci U S A 101, 17873-17878.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17873-17878
    • Zhao, Y.1    Scheuer, T.2    Catterall, W.A.3
  • 109
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a potassium channel-Fab complex at 2.0 Å resolution
    • Zhou Y, Morais-Cabral JH, Kaufman A & MacKinnon R (2001). Chemistry of ion coordination and hydration revealed by a potassium channel-Fab complex at 2.0 Å 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.