메뉴 건너뛰기




Volumn 541, Issue 7635, 2017, Pages 46-51

Cryo-EM structure of the open high-conductance Ca2+ -activated K+ channel

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DIVALENT CATION; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; MAGNESIUM; SLO1 CHANNEL; UNCLASSIFIED DRUG; LIPID BILAYER; PROTEIN SUBUNIT;

EID: 85016145318     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature20608     Document Type: Article
Times cited : (194)

References (79)
  • 1
    • 0019858611 scopus 로고
    • Single channel recordings of Ca2+-activated K+ currents in rat muscle cell culture
    • Pallotta, B. S., Magleby, K. L. & Barrett, J. N. Single channel recordings of Ca2+-activated K+ currents in rat muscle cell culture. Nature 293, 471-474 (1981).
    • (1981) Nature , vol.293 , pp. 471-474
    • Pallotta, B.S.1    Magleby, K.L.2    Barrett, J.N.3
  • 2
    • 0019827872 scopus 로고
    • Ca-dependent K channels with large unitary conductance in chromaffin cell membranes
    • Marty, A. Ca-dependent K channels with large unitary conductance in chromaffin cell membranes. Nature 291, 497-500 (1981)
    • (1981) Nature , vol.291 , pp. 497-500
    • Marty, A.1
  • 3
    • 0013492901 scopus 로고
    • Reconstitution in planar lipid bilayers of a Ca2+-dependent K+ channel from transverse tubule membranes isolated from rabbit skeletal muscle
    • Latorre, R., Vergara, C. & Hidalgo, C. Reconstitution in planar lipid bilayers of a Ca2+-dependent K+ channel from transverse tubule membranes isolated from rabbit skeletal muscle. Proc. Natl Acad. Sci. USA 79, 805-809 (1982).
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 805-809
    • Latorre, R.1    Vergara, C.2    Hidalgo, C.3
  • 4
    • 0020000206 scopus 로고
    • Properties of single calciumactivated potassium channels in cultured rat muscle
    • Barrett, J. N., Magleby, K. L. & Pallotta, B. S. Properties of single calciumactivated potassium channels in cultured rat muscle. J. Physiol. (Lond.) 331, 211-230 (1982).
    • (1982) J. Physiol. (Lond.) , vol.331 , pp. 211-230
    • Barrett, J.N.1    Magleby, K.L.2    Pallotta, B.S.3
  • 5
    • 84886994171 scopus 로고    scopus 로고
    • A BK (Slo1) channel journey from molecule to physiology
    • Contreras, G. F. et al. A BK (Slo1) channel journey from molecule to physiology. Channels (Austin) 7, 442-458 (2013).
    • (2013) Channels (Austin) , vol.7 , pp. 442-458
    • Contreras, G.F.1
  • 6
    • 0035054180 scopus 로고    scopus 로고
    • Structure of the RCK domain from the e coli K+ channel and demonstration of its presence in the human BK channel
    • Jiang, Y., Pico, A., Cadene, M., Chait, B. T. & MacKinnon, R. Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel. Neuron 29, 593-601 (2001).
    • (2001) Neuron , vol.29 , pp. 593-601
    • Jiang, Y.1    Pico, A.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 7
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S. B., Campbell, E. B. & Mackinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903 (2005).
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 8
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • Long, S. B., Tao, X., Campbell, E. B. & MacKinnon, R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450, 376-382 (2007).
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 9
    • 77954659083 scopus 로고    scopus 로고
    • Structure of the gating ring from the human large-conductance Ca2+-gated K+ channel
    • Wu, Y., Yang, Y., Ye, S. & Jiang, Y. Structure of the gating ring from the human large-conductance Ca2+-gated K+ channel. Nature 466, 393-397 (2010).
    • (2010) Nature , vol.466 , pp. 393-397
    • Wu, Y.1    Yang, Y.2    Ye, S.3    Jiang, Y.4
  • 10
    • 77954591491 scopus 로고    scopus 로고
    • Structure of the human BK channel Ca2+-activation apparatus at 3 0 A resolution
    • Yuan, P., Leonetti, M. D., Pico, A. R., Hsiung, Y. & MacKinnon, R. Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution. Science 329, 182-186 (2010).
    • (2010) Science , vol.329 , pp. 182-186
    • Yuan, P.1    Leonetti, M.D.2    Pico, A.R.3    Hsiung, Y.4    MacKinnon, R.5
  • 11
    • 84855427565 scopus 로고    scopus 로고
    • Open structure of the Ca2+ gating ring in the high-conductance Ca2+-activated K+ channel
    • Yuan, P., Leonetti, M. D., Hsiung, Y. & MacKinnon, R. Open structure of the Ca2+ gating ring in the high-conductance Ca2+-activated K+ channel. Nature 481, 94-97 (2011).
    • (2011) Nature , vol.481 , pp. 94-97
    • Yuan, P.1    Leonetti, M.D.2    Hsiung, Y.3    MacKinnon, R.4
  • 12
    • 0030852701 scopus 로고    scopus 로고
    • A novel calcium-sensing domain in the BK channel
    • Schreiber, M. & Salkoff, L. A novel calcium-sensing domain in the BK channel. Biophys. J. 73, 1355-1363 (1997).
    • (1997) Biophys. J , vol.73 , pp. 1355-1363
    • Schreiber, M.1    Salkoff, L.2
  • 13
    • 0037158754 scopus 로고    scopus 로고
    • Multiple regulatory sites in large-conductance calcium-activated potassium channels
    • Xia, X. M., Zeng, X. & Lingle, C. J. Multiple regulatory sites in large-conductance calcium-activated potassium channels. Nature 418, 880-884 (2002).
    • (2002) Nature , vol.418 , pp. 880-884
    • Xia, X.M.1    Zeng, X.2    Lingle, C.J.3
  • 14
    • 78649873403 scopus 로고    scopus 로고
    • Ion sensing in the RCK1 domain of BK channels
    • Zhang, G. et al. Ion sensing in the RCK1 domain of BK channels. Proc. Natl Acad. Sci. USA 107, 18700-18705 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18700-18705
    • Zhang, G.1
  • 15
    • 0036023399 scopus 로고    scopus 로고
    • Elimination of the BKCa channel's high-affinity Ca2+ sensitivity
    • Bao, L., Rapin, A. M., Holmstrand, E. C. & Cox, D. H. Elimination of the BKCa channel's high-affinity Ca2+ sensitivity. J. Gen. Physiol. 120, 173-189 (2002).
    • (2002) J. Gen. Physiol , vol.120 , pp. 173-189
    • Bao, L.1    Rapin, A.M.2    Holmstrand, E.C.3    Cox, D.H.4
  • 16
    • 2342481193 scopus 로고    scopus 로고
    • Mapping the BKCa channel's "Ca2+ bowl": Side-chains essential for Ca2+ sensing
    • Bao, L., Kaldany, C., Holmstrand, E. C. & Cox, D. H. Mapping the BKCa channel's "Ca2+ bowl": side-chains essential for Ca2+ sensing. J. Gen. Physiol. 123, 475-489 (2004).
    • (2004) J. Gen. Physiol , vol.123 , pp. 475-489
    • Bao, L.1    Kaldany, C.2    Holmstrand, E.C.3    Cox, D.H.4
  • 17
    • 0022556461 scopus 로고
    • Allosteric effects of Mg2+ on the gating of Ca2+-activated K+ channels from mammalian skeletal muscle
    • Golowasch, J., Kirkwood, A. & Miller, C. Allosteric effects of Mg2+ on the gating of Ca2+-activated K+ channels from mammalian skeletal muscle. J. Exp. Biol. 124, 5-13 (1986).
    • (1986) J. Exp. Biol , vol.124 , pp. 5-13
    • Golowasch, J.1    Kirkwood, A.2    Miller, C.3
  • 18
    • 0023718751 scopus 로고
    • Activation by divalent cations of a Ca2+-activated K+ channel from skeletal muscle membrane
    • Oberhauser, A., Alvarez, O. & Latorre, R. Activation by divalent cations of a Ca2+-activated K+ channel from skeletal muscle membrane. J. Gen. Physiol. 92, 67-86 (1988).
    • (1988) J. Gen. Physiol , vol.92 , pp. 67-86
    • Oberhauser, A.1    Alvarez, O.2    Latorre, R.3
  • 19
    • 0037158733 scopus 로고    scopus 로고
    • Mechanism of magnesium activation of calcium-activated potassium channels
    • Shi, J. et al. Mechanism of magnesium activation of calcium-activated potassium channels. Nature 418, 876-880 (2002).
    • (2002) Nature , vol.418 , pp. 876-880
    • Shi, J.1
  • 20
    • 55549119918 scopus 로고    scopus 로고
    • Activation of Slo1 BK channels by Mg2+ coordinated between the voltage sensor and RCK1 domains
    • Yang, H. et al. Activation of Slo1 BK channels by Mg2+ coordinated between the voltage sensor and RCK1 domains. Nat. Struct. Mol. Biol. 15, 1152-1159 (2008).
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 1152-1159
    • Yang, H.1
  • 21
    • 85177148143 scopus 로고
    • Pharmacological characterization of five cloned voltagegated K+ channels
    • 1.5, and 3.1, stably expressed in mammalian cell lines. Mol. Pharmacol. 45, 1227-1234
    • Grissmer, S. et al. Pharmacological characterization of five cloned voltagegated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol. Pharmacol. 45, 1227-1234 (1994).
    • (1994) Types Kv1.1 , vol.1-2 , pp. 1-3
    • Grissmer, S.1
  • 22
    • 10644297151 scopus 로고    scopus 로고
    • The appearance of a protein kinase A-regulated splice isoform of slo is associated with the maturation of neurons that control reproductive behavior
    • Zhang, Y. et al. The appearance of a protein kinase A-regulated splice isoform of slo is associated with the maturation of neurons that control reproductive behavior. J. Biol. Chem. 279, 52324-52330 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 52324-52330
    • Zhang, Y.1
  • 23
    • 0036714915 scopus 로고    scopus 로고
    • Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels
    • Horrigan, F. T. & Aldrich, R. W. Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels. J. Gen. Physiol. 120, 267-305 (2002).
    • (2002) J. Gen. Physiol , vol.120 , pp. 267-305
    • Horrigan, F.T.1    Aldrich, R.W.2
  • 24
    • 0030911735 scopus 로고    scopus 로고
    • Voltage-controlled gating in a large conductance Ca2+-sensitive K+channel (hslo)
    • Stefani, E. et al. Voltage-controlled gating in a large conductance Ca2+-sensitive K+channel (hslo). Proc. Natl Acad. Sci. USA 94, 5427-5431 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5427-5431
    • Stefani, E.1
  • 25
    • 0032771042 scopus 로고    scopus 로고
    • Allosteric voltage gating of potassium channels II Mslo channel gating charge movement in the absence of Ca2+
    • Horrigan, F. T. & Aldrich, R. W. Allosteric voltage gating of potassium channels II. Mslo channel gating charge movement in the absence of Ca2+. J. Gen. Physiol. 114, 305-336 (1999).
    • (1999) J. Gen. Physiol , vol.114 , pp. 305-336
    • Horrigan, F.T.1    Aldrich, R.W.2
  • 26
    • 0032811552 scopus 로고    scopus 로고
    • Allosteric voltage gating of potassium channels i Mslo ionic currents in the absence of Ca2+
    • Horrigan, F. T., Cui, J. & Aldrich, R. W. Allosteric voltage gating of potassium channels I. Mslo ionic currents in the absence of Ca2+. J. Gen. Physiol. 114, 277-304 (1999).
    • (1999) J. Gen. Physiol , vol.114 , pp. 277-304
    • Horrigan, F.T.1    Cui, J.2    Aldrich, R.W.3
  • 27
    • 0019229699 scopus 로고
    • The variance of sodium current fluctuations at the node of Ranvier
    • Sigworth, F. J. The variance of sodium current fluctuations at the node of Ranvier. J. Physiol. (Lond.) 307, 97-129 (1980).
    • (1980) J. Physiol. (Lond.) , vol.307 , pp. 97-129
    • Sigworth, F.J.1
  • 28
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1 2: Structural basis of electromechanical coupling
    • Long, S. B., Campbell, E. B. & Mackinnon, R. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908 (2005).
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 30
    • 84859651420 scopus 로고    scopus 로고
    • Mechanism of voltage gating in potassium channels
    • Jensen, M. O. et al. Mechanism of voltage gating in potassium channels. Science 336, 229-233 (2012).
    • (2012) Science , vol.336 , pp. 229-233
    • Jensen, M.O.1
  • 31
    • 27544516349 scopus 로고    scopus 로고
    • Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel
    • Ruta, V., Chen, J. & MacKinnon, R. Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel. Cell 123, 463-475 (2005).
    • (2005) Cell , vol.123 , pp. 463-475
    • Ruta, V.1    Chen, J.2    MacKinnon, R.3
  • 32
    • 77951728181 scopus 로고    scopus 로고
    • Location of modulatory beta subunits in BK potassium channels
    • Liu, G. et al. Location of modulatory beta subunits in BK potassium channels. J. Gen. Physiol. 135, 449-459 (2010).
    • (2010) J. Gen. Physiol , vol.135 , pp. 449-459
    • Liu, G.1
  • 33
    • 0142185496 scopus 로고    scopus 로고
    • The occupancy of ions in the K+ selectivity filter: Charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates
    • Zhou, Y. & MacKinnon, R. The occupancy of ions in the K+ selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates. J. Mol. Biol. 333, 965-975 (2003).
    • (2003) J. Mol. Biol , vol.333 , pp. 965-975
    • Zhou, Y.1    MacKinnon, R.2
  • 34
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1 8 A resolution
    • Nishida, M. & MacKinnon, R. Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution. Cell 111, 957-965 (2002).
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2
  • 35
    • 84946908578 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of the Slo2.2 Na+-activated K+ channel
    • Hite, R. K. et al. Cryo-electron microscopy structure of the Slo2.2 Na+-activated K+ channel. Nature 527, 198-203 (2015).
    • (2015) Nature , vol.527 , pp. 198-203
    • Hite, R.K.1
  • 36
    • 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., Niu, X. & Magleby, K. L. 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).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9017-9022
    • Brelidze, T.I.1    Niu, X.2    Magleby, K.L.3
  • 37
    • 0043074453 scopus 로고    scopus 로고
    • Electrostatic tuning of ion conductance in potassium channels
    • Nimigean, C. M., Chappie, J. S. & Miller, C. Electrostatic tuning of ion conductance in potassium channels. Biochemistry 42, 9263-9268 (2003).
    • (2003) Biochemistry , vol.42 , pp. 9263-9268
    • Nimigean, C.M.1    Chappie, J.S.2    Miller, C.3
  • 39
    • 3142682254 scopus 로고    scopus 로고
    • Unique inner pore properties of BK channels revealed by quaternary ammonium block
    • Li, W. & Aldrich, R. W. Unique inner pore properties of BK channels revealed by quaternary ammonium block. J. Gen. Physiol. 124, 43-57 (2004).
    • (2004) J. Gen. Physiol , vol.124 , pp. 43-57
    • Li, W.1    Aldrich, R.W.2
  • 40
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • Armstrong, C. M. & Bezanilla, F. Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol. 63, 533-552 (1974).
    • (1974) J. Gen. Physiol , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Bezanilla, F.2
  • 41
    • 0030175867 scopus 로고    scopus 로고
    • Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel
    • Seoh, S. A., Sigg, D., Papazian, D. M. & Bezanilla, F. Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron 16, 1159-1167 (1996).
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 42
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4 segment to gating charge in the Shaker K+ channel
    • Aggarwal, S. K. & MacKinnon, R. Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16, 1169-1177 (1996).
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 43
    • 85016153996 scopus 로고    scopus 로고
    • Structural basis for gating the highconductance Ca2+-activated K+ channel
    • Hite, R. K., Tao, X. & MacKinnon, R. Structural basis for gating the highconductance Ca2+-activated K+ channel. Nature http://dx.doi.org/10.1038/ nature20775 (2016).
    • (2016) Nature
    • Hite, R.K.1    Tao, X.2    MacKinnon, R.3
  • 44
    • 0035163147 scopus 로고    scopus 로고
    • Intracellular Mg2+ enhances the function of BK-type Ca2+-activated K+ channels
    • Shi, J. & Cui, J. Intracellular Mg2+ enhances the function of BK-type Ca2+-activated K+ channels. J. Gen. Physiol. 118, 589-606 (2001).
    • (2001) J. Gen. Physiol , vol.118 , pp. 589-606
    • Shi, J.1    Cui, J.2
  • 45
    • 2142859139 scopus 로고    scopus 로고
    • Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc
    • Katz, A. M., Glusker, J. P., Beebe, S. A. & Bock, C. W. Calcium ion coordination: a comparison with that of beryllium, magnesium, and zinc. J. Am. Chem. Soc. 1, 5752-5763 (1996).
    • (1996) J. Am. Chem. Soc , vol.1 , pp. 5752-5763
    • Katz, A.M.1    Glusker, J.P.2    Beebe, S.A.3    Bock, C.W.4
  • 46
    • 0000808787 scopus 로고
    • Coordination of water to magnesium cations
    • Bock, C. W., Kaufman, A. & Glusker, J. P. Coordination of water to magnesium cations. Inorg. Chem. 33, 419-427 (1994).
    • (1994) Inorg. Chem , vol.33 , pp. 419-427
    • Bock, C.W.1    Kaufman, A.2    Glusker, J.P.3
  • 47
    • 33749013044 scopus 로고    scopus 로고
    • Intra-and intersubunit cooperativity in activation of BK channels by Ca2+
    • Qian, X., Niu, X. & Magleby, K. L. Intra-and intersubunit cooperativity in activation of BK channels by Ca2+. J. Gen. Physiol. 128, 389-404 (2006).
    • (2006) J. Gen. Physiol , vol.128 , pp. 389-404
    • Qian, X.1    Niu, X.2    Magleby, K.L.3
  • 48
    • 59449101655 scopus 로고    scopus 로고
    • Measurements of the BKCa channel's high-affinity Ca2+ binding constants: Effects of membrane voltage
    • Sweet, T. B. & Cox, D. H. Measurements of the BKCa channel's high-affinity Ca2+ binding constants: effects of membrane voltage. J. Gen. Physiol. 132, 491-505 (2008).
    • (2008) J. Gen. Physiol , vol.132 , pp. 491-505
    • Sweet, T.B.1    Cox, D.H.2
  • 49
    • 84861952634 scopus 로고    scopus 로고
    • Crystal structure of an orthologue of the NaChBac voltagegated sodium channel
    • Zhang, X. et al. Crystal structure of an orthologue of the NaChBac voltagegated sodium channel. Nature 486, 130-134 (2012).
    • (2012) Nature , vol.486 , pp. 130-134
    • Zhang, X.1
  • 50
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J., Gamal El-Din, T. M., Scheuer, T., Zheng, N. & Catterall, W. A. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature. 486. 135-139( 2012).
    • (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
  • 51
    • 84960906119 scopus 로고    scopus 로고
    • Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana
    • Guo, J. et al. Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana. Nature 531, 196-201 (2016).
    • (2016) Nature , vol.531 , pp. 196-201
    • Guo, J.1
  • 52
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: Generating accurate representations of channel and interior surfaces in molecular structures
    • Ho, B. K. G. F. HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct. Biol. 8, (2008).
    • (2008) BMC Struct. Biol , vol.8
    • Ho, B.K.G.F.1
  • 53
    • 66749153179 scopus 로고    scopus 로고
    • A carboxy-terminal affinity tag for the purification and mass spectrometric characterization of integral membrane proteins
    • Wong, J. P., Reboul, E., Molday, R. S. & Kast, J. A carboxy-terminal affinity tag for the purification and mass spectrometric characterization of integral membrane proteins. J. Proteome Res. 8, 2388-2396 (2009).
    • (2009) J. Proteome Res , vol.8 , pp. 2388-2396
    • Wong, J.P.1    Reboul, E.2    Molday, R.S.3    Kast, J.4
  • 54
    • 39749193861 scopus 로고    scopus 로고
    • A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins
    • Rothbauer, U. et al. A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol. Cell. Proteomics 7, 282-289 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 282-289
    • Rothbauer, U.1
  • 55
    • 84927174857 scopus 로고    scopus 로고
    • A robust pipeline for rapid production of versatile nanobody repertoires
    • Fridy, P. C. et al. A robust pipeline for rapid production of versatile nanobody repertoires. Nat. Methods 11, 1253-1260 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 1253-1260
    • Fridy, P.C.1
  • 56
    • 84916634632 scopus 로고    scopus 로고
    • Quantitative analysis of mammalian GIRK2 channel regulation by G proteins, the signaling lipid PIP2 and Na+ in a reconstituted system
    • Wang, W., Whorton, M. R. & MacKinnon, R. Quantitative analysis of mammalian GIRK2 channel regulation by G proteins, the signaling lipid PIP2 and Na+ in a reconstituted system. eLife 3, e03671 (2014).
    • (2014) ELife , vol.3 , pp. e03671
    • Wang, W.1    Whorton, M.R.2    MacKinnon, R.3
  • 57
    • 0017796425 scopus 로고
    • Gating currents and charge movements in excitable membranes
    • Almers, W. Gating currents and charge movements in excitable membranes. Rev. Physiol. Biochem. Pharmacol. 82, 96-190 (1978)
    • (1978) Rev. Physiol. Biochem. Pharmacol , vol.82 , pp. 96-190
    • Almers, W.1
  • 58
    • 0018908202 scopus 로고
    • Survival of K+ permeability and gating currents in squid axons perfused with K+-free media
    • Almers, W. & Armstrong, C. M. Survival of K+ permeability and gating currents in squid axons perfused with K+-free media. J. Gen. Physiol. 75, 61-78 (1980).
    • (1980) J. Gen. Physiol , vol.75 , pp. 61-78
    • Almers, W.1    Armstrong, C.M.2
  • 60
    • 0029610155 scopus 로고
    • Transfer of twelve charges is needed to open skeletal muscle Na+ channels
    • Hirschberg, B., Rovner, A., Lieberman, M. & Patlak, J. Transfer of twelve charges is needed to open skeletal muscle Na+ channels. J. Gen. Physiol. 106, 1053-1068 (1995).
    • (1995) J. Gen. Physiol , vol.106 , pp. 1053-1068
    • Hirschberg, B.1    Rovner, A.2    Lieberman, M.3    Patlak, J.4
  • 61
    • 0029741699 scopus 로고    scopus 로고
    • Effective gating charges per channel in voltage-dependent K+ and Ca2+ channels
    • Noceti, F. et al. Effective gating charges per channel in voltage-dependent K+ and Ca2+ channels. J. Gen. Physiol. 108, 143-155 (1996).
    • (1996) J. Gen. Physiol , vol.108 , pp. 143-155
    • Noceti, F.1
  • 62
    • 0031015351 scopus 로고    scopus 로고
    • Total charge movement per channel the relation between gating charge displacement and the voltage sensitivity of activation
    • Sigg, D. & Bezanilla, F. Total charge movement per channel. The relation between gating charge displacement and the voltage sensitivity of activation. J. Gen. Physiol. 109, 27-39 (1997).
    • (1997) J. Gen. Physiol , vol.109 , pp. 27-39
    • Sigg, D.1    Bezanilla, F.2
  • 63
    • 0016683376 scopus 로고
    • Channel noise in nerve membranes and lipid bilayers
    • Conti, F. & Wanke, E. Channel noise in nerve membranes and lipid bilayers. Q. Rev. Biophys. 8, 451-506 (1975).
    • (1975) Q. Rev. Biophys , vol.8 , pp. 451-506
    • Conti, F.1    Wanke, E.2
  • 64
    • 0017659569 scopus 로고
    • Sodium channels in nerve apparently have two conductance states
    • Sigworth, F. J. Sodium channels in nerve apparently have two conductance states. Nature 270, 265-267 (1977).
    • (1977) Nature , vol.270 , pp. 265-267
    • Sigworth, F.J.1
  • 65
    • 33748114293 scopus 로고    scopus 로고
    • Empirical considerations regarding the use of ensemble-variance analysis of macroscopic currents
    • Lingle, C. J. Empirical considerations regarding the use of ensemble-variance analysis of macroscopic currents. J. Neurosci. Methods 158, 121-132 (2006).
    • (2006) J. Neurosci. Methods , vol.158 , pp. 121-132
    • Lingle, C.J.1
  • 66
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (2005) J. Struct. Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 67
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2 6 A reconstruction of rotavirus VP6
    • Grant, T. & Grigorieff, N. Measuring the optimal exposure for single particle cryo-EM using a 2.6 A reconstruction of rotavirus VP6. eLife 4, e06980 (2015).
    • (2015) ELife , vol.4 , pp. e06980
    • Grant, T.1    Grigorieff, N.2
  • 68
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: Fast and accurate defocus estimation from electron micrographs
    • Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216-221 (2015).
    • (2015) J. Struct. Biol , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 69
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 70
    • 84946473054 scopus 로고    scopus 로고
    • Alignment of cryo-EM movies of individual particles by optimization of image translations
    • Rubinstein, J. L. & Brubaker, M. A. Alignment of cryo-EM movies of individual particles by optimization of image translations. J. Struct. Biol. 192, 188-195 (2015).
    • (2015) J. Struct. Biol , vol.192 , pp. 188-195
    • Rubinstein, J.L.1    Brubaker, M.A.2
  • 71
    • 84959182065 scopus 로고    scopus 로고
    • High resolution single particle refinement in EMAN2 1
    • Bell, J. M., Chen, M., Baldwin, P. R. & Ludtke, S. J. High resolution single particle refinement in EMAN2.1. Methods 100, 25-34 (2016).
    • (2016) Methods , vol.100 , pp. 25-34
    • Bell, J.M.1    Chen, M.2    Baldwin, P.R.3    Ludtke, S.J.4
  • 72
    • 84883447961 scopus 로고    scopus 로고
    • Likelihood-based classification of cryo-EM images using FREALIGN
    • Lyumkis, D., Brilot, A. F., Theobald, D. L. & Grigorieff, N. Likelihood-based classification of cryo-EM images using FREALIGN. J. Struct. Biol. 183, 377-388 (2013).
    • (2013) J. Struct. Biol , vol.183 , pp. 377-388
    • Lyumkis, D.1    Brilot, A.F.2    Theobald, D.L.3    Grigorieff, N.4
  • 73
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 74
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 76
    • 80053642374 scopus 로고    scopus 로고
    • The Phenix software for automated determination of macromolecular structures
    • Adams, P. D. et al. The Phenix software for automated determination of macromolecular structures. Methods 55, 94-106 (2011).
    • (2011) Methods , vol.55 , pp. 94-106
    • Adams, P.D.1
  • 77
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D , vol.71 , pp. 136-153
    • Brown, A.1
  • 78
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 79
    • 84884682632 scopus 로고    scopus 로고
    • Collaboration gets the most out of software
    • Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013)
    • (2013) ELife , vol.2 , pp. e01456
    • Morin, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.