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Volumn 105, Issue 1, 2013, Pages 108-115

Optically detected structural change in the N-terminal region of the voltage-sensor domain

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; PHOSPHATASE; RHODAMINE; TETRAMETHYLRHODAMINE;

EID: 84879806478     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.05.051     Document Type: Article
Times cited : (20)

References (38)
  • 2
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Y. Murata, and H. Iwasaki Y. Okamura Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor Nature 435 2005 1239 1243
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Okamura, Y.3
  • 3
    • 0022499391 scopus 로고
    • Expression of functional sodium channels from cloned cDNA
    • M. Noda, and T. Ikeda S. Numa Expression of functional sodium channels from cloned cDNA Nature 322 1986 826 828
    • (1986) Nature , vol.322 , pp. 826-828
    • Noda, M.1    Ikeda, T.2    Numa, S.3
  • 4
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K+ channel
    • Y. Jiang, and A. Lee R. MacKinnon X-ray structure of a voltage-dependent K+ channel Nature 423 2003 33 41
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1    Lee, A.2    Mackinnon, R.3
  • 5
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • S.B. Long, E.B. Campbell, and R. Mackinnon Crystal structure of a mammalian voltage-dependent Shaker family K+ channel Science 309 2005 897 903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 6
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • S.B. Long, and X. Tao R. MacKinnon Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment Nature 450 2007 376 382
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Mackinnon, R.3
  • 7
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • J. Payandeh, and T. Scheuer W.A. Catterall The crystal structure of a voltage-gated sodium channel Nature 475 2011 353 358
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Catterall, W.A.3
  • 8
    • 23844459909 scopus 로고    scopus 로고
    • Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement
    • B. Chanda, and O.K. Asamoah F. Bezanilla Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement Nature 436 2005 852 856
    • (2005) Nature , vol.436 , pp. 852-856
    • Chanda, B.1    Asamoah, O.K.2    Bezanilla, F.3
  • 9
    • 35648975390 scopus 로고    scopus 로고
    • Tarantula toxins interact with voltage sensors within lipid membranes
    • M. Milescu, and J. Vobecky K.J. Swartz Tarantula toxins interact with voltage sensors within lipid membranes J. Gen. Physiol. 130 2007 497 511
    • (2007) J. Gen. Physiol. , vol.130 , pp. 497-511
    • Milescu, M.1    Vobecky, J.2    Swartz, K.J.3
  • 10
    • 27544516349 scopus 로고    scopus 로고
    • Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel
    • V. Ruta, J. Chen, and R. MacKinnon Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel Cell 123 2005 463 475
    • (2005) Cell , vol.123 , pp. 463-475
    • Ruta, V.1    Chen, J.2    Mackinnon, R.3
  • 11
    • 0029084477 scopus 로고
    • Evidence for voltage-dependent S4 movement in sodium channels
    • N. Yang, and R. Horn Evidence for voltage-dependent S4 movement in sodium channels Neuron 15 1995 213 218
    • (1995) Neuron , vol.15 , pp. 213-218
    • Yang, N.1    Horn, R.2
  • 12
    • 34748848687 scopus 로고    scopus 로고
    • Closing in on the resting state of the Shaker K(+) channel
    • M.M. Pathak, and V. Yarov-Yarovoy E.Y. Isacoff Closing in on the resting state of the Shaker K(+) channel Neuron 56 2007 124 140
    • (2007) Neuron , vol.56 , pp. 124-140
    • Pathak, M.M.1    Yarov-Yarovoy, V.2    Isacoff, E.Y.3
  • 13
    • 0033576706 scopus 로고    scopus 로고
    • Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel
    • K.S. Glauner, and L.M. Mannuzzu E.Y. Isacoff Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel Nature 402 1999 813 817
    • (1999) Nature , vol.402 , pp. 813-817
    • Glauner, K.S.1    Mannuzzu, L.M.2    Isacoff, E.Y.3
  • 14
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • A. Cha, and G.E. Snyder F. Bezanilla Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy Nature 402 1999 809 813
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Bezanilla, F.3
  • 15
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • K.J. Swartz Sensing voltage across lipid membranes Nature 456 2008 891 897
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 16
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • W.A. Catterall Ion channel voltage sensors: structure, function, and pathophysiology Neuron 67 2010 915 928
    • (2010) Neuron , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 17
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K+ channel
    • Y. Jiang, and V. Ruta R. MacKinnon The principle of gating charge movement in a voltage-dependent K+ channel Nature 423 2003 42 48
    • (2003) Nature , vol.423 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Mackinnon, R.3
  • 18
    • 0036846783 scopus 로고    scopus 로고
    • Coupling between voltage sensors and activation gate in voltage-gated K+ channels
    • Z. Lu, A.M. Klem, and Y. Ramu Coupling between voltage sensors and activation gate in voltage-gated K+ channels J. Gen. Physiol. 120 2002 663 676
    • (2002) J. Gen. Physiol. , vol.120 , pp. 663-676
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 19
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Z. Lu, A.M. Klem, and Y. Ramu Ion conduction pore is conserved among potassium channels Nature 413 2001 809 813
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 20
    • 55849098431 scopus 로고    scopus 로고
    • Engineering and characterization of an enhanced fluorescent protein voltage sensor
    • D. Dimitrov, and Y. He T. Knöpfel Engineering and characterization of an enhanced fluorescent protein voltage sensor PLoS ONE 2 2007 e440
    • (2007) PLoS ONE , vol.2 , pp. 440
    • Dimitrov, D.1    He, Y.2    Knöpfel, T.3
  • 21
    • 48449091054 scopus 로고    scopus 로고
    • Improving membrane voltage measurements using FRET with new fluorescent proteins
    • H. Tsutsui, and S. Karasawa A. Miyawaki Improving membrane voltage measurements using FRET with new fluorescent proteins Nat. Methods 5 2008 683 685
    • (2008) Nat. Methods , vol.5 , pp. 683-685
    • Tsutsui, H.1    Karasawa, S.2    Miyawaki, A.3
  • 22
    • 0034662681 scopus 로고    scopus 로고
    • Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis
    • A. Sawano, and A. Miyawaki Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis Nucleic Acids Res. 28 2000 E78
    • (2000) Nucleic Acids Res. , vol.28 , pp. 78
    • Sawano, A.1    Miyawaki, A.2
  • 23
    • 34548725637 scopus 로고    scopus 로고
    • Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2
    • Y. Murata, and Y. Okamura Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2 J. Physiol. 583 2007 875 889
    • (2007) J. Physiol. , vol.583 , pp. 875-889
    • Murata, Y.1    Okamura, Y.2
  • 24
    • 0026655809 scopus 로고
    • Maintenance of Xenopus laevis and oocyte injection
    • A.L. Goldin Maintenance of Xenopus laevis and oocyte injection Methods Enzymol. 207 1992 266 279
    • (1992) Methods Enzymol. , vol.207 , pp. 266-279
    • Goldin, A.L.1
  • 25
    • 0030048243 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • L.M. Mannuzzu, M.M. Moronne, and E.Y. Isacoff Direct physical measure of conformational rearrangement underlying potassium channel gating Science 271 1996 213 216
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 28
    • 0033680734 scopus 로고    scopus 로고
    • Reconstructing voltage sensor-pore interaction from a fluorescence scan of a voltage-gated K+ channel
    • C.S. Gandhi, E. Loots, and E.Y. Isacoff Reconstructing voltage sensor-pore interaction from a fluorescence scan of a voltage-gated K+ channel Neuron 27 2000 585 595
    • (2000) Neuron , vol.27 , pp. 585-595
    • Gandhi, C.S.1    Loots, E.2    Isacoff, E.Y.3
  • 29
    • 68349127373 scopus 로고    scopus 로고
    • HaloTag7: A genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification
    • R.F. Ohana, and L.P. Encell K.V. Wood HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification Protein Expr. Purif. 68 2009 110 120
    • (2009) Protein Expr. Purif. , vol.68 , pp. 110-120
    • Ohana, R.F.1    Encell, L.P.2    Wood, K.V.3
  • 30
    • 85056069561 scopus 로고    scopus 로고
    • Development of a dehalogenase-based protein fusion tag capable of rapid, selective and covalent attachment to customizable ligands
    • L.P. Encell, and R. Friedman Ohana K.V. Wood Development of a dehalogenase-based protein fusion tag capable of rapid, selective and covalent attachment to customizable ligands Curr. Chem. Genomics 6 2012 55 71
    • (2012) Curr. Chem. Genomics , vol.6 , pp. 55-71
    • Encell, L.P.1    Friedman Ohana, R.2    Wood, K.V.3
  • 31
    • 77954634414 scopus 로고    scopus 로고
    • Visualizing voltage dynamics in zebrafish heart
    • H. Tsutsui, and S. Higashijima Y. Okamura Visualizing voltage dynamics in zebrafish heart J. Physiol. 588 2010 2017 2021
    • (2010) J. Physiol. , vol.588 , pp. 2017-2021
    • Tsutsui, H.1    Higashijima, S.2    Okamura, Y.3
  • 32
    • 0345166933 scopus 로고    scopus 로고
    • Molecular movement of the voltage sensor in a K channel
    • A. Broomand, and R. Männikkö F. Elinder Molecular movement of the voltage sensor in a K channel J. Gen. Physiol. 122 2003 741 748
    • (2003) J. Gen. Physiol. , vol.122 , pp. 741-748
    • Broomand, A.1    Männikkö, R.2    Elinder, F.3
  • 33
    • 0344256586 scopus 로고    scopus 로고
    • The orientation and molecular movement of a k(+) channel voltage-sensing domain
    • C.S. Gandhi, and E. Clark E.Y. Isacoff The orientation and molecular movement of a k(+) channel voltage-sensing domain Neuron 40 2003 515 525
    • (2003) Neuron , vol.40 , pp. 515-525
    • Gandhi, C.S.1    Clark, E.2    Isacoff, E.Y.3
  • 34
    • 66149157329 scopus 로고    scopus 로고
    • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels
    • S.Y. Lee, A. Banerjee, and R. MacKinnon Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels PLoS Biol. 7 2009 e47
    • (2009) PLoS Biol. , vol.7 , pp. 47
    • Lee, S.Y.1    Banerjee, A.2    Mackinnon, R.3
  • 35
    • 78651087721 scopus 로고    scopus 로고
    • KCNE1 alters the voltage sensor movements necessary to open the KCNQ1 channel gate
    • J.D. Osteen, and C. Gonzalez R.S. Kass KCNE1 alters the voltage sensor movements necessary to open the KCNQ1 channel gate Proc. Natl. Acad. Sci. USA 107 2010 22710 22715
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22710-22715
    • Osteen, J.D.1    Gonzalez, C.2    Kass, R.S.3
  • 36
    • 80052626500 scopus 로고    scopus 로고
    • Nano-environmental changes by KCNE proteins modify KCNQ channel function
    • K. Nakajo, and Y. Kubo Nano-environmental changes by KCNE proteins modify KCNQ channel function Channels (Austin) 5 2011 397 401
    • (2011) Channels (Austin) , vol.5 , pp. 397-401
    • Nakajo, K.1    Kubo, Y.2
  • 37
    • 33846694346 scopus 로고    scopus 로고
    • Structure prediction for the down state of a potassium channel voltage sensor
    • M. Grabe, and H.C. Lai L.Y. Jan Structure prediction for the down state of a potassium channel voltage sensor Nature 445 2007 550 553
    • (2007) Nature , vol.445 , pp. 550-553
    • Grabe, M.1    Lai, H.C.2    Jan, L.Y.3
  • 38
    • 33748943301 scopus 로고    scopus 로고
    • Non-conducting functions of voltage-gated ion channels
    • L.K. Kaczmarek Non-conducting functions of voltage-gated ion channels Nat. Rev. Neurosci. 7 2006 761 771
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 761-771
    • Kaczmarek, L.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.