메뉴 건너뛰기




Volumn 100, Issue 4, 2011, Pages 875-884

Interaction of diverse voltage sensor homologs with lipid bilayers revealed by self-assembly simulations

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79951822448     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.11.049     Document Type: Article
Times cited : (12)

References (91)
  • 2
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft, F. M. 2006. From molecule to malady. Nature. 440:440-447.
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 3
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • DOI 10.1038/nature03650
    • Murata, Y., H. Iwasaki, ..., Y. Okamura. 2005. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature. 435:1239-1243. (Pubitemid 40943089)
    • (2005) Nature , vol.435 , Issue.7046 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 4
    • 33646358260 scopus 로고    scopus 로고
    • Avoltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I. S., M. M. Moran, ..., D. E. Clapham. 2006. Avoltage-gated proton-selective channel lacking the pore domain. Nature. 440:1213-1216.
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Clapham, D.E.3
  • 5
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensordomain protein is a voltage-gated proton channel
    • Sasaki, M., M. Takagi, and Y. Okamura. 2006. A voltage sensordomain protein is a voltage-gated proton channel. Science. 312:589-592.
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 7
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N. E., K. McCormack, ..., F. J. Sigworth. 1992. The size of gating charge in wild-type and mutant Shaker potassium channels. Science. 255:1712-1715.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Sigworth, F.J.3
  • 8
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80143-9
    • + channel. Neuron. 16:1169-1177. (Pubitemid 26227238)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 11
    • 0029845542 scopus 로고    scopus 로고
    • Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel
    • DOI 10.1007/s004240050253
    • Yusaf, S. P., D. Wray, and A. Sivaprasadarao. 1996. Measurement of the movement of the S4 segment during the activation of a voltagegated potassium channel. Pflugers Arch. 433:91-97. (Pubitemid 26405626)
    • (1996) Pflugers Archiv European Journal of Physiology , vol.433 , Issue.1-2 , pp. 91-97
    • Yusaf, S.P.1    Wray, D.2    Sivaprasadarao, A.3
  • 14
    • 27544516349 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/j.cell.2005.08.041, PII S0092867405009128
    • + channel. Cell. 123:463-475. (Pubitemid 41546676)
    • (2005) Cell , vol.123 , Issue.3 , pp. 463-475
    • Ruta, V.1    Chen, J.2    MacKinnon, R.3
  • 15
    • 77950488909 scopus 로고    scopus 로고
    • A gating charge transfer center in voltage sensors
    • Tao, X., A. Lee, ..., R. MacKinnon. 2010. A gating charge transfer center in voltage sensors. Science. 328:67-73.
    • (2010) Science , vol.328 , pp. 67-73
    • Tao, X.1    Lee, A.2    MacKinnon, R.3
  • 19
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based x-ray crystallographic refinement
    • Chen, X., Q. Wang, ..., J. Ma. 2010. Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based x-ray crystallographic refinement. Proc. Natl. Acad. Sci. USA. 107:11352-11357.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ma, J.3
  • 20
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • + channel in a lipid membrane-like environment. Nature. 450:376-382. (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 22
    • 77950423127 scopus 로고    scopus 로고
    • The activated state of a sodium channel voltage sensor in a membrane environment
    • Chakrapani, S., P. Sompornpisut, ..., E. Perozo. 2010. The activated state of a sodium channel voltage sensor in a membrane environment. Proc. Natl. Acad. Sci. USA. 107:5435-5440.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5435-5440
    • Chakrapani, S.1    Sompornpisut, P.2    Perozo, E.3
  • 23
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • DOI 10.1038/35101535
    • Lu, Z., A. M. Klem, and Y. Ramu. 2001. Ion conduction pore is conserved among potassium channels. Nature. 413:809-813. (Pubitemid 33026842)
    • (2001) Nature , vol.413 , Issue.6858 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 24
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • DOI 10.1038/nature06266, PII NATURE06266
    • Alabi, A. A., M. I. Bahamonde, ..., K. J. Swartz. 2007. Portability of paddle motif function and pharmacology in voltage sensors. Nature. 450:370-375. (Pubitemid 350126744)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 370-375
    • Alabi, A.A.1    Bahamonde, M.I.2    Jung, H.J.3    Kim, J.I.4    Swartz, K.J.5
  • 25
    • 56249091754 scopus 로고    scopus 로고
    • Deconstructing voltage sensor function and pharmacology in sodium channels
    • Bosmans, F., M. F. Martin-Eauclaire, and K. J. Swartz. 2008. Deconstructing voltage sensor function and pharmacology in sodium channels. Nature. 456:202-208.
    • (2008) Nature , vol.456 , pp. 202-208
    • Bosmans, F.1    Martin-Eauclaire, M.F.2    Swartz, K.J.3
  • 26
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • DOI 10.1038/nature05416, PII NATURE05416
    • Schmidt, D., Q. X. Jiang, and R. MacKinnon. 2006. Phospholipids and the origin of cationic gating charges in voltage sensors. Nature. 444:775-779. (Pubitemid 44949608)
    • (2006) Nature , vol.444 , Issue.7120 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    MacKinnon, R.3
  • 27
    • 33747062707 scopus 로고    scopus 로고
    • Enzymatic activation of voltage-gated potassium channels
    • DOI 10.1038/nature04880, PII NATURE04880
    • Ramu, Y., Y. Xu, and Z. Lu. 2006. Enzymatic activation of voltagegated potassium channels. Nature. 442:696-699. (Pubitemid 44215325)
    • (2006) Nature , vol.442 , Issue.7103 , pp. 696-699
    • Ramu, Y.1    Xu, Y.2    Lu, Z.3
  • 28
    • 39149109885 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1038/nature06618, PII NATURE06618
    • + channels. Nature. 451:826-829. (Pubitemid 351253175)
    • (2008) Nature , vol.451 , Issue.7180 , pp. 826-829
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 29
    • 85031251268 scopus 로고    scopus 로고
    • Influence of membrane alterations on the inhibition of K-v channels by voltage sensor toxins
    • Milescu, M., and K. J. Swartz. 2007. Influence of membrane alterations on the inhibition of K-v channels by voltage sensor toxins. Biophys. J. 1 (Suppl Pt): 295A-296A.
    • (2007) Biophys. J. , vol.1 , Issue.SUPPL. PT
    • Milescu, M.1    Swartz, K.J.2
  • 31
    • 5644258235 scopus 로고    scopus 로고
    • + channel in a lipid bilayer
    • DOI 10.1126/science.1101373
    • + channel in a lipid bilayer. Science. 306:491-495. (Pubitemid 39372450)
    • (2004) Science , vol.306 , Issue.5695 , pp. 491-495
    • Cuello, L.G.1    Cortes, D.M.2    Perozo, E.3
  • 32
    • 70349840420 scopus 로고    scopus 로고
    • Interactions between lipids and voltage sensor paddles detected with tarantula toxins
    • Milescu, M., F. Bosmans, ..., K. J. Swartz. 2009. Interactions between lipids and voltage sensor paddles detected with tarantula toxins. Nat. Struct. Mol. Biol. 16:1080-1085.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1080-1085
    • Milescu, M.1    Bosmans, F.2    Swartz, K.J.3
  • 33
    • 0037426919 scopus 로고    scopus 로고
    • A fluorometric approach to local electric field measurements in a voltage-gated ion channel
    • DOI 10.1016/S0896-6273(02)01126-1
    • Asamoah, O. K., J. P. Wuskell, ..., F. Bezanilla. 2003. A fluorometric approach to local electric field measurements in a voltage-gated ion channel. Neuron. 37:85-97. (Pubitemid 36106436)
    • (2003) Neuron , vol.37 , Issue.1 , pp. 85-97
    • Asamoah, O.K.1    Wuskell, J.P.2    Loew, L.M.3    Bezanilla, F.4
  • 34
    • 25644437209 scopus 로고    scopus 로고
    • Focused electric field across the voltage sensor of potassium channels
    • DOI 10.1016/j.neuron.2005.08.020, PII S0896627305006951
    • Ahern, C. A., and R. Horn. 2005. Focused electric field across the voltage sensor of potassium channels. Neuron. 48:25-29. (Pubitemid 41384163)
    • (2005) Neuron , vol.48 , Issue.1 , pp. 25-29
    • Ahern, C.A.1    Horn, R.2
  • 35
    • 70849119657 scopus 로고    scopus 로고
    • Structure and hydration of membranes embedded with voltage-sensing domains
    • Krepkiy, D., M. Mihailescu, ..., K. J. Swartz. 2009. Structure and hydration of membranes embedded with voltage-sensing domains. Nature. 462:473-479.
    • (2009) Nature , vol.462 , pp. 473-479
    • Krepkiy, D.1    Mihailescu, M.2    Swartz, K.J.3
  • 37
    • 33646135082 scopus 로고    scopus 로고
    • Environment of the gating charges in the Kv1.2 Shaker potassium channel
    • Treptow, W., and M. Tarek. 2006. Environment of the gating charges in the Kv1.2 Shaker potassium channel. Biophys. J. 90: L64-L66.
    • (2006) Biophys. J. , vol.90
    • Treptow, W.1    Tarek, M.2
  • 38
    • 34547628129 scopus 로고    scopus 로고
    • + channel in a membrane environment
    • DOI 10.1529/biophysj.107.112540
    • + channel in a membrane environment. Biophys. J. 93:3070-3082. (Pubitemid 350097098)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3070-3082
    • Jogini, V.1    Roux, B.2
  • 39
    • 33846785439 scopus 로고    scopus 로고
    • How Does a Voltage Sensor Interact with a Lipid Bilayer? Simulations of a Potassium Channel Domain
    • DOI 10.1016/j.str.2007.01.004, PII S0969212607000330
    • Sands, Z. A., and M. S. P. Sansom. 2007. How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain. Structure. 15:235-244. (Pubitemid 46209817)
    • (2007) Structure , vol.15 , Issue.2 , pp. 235-244
    • Sands, Z.A.1    Sansom, M.S.P.2
  • 40
    • 50349088433 scopus 로고    scopus 로고
    • Molecular dynamics simulation of Kv channel voltage sensor helix in a lipid membrane with applied electric field
    • Nishizawa, M., and K. Nishizawa. 2008. Molecular dynamics simulation of Kv channel voltage sensor helix in a lipid membrane with applied electric field. Biophys. J. 95:1729-1744.
    • (2008) Biophys. J. , vol.95 , pp. 1729-1744
    • Nishizawa, M.1    Nishizawa, K.2
  • 41
    • 67849095786 scopus 로고    scopus 로고
    • Initial response of the potassium channel voltage sensor to a transmembrane potential
    • Treptow, W., M. Tarek, and M. L. Klein. 2009. Initial response of the potassium channel voltage sensor to a transmembrane potential. J. Am. Chem. Soc. 131:2107-2109.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2107-2109
    • Treptow, W.1    Tarek, M.2    Klein, M.L.3
  • 42
    • 61449172924 scopus 로고    scopus 로고
    • Conformational changes and slow dynamics through microsecond polarized atomistic molecular simulation of an integral Kv1.2 ion channel
    • Bjelkmar, P., P. S. Niemela, ..., E. Lindahl. 2009. Conformational changes and slow dynamics through microsecond polarized atomistic molecular simulation of an integral Kv1.2 ion channel. PLoS Comp. Biol. 5: e1000289.
    • (2009) PLoS Comp. Biol. , vol.5
    • Bjelkmar, P.1    Niemela, P.S.2    Lindahl, E.3
  • 43
    • 77953578254 scopus 로고    scopus 로고
    • Down-state model of the voltage-sensing domain of a potassium channel
    • Schow, E. V., J. A. Freites, ..., D. J. Tobias. 2010. Down-state model of the voltage-sensing domain of a potassium channel. Biophys. J. 98:2857-2866.
    • (2010) Biophys. J. , vol.98 , pp. 2857-2866
    • Schow, E.V.1    Freites, J.A.2    Tobias, D.J.3
  • 45
    • 2342473866 scopus 로고    scopus 로고
    • Coarse grain models and the computer simulation of soft materials
    • Nielsen, S. O., C. F. Lopez, ..., M. L. Klein. 2004. Coarse grain models and the computer simulation of soft materials. J. Phys. Condens. Matter. 16: R481-R512.
    • (2004) J. Phys. Condens. Matter. , vol.16
    • Nielsen, S.O.1    Lopez, C.F.2    Klein, M.L.3
  • 46
    • 17844379740 scopus 로고    scopus 로고
    • Structure and dynamics of model pore insertion into a membrane
    • DOI 10.1529/biophysj.104.053769
    • Lopez, C. F., S. O. Nielsen, ..., M. L. Klein. 2005. Structure and dynamics of model pore insertion into a membrane. Biophys. J. 88:3083-3094. (Pubitemid 40586563)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3083-3094
    • Lopez, C.F.1    Nielsen, S.O.2    Ensing, B.3    Moore, P.B.4    Klein, M.L.5
  • 47
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J., A. H. de Vries, and A. E. Mark. 2004. Coarse grained model for semiquantitative lipid simulations. J. Phys. Chem. B. 108:750-760.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 48
    • 33644644163 scopus 로고    scopus 로고
    • Insertion and assembly of membrane proteins via simulation
    • DOI 10.1021/ja0569104
    • Bond, P. J., and M. S. P. Sansom. 2006. Insertion and assembly of membrane proteins via simulation. J. Am. Chem. Soc. 128:2697-2704. (Pubitemid 43327948)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.8 , pp. 2697-2704
    • Bond, P.J.1    Sansom, M.S.P.2
  • 49
    • 33847242278 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of membrane proteins and peptides
    • Bond, P. J., J. Holyoake, ..., M. S. Sansom. 2007. Coarse-grained molecular dynamics simulations of membrane proteins and peptides. J. Struct. Biol. 157:593-605.
    • (2007) J. Struct. Biol. , vol.157 , pp. 593-605
    • Bond, P.J.1    Holyoake, J.2    Sansom, M.S.3
  • 51
    • 41449119304 scopus 로고    scopus 로고
    • Coarse-Grained MD Simulations of Membrane Protein-Bilayer Self-Assembly
    • DOI 10.1016/j.str.2008.01.014, PII S0969212608000683
    • Scott, K. A., P. J. Bond, ..., M. S. P. Sansom. 2008. Coarse-grained MD simulations of membrane protein-bilayer self-assembly. Structure. 16:621-630. (Pubitemid 351458703)
    • (2008) Structure , vol.16 , Issue.4 , pp. 621-630
    • Scott, K.A.1    Bond, P.J.2    Ivetac, A.3    Chetwynd, A.P.4    Khalid, S.5    Sansom, M.S.P.6
  • 52
    • 45949109759 scopus 로고    scopus 로고
    • Gating motions in voltage-gated potassium channels revealed by coarse-grained molecular dynamics simulations
    • Treptow, W., S.-J. Marrink, and M. Tarek. 2008. Gating motions in voltage-gated potassium channels revealed by coarse-grained molecular dynamics simulations. J. Phys. Chem. B. 112:3277-3282.
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 3277-3282
    • Treptow, W.1    Marrink, S.-J.2    Tarek, M.3
  • 53
    • 64749106745 scopus 로고    scopus 로고
    • Systematic multiscale simulation of membrane protein systems
    • Ayton, G. S., and G. A. Voth. 2009. Systematic multiscale simulation of membrane protein systems. Curr. Opin. Struct. Biol. 19:138-144.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 138-144
    • Ayton, G.S.1    Voth, G.A.2
  • 55
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh, K., K. Misawa, ..., T. Miyata. 2002. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 30:3059-3066. (Pubitemid 34851225)
    • (2002) Nucleic Acids Research , vol.30 , Issue.14 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.-I.3    Miyata, T.4
  • 56
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and J. G. Henikoff. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA. 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 57
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • DOI 10.1006/jmbi.2001.4762
    • Shi, J., T. L. Blundell, and K. Mizuguchi. 2001. FUGUE: sequencestructure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310:243-257. (Pubitemid 32619966)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.1 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 58
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A., and T. L. Blundell. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815. (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 60
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • DOI 10.1002/prot.340170404
    • Sippl, M. J. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins. 17:355-362. (Pubitemid 23358545)
    • (1993) Proteins: Structure, Function and Genetics , vol.17 , Issue.4 , pp. 355-362
    • Sippl, M.J.1
  • 61
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R., J. U. Bowie, and D. Eisenberg. 1992. Assessment of protein models with three-dimensional profiles. Nature. 356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 62
    • 12344295462 scopus 로고    scopus 로고
    • ViTO: Tool for refinement of protein sequence-structure alignments
    • DOI 10.1093/bioinformatics/bth429
    • Catherinot, V., and G. Labesse. 2004. ViTO: tool for refinement of protein sequence-structure alignments. Bioinformatics. 20:3694-3696. (Pubitemid 40136819)
    • (2004) Bioinformatics , vol.20 , Issue.18 , pp. 3694-3696
    • Catherinot, V.1    Labesse, G.2
  • 63
    • 53249150686 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer
    • Bond, P. J., C. L. Wee, and M. S. P. Sansom. 2008. Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer. Biochemistry. 47:11321-11331.
    • (2008) Biochemistry , vol.47 , pp. 11321-11331
    • Bond, P.J.1    Wee, C.L.2    Sansom, M.S.P.3
  • 64
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • DOI 10.1007/S008940100045
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317. (Pubitemid 36153547)
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 66
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H. J. C., J. P. M. Postma, ..., J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81:3684-3690.
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 67
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • DOI 10.1126/science.1065635
    • Ren, D. J., B. Navarro, ..., D. E. Clapham. 2001. A prokaryotic voltage-gated sodium channel. Science. 294:2372-2375. (Pubitemid 33140564)
    • (2001) Science , vol.294 , Issue.5550 , pp. 2372-2375
    • Ren, D.1    Navarro, B.2    Xu, H.3    Yue, L.4    Shi, Q.5    Clapham, D.E.6
  • 69
    • 34548557186 scopus 로고    scopus 로고
    • Properties of mixed DOTAP - DPPC bilayer membranes as reported by differential scanning calorimetry and dynamic light scattering measurements
    • DOI 10.1021/jp071722g
    • Cinelli, S., G. Onori, ..., M. Diociaiuti. 2007. Properties of mixed DO-TAP-DPPC bilayer membranes as reported by differential scanning calorimetry and dynamic light scattering measurements. J. Phys. Chem. B. 111:10032-10039. (Pubitemid 47387889)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.33 , pp. 10032-10039
    • Cinelli, S.1    Onori, G.2    Zuzzi, S.3    Bordi, F.4    Cametti, C.5    Sennato, S.6    Diociaiuti, M.7
  • 70
    • 70349436810 scopus 로고    scopus 로고
    • Protein contents in biological membranes can explain abnormal solvation of charged and polar residues
    • Johansson, A. C. V., and E. Lindahl. 2009. Protein contents in biological membranes can explain abnormal solvation of charged and polar residues. Proc. Natl. Acad. Sci. USA. 106:15684-15689.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15684-15689
    • Johansson, A.C.V.1    Lindahl, E.2
  • 75
    • 0033576706 scopus 로고    scopus 로고
    • Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel
    • Glauner, K. S., L. M. Mannuzzu, ..., E. Y. Isacoff. 1999. Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel. Nature. 402:813-817.
    • (1999) Nature , vol.402 , pp. 813-817
    • Glauner, K.S.1    Mannuzzu, L.M.2    Isacoff, E.Y.3
  • 76
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • Cha, A., G. E. Snyder, ..., F. Bezanilla. 1999. Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature. 402:809-813.
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Bezanilla, F.3
  • 77
    • 46149091062 scopus 로고    scopus 로고
    • + Channels
    • DOI 10.1016/j.neuron.2008.05.006, PII S0896627308004157
    • + channels. Neuron. 59:98-109. (Pubitemid 351905849)
    • (2008) Neuron , vol.59 , Issue.1 , pp. 98-109
    • Posson, D.J.1    Selvin, P.R.2
  • 79
    • 0037167878 scopus 로고    scopus 로고
    • Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages
    • DOI 10.1038/nature01038
    • Männikkö, R., F. Elinder, and H. P. Larsson. 2002. Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages. Nature. 419:837-841. (Pubitemid 35238569)
    • (2002) Nature , vol.419 , Issue.6909 , pp. 837-841
    • Mannikko, R.1    Elinder, F.2    Larsson, H.P.3
  • 80
    • 33748125213 scopus 로고    scopus 로고
    • Reversal of HCN channel voltage dependence via bridging of the S4-S5 linker and post-S6
    • DOI 10.1085/jgp.200609590
    • Prole, D. L., and G. Yellen. 2006. Reversal of HCN channel voltage dependence via bridging of the S4-S5 linker and Post-S6. J. Gen. Physiol. 128:273-282. (Pubitemid 44306707)
    • (2006) Journal of General Physiology , vol.128 , Issue.3 , pp. 273-282
    • Prole, D.L.1    Yellen, G.2
  • 81
    • 0036143456 scopus 로고    scopus 로고
    • Voltage-controlled gating at the intracellular entrance to a hyperpolarization-activated cation channel
    • DOI 10.1085/jgp.119.1.83
    • Rothberg, B. S., K. S. Shin, ..., G. Yellen. 2002. Voltage-controlled gating at the intracellular entrance to a hyperpolarization-activated cation channel. J. Gen. Physiol. 119:83-91. (Pubitemid 34074595)
    • (2002) Journal of General Physiology , vol.119 , Issue.1 , pp. 83-91
    • Rothberg, B.S.1    Shin, K.S.2    Phale, P.S.3    Yellen, G.4
  • 82
    • 0347302947 scopus 로고    scopus 로고
    • Changes in Local S4 Environment Provide a Voltage-sensing Mechanism for Mammalian Hyperpolarization-activated HCN Channels
    • DOI 10.1085/jgp.200308918
    • Bell, D. C., H. Yao, ..., S. A. Siegelbaum. 2004. Changes in local S4 environment provide a voltage-sensing mechanism for mammalian hyperpolarization-activated HCN channels. J. Gen. Physiol. 123:5-19. (Pubitemid 38082783)
    • (2004) Journal of General Physiology , vol.123 , Issue.1 , pp. 5-19
    • Bell, D.C.1    Yao, H.2    Saenger, R.C.3    Riley, J.H.4    Siegelbaum, S.A.5
  • 83
    • 33750975638 scopus 로고    scopus 로고
    • v Channel
    • DOI 10.1016/j.neuron.2006.10.005, PII S089662730600804X
    • Soler-Llavina, G. J., T. H. Chang, and K. J. Swartz. 2006. Functional interactions at the interface between voltage-sensing and pore domains in the Shaker Kv channel. Neuron. 52:623-634. (Pubitemid 44750565)
    • (2006) Neuron , vol.52 , Issue.4 , pp. 623-634
    • Soler-Llavina, G.J.1    Chang, T.-H.2    Swartz, K.J.3
  • 84
  • 85
    • 50549097744 scopus 로고    scopus 로고
    • Assessing atomistic and coarse-grained force fields for protein-lipid interactions: The formidable challenge of an ionizable side chain in a membrane
    • Vorobyov, I., L. Li, and T. W. Allen. 2008. Assessing atomistic and coarse-grained force fields for protein-lipid interactions: the formidable challenge of an ionizable side chain in a membrane. J. Phys. Chem. B. 112:9588-9602.
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 9588-9602
    • Vorobyov, I.1    Li, L.2    Allen, T.W.3
  • 86
    • 77952569092 scopus 로고    scopus 로고
    • Changes in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations
    • Vostrikov, V. V., B. A. Hall, ..., M. S. Sansom. 2010. Changes in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations. J. Am. Chem. Soc. 132:5803-5811.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5803-5811
    • Vostrikov, V.V.1    Hall, B.A.2    Sansom, M.S.3
  • 87
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • DOI 10.1016/j.bbamem.2004.05.012, PII S0005273604001592, Lipid-Protein Interactions
    • Lee, A. G. 2004. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta. 1666:62-87. (Pubitemid 39425199)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 62-87
    • Lee, A.G.1
  • 88
    • 55749104248 scopus 로고    scopus 로고
    • Embedded cholesterol in the nicotinic acetylcholine receptor
    • Brannigan, G., J. Hénin, ..., M. L. Klein. 2008. Embedded cholesterol in the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. USA. 105:14418-14423.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14418-14423
    • Brannigan, G.1    Hénin, J.2    Klein, M.L.3
  • 89
    • 77953453090 scopus 로고    scopus 로고
    • The action of cardiolipin on the bacterial translocon
    • Gold, V. A. M., A. Robson, ..., I. Collinson. 2010. The action of cardiolipin on the bacterial translocon. Proc. Natl. Acad. Sci. USA. 107:10044-10049.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 10044-10049
    • Gold, V.A.M.1    Robson, A.2    Collinson, I.3
  • 90
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe, H. J., T. J. Stevens, and S. Munro. 2010. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell. 142:158-169.
    • (2010) Cell. , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 91
    • 0022550940 scopus 로고
    • Identification of protein sequence homology by consensus template alignment
    • Taylor, W. R. 1986. Identification of protein sequence homology by consensus template alignment. J. Mol. Biol. 188:233-258.
    • (1986) J. Mol. Biol. , vol.188 , pp. 233-258
    • Taylor, W.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.