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Volumn 88, Issue 2, 2005, Pages 959-970

The transmembrane domain of the acetylcholine receptor: Insights from simulations on synthetic peptide models

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CHOLINERGIC RECEPTOR; DIMYRISTOYLPHOSPHATIDYLCHOLINE; HYDROCARBON; ION CHANNEL; NEUROTRANSMITTER; NICOTINIC RECEPTOR; SYNTHETIC PEPTIDE; PEPTIDE;

EID: 21244436322     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.049726     Document Type: Article
Times cited : (20)

References (77)
  • 1
    • 0242573122 scopus 로고    scopus 로고
    • Aquaporin water channels: Molecular mechanisms for human diseases
    • Agre, P., and D. Kozono. 2003. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 555:72-78.
    • (2003) FEBS Lett. , vol.555 , pp. 72-78
    • Agre, P.1    Kozono, D.2
  • 2
    • 0027987062 scopus 로고
    • Identification of acetylcholine-receptor channel-lining residues in the entire M2 segment of the α subunit
    • Akabas, M. H., C. Kaufmann, P. Archdeacon, and A. Karlin. 1994. Identification of acetylcholine-receptor channel-lining residues in the entire M2 segment of the α subunit. Neuron. 13:919-927.
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 3
    • 0037152843 scopus 로고    scopus 로고
    • Intermittent permeation of cylindrical nanopores by water
    • Allen, R., S. Melchionna, and J. P. Hansen. 2002. Intermittent permeation of cylindrical nanopores by water. Phys. Rev. Lett. 89:175502.
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 175502
    • Allen, R.1    Melchionna, S.2    Hansen, J.P.3
  • 5
    • 0142073070 scopus 로고    scopus 로고
    • A prokaryotic glutamate receptor: Homology modelling and molecular dynamics simulations of GluR0
    • Arinaminpathy, Y., P. C. Biggin, I. H. Shrivastava, and M. S. P. Sansom. 2003. A prokaryotic glutamate receptor: homology modelling and molecular dynamics simulations of GluR0. FEBS Lett. 553:321-327.
    • (2003) FEBS Lett. , vol.553 , pp. 321-327
    • Arinaminpathy, Y.1    Biggin, P.C.2    Shrivastava, I.H.3    Sansom, M.S.P.4
  • 6
    • 0035963778 scopus 로고    scopus 로고
    • Molecular dynamics study of the effect of surfactant on a biomembrane
    • Bandyopadhyay, S., J. Shelley, and M. L. Klein. 2001. Molecular dynamics study of the effect of surfactant on a biomembrane. J. Phys. Chem. B. 105:5979-5986.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5979-5986
    • Bandyopadhyay, S.1    Shelley, J.2    Klein, M.L.3
  • 7
    • 0142027322 scopus 로고    scopus 로고
    • Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains
    • Barrantes, F. J. 2003. Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains. Curr. Opin. Drug Disc. 6:620-632.
    • (2003) Curr. Opin. Drug Disc. , vol.6 , pp. 620-632
    • Barrantes, F.J.1
  • 8
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass, R. B., P. Strop, M. T. Barclay, and D. C. Rees. 2002. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science. 298:1582-1587.
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.T.3    Rees, D.C.4
  • 9
    • 0038472282 scopus 로고    scopus 로고
    • Liquid-vapor oscillations of water in hydrophobic nanopores
    • Beckstein, O., and M. S. P. Sansom. 2003. Liquid-vapor oscillations of water in hydrophobic nanopores. Proc. Natl. Acad. Sci. USA. 100:7063-7068.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7063-7068
    • Beckstein, O.1    Sansom, M.S.P.2
  • 11
    • 0037159727 scopus 로고    scopus 로고
    • Force and voltage sensors in one structure
    • Bezanilla, F., and E. Perozo. 2002. Force and voltage sensors in one structure. Science. 298:1562-1363.
    • (2002) Science , vol.298 , pp. 1562-11363
    • Bezanilla, F.1    Perozo, E.2
  • 12
    • 0002128853 scopus 로고    scopus 로고
    • Evolution of membranes from a physics perspective
    • Bloom, M. 1998. Evolution of membranes from a physics perspective. Biol. Skr. Dan. Vid. Selsk. 49:13-17.
    • (1998) Biol. Skr. Dan. Vid. Selsk. , vol.49 , pp. 13-17
    • Bloom, M.1
  • 13
    • 0035996998 scopus 로고    scopus 로고
    • OmpA: A pore or not a pore? Simulation and modeling studies
    • Bond, P. J., J. D. Faraldo-Gómez, and M. S. P. Sansom. 2002. OmpA: a pore or not a pore? Simulation and modeling studies. Biophys. J. 83:763-775.
    • (2002) Biophys. J. , vol.83 , pp. 763-775
    • Bond, P.J.1    Faraldo-Gómez, J.D.2    Sansom, M.S.P.3
  • 14
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an Ach-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., W. J. van Dijk, R. V. Klaassen, M. Schuurmans, J. van der Oost, A. B. Smit, and T. K. Sixma. 2001. Crystal structure of an Ach-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature. 411:269-276.
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    Van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    Van Der Oost, J.5    Smit, A.B.6    Sixma, T.K.7
  • 15
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • Brown, M. F. 1994. Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids. 73:159-180.
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 16
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang, G., R. H. Spencer, A. T. Lee, M. T. Barclay, and D. C. Rees. 1998. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 17
    • 0027443270 scopus 로고
    • Chemical signaling in the brain
    • Changeux, J. P. 1993. Chemical signaling in the brain. Scien. Amer. 1:58-62.
    • (1993) Scien. Amer. , vol.1 , pp. 58-62
    • Changeux, J.P.1
  • 18
    • 0033119869 scopus 로고    scopus 로고
    • Mutational analysis of the charge selectivity filter of the alpha 7 nicotinic acetylcholine receptor
    • Corringer, P. J., S. Bertrand, J. L. Galzi, A. Devillers-Thiery, J. P. Changeux, and D. Bertrand. 1999. Mutational analysis of the charge selectivity filter of the alpha 7 nicotinic acetylcholine receptor. Neuron. 22:831-843.
    • (1999) Neuron , vol.22 , pp. 831-843
    • Corringer, P.J.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiery, A.4    Changeux, J.P.5    Bertrand, D.6
  • 20
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 22
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 a reveals the molecular basis of anion selectivity
    • Dutzler, R., E. B. Campbell, M. Cadene, B. T. Chait, and R. MacKinnon. 2002. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature. 415:287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 23
    • 1842682281 scopus 로고    scopus 로고
    • Electric field-controlled water permeation coupled to ion transport through a nanopore
    • Dzubiella, J., R. Allen, and J. P. Hansen. 2004. Electric field-controlled water permeation coupled to ion transport through a nanopore. J. Chem. Phys. 120:5001-5004.
    • (2004) J. Chem. Phys. , vol.120 , pp. 5001-5004
    • Dzubiella, J.1    Allen, R.2    Hansen, J.P.3
  • 24
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S. E., and A. D. MacKerell Jr. 2000. An improved empirical potential energy function for molecular simulations of phospholipids. J. Phys. Chem. B. 104:7510-7515.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell Jr., A.D.2
  • 25
    • 0035900249 scopus 로고    scopus 로고
    • Arginine-phosphate salt bridges in protein-DNA complexes: A Car-Parrinello study
    • Frigyes, D., F. Alber, S. Pongor, and P. Carloni. 2001. Arginine-phosphate salt bridges in protein-DNA complexes: a Car-Parrinello study. J. Mol. Struct. 574:39-45.
    • (2001) J. Mol. Struct. , vol.574 , pp. 39-45
    • Frigyes, D.1    Alber, F.2    Pongor, S.3    Carloni, P.4
  • 26
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • Galzi, J. L., A. Devillers-Thiery, N. Hussy, S. Bertrand, J. P. Changeux, and D. Bertrand. 1992. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature. 359:500-505.
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.L.1    Devillers-Thiery, A.2    Hussy, N.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 27
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • Grosman, C., M. Zhou, and A. Auerbach. 2000. Mapping the conformational wave of acetylcholine receptor channel gating. Nature. 403:773-776.
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 28
    • 2342472669 scopus 로고    scopus 로고
    • Oily barbarians breach ion channel gates
    • Hilgemann, D. W. 2004. Oily barbarians breach ion channel gates. Science. 304:223-224.
    • (2004) Science , vol.304 , pp. 223-224
    • Hilgemann, D.W.1
  • 30
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • Hummer, G., J. C. Rasaiah, and J. P. Noworyta. 2001. Water conduction through the hydrophobic channel of a carbon nanotube. Nature. 414:188-190.
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 31
    • 0029878720 scopus 로고    scopus 로고
    • VMD - Visual molecular dynamics
    • Humphrey, W., A. Dalke, and K. Schulten. 1996. VMD - visual molecular dynamics. J. Mol. Graph. 14:33-38. http://www.ks.uiuc.edu/Research/vmd/
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 32
    • 0035979711 scopus 로고    scopus 로고
    • Neuronal nicotinic receptors: From protein structure to function
    • Jtier, V., and D. Bertrand. 2001. Neuronal nicotinic receptors: from protein structure to function. FEBS Lett. 504:118-125.
    • (2001) FEBS Lett. , vol.504 , pp. 118-125
    • Jtier, V.1    Bertrand, D.2
  • 34
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B. T. Chait, and R. MacKinnon. 2002b. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 38
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A. 2002. Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 3:102-114.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 39
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of the nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and A. Akabas. 1995. Toward a structural basis for the function of the nicotinic acetylcholine receptors and their cousins. Neuron. 15:1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, A.2
  • 40
    • 0041806486 scopus 로고    scopus 로고
    • A cytoplasmic region determines single-channel conductance in 5-HT3 receptors
    • Kelley, S. P., J. I. Dunlop, E. F. Kirkness, J. J. Lambert, and J. A. Peters. 2003. A cytoplasmic region determines single-channel conductance in 5-HT3 receptors. Nature. 424:321-324.
    • (2003) Nature , vol.424 , pp. 321-324
    • Kelley, S.P.1    Dunlop, J.I.2    Kirkness, E.F.3    Lambert, J.J.4    Peters, J.A.5
  • 41
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • Killian, J. A. 2003. Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett. 555:134-138.
    • (2003) FEBS Lett. , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 43
    • 0033996292 scopus 로고    scopus 로고
    • Structure and dynamics of the pore-lining helix of the nicotinic acetylcholine receptor: MD simulations in water, lipid bilayers, and transbilayer bundles
    • Law, R. J., L. R. Forrest, K. M. Ranatunga, P. La Rocca, D. P. Tieleman, and M. S. P. Sansom. 2000. Structure and dynamics of the pore-lining helix of the nicotinic acetylcholine receptor: MD simulations in water, lipid bilayers, and transbilayer bundles. Proteins. 39:47-55.
    • (2000) Proteins , vol.39 , pp. 47-55
    • Law, R.J.1    Forrest, L.R.2    Ranatunga, K.M.3    La Rocca, P.4    Tieleman, D.P.5    Sansom, M.S.P.6
  • 44
    • 12244294449 scopus 로고    scopus 로고
    • Pores formed by the nicotinic receptor M2δ peptide: A molecular dynamics simulations study
    • Law, R. J., D. P. Tieleman, and M. S. P. Sansom. 2003. Pores formed by the nicotinic receptor M2δ peptide: a molecular dynamics simulations study. Biophys. J. 84:14-27.
    • (2003) Biophys. J. , vol.84 , pp. 14-27
    • Law, R.J.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 45
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J. D., Z. R. Wasserman, and W. F. DeGrado. 1988. Synthetic amphiphilic peptide models for protein ion channels. Science. 240:1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    Degrado, W.F.3
  • 46
    • 0034986892 scopus 로고    scopus 로고
    • Structure of ligand-gated ion channels: Critical assessment of biochemical data supports novel topology
    • Leite, J. F., and M. Cascio. 2001. Structure of ligand-gated ion channels: critical assessment of biochemical data supports novel topology. Mol. Cell. Neurosci. 17:777-792.
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 777-792
    • Leite, J.F.1    Cascio, M.2
  • 48
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • MacKinnon, R. 2003. Potassium channels. FEBS Lett. 555:62-65.
    • (2003) FEBS Lett. , vol.555 , pp. 62-65
    • MacKinnon, R.1
  • 49
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Y. Fujiyoshi, and N. Unwin. 2003. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 423:949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 50
    • 0029150299 scopus 로고
    • Design of molecular function: Channels of communication
    • Montal, M. 1995. Design of molecular function: channels of communication. Annu. Rev. Biophys. Biomol. Struct. 24:31-57.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 31-57
    • Montal, M.1
  • 51
    • 0037064250 scopus 로고    scopus 로고
    • The structure of the M2 channel-lining segment from the nicotinic acetylcholine receptor
    • Montal, M., and S. J. Opella. 2002. The structure of the M2 channel-lining segment from the nicotinic acetylcholine receptor. Biochim. Biophys. Acta. 1555:287-293.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 287-293
    • Montal, M.1    Opella, S.J.2
  • 52
    • 0027403316 scopus 로고
    • Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
    • Oblatt-Montal, M., T. Iwamoto, J. M. Tomich, and M. Montal. 1993. Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor. FEBS Lett. 320:261-266.
    • (1993) FEBS Lett. , vol.320 , pp. 261-266
    • Oblatt-Montal, M.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 53
    • 0010528163 scopus 로고
    • M2-δ, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor
    • Oiki, S., W. Danho, V. Madison, and M. Montal. 1988. M2-δ, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Proc. Natl. Acad. Sci. USA. 85:8703-8707.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8703-8707
    • Oiki, S.1    Danho, W.2    Madison, V.3    Montal, M.4
  • 54
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S. J., F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, and M. Montal. 1999. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6:374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 55
    • 0037678992 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl
    • Pandit, S. A., D. Bostick, and M. L. Berkowitz. 2003. Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl. Biophys. J. 84:3743-3750.
    • (2003) Biophys. J. , vol.84 , pp. 3743-3750
    • Pandit, S.A.1    Bostick, D.2    Berkowitz, M.L.3
  • 56
    • 0032811126 scopus 로고    scopus 로고
    • Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α-subunit
    • Pashkov, V. S., I. V. Maslennikove, L. D. Tchikin, R. G. Efremov, V. T. Ivanov, and A. S. Arseniev. 1999. Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α-subunit. FEBS Lett. 457:117-121.
    • (1999) FEBS Lett. , vol.457 , pp. 117-121
    • Pashkov, V.S.1    Maslennikove, I.V.2    Tchikin, L.D.3    Efremov, R.G.4    Ivanov, V.T.5    Arseniev, A.S.6
  • 57
    • 0036286853 scopus 로고    scopus 로고
    • Lipid bilayers, NMR relaxation, and computer simulations
    • Pastor, R. W., R. M. Venable, and S. E. Feller. 2002. Lipid bilayers, NMR relaxation, and computer simulations. Acc. Chem. Res. 35:438-446.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 438-446
    • Pastor, R.W.1    Venable, R.M.2    Feller, S.E.3
  • 58
    • 0038440700 scopus 로고    scopus 로고
    • Molecular dynamics simulations of lipid bilayers: Major artifacts due to truncating electrostatic interactions
    • Patra, M., M. Karttunen, M. Hyvonen, E. Falck, P. Lindqvist, and I. Vattulainen. 2003. Molecular dynamics simulations of lipid bilayers: major artifacts due to truncating electrostatic interactions. Biophys. J. 84:3636-3645.
    • (2003) Biophys. J. , vol.84 , pp. 3636-3645
    • Patra, M.1    Karttunen, M.2    Hyvonen, M.3    Falck, E.4    Lindqvist, P.5    Vattulainen, I.6
  • 59
    • 0036280795 scopus 로고    scopus 로고
    • Computational studies of the gramicidin channel
    • Roux, B. 2002. Computational studies of the gramicidin channel. Acc. Chem. Res. 35:366-375.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 366-375
    • Roux, B.1
  • 60
    • 0036555117 scopus 로고    scopus 로고
    • Towards an understanding of complex biological membranes from atomistic molecular dynamics simulations
    • Saiz, L., S. Bandyopadhyay, and M. L. Klein. 2002. Towards an understanding of complex biological membranes from atomistic molecular dynamics simulations. Bioscience Rep. 22:151-173.
    • (2002) Bioscience Rep. , vol.22 , pp. 151-173
    • Saiz, L.1    Bandyopadhyay, S.2    Klein, M.L.3
  • 61
    • 1542365497 scopus 로고    scopus 로고
    • Effect of the pore region of a transmembrane ion-channel on the physical properties of a simple membrane
    • Saiz, L., S. Bandyopadhyay, and M. L. Klein. 2004. Effect of the pore region of a transmembrane ion-channel on the physical properties of a simple membrane. J. Phys. Chem. B. 108:2608-2613.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2608-2613
    • Saiz, L.1    Bandyopadhyay, S.2    Klein, M.L.3
  • 62
    • 0036286655 scopus 로고    scopus 로고
    • Computer simulation studies of model biological membranes
    • Saiz, L., and M. L. Klein. 2002. Computer simulation studies of model biological membranes. Acc. Chem. Res. 35:482-489.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 482-489
    • Saiz, L.1    Klein, M.L.2
  • 63
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: The role of prolines in signalling via transmembrane alpha-helices
    • Sansom, M. S. P., and H. Weinstein. 2000. Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices. Trends Pharmacol. Sci. 21:445-451.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.P.1    Weinstein, H.2
  • 67
    • 0035312897 scopus 로고    scopus 로고
    • Electrostatics calculations: Recent methodological advances and applications to membranes
    • Tobias, D. J. 2001. Electrostatics calculations: recent methodological advances and applications to membranes. Curr. Op. Struct. Bio. 11:253-261.
    • (2001) Curr. Op. Struct. Bio. , vol.11 , pp. 253-261
    • Tobias, D.J.1
  • 68
    • 0024290709 scopus 로고
    • Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membranes
    • Toyoshima, C., and N. Unwin. 1988. Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membranes. Nature. 336:247-250.
    • (1988) Nature , vol.336 , pp. 247-250
    • Toyoshima, C.1    Unwin, N.2
  • 69
    • 33646650705 scopus 로고
    • Reversible multiple time scale molecular dynamics
    • Tuckerman, M. E., B. J. Berne, and G. J. Martyna. 1992. Reversible multiple time scale molecular dynamics. J. Chem. Phys. 97:1990-2001.
    • (1992) J. Chem. Phys. , vol.97 , pp. 1990-2001
    • Tuckerman, M.E.1    Berne, B.J.2    Martyna, G.J.3
  • 70
    • 0034625286 scopus 로고    scopus 로고
    • Exploiting multiple levels of parallelism in molecular dynamics based calculations via modern techniques and software paradigms on distributed memory computers
    • Tuckerman, M. E., D. A. Yarne, S. O. Samuelson, A. L. Hughes, and G. J. Martyna. 2000. Exploiting multiple levels of parallelism in molecular dynamics based calculations via modern techniques and software paradigms on distributed memory computers. Comput. Phys. Commun. 128:333-376.
    • (2000) Comput. Phys. Commun. , vol.128 , pp. 333-376
    • Tuckerman, M.E.1    Yarne, D.A.2    Samuelson, S.O.3    Hughes, A.L.4    Martyna, G.J.5
  • 71
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. 1993. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 72
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. 1995. Acetylcholine receptor channel imaged in the open state. Nature. 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 73
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • Unwin, N. 2003. Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy. FEBS Lett. 555:91-95.
    • (2003) FEBS Lett. , vol.555 , pp. 91-95
    • Unwin, N.1
  • 75
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • White, S. H., and M. C. Wiener. 1992. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys. J. 61:434-447.
    • (1992) Biophys. J. , vol.61 , pp. 434-447
    • White, S.H.1    Wiener, M.C.2
  • 77
    • 0034640212 scopus 로고    scopus 로고
    • Two possible conducting states of the influenza a virus M2 ion-channel
    • Zhong, Q. F., D. M. Newns, P. Pattnaik, J. D. Lear, and M. L. Klein. 2000. Two possible conducting states of the influenza A virus M2 ion-channel. FEBS Lett. 473:195-198.
    • (2000) FEBS Lett. , vol.473 , pp. 195-198
    • Zhong, Q.F.1    Newns, D.M.2    Pattnaik, P.3    Lear, J.D.4    Klein, M.L.5


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