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Volumn 1716, Issue 1, 2005, Pages 1-10

Computational analysis of mutations in the transmembrane region of Vpu from HIV-1

Author keywords

HIV 1; Molecular dynamics simulation; Mutant; Protein structure; Viral membrane protein; Vpu

Indexed keywords

VPU PROTEIN;

EID: 25444474166     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2005.07.012     Document Type: Article
Times cited : (9)

References (63)
  • 1
    • 0037079570 scopus 로고    scopus 로고
    • Computational alanine scanning of the 1:1 human growth hormone-receptor complex
    • S. Huo, I. Massova, and P.A. Kollman Computational alanine scanning of the 1:1 human growth hormone-receptor complex J. Comput. Chem. 23 2002 15 27
    • (2002) J. Comput. Chem. , vol.23 , pp. 15-27
    • Huo, S.1    Massova, I.2    Kollman, P.A.3
  • 2
    • 0036285982 scopus 로고    scopus 로고
    • Membrane structure of the human immunodeficiencey virus gp41 fusion domain by molecular dynamics simulations
    • S. Kamath, and T.C. Wong Membrane structure of the human immunodeficiencey virus gp41 fusion domain by molecular dynamics simulations Biophys. J. 83 2002 135 143
    • (2002) Biophys. J. , vol.83 , pp. 135-143
    • Kamath, S.1    Wong, T.C.2
  • 3
    • 0037427955 scopus 로고    scopus 로고
    • Membrane structure of the human immunodeficiency virus gp41 fusion peptide by molecular dynamics simulation: II. the glycine mutant
    • T.C. Wong Membrane structure of the human immunodeficiency virus gp41 fusion peptide by molecular dynamics simulation: II. The glycine mutant Biochim. Biophys. Acta 1609 2003 45 54
    • (2003) Biochim. Biophys. Acta , vol.1609 , pp. 45-54
    • Wong, T.C.1
  • 4
    • 0023677668 scopus 로고
    • Novel gene of HIV-1, vpu, and its 16-kilodalton product
    • K. Strebel, T. Klimkait, and M.A. Martin Novel gene of HIV-1, vpu, and its 16-kilodalton product Science 241 1988 1221 1223
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 5
    • 0023729963 scopus 로고
    • Identification of a protein encoded by the vpu gene of HIV-1
    • E.A. Cohen, E.F. Terwilliger, J.G. Sodroski, and W.A. Haseltine Identification of a protein encoded by the vpu gene of HIV-1 Nature 334 1988 532 534
    • (1988) Nature , vol.334 , pp. 532-534
    • Cohen, E.A.1    Terwilliger, E.F.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 6
    • 0027209705 scopus 로고
    • Human-immunodeficiency- virus type-1 Vpu protein is an oligomeric type-I integral membrane protein
    • F. Maldarelli, M.Y. Chen, R.L. Willey, and K. Strebel Human-immunodeficiency- virus type-1 Vpu protein is an oligomeric type-I integral membrane protein J. Virol. 67 1993 5056 5061
    • (1993) J. Virol. , vol.67 , pp. 5056-5061
    • Maldarelli, F.1    Chen, M.Y.2    Willey, R.L.3    Strebel, K.4
  • 7
  • 8
    • 0024381228 scopus 로고
    • Molecular and biochemical analysis of human deficiency virus type 1 vpu protein
    • K. Strebel, T. Klimkait, F. Maldarelli, and M.A. Martin Molecular and biochemical analysis of human deficiency virus type 1 vpu protein J. Virol. 63 1989 3784 3791
    • (1989) J. Virol. , vol.63 , pp. 3784-3791
    • Strebel, K.1    Klimkait, T.2    Maldarelli, F.3    Martin, M.A.4
  • 9
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • R.L. Willey, F. Maldarelli, M.A. Martin, and K. Strebel Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4 J. Virol. 66 1992 7193 7200
    • (1992) J. Virol. , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 10
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • U. Schubert, A.V. Ferrer-Montiel, M. Oblatt-Montal, P. Henklein, K. Strebel, and M. Montal Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells FEBS Lett. 398 1996 12 18
    • (1996) FEBS Lett. , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 11
    • 0028816432 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: Implications for the mechanism of degradation
    • S. Bour, U. Schubert, and K. Strebel The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation J. Virol. 69 1995 1510 1520
    • (1995) J. Virol. , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 12
    • 0030069139 scopus 로고    scopus 로고
    • The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains
    • U. Schubert, S. Bour, A.V. Ferrer-Montiel, M. Montal, F. Maldarelli, and K. Strebel The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains J. Virol. 70 1996 809 819
    • (1996) J. Virol. , vol.70 , pp. 809-819
    • Schubert, U.1    Bour, S.2    Ferrer-Montiel, A.V.3    Montal, M.4    Maldarelli, F.5    Strebel, K.6
  • 13
    • 0031908685 scopus 로고    scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Vpu transmembrane domain that promotes the enhanced release of virus-like particles from the plasma membrane of mammalian cells
    • M. Paul, S. Mazumder, N. Raja, and M.A. Jabbar Mutational analysis of the human immunodeficiency virus type 1 Vpu transmembrane domain that promotes the enhanced release of virus-like particles from the plasma membrane of mammalian cells J. Virol. 72 1998 1270 1279
    • (1998) J. Virol. , vol.72 , pp. 1270-1279
    • Paul, M.1    Mazumder, S.2    Raja, N.3    Jabbar, M.A.4
  • 15
    • 0029977571 scopus 로고    scopus 로고
    • Solution structure of the cytoplasmic domain of the human immunodeficiency virus type 1 encoded virus protein U (Vpu)
    • T. Federau, U. Schubert, J. Floßdorf, P. Henklein, D. Schomburg, and V. Wray Solution structure of the cytoplasmic domain of the human immunodeficiency virus type 1 encoded virus protein U (Vpu) Int. J. Pept. Protein Res. 47 1996 297 310
    • (1996) Int. J. Pept. Protein Res. , vol.47 , pp. 297-310
    • Federau, T.1    Schubert, U.2    Floßdorf, J.3    Henklein, P.4    Schomburg, D.5    Wray, V.6
  • 16
    • 0030943906 scopus 로고    scopus 로고
    • Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmatic domain in solution
    • D. Willbold, S. Hoffmann, and P. Rösch Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmatic domain in solution Eur. J. Biochem. 245 1997 581 588
    • (1997) Eur. J. Biochem. , vol.245 , pp. 581-588
    • Willbold, D.1    Hoffmann, S.2    Rösch, P.3
  • 18
    • 0033586794 scopus 로고    scopus 로고
    • Solution structure and orientation of the transmembrane anchor domain of the HIV-1-encoded virus protein U by high resolution and solid-state NMR spectroscopy
    • V. Wray, R. Kinder, T. Federau, P. Henklein, B. Bechinger, and U. Schubert Solution structure and orientation of the transmembrane anchor domain of the HIV-1-encoded virus protein U by high resolution and solid-state NMR spectroscopy Biochemistry 38 1999 5272 5282
    • (1999) Biochemistry , vol.38 , pp. 5272-5282
    • Wray, V.1    Kinder, R.2    Federau, T.3    Henklein, P.4    Bechinger, B.5    Schubert, U.6
  • 19
    • 0032819359 scopus 로고    scopus 로고
    • Vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching
    • A. Kukol, and I.T. Arkin Vpu transmembrane peptide structure obtained by site-specific Fourier transform infrared dichroism and global molecular dynamics searching Biophys. J. 77 1999 1594 1601
    • (1999) Biophys. J. , vol.77 , pp. 1594-1601
    • Kukol, A.1    Arkin, I.T.2
  • 20
    • 0032506276 scopus 로고    scopus 로고
    • Structural and functional analysis of the membrane-spanning domain of the Human Immunodeficiency Virus Type 1 Vpu protein
    • E. Tiganos, J. Friborg, B. Allain, N.G. Daniel, X.-J. Yao, and E.A. Cohen Structural and functional analysis of the membrane-spanning domain of the Human Immunodeficiency Virus Type 1 Vpu protein Virology 251 1998 96 107
    • (1998) Virology , vol.251 , pp. 96-107
    • Tiganos, E.1    Friborg, J.2    Allain, B.3    Daniel, N.G.4    Yao, X.-J.5    Cohen, E.A.6
  • 22
    • 0028070549 scopus 로고
    • Parallel helix bundles and ion channels: Molecular modelling via simulated annealing and restrained molecular dynamics
    • I.D. Kerr, R. Sankararamakrishnan, O.S. Smart, and M.S.P. Sansom Parallel helix bundles and ion channels: molecular modelling via simulated annealing and restrained molecular dynamics Biophys. J. 67 1994 1501 1515
    • (1994) Biophys. J. , vol.67 , pp. 1501-1515
    • Kerr, I.D.1    Sankararamakrishnan, R.2    Smart, O.S.3    Sansom, M.S.P.4
  • 25
    • 0037062579 scopus 로고    scopus 로고
    • Bundles consisting of extended transmembrane segments of Vpu from HIV-1: Computer simulations and conductance measurements
    • F.S. Cordes, A. Tustian, M.S.P. Sansom, A. Watts, and W.B. Fischer Bundles consisting of extended transmembrane segments of Vpu from HIV-1: computer simulations and conductance measurements Biochemistry 41 2002 7359 7365
    • (2002) Biochemistry , vol.41 , pp. 7359-7365
    • Cordes, F.S.1    Tustian, A.2    Sansom, M.S.P.3    Watts, A.4    Fischer, W.B.5
  • 26
    • 0032951553 scopus 로고    scopus 로고
    • Alamethicin helices in a bilayer and in solution: Molecular dynamics simulations
    • D.P. Tieleman, M.S.P. Sansom, and H.J.C. Berendsen Alamethicin helices in a bilayer and in solution: molecular dynamics simulations Biophys. J. 76 1999 40 49
    • (1999) Biophys. J. , vol.76 , pp. 40-49
    • Tieleman, D.P.1    Sansom, M.S.P.2    Berendsen, H.J.C.3
  • 27
    • 0032992048 scopus 로고    scopus 로고
    • Defining the transmembrane helix of M2 protein from influenza a by molecular dynamics simulations in a lipid bilayer
    • L.R. Forrest, D.P. Tieleman, and M.S.P. Sansom Defining the transmembrane helix of M2 protein from influenza A by molecular dynamics simulations in a lipid bilayer Biophys. J. 76 1999 1886 1896
    • (1999) Biophys. J. , vol.76 , pp. 1886-1896
    • Forrest, L.R.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 28
    • 0034030929 scopus 로고    scopus 로고
    • Exploring models of the influenza a M2 channel: MD simulations in a phospholipid bilayer
    • L.R. Forrest, A. Kukol, I.T. Arkin, D.P. Tieleman, and M.S. Sansom Exploring models of the influenza A M2 channel: MD simulations in a phospholipid bilayer Biophys. J. 78 2000 55 69
    • (2000) Biophys. J. , vol.78 , pp. 55-69
    • Forrest, L.R.1    Kukol, A.2    Arkin, I.T.3    Tieleman, D.P.4    Sansom, M.S.5
  • 30
    • 0030891182 scopus 로고    scopus 로고
    • Ion channels formed by HIV-1 Vpu: A modelling and simulation study
    • A.L. Grice, I.D. Kerr, and M.S.P. Sansom Ion channels formed by HIV-1 Vpu: a modelling and simulation study FEBS Lett. 405 1997 299 304
    • (1997) FEBS Lett. , vol.405 , pp. 299-304
    • Grice, A.L.1    Kerr, I.D.2    Sansom, M.S.P.3
  • 31
    • 0036708437 scopus 로고    scopus 로고
    • Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the Human Immunodeficiency Virus HIV-1
    • C.F. Lopez, M. Montal, J.K. Blasie, M.L. Klein, and P.B. Moore Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the Human Immunodeficiency Virus HIV-1 Biophys. J. 83 2002 1259 1267
    • (2002) Biophys. J. , vol.83 , pp. 1259-1267
    • Lopez, C.F.1    Montal, M.2    Blasie, J.K.3    Klein, M.L.4    Moore, P.B.5
  • 32
    • 0030404988 scopus 로고    scopus 로고
    • Hole: A program for the analysis of the pore dimensions of ion channel structural models
    • O.S. Smart, J.G. Neduvelil, X. Wang, B.A. Wallace, and M.S.P. Sansom Hole: a program for the analysis of the pore dimensions of ion channel structural models J. Mol. Graph. 14 1996 354 360
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5
  • 33
  • 34
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • N. Unwin Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy FEBS Lett. 555 2003 91 95
    • (2003) FEBS Lett. , vol.555 , pp. 91-95
    • Unwin, N.1
  • 35
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • G. Chang, R.H. Spencer, A.T. Lee, M.T. Barclay, and D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel Science 282 1998 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
  • 36
    • 0034613258 scopus 로고    scopus 로고
    • Correlating a protein structure with function of a bacterial mechanosensitive channel
    • P.C. Moe, G. Levin, and P. Blount Correlating a protein structure with function of a bacterial mechanosensitive channel J. Biol. Chem. 275 2000 31121 31127
    • (2000) J. Biol. Chem. , vol.275 , pp. 31121-31127
    • Moe, P.C.1    Levin, G.2    Blount, P.3
  • 37
    • 2142715470 scopus 로고    scopus 로고
    • Water dynamics and dewetting transitions in the small mechanosensitive channel MscS
    • A. Anishkin, and S. Sukharev Water dynamics and dewetting transitions in the small mechanosensitive channel MscS Biophys. J. 86 2004 2883 2895
    • (2004) Biophys. J. , vol.86 , pp. 2883-2895
    • Anishkin, A.1    Sukharev, S.2
  • 38
    • 0141645622 scopus 로고    scopus 로고
    • Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1
    • S.H. Park, A.A. Mrse, A.A. Nevzorov, M.F. Mesleh, M. Oblatt-Montal, M. Montal, and S.J. Opella Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1 J. Mol. Biol. 333 2003 409 424
    • (2003) J. Mol. Biol. , vol.333 , pp. 409-424
    • Park, S.H.1    Mrse, A.A.2    Nevzorov, A.A.3    Mesleh, M.F.4    Oblatt-Montal, M.5    Montal, M.6    Opella, S.J.7
  • 39
    • 1942502838 scopus 로고    scopus 로고
    • Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel
    • K. Hsu, J. Seharaseyon, P. Dong, S. Bour, and E. Marbán Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel Mol. Cell 14 2004 259 267
    • (2004) Mol. Cell , vol.14 , pp. 259-267
    • Hsu, K.1    Seharaseyon, J.2    Dong, P.3    Bour, S.4    Marbán, E.5
  • 41
    • 0035829539 scopus 로고    scopus 로고
    • Water conducting through the hydrophobic channel of a carbon nanotube
    • G. Hummer, J.C. Rasaiah, and J.P. Noworyta Water conducting through the hydrophobic channel of a carbon nanotube Nature 414 2001 188 190
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 42
    • 0041877629 scopus 로고    scopus 로고
    • Molecular dynamics investigation of water permeation through nanopores
    • R. Allen, J.-P. Hansen, and S. Melchionna Molecular dynamics investigation of water permeation through nanopores J. Chem. Phys. 119 2003 3905 3919
    • (2003) J. Chem. Phys. , vol.119 , pp. 3905-3919
    • Allen, R.1    Hansen, J.-P.2    Melchionna, S.3
  • 43
    • 33748573642 scopus 로고    scopus 로고
    • The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores
    • O. Beckstein, and M.S.P. Sansom The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores Phys. Biol. 1 2004 42 52
    • (2004) Phys. Biol. , vol.1 , pp. 42-52
    • Beckstein, O.1    Sansom, M.S.P.2
  • 44
    • 0025882246 scopus 로고
    • Ion transport in a model gramicidin channel: Structure and thermodynamics
    • B. Roux, and M. Karplus Ion transport in a model gramicidin channel: structure and thermodynamics Biophys. J. 59 1991 961 981
    • (1991) Biophys. J. , vol.59 , pp. 961-981
    • Roux, B.1    Karplus, M.2
  • 45
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • G.A. Woolley, and B.A. Wallace Model ion channels: gramicidin and alamethicin J. Membr. Biol. 129 1992 109 136
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 46
    • 0033061633 scopus 로고    scopus 로고
    • Simulation study of a gramicidin/lipid bilayer system in excess water and lipid: I. Structure of the molecular complex
    • S.-W. Chiu, S. Subramaniam, and E. Jakobsson Simulation study of a gramicidin/lipid bilayer system in excess water and lipid: I. Structure of the molecular complex Biophys. J. 76 1999 1929 1938
    • (1999) Biophys. J. , vol.76 , pp. 1929-1938
    • Chiu, S.-W.1    Subramaniam, S.2    Jakobsson, E.3
  • 47
    • 0036109653 scopus 로고    scopus 로고
    • Water permeation through gramicidin A: Desformylation and the double helix: A molecular dynamics study
    • B.L. de Groot, D.P. Tieleman, P. Pohl, and H. Grubmüller Water permeation through gramicidin A: desformylation and the double helix: a molecular dynamics study Biophys. J. 82 2002 2934 2942
    • (2002) Biophys. J. , vol.82 , pp. 2934-2942
    • De Groot, B.L.1    Tieleman, D.P.2    Pohl, P.3    Grubmüller, H.4
  • 48
    • 0000951252 scopus 로고    scopus 로고
    • Effect of electrostatic force truncation on interfacial and transport properties of water
    • S.E. Feller, R.W. Pastor, A. Rojnuckarin, S. Bogusz, and B.R. Brooks Effect of electrostatic force truncation on interfacial and transport properties of water J. Phys. Chem. 100 1996 17011 17020
    • (1996) J. Phys. Chem. , vol.100 , pp. 17011-17020
    • Feller, S.E.1    Pastor, R.W.2    Rojnuckarin, A.3    Bogusz, S.4    Brooks, B.R.5
  • 50
    • 0001029719 scopus 로고
    • On finite-size effects in computer simulations using the Ewald potential
    • F. Figueirido, G.S. Del Buono, and R.M. Levy On finite-size effects in computer simulations using the Ewald potential J. Chem. Phys. 103 1995 6133 6142
    • (1995) J. Chem. Phys. , vol.103 , pp. 6133-6142
    • Figueirido, F.1    Del Buono, G.S.2    Levy, R.M.3
  • 51
    • 0001490366 scopus 로고    scopus 로고
    • Calculating electrostatic interactions using the particle-particle particle-mesh method with nonperiodic long-range interactions
    • B.A. Luty, and W.F. van Gunsteren Calculating electrostatic interactions using the particle-particle particle-mesh method with nonperiodic long-range interactions J. Phys. Chem. 100 1996 2581 2587
    • (1996) J. Phys. Chem. , vol.100 , pp. 2581-2587
    • Luty, B.A.1    Van Gunsteren, W.F.2
  • 53
    • 0026755515 scopus 로고
    • Cutoff size does strongly influence molecular dynamics results on solvated polypeptides
    • H. Schreiber, and O. Steinhauser Cutoff size does strongly influence molecular dynamics results on solvated polypeptides Biochemistry 31 1992 5856 5860
    • (1992) Biochemistry , vol.31 , pp. 5856-5860
    • Schreiber, H.1    Steinhauser, O.2
  • 55
    • 0000112790 scopus 로고    scopus 로고
    • Ewald artifacts in liquid state molecular dynamics simulations
    • P.E. Smith, and B.M. Pettitt Ewald artifacts in liquid state molecular dynamics simulations J. Chem. Phys. 105 1996 4289 4293
    • (1996) J. Chem. Phys. , vol.105 , pp. 4289-4293
    • Smith, P.E.1    Pettitt, B.M.2
  • 56
    • 0001476142 scopus 로고    scopus 로고
    • On the presence of rotational Ewald artifacts in the equilibrium and dynamical properties of a zwitterionic tetrapeptide in aqueous solution
    • P.E. Smith, H.D. Blatt, and B.M. Pettitt On the presence of rotational Ewald artifacts in the equilibrium and dynamical properties of a zwitterionic tetrapeptide in aqueous solution J. Phys. Chem. B 101 1997 3886 3890
    • (1997) J. Phys. Chem. B , vol.101 , pp. 3886-3890
    • Smith, P.E.1    Blatt, H.D.2    Pettitt, B.M.3
  • 57
    • 0037007814 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a K channel model: Sensitivity to changes in ions, waters, and membrane environment
    • C.E. Capener, and M.S.P. Sansom Molecular dynamics simulations of a K channel model: sensitivity to changes in ions, waters, and membrane environment J. Phys. Chem. B 106 2002 4543 4551
    • (2002) J. Phys. Chem. B , vol.106 , pp. 4543-4551
    • Capener, C.E.1    Sansom, M.S.P.2
  • 58
    • 0039179572 scopus 로고    scopus 로고
    • Ion channels, permeation, and electrostatics: Insight into the function of KcsA
    • B. Roux, S. Berneche, and W. Im Ion channels, permeation, and electrostatics: insight into the function of KcsA Biochemistry 39 2000 13295 13306
    • (2000) Biochemistry , vol.39 , pp. 13295-13306
    • Roux, B.1    Berneche, S.2    Im, W.3
  • 59
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • N. Unwin Nicotinic acetylcholine receptor at 9 Å resolution J. Mol. Biol. 229 1993 1101 1124
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 60
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • N. Unwin Acetylcholine receptor channel imaged in the open state Nature 373 1995 37 43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1


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