메뉴 건너뛰기




Volumn 8, Issue 9, 2012, Pages

The p7 Protein of Hepatitis C Virus Forms Structurally Plastic, Minimalist Ion Channels

Author keywords

[No Author keywords available]

Indexed keywords

IONS; MOLECULAR DYNAMICS; PROTEINS; SELF ASSEMBLY; VIRUSES;

EID: 84866943211     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002702     Document Type: Article
Times cited : (60)

References (73)
  • 1
    • 23944506014 scopus 로고    scopus 로고
    • Global epidemiology of hepatitis C virus infection
    • Shepard C, Finelli L, Alter M, (2005) Global epidemiology of hepatitis C virus infection. Lancet Infect Dis 5: 558-567.
    • (2005) Lancet Infect Dis , vol.5 , pp. 558-567
    • Shepard, C.1    Finelli, L.2    Alter, M.3
  • 2
    • 59149085501 scopus 로고    scopus 로고
    • The global burden of hepatitis C
    • Lavanchy D, (2009) The global burden of hepatitis C. Liver Int 29: 74-81.
    • (2009) Liver Int , vol.29 , pp. 74-81
    • Lavanchy, D.1
  • 3
    • 65449136656 scopus 로고    scopus 로고
    • Diagnosis, management, and treatment of hepatitis C: An update
    • Ghany MG, Strader DB, Thomas DL, Seeff LB, (2009) Diagnosis, management, and treatment of hepatitis C: An update. Hepatology 49: 1335-1374.
    • (2009) Hepatology , vol.49 , pp. 1335-1374
    • Ghany, M.G.1    Strader, D.B.2    Thomas, D.L.3    Seeff, L.B.4
  • 4
    • 25844523297 scopus 로고    scopus 로고
    • Consensus proposals for a unified system of nomenclature of hepatitis C virus genotypes
    • Simmonds P, Bukh J, Combet C, Deléage G, Enomoto N, et al. (2005) Consensus proposals for a unified system of nomenclature of hepatitis C virus genotypes. Hepatology 42: 962-973.
    • (2005) Hepatology , vol.42 , pp. 962-973
    • Simmonds, P.1    Bukh, J.2    Combet, C.3    Deléage, G.4    Enomoto, N.5
  • 5
    • 0034120427 scopus 로고    scopus 로고
    • Clinical significance of hepatitis C virus genotypes
    • Zein NN, (2000) Clinical significance of hepatitis C virus genotypes. Clin Microbiol Rev 13: 223-235.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 223-235
    • Zein, N.N.1
  • 6
    • 59149103417 scopus 로고    scopus 로고
    • Hepatitis B and hepatitis C in 2009
    • Marcellin P, (2009) Hepatitis B and hepatitis C in 2009. Liver Int 29: 1-8.
    • (2009) Liver Int , vol.29 , pp. 1-8
    • Marcellin, P.1
  • 7
    • 61949320778 scopus 로고    scopus 로고
    • Development and characterization of hepatitis C virus genotype 1-7 cell culture systems: role of CD81 and scavenger receptor class B type I and effect of antiviral drugs
    • Gottwein J, Scheel T, Jensen T, Lademann J, Prentoe J, et al. (2009) Development and characterization of hepatitis C virus genotype 1-7 cell culture systems: role of CD81 and scavenger receptor class B type I and effect of antiviral drugs. Hepatology 49: 364-377.
    • (2009) Hepatology , vol.49 , pp. 364-377
    • Gottwein, J.1    Scheel, T.2    Jensen, T.3    Lademann, J.4    Prentoe, J.5
  • 8
    • 75149151884 scopus 로고    scopus 로고
    • Resistance to direct antiviral agents in patients with hepatitis C virus infection
    • Sarrazin C, Zeuzem S, (2010) Resistance to direct antiviral agents in patients with hepatitis C virus infection. Gastroenterology 138: 447-462.
    • (2010) Gastroenterology , vol.138 , pp. 447-462
    • Sarrazin, C.1    Zeuzem, S.2
  • 9
    • 33845965324 scopus 로고    scopus 로고
    • Hepatitis C virus p7 membrane protein quasispecies variability in chronically infected patients treated with interferon and ribavirin, with or without amantadine
    • Castelain S, Bonte D, Penin F, François C, Capron D, et al. (2007) Hepatitis C virus p7 membrane protein quasispecies variability in chronically infected patients treated with interferon and ribavirin, with or without amantadine. J Med Virol 79: 144-154.
    • (2007) J Med Virol , vol.79 , pp. 144-154
    • Castelain, S.1    Bonte, D.2    Penin, F.3    François, C.4    Capron, D.5
  • 10
    • 79959569817 scopus 로고    scopus 로고
    • Resistance mutations define specific antiviral effects for inhibitors of the hepatitis C virus (HCV) p7 ion channel
    • Foster TL, Verow M, Wozniak AL, Bentham MJ, Thompson J, et al. (2011) Resistance mutations define specific antiviral effects for inhibitors of the hepatitis C virus (HCV) p7 ion channel. Hepatology 54: 79-90.
    • (2011) Hepatology , vol.54 , pp. 79-90
    • Foster, T.L.1    Verow, M.2    Wozniak, A.L.3    Bentham, M.J.4    Thompson, J.5
  • 11
    • 77951296857 scopus 로고    scopus 로고
    • A novel hepatitis C virus p7 ion channel inhibitor, BIT225, inhibits bovine viral diarrhea virus in vitro and shows synergism with recombinant interferon-α-2b and nucleoside analogues
    • Luscombe CA, Huang Z, Murray MG, Miller M, Wilkinson J, et al. (2010) A novel hepatitis C virus p7 ion channel inhibitor, BIT225, inhibits bovine viral diarrhea virus in vitro and shows synergism with recombinant interferon-α-2b and nucleoside analogues. Antiviral Res 86: 144-153.
    • (2010) Antiviral Res , vol.86 , pp. 144-153
    • Luscombe, C.A.1    Huang, Z.2    Murray, M.G.3    Miller, M.4    Wilkinson, J.5
  • 12
    • 0025217987 scopus 로고
    • Hepatitis C virus: the major causative agent of viral non-A, non-B hepatitis
    • Choo QL, Weiner AJ, Overby LR, Kuo G, Houghton M, et al. (1990) Hepatitis C virus: the major causative agent of viral non-A, non-B hepatitis. Br Med Bull 46: 423-441.
    • (1990) Br Med Bull , vol.46 , pp. 423-441
    • Choo, Q.L.1    Weiner, A.J.2    Overby, L.R.3    Kuo, G.4    Houghton, M.5
  • 13
    • 70349730223 scopus 로고    scopus 로고
    • The long and winding road leading to the identification of the hepatitis C virus
    • Houghton M, (2009) The long and winding road leading to the identification of the hepatitis C virus. J Hepatol 51: 939-948.
    • (2009) J Hepatol , vol.51 , pp. 939-948
    • Houghton, M.1
  • 15
    • 0037472806 scopus 로고    scopus 로고
    • The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug amantadine
    • Griffin SD, Beales LP, Clarke DS, Worsfold O, Evans SD, et al. (2003) The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug amantadine. FEBS Lett 535: 34-38.
    • (2003) FEBS Lett , vol.535 , pp. 34-38
    • Griffin, S.D.1    Beales, L.P.2    Clarke, D.S.3    Worsfold, O.4    Evans, S.D.5
  • 16
    • 77957789317 scopus 로고    scopus 로고
    • NMR structure and ion channel activity of the p7 protein from hepatitis C virus
    • Montserret R, Saint N, Vanbelle C, Salvay AG, Simorre JP, et al. (2010) NMR structure and ion channel activity of the p7 protein from hepatitis C virus. J Biol Chem 285: 31446-31461.
    • (2010) J Biol Chem , vol.285 , pp. 31446-31461
    • Montserret, R.1    Saint, N.2    Vanbelle, C.3    Salvay, A.G.4    Simorre, J.P.5
  • 17
    • 33846005485 scopus 로고    scopus 로고
    • Evidence for the formation of a heptameric ion channel complex by the hepatitis C virus p7 protein in vitro
    • Clarke D, Griffin S, Beales L, Gelais CS, Burgess S, et al. (2006) Evidence for the formation of a heptameric ion channel complex by the hepatitis C virus p7 protein in vitro. J Biol Chem 281: 37057-37068.
    • (2006) J Biol Chem , vol.281 , pp. 37057-37068
    • Clarke, D.1    Griffin, S.2    Beales, L.3    Gelais, C.S.4    Burgess, S.5
  • 18
    • 69149090877 scopus 로고    scopus 로고
    • The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopy
    • Luik P, Chew C, Aittoniemi J, Chang J, Jr PW, et al. (2009) The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopy. Proc Natl Acad Sci USA 106: 12712-12716.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12712-12716
    • Luik, P.1    Chew, C.2    Aittoniemi, J.3    Chang, J.4    Jr, P.W.5
  • 19
    • 0038284830 scopus 로고    scopus 로고
    • The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivatives
    • Pavlović D, Neville DCA, Argaud O, Blumberg B, Dwek RA, et al. (2003) The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivatives. Proc Natl Acad Sci USA 100: 6104-6108.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6104-6108
    • Pavlović, D.1    Neville, D.C.A.2    Argaud, O.3    Blumberg, B.4    Dwek, R.A.5
  • 20
    • 1642450632 scopus 로고    scopus 로고
    • Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride
    • Premkumar A, Wilson L, Ewart G, Gage P, (2004) Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride. FEBS Lett 557: 99-103.
    • (2004) FEBS Lett , vol.557 , pp. 99-103
    • Premkumar, A.1    Wilson, L.2    Ewart, G.3    Gage, P.4
  • 21
    • 34547418131 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus p7 membrane channels in a liposome-based assay system
    • StGelais C, Tuthill TJ, Clarke DS, Rowlands DJ, Harris M, et al. (2007) Inhibition of hepatitis C virus p7 membrane channels in a liposome-based assay system. Antiviral Res 76: 48-58.
    • (2007) Antiviral Res , vol.76 , pp. 48-58
    • StGelais, C.1    Tuthill, T.J.2    Clarke, D.S.3    Rowlands, D.J.4    Harris, M.5
  • 22
    • 67749139975 scopus 로고    scopus 로고
    • Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro
    • StGelais C, Foster TL, Verow M, Atkins E, Fishwick CWG, et al. (2009) Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro. J Virol 83: 7970-7981.
    • (2009) J Virol , vol.83 , pp. 7970-7981
    • StGelais, C.1    Foster, T.L.2    Verow, M.3    Atkins, E.4    Fishwick, C.W.G.5
  • 23
    • 0141816748 scopus 로고    scopus 로고
    • The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences
    • Sakai A, Claire MS, Faulk K, Govindarajan S, Emerson SU, et al. (2003) The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences. Proc Natl Acad Sci USA 100: 11646-11651.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11646-11651
    • Sakai, A.1    Claire, M.S.2    Faulk, K.3    Govindarajan, S.4    Emerson, S.U.5
  • 24
    • 34547734952 scopus 로고    scopus 로고
    • Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus
    • Jones CT, Murray CL, Eastman DK, Tassello J, Rice CM, (2007) Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus. J Virol 81: 8374-8383.
    • (2007) J Virol , vol.81 , pp. 8374-8383
    • Jones, C.T.1    Murray, C.L.2    Eastman, D.K.3    Tassello, J.4    Rice, C.M.5
  • 25
    • 34547616693 scopus 로고    scopus 로고
    • Hepatitis C virus p7 protein is crucial for assembly and release of infectious virions
    • Steinmann E, Penin F, Kallis S, Patel AH, Bartenschlager R, et al. (2007) Hepatitis C virus p7 protein is crucial for assembly and release of infectious virions. PLoS Pathog 3: 0962-0971.
    • (2007) PLoS Pathog , vol.3 , pp. 0962-0971
    • Steinmann, E.1    Penin, F.2    Kallis, S.3    Patel, A.H.4    Bartenschlager, R.5
  • 26
    • 78149341400 scopus 로고    scopus 로고
    • Intracellular proton conductance of the hepatitis C virus p7 protein and its contribution to infectious virus production
    • Wozniak AL, Griffin S, Rowlands D, Harris M, Yi M, et al. (2010) Intracellular proton conductance of the hepatitis C virus p7 protein and its contribution to infectious virus production. PLoS Pathog 6: 1-17.
    • (2010) PLoS Pathog , vol.6 , pp. 1-17
    • Wozniak, A.L.1    Griffin, S.2    Rowlands, D.3    Harris, M.4    Yi, M.5
  • 27
    • 79952131523 scopus 로고    scopus 로고
    • Hepatitis C virus p7 - a viroporin crucial for virus assembly and an emerging target for antiviral therapy
    • Steinmann E, Pietschmann T, (2010) Hepatitis C virus p7- a viroporin crucial for virus assembly and an emerging target for antiviral therapy. Viruses 2: 2078-2095.
    • (2010) Viruses , vol.2 , pp. 2078-2095
    • Steinmann, E.1    Pietschmann, T.2
  • 28
    • 78651252353 scopus 로고    scopus 로고
    • Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly
    • Jirasko V, Montserret R, Lee JY, Gouttenoire J, Moradpour D, et al. (2010) Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. PLoS Pathog 6: 1-22.
    • (2010) PLoS Pathog , vol.6 , pp. 1-22
    • Jirasko, V.1    Montserret, R.2    Lee, J.Y.3    Gouttenoire, J.4    Moradpour, D.5
  • 29
    • 78951472458 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes
    • Stapleford KA, Lindenbach BD, (2011) Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes. J Virol 85: 1706-1717.
    • (2011) J Virol , vol.85 , pp. 1706-1717
    • Stapleford, K.A.1    Lindenbach, B.D.2
  • 30
    • 77956397284 scopus 로고    scopus 로고
    • Role of lipid metabolism in hepatitis C virus assembly and entry
    • Popescu C, Dubuisson J, (2010) Role of lipid metabolism in hepatitis C virus assembly and entry. Biol Cell 102: 63-74.
    • (2010) Biol Cell , vol.102 , pp. 63-74
    • Popescu, C.1    Dubuisson, J.2
  • 31
    • 78650062692 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and non-structural proteins
    • Ma Y, Anantpadma M, Timpe JM, Shanmugam S, Singh SM, et al. (2011) Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and non-structural proteins. J Virol 85: 86-97.
    • (2011) J Virol , vol.85 , pp. 86-97
    • Ma, Y.1    Anantpadma, M.2    Timpe, J.M.3    Shanmugam, S.4    Singh, S.M.5
  • 32
    • 79955778897 scopus 로고    scopus 로고
    • The subcellular localization of the hepatitis C virus non-structural protein NS2 is regulated by an ion channel-independent function of the p7 protein
    • Tedbury P, Welbourn S, Pause A, King B, Griffin S, et al. (2011) The subcellular localization of the hepatitis C virus non-structural protein NS2 is regulated by an ion channel-independent function of the p7 protein. J Gen Virol 92: 819-830.
    • (2011) J Gen Virol , vol.92 , pp. 819-830
    • Tedbury, P.1    Welbourn, S.2    Pause, A.3    King, B.4    Griffin, S.5
  • 33
    • 79960951066 scopus 로고    scopus 로고
    • A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly
    • Boson B, Granio O, Bartenschlager R, Cosset FL, (2011) A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly. PLoS Pathog 7: e1002144-e1002144.
    • (2011) PLoS Pathog , vol.7
    • Boson, B.1    Granio, O.2    Bartenschlager, R.3    Cosset, F.L.4
  • 34
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of inuenza A virus
    • Schnell JR, Chou JJ, (2008) Structure and mechanism of the M2 proton channel of inuenza A virus. Nature 451: 591-596.
    • (2008) Nature , vol.451 , pp. 591-596
    • Schnell, J.R.1    Chou, J.J.2
  • 35
    • 78650261371 scopus 로고    scopus 로고
    • Viral proteins function as ion channels
    • Wang K, Xie S, Sun B, (2011) Viral proteins function as ion channels. Biochim Biophys Acta 1808: 510-515.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 510-515
    • Wang, K.1    Xie, S.2    Sun, B.3
  • 36
    • 0041834450 scopus 로고    scopus 로고
    • Demonstrating the intrinsic ion channel activity of virally encoded proteins
    • Kelly ML, Cook JA, Brown-Augsburger P, Heinz BA, Smith MC, et al. (2003) Demonstrating the intrinsic ion channel activity of virally encoded proteins. FEBS Lett 552: 61-67.
    • (2003) FEBS Lett , vol.552 , pp. 61-67
    • Kelly, M.L.1    Cook, J.A.2    Brown-Augsburger, P.3    Heinz, B.A.4    Smith, M.C.5
  • 39
    • 0037133750 scopus 로고    scopus 로고
    • Viral ion channels: structure and function
    • Fischer WB, Sansom MS, (2002) Viral ion channels: structure and function. Biochim Biophys Acta 1561: 27-45.
    • (2002) Biochim Biophys Acta , vol.1561 , pp. 27-45
    • Fischer, W.B.1    Sansom, M.S.2
  • 40
    • 39749180320 scopus 로고    scopus 로고
    • Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism
    • Mehnert T, Routh A, Judge PJ, Lam YH, Fischer D, et al. (2007) Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism. Proteins 70: 1488-1497.
    • (2007) Proteins , vol.70 , pp. 1488-1497
    • Mehnert, T.1    Routh, A.2    Judge, P.J.3    Lam, Y.H.4    Fischer, D.5
  • 41
    • 78650280529 scopus 로고    scopus 로고
    • Viral channel forming proteins - modeling the target
    • Fischer WB, Hsu HJ, (2011) Viral channel forming proteins- modeling the target. Biochim Biophys Acta 1808: 561-571.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 561-571
    • Fischer, W.B.1    Hsu, H.J.2
  • 43
    • 61549097231 scopus 로고    scopus 로고
    • Structural and functional analysis of the HCV p7 protein
    • Second Edition. Volume 510. Tang H, editor. New York: Humana Press
    • Saint N, Montserret R, Chipot C, Penin F (2009) Structural and functional analysis of the HCV p7 protein. In: Hepatitis C: Methods and Protocols. Second Edition. Volume 510. Tang H, editor. New York: Humana Press. pp. 125-143.
    • (2009) Hepatitis C: Methods and Protocols , pp. 125-143
    • Saint, N.1    Montserret, R.2    Chipot, C.3    Penin, F.4
  • 44
    • 77955655001 scopus 로고    scopus 로고
    • NMR studies of p7 protein from hepatitis C virus
    • Cook GA, Opella SJ, (2010) NMR studies of p7 protein from hepatitis C virus. Eur Biophys J 39: 1097-1104.
    • (2010) Eur Biophys J , vol.39 , pp. 1097-1104
    • Cook, G.A.1    Opella, S.J.2
  • 45
    • 79954824393 scopus 로고    scopus 로고
    • Secondary structure, dynamics, and architecture of the p7 membrane protein from hepatitis C virus by NMR spectroscopy
    • Cook GA, Opella SJ, (2011) Secondary structure, dynamics, and architecture of the p7 membrane protein from hepatitis C virus by NMR spectroscopy. Biochim Biophys Acta 1808: 1448-1453.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1448-1453
    • Cook, G.A.1    Opella, S.J.2
  • 46
    • 78650269727 scopus 로고    scopus 로고
    • Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1
    • Cook GA, Zhang H, Park SH, Wang Y, Opella SJ, (2010) Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1. Biochim Biophys Acta 1808: 554-560.
    • (2010) Biochim Biophys Acta , vol.1808 , pp. 554-560
    • Cook, G.A.1    Zhang, H.2    Park, S.H.3    Wang, Y.4    Opella, S.J.5
  • 47
    • 31544478873 scopus 로고    scopus 로고
    • Protein-protein interactions: Modeling the hepatitis C virus ion channel p7
    • Patargias G, Zitzmann N, Dwek R, Fischer WB, (2006) Protein-protein interactions: Modeling the hepatitis C virus ion channel p7. J Med Chem 49: 648-655.
    • (2006) J Med Chem , vol.49 , pp. 648-655
    • Patargias, G.1    Zitzmann, N.2    Dwek, R.3    Fischer, W.B.4
  • 48
    • 77957299044 scopus 로고    scopus 로고
    • Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers
    • Lu JX, Sharpe S, Ghirlando R, Yau WM, Tycko R, (2010) Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers. Protein Sci 19: 1877-1896.
    • (2010) Protein Sci , vol.19 , pp. 1877-1896
    • Lu, J.X.1    Sharpe, S.2    Ghirlando, R.3    Yau, W.M.4    Tycko, R.5
  • 49
    • 0042335653 scopus 로고    scopus 로고
    • Structure-function correlates of Vpu, a membrane protein of HIV-1
    • Montal M, (2003) Structure-function correlates of Vpu, a membrane protein of HIV-1. FEBS Lett 552: 47-53.
    • (2003) FEBS Lett , vol.552 , pp. 47-53
    • Montal, M.1
  • 50
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • Tieleman DP, Hess B, Sansom MSP, (2002) Analysis and evaluation of channel models: Simulations of alamethicin. Biophys J 83: 2393-2407.
    • (2002) Biophys J , vol.83 , pp. 2393-2407
    • Tieleman, D.P.1    Hess, B.2    Sansom, M.S.P.3
  • 51
    • 49149107480 scopus 로고    scopus 로고
    • A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine
    • Yi M, Cross TA, Zhou HX, (2008) A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine. J Phys Chem B 112: 7977-7979.
    • (2008) J Phys Chem B , vol.112 , pp. 7977-7979
    • Yi, M.1    Cross, T.A.2    Zhou, H.X.3
  • 52
    • 78751688849 scopus 로고    scopus 로고
    • High-performance scalable molecular dynamics simulations of a polarizable force field based on classical Drude oscillators in NAMD
    • Jiang W, Hardy D, Phillips J, MacKerell A, Schulten K, et al. (2011) High-performance scalable molecular dynamics simulations of a polarizable force field based on classical Drude oscillators in NAMD. J Phys Chem Lett 2: 87-92.
    • (2011) J Phys Chem Lett , vol.2 , pp. 87-92
    • Jiang, W.1    Hardy, D.2    Phillips, J.3    MacKerell, A.4    Schulten, K.5
  • 53
    • 84855431691 scopus 로고    scopus 로고
    • Improved parameterization of Li+, Na+, K+, and Mg2+ ions for all-atom molecular dynamics simulations of nucleic acid systems
    • Yoo J, Aksimentiev A, (2012) Improved parameterization of Li+, Na+, K+, and Mg2+ ions for all-atom molecular dynamics simulations of nucleic acid systems. J Phys Chem Lett 3: 45-50.
    • (2012) J Phys Chem Lett , vol.3 , pp. 45-50
    • Yoo, J.1    Aksimentiev, A.2
  • 54
    • 33646193716 scopus 로고    scopus 로고
    • Electrostatic properties of the mechanosensitive channel of small conductance MscS
    • Sotomayor M, van der Straaten TA, Ravaioli U, Schulten K, (2006) Electrostatic properties of the mechanosensitive channel of small conductance MscS. Biophys J 90: 3496-3510.
    • (2006) Biophys J , vol.90 , pp. 3496-3510
    • Sotomayor, M.1    van der Straaten, T.A.2    Ravaioli, U.3    Schulten, K.4
  • 55
    • 33846828514 scopus 로고    scopus 로고
    • Ion conduction through MscS as determined by electrophysiology and simulation
    • Sotomayor M, Vasquez V, Perozo E, Schulten K, (2007) Ion conduction through MscS as determined by electrophysiology and simulation. Biophys J 92: 886-902.
    • (2007) Biophys J , vol.92 , pp. 886-902
    • Sotomayor, M.1    Vasquez, V.2    Perozo, E.3    Schulten, K.4
  • 56
    • 70349267547 scopus 로고    scopus 로고
    • Molecular Dynamics Flexible Fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography
    • Trabuco LG, Villa E, Schreiner E, Harrison CB, Schulten K, (2009) Molecular Dynamics Flexible Fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography. Methods 49: 174-180.
    • (2009) Methods , vol.49 , pp. 174-180
    • Trabuco, L.G.1    Villa, E.2    Schreiner, E.3    Harrison, C.B.4    Schulten, K.5
  • 57
    • 59049096394 scopus 로고    scopus 로고
    • Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
    • Villa E, Sengupta J, Trabuco LG, LeBarron J, Baxter WT, et al. (2009) Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proc Natl Acad Sci USA 106: 1063-1068.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1063-1068
    • Villa, E.1    Sengupta, J.2    Trabuco, L.G.3    LeBarron, J.4    Baxter, W.T.5
  • 58
    • 71549124362 scopus 로고    scopus 로고
    • Structural insight into nascent polypeptide chain-mediated translational stalling
    • Seidelt B, Innis CA, Wilson DN, Gartmann M, Armache JP, et al. (2009) Structural insight into nascent polypeptide chain-mediated translational stalling. Science 326: 1412-1415.
    • (2009) Science , vol.326 , pp. 1412-1415
    • Seidelt, B.1    Innis, C.A.2    Wilson, D.N.3    Gartmann, M.4    Armache, J.P.5
  • 60
    • 52649086195 scopus 로고    scopus 로고
    • Exploring the conformational space of Vpu from HIV-1: A versatile and adaptable protein
    • Krüger J, Fischer WB, (2008) Exploring the conformational space of Vpu from HIV-1: A versatile and adaptable protein. J Comp Chem 29: 2416-2424.
    • (2008) J Comp Chem , vol.29 , pp. 2416-2424
    • Krüger, J.1    Fischer, W.B.2
  • 61
    • 79960631284 scopus 로고    scopus 로고
    • The inuence of different lipid environments on the structure and function of the hepatitis C virus p7 ion channel protein
    • Whitfield T, Miles AJ, Scheinost JC, Offer J, Wentworth P, et al. (2011) The inuence of different lipid environments on the structure and function of the hepatitis C virus p7 ion channel protein. Mol Membr Biol 28: 254-264.
    • (2011) Mol Membr Biol , vol.28 , pp. 254-264
    • Whitfield, T.1    Miles, A.J.2    Scheinost, J.C.3    Offer, J.4    Wentworth, P.5
  • 62
    • 38049161643 scopus 로고    scopus 로고
    • Viroporins from RNA viruses induce caspase-dependent apoptosis
    • Madan V, Castello A, Carrasco L, (2008) Viroporins from RNA viruses induce caspase-dependent apoptosis. Cell Microbiol 10: 437-451.
    • (2008) Cell Microbiol , vol.10 , pp. 437-451
    • Madan, V.1    Castello, A.2    Carrasco, L.3
  • 63
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution
    • Zhou Y, Morais-Cabral JH, Kaufman A, MacKinnon R, (2001) Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution. Nature 414: 43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 64
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco LG, Villa E, Mitra K, Frank J, Schulten K, (2008) Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16: 673-683.
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 65
    • 48549102871 scopus 로고    scopus 로고
    • United-atom acyl chains for CHARMM phospholipids
    • Hénin J, Shinoda W, Klein ML, (2008) United-atom acyl chains for CHARMM phospholipids. J Phys Chem Bio 112: 7008-7015.
    • (2008) J Phys Chem Bio , vol.112 , pp. 7008-7015
    • Hénin, J.1    Shinoda, W.2    Klein, M.L.3
  • 68
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell AD Jr, Feig M, Brooks CL III, (2004) Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comp Chem 25: 1400-1415.
    • (2004) J Comp Chem , vol.25 , pp. 1400-1415
    • MacKerell Jr., A.D.1    Feig, M.2    Brooks III., C.L.3
  • 70
    • 84963146276 scopus 로고
    • Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions
    • Grubmüller H, Heller H, Windemuth A, Schulten K, (1991) Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions. Mol Sim 6: 121-142.
    • (1991) Mol Sim , vol.6 , pp. 121-142
    • Grubmüller, H.1    Heller, H.2    Windemuth, A.3    Schulten, K.4
  • 71
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen LG, (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.G.3
  • 72
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller SE, Zhang Y, Pastor RW, Brooks BR, (1995) Constant pressure molecular dynamics simulation: The Langevin piston method. J Chem Phys 103: 4613-4621.
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 73
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MSP, (1996) HOLE: A program for the analysis of the pore dimensions of ion channel structural models. J Mol Graphics 14: 354-360.
    • (1996) J Mol Graphics , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.