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Volumn 22, Issue 11, 2013, Pages 1623-1638

Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR

Author keywords

Chemical shift prediction; Conformational change; Influenza M2; Membrane protein

Indexed keywords

CHOLESTEROL; PROTEIN M2;

EID: 84892701827     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2368     Document Type: Article
Times cited : (54)

References (81)
  • 1
    • 68249121326 scopus 로고    scopus 로고
    • Structure and function of the influenza A M2 proton channel
    • Cady SD, Luo WB, Hu FH, Hong M (2009) Structure and function of the influenza A M2 proton channel. Biochemistry 48:7356-7364.
    • (2009) Biochemistry , vol.48 , pp. 7356-7364
    • Cady, S.D.1    Luo, W.B.2    Hu, F.H.3    Hong, M.4
  • 2
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto LH, Holsinger LJ, Lamb RA (1992) Influenza virus M2 protein has ion channel activity. Cell 69:517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 3
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of infhluenza A and B viruses
    • Pinto LH, Lamb RA (2006) The M2 proton channels of infhluenza A and B viruses. J Biol Chem 281:8997-9000.
    • (2006) J Biol Chem , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 4
    • 84867681380 scopus 로고    scopus 로고
    • Structural basis for proton conduction and inhibition by the influenza M2 protein
    • Hong M, Degrado WF (2012) Structural basis for proton conduction and inhibition by the influenza M2 protein. Protein Sci 21:1620-1633.
    • (2012) Protein Sci , vol.21 , pp. 1620-1633
    • Hong, M.1    Degrado, W.F.2
  • 5
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman JS, Lamb RA (2011) Influenza virus assembly and budding. Virology 411:229-236.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 6
    • 0021893484 scopus 로고
    • Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface
    • Lamb RA, Zebedee SL, Richardson CD (1985) Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface. Cell 40:627-633.
    • (1985) Cell , vol.40 , pp. 627-633
    • Lamb, R.A.1    Zebedee, S.L.2    Richardson, C.D.3
  • 7
    • 0022345295 scopus 로고
    • Characterization of the influenza virus M2 integral membrane protein and expression at the infected-cell surface from cloned cDNA
    • Zebedee SL, Richardson CD, Lamb RA (1985) Characterization of the influenza virus M2 integral membrane protein and expression at the infected-cell surface from cloned cDNA. J Virol 56:502-511.
    • (1985) J Virol , vol.56 , pp. 502-511
    • Zebedee, S.L.1    Richardson, C.D.2    Lamb, R.A.3
  • 8
    • 0025923280 scopus 로고
    • Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • Holsinger LJ, Lamb RA (1991) Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183:32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 9
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue RJ, Hay AJ (1991) Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology 180:617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 10
    • 0028980598 scopus 로고
    • Activation of the M2 ion channel of influenza virus: A role for the transmembrane domain histidine residue
    • Wang C, Lamb RA, Pinto LH (1995) Activation of the M2 ion channel of influenza virus: a role for the transmembrane domain histidine residue. Biophys J 69: 1363-1371.
    • (1995) Biophys J , vol.69 , pp. 1363-1371
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 11
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
    • Tang Y, Zaitseva F, Lamb RA, Pinto LH (2002) The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J Biol Chem 277:39880-39886.
    • (2002) J Biol Chem , vol.277 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 12
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: Characterization of the amantadine block
    • Wang C, Takeuchi K, Pinto LH, Lamb RA (1993) Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J Virol 67:5585-5594.
    • (1993) J Virol , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 13
    • 0022157043 scopus 로고
    • The molecular basis of the specific antiinfluenza action of amantadine
    • Hay AJ, Wolstenholme AJ, Skehel JJ, Smith MH (1985) The molecular basis of the specific antiinfluenza action of amantadine. EMBO J 4:3021-3024.
    • (1985) EMBO J , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 14
  • 17
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell JR, Chou JJ (2008) Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451:591-595.
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 18
    • 77955576540 scopus 로고    scopus 로고
    • Magic angle spinning NMR investigation of influenza A M218260: Support for an allosteric mechanism of inhibition
    • Andreas LB, Eddy MT, Pielak RM, Chou JJ, Griffin RG (2010) Magic angle spinning NMR investigation of influenza A M218260: support for an allosteric mechanism of inhibition. J Am Chem Soc 132:10958-10960.
    • (2010) J Am Chem Soc , vol.132 , pp. 10958-10960
    • Andreas, L.B.1    Eddy, M.T.2    Pielak, R.M.3    Chou, J.J.4    Griffin, R.G.5
  • 19
    • 40349105892 scopus 로고    scopus 로고
    • Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel
    • Cady SD, Hong M (2008) Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proc Natl Acad Sci USA 105:1483-1488.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1483-1488
    • Cady, S.D.1    Hong, M.2
  • 20
    • 76249125649 scopus 로고    scopus 로고
    • Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers
    • Cady SD, Schmidt-Rohr K, Wang J, Soto CS, DeGrado WF, Hong M (2010) Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers. Nature 463:689-692.
    • (2010) Nature , vol.463 , pp. 689-692
    • Cady, S.D.1    Schmidt-Rohr, K.2    Wang, J.3    Soto, C.S.4    Degrado, W.F.5    Hong, M.6
  • 21
    • 77958162674 scopus 로고    scopus 로고
    • Mechanisms of proton conduction and gating by influenza M2 proton channels from solid-state NMR
    • Hu F, Luo W, Hong M (2010) Mechanisms of proton conduction and gating by influenza M2 proton channels from solid-state NMR. Science 330:505-509.
    • (2010) Science , vol.330 , pp. 505-509
    • Hu, F.1    Luo, W.2    Hong, M.3
  • 22
    • 77958156306 scopus 로고    scopus 로고
    • Atomistic mechanism of the influenza A proton channel from a structure solved in a lipid bilayer
    • Sharma M, Yi M, Dong H, Qin H, Peterson E, Busath D, Zhou HX, Cross TA (2010) Atomistic mechanism of the influenza A proton channel from a structure solved in a lipid bilayer. Science 330:509-512.
    • (2010) Science , vol.330 , pp. 509-512
    • Sharma, M.1    Yi, M.2    Dong, H.3    Qin, H.4    Peterson, E.5    Busath, D.6    Zhou, H.X.7    Cross, T.A.8
  • 23
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • Duong-Ly KC, Nanda V, DeGrado WF, Howard KP (2005) The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci 14:856-861.
    • (2005) Protein Sci , vol.14 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    Degrado, W.F.3    Howard, K.P.4
  • 25
    • 34247847729 scopus 로고    scopus 로고
    • Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: A 2H, 13C, and 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle
    • Cady SD, Goodman C, C.Tatko, DeGrado WF, Hong M (2007) Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: a 2H, 13C, and 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle. J Am Chem Soc 129:5719-5729.
    • (2007) J Am Chem Soc , vol.129 , pp. 5719-5729
    • Cady, S.D.1    Goodman, C.2    Tatko, C.3    Degrado, W.F.4    Hong, M.5
  • 26
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus
    • Hu J, Asbury T, Achuthan S, Li C, Bertram R, Quine JR, Fu R, Cross TA (2007) Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Biophys J 92: 4335-4343.
    • (2007) Biophys J , vol.92 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Achuthan, S.3    Li, C.4    Bertram, R.5    Quine, J.R.6    Fu, R.7    Cross, T.A.8
  • 27
    • 0034775070 scopus 로고    scopus 로고
    • Structure of the the transmembrane region of the M2 protein H1 channel
    • Wang J, Kim S, Kovacs F, Cross TA (2001) Structure of the the transmembrane region of the M2 protein H1 channel. Prot Sci 10:2241-2250.
    • (2001) Prot Sci , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 28
    • 58149345493 scopus 로고    scopus 로고
    • Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: The role of Ser31 in amantadine binding
    • Cady SD, Mishanina TV, Hong M (2009) Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantadine binding. J Mol Biol 385:1127-1141.
    • (2009) J Mol Biol , vol.385 , pp. 1127-1141
    • Cady, S.D.1    Mishanina, T.V.2    Hong, M.3
  • 29
    • 80855128789 scopus 로고    scopus 로고
    • Structural investigation of rimantadine inhibition of the AM2-BM2 chimera channel of influenza viruses
    • Pielak RM, Oxenoid K, Chou JJ (2011) Structural investigation of rimantadine inhibition of the AM2-BM2 chimera channel of influenza viruses. Structure 19:1655-1663.
    • (2011) Structure , vol.19 , pp. 1655-1663
    • Pielak, R.M.1    Oxenoid, K.2    Chou, J.J.3
  • 30
    • 79953041331 scopus 로고    scopus 로고
    • Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy
    • Cady SD, Wang J, Wu Y, DeGrado WF, Hong M (2011) Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy. J Am Chem Soc 133:4274-4284.
    • (2011) J Am Chem Soc , vol.133 , pp. 4274-4284
    • Cady, S.D.1    Wang, J.2    Wu, Y.3    Degrado, W.F.4    Hong, M.5
  • 31
    • 49449093199 scopus 로고    scopus 로고
    • Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel
    • Jing X, Ma C, Ohigashi Y, Oliveira FA, Jardetzky TS, Pinto LH, Lamb RA (2008) Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel. Proc Natl Acad Sci USA 105:10967-10972.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10967-10972
    • Jing, X.1    Ma, C.2    Ohigashi, Y.3    Oliveira, F.A.4    Jardetzky, T.S.5    Pinto, L.H.6    Lamb, R.A.7
  • 32
    • 77956383657 scopus 로고    scopus 로고
    • Coexistence of two adamantane binding sites in the influenza A M2 ion channel
    • Rosenberg MR, Casarotto MG (2010) Coexistence of two adamantane binding sites in the influenza A M2 ion channel. Proc Natl Acad Sci USA 107:13866-13871.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13866-13871
    • Rosenberg, M.R.1    Casarotto, M.G.2
  • 33
    • 78649796981 scopus 로고    scopus 로고
    • Conformational plasticity of the influenza A M2 transmembrane peptide in lipid bilayers under varying pH, drug binding and membrane thickness
    • Hu F, Luo W, Cady SD, Hong M (2011) Conformational plasticity of the influenza A M2 transmembrane peptide in lipid bilayers under varying pH, drug binding and membrane thickness. Biochim Biophys Acta 1808:415-423.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 415-423
    • Hu, F.1    Luo, W.2    Cady, S.D.3    Hong, M.4
  • 34
    • 36849047240 scopus 로고    scopus 로고
    • Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel
    • Li C, Qin H, Gao FP, Cross TA (2007) Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel. Biochim Biophys Acta 1768:3162-3170.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 3162-3170
    • Li, C.1    Qin, H.2    Gao, F.P.3    Cross, T.A.4
  • 35
    • 67650080518 scopus 로고    scopus 로고
    • Immobilization of the influenza A M2 transmembrane peptide in virusenvelope mimetic lipid membranes: A solid-state NMR investigation
    • Luo W, Cady SD, Hong M (2009) Immobilization of the influenza A M2 transmembrane peptide in virusenvelope mimetic lipid membranes: a solid-state NMR investigation. Biochemistry 48:6361-6368.
    • (2009) Biochemistry , vol.48 , pp. 6361-6368
    • Luo, W.1    Cady, S.D.2    Hong, M.3
  • 36
    • 79960884898 scopus 로고    scopus 로고
    • Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein
    • Cady SD, Wang T, Hong M (2011) Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein. J Am Chem Soc 133:11572-11579.
    • (2011) J Am Chem Soc , vol.133 , pp. 11572-11579
    • Cady, S.D.1    Wang, T.2    Hong, M.3
  • 37
    • 0027339698 scopus 로고
    • Influenza virus M2 protein: A molecular modeling study of the ion channel
    • Sansom MSP, Kerr ID (1993) Influenza virus M2 protein: A molecular modeling study of the ion channel. Protein Eng 6:65-74.
    • (1993) Protein Eng , vol.6 , pp. 65-74
    • Sansom, M.S.P.1    Kerr, I.D.2
  • 38
    • 36549041108 scopus 로고    scopus 로고
    • Proton transport behavior through the influenza A M2 channel: Insights from molecular simulation
    • Chen H, Wu Y, Voth GA (2007) Proton transport behavior through the influenza A M2 channel: insights from molecular simulation. Biophys J 93:3470-3479.
    • (2007) Biophys J , vol.93 , pp. 3470-3479
    • Chen, H.1    Wu, Y.2    Voth, G.A.3
  • 40
    • 84857711312 scopus 로고    scopus 로고
    • NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel
    • Hu F, Schmidt-Rohr K, Hong M (2012) NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel. J Am Chem Soc 134:3703-3713.
    • (2012) J Am Chem Soc , vol.134 , pp. 3703-3713
    • Hu, F.1    Schmidt-Rohr, K.2    Hong, M.3
  • 41
    • 84866359064 scopus 로고    scopus 로고
    • Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shifts
    • Hong M, Fritzsching KJ, Williams JK (2012) Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shifts. J Am Chem Soc 134:14753-14755.
    • (2012) J Am Chem Soc , vol.134 , pp. 14753-14755
    • Hong, M.1    Fritzsching, K.J.2    Williams, J.K.3
  • 42
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian C, Gao PF, Pinto LH, Lamb RA, Cross TA (2003) Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci 12:2597-2605.
    • (2003) Protein Sci , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 43
    • 0031909858 scopus 로고    scopus 로고
    • The M2 ectodomain is important for its incorporation into influenza A virions
    • Park EK, Castrucci MR, Portner A, Kawaoka Y (1998) The M2 ectodomain is important for its incorporation into influenza A virions. J Virol 72:2449-2455.
    • (1998) J Virol , vol.72 , pp. 2449-2455
    • Park, E.K.1    Castrucci, M.R.2    Portner, A.3    Kawaoka, Y.4
  • 44
    • 0026004791 scopus 로고
    • Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins
    • Ito T, Gorman OT, Kawaoka Y, Bean WJ, Webster RG (1991) Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins. J Virol 65:5491-5498.
    • (1991) J Virol , vol.65 , pp. 5491-5498
    • Ito, T.1    Gorman, O.T.2    Kawaoka, Y.3    Bean, W.J.4    Webster, R.G.5
  • 45
    • 0032874490 scopus 로고    scopus 로고
    • A universal influenza A vaccine based on the extracellular domain of the M2 protein
    • Neirynck S, Deroo T, Saelens X, Vanlandschoot P, Jou WM, Fiers W (1999) A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nat Med 5:1157-1163.
    • (1999) Nat Med , vol.5 , pp. 1157-1163
    • Neirynck, S.1    Deroo, T.2    Saelens, X.3    Vanlandschoot, P.4    Jou, W.M.5    Fiers, W.6
  • 46
    • 0037456637 scopus 로고    scopus 로고
    • N-terminus of M2 protein could induce antibodies with inhibitory activity against influenza virus replication
    • Liu W, Li H, Chen YH (2003) N-terminus of M2 protein could induce antibodies with inhibitory activity against influenza virus replication. FEMS Immunol Med Microbiol 35:141-146.
    • (2003) FEMS Immunol Med Microbiol , vol.35 , pp. 141-146
    • Liu, W.1    Li, H.2    Chen, Y.H.3
  • 47
    • 0028895957 scopus 로고
    • Analysis of the posttranslational modifications of the influenza virus M2 protein
    • Holsinger LJ, Shaughnessy MA, Micko A, Pinto LH, Lamb RA (1995) Analysis of the posttranslational modifications of the influenza virus M2 protein. J Virol 69: 1219-1225.
    • (1995) J Virol , vol.69 , pp. 1219-1225
    • Holsinger, L.J.1    Shaughnessy, M.A.2    Micko, A.3    Pinto, L.H.4    Lamb, R.A.5
  • 48
    • 0030973121 scopus 로고    scopus 로고
    • The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer
    • Sakaguchi T, Tu Q, Pinto LH, Lamb RA (1997) The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer Proc Natl Acad Sci USA 94:5000-5005.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5000-5005
    • Sakaguchi, T.1    Tu, Q.2    Pinto, L.H.3    Lamb, R.A.4
  • 49
    • 0023820458 scopus 로고
    • Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions
    • Zebedee SL, Lamb RA (1988) Influenza A virus M2 protein: monoclonal antibody restriction of virus growth and detection of M2 in virions. J Virol 62:2762-2772.
    • (1988) J Virol , vol.62 , pp. 2762-2772
    • Zebedee, S.L.1    Lamb, R.A.2
  • 50
    • 0343083874 scopus 로고
    • Growth restriction of influenza A virus by M2 protein antibody is genetically linked to the M1 protein
    • Zebedee SL, Lamb RA (1989) Growth restriction of influenza A virus by M2 protein antibody is genetically linked to the M1 protein. Proc Natl Acad Sci USA 86: 1061-1065.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1061-1065
    • Zebedee, S.L.1    Lamb, R.A.2
  • 51
    • 77951437276 scopus 로고    scopus 로고
    • Influenza virus M2 ion channel protein is necessary for filamentous virion formation
    • Rossman JS, Jing X, Leser GP, Balannik V, Pinto LH, Lamb RA (2010) Influenza virus M2 ion channel protein is necessary for filamentous virion formation. J Virol 84:5078-5088.
    • (2010) J Virol , vol.84 , pp. 5078-5088
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Balannik, V.4    Pinto, L.H.5    Lamb, R.A.6
  • 53
    • 53749092893 scopus 로고    scopus 로고
    • The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding
    • Chen BJ, Leser GP, Jackson D, Lamb RA (2008) The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding. J Virol 82:10059-10070.
    • (2008) J Virol , vol.82 , pp. 10059-10070
    • Chen, B.J.1    Leser, G.P.2    Jackson, D.3    Lamb, R.A.4
  • 54
    • 33746810932 scopus 로고    scopus 로고
    • Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus production
    • McCown MF, Pekosz A (2006) Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus production. J Virol 80:8178-8189.
    • (2006) J Virol , vol.80 , pp. 8178-8189
    • McCown, M.F.1    Pekosz, A.2
  • 55
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman JS, Jing X, Leser GP, Lamb RA (2010) Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 142:902-913.
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 56
    • 84879842138 scopus 로고    scopus 로고
    • Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information
    • Fritzsching KJ, Yang Y, Schmidt-Rohr K, Hong M (2013) Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information. J Biomol NMR 56:155-167.
    • (2013) J Biomol NMR , vol.56 , pp. 155-167
    • Fritzsching, K.J.1    Yang, Y.2    Schmidt-Rohr, K.3    Hong, M.4
  • 57
    • 84868197516 scopus 로고    scopus 로고
    • PACSY, a relational database management system for protein structure and chemical shift analysis
    • Lee W, Yu W, Kim S, Chang I, Lee W, Markley JL (2012) PACSY, a relational database management system for protein structure and chemical shift analysis. J Biomol NMR 54:169-179.
    • (2012) J Biomol NMR , vol.54 , pp. 169-179
    • Lee, W.1    Yu, W.2    Kim, S.3    Chang, I.4    Lee, W.5    Markley, J.L.6
  • 58
    • 62649113057 scopus 로고    scopus 로고
    • Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy
    • Ader C, Schneider R, Seidel K, Etzkorn M, Becker S, Baldus M (2009) Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy. J Am Chem Soc 131:170-176.
    • (2009) J Am Chem Soc , vol.131 , pp. 170-176
    • Ader, C.1    Schneider, R.2    Seidel, K.3    Etzkorn, M.4    Becker, S.5    Baldus, M.6
  • 59
    • 0037028547 scopus 로고    scopus 로고
    • Membrane protein topology probed by 1H spin diffusion from lipids using solid-state NMR spectroscopy
    • Huster D, Yao XL, Hong M (2002) Membrane protein topology probed by 1H spin diffusion from lipids using solid-state NMR spectroscopy. J Am Chem Soc 124: 874-883.
    • (2002) J Am Chem Soc , vol.124 , pp. 874-883
    • Huster, D.1    Yao, X.L.2    Hong, M.3
  • 60
    • 0032572058 scopus 로고    scopus 로고
    • A novel tool for probing membrane protein structure: Solid-state NMR with proton spin diffusion and Xnucleus detection
    • Kumashiro KK, Schmidt-Rohr K, Murphy OJ, Ouellette KL, Cramer WA, Thompson LK (1998) A novel tool for probing membrane protein structure: solid-state NMR with proton spin diffusion and Xnucleus detection. J Am Chem Soc 120:5043-5051.
    • (1998) J Am Chem Soc , vol.120 , pp. 5043-5051
    • Kumashiro, K.K.1    Schmidt-Rohr, K.2    Murphy, O.J.3    Ouellette, K.L.4    Cramer, W.A.5    Thompson, L.K.6
  • 61
    • 77749267718 scopus 로고    scopus 로고
    • Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy
    • Luo W, Hong M (2010) Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy. J Am Chem Soc 132:2378-2384.
    • (2010) J Am Chem Soc , vol.132 , pp. 2378-2384
    • Luo, W.1    Hong, M.2
  • 62
    • 80051673221 scopus 로고    scopus 로고
    • SHIFTX2: Significantly improved protein chemical shift prediction
    • Han B, Liu Y, Ginzinger SW, Wishart D (2011) SHIFTX2: significantly improved protein chemical shift prediction J Biomol NMR 50:43-57.
    • (2011) J Biomol NMR , vol.50 , pp. 43-57
    • Han, B.1    Liu, Y.2    Ginzinger, S.W.3    Wishart, D.4
  • 63
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G (2008) Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321:1206-1210.
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 64
    • 84883453017 scopus 로고    scopus 로고
    • 13C structuring shifts for the analysis of model beta-hairpins and beta-sheets in proteins: Diagnostic shifts appear only at the cross-strand H-bonded residues
    • Shu I, Scian M, Stewart JM, Kier BL, Andersen NH (2013) 13C structuring shifts for the analysis of model beta-hairpins and beta-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues. J Biomol NMR:1-17.
    • (2013) J Biomol , vol.NMR , pp. 1-17
    • Shu, I.1    Scian, M.2    Stewart, J.M.3    Kier, B.L.4    Andersen, N.H.5
  • 68
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337:635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 70
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele P, Rietveld A, Wilk T, Simons K (1999) Influenza viruses select ordered lipid domains during budding from the plasma membrane. J Biol Chem 274: 2038-2044.
    • (1999) J Biol Chem , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 71
    • 27644440465 scopus 로고    scopus 로고
    • Influenza virus assembly and budding in raft-derived microdomains: A quantitative analysis of the surface distribution of HA, NA and M2 proteins
    • Leser GP, Lamb RA (2005) Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins. Virology 342:215-227.
    • (2005) Virology , vol.342 , pp. 215-227
    • Leser, G.P.1    Lamb, R.A.2
  • 72
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1
    • Harris A, Forouhar F, Qiu S, Sha B, Luo M (2001) The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 289:34-44.
    • (2001) Virology , vol.289 , pp. 34-44
    • Harris, A.1    Forouhar, F.2    Qiu, S.3    Sha, B.4    Luo, M.5
  • 75
    • 0037125949 scopus 로고    scopus 로고
    • Expression and initial structural insights from solidstate NMR of the M2 proton channel from influenza A virus
    • Tian C, Tobler K, Lamb RA, Pinto LH, Cross TA (2002) Expression and initial structural insights from solidstate NMR of the M2 proton channel from influenza A virus. Biochemistry 41:11294-11300.
    • (2002) Biochemistry , vol.41 , pp. 11294-11300
    • Tian, C.1    Tobler, K.2    Lamb, R.A.3    Pinto, L.H.4    Cross, T.A.5
  • 76
    • 84863156305 scopus 로고    scopus 로고
    • NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide
    • Wang T, Cady SD, Hong M (2012) NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide. Biophys J 102:787-794.
    • (2012) Biophys J , vol.102 , pp. 787-794
    • Wang, T.1    Cady, S.D.2    Hong, M.3
  • 77
    • 0042995329 scopus 로고    scopus 로고
    • Chemical shift referencing in MAS solid state NMR
    • Morcombe CR, Zilm KW (2003) Chemical shift referencing in MAS solid state NMR. J Magn Reson 162:479-486.
    • (2003) J Magn Reson , vol.162 , pp. 479-486
    • Morcombe, C.R.1    Zilm, K.W.2
  • 78
    • 0000953276 scopus 로고    scopus 로고
    • C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR
    • Takegoshi K, Nakamura S, Terao T (2001) C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem Phys Lett 344:631-637.
    • (2001) Chem Phys Lett , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 79
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G (2004) Making optimal use of empirical energy functions: force-field parameterization in crystal space. Proteins 57:678-683.
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 80
    • 70450194574 scopus 로고    scopus 로고
    • Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins
    • Simone AD, Cavalli A, Hsu SD, Vranken W, Vendruscolo M (2009) Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins. J Am Chem Soc 131:16332-16333.
    • (2009) J Am Chem Soc , vol.131 , pp. 16332-16333
    • Simone, A.D.1    Cavalli, A.2    Hsu, S.D.3    Vranken, W.4    Vendruscolo, M.5
  • 81
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1


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