메뉴 건너뛰기




Volumn 113, Issue 27, 2016, Pages E3844-E3851

Immobilization of the N-terminal helix stabilizes prefusion paramyxovirus fusion proteins

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; POLYCLONAL ANTIBODY; VIRUS PROTEIN; VIRUS FUSION PROTEIN;

EID: 84977264504     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1608349113     Document Type: Article
Times cited : (4)

References (60)
  • 1
    • 72849124628 scopus 로고    scopus 로고
    • Transmission of human infection with Nipah virus
    • Luby SP, Gurley ES, Hossain MJ (2009) Transmission of human infection with Nipah virus. Clin Infect Dis 49(11):1743-1748.
    • (2009) Clin Infect Dis , vol.49 , Issue.11 , pp. 1743-1748
    • Luby, S.P.1    Gurley, E.S.2    Hossain, M.J.3
  • 2
    • 84874449497 scopus 로고    scopus 로고
    • Interdisciplinary approaches to understanding disease emergence: The past, present, and future drivers of Nipah virus emergence
    • Daszak P, et al. (2013) Interdisciplinary approaches to understanding disease emergence: The past, present, and future drivers of Nipah virus emergence. Proc Natl Acad Sci USA 110(Suppl 1):3681-3688.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 3681-3688
    • Daszak, P.1
  • 3
    • 84860279802 scopus 로고    scopus 로고
    • Bats host major mammalian paramyxoviruses
    • Drexler JF, et al. (2012) Bats host major mammalian paramyxoviruses. Nat Commun 3(796):796.
    • (2012) Nat Commun , vol.3 , Issue.796 , pp. 796
    • Drexler, J.F.1
  • 4
    • 84939980103 scopus 로고    scopus 로고
    • Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry
    • 60th Anniversary Issue 518-531
    • Bose S, Jardetzky TS, Lamb RA (2015) Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry. Virology 479-480(60th Anniversary Issue): 518-531.
    • (2015) Virology , pp. 479-480
    • Bose, S.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 5
    • 84937761010 scopus 로고    scopus 로고
    • Viral membrane fusion
    • 498-507
    • Harrison SC (2015) Viral membrane fusion. Virology 479-480:498-507.
    • (2015) Virology , pp. 479-480
    • Harrison, S.C.1
  • 6
    • 0015990842 scopus 로고
    • Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus
    • Scheid A, Choppin PW (1974) Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57(2):475-490.
    • (1974) Virology , vol.57 , Issue.2 , pp. 475-490
    • Scheid, A.1    Choppin, P.W.2
  • 7
    • 0015732097 scopus 로고
    • Trypsin action on the growth of Sendai virus in tissue culture cells. 3. Structural difference of Sendai viruses grown in eggs and tissue culture cells
    • Homma M, Ouchi M (1973) Trypsin action on the growth of Sendai virus in tissue culture cells. 3. Structural difference of Sendai viruses grown in eggs and tissue culture cells. JVirol12(6):1457-1465.
    • (1973) J Virol , vol.12 , Issue.6 , pp. 1457-1465
    • Homma, M.1    Ouchi, M.2
  • 8
    • 0017113513 scopus 로고
    • Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus
    • Nagai Y, Klenk H-D, Rott R (1976) Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology 72(2):494-508.
    • (1976) Virology , vol.72 , Issue.2 , pp. 494-508
    • Nagai, Y.1    Klenk, H.-D.2    Rott, R.3
  • 9
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS (2006) Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439(7072): 38-44.
    • (2006) Nature , vol.439 , Issue.7072 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 10
    • 84861315738 scopus 로고    scopus 로고
    • Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site
    • Wen X, et al. (2012) Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site. Nat Struct Mol Biol 19(4):461-463.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.4 , pp. 461-463
    • Wen, X.1
  • 11
    • 84878349946 scopus 로고    scopus 로고
    • Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    • McLellan JS, et al. (2013) Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody. Science 340(6136):1113-1117.
    • (2013) Science , vol.340 , Issue.6136 , pp. 1113-1117
    • McLellan, J.S.1
  • 12
    • 84953222042 scopus 로고    scopus 로고
    • Crystal structure of the pre-fusion Nipah virus fusion glycoprotein reveals a novel hexamer-of-trimers assembly
    • Xu K, et al. (2015) Crystal structure of the pre-fusion Nipah virus fusion glycoprotein reveals a novel hexamer-of-trimers assembly. PLoS Pathog 11(12):e1005322.
    • (2015) PLoS Pathog , vol.11 , Issue.12 , pp. e1005322
    • Xu, K.1
  • 13
    • 84955495688 scopus 로고    scopus 로고
    • Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form
    • Wong JJ, Paterson RG, Lamb RA, Jardetzky TS (2016) Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form. Proc Natl Acad Sci USA 113(4): 1056-1061.
    • (2016) Proc Natl Acad Sci USA , vol.113 , Issue.4 , pp. 1056-1061
    • Wong, J.J.1    Paterson, R.G.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 14
    • 21544470513 scopus 로고    scopus 로고
    • Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein
    • Yin HS, Paterson RG, Wen X, Lamb RA, Jardetzky TS (2005) Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein. Proc Natl Acad Sci USA 102(26):9288-9293.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.26 , pp. 9288-9293
    • Yin, H.S.1    Paterson, R.G.2    Wen, X.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 15
    • 77953021928 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus F protein in the post-fusion conformation
    • Swanson K, et al. (2010) Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology 402(2):372-379.
    • (2010) Virology , vol.402 , Issue.2 , pp. 372-379
    • Swanson, K.1
  • 16
    • 79960387921 scopus 로고    scopus 로고
    • Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    • McLellan JS, Yang Y, Graham BS, Kwong PD (2011) Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes. J Virol 85(15):7788-7796.
    • (2011) J Virol , vol.85 , Issue.15 , pp. 7788-7796
    • McLellan, J.S.1    Yang, Y.2    Graham, B.S.3    Kwong, P.D.4
  • 17
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding
    • Bishop KA, et al. (2008) Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding. J Virol 82(22): 11398-11409.
    • (2008) J Virol , vol.82 , Issue.22 , pp. 11398-11409
    • Bishop, K.A.1
  • 18
    • 8644256749 scopus 로고    scopus 로고
    • Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    • Melanson VR, Iorio RM (2004) Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein. J Virol 78(23):13053-13061.
    • (2004) J Virol , vol.78 , Issue.23 , pp. 13053-13061
    • Melanson, V.R.1    Iorio, R.M.2
  • 19
    • 84894071400 scopus 로고    scopus 로고
    • Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cells
    • Bose S, Song AS, Jardetzky TS, Lamb RA (2014) Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cells. J Virol 88(8):3925-3941.
    • (2014) J Virol , vol.88 , Issue.8 , pp. 3925-3941
    • Bose, S.1    Song, A.S.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 20
    • 84855845971 scopus 로고    scopus 로고
    • Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion
    • Bose S, et al. (2011) Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J Virol 85(24):12855-12866.
    • (2011) J Virol , vol.85 , Issue.24 , pp. 12855-12866
    • Bose, S.1
  • 21
    • 84866859065 scopus 로고    scopus 로고
    • Fusion activation by a headless parainfluenza virus 5 hemagglutininneuraminidase stalk suggests a modular mechanism for triggering
    • Bose S, et al. (2012) Fusion activation by a headless parainfluenza virus 5 hemagglutininneuraminidase stalk suggests a modular mechanism for triggering. Proc Natl Acad Sci USA 109(39):E2625-E2634.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.39 , pp. E2625-E2634
    • Bose, S.1
  • 22
    • 84883271554 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 (PIV5) hemagglutininneuraminidase (HN) ectodomain
    • Welch BD, et al. (2013) Structure of the parainfluenza virus 5 (PIV5) hemagglutininneuraminidase (HN) ectodomain. PLoS Pathog 9(8):e1003534.
    • (2013) PLoS Pathog , vol.9 , Issue.8 , pp. e1003534
    • Welch, B.D.1
  • 23
    • 84866152545 scopus 로고    scopus 로고
    • Structure of the ulster strain newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence
    • Yuan P, Paterson RG, Leser GP, Lamb RA, Jardetzky TS (2012) Structure of the ulster strain newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence. PLoS Pathog 8(8):e1002855.
    • (2012) PLoS Pathog , vol.8 , Issue.8 , pp. e1002855
    • Yuan, P.1    Paterson, R.G.2    Leser, G.P.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 24
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan P, et al. (2011) Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc Natl Acad Sci USA 108(36):14920-14925.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.36 , pp. 14920-14925
    • Yuan, P.1
  • 25
    • 84888271006 scopus 로고    scopus 로고
    • Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry
    • Liu Q, et al. (2013) Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry. PLoS Pathog 9(11):e1003770.
    • (2013) PLoS Pathog , vol.9 , Issue.11 , pp. e1003770
    • Liu, Q.1
  • 26
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell S, Takimoto T, Portner A, Taylor G (2000) Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat Struct Biol 7(11):1068-1074.
    • (2000) Nat Struct Biol , vol.7 , Issue.11 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 27
    • 0346654073 scopus 로고    scopus 로고
    • Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III
    • Lawrence MC, et al. (2004) Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J Mol Biol 335(5):1343-1357.
    • (2004) J Mol Biol , vol.335 , Issue.5 , pp. 1343-1357
    • Lawrence, M.C.1
  • 28
    • 44849140504 scopus 로고    scopus 로고
    • Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2
    • Bowden TA, et al. (2008) Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2. Nat Struct Mol Biol 15(6):567-572.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.6 , pp. 567-572
    • Bowden, T.A.1
  • 29
    • 84903484765 scopus 로고    scopus 로고
    • Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting
    • Poor TA, et al. (2014) Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting. Proc Natl Acad Sci USA 111(25): E2596-E2605.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.25 , pp. E2596-E2605
    • Poor, T.A.1
  • 30
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell CJ, Jardetzky TS, Lamb RA (2001) Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion. EMBO J 20(15):4024-4034.
    • (2001) EMBO J , vol.20 , Issue.15 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 31
    • 0242298583 scopus 로고    scopus 로고
    • A dual-functional paramyxovirus F protein regulatory switch segment: Activation and membrane fusion
    • Russell CJ, Kantor KL, Jardetzky TS, Lamb RA (2003) A dual-functional paramyxovirus F protein regulatory switch segment: Activation and membrane fusion. J Cell Biol 163(2):363-374.
    • (2003) J Cell Biol , vol.163 , Issue.2 , pp. 363-374
    • Russell, C.J.1    Kantor, K.L.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 32
    • 84862908780 scopus 로고    scopus 로고
    • Capture and imaging of a prehairpin fusion intermediate of the paramyxovirus PIV5
    • Kim YH, et al. (2011) Capture and imaging of a prehairpin fusion intermediate of the paramyxovirus PIV5. Proc Natl Acad Sci USA 108(52):20992-20997.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.52 , pp. 20992-20997
    • Kim, Y.H.1
  • 33
    • 84939155883 scopus 로고    scopus 로고
    • A cysteine zipper stabilizes a pre-fusion F glycoprotein vaccine for respiratory syncytial virus
    • Stewart-Jones GB, et al. (2015) A cysteine zipper stabilizes a pre-fusion F glycoprotein vaccine for respiratory syncytial virus. PLoS One 10(6):e0128779.
    • (2015) PLoS One , vol.10 , Issue.6 , pp. e0128779
    • Stewart-Jones, G.B.1
  • 34
    • 84887277978 scopus 로고    scopus 로고
    • Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    • McLellan JS, et al. (2013) Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus. Science 342(6158):592-598.
    • (2013) Science , vol.342 , Issue.6158 , pp. 592-598
    • McLellan, J.S.1
  • 35
    • 84940920476 scopus 로고    scopus 로고
    • A highly stable prefusion RSV F vaccine derived from structural analysis of the fusion mechanism
    • Krarup A, et al. (2015) A highly stable prefusion RSV F vaccine derived from structural analysis of the fusion mechanism. Nat Commun 6:8143.
    • (2015) Nat Commun , vol.6 , pp. 8143
    • Krarup, A.1
  • 36
    • 0030775365 scopus 로고    scopus 로고
    • Role of a single amino acid at the amino terminus of the simian virus 5 F2 subunit in syncytium formation
    • Ito M, et al. (1997) Role of a single amino acid at the amino terminus of the simian virus 5 F2 subunit in syncytium formation. J Virol 71(12):9855-9858.
    • (1997) J Virol , vol.71 , Issue.12 , pp. 9855-9858
    • Ito, M.1
  • 37
    • 0034712879 scopus 로고    scopus 로고
    • Fusion protein of the paramyxovirus SV5: Destabilizing and stabilizing mutants of fusion activation
    • Paterson RG, Russell CJ, Lamb RA (2000) Fusion protein of the paramyxovirus SV5: Destabilizing and stabilizing mutants of fusion activation. Virology 270(1):17-30.
    • (2000) Virology , vol.270 , Issue.1 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 38
    • 84923167132 scopus 로고    scopus 로고
    • On the stability of parainfluenza virus 5 F proteins
    • Poor TA, et al. (2015) On the stability of parainfluenza virus 5 F proteins. J Virol 89(6): 3438-3441.
    • (2015) J Virol , vol.89 , Issue.6 , pp. 3438-3441
    • Poor, T.A.1
  • 39
    • 0023442009 scopus 로고
    • Isolation and characterization of monoclonal antibodies to simian virus 5 and their use in revealing antigenic differences between human, canine and simian isolates
    • Randall RE, Young DF, Goswami KKA, Russell WC (1987) Isolation and characterization of monoclonal antibodies to simian virus 5 and their use in revealing antigenic differences between human, canine and simian isolates. J Gen Virol 68 (Pt 11):2769-2780.
    • (1987) J Gen Virol , vol.68 , pp. 2769-2780
    • Randall, R.E.1    Young, D.F.2    Goswami, K.K.A.3    Russell, W.C.4
  • 40
    • 84867351430 scopus 로고    scopus 로고
    • Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein
    • Welch BD, et al. (2012) Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein. Proc Natl Acad Sci USA 109(41):16672-16677.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.41 , pp. 16672-16677
    • Welch, B.D.1
  • 41
    • 34447578470 scopus 로고    scopus 로고
    • The association of tetrameric acetylcholinesterase with ColQ tail: A block normal mode analysis
    • Zhang D, McCammon JA (2005) The association of tetrameric acetylcholinesterase with ColQ tail: A block normal mode analysis. PLOS Comput Biol 1(6):e62. \
    • (2005) PLOS Comput Biol , vol.1 , Issue.6 , pp. e62
    • Zhang, D.1    McCammon, J.A.2
  • 42
    • 0037168602 scopus 로고    scopus 로고
    • Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase. PhCH2O- complex
    • Luo J, Bruice TC (2002) Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase.PhCH2O- complex. Proc Natl Acad Sci USA 99(26):16597-16600.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.26 , pp. 16597-16600
    • Luo, J.1    Bruice, T.C.2
  • 43
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young MA, Gonfloni S, Superti-Furga G, Roux B, Kuriyan J (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105(1):115-126.
    • (2001) Cell , vol.105 , Issue.1 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 44
    • 84921511844 scopus 로고    scopus 로고
    • Exploring a non-ATP pocket for potential allosteric modulation of PI3Kα
    • Gkeka P, Papafotika A, Christoforidis S, Cournia Z (2015) Exploring a non-ATP pocket for potential allosteric modulation of PI3Kα. J Phys Chem B 119(3):1002-1016.
    • (2015) J Phys Chem B , vol.119 , Issue.3 , pp. 1002-1016
    • Gkeka, P.1    Papafotika, A.2    Christoforidis, S.3    Cournia, Z.4
  • 45
    • 84866527691 scopus 로고    scopus 로고
    • Base of the measles virus fusion trimer head receives the signal that triggers membrane fusion
    • Apte-Sengupta S, et al. (2012) Base of the measles virus fusion trimer head receives the signal that triggers membrane fusion. J Biol Chem 287(39):33026-33035.
    • (2012) J Biol Chem , vol.287 , Issue.39 , pp. 33026-33035
    • Apte-Sengupta, S.1
  • 46
    • 84920811285 scopus 로고    scopus 로고
    • Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head
    • Avila M, et al. (2015) Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head. J Virol 89(2):1445-1451.
    • (2015) J Virol , vol.89 , Issue.2 , pp. 1445-1451
    • Avila, M.1
  • 47
    • 2342512265 scopus 로고    scopus 로고
    • Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion
    • Li J, Quinlan E, Mirza A, Iorio RM (2004) Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion. J Virol 78(10): 5299-5310.
    • (2004) J Virol , vol.78 , Issue.10 , pp. 5299-5310
    • Li, J.1    Quinlan, E.2    Mirza, A.3    Iorio, R.M.4
  • 48
    • 84884413000 scopus 로고    scopus 로고
    • Cross-neutralization of four paramyxoviruses by a human monoclonal antibody
    • Corti D, et al. (2013) Cross-neutralization of four paramyxoviruses by a human monoclonal antibody. Nature 501(7467):439-443.
    • (2013) Nature , vol.501 , Issue.7467 , pp. 439-443
    • Corti, D.1
  • 49
    • 70350277403 scopus 로고    scopus 로고
    • Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: Implications for the mechanism of fusion triggering
    • Connolly SA, Leser GP, Jardetzky TS, Lamb RA (2009) Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: Implications for the mechanism of fusion triggering. JVirol83(21): 10857-10868.
    • (2009) JVirol83 , vol.21 , pp. 10857-10868
    • Connolly, S.A.1    Leser, G.P.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 50
    • 84888072258 scopus 로고    scopus 로고
    • Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability
    • Bose S, et al. (2013) Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability. J Virol 87 (24):13520-13531.
    • (2013) J Virol , vol.87 , Issue.24 , pp. 13520-13531
    • Bose, S.1
  • 51
    • 84907432523 scopus 로고    scopus 로고
    • Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies
    • Welch BD, et al. (2014) Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies. J Virol 88(20):11713-11725.
    • (2014) J Virol , vol.88 , Issue.20 , pp. 11713-11725
    • Welch, B.D.1
  • 52
    • 0002285832 scopus 로고
    • The molecular biology of influenza viruses and paramyxoviruses
    • eds Davidson A, Elliott RM (IRL Oxford Univ Press, Oxford)
    • Paterson RG, Lamb RA (1993) The molecular biology of influenza viruses and paramyxoviruses. Molecular Virology: A Practical Approach, eds Davidson A, Elliott RM (IRL Oxford Univ Press, Oxford), pp 35-73.
    • (1993) Molecular Virology: A Practical Approach , pp. 35-73
    • Paterson, R.G.1    Lamb, R.A.2
  • 55
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips JC, et al. (2005) Scalable molecular dynamics with NAMD. J Comput Chem 26(16):1781-1802.
    • (2005) J Comput Chem , vol.26 , Issue.16 , pp. 1781-1802
    • Phillips, J.C.1
  • 56
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V, et al. (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65(3):712-725.
    • (2006) Proteins , vol.65 , Issue.3 , pp. 712-725
    • Hornak, V.1
  • 58
    • 84863083844 scopus 로고    scopus 로고
    • Evaluating the effects of cutoffs and treatment of long-range electrostatics in protein folding simulations
    • Piana S, et al. (2012) Evaluating the effects of cutoffs and treatment of long-range electrostatics in protein folding simulations. PLoS One 7(6):e39918.
    • (2012) PLoS One , vol.7 , Issue.6 , pp. e39918
    • Piana, S.1
  • 59
    • 84864698047 scopus 로고    scopus 로고
    • Dynamical probing of allosteric control in nuclear receptors
    • Cunningham MA (2012) Dynamical probing of allosteric control in nuclear receptors. J Mol Model 18(7):3147-3152.
    • (2012) J Mol Model , vol.18 , Issue.7 , pp. 3147-3152
    • Cunningham, M.A.1
  • 60
    • 41349089279 scopus 로고    scopus 로고
    • Convergence of sampling in protein simulations
    • Hess B (2002) Convergence of sampling in protein simulations. Phys Rev E Stat Nonlin Soft Matter Phys 65(3 Pt 1):031910.
    • (2002) Phys Rev e Stat Nonlin Soft Matter Phys , vol.65 , Issue.3 , pp. 031910
    • Hess, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.