메뉴 건너뛰기




Volumn 86, Issue 12, 2012, Pages 6386-6393

Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein b ectodomain contribute to its refolding during the fusion step of virus entry

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN B;

EID: 84864021796     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00104-12     Document Type: Article
Times cited : (26)

References (61)
  • 1
  • 2
    • 34548158909 scopus 로고    scopus 로고
    • Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity
    • Backovic M, Jardetzky TS, Longnecker R. 2007. Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity. J. Virol. 81:9596 -9600.
    • (2007) J. Virol. , vol.81 , pp. 9596-9600
    • Backovic, M.1    Jardetzky, T.S.2    Longnecker, R.3
  • 4
    • 0027461939 scopus 로고
    • Truncation of the carboxy-terminal 28 amino acids of glycoprotein B specified by herpes simplex virus type 1 mutant amb1511-7 causes extensive cell fusion
    • Baghian A, Huang L, Newman S, Jayachandra S, Kousoulas KG. 1993. Truncation of the carboxy-terminal 28 amino acids of glycoprotein B specified by herpes simplex virus type 1 mutant amb1511-7 causes extensive cell fusion. J. Virol. 67:2396 -2401.
    • (1993) J. Virol. , vol.67 , pp. 2396-2401
    • Baghian, A.1    Huang, L.2    Newman, S.3    Jayachandra, S.4    Kousoulas, K.G.5
  • 5
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker KA, Dutch RE, Lamb RA, Jardetzky TS. 1999. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3:309 -319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 6
    • 34247115646 scopus 로고    scopus 로고
    • Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions
    • Bender FC, et al. 2007. Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions. J. Virol. 81: 3827-3841.
    • (2007) J. Virol. , vol.81 , pp. 3827-3841
    • Bender, F.C.1
  • 7
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. 1994. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature 371: 37- 43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 8
    • 0023101293 scopus 로고
    • Linkerinsertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1
    • Cai WZ, Person S, Warner SC, Zhou JH, DeLuca NA. 1987. Linkerinsertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1. J. Virol. 61:714-721.
    • (1987) J. Virol. , vol.61 , pp. 714-721
    • Cai, W.Z.1    Person, S.2    Warner, S.C.3    Zhou, J.H.4    DeLuca, N.A.5
  • 9
    • 80052075784 scopus 로고    scopus 로고
    • Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment
    • Cairns TM, et al. 2011. Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment. J. Virol. 85:6175- 6184.
    • (2011) J. Virol. , vol.85 , pp. 6175-6184
    • Cairns, T.M.1
  • 10
    • 77951490223 scopus 로고    scopus 로고
    • Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions
    • Chowdary TK, Heldwein EE. 2010. Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions. J. Virol. 84:4923- 4935.
    • (2010) J. Virol. , vol.84 , pp. 4923-4935
    • Chowdary, T.K.1    Heldwein, E.E.2
  • 11
  • 12
    • 0038758772 scopus 로고    scopus 로고
    • Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface
    • Connolly SA, et al. 2003. Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface. J. Virol. 77:8127- 8140.
    • (2003) J. Virol. , vol.77 , pp. 8127-8140
    • Connolly, S.A.1
  • 13
    • 0033809570 scopus 로고    scopus 로고
    • Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein
    • Delos SE, White JM. 2000. Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein. J. Virol 74:9738 -9741.
    • (2000) J. Virol , vol.74 , pp. 9738-9741
    • Delos, S.E.1    White, J.M.2
  • 14
    • 77549086793 scopus 로고    scopus 로고
    • Low pH-induced conformational change in herpes simplex virus glycoprotein B
    • Dollery SJ, Delboy MG, Nicola AV. 2010. Low pH-induced conformational change in herpes simplex virus glycoprotein B. J. Virol. 84:3759- 3766.
    • (2010) J. Virol. , vol.84 , pp. 3759-3766
    • Dollery, S.J.1    Delboy, M.G.2    Nicola, A.V.3
  • 15
    • 80053964873 scopus 로고    scopus 로고
    • Low-pHdependent changes in the conformational and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity
    • Dollery SJ, Wright CC, Johnson DC, Nicola AV. 2011. Low-pHdependent changes in the conformational and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity. J. Virol. 85:9964 -9973.
    • (2011) J. Virol. , vol.85 , pp. 9964-9973
    • Dollery, S.J.1    Wright, C.C.2    Johnson, D.C.3    Nicola, A.V.4
  • 16
    • 0036720396 scopus 로고    scopus 로고
    • Truncation of herpes simplex virus type 2 glycoprotein B increases its cell surface expression and activity in cell-cell fusion, but these properties are unrelated
    • Fan Z, et al. 2002. Truncation of herpes simplex virus type 2 glycoprotein B increases its cell surface expression and activity in cell-cell fusion, but these properties are unrelated. J. Virol. 76:9271-9283.
    • (2002) J. Virol. , vol.76 , pp. 9271-9283
    • Fan, Z.1
  • 17
    • 84875007392 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 18
    • 0035882168 scopus 로고    scopus 로고
    • An alpha-helical domain within the carboxyl terminus of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) is associated with cell fusion and resistance to heparin inhibition of cell fusion
    • Foster TP, Melancon JM, Kousoulas KG. 2001. An alpha-helical domain within the carboxyl terminus of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) is associated with cell fusion and resistance to heparin inhibition of cell fusion. Virology 287:18 -29.
    • (2001) Virology , vol.287 , pp. 18-29
    • Foster, T.P.1    Melancon, J.M.2    Kousoulas, K.G.3
  • 19
    • 43149104981 scopus 로고    scopus 로고
    • The identification and characterization of fusogenic domains in herpesvirus glycoprotein B molecules
    • Galdiero S, et al. 2008. The identification and characterization of fusogenic domains in herpesvirus glycoprotein B molecules. Chem. Biochem. 9:758 -767.
    • (2008) Chem. Biochem. , vol.9 , pp. 758-767
    • Galdiero, S.1
  • 20
    • 0034007798 scopus 로고    scopus 로고
    • Cellular expression of alphaherpesvirus gD interferes with entry of homologous and heterologous alphaherpesviruses by blocking access to a shared gD receptor
    • Geraghty RJ, Jogger CR, Spear PG. 2000. Cellular expression of alphaherpesvirus gD interferes with entry of homologous and heterologous alphaherpesviruses by blocking access to a shared gD receptor. Virology 268:147-158.
    • (2000) Virology , vol.268 , pp. 147-158
    • Geraghty, R.J.1    Jogger, C.R.2    Spear, P.G.3
  • 21
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280:1618 -1620.
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 22
    • 67449093075 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    • Hannah BP, et al. 2009. Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops. J. Virol. 83:6825- 6836.
    • (2009) J. Virol. , vol.83 , pp. 6825-6836
    • Hannah, B.P.1
  • 24
    • 44749091723 scopus 로고    scopus 로고
    • Entry of herpesviruses into mammalian cells
    • Heldwein EE, Krummenacher C. 2008. Entry of herpesviruses into mammalian cells. Cell. Mol. Life Sci. 65:1653-1668.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1653-1668
    • Heldwein, E.E.1    Krummenacher, C.2
  • 25
    • 33746005904 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein B from herpes simplex virus 1
    • Heldwein EE, et al. 2006. Crystal structure of glycoprotein B from herpes simplex virus 1. Science 313:217-220.
    • (2006) Science , vol.313 , pp. 217-220
    • Heldwein, E.E.1
  • 26
    • 0028236443 scopus 로고
    • Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulfate and glycoprotein B
    • Herold BC, Visalli RJ, Susmarski N, Brandt CR, Spear PG. 1994. Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulfate and glycoprotein B. J. Gen. Virol. 75: 1211-1222.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1211-1222
    • Herold, B.C.1    Visalli, R.J.2    Susmarski, N.3    Brandt, C.R.4    Spear, P.G.5
  • 27
    • 0026026623 scopus 로고
    • Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity
    • Herold BC, WuDunn D, Soltys N, Spear PG. 1991. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 65:1090 -1098.
    • (1991) J. Virol. , vol.65 , pp. 1090-1098
    • Herold, B.C.1    WuDunn, D.2    Soltys, N.3    Spear, P.G.4
  • 28
    • 0023941343 scopus 로고
    • Monoclonal antibodies define a domain on herpes simplex virus glycoprotein B involved in virus penetration
    • Highlander SL, Cai WH, Person S, Levine M, Glorioso JC. 1988. Monoclonal antibodies define a domain on herpes simplex virus glycoprotein B involved in virus penetration. J. Virol. 62:1881-1888.
    • (1988) J. Virol. , vol.62 , pp. 1881-1888
    • Highlander, S.L.1    Cai, W.H.2    Person, S.3    Levine, M.4    Glorioso, J.C.5
  • 29
    • 84055179004 scopus 로고    scopus 로고
    • X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation
    • Igonet S, et al. 2011. X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation. Proc. Natl. Acad. Sci. U. S. A. 108:19967-19972.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 19967-19972
    • Igonet, S.1
  • 30
    • 0032849336 scopus 로고    scopus 로고
    • Mutational analysis of the putative fusion domain of Ebola virus glycoprotein
    • Ito H, Watanabe S, Sanchez A, Whitt MA, Kawaoka Y. 1999. Mutational analysis of the putative fusion domain of Ebola virus glycoprotein. J. Virol. 73:8907- 8912.
    • (1999) J. Virol. , vol.73 , pp. 8907-8912
    • Ito, H.1    Watanabe, S.2    Sanchez, A.3    Whitt, M.A.4    Kawaoka, Y.5
  • 31
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J, Loureiro S, Abrescia NG, Stuart DI, Jones IM. 2008. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 15:1024 -1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 32
    • 34547585371 scopus 로고    scopus 로고
    • Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-1 are critical for pH-dependent membrane fusion and infectivity
    • Klewitz C, Klenk HD, ter Meulen J. 2007. Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-1 are critical for pH-dependent membrane fusion and infectivity. J. Gen. Virol. 88:2320 -2328.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2320-2328
    • Klewitz, C.1    Klenk, H.D.2    ter Meulen, J.3
  • 33
    • 0033551053 scopus 로고    scopus 로고
    • Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins
    • Kobe B, Center RJ, Kemp BE, Poumbourios P. 1999. Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins. Proc. Natl. Acad. Sci. U. S. A. 96:4319-4324.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4319-4324
    • Kobe, B.1    Center, R.J.2    Kemp, B.E.3    Poumbourios, P.4
  • 34
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: lessons from paramyxovirus F
    • Lamb RA, Jardetzky TS. 2007. Structural basis of viral invasion: lessons from paramyxovirus F. Curr. Opin. Struct. Biol. 17:427- 436.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 35
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee JE, et al. 2008. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454:177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1
  • 36
    • 82755163036 scopus 로고    scopus 로고
    • Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugating peptide, a new antiviral strategy for influenza virus
    • Lee KK, et al. 2011. Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugating peptide, a new antiviral strategy for influenza virus. J. Biol. Chem. 286:42141- 42149.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42141-42149
    • Lee, K.K.1
  • 37
    • 33645796461 scopus 로고    scopus 로고
    • Identification of functional domains in herpes simplex virus 2 glycoprotein B
    • Li W, Minova-Foster TJ, Norton DD, Muggeridge MI. 2006. Identification of functional domains in herpes simplex virus 2 glycoprotein B. J. Virol. 80:3792-3800.
    • (2006) J. Virol. , vol.80 , pp. 3792-3800
    • Li, W.1    Minova-Foster, T.J.2    Norton, D.D.3    Muggeridge, M.I.4
  • 38
    • 34548778580 scopus 로고    scopus 로고
    • Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B
    • Lin E, Spear PG. 2007. Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B. Proc. Natl. Acad. Sci. U. S. A. 104:13140 -13145.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 13140-13145
    • Lin, E.1    Spear, P.G.2
  • 39
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, et al. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413- 423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1
  • 40
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • Montgomery RI, Warner MS, Lum BJ, Spear PG. 1996. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87:427- 436.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 41
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pHdependent endocytic pathway
    • Nicola AV, Hou J, Major EO, Stras SE. 2005. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pHdependent endocytic pathway. J. Virol. 79:7609 -7616.
    • (2005) J. Virol. , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3    Stras, S.E.4
  • 42
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • Nicola AV, McEvoy AM, Straus SE. 2003. Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J. Virol. 77:5324 -5332.
    • (2003) J. Virol. , vol.77 , pp. 5324-5332
    • Nicola, A.V.1    McEvoy, A.M.2    Straus, S.E.3
  • 43
    • 0031835330 scopus 로고    scopus 로고
    • Use of a neural network secondary structure prediction to define targets to mutagenesis of herpes simplex virus glycoprotein B
    • Norton DD, Dwyer DS, Muggeridge MI. 1998. Use of a neural network secondary structure prediction to define targets to mutagenesis of herpes simplex virus glycoprotein B. Virus Res. 55:37- 48.
    • (1998) Virus Res , vol.55 , pp. 37-48
    • Norton, D.D.1    Dwyer, D.S.2    Muggeridge, M.I.3
  • 44
    • 0033557076 scopus 로고    scopus 로고
    • Host range of human T-cell leukemia virus type I analyzed by a cell fusiondependent reporter gene activation assay
    • Okuma K, Nakamura M, Nakano S, Niho Y, Matsuura Y. 1999. Host range of human T-cell leukemia virus type I analyzed by a cell fusiondependent reporter gene activation assay. Virology 254:235-244.
    • (1999) Virology , vol.254 , pp. 235-244
    • Okuma, K.1    Nakamura, M.2    Nakano, S.3    Niho, Y.4    Matsuura, Y.5
  • 45
    • 0022372539 scopus 로고
    • Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions
    • Para MF, Parish ML, Nobel AG, Spear PG. 1985. Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions. J. Virol. 55:483- 488.
    • (1985) J. Virol. , vol.55 , pp. 483-488
    • Para, M.F.1    Parish, M.L.2    Nobel, A.G.3    Spear, P.G.4
  • 46
    • 0345059375 scopus 로고    scopus 로고
    • Leash in the groove mechanism of membrane fusion
    • Park HE, Gruenke JA, White JM. 2003. Leash in the groove mechanism of membrane fusion. Nat. Struct. Biol. 10:1048 -1053.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1048-1053
    • Park, H.E.1    Gruenke, J.A.2    White, J.M.3
  • 47
    • 0024458284 scopus 로고
    • Domain structure of herpes simplex virus 1 glycoprotein B: neutralizing epitopes map in regions of continuous and discontinuous residues
    • Pereira L, Ali M, Kousoulas K, Huo B, Banks T. 1989. Domain structure of herpes simplex virus 1 glycoprotein B: neutralizing epitopes map in regions of continuous and discontinuous residues. Virology 172:11-24.
    • (1989) Virology , vol.172 , pp. 11-24
    • Pereira, L.1    Ali, M.2    Kousoulas, K.3    Huo, B.4    Banks, T.5
  • 48
    • 0035915995 scopus 로고    scopus 로고
    • Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate
    • Pertel PE, Fridberg A, Parish ML, Spear PG. 2001. Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate. Virology 279:313-324.
    • (2001) Virology , vol.279 , pp. 313-324
    • Pertel, P.E.1    Fridberg, A.2    Parish, M.L.3    Spear, P.G.4
  • 49
    • 0037372265 scopus 로고    scopus 로고
    • An antiviral peptide targets a coiled-coil domain of human T-cell leukemia virus envelope protein
    • Pinon JD, Kelly SM, Price NC, Flanagan JU, Brightly DW. 2003. An antiviral peptide targets a coiled-coil domain of human T-cell leukemia virus envelope protein. J. Virol. 77:3281-3290.
    • (2003) J. Virol. , vol.77 , pp. 3281-3290
    • Pinon, J.D.1    Kelly, S.M.2    Price, N.C.3    Flanagan, J.U.4    Brightly, D.W.5
  • 50
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche S, Bressanelli S, Rey FA, Gaudin Y. 2006. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 313:187-191.
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 51
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • Roche S, Rey FA, Gaudin Y, Bressanelli S. 2007. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 315: 843-848.
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 52
    • 32844470262 scopus 로고    scopus 로고
    • Alanine substitution of conserved residues in the cytoplasmic tail of herpes simplex virus gB can enhance or abolish cell fusion activity and viral entry
    • Ruel N, Zago A, Spear PG. 2006. Alanine substitution of conserved residues in the cytoplasmic tail of herpes simplex virus gB can enhance or abolish cell fusion activity and viral entry. Virology 346:229 -237.
    • (2006) Virology , vol.346 , pp. 229-237
    • Ruel, N.1    Zago, A.2    Spear, P.G.3
  • 53
    • 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. 20:4024- 4034.
    • (2001) EMBO J , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 54
    • 75449120351 scopus 로고    scopus 로고
    • Fusiondeficient insertion mutants of herpes simplex virus 1 glycoprotein B adopt the trimeric postfusion conformation
    • Silverman JL, Sharma S, Cairns TM, Heldwein EE. 2010. Fusiondeficient insertion mutants of herpes simplex virus 1 glycoprotein B adopt the trimeric postfusion conformation. J. Virol. 84:2001-2012.
    • (2010) J. Virol. , vol.84 , pp. 2001-2012
    • Silverman, J.L.1    Sharma, S.2    Cairns, T.M.3    Heldwein, E.E.4
  • 55
    • 78649413011 scopus 로고    scopus 로고
    • Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus 1
    • Stampfer SD, Lou H, Cohen GC, Eisenberg RJ, Heldwein EE. 2010. Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus 1. J. Virol. 84:12924 -12933.
    • (2010) J. Virol. , vol.84 , pp. 12924-12933
    • Stampfer, S.D.1    Lou, H.2    Cohen, G.C.3    Eisenberg, R.J.4    Heldwein, E.E.5
  • 56
    • 3042550474 scopus 로고    scopus 로고
    • Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail
    • Waning DL, Russell CJ, Jardetzky TS, Lamb RA. 2004. Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail. Proc. Natl. Acad. Sci. U. S. A. 101:9217-9222.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9217-9222
    • Waning, D.L.1    Russell, C.J.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 58
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White JM, Delos SE, Brecher M, Schornberg K. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189 -219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 59
    • 84875003375 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 60
    • 25144488199 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain on the gp41 cytoplasmic tail
    • Wyss S, et al. 2005. Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain on the gp41 cytoplasmic tail. J. Virol. 79:12231-12241.
    • (2005) J. Virol. , vol.79 , pp. 12231-12241
    • Wyss, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.