메뉴 건너뛰기




Volumn 10, Issue 9, 2014, Pages

Functional Fluorescent Protein Insertions in Herpes Simplex Virus gB Report on gB Conformation before and after Execution of Membrane Fusion

Author keywords

[No Author keywords available]

Indexed keywords

CERULEAN FLUORESCENT PROTEIN; FLUORESCENT PROTEIN; UNCLASSIFIED DRUG; VENUS FLUORESCENT PROTEIN; VIRUS GLYCOPROTEIN; VIRUS GLYCOPROTEIN GB; BACTERIAL PROTEIN; GLYCOPROTEIN B, SIMPLEXVIRUS; PHOTOPROTEIN; VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN; YELLOW FLUORESCENT PROTEIN, BACTERIA;

EID: 84907584425     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004373     Document Type: Article
Times cited : (38)

References (63)
  • 1
    • 0037108418 scopus 로고    scopus 로고
    • Age-specific prevalence of infection with herpes simplex virus types 2 and 1: a global review
    • Smith JS, Robinson NJ, (2002) Age-specific prevalence of infection with herpes simplex virus types 2 and 1: a global review. J Infect Dis 186: Suppl 1 S3–28.
    • (2002) J Infect Dis , vol.186 , pp. S3-S28
    • Smith, J.S.1    Robinson, N.J.2
  • 2
    • 77951244078 scopus 로고    scopus 로고
    • Seroprevalence of herpes simplex virus type 2 among persons aged 14–49 years–United States, 2005–2008
    • CDC (2010) Seroprevalence of herpes simplex virus type 2 among persons aged 14–49 years–United States, 2005–2008. MMWR Morb Mortal Wkly Rep 59: 456–459.
    • (2010) MMWR Morb Mortal Wkly Rep , vol.59 , pp. 456-459
  • 3
    • 79953848750 scopus 로고    scopus 로고
    • Genital shedding of herpes simplex virus among symptomatic and asymptomatic persons with HSV-2 infection
    • Tronstein E, Johnston C, Huang ML, Selke S, Magaret A, et al. (2011) Genital shedding of herpes simplex virus among symptomatic and asymptomatic persons with HSV-2 infection. JAMA 305: 1441–1449.
    • (2011) JAMA , vol.305 , pp. 1441-1449
    • Tronstein, E.1    Johnston, C.2    Huang, M.L.3    Selke, S.4    Magaret, A.5
  • 4
    • 84865157180 scopus 로고    scopus 로고
    • Herpes simplex epithelial and stromal keratitis: an epidemiologic update
    • Farooq AV, Shukla D, (2012) Herpes simplex epithelial and stromal keratitis: an epidemiologic update. Surv Ophthalmol 57: 448–462.
    • (2012) Surv Ophthalmol , vol.57 , pp. 448-462
    • Farooq, A.V.1    Shukla, D.2
  • 6
    • 18744382150 scopus 로고    scopus 로고
    • Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1
    • Milne RS, Nicola AV, Whitbeck JC, Eisenberg RJ, Cohen GH, (2005) Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1. J Virol 79: 6655–6663.
    • (2005) J Virol , vol.79 , pp. 6655-6663
    • Milne, R.S.1    Nicola, A.V.2    Whitbeck, J.C.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 7
    • 84863596435 scopus 로고    scopus 로고
    • Ultrastructural visualization of individual tegument protein dissociation during entry of herpes simplex virus 1 into human and rat dorsal root ganglion neurons
    • Aggarwal A, Miranda-Saksena M, Boadle RA, Kelly BJ, Diefenbach RJ, et al. (2012) Ultrastructural visualization of individual tegument protein dissociation during entry of herpes simplex virus 1 into human and rat dorsal root ganglion neurons. J Virol 86: 6123–6137.
    • (2012) J Virol , vol.86 , pp. 6123-6137
    • Aggarwal, A.1    Miranda-Saksena, M.2    Boadle, R.A.3    Kelly, B.J.4    Diefenbach, R.J.5
  • 8
    • 80054000888 scopus 로고    scopus 로고
    • Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin- and cholesterol-dependent
    • Rahn E, Petermann P, Hsu MJ, Rixon FJ, Knebel-Morsdorf D, (2011) Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin- and cholesterol-dependent. PLoS One 6: e25464.
    • (2011) PLoS One , vol.6 , pp. e25464
    • Rahn, E.1    Petermann, P.2    Hsu, M.J.3    Rixon, F.J.4    Knebel-Morsdorf, D.5
  • 9
    • 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
  • 10
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: a structural view of the herpesvirus entry machinery
    • Connolly SA, Jackson JO, Jardetzky TS, Longnecker R, (2011) Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol 9: 369–381.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 12
    • 78049513712 scopus 로고    scopus 로고
    • Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB
    • Atanasiu D, Saw WT, Cohen GH, Eisenberg RJ, (2010) Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB. J Virol 84: 12292–12299.
    • (2010) J Virol , vol.84 , pp. 12292-12299
    • Atanasiu, D.1    Saw, W.T.2    Cohen, G.H.3    Eisenberg, R.J.4
  • 13
    • 84880072554 scopus 로고    scopus 로고
    • Regulation of Herpes Simplex Virus gB-Induced Cell-Cell Fusion by Mutant Forms of gH/gL in the Absence of gD and Cellular Receptors
    • Atanasiu D, Cairns TM, Whitbeck JC, Saw WT, Rao S, et al. (2013) Regulation of Herpes Simplex Virus gB-Induced Cell-Cell Fusion by Mutant Forms of gH/gL in the Absence of gD and Cellular Receptors. MBio 4 e00046–13 doi:10.1128/mBio.00046-13
    • (2013) MBio , vol.4
    • Atanasiu, D.1    Cairns, T.M.2    Whitbeck, J.C.3    Saw, W.T.4    Rao, S.5
  • 14
    • 77950513683 scopus 로고    scopus 로고
    • Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion
    • Atanasiu D, Whitbeck JC, de Leon MP, Lou H, Hannah BP, et al. (2010) Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion. J Virol 84: 3825–3834.
    • (2010) J Virol , vol.84 , pp. 3825-3834
    • Atanasiu, D.1    Whitbeck, J.C.2    De Leon, M.P.3    Lou, H.4    Hannah, B.P.5
  • 15
    • 0037393393 scopus 로고    scopus 로고
    • HIV-1: nature's master of disguise
    • Mascola JR, Montefiori DC, (2003) HIV-1: nature's master of disguise. Nat Med 9: 393–394.
    • (2003) Nat Med , vol.9 , pp. 393-394
    • Mascola, J.R.1    Montefiori, D.C.2
  • 16
    • 77952969448 scopus 로고    scopus 로고
    • Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design
    • Wei CJ, Boyington JC, Dai K, Houser KV, Pearce MB, et al. (2010) Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design. Sci Transl Med 2: 24ra21.
    • (2010) Sci Transl Med , vol.2 , pp. 24ra21
    • Wei, C.J.1    Boyington, J.C.2    Dai, K.3    Houser, K.V.4    Pearce, M.B.5
  • 17
    • 84878349946 scopus 로고    scopus 로고
    • Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    • McLellan JS, Chen M, Leung S, Graepel KW, Du X, et al. (2013) Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody. Science 340: 1113–1117.
    • (2013) Science , vol.340 , pp. 1113-1117
    • Mclellan, J.S.1    Chen, M.2    Leung, S.3    Graepel, K.W.4    Du, X.5
  • 19
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison SC, (2008) Viral membrane fusion. Nat Struct Mol Biol 15: 690–698.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 690-698
    • Harrison, S.C.1
  • 20
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS, (2001) Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 70: 777–810.
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 21
    • 84855673964 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Plemper RK, (2011) Cell entry of enveloped viruses. Curr Opin Virol 1: 92–100.
    • (2011) Curr Opin Virol , vol.1 , pp. 92-100
    • Plemper, R.K.1
  • 22
    • 33746005904 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein B from herpes simplex virus 1
    • Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, 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    Lou, H.2    Bender, F.C.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 23
    • 62449188223 scopus 로고    scopus 로고
    • Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
    • Backovic M, Longnecker R, Jardetzky TS, (2009) Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B. Proc Natl Acad Sci U S A 106: 2880–2885.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2880-2885
    • Backovic, M.1    Longnecker, R.2    Jardetzky, T.S.3
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 64549129051 scopus 로고    scopus 로고
    • Class III viral membrane fusion proteins
    • Backovic M, Jardetzky TS, (2009) Class III viral membrane fusion proteins. Curr Opin Struct Biol 19: 189–196.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 189-196
    • Backovic, M.1    Jardetzky, T.S.2
  • 28
    • 34247115646 scopus 로고    scopus 로고
    • Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions
    • Bender FC, Samanta M, Heldwein EE, de Leon MP, Bilman E, 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    Samanta, M.2    Heldwein, E.E.3    De Leon, M.P.4    Bilman, E.5
  • 29
    • 67449093075 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    • Hannah BP, Cairns TM, Bender FC, Whitbeck JC, Lou H, 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    Cairns, T.M.2    Bender, F.C.3    Whitbeck, J.C.4    Lou, H.5
  • 30
    • 84877706768 scopus 로고    scopus 로고
    • Extensive Mutagenesis of the HSV-1 gB Ectodomain Reveals Remarkable Stability of Its Postfusion Form
    • Vitu E, Sharma S, Stampfer SD, Heldwein EE, (2013) Extensive Mutagenesis of the HSV-1 gB Ectodomain Reveals Remarkable Stability of Its Postfusion Form. J Mol Biol 425: 2056–2071.
    • (2013) J Mol Biol , vol.425 , pp. 2056-2071
    • Vitu, E.1    Sharma, S.2    Stampfer, S.D.3    Heldwein, E.E.4
  • 31
    • 84864021796 scopus 로고    scopus 로고
    • 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
    • Connolly SA, Longnecker R, (2012) 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. J Virol 86: 6386–6393.
    • (2012) J Virol , vol.86 , pp. 6386-6393
    • Connolly, S.A.1    Longnecker, R.2
  • 32
    • 84872166777 scopus 로고    scopus 로고
    • The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes
    • Shelly SS, Cairns TM, Whitbeck JC, Lou H, Krummenacher C, et al. (2012) The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes. MBio 3: e00429–00412.
    • (2012) MBio , vol.3 , pp. 00412-e00429
    • Shelly, S.S.1    Cairns, T.M.2    Whitbeck, J.C.3    Lou, H.4    Krummenacher, C.5
  • 33
    • 0035993289 scopus 로고    scopus 로고
    • Incorporation of green fluorescent protein into the essential envelope glycoprotein B of herpes simplex virus type 1
    • Potel C, Kaelin K, Gautier I, Lebon P, Coppey J, et al. (2002) Incorporation of green fluorescent protein into the essential envelope glycoprotein B of herpes simplex virus type 1. J Virol Methods 105: 13–23.
    • (2002) J Virol Methods , vol.105 , pp. 13-23
    • Potel, C.1    Kaelin, K.2    Gautier, I.3    Lebon, P.4    Coppey, J.5
  • 34
    • 0141731153 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 glycoprotein B sorting in hippocampal neurons
    • Potel C, Kaelin K, Danglot L, Triller A, Vannier C, et al. (2003) Herpes simplex virus type 1 glycoprotein B sorting in hippocampal neurons. J Gen Virol 84: 2613–2624.
    • (2003) J Gen Virol , vol.84 , pp. 2613-2624
    • Potel, C.1    Kaelin, K.2    Danglot, L.3    Triller, A.4    Vannier, C.5
  • 35
    • 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
  • 36
    • 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
  • 37
    • 78649413011 scopus 로고    scopus 로고
    • Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1
    • Stampfer SD, Lou H, Cohen GH, Eisenberg RJ, Heldwein EE, (2010) Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. J Virol 84: 12924–12933.
    • (2010) J Virol , vol.84 , pp. 12924-12933
    • Stampfer, S.D.1    Lou, H.2    Cohen, G.H.3    Eisenberg, R.J.4    Heldwein, E.E.5
  • 38
    • 84870176684 scopus 로고    scopus 로고
    • Generation of a dual-functional split-reporter protein for monitoring membrane fusion using self-associating split GFP
    • Ishikawa H, Meng F, Kondo N, Iwamoto A, Matsuda Z, (2012) Generation of a dual-functional split-reporter protein for monitoring membrane fusion using self-associating split GFP. Protein Eng Des Sel 25: 813–820.
    • (2012) Protein Eng Des Sel , vol.25 , pp. 813-820
    • Ishikawa, H.1    Meng, F.2    Kondo, N.3    Iwamoto, A.4    Matsuda, Z.5
  • 39
    • 84886891960 scopus 로고    scopus 로고
    • Dual Split Protein-Based Fusion Assay Reveals that Mutations to Herpes Simplex Virus (HSV) Glycoprotein gB Alter the Kinetics of Cell-Cell Fusion Induced by HSV Entry Glycoproteins
    • Atanasiu D, Saw WT, Gallagher JR, Hannah BP, Matsuda Z, et al. (2013) Dual Split Protein-Based Fusion Assay Reveals that Mutations to Herpes Simplex Virus (HSV) Glycoprotein gB Alter the Kinetics of Cell-Cell Fusion Induced by HSV Entry Glycoproteins. J Virol 87: 11332–11345.
    • (2013) J Virol , vol.87 , pp. 11332-11345
    • Atanasiu, D.1    Saw, W.T.2    Gallagher, J.R.3    Hannah, B.P.4    Matsuda, Z.5
  • 40
    • 0031963977 scopus 로고    scopus 로고
    • Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system
    • Turner A, Bruun B, Minson T, Browne H, (1998) Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system. J Virol 72: 873–875.
    • (1998) J Virol , vol.72 , pp. 873-875
    • Turner, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 41
    • 84896724942 scopus 로고    scopus 로고
    • Mechanism of neutralization of HSV by antibodies directed at the fusion domain of glycoprotein B
    • Cairns TM, Fontana J, Huang ZY, Whitbeck JC, Atanasiu D, et al. (2014) Mechanism of neutralization of HSV by antibodies directed at the fusion domain of glycoprotein B. J Virol 88: 2677–89 doi:10.1128/JVI.03200-13
    • (2014) J Virol , vol.88 , pp. 2677-2689
    • Cairns, T.M.1    Fontana, J.2    Huang, Z.Y.3    Whitbeck, J.C.4    Atanasiu, D.5
  • 42
    • 0021715322 scopus 로고
    • Evidence for post-translational glycosylation of a nonglycosylated precursor protein of herpes simplex virus type 1
    • Compton T, Courtney RJ, (1984) Evidence for post-translational glycosylation of a nonglycosylated precursor protein of herpes simplex virus type 1. J Virol 52: 630–637.
    • (1984) J Virol , vol.52 , pp. 630-637
    • Compton, T.1    Courtney, R.J.2
  • 43
    • 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
  • 44
    • 84859867549 scopus 로고    scopus 로고
    • Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cells
    • Day RN, Davidson MW, (2012) Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cells. Bioessays 34: 341–350.
    • (2012) Bioessays , vol.34 , pp. 341-350
    • Day, R.N.1    Davidson, M.W.2
  • 45
    • 24644432375 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry
    • Bender FC, Whitbeck JC, Lou H, Cohen GH, Eisenberg RJ, (2005) Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry. J Virol 79: 11588–11597.
    • (2005) J Virol , vol.79 , pp. 11588-11597
    • Bender, F.C.1    Whitbeck, J.C.2    Lou, H.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 46
    • 11144232294 scopus 로고    scopus 로고
    • Engineering glycoprotein B of bovine herpesvirus 1 to function as transporter for secreted proteins: a new protein expression approach
    • Keil GM, Hohle C, Giesow K, Konig P, (2005) Engineering glycoprotein B of bovine herpesvirus 1 to function as transporter for secreted proteins: a new protein expression approach. J Virol 79: 791–799.
    • (2005) J Virol , vol.79 , pp. 791-799
    • Keil, G.M.1    Hohle, C.2    Giesow, K.3    Konig, P.4
  • 47
    • 84881477785 scopus 로고    scopus 로고
    • The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction
    • Maurer UE, Zeev-Ben-Mordehai T, Pandurangan AP, Cairns TM, Hannah BP, et al. (2013) The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction. Structure 21: 1396–1405.
    • (2013) Structure , vol.21 , pp. 1396-1405
    • Maurer, U.E.1    Zeev-Ben-Mordehai, T.2    Pandurangan, A.P.3    Cairns, T.M.4    Hannah, B.P.5
  • 49
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • Guerriero CJ, Brodsky JL, (2011) The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiol Rev 92: 537–576.
    • (2011) Physiol Rev , vol.92 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 51
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway
    • Nicola AV, Hou J, Major EO, Straus SE, (2005) Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent 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    Straus, S.E.4
  • 52
    • 84867084476 scopus 로고    scopus 로고
    • Improving FRET dynamic range with bright green and red fluorescent proteins
    • Lam AJ, St-Pierre F, Gong Y, Marshall JD, Cranfill PJ, et al. (2012) Improving FRET dynamic range with bright green and red fluorescent proteins. Nat Methods 9: 1005–1012.
    • (2012) Nat Methods , vol.9 , pp. 1005-1012
    • Lam, A.J.1    St-Pierre, F.2    Gong, Y.3    Marshall, J.D.4    Cranfill, P.J.5
  • 53
    • 33845443776 scopus 로고    scopus 로고
    • Cerulean, Venus, and VenusY67C FRET reference standards
    • Koushik SV, Chen H, Thaler C, Puhl HL, 3rdVogel SS, (2006) Cerulean, Venus, and VenusY67C FRET reference standards. Biophys J 91: L99–L101.
    • (2006) Biophys J , vol.91 , pp. L99-L101
    • Koushik, S.V.1    Chen, H.2    Thaler, C.3    Puhl, H.L.4    Vogel, S.S.5
  • 54
    • 51649126210 scopus 로고    scopus 로고
    • Energy migration alters the fluorescence lifetime of Cerulean: implications for fluorescence lifetime imaging Forster resonance energy transfer measurements
    • Koushik SV, Vogel SS, (2008) Energy migration alters the fluorescence lifetime of Cerulean: implications for fluorescence lifetime imaging Forster resonance energy transfer measurements. J Biomed Opt 13: 031204.
    • (2008) J Biomed Opt , vol.13 , pp. 031204
    • Koushik, S.V.1    Vogel, S.S.2
  • 55
    • 73949125038 scopus 로고    scopus 로고
    • Retrograde axon transport of herpes simplex virus and pseudorabies virus: a live-cell comparative analysis
    • Antinone SE, Smith GA, (2010) Retrograde axon transport of herpes simplex virus and pseudorabies virus: a live-cell comparative analysis. J Virol 84: 1504–1512.
    • (2010) J Virol , vol.84 , pp. 1504-1512
    • Antinone, S.E.1    Smith, G.A.2
  • 56
    • 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
  • 57
    • 34547567980 scopus 로고    scopus 로고
    • OligoCalc: an online oligonucleotide properties calculator
    • Kibbe WA, (2007) OligoCalc: an online oligonucleotide properties calculator. Nucleic Acids Res 35: W43–46.
    • (2007) Nucleic Acids Res , vol.35 , pp. W43-46
    • Kibbe, W.A.1
  • 58
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis
    • Wang W, Malcolm BA, (1999) Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange Site-Directed Mutagenesis. Biotechniques 26: 680–682.
    • (1999) Biotechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 59
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C, Vieira J, Messing J, (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103–119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 60
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa H, Yamamura K, Miyazaki J, (1991) Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108: 193–199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 61
    • 0034986067 scopus 로고    scopus 로고
    • Development of a syngenic murine B16 cell line-derived melanoma susceptible to destruction by neuroattenuated HSV-1
    • Miller CG, Krummenacher C, Eisenberg RJ, Cohen GH, Fraser NW, (2001) Development of a syngenic murine B16 cell line-derived melanoma susceptible to destruction by neuroattenuated HSV-1. Mol Ther 3: 160–168.
    • (2001) Mol Ther , vol.3 , pp. 160-168
    • Miller, C.G.1    Krummenacher, C.2    Eisenberg, R.J.3    Cohen, G.H.4    Fraser, N.W.5
  • 62
    • 0022498630 scopus 로고
    • Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing (“native” gel) system of polyacrylamide gel electrophoresis coupled with Western blotting
    • Cohen GH, Isola VJ, Kuhns J, Berman PW, Eisenberg RJ, (1986) Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing (“native” gel) system of polyacrylamide gel electrophoresis coupled with Western blotting. J Virol 60: 157–166.
    • (1986) J Virol , vol.60 , pp. 157-166
    • Cohen, G.H.1    Isola, V.J.2    Kuhns, J.3    Berman, P.W.4    Eisenberg, R.J.5
  • 63
    • 0027954404 scopus 로고
    • High-level expression and purification of secreted forms of herpes simplex virus type 1 glycoprotein gD synthesized by baculovirus-infected insect cells
    • Sisk WP, Bradley JD, Leipold RJ, Stoltzfus AM, Ponce de Leon M, et al. (1994) High-level expression and purification of secreted forms of herpes simplex virus type 1 glycoprotein gD synthesized by baculovirus-infected insect cells. J Virol 68: 766–775.
    • (1994) J Virol , vol.68 , pp. 766-775
    • Sisk, W.P.1    Bradley, J.D.2    Leipold, R.J.3    Stoltzfus, A.M.4    Ponce De Leon, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.