메뉴 건너뛰기




Volumn 4, Issue 1, 2013, Pages

Modulation of Epstein-Barr virus glycoprotein B (gB) fusion activity by the gB cytoplasmic tail domain

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLYCOPROTEIN B; HYBRID PROTEIN; EPSTEIN BARR VIRUS GLYCOPROTEIN GP110; EPSTEIN-BARR VIRUS GLYCOPROTEIN GP110; MUTANT PROTEIN; VIRUS PROTEIN;

EID: 84874610863     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00571-12     Document Type: Article
Times cited : (30)

References (60)
  • 1
    • 34249064632 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Rickinson AB, Kieff E. 2007. Epstein-Barr virus, p 2657-2701. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 2657-2701
    • Rickinson, A.B.1    Kieff, E.2
  • 3
    • 0033610075 scopus 로고    scopus 로고
    • A model for persistent infection with Epstein-Barr virus: The stealth virus of human B cells
    • Thorley-Lawson DA, Babcock GJ. 1999. A model for persistent infection with Epstein-Barr virus: the stealth virus of human B cells. Life Sci. 65: 1433-1453.
    • (1999) Life Sci. , vol.65 , pp. 1433-1453
    • Thorley-Lawson, D.A.1    Babcock, G.J.2
  • 4
    • 0141632878 scopus 로고    scopus 로고
    • Herpesvirus entry: An update
    • Spear PG, Longnecker R. 2003. Herpesvirus entry: an update. J. Virol. 77:10179-10185.
    • (2003) J. Virol. , vol.77 , pp. 10179-10185
    • Spear, P.G.1    Longnecker, R.2
  • 5
  • 6
    • 0022382343 scopus 로고
    • Epstein-Barr virus genome may encode a protein showing significant amino acid and predicted secondary structure homology with glycoprotein B of herpes simplex virus 1
    • Pellett PE, Biggin MD, Barrell B, Roizman B. 1985. Epstein-Barr virus genome may encode a protein showing significant amino acid and predicted secondary structure homology with glycoprotein B of herpes simplex virus 1. J. Virol. 56:807-813.
    • (1985) J. Virol. , vol.56 , pp. 807-813
    • Pellett, P.E.1    Biggin, M.D.2    Barrell, B.3    Roizman, B.4
  • 7
    • 35348938515 scopus 로고    scopus 로고
    • Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins
    • Backovic M, Leser GP, Lamb RA, Longnecker R, Jardetzky TS. 2007. Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins. Virology 368:102-113.
    • (2007) Virology , vol.368 , pp. 102-113
    • Backovic, M.1    Leser, G.P.2    Lamb, R.A.3    Longnecker, R.4    Jardetzky, T.S.5
  • 8
    • 0027244528 scopus 로고
    • Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring
    • Rasile L, Ghosh K, Raviprakash K, Ghosh HP. 1993. Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring. J. Virol. 67:4856-4866.
    • (1993) J. Virol. , vol.67 , pp. 4856-4866
    • Rasile, L.1    Ghosh, K.2    Raviprakash, K.3    Ghosh, H.P.4
  • 9
    • 0023115697 scopus 로고
    • Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB
    • Gong M, Ooka T, Matsuo T, Kieff E. 1987. Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J. Virol. 61:499-508.
    • (1987) J. Virol. , vol.61 , pp. 499-508
    • Gong, M.1    Ooka, T.2    Matsuo, T.3    Kieff, E.4
  • 10
    • 0027933801 scopus 로고
    • Function of glycoprotein B homologues of the family Herpesviridae
    • Pereira L. 1994. Function of glycoprotein B homologues of the family Herpesviridae. Infect. Agents Dis. 3:9-28.
    • (1994) Infect. Agents Dis. , vol.3 , pp. 9-28
    • Pereira, L.1
  • 13
    • 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
  • 14
    • 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
  • 16
    • 34247570805 scopus 로고    scopus 로고
    • Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B
    • Hannah BP, Heldwein EE, Bender FC, Cohen GH, Eisenberg RJ. 2007. Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B. J. Virol. 81:4858-4865.
    • (2007) J. Virol. , vol.81 , pp. 4858-4865
    • Hannah, B.P.1    Heldwein, E.E.2    Bender, F.C.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 17
    • 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
  • 18
    • 0025218465 scopus 로고
    • Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110
    • Gong M, Kieff E. 1990. Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. J. Virol. 64:1507-1516.
    • (1990) J. Virol. , vol.64 , pp. 1507-1516
    • Gong, M.1    Kieff, E.2
  • 19
    • 0030935618 scopus 로고    scopus 로고
    • The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication
    • Lee SK, Longnecker R. 1997. The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication. J. Virol. 71:4092-4097.
    • (1997) J. Virol. , vol.71 , pp. 4092-4097
    • Lee, S.K.1    Longnecker, R.2
  • 20
    • 0344718027 scopus 로고    scopus 로고
    • Four consecutive arginine residues at positions 836-839 of EBV gp110 determine intracellular localization of gp110
    • Lee SK. 1999. Four consecutive arginine residues at positions 836-839 of EBV gp110 determine intracellular localization of gp110. Virology 264: 350-358.
    • (1999) Virology , vol.264 , pp. 350-358
    • Lee, S.K.1
  • 21
    • 0035841670 scopus 로고    scopus 로고
    • Different functional domains in the cytoplasmic tail of glycoprotein B are involved in Epstein-Barr virusinduced membrane fusion
    • Haan KM, Lee SK, Longnecker R. 2001. Different functional domains in the cytoplasmic tail of glycoprotein B are involved in Epstein-Barr virusinduced membrane fusion. Virology 290:106-114.
    • (2001) Virology , vol.290 , pp. 106-114
    • Haan, K.M.1    Lee, S.K.2    Longnecker, R.3
  • 22
    • 10644269347 scopus 로고    scopus 로고
    • Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins
    • McShane MP, Longnecker R. 2004. Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins. Proc. Natl. Acad. Sci. U. S. A. 101:17474-17479.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17474-17479
    • McShane, M.P.1    Longnecker, R.2
  • 23
    • 58149487663 scopus 로고    scopus 로고
    • Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis
    • Reimer JJ, Backovic M, Deshpande CG, Jardetzky T, Longnecker R. 2009. Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis. J. Virol. 83:734-747.
    • (2009) J. Virol. , vol.83 , pp. 734-747
    • Reimer, J.J.1    Backovic, M.2    Deshpande, C.G.3    Jardetzky, T.4    Longnecker, R.5
  • 24
    • 77954287478 scopus 로고    scopus 로고
    • Protein annotation and modeling servers at university college London
    • Buchan DW, Ward SM, Lobley AE, Nugent TC, Bryson K, Jones DT. 2010. Protein annotation and modeling servers at university college London. Nucleic Acids Res. 38 (Web Server issue):W563-W568. http://dx.doi.org/10.1093/nar/gkp871.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.WEB SERVER ISSUE
    • Buchan, D.W.1    Ward, S.M.2    Lobley, A.E.3    Nugent, T.C.4    Bryson, K.5    Jones, D.T.6
  • 25
    • 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
  • 26
    • 0002109061 scopus 로고
    • Membrane fusion induced by herpes simplex virus
    • In Bentz J (ed), CRC Press, Boca Raton, FL
    • Spear PG. 1993. Membrane fusion induced by herpes simplex virus, p 201-232. In Bentz J (ed), Viral fusion mechanisms. CRC Press, Boca Raton, FL.
    • (1993) Viral fusion mechanisms , pp. 201-232
    • Spear, P.G.1
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 5344271790 scopus 로고    scopus 로고
    • Identification of syncytial mutations in a clinical isolate of herpes simplex virus 2
    • Muggeridge MI, Grantham ML, Johnson FB. 2004. Identification of syncytial mutations in a clinical isolate of herpes simplex virus 2. Virology 328:244-253.
    • (2004) Virology , vol.328 , pp. 244-253
    • Muggeridge, M.I.1    Grantham, M.L.2    Johnson, F.B.3
  • 31
    • 0037406782 scopus 로고    scopus 로고
    • A single amino acid substitution in the cytoplasmic tail of the glycoprotein B of herpes simplex virus 1 affects both syncytium formation and binding to intracellular heparan sulfate
    • Diakidi-Kosta A, Michailidou G, Kontogounis G, Sivropoulou A, Arsenakis M. 2003. A single amino acid substitution in the cytoplasmic tail of the glycoprotein B of herpes simplex virus 1 affects both syncytium formation and binding to intracellular heparan sulfate. Virus Res. 93: 99-108.
    • (2003) Virus Res. , vol.93 , pp. 99-108
    • Diakidi-Kosta, A.1    Michailidou, G.2    Kontogounis, G.3    Sivropoulou, A.4    Arsenakis, M.5
  • 32
    • 0023705653 scopus 로고
    • Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion
    • Cai WH, Gu B, Person S. 1988. Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. J. Virol. 62:2596-2604.
    • (1988) J. Virol. , vol.62 , pp. 2596-2604
    • Cai, W.H.1    Gu, B.2    Person, S.3
  • 33
    • 0023769585 scopus 로고
    • The carboxy-terminal 41 amino acids of herpes simplex virus type 1 glycoprotein B are not essential for production of infectious virus particles
    • Huff V, Cai W, Glorioso JC, Levine M. 1988. The carboxy-terminal 41 amino acids of herpes simplex virus type 1 glycoprotein B are not essential for production of infectious virus particles. J. Virol. 62:4403-4406.
    • (1988) J. Virol. , vol.62 , pp. 4403-4406
    • Huff, V.1    Cai, W.2    Glorioso, J.C.3    Levine, M.4
  • 34
    • 0027447862 scopus 로고
    • Syncytium-inducing mutations localize to two discrete regions within the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B
    • Gage PJ, Levine M, Glorioso JC. 1993. Syncytium-inducing mutations localize to two discrete regions within the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B. J. Virol. 67:2191-2201.
    • (1993) J. Virol. , vol.67 , pp. 2191-2201
    • Gage, P.J.1    Levine, M.2    Glorioso, J.C.3
  • 35
    • 0027186566 scopus 로고
    • Two novel single amino acid syncytial mutations in the carboxy terminus of glycoprotein B of herpes simplex virus type 1 confer a unique pathogenic phenotype
    • Engel JP, Boyer EP, Goodman JL. 1993. Two novel single amino acid syncytial mutations in the carboxy terminus of glycoprotein B of herpes simplex virus type 1 confer a unique pathogenic phenotype. Virology 192: 112-120.
    • (1993) Virology , vol.192 , pp. 112-120
    • Engel, J.P.1    Boyer, E.P.2    Goodman, J.L.3
  • 36
    • 0021165912 scopus 로고
    • Nucleotide sequence of a region of the herpes simplex virus type 1 gB glycoprotein gene: Mutations affecting rate of virus entry and cell fusion
    • Bzik DJ, Fox BA, DeLuca NA, Person S. 1984. Nucleotide sequence of a region of the herpes simplex virus type 1 gB glycoprotein gene: mutations affecting rate of virus entry and cell fusion. Virology 137:185-190.
    • (1984) Virology , vol.137 , pp. 185-190
    • Bzik, D.J.1    Fox, B.A.2    DeLuca, N.A.3    Person, S.4
  • 37
    • 4544238497 scopus 로고    scopus 로고
    • Conserved cytoplasmic domain sequences mediate the ER export of VZV, HSV-1, and HCMV gB
    • Heineman TC, Connolly P, Hall SL, Assefa D. 2004. Conserved cytoplasmic domain sequences mediate the ER export of VZV, HSV-1, and HCMV gB. Virology 328:131-141.
    • (2004) Virology , vol.328 , pp. 131-141
    • Heineman, T.C.1    Connolly, P.2    Hall, S.L.3    Assefa, D.4
  • 38
    • 0028325878 scopus 로고
    • Cyclosporin A resistance of herpes simplex virus-induced "fusion from within" as a phenotypical marker of mutations in the Syn 3 locus of the glycoprotein B gene
    • Walev I, Lingen M, Lazzaro M, Weise K, Falke D. 1994. Cyclosporin A resistance of herpes simplex virus-induced "fusion from within" as a phenotypical marker of mutations in the Syn 3 locus of the glycoprotein B gene. Virus Genes 8:83-86.
    • (1994) Virus Genes , vol.8 , pp. 83-86
    • Walev, I.1    Lingen, M.2    Lazzaro, M.3    Weise, K.4    Falke, D.5
  • 39
    • 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, Grantham ML, Smith MS, Anderson ES, Cardelli JA, Muggeridge MI. 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    Grantham, M.L.2    Smith, M.S.3    Anderson, E.S.4    Cardelli, J.A.5    Muggeridge, M.I.6
  • 40
    • 37049021144 scopus 로고    scopus 로고
    • Contribution of endocytic motifs in the cytoplasmic tail of herpes simplex virus type 1 glycoprotein B to virus replication and cell-cell fusion
    • Beitia Ortiz de Zarate I, Cantero-Aguilar L, Longo M, Berlioz-Torrent C, Rozenberg F. 2007. Contribution of endocytic motifs in the cytoplasmic tail of herpes simplex virus type 1 glycoprotein B to virus replication and cell-cell fusion. J. Virol. 81:13889-13903.
    • (2007) J. Virol. , vol.81 , pp. 13889-13903
    • Beitia Ortiz de Zarate, I.1    Cantero-Aguilar, L.2    Longo, M.3    Berlioz-Torrent, C.4    Rozenberg, F.5
  • 41
    • 0345742558 scopus 로고    scopus 로고
    • Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity
    • Beitia Ortiz de Zarate I, Kaelin K, Rozenberg F. 2004. Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity. J. Virol. 78: 1540-1551.
    • (2004) J. Virol. , vol.78 , pp. 1540-1551
    • Beitia Ortiz de Zarate, I.1    Kaelin, K.2    Rozenberg, F.3
  • 42
    • 0033928392 scopus 로고    scopus 로고
    • Pseudorabies virus glycoprotein M inhibits membrane fusion
    • Klupp BG, Nixdorf R, Mettenleiter TC. 2000. Pseudorabies virus glycoprotein M inhibits membrane fusion. J. Virol. 74:6760-6768.
    • (2000) J. Virol. , vol.74 , pp. 6760-6768
    • Klupp, B.G.1    Nixdorf, R.2    Mettenleiter, T.C.3
  • 43
    • 0029041584 scopus 로고
    • Mutated forms of human cytomegalovirus glycoprotein B are impaired in inducing syncytium formation
    • Tugizov S, Wang Y, Qadri I, Navarro D, Maidji E, Pereira L. 1995. Mutated forms of human cytomegalovirus glycoprotein B are impaired in inducing syncytium formation. Virology 209:580-591.
    • (1995) Virology , vol.209 , pp. 580-591
    • Tugizov, S.1    Wang, Y.2    Qadri, I.3    Navarro, D.4    Maidji, E.5    Pereira, L.6
  • 44
    • 0029817743 scopus 로고    scopus 로고
    • Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion
    • Bold S, Ohlin M, Garten W, Radsak K. 1996. Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion. J. Gen. Virol. 77:2297-2302.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2297-2302
    • Bold, S.1    Ohlin, M.2    Garten, W.3    Radsak, K.4
  • 45
    • 0036226223 scopus 로고    scopus 로고
    • Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell fusion
    • Pertel PE. 2002. Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell fusion. J. Virol. 76:4390-4400.
    • (2002) J. Virol. , vol.76 , pp. 4390-4400
    • Pertel, P.E.1
  • 46
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh M, McMahon HT. 1999. The structural era of endocytosis. Science 285:215-220.
    • (1999) Science , vol.285 , pp. 215-220
    • Marsh, M.1    McMahon, H.T.2
  • 47
    • 0033942487 scopus 로고    scopus 로고
    • Effects of truncation of the carboxy terminus of pseudorabies virus glycoprotein B on infectivity
    • Nixdorf R, Klupp BG, Karger A, Mettenleiter TC. 2000. Effects of truncation of the carboxy terminus of pseudorabies virus glycoprotein B on infectivity. J. Virol. 74:7137-7145.
    • (2000) J. Virol. , vol.74 , pp. 7137-7145
    • Nixdorf, R.1    Klupp, B.G.2    Karger, A.3    Mettenleiter, T.C.4
  • 48
    • 84864390291 scopus 로고    scopus 로고
    • Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation
    • Silverman JL, Greene NG, King DS, Heldwein EE. 2012. Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation. J. Virol. 86:8171-8184.
    • (2012) J. Virol. , vol.86 , pp. 8171-8184
    • Silverman, J.L.1    Greene, N.G.2    King, D.S.3    Heldwein, E.E.4
  • 49
    • 0037144412 scopus 로고    scopus 로고
    • Identification of a non-canonical tyrosine-based endocytic motif in an ionotropic receptor
    • Royle SJ, Bobanovic LK, Murrell-Lagnado RD. 2002. Identification of a non-canonical tyrosine-based endocytic motif in an ionotropic receptor. J. Biol. Chem. 277:35378-35385.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35378-35385
    • Royle, S.J.1    Bobanovic, L.K.2    Murrell-Lagnado, R.D.3
  • 50
    • 23844475775 scopus 로고    scopus 로고
    • Non-canonical YXXGPhi endocytic motifs: Recognition by AP2 and preferential utilization in P2X4 receptors
    • Royle SJ, Qureshi OS, Bobanovic LK, Evans PR, Owen DJ, Murrell-Lagnado RD. 2005. Non-canonical YXXGPhi endocytic motifs: recognition by AP2 and preferential utilization in P2X4 receptors. J. Cell Sci. 118:3073-3080.
    • (2005) J. Cell Sci. , vol.118 , pp. 3073-3080
    • Royle, S.J.1    Qureshi, O.S.2    Bobanovic, L.K.3    Evans, P.R.4    Owen, D.J.5    Murrell-Lagnado, R.D.6
  • 51
    • 50349103474 scopus 로고    scopus 로고
    • Membrane binding properties of EBV gp110 C-terminal domain; evidences for structural transition in the membrane environment
    • Park SJ, Seo MD, Lee SK, Lee BJ. 2008. Membrane binding properties of EBV gp110 C-terminal domain; evidences for structural transition in the membrane environment. Virology 379:181-190.
    • (2008) Virology , vol.379 , pp. 181-190
    • Park, S.J.1    Seo, M.D.2    Lee, S.K.3    Lee, B.J.4
  • 52
    • 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
  • 53
    • 0033953651 scopus 로고    scopus 로고
    • An amino acid in the heptad repeat 1 domain is important for the haemagglutininneuraminidase-independent fusing activity of simian virus 5 fusion protein
    • Ito M, Nishio M, Komada H, Ito Y, Tsurudome M. 2000. An amino acid in the heptad repeat 1 domain is important for the haemagglutininneuraminidase-independent fusing activity of simian virus 5 fusion protein. J. Gen. Virol. 81:719-727.
    • (2000) J. Gen. Virol. , vol.81 , pp. 719-727
    • Ito, M.1    Nishio, M.2    Komada, H.3    Ito, Y.4    Tsurudome, M.5
  • 55
    • 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
  • 56
    • 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 270:17-30.
    • (2000) Virology , vol.270 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 57
    • 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
    • 2442712656 scopus 로고    scopus 로고
    • Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusion
    • Silva AL, Omerovic J, Jardetzky TS, Longnecker R. 2004. Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusion. J. Virol. 78:5946-5956.
    • (2004) J. Virol. , vol.78 , pp. 5946-5956
    • Silva, A.L.1    Omerovic, J.2    Jardetzky, T.S.3    Longnecker, R.4
  • 59
    • 25144501552 scopus 로고    scopus 로고
    • The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells
    • Omerovic J, Lev L, Longnecker R. 2005. The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells. J. Virol. 79:12408-12415.
    • (2005) J. Virol. , vol.79 , pp. 12408-12415
    • Omerovic, J.1    Lev, L.2    Longnecker, R.3
  • 60
    • 23844473554 scopus 로고    scopus 로고
    • Mutations of Epstein-Barr virus gH that are differentially able to support fusion with B cells or epithelial cells
    • Wu L, Borza CM, Hutt-Fletcher LM. 2005. Mutations of Epstein-Barr virus gH that are differentially able to support fusion with B cells or epithelial cells. J. Virol. 79:10923-10930.
    • (2005) J. Virol. , vol.79 , pp. 10923-10930
    • Wu, L.1    Borza, C.M.2    Hutt-Fletcher, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.