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Volumn 10, Issue 12, 2014, Pages

Rubella Virus: First Calcium-Requiring Viral Fusion Protein

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CELL SURFACE RECEPTOR; LIPOSOME; TRYPSIN; VIRUS FUSION PROTEIN; VIRUS RNA; CALCIUM; MEMBRANE FUSION PROTEIN; VIRUS PROTEIN;

EID: 84919622976     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004530     Document Type: Article
Times cited : (50)

References (61)
  • 1
    • 0028028506 scopus 로고
    • Molecular biology of rubella virus
    • Frey TK, (1994) Molecular biology of rubella virus. Adv Virus Res 44: 69–160.
    • (1994) Adv Virus Res , vol.44 , pp. 69-160
    • Frey, T.K.1
  • 2
    • 42449163256 scopus 로고    scopus 로고
    • Rubella Virus
    • Hobman T, Chantler J (2007) Rubella Virus. In: Knipe DM, Howley PM, editors. Fields Virology. 5th ed. Philadelphia, PA: Lippincott Williams and Wilkins. 1069–1100.
    • (2007) , pp. 1069-1100
    • Hobman, T.1    Chantler, J.2    Knipe, D.M.3    Howley, P.M.4
  • 3
    • 0022032389 scopus 로고
    • The history and medical consequences of rubella
    • Cooper LZ, (1985) The history and medical consequences of rubella. Rev Infect Dis 7 Suppl 1: S2–10.
    • (1985) Rev Infect Dis , vol.7 , pp. 2-10
    • Cooper, L.Z.1
  • 5
    • 84919610519 scopus 로고    scopus 로고
    • Measles and Rubella Initiative Annual Report
    • Measles and Rubella Initiative Annual Report. WHO Annual Report
    • WHO Annual Report
  • 9
    • 0026357241 scopus 로고
    • Oligomerization of the structural proteins of rubella virus
    • Baron MD, Forsell K, (1991) Oligomerization of the structural proteins of rubella virus. Virology 185: 811–819.
    • (1991) Virology , vol.185 , pp. 811-819
    • Baron, M.D.1    Forsell, K.2
  • 10
    • 0030866797 scopus 로고    scopus 로고
    • Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein
    • Hobman TC, Lemon HF, Jewell K, (1997) Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein. J Virol 71: 7670–7680.
    • (1997) J Virol , vol.71 , pp. 7670-7680
    • Hobman, T.C.1    Lemon, H.F.2    Jewell, K.3
  • 11
    • 0026775265 scopus 로고
    • The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment
    • Hobman TC, Woodward L, Farquhar MG, (1992) The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment. J Cell Biol 118: 795–811.
    • (1992) J Cell Biol , vol.118 , pp. 795-811
    • Hobman, T.C.1    Woodward, L.2    Farquhar, M.G.3
  • 12
    • 0029064295 scopus 로고
    • Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal
    • Hobman TC, Woodward L, Farquhar MG, (1995) Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal. Mol Biol Cell 6: 7–20.
    • (1995) Mol Biol Cell , vol.6 , pp. 7-20
    • Hobman, T.C.1    Woodward, L.2    Farquhar, M.G.3
  • 13
    • 50649097269 scopus 로고    scopus 로고
    • Togaviridae: The Viruses and Their Replication
    • Kuhn RJ (2007) Togaviridae: The Viruses and Their Replication. In: Knipe DM, Howley PM, editors. Fields Virology. Fifth ed. Philadelphia, PA: Lippincott, Williams and Wilkins. 1001–1022.
    • (2007) , pp. 1001-1022
    • Kuhn, R.J.1    Knipe, D.M.2    Howley, P.M.3
  • 14
    • 0028065160 scopus 로고
    • Assembly of rubella virus structural proteins into virus-like particles in transfected cells
    • Hobman TC, Lundstrom ML, Mauracher CA, Woodward L, Gillam S, et al. (1994) Assembly of rubella virus structural proteins into virus-like particles in transfected cells. Virology 202: 574–585.
    • (1994) Virology , vol.202 , pp. 574-585
    • Hobman, T.C.1    Lundstrom, M.L.2    Mauracher, C.A.3    Woodward, L.4    Gillam, S.5
  • 15
    • 0042062406 scopus 로고    scopus 로고
    • Structural maturation of rubella virus in the Golgi complex
    • Risco C, Carrascosa JL, Frey TK, (2003) Structural maturation of rubella virus in the Golgi complex. Virology 312: 261–269.
    • (2003) Virology , vol.312 , pp. 261-269
    • Risco, C.1    Carrascosa, J.L.2    Frey, T.K.3
  • 16
    • 0028226159 scopus 로고
    • Expression and characterization of virus-like particles containing rubella virus structural proteins
    • Qiu Z, Ou D, Hobman TC, Gillam S, (1994) Expression and characterization of virus-like particles containing rubella virus structural proteins. J Virol 68: 4086–4091.
    • (1994) J Virol , vol.68 , pp. 4086-4091
    • Qiu, Z.1    Ou, D.2    Hobman, T.C.3    Gillam, S.4
  • 17
    • 0021965747 scopus 로고
    • Antibody response to individual rubella virus proteins in congenital and other rubella virus infections
    • Katow S, Sugiura A, (1985) Antibody response to individual rubella virus proteins in congenital and other rubella virus infections. J Clin Microbiol 21: 449–451.
    • (1985) J Clin Microbiol , vol.21 , pp. 449-451
    • Katow, S.1    Sugiura, A.2
  • 18
    • 0000853902 scopus 로고
    • A model of the structural organization of rubella virions
    • Waxham MN, Wolinsky JS, (1985) A model of the structural organization of rubella virions. Rev Infect Dis 7 Suppl 1: S133–139.
    • (1985) Rev Infect Dis , vol.7 , pp. 133-139
    • Waxham, M.N.1    Wolinsky, J.S.2
  • 19
    • 80055103942 scopus 로고    scopus 로고
    • Identification of the myelin oligodendrocyte glycoprotein as a cellular receptor for rubella virus
    • Cong H, Jiang Y, Tien P, (2011) Identification of the myelin oligodendrocyte glycoprotein as a cellular receptor for rubella virus. J Virol 85: 11038–11047.
    • (2011) J Virol , vol.85 , pp. 11038-11047
    • Cong, H.1    Jiang, Y.2    Tien, P.3
  • 20
    • 0033791859 scopus 로고    scopus 로고
    • Rubella virus replication and links to teratogenicity
    • Lee JY, Bowden DS, (2000) Rubella virus replication and links to teratogenicity. Clin Microbiol Rev 13: 571–587.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 571-587
    • Lee, J.Y.1    Bowden, D.S.2
  • 21
    • 10044236498 scopus 로고    scopus 로고
    • Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells
    • Kee SH, Cho EJ, Song JW, Park KS, Baek LJ, et al. (2004) Effects of endocytosis inhibitory drugs on rubella virus entry into VeroE6 cells. Microbiol Immunol 48: 823–829.
    • (2004) Microbiol Immunol , vol.48 , pp. 823-829
    • Kee, S.H.1    Cho, E.J.2    Song, J.W.3    Park, K.S.4    Baek, L.J.5
  • 22
    • 78049487538 scopus 로고    scopus 로고
    • Alphavirus entry and membrane fusion
    • Kielian M, Chanel-Vos C, Liao M, (2010) Alphavirus entry and membrane fusion. Viruses 2: 796–825.
    • (2010) Viruses , vol.2 , pp. 796-825
    • Kielian, M.1    Chanel-Vos, C.2    Liao, M.3
  • 23
    • 0030024566 scopus 로고    scopus 로고
    • Pathway of rubella virus infectious entry into Vero cells
    • Petruzziello R, Orsi N, Macchia S, Rieti S, Frey TK, et al. (1996) Pathway of rubella virus infectious entry into Vero cells. J Gen Virol 77(Pt 2): 303–308.
    • (1996) J Gen Virol , vol.77(Pt 2) , pp. 303-308
    • Petruzziello, R.1    Orsi, N.2    Macchia, S.3    Rieti, S.4    Frey, T.K.5
  • 24
    • 0023768226 scopus 로고
    • Low pH-induced conformational change of rubella virus envelope proteins
    • Katow S, Sugiura A, (1988) Low pH-induced conformational change of rubella virus envelope proteins. J Gen Virol 69(Pt 11): 2797–2807.
    • (1988) J Gen Virol , vol.69(Pt 11) , pp. 2797-2807
    • Katow, S.1    Sugiura, A.2
  • 25
    • 0033934282 scopus 로고    scopus 로고
    • Mutations in the E1 hydrophobic domain of rubella virus impair virus infectivity but not virus assembly
    • Qiu Z, Yao J, Cao H, Gillam S, (2000) Mutations in the E1 hydrophobic domain of rubella virus impair virus infectivity but not virus assembly. J Virol 74: 6637–6642.
    • (2000) J Virol , vol.74 , pp. 6637-6642
    • Qiu, Z.1    Yao, J.2    Cao, H.3    Gillam, S.4
  • 26
    • 0031657977 scopus 로고    scopus 로고
    • Effects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity
    • Yang D, Hwang D, Qiu Z, Gillam S, (1998) Effects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity. J Virol 72: 8747–8755.
    • (1998) J Virol , vol.72 , pp. 8747-8755
    • Yang, D.1    Hwang, D.2    Qiu, Z.3    Gillam, S.4
  • 27
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: more than one way to make a hairpin
    • Kielian M, Rey FA, (2006) Virus membrane fusion proteins: more than one way to make a hairpin. Nature Reviews Microbiology 4: 67–76.
    • (2006) Nature Reviews Microbiology , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 28
    • 84872973964 scopus 로고    scopus 로고
    • Functional and evolutionary insight from the crystal structure of rubella virus protein E1
    • DuBois RM, Vaney MC, Tortorici MA, Kurdi RA, Barba-Spaeth G, et al. (2013) Functional and evolutionary insight from the crystal structure of rubella virus protein E1. Nature 493: 552–556.
    • (2013) Nature , vol.493 , pp. 552-556
    • DuBois, R.M.1    Vaney, M.C.2    Tortorici, M.A.3    Kurdi, R.A.4    Barba-Spaeth, G.5
  • 29
    • 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
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • Gerasimenko JV, Tepikin AV, Petersen OH, Gerasimenko OV, (1998) Calcium uptake via endocytosis with rapid release from acidifying endosomes. Curr Biol 8: 1335–1338.
    • (1998) Curr Biol , vol.8 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 34
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao M, Kielian M, (2005) Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J Cell Biol 171: 111–120.
    • (2005) J Cell Biol , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 35
    • 0001696895 scopus 로고
    • pH-dependent fusion between the Semliki Forest virus membrane and liposomes
    • White J, Helenius A, (1980) pH-dependent fusion between the Semliki Forest virus membrane and liposomes. Proc Natl Acad Sci U S A 77: 3273–3277.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 3273-3277
    • White, J.1    Helenius, A.2
  • 36
    • 80052208901 scopus 로고    scopus 로고
    • Hepatitis C virus is primed by CD81 protein for low pH-dependent fusion
    • Sharma NR, Mateu G, Dreux M, Grakoui A, Cosset FL, et al. (2011) Hepatitis C virus is primed by CD81 protein for low pH-dependent fusion. J Biol Chem 286: 30361–30376.
    • (2011) J Biol Chem , vol.286 , pp. 30361-30376
    • Sharma, N.R.1    Mateu, G.2    Dreux, M.3    Grakoui, A.4    Cosset, F.L.5
  • 37
    • 70350327357 scopus 로고    scopus 로고
    • E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein
    • Liu CY, Kielian M, (2009) E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein. J Virol 83: 11298–11306.
    • (2009) J Virol , vol.83 , pp. 11298-11306
    • Liu, C.Y.1    Kielian, M.2
  • 38
    • 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
  • 39
    • 0027404892 scopus 로고
    • Calcium ions are required for cell fusion mediated by the CD4-human immunodeficiency virus type 1 envelope glycoprotein interaction
    • Dimitrov DS, Broder CC, Berger EA, Blumenthal R, (1993) Calcium ions are required for cell fusion mediated by the CD4-human immunodeficiency virus type 1 envelope glycoprotein interaction. Journal of virology 67: 1647–1652.
    • (1993) Journal of virology , vol.67 , pp. 1647-1652
    • Dimitrov, D.S.1    Broder, C.C.2    Berger, E.A.3    Blumenthal, R.4
  • 40
    • 0027479875 scopus 로고
    • Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly
    • Haynes JI, 2ndChang D, Consigli RA, (1993) Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly. J Virol 67: 2486–2495.
    • (1993) J Virol , vol.67 , pp. 2486-2495
    • Haynes, J.I.1    Chang, D.2    Consigli, R.A.3
  • 41
    • 0034715826 scopus 로고    scopus 로고
    • Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers
    • Dormitzer PR, Greenberg HB, Harrison SC, (2000) Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers. Virology 277: 420–428.
    • (2000) Virology , vol.277 , pp. 420-428
    • Dormitzer, P.R.1    Greenberg, H.B.2    Harrison, S.C.3
  • 42
    • 34848916433 scopus 로고    scopus 로고
    • Luminal chloride-dependent activation of endosome calcium channels: patch clamp study of enlarged endosomes
    • Saito M, Hanson PI, Schlesinger P, (2007) Luminal chloride-dependent activation of endosome calcium channels: patch clamp study of enlarged endosomes. J Biol Chem 282: 27327–27333.
    • (2007) J Biol Chem , vol.282 , pp. 27327-27333
    • Saito, M.1    Hanson, P.I.2    Schlesinger, P.3
  • 43
    • 0036472494 scopus 로고    scopus 로고
    • pH-dependent regulation of lysosomal calcium in macrophages
    • Christensen KA, Myers JT, Swanson JA, (2002) pH-dependent regulation of lysosomal calcium in macrophages. J Cell Sci 115: 599–607.
    • (2002) J Cell Sci , vol.115 , pp. 599-607
    • Christensen, K.A.1    Myers, J.T.2    Swanson, J.A.3
  • 44
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • Lakadamyali M, Rust MJ, Zhuang X, (2006) Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 124: 997–1009.
    • (2006) Cell , vol.124 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 45
    • 55549134611 scopus 로고    scopus 로고
    • Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium
    • Lloyd-Evans E, Morgan AJ, He X, Smith DA, Elliot-Smith E, et al. (2008) Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium. Nat Med 14: 1247–1255.
    • (2008) Nat Med , vol.14 , pp. 1247-1255
    • Lloyd-Evans, E.1    Morgan, A.J.2    He, X.3    Smith, D.A.4    Elliot-Smith, E.5
  • 46
    • 84884680449 scopus 로고    scopus 로고
    • Viral membrane fusion and nucleocapsid delivery into the cytoplasm are distinct events in some flaviviruses
    • Nour AM, Li Y, Wolenski J, Modis Y, (2013) Viral membrane fusion and nucleocapsid delivery into the cytoplasm are distinct events in some flaviviruses. PLoS pathogens 9: e1003585.
    • (2013) PLoS pathogens , vol.9 , pp. e1003585
    • Nour, A.M.1    Li, Y.2    Wolenski, J.3    Modis, Y.4
  • 47
    • 33947113954 scopus 로고    scopus 로고
    • Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family
    • Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, et al. (2007) Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family. Immunity 26: 299–310.
    • (2007) Immunity , vol.26 , pp. 299-310
    • Santiago, C.1    Ballesteros, A.2    Tami, C.3    Martinez-Munoz, L.4    Kaplan, G.G.5
  • 48
    • 0029872616 scopus 로고    scopus 로고
    • Phospholipid composition dependence of Ca2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV
    • Fukuda M, Kojima T, Mikoshiba K, (1996) Phospholipid composition dependence of Ca2+-dependent phospholipid binding to the C2A domain of synaptotagmin IV. J Biol Chem 271: 8430–8434.
    • (1996) J Biol Chem , vol.271 , pp. 8430-8434
    • Fukuda, M.1    Kojima, T.2    Mikoshiba, K.3
  • 49
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: disparate players and common principles
    • Martens S, McMahon HT, (2008) Mechanisms of membrane fusion: disparate players and common principles. Nat Rev Mol Cell Biol 9: 543–556.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 50
    • 33747453911 scopus 로고    scopus 로고
    • Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains
    • Herrick DZ, Sterbling S, Rasch KA, Hinderliter A, Cafiso DS, (2006) Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains. Biochemistry 45: 9668–9674.
    • (2006) Biochemistry , vol.45 , pp. 9668-9674
    • Herrick, D.Z.1    Sterbling, S.2    Rasch, K.A.3    Hinderliter, A.4    Cafiso, D.S.5
  • 51
    • 33748442138 scopus 로고    scopus 로고
    • Ca2+-triggered simultaneous membrane penetration of the tandem C2-domains of synaptotagmin I
    • Hui E, Bai J, Chapman ER, (2006) Ca2+-triggered simultaneous membrane penetration of the tandem C2-domains of synaptotagmin I. Biophys J 91: 1767–1777.
    • (2006) Biophys J , vol.91 , pp. 1767-1777
    • Hui, E.1    Bai, J.2    Chapman, E.R.3
  • 52
    • 77949900365 scopus 로고    scopus 로고
    • T cell/transmembrane, Ig, and mucin-3 allelic variants differentially recognize phosphatidylserine and mediate phagocytosis of apoptotic cells
    • DeKruyff RH, Bu X, Ballesteros A, Santiago C, Chim YL, et al. (2010) T cell/transmembrane, Ig, and mucin-3 allelic variants differentially recognize phosphatidylserine and mediate phagocytosis of apoptotic cells. J Immunol 184: 1918–1930.
    • (2010) J Immunol , vol.184 , pp. 1918-1930
    • DeKruyff, R.H.1    Bu, X.2    Ballesteros, A.3    Santiago, C.4    Chim, Y.L.5
  • 54
    • 0033057248 scopus 로고    scopus 로고
    • Mutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release
    • Yao J, Gillam S, (1999) Mutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release. J Virol 73: 4622–4630.
    • (1999) J Virol , vol.73 , pp. 4622-4630
    • Yao, J.1    Gillam, S.2
  • 56
    • 0031969430 scopus 로고    scopus 로고
    • fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit
    • Glomb-Reinmund S, Kielian M, (1998) fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit. J Virol 72: 4281–4287.
    • (1998) J Virol , vol.72 , pp. 4281-4287
    • Glomb-Reinmund, S.1    Kielian, M.2
  • 57
    • 0025912001 scopus 로고
    • In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000-molecular-weight membrane protein modulates virus release
    • Liljestrom P, Lusa S, Huylebroeck D, Garoff H, (1991) In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000-molecular-weight membrane protein modulates virus release. J Virol 65: 4107–4113.
    • (1991) J Virol , vol.65 , pp. 4107-4113
    • Liljestrom, P.1    Lusa, S.2    Huylebroeck, D.3    Garoff, H.4
  • 58
    • 50949095260 scopus 로고    scopus 로고
    • Differential cholesterol binding by class II fusion proteins determines membrane fusion properties
    • Umashankar M, Sanchez-San Martin C, Liao M, Reilly B, Guo A, et al. (2008) Differential cholesterol binding by class II fusion proteins determines membrane fusion properties. J Virol 82: 9245–9253.
    • (2008) J Virol , vol.82 , pp. 9245-9253
    • Umashankar, M.1    Sanchez-San Martin, C.2    Liao, M.3    Reilly, B.4    Guo, A.5
  • 59
    • 10044283361 scopus 로고    scopus 로고
    • A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion
    • Chanel-Vos C, Kielian M, (2004) A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion. J Virol 78: 13543–13552.
    • (2004) J Virol , vol.78 , pp. 13543-13552
    • Chanel-Vos, C.1    Kielian, M.2
  • 60
    • 0025165605 scopus 로고
    • Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein
    • Kielian M, Jungerwirth S, Sayad KU, DeCandido S, (1990) Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein. J Virol 64: 4614–4624.
    • (1990) J Virol , vol.64 , pp. 4614-4624
    • Kielian, M.1    Jungerwirth, S.2    Sayad, K.U.3    DeCandido, S.4
  • 61
    • 0033918941 scopus 로고    scopus 로고
    • Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion
    • Chatterjee PK, Vashishtha M, Kielian M, (2000) Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion. J Virol 74: 1623–1631.
    • (2000) J Virol , vol.74 , pp. 1623-1631
    • Chatterjee, P.K.1    Vashishtha, M.2    Kielian, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.