메뉴 건너뛰기




Volumn 11, Issue 8, 2003, Pages 374-382

Animal cell invasion by a large nonenveloped virus: Reovirus delivers the goods

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS PROTEIN; CAPSID PROTEIN; MU1 PROTEIN, REOVIRUS; RNA BINDING PROTEIN; SIGMA PROTEIN 3, REOVIRUS;

EID: 0141907317     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(03)00178-1     Document Type: Review
Times cited : (67)

References (64)
  • 1
    • 0025936096 scopus 로고
    • Mechanisms of viral pathogenesis. Distinct forms of reoviruses and their roles during replication in cells and host
    • Nibert M.L., et al. Mechanisms of viral pathogenesis. Distinct forms of reoviruses and their roles during replication in cells and host. J. Clin. Invest. 88:1991;727-734.
    • (1991) J. Clin. Invest. , vol.88 , pp. 727-734
    • Nibert, M.L.1
  • 2
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:2000;531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 3
    • 0003233562 scopus 로고    scopus 로고
    • Principles of virus structure
    • D.M. Knipe, & P.M. Howley. Lippincott Williams & Wilkins
    • Harrison S.C. Principles of virus structure. Knipe D.M., Howley P.M. Fields Virology. 2001;53-85 Lippincott Williams & Wilkins.
    • (2001) Fields Virology , pp. 53-85
    • Harrison, S.C.1
  • 4
    • 0034905041 scopus 로고    scopus 로고
    • The machinery for flavivirus fusion with host cell membranes
    • Heinz F.X., Allison S.L. The machinery for flavivirus fusion with host cell membranes. Curr. Opin. Microbiol. 4:2001;450-455.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 450-455
    • Heinz, F.X.1    Allison, S.L.2
  • 5
    • 0031606858 scopus 로고    scopus 로고
    • The structure and function of nodavirus particles: A paradigm for understanding chemical biology
    • Schneemann A., et al. The structure and function of nodavirus particles: a paradigm for understanding chemical biology. Adv. Virus Res. 50:1998;381-446.
    • (1998) Adv. Virus Res. , vol.50 , pp. 381-446
    • Schneemann, A.1
  • 6
    • 0036403802 scopus 로고    scopus 로고
    • Poliovirus cell entry: Common structural themes in viral cell entry pathways
    • Hogle J.M. Poliovirus cell entry: common structural themes in viral cell entry pathways. Annu. Rev. Microbiol. 56:2002;677-702.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 677-702
    • Hogle, J.M.1
  • 7
    • 0001123624 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • D.M. Knipe, & P.M. Howley. Lippincott Williams & Wilkins
    • Nibert M.L., Schiff L.A. Reoviruses and their replication. Knipe D.M., Howley P.M. Fields Virology. 2001;1679-1728 Lippincott Williams & Wilkins.
    • (2001) Fields Virology , pp. 1679-1728
    • Nibert, M.L.1    Schiff, L.A.2
  • 8
    • 0001581287 scopus 로고    scopus 로고
    • Rotaviruses and their replication
    • D.M. Knipe, & P.M. Howley. Lippincott Williams & Wilkins
    • Estes M.K. Rotaviruses and their replication. Knipe D.M., Howley P.M. Fields Virology. 2001;1679-1728 Lippincott Williams & Wilkins.
    • (2001) Fields Virology , pp. 1679-1728
    • Estes, M.K.1
  • 9
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • Reinisch K.M., et al. Structure of the reovirus core at 3.6 Å resolution. Nature. 404:2000;960-967.
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1
  • 10
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein λ2
    • Luongo C.L., et al. Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein λ2. J. Biol. Chem. 275:2000;2804-2810.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2804-2810
    • Luongo, C.L.1
  • 11
    • 0035036348 scopus 로고    scopus 로고
    • Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein
    • Chandran K., et al. Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. J. Virol. 75:2001;5335-5342.
    • (2001) J. Virol. , vol.75 , pp. 5335-5342
    • Chandran, K.1
  • 12
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber
    • Chappell J.D., et al. Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber. EMBO J. 21:2002;1-11.
    • (2002) EMBO J. , vol.21 , pp. 1-11
    • Chappell, J.D.1
  • 13
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, μ1, in a complex with is protector protein, σ3
    • Liemann S., et al. Structure of the reovirus membrane-penetration protein, μ1, in a complex with is protector protein, σ3. Cell. 108:2002;283-295.
    • (2002) Cell , vol.108 , pp. 283-295
    • Liemann, S.1
  • 14
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden K.A., et al. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122:1993;1023-1041.
    • (1993) J. Cell Biol. , vol.122 , pp. 1023-1041
    • Dryden, K.A.1
  • 15
    • 0345196599 scopus 로고    scopus 로고
    • Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: An approach for analyzing σ3 functions during virus entry
    • Jane-Valbuena J., et al. Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: an approach for analyzing σ3 functions during virus entry. J. Virol. 73:1999;2963-2973.
    • (1999) J. Virol. , vol.73 , pp. 2963-2973
    • Jane-Valbuena, J.1
  • 16
    • 0032899595 scopus 로고    scopus 로고
    • In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins μ1 and σ3
    • Chandran K., et al. In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins μ1 and σ3. J. Virol. 73:1999;3941-3950.
    • (1999) J. Virol. , vol.73 , pp. 3941-3950
    • Chandran, K.1
  • 17
    • 0036233299 scopus 로고    scopus 로고
    • Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein σ3
    • Jane-Valbuena J., et al. Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein σ3. J. Virol. 76:2002;5184-5197.
    • (2002) J. Virol. , vol.76 , pp. 5184-5197
    • Jane-Valbuena, J.1
  • 18
    • 0036149374 scopus 로고    scopus 로고
    • Thermostability of reovirus disassembly intermediates (ISVPs) correlates with genetic, biochemical, and thermodynamic properties of major surface protein μ1
    • Middleton J.K., et al. Thermostability of reovirus disassembly intermediates (ISVPs) correlates with genetic, biochemical, and thermodynamic properties of major surface protein μ1. J. Virol. 76:2002;1051-1061.
    • (2002) J. Virol. , vol.76 , pp. 1051-1061
    • Middleton, J.K.1
  • 19
    • 0036776316 scopus 로고    scopus 로고
    • A single mutation in the carboxy terminus of reovirus outer-capsid protein σ3 confers enhanced kinetics of σ3 proteolysis, resistance to inhibitors of viral disassembly, and alterations in σ3 structure
    • Wilson G.J., et al. A single mutation in the carboxy terminus of reovirus outer-capsid protein σ3 confers enhanced kinetics of σ3 proteolysis, resistance to inhibitors of viral disassembly, and alterations in σ3 structure. J. Virol. 76:2002;9832-9843.
    • (2002) J. Virol. , vol.76 , pp. 9832-9843
    • Wilson, G.J.1
  • 20
    • 0027185672 scopus 로고
    • Rescue of infectivity by in vitro transcapsidation of rotavirus single-shelled particles
    • Chen D., Ramig R.F. Rescue of infectivity by in vitro transcapsidation of rotavirus single-shelled particles. Virology. 192:1993;422-429.
    • (1993) Virology , vol.192 , pp. 422-429
    • Chen, D.1    Ramig, R.F.2
  • 21
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution
    • Olland A.M., et al. Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution. EMBO J. 20:2001;979-989.
    • (2001) EMBO J. , vol.20 , pp. 979-989
    • Olland, A.M.1
  • 22
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage - Structural studies of reovirus polymerase λ3
    • Tao Y., et al. RNA synthesis in a cage - structural studies of reovirus polymerase λ3. Cell. 111:2002;733-745.
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1
  • 23
    • 0027432147 scopus 로고
    • Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2
    • Xu P., et al. Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2. Virology. 197:1993;726-731.
    • (1993) Virology , vol.197 , pp. 726-731
    • Xu, P.1
  • 24
    • 0036889158 scopus 로고    scopus 로고
    • The hydrophilic amino-terminal arm of reovirus core shell protein λ1 is dispensable for particle assembly
    • Kim J., et al. The hydrophilic amino-terminal arm of reovirus core shell protein λ1 is dispensable for particle assembly. J. Virol. 76:2002;12211-12222.
    • (2002) J. Virol. , vol.76 , pp. 12211-12222
    • Kim, J.1
  • 25
    • 0035520610 scopus 로고    scopus 로고
    • Reoviruses and the host cell
    • Tyler K.L., et al. Reoviruses and the host cell. Trends Microbiol. 9:2001;560-564.
    • (2001) Trends Microbiol. , vol.9 , pp. 560-564
    • Tyler, K.L.1
  • 26
    • 0037341386 scopus 로고    scopus 로고
    • Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins
    • Stehle T., Dermody T.S. Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins. Rev. Med. Virol. 13:2003;123-132.
    • (2003) Rev. Med. Virol. , vol.13 , pp. 123-132
    • Stehle, T.1    Dermody, T.S.2
  • 27
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes W., et al. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell. 103:2000;679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1
  • 28
    • 0019870337 scopus 로고
    • Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses
    • White J., et al. Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses. J. Cell Biol. 89:1981;674-679.
    • (1981) J. Cell Biol. , vol.89 , pp. 674-679
    • White, J.1
  • 29
    • 0037405104 scopus 로고    scopus 로고
    • Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: Role of receptors and low pH
    • Brabec M., et al. Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: role of receptors and low pH. J. Virol. 77:2003;5370-5377.
    • (2003) J. Virol. , vol.77 , pp. 5370-5377
    • Brabec, M.1
  • 30
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker L.J., et al. Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J. Virol. 61:1987;2351-2361.
    • (1987) J. Virol. , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1
  • 31
    • 0029655850 scopus 로고    scopus 로고
    • The entry of reovirus into L cells is dependent on vacuolar proton-ATPase activity
    • Martinez C.G., et al. The entry of reovirus into L cells is dependent on vacuolar proton-ATPase activity. J. Virol. 70:1996;576-579.
    • (1996) J. Virol. , vol.70 , pp. 576-579
    • Martinez, C.G.1
  • 32
    • 0030999547 scopus 로고    scopus 로고
    • Mutations in reovirus outer-capsid protein σ3 selected during persistent infections of L cells confer resistance to protease inhibitor E64
    • Baer G.S., Dermody T.S. Mutations in reovirus outer-capsid protein σ3 selected during persistent infections of L cells confer resistance to protease inhibitor E64. J. Virol. 71:1997;4921-4928.
    • (1997) J. Virol. , vol.71 , pp. 4921-4928
    • Baer, G.S.1    Dermody, T.S.2
  • 33
    • 0032830324 scopus 로고    scopus 로고
    • Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly
    • Baer G.S., et al. Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly. J. Virol. 73:1999;9532-9543.
    • (1999) J. Virol. , vol.73 , pp. 9532-9543
    • Baer, G.S.1
  • 34
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • Ebert D.H., et al. Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J. Biol. Chem. 277:2002;24609-24617.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24609-24617
    • Ebert, D.H.1
  • 35
    • 0032567111 scopus 로고    scopus 로고
    • No role for pepstatin-A-sensitive acidic proteinases in reovirus infections of L or MDCK cells
    • Kothandaraman S., et al. No role for pepstatin-A-sensitive acidic proteinases in reovirus infections of L or MDCK cells. Virology. 251:1998;264-272.
    • (1998) Virology , vol.251 , pp. 264-272
    • Kothandaraman, S.1
  • 36
    • 0035101193 scopus 로고    scopus 로고
    • Adaptation of reovirus to growth in the presence of protease inhibitor E64 segregates with a mutation in the carboxy terminus of viral outer- capsid protein σ3
    • Ebert D.H., et al. Adaptation of reovirus to growth in the presence of protease inhibitor E64 segregates with a mutation in the carboxy terminus of viral outer- capsid protein σ3. J. Virol. 75:2001;3197-3206.
    • (2001) J. Virol. , vol.75 , pp. 3197-3206
    • Ebert, D.H.1
  • 37
    • 0036310562 scopus 로고    scopus 로고
    • Addition of exogenous protease facilitates reovirus infection in many restrictive cells
    • Golden J.W., et al. Addition of exogenous protease facilitates reovirus infection in many restrictive cells. J. Virol. 76:2002;7430-7443.
    • (2002) J. Virol. , vol.76 , pp. 7430-7443
    • Golden, J.W.1
  • 38
    • 85030968018 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and kinetics of its digestion as determined by mass spectrometry
    • in press
    • Mendez, I. et al. Structure of the reovirus outer capsid and kinetics of its digestion as determined by mass spectrometry. Virology (in press).
    • Virology
    • Mendez, I.1
  • 39
    • 0036094683 scopus 로고    scopus 로고
    • Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum
    • Lorenz I.C., et al. Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum. J. Virol. 76:2002;5480-5491.
    • (2002) J. Virol. , vol.76 , pp. 5480-5491
    • Lorenz, I.C.1
  • 40
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: A hydrophobic conformer of reovirus penetration protein μ1 mediates membrane disruption
    • Chandran K., et al. Strategy for nonenveloped virus entry: a hydrophobic conformer of reovirus penetration protein μ1 mediates membrane disruption. J. Virol. 76:2002;9920-9933.
    • (2002) J. Virol. , vol.76 , pp. 9920-9933
    • Chandran, K.1
  • 41
    • 0023055082 scopus 로고
    • PH dependent lysis of liposomes by adenovirus
    • Blumenthal R., et al. pH dependent lysis of liposomes by adenovirus. Biochemistry. 25:1986;2231-2237.
    • (1986) Biochemistry , vol.25 , pp. 2231-2237
    • Blumenthal, R.1
  • 42
    • 0026686139 scopus 로고
    • Interaction of rotavirus particles with liposomes
    • Nandi P., et al. Interaction of rotavirus particles with liposomes. J. Virol. 66:1992;3363-3367.
    • (1992) J. Virol. , vol.66 , pp. 3363-3367
    • Nandi, P.1
  • 43
    • 0019474782 scopus 로고
    • PH-dependent hemolysis by influenza, Semliki, Forest virus, and Sendai virus
    • Lenard J., Miller D.K. pH-dependent hemolysis by influenza, Semliki, Forest virus, and Sendai virus. Virology. 110:1981;479-482.
    • (1981) Virology , vol.110 , pp. 479-482
    • Lenard, J.1    Miller, D.K.2
  • 44
    • 0018688771 scopus 로고
    • Two modes of entry of reovirus particles into L cells
    • Borsa J., et al. Two modes of entry of reovirus particles into L cells. J. Gen. Virol. 45:1979;161-170.
    • (1979) J. Gen. Virol. , vol.45 , pp. 161-170
    • Borsa, J.1
  • 45
    • 0027296972 scopus 로고
    • Reovirus M2 gene is associated with chromium release from mouse L cells
    • Lucia-Jandris P., et al. Reovirus M2 gene is associated with chromium release from mouse L cells. J. Virol. 67:1993;5339-5345.
    • (1993) J. Virol. , vol.67 , pp. 5339-5345
    • Lucia-Jandris, P.1
  • 46
    • 0031060329 scopus 로고    scopus 로고
    • Characterization of the ion channels formed by poliovirus in planar lipid membranes
    • Tosteson M.T., Chow M. Characterization of the ion channels formed by poliovirus in planar lipid membranes. J. Virol. 71:1997;507-511.
    • (1997) J. Virol. , vol.71 , pp. 507-511
    • Tosteson, M.T.1    Chow, M.2
  • 47
    • 0031964230 scopus 로고    scopus 로고
    • Protease cleavage of reovirus capsid protein μ1/μ1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle
    • Chandran K., Nibert M.L. Protease cleavage of reovirus capsid protein μ1/μ1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle. J. Virol. 72:1998;467-475.
    • (1998) J. Virol. , vol.72 , pp. 467-475
    • Chandran, K.1    Nibert, M.L.2
  • 48
    • 0029656249 scopus 로고    scopus 로고
    • Role of the μ1 protein in reovirus stability and capacity to cause chromium release from host cells
    • Hooper J.W., Fields B.N. Role of the μ1 protein in reovirus stability and capacity to cause chromium release from host cells. J. Virol. 70:1996;459-467.
    • (1996) J. Virol. , vol.70 , pp. 459-467
    • Hooper, J.W.1    Fields, B.N.2
  • 49
    • 0026088718 scopus 로고
    • Mammalian reoviruses contain a myristoylated structural protein
    • Nibert M.L., et al. Mammalian reoviruses contain a myristoylated structural protein. J. Virol. 65:1991;1960-1967.
    • (1991) J. Virol. , vol.65 , pp. 1960-1967
    • Nibert, M.L.1
  • 50
    • 0015398520 scopus 로고
    • Studies on the effect of chymotrypsin on reovirions
    • Joklik W.K. Studies on the effect of chymotrypsin on reovirions. Virology. 49:1972;700-715.
    • (1972) Virology , vol.49 , pp. 700-715
    • Joklik, W.K.1
  • 51
    • 0015416711 scopus 로고
    • Transcription by infectious subviral particles of reovirus
    • Shatkin A.J., LaFiandra A.J. Transcription by infectious subviral particles of reovirus. J. Virol. 10:1972;698-706.
    • (1972) J. Virol. , vol.10 , pp. 698-706
    • Shatkin, A.J.1    LaFiandra, A.J.2
  • 52
    • 0033942486 scopus 로고    scopus 로고
    • The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol
    • Nakano M., et al. The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol. J. Virol. 74:2000;7085-7095.
    • (2000) J. Virol. , vol.74 , pp. 7085-7095
    • Nakano, M.1
  • 53
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr C.M., et al. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. U. S. A. 94:1997;14306-14313.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14306-14313
    • Carr, C.M.1
  • 54
    • 0035039737 scopus 로고    scopus 로고
    • Kinetic analysis of the effect of poliovirus receptor on viral uncoating: The receptor as a catalyst
    • Tsang S.K., et al. Kinetic analysis of the effect of poliovirus receptor on viral uncoating: the receptor as a catalyst. J. Virol. 75:2001;4984-4989.
    • (2001) J. Virol. , vol.75 , pp. 4984-4989
    • Tsang, S.K.1
  • 55
    • 0016311364 scopus 로고
    • Reovirus transcriptase activation in vitro: Involvement of an endogenous uncoating activity in the second stage of the process
    • Borsa J., et al. Reovirus transcriptase activation in vitro: involvement of an endogenous uncoating activity in the second stage of the process. Intervirology. 4:1974;171-188.
    • (1974) Intervirology , vol.4 , pp. 171-188
    • Borsa, J.1
  • 56
    • 0036891887 scopus 로고    scopus 로고
    • Requirement for vacuolar H+ -ATPase activity and Ca2+ gradient during entry of rotavirus into MA104 cells
    • Chemello M.E., et al. Requirement for vacuolar H+ -ATPase activity and Ca2+ gradient during entry of rotavirus into MA104 cells. J. Virol. 76:2002;13083-13087.
    • (2002) J. Virol. , vol.76 , pp. 13083-13087
    • Chemello, M.E.1
  • 57
    • 0036139959 scopus 로고    scopus 로고
    • Ionic strength- and temperature-induced K(Ca) shifts in the uncoating reaction of rotavirus strains RF and SA11: Correlation with membrane permeabilization
    • Martin S., et al. Ionic strength- and temperature-induced K(Ca) shifts in the uncoating reaction of rotavirus strains RF and SA11: correlation with membrane permeabilization. J. Virol. 76:2002;552-559.
    • (2002) J. Virol. , vol.76 , pp. 552-559
    • Martin, S.1
  • 58
    • 0027463283 scopus 로고
    • Isolation and genetic characterization of ethanol-resistant reovirus mutants
    • Wessner D.R., Fields B.N. Isolation and genetic characterization of ethanol-resistant reovirus mutants. J. Virol. 67:1993;2442-2447.
    • (1993) J. Virol. , vol.67 , pp. 2442-2447
    • Wessner, D.R.1    Fields, B.N.2
  • 59
    • 0028899793 scopus 로고
    • The reovirus mutant tsA279 has temperature-sensitive lesions in the M2 and L2 genes: The M2 gene is associated with decreased viral protein production and blockade in transmembrane transport
    • Hazelton P.R., Coombs K.M. The reovirus mutant tsA279 has temperature-sensitive lesions in the M2 and L2 genes: the M2 gene is associated with decreased viral protein production and blockade in transmembrane transport. Virology. 207:1995;46-58.
    • (1995) Virology , vol.207 , pp. 46-58
    • Hazelton, P.R.1    Coombs, K.M.2
  • 60
    • 0029916264 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: Prototypes of pore-forming bacterial cytolysins
    • Bhakdi S., et al. Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch. Microbiol. 165:1996;73-79.
    • (1996) Arch. Microbiol. , vol.165 , pp. 73-79
    • Bhakdi, S.1
  • 61
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta. 1462:1999;55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 62
    • 0031894126 scopus 로고    scopus 로고
    • The TolQRA proteins are required for membrane insertion of the major capsid protein of the filamentous phage f1 during infection
    • Click E.M., Webster R.E. The TolQRA proteins are required for membrane insertion of the major capsid protein of the filamentous phage f1 during infection. J. Bacteriol. 180:1998;1723-1728.
    • (1998) J. Bacteriol. , vol.180 , pp. 1723-1728
    • Click, E.M.1    Webster, R.E.2
  • 63
    • 0035830509 scopus 로고    scopus 로고
    • Junction adhesion molecule is a receptor for reovirus
    • Barton E.S., et al. Junction adhesion molecule is a receptor for reovirus. Cell. 104:2001;441-451.
    • (2001) Cell , vol.104 , pp. 441-451
    • Barton, E.S.1
  • 64
    • 0019403390 scopus 로고
    • Reovirus: Evidence for a second step in the intracellular uncoating and transcriptase activation process
    • Borsa J., et al. Reovirus: evidence for a second step in the intracellular uncoating and transcriptase activation process. Virology. 111:1981;191-200.
    • (1981) Virology , vol.111 , pp. 191-200
    • Borsa, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.