메뉴 건너뛰기




Volumn 343, Issue 1, 2010, Pages 91-119

From touchdown to transcription: The reovirus cell entry pathway

Author keywords

[No Author keywords available]

Indexed keywords

ATTACHMENT PROTEIN SIGMA1; BETA1 INTEGRIN; CAPSID PROTEIN; CATHEPSIN; CLATHRIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; JUNCTIONAL ADHESION MOLECULE A; OUTER CAPSID PROTEIN MU1; OUTER CAPSID PROTEIN SIGMA3; SIALIC ACID; UNCLASSIFIED DRUG; VIRUS PROTEIN; CELL ADHESION MOLECULE; IMMUNOGLOBULIN; JUNCTIONAL ADHESION MOLECULE A , HUMAN; JUNCTIONAL ADHESION MOLECULE-A , HUMAN;

EID: 78649401990     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/82-2010-32     Document Type: Article
Times cited : (73)

References (155)
  • 2
    • 48749094796 scopus 로고    scopus 로고
    • A positive-feedback mechanism promotes reovirus particle conversion to the intermediate associated with membrane penetration
    • Agosto MA, Myers KS, Ivanovic T, Nibert ML (2008) A positive-feedback mechanism promotes reovirus particle conversion to the intermediate associated with membrane penetration. Proc Natl Acad Sci USA 105:10571-10576
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10571-10576
    • Agosto, M.A.1    Myers, K.S.2    Ivanovic, T.3    Nibert, M.L.4
  • 3
    • 0028061661 scopus 로고
    • Proteolytic processing of reovirus is required for adherence to intestinal M cells
    • Amerongen HM, Wilson GAR, Fields BN, Neutra MR (1994) Proteolytic processing of reovirus is required for adherence to intestinal M cells. J Virol 68:8428-8432 (Pubitemid 24362742)
    • (1994) Journal of Virology , vol.68 , Issue.12 , pp. 8428-8432
    • Amerongen, H.M.1    Wilson, G.A.R.2    Fields, B.N.3    Neutra, M.R.4
  • 5
    • 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 GS, Dermody TS (1997) Mutations in reovirus outer-capsid protein s3 selected during persistent infections of L cells confer resistance to protease inhibitor E64. J Virol 71:4921-4928 (Pubitemid 27258159)
    • (1997) Journal of Virology , vol.71 , Issue.7 , pp. 4921-4928
    • Baer, G.S.1    Dermody, T.S.2
  • 6
    • 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 GS, Ebert DH, Chung CJ, Erickson AH, Dermody TS (1999) Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly. J Virol 73:9532-9543 (Pubitemid 29487109)
    • (1999) Journal of Virology , vol.73 , Issue.11 , pp. 9532-9543
    • Baer, G.S.1    Ebert, D.H.2    Chung, C.J.3    Erickson, A.H.4    Dermody, T.S.5
  • 8
    • 0035910468 scopus 로고    scopus 로고
    • Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening
    • DOI 10.1074/jbc.M004680200
    • Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS (2001a) Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200-2211 (Pubitemid 32109703)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 2200-2211
    • Barton, E.S.1    Connolly, J.L.2    Forrest, J.C.3    Chappell, J.D.4    Dermody, T.S.5
  • 11
    • 0025249289 scopus 로고
    • Intraluminal proteolytic activation plays an important role in replication of type 1 retrovirus in the intestines of neonatal mice
    • Bass DM, Bodkin D, Dambrauskas R, Trier JS, Fields BN, Wolf JL (1990) Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice. J Virol 64:1830-1833 (Pubitemid 20104925)
    • (1990) Journal of Virology , vol.64 , Issue.4 , pp. 1830-1833
    • Bass, D.M.1    Bodkin, D.2    Dambrauskas, R.3    Trier, J.S.4    Fields, B.N.5    Wolf, J.L.6
  • 12
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • DOI 10.1146/annurev.immunol.17.1.657
    • Berger EA, Murphy PM, Farber JM (1999) Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease. Annu Rev lmmunol 17:657-700 (Pubitemid 29241137)
    • (1999) Annual Review of Immunology , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 13
    • 0024418092 scopus 로고
    • Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice
    • Bodkin DK, Nibert ML, Fields BN (1989) Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice. J Virol 63:4676-4681 (Pubitemid 19257843)
    • (1989) Journal of Virology , vol.63 , Issue.11 , pp. 4676-4681
    • Bodkin, D.K.1    Nibert, M.L.2    Fields, B.N.3
  • 14
    • 0018688771 scopus 로고
    • Two modes of entry of reovirus particles into L cells
    • Borsa J, Morash BD, Sargent MD, Copps TP, Lievaart PA, Szekely JG (1979) Two modes of entry of reovirus particles into L cells. J Gen Virol 45:161-170 (Pubitemid 10233424)
    • (1979) Journal of General Virology , vol.45 , Issue.1 , pp. 161-170
    • Borsa, J.1    Morash, B.D.2    Sargent, M.D.3
  • 15
    • 0019403390 scopus 로고
    • Reovirus: Evidence for a second step in the intracellular uncoating and transcriptase activation process
    • DOI 10.1016/0042-6822(81)90664-4
    • Borsa J, Sargent MD, Lievaart PA, Copps TP (1981) Reovirus: Evidence for a second step in the intracellular uncoating and transcriptase activation process. Virology 111:191-200 (Pubitemid 11047689)
    • (1981) Virology , vol.111 , Issue.1 , pp. 191-200
    • Borsa, J.1    Sargent, M.D.2    Lievaart, P.A.3    Copps, T.P.4
  • 16
    • 0035450448 scopus 로고    scopus 로고
    • Mammalian reovirus L2 gene and λ2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing
    • DOI 10.1006/viro.2001.1052
    • Breun LA, Broering TJ, McCutcheon AM, Harrison SJ, Luongo CL, Nibert ML (2001) Mammalian reovirus L2 gene and l2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing. Virology 287:333-348 (Pubitemid 32804019)
    • (2001) Virology , vol.287 , Issue.2 , pp. 333-348
    • Breun, L.A.1    Broering, T.J.2    McCutcheon, A.M.3    Harrison, S.J.4    Luongo, C.L.5    Nibert, M.L.6
  • 18
    • 2942666429 scopus 로고    scopus 로고
    • A molecular dynamics study of reovirus attachment protein σ1 reveals conformational changes in σ1 structure
    • DOI 10.1529/biophysj.103.030825
    • Cavalli A, Prota AE, Stehle T, Dermody TS, Recanatini M, Folkers G, Scapozza L (2004) A molecular dynamics study of reovirus attachment protein s1 reveals conformational changes in s1 structure. Biophys J 86:3423-3431 (Pubitemid 38780227)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3423-3431
    • Cavalli, A.1    Prota, A.E.2    Stehle, T.3    Dermody, T.S.4    Recanatini, M.5    Folkers, G.6    Scapozzat, L.7
  • 19
    • 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 ML (1998) Protease cleavage of reovirus capsid protein m1/m1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle. J Virol 72:467-475 (Pubitemid 28048860)
    • (1998) Journal of Virology , vol.72 , Issue.1 , pp. 467-475
    • Chandran, K.1    Nibert, M.L.2
  • 21
    • 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
    • DOI 10.1128/JVI.75.11.5335-5342.2001
    • Chandran K, Zhang X, Olson NH, Walker SB, Chappell JD, Dermody TS, Baker TS, Nibert ML (2001) Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. J Virol 75:5335-5342 (Pubitemid 32448555)
    • (2001) Journal of Virology , vol.75 , Issue.11 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.H.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 22
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: A hydrophobic conformer of the reovirus membrane penetration protein μ1 mediates membrane disruption
    • DOI 10.1128/JVI.76.19.9920-9933.2002
    • Chandran K, Farsetta DL, Nibert ML (2002) Strategy for nonenveloped virus entry: A hydrophobic conformer of the reovirus membrane penetration protein m1 mediates membrane disruption. J Virol 76:9920-9933 (Pubitemid 35006531)
    • (2002) Journal of Virology , vol.76 , Issue.19 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 23
    • 0345166984 scopus 로고    scopus 로고
    • The δ Region of Outer-Capsid Protein μ1 Undergoes Conformational Change and Release from Reovirus Particles during Cell Entry
    • DOI 10.1128/JVI.77.24.13361-13375.2003
    • Chandran K, Parker JS, Ehrlich M, Kirchhausen T, Nibert ML (2003) The delta region of outercapsid protein m1 undergoes conformational change and release from reovirus particles during cell entry. J Virol 77:13361-13375 (Pubitemid 37494330)
    • (2003) Journal of Virology , vol.77 , Issue.24 , pp. 13361-13375
    • Chandran, K.1    Parker, J.S.L.2    Ehrlich, M.3    Kirchhausen, T.4    Nibert, M.L.5
  • 24
    • 19144365133 scopus 로고    scopus 로고
    • Virology: Endosomal proteolysis of the ebola virus glycoprotein is necessary for infection
    • DOI 10.1126/science.1110656
    • Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM (2005) Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643-1645 (Pubitemid 40807517)
    • (2005) Science , vol.308 , Issue.5728 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 25
    • 0015166005 scopus 로고
    • Fate of parental reovirus in infected cell
    • Chang CT, Zweerink HJ (1971) Fate of parental reovirus in infected cell. Virology 46:544-555
    • (1971) Virology , vol.46 , pp. 544-555
    • Chang, C.T.1    Zweerink, H.J.2
  • 26
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • DOI 10.1146/annurev.physiol.59.1.63
    • Chapman HA, Riese RJ, Shi GP (1997) Emerging roles for cysteine proteases in human biology. Annu Rev Physiol 59:63-88 (Pubitemid 27142435)
    • (1997) Annual Review of Physiology , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.-P.3
  • 27
    • 0031054246 scopus 로고    scopus 로고
    • Mutations in type 3 reovirus that determine binding to sialic acid are contained in the fibrous tail domain of viral attachment protein σ1
    • Chappell JD, Gunn VL, Wetzel JD, Baer GS, Dermody TS (1997) Mutations in type 3 reovirus that determine binding to sialic acid are contained in the fibrous tail domain of viral attachment protein s1. J Virol 71:1834-1841 (Pubitemid 27078560)
    • (1997) Journal of Virology , vol.71 , Issue.3 , pp. 1834-1841
    • Chappell, J.D.1    Gunn, V.L.2    Wetzel, J.D.3    Baer, G.S.4    Dermody, T.S.5
  • 28
    • 0031714794 scopus 로고    scopus 로고
    • Cleavage susceptibility of reovirus attachment protein σ1 during proteolytic disassembly of virions is determined by a sequence polymorphism in the σ1 neck
    • Chappell JD, Barton ES, Smith TH, Baer GS, Duong DT, Nibert ML, Dermody TS (1998) Cleavage susceptibility of reovirus attachment protein s1 during proteolytic disassembly of virions is determined by a sequence polymorphism in the s1 neck. J Virol 72:8205-8213 (Pubitemid 28421817)
    • (1998) Journal of Virology , vol.72 , Issue.10 , pp. 8205-8213
    • Chappell, J.D.1    Barton, E.S.2    Smith, T.H.3    Baer, G.S.4    Duong, D.T.5    Nibert, M.L.6    Dermody, T.S.7
  • 29
    • 0033861681 scopus 로고    scopus 로고
    • Identification of carbohydrate-binding domains in the attachment proteins of type 1 and type 3 reoviruses
    • DOI 10.1128/JVI.74.18.8472-8479.2000
    • Chappell JD, Duong JL, Wright BW, Dermody TS (2000) Identification of carbohydrate-binding domains in the attachment proteins of type 1 and type 3 reoviruses. J Virol 74:8472-8479 (Pubitemid 30666697)
    • (2000) Journal of Virology , vol.74 , Issue.18 , pp. 8472-8479
    • Chappell, J.D.1    Duong, J.L.2    Wright, B.W.3    Dermody, T.S.4
  • 30
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber
    • DOI 10.1093/emboj/21.1.1
    • Chappell JD, Prota A, Dermody TS, Stehle T (2002) Crystal structure of reovirus attachment protein s1 reveals evolutionary relationship to adenovirus fiber. EMBO J 21:1-11 (Pubitemid 34087069)
    • (2002) EMBO Journal , vol.21 , Issue.1-2 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 31
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen WJ, Goldstein JL, Brown MS (1990) NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J Biol Chem 265:3116-3123
    • (1990) J Biol Chem , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 33
    • 0022478937 scopus 로고
    • Reovirus guanylyltransferase is L2 gene product lambda 2
    • Cleveland DR, Zarbl H, Millward S (1986) Reovirus guanylyltransferase is L2 gene product lambda 2. J Virol 60:307-311 (Pubitemid 16003176)
    • (1986) Journal of Virology , vol.60 , Issue.1 , pp. 307-311
    • Cleveland, D.R.1    Zarbl, H.2    Millward, S.3
  • 34
    • 0032515141 scopus 로고    scopus 로고
    • Reovirus therapy of tumors with activated Ras pathway
    • Coffey MC, Strong JE, Forsyth PA, Lee PW (1998) Reovirus therapy of tumors with activated Ras pathway. Science 282:1332-1334 (Pubitemid 28524498)
    • (1998) Science , vol.282 , Issue.5392 , pp. 1332-1334
    • Coffey, M.C.1    Strong, J.E.2    Forsyth, P.A.3    Lee, P.W.K.4
  • 35
    • 33748641937 scopus 로고    scopus 로고
    • Reovirus outer capsid protein μ1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria
    • DOI 10.1128/JVI.02601-05
    • Coffey CM, Sheh A, Kim IS, Chandran K, Nibert ML, Parker JS (2006) Reovirus outer capsid protein m1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J Virol 80:8422-8438 (Pubitemid 44384855)
    • (2006) Journal of Virology , vol.80 , Issue.17 , pp. 8422-8438
    • Coffey, C.M.1    Sheh, A.2    Kim, I.S.3    Chandran, K.4    Nibert, M.L.5    Parker, J.S.L.6
  • 36
    • 0036147875 scopus 로고    scopus 로고
    • Virion disassembly is required for apoptosis induced by reovirus
    • DOI 10.1128/JVI.76.4.1632-1641.2002
    • Connolly JL, Dermody TS (2002) Virion disassembly is required for apoptosis induced by reovirus. J Virol 76:1632-1641 (Pubitemid 34094610)
    • (2002) Journal of Virology , vol.76 , Issue.4 , pp. 1632-1641
    • Connolly, J.L.1    Dermody, T.S.2
  • 38
    • 0035043244 scopus 로고    scopus 로고
    • Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis
    • DOI 10.1128/JVI.75.9.4029-4039.2001
    • Connolly JL, Barton ES, Dermody TS (2001) Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis. J Virol 75:4029-4039 (Pubitemid 32410115)
    • (2001) Journal of Virology , vol.75 , Issue.9 , pp. 4029-4039
    • Connolly, J.L.1    Barton, E.S.2    Dermody, T.S.3
  • 39
    • 0032579850 scopus 로고    scopus 로고
    • Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles
    • DOI 10.1006/viro.1998.9061
    • Coombs KM (1998) Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles. Virology 243:218-228 (Pubitemid 28384186)
    • (1998) Virology , vol.243 , Issue.1 , pp. 218-228
    • Coombs, K.M.1
  • 40
    • 0344942597 scopus 로고    scopus 로고
    • Genome delivery and ion channel properties are altered in VP4 mutants of poliovirus
    • DOI 10.1128/JVI.77.9.5266-5274.2003
    • Danthi P, Tosteson M, Li QH, Chow M (2003) Genome delivery and ion channel properties are altered in VP4 mutants of poliovirus. J Virol 77:5266-5274 (Pubitemid 36460940)
    • (2003) Journal of Virology , vol.77 , Issue.9 , pp. 5266-5274
    • Darithi, P.1    Tosteson, M.2    Li, Q.-H.3    Chow, M.4
  • 41
    • 31144446888 scopus 로고    scopus 로고
    • JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis
    • DOI 10.1128/JVI.80.3.1261-1270.2006
    • Danthi P, Hansberger MW, Campbell JA, Forrest JC, Dermody TS (2006) JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis. J Virol 80:1261-1270 (Pubitemid 43134083)
    • (2006) Journal of Virology , vol.80 , Issue.3 , pp. 1261-1270
    • Danthi, P.1    Hansberger, M.W.2    Campbell, J.A.3    Forrest, J.C.4    Dermody, T.S.5
  • 42
    • 58149268150 scopus 로고    scopus 로고
    • Independent regulation of reovirus membrane penetration and apoptosis by the m1 f domain
    • Danthi P, Coffey CM, Parker JS, Abel TW, Dermody TS (2008a) Independent regulation of reovirus membrane penetration and apoptosis by the m1 f domain. PLoS Pathog 4:e1000248
    • (2008) PLoS Pathog , vol.4
    • Danthi, P.1    Coffey, C.M.2    Parker, J.S.3    Abel, T.W.4    Dermody, T.S.5
  • 43
    • 37349062727 scopus 로고    scopus 로고
    • Reovirus apoptosis and virulence are regulated by host cell membrane penetration efficiency
    • DOI 10.1128/JVI.01739-07
    • Danthi P, Kobayashi T, Holm GH, Hansberger MW, Abel TW, Dermody TS (2008b) Reovirus apoptosis and virulence are regulated by host cell membrane-penetration efficiency. J Virol 82:161-172 (Pubitemid 350309133)
    • (2008) Journal of Virology , vol.82 , Issue.1 , pp. 161-172
    • Danthi, P.1    Kobayashi, T.2    Holm, G.H.3    Hansberger, M.W.4    Abel, T.W.5    Dermody, T.S.6
  • 44
    • 0022456630 scopus 로고
    • The J.D. mutation in familial hypercholesterolemia: Amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors
    • Davis CG, Lehrman MA, Russell DW, Anderson RG, Brown MS, Goldstein JL (1986) The J.D. mutation in familial hypercholesterolemia: Amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors. Cell 45:15-24 (Pubitemid 16046624)
    • (1986) Cell , vol.45 , Issue.1 , pp. 15-24
    • Davis, C.G.1    Lehrman, M.A.2    Russell, D.W.3
  • 45
    • 0025049962 scopus 로고
    • A σ1 region important for hemagglutination by serotype 3 reovirus strains
    • Dermody TS, Nibert ML, Bassel-Duby R, Fields BN (1990) A sigma 1 region important for hemagglutination by serotype 3 reovirus strains. J Virol 64:5173-5176 (Pubitemid 20329843)
    • (1990) Journal of Virology , vol.64 , Issue.10 , pp. 5173-5176
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 46
    • 0027523233 scopus 로고
    • Cells and viruses with mutations affecting viral entry are selected during persistent infections of L cells with mammalian reoviruses
    • Dermody TS, Nibert ML, Wetzel JD, Tong X, Fields BN (1993) Cells and viruses with mutations affecting viral entry are selected during persistent infections of L cells with mammalian reoviruses. J Virol 67:2055-2063 (Pubitemid 23088379)
    • (1993) Journal of Virology , vol.67 , Issue.4 , pp. 2055-2063
    • Dermody, T.S.1    Nibert, M.L.2    Wetzel, J.D.3    Tong, X.4    Fields, B.N.5
  • 48
    • 0020079241 scopus 로고
    • Activation and characterization of the reovirus transcriptase: Genetic analysis
    • Drayna D, Fields BN (1982) Activation and characterization of the reovirus transcriptase: Genetic analysis. J Virol 41:110-118 (Pubitemid 12197303)
    • (1982) Journal of Virology , vol.41 , Issue.1 , pp. 110-118
    • Drayna, D.1    Fields, B.N.2
  • 49
    • 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 KA, Wang G, Yeager M, Nibert ML, Coombs KM, Furlong DB, Fields BN, Baker TS (1993) 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 122:1023-1041 (Pubitemid 23254171)
    • (1993) Journal of Cell Biology , vol.122 , Issue.5 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 50
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • DOI 10.1006/viro.1998.9146
    • Dryden KA, Farsetta DL, Wang G, Keegan JM, Fields BN, Baker TS, Nibert ML (1998) Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology 245:33-46 (Pubitemid 28384075)
    • (1998) Virology , vol.245 , Issue.1 , pp. 33-46
    • Dryden, K.A.1    Farsetta, D.L.2    Wang, G.3    Keegan, J.M.4    Fields, B.N.5    Baker, T.S.6    Nibert, M.L.7
  • 51
    • 0018083242 scopus 로고
    • Differential sensitivity of normal and transformed human cells to reovirus infection
    • Duncan MR, Stanish SM, Cox DC (1978) Differential sensitivity of normal and transformed human cells to reovirus infection. J Virol 28:444-449 (Pubitemid 9041701)
    • (1978) Journal of Virology , vol.28 , Issue.2 , pp. 444-449
    • Duncan, M.R.1    Stanish, S.M.2    Cox, D.C.3
  • 52
    • 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
    • DOI 10.1128/JVI.75.7.3197-3206.2001
    • Ebert DH, Wetzel JD, Brumbaugh DE, Chance SR, Stobie LE, Baer GS, Dermody TS (2001) 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 s3. J Virol 75:3197-3206 (Pubitemid 32225883)
    • (2001) Journal of Virology , vol.75 , Issue.7 , pp. 3197-3206
    • Ebert, D.H.1    Wetzel, J.D.2    Brumbaugh, D.E.3    Chance, S.R.4    Stobie, L.E.5    Baer, G.S.6    Dermody, T.S.7
  • 53
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • DOI 10.1074/jbc.M201107200
    • Ebert DH, Deussing J, Peters C, Dermody TS (2002) Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J Biol Chem 277:24609-24617 (Pubitemid 34951989)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 54
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random initiation and stabilization of clathrin-coated pits
    • DOI 10.1016/j.cell.2004.08.017, PII S0092867404007901
    • Ehrlich M, Boll W, Van Oijen A, Hariharan R, Chandran K, Nibert ML, Kirchhausen T (2004) Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell 118:591-605 (Pubitemid 39179712)
    • (2004) Cell , vol.118 , Issue.5 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3    Hariharan, R.4    Chandran, K.5    Nibert, M.L.6    Kirchhausen, T.7
  • 55
    • 0025320720 scopus 로고
    • Active site localization in a viral mRNA capping enzyme
    • Fausnaugh J, Shatkin AJ (1990) Active site localization in a viral mRNA capping enzyme. J Biol Chem 265:7669-7672
    • (1990) J Biol Chem , vol.265 , pp. 7669-7672
    • Fausnaugh, J.1    Shatkin, A.J.2
  • 56
    • 3242794249 scopus 로고    scopus 로고
    • Peyer's patch dendritic cells process viral antigen from apoptotic epithelial cells in the intestine of reovirus-infected mice
    • DOI 10.1084/jem.20041132
    • Fleeton M, Contractor N, Leon F, Wetzel JD, Dermody TS, Kelsall B (2004) Peyer's patch dendritic cells process viral antigen from apoptotic epithelial cells in the intestine of reovirus- infected mice. J Exp Med 200:235-245 (Pubitemid 38982182)
    • (2004) Journal of Experimental Medicine , vol.200 , Issue.2 , pp. 235-245
    • Fleeton, M.N.1    Contractor, N.2    Leon, F.3    Denise Wetzel, J.4    Dermody, T.S.5    Kelsall, B.L.6
  • 57
    • 0346220255 scopus 로고    scopus 로고
    • Structure-function analysis of reovirus binding to junctional adhesion molecule 1. Implications for the mechanism of reovirus attachment
    • DOI 10.1074/jbc.M305649200
    • Forrest JC, Campbell JA, Schelling P, Stehle T, Dermody TS (2003) Structure-function analysis of reovirus binding to junctional adhesion molecule 1. Implications for the mechanism of reovirus attachment. J Biol Chem 278:48434-48444 (Pubitemid 37523299)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 48434-48444
    • Forrest, J.C.1    Campbell, J.A.2    Schelling, P.3    Stehle, T.4    Dermody, T.S.5
  • 58
    • 0025372616 scopus 로고
    • Molecular structure of the cell-attachment protein of reovirus: Correlation of computer-processed electron micrographs with sequence-based predictions
    • Fraser RDB, Furlong DB, Trus BL, Nibert ML, Fields BN, Steven AC (1990) Molecular structure of the cell-attachment protein of reovirus: Correlation of computer-processed electron micrographs with sequence-based predictions. J Virol 64:2990-3000 (Pubitemid 20171291)
    • (1990) Journal of Virology , vol.64 , Issue.6 , pp. 2990-3000
    • Fraser, R.D.B.1    Furlong, D.B.2    Trus, B.L.3    Nibert, M.L.4    Fields, B.N.5    Steven, A.C.6
  • 59
    • 0023945392 scopus 로고
    • Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles
    • Furlong DB, Nibert ML, Fields BN (1988) Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles. J Virol 62:246-256 (Pubitemid 18050814)
    • (1988) Journal of Virology , vol.62 , Issue.1 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 60
    • 0017141875 scopus 로고
    • Mechanism of formation of reovirus mRNA 50-terminal blocked and methylated sequence M7 GpppGm pC
    • Furuichi Y, Muthukrishnan S, Tomasz J, Shatkin AJ (1976) Mechanism of formation of reovirus mRNA 50-terminal blocked and methylated sequence M7 GpppGm pC. J Biol Chem 251:5043-5053
    • (1976) J Biol Chem , vol.251 , pp. 5043-5053
    • Furuichi, Y.1    Muthukrishnan, S.2    Tomasz, J.3    Shatkin, A.J.4
  • 61
    • 0022341988 scopus 로고
    • Effect of neuraminidase treatment of cells and effect of soluble glycoproteins on type 3 reovirus attachment to murine L cells
    • Gentsch JR, Pacitti AF (1985) Effect of neuraminidase treatment of cells and effect of soluble glycoproteins on type 3 reovirus attachment to murine L cells. J Virol 56:356-364 (Pubitemid 16192319)
    • (1985) Journal of Virology , vol.56 , Issue.2 , pp. 356-364
    • Gentsch, J.R.1    Pacitti, A.F.2
  • 62
    • 0023442473 scopus 로고
    • Differential interaction of reovirus type 3 with sialylated receptor components on animal cells
    • Gentsch JR, Pacitti AF (1987) Differential interaction of reovirus type 3 with sialylated receptor components on animal cells. Virology 161:245-248
    • (1987) Virology , vol.161 , pp. 245-248
    • Gentsch, J.R.1    Pacitti, A.F.2
  • 63
    • 0015151975 scopus 로고
    • Viral RNA polymerases: Electron microscopy of reovirus reaction cores
    • Gillies S, Bullivant S, Bellamy AR (1971) Viral RNA polymerases: Electron microscopy of reovirus reaction cores. Science 174:694-696
    • (1971) Science , vol.174 , pp. 694-696
    • Gillies, S.1    Bullivant, S.2    Bellamy, A.R.3
  • 70
    • 0003233562 scopus 로고    scopus 로고
    • Principles of virus structure
    • Knipe DM, Howley PM (eds), 4th edn. Lippincott-Raven, Philadelphia
    • Harrison S (2001) Principles of virus structure. In: Knipe DM, Howley PM (eds) Fields virology, 4th edn. Lippincott-Raven, Philadelphia, pp 53-85
    • (2001) Fields Virology , pp. 53-85
    • Harrison, S.1
  • 71
    • 0038082242 scopus 로고    scopus 로고
    • The viral σ1 protein and glycoconjugates containing α2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces
    • DOI 10.1128/JVI.77.14.7964-7977.2003
    • Helander A, Silvey KJ, Mantis NJ, Hutchings AB, Chandran K, Lucas WT, Nibert ML, Neutra MR (2003) The viral s1 protein and glycoconjugates containing a2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces. J Virol 77:7964-7977 (Pubitemid 36792793)
    • (2003) Journal of Virology , vol.77 , Issue.14 , pp. 7964-7977
    • Helander, A.1    Silvey, K.J.2    Mantis, N.J.3    Hutchings, A.B.4    Chandran, K.5    Lucas, W.T.6    Nibert, M.L.7    Neutra, M.R.8
  • 73
    • 34547578038 scopus 로고    scopus 로고
    • Retinoic acid-inducible gene-I and interferon-β promoter stimulator-1 augment proapoptotic responses following mammalian reovirus infection via interferon regulatory factor-3
    • DOI 10.1074/jbc.M702112200
    • Holm GH, Zurney J, Tumilasci V, Danthi P, Hiscott J, Sherry B, Dermody TS (2007) Retinoic acid-inducible gene-I and interferon-b promoter stimulator-1 augment proapoptotic responses following mammalian reovirus infection via interferon regulatory factor-3. J Biol Chem 282:21953-21961 (Pubitemid 47195783)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 21953-21961
    • Holm, G.H.1    Zurney, J.2    Tumilasci, V.3    Leveille, S.4    Danthi, P.5    Hiscott, J.6    Sherry, B.7    Dermody, T.S.8
  • 74
    • 0029656249 scopus 로고    scopus 로고
    • Role of the m1 protein in reovirus stability and capacity to cause chromium release from host cells
    • Hooper JW, Fields BN (1996) Role of the m1 protein in reovirus stability and capacity to cause chromium release from host cells. J Virol 70:459-467
    • (1996) J Virol , vol.70 , pp. 459-467
    • Hooper, J.W.1    Fields, B.N.2
  • 76
    • 34249654610 scopus 로고    scopus 로고
    • A role for molecular chaperone Hsc70 in reovirus outer capsid disassembly
    • DOI 10.1074/jbc.M610258200
    • Ivanovic T, Agosto MA, Chandran K, Nibert ML (2007) A role for molecular chaperone Hsc70 in reovirus outer-capsid disassembly. J Biol Chem 282:12210-12219 (Pubitemid 47100676)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 12210-12219
    • Ivanovic, T.1    Agosto, M.A.2    Chandran, K.3    Nibert, M.L.4
  • 77
    • 42449151315 scopus 로고    scopus 로고
    • Peptides released from reovirus outer capsid form membrane pores that recruit virus particles
    • DOI 10.1038/emboj.2008.60, PII EMBOJ200860
    • Ivanovic T, Agosto MA, Zhang L, Chandran K, Harrison SC, Nibert ML (2008) Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. EMBO J 27:1289-1298 (Pubitemid 351574754)
    • (2008) EMBO Journal , vol.27 , Issue.8 , pp. 1289-1298
    • Ivanovic, T.1    Agosto, M.A.2    Zhang, L.3    Chandran, K.4    Harrison, S.C.5    Nibert, M.L.6
  • 78
    • 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
    • Jané-Valbuena J, Nibert ML, Spencer SM, Walker SB, Baker TS, Chen Y, Centonze VE, Schiff LA (1999) Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed s3 protein: An approach for analyzing s3 functions during virus entry. J Virol 73:2963-2973 (Pubitemid 29135685)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 2963-2973
    • Jane-Valbuena, J.1    Nibert, M.L.2    Spencer, S.M.3    Walker, S.B.4    Baker, T.S.5    Chen, Y.6    Centonze, V.E.7    Schiff, L.A.8
  • 79
    • 0036233299 scopus 로고    scopus 로고
    • Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein σ3
    • DOI 10.1128/JVI.76.10.5184-5197.2002
    • Jané-Valbuena J, Breun LA, Schiff LA, Nibert ML (2002) Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein s3. J Virol 76:5184-5197 (Pubitemid 34441722)
    • (2002) Journal of Virology , vol.76 , Issue.10 , pp. 5184-5197
    • Jane-Valbuena, J.1    Breun, L.A.2    Schiff, L.A.3    Nibert, M.L.4
  • 80
    • 0022626445 scopus 로고
    • Viral shedding and transmission between hosts determined by reovirus L2 gene
    • Keroack M, Fields BN (1986) Viral shedding and transmission between hosts determined by reovirus L2 gene. Science 232:1635-1638 (Pubitemid 16095604)
    • (1986) Science , vol.232 , Issue.4758 , pp. 1635-1638
    • Keroack, M.1    Fields, B.E.2
  • 83
    • 45749150395 scopus 로고    scopus 로고
    • Bovine papillomavirus type 1: From clathrin to caveolin
    • DOI 10.1128/JVI.00569-08
    • Laniosz V, Holthusen KA, Meneses PI (2008) Bovine papillomavirus type 1: From clathrin to caveolin. J Virol 82:6288-6298 (Pubitemid 351875108)
    • (2008) Journal of Virology , vol.82 , Issue.13 , pp. 6288-6298
    • Laniosz, V.1    Holthusen, K.A.2    Meneses, P.I.3
  • 84
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3
    • DOI 10.1016/S0092-8674(02)00612-8
    • Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC (2002) Structure of the reovirus membrane-penetration protein, m1, in a complex with its protector protein, s3. Cell 108:283-295 (Pubitemid 34161147)
    • (2002) Cell , vol.108 , Issue.2 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 85
    • 0027296972 scopus 로고
    • Reovirus M2 gene is associated with chromium release from mouse L cells
    • Lucia-Jandris P, Hooper JW, Fields BN (1993) Reovirus M2 gene is associated with chromium release from mouse L cells. J Virol 67:5339-5345 (Pubitemid 23241366)
    • (1993) Journal of Virology , vol.67 , Issue.9 , pp. 5339-5345
    • Lucia-Jandris, P.1    Hooper, J.W.2    Fields, B.N.3
  • 86
    • 0032508690 scopus 로고    scopus 로고
    • Binding site for S-adenosyl-L-methionine in a central region of mammalian reovirus λ2 protein. Evidence for activities in mRNA cap methylation
    • DOI 10.1074/jbc.273.37.23773
    • Luongo CL, Contreras CM, Farsetta DL, Nibert ML (1998) Binding site for S-adenosyl-Lmethionine in a central region of mammalian orthoreovirus l2 protein. Evidence for activities in mRNA cap methylation. J Biol Chem 273:23773-23780 (Pubitemid 28435710)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 23773-23780
    • Luongo, C.L.1    Contreras, C.M.2    Farsetta, D.L.3    Nibert, M.L.4
  • 87
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein λ2
    • DOI 10.1074/jbc.275.4.2804
    • Luongo CL, Reinisch KM, Harrison SC, Nibert ML (2000) Identification of the mRNA guanylyltransferase region and active site in reovirus l2 protein. J Biol Chem 275:2804-2810 (Pubitemid 30082052)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 89
    • 41149103877 scopus 로고    scopus 로고
    • NPXY motifs in the β1 integrin cytoplasmic tail are required for functional reovirus entry
    • DOI 10.1128/JVI.01612-07
    • Maginnis MS, Mainou BA, Derdowski AM, Johnson EM, Zent R, Dermody TS (2008) NPXY motifs in the b1 integrin cytoplasmic tail are required for functional reovirus entry. J Virol 82:3181-3191 (Pubitemid 351429899)
    • (2008) Journal of Virology , vol.82 , Issue.7 , pp. 3181-3191
    • Maginnis, M.S.1    Mainou, B.A.2    Derdowski, A.3    Johnson, E.M.4    Zent, R.5    Dermody, T.S.6
  • 90
    • 0036935194 scopus 로고    scopus 로고
    • Type 3 reovirus neuroinvasion after intramuscular inoculation: Direct invasion of nerve terminals and age-dependent pathogenesis
    • DOI 10.1006/viro.2002.1699
    • Mann MA, Knipe DM, Fischbach GD, Fields BN (2002) Type 3 reovirus neuroinvasion after intramuscular inoculation: Direct invasion of nerve terminals and age-dependent pathogenesis. Virology 303:222-231 (Pubitemid 36069187)
    • (2002) Virology , vol.303 , Issue.2 , pp. 222-231
    • Mann, M.A.1    Knipe, D.M.2    Fischbach, G.D.3    Fields, B.N.4
  • 91
    • 0025947194 scopus 로고
    • Isolation and enzymatic characterization of protein l2, the reovirus guanylyltransferase
    • Mao ZX, Joklik WK (1991) Isolation and enzymatic characterization of protein l2, the reovirus guanylyltransferase. Virology 185:377-386
    • (1991) Virology , vol.185 , pp. 377-386
    • Mao, Z.X.1    Joklik, W.K.2
  • 93
    • 0018083729 scopus 로고
    • The nature of the polypeptide encoded by each of the 10 double-stranded RNA segments of reovirus type 3
    • McCrae MA, Joklik WK (1978) The nature of the polypeptide encoded by each of the ten doublestranded RNA segments of reovirus type 3. Virology 89:578-593 (Pubitemid 9055906)
    • (1978) Virology , vol.89 , Issue.2 , pp. 578-593
    • McCrae, M.A.1    Joklik, W.K.2
  • 94
    • 0038045776 scopus 로고    scopus 로고
    • Digestion pattern of reovirus outer capsid protein σ3 determined by mass spectrometry
    • DOI 10.1016/S0042-6822(03)00154-5
    • Mendez II, She YM, Ens W, Coombs KM (2003) Digestion pattern of reovirus outer capsid protein s3 determined by mass spectrometry. Virology 311:289-304 (Pubitemid 36808772)
    • (2003) Virology , vol.311 , Issue.2 , pp. 289-304
    • Mendez, I.I.1    She, Y.-M.2    Ens, W.3    Coombs, K.M.4
  • 95
    • 17044438215 scopus 로고    scopus 로고
    • The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture
    • Merckel MC, Huiskonen JT, Bamford DH, Goldman A, Tuma R (2005) The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Mol Cell 18:161-170
    • (2005) Mol Cell , vol.18 , pp. 161-170
    • Merckel, M.C.1    Huiskonen, J.T.2    Bamford, D.H.3    Goldman, A.4    Tuma, R.5
  • 96
    • 0020028581 scopus 로고
    • The symmetry of the reovirus outer shell
    • DOI 10.1016/S0022-5320(82)80004-X
    • Metcalf P (1982) The symmetry of the reovirus outer shell. J Ultrastruct Res 78:292-301 (Pubitemid 12127627)
    • (1982) Journal of Ultrastructure Research , vol.78 , Issue.3 , pp. 292-301
    • Metcalf, P.1
  • 97
    • 34147164393 scopus 로고    scopus 로고
    • Thermostabilizing mutations in reovirus outer-capsid protein μ1 selected by heat inactivation of infectious subvirion particles
    • DOI 10.1016/j.virol.2006.11.024, PII S0042682206008737
    • Middleton JK, Agosto MA, Severson TF, Yin J, Nibert ML (2007) Thermostabilizing mutations in reovirus outer-capsid protein m1 selected by heat inactivation of infectious subvirion particles. Virology 361:412-425 (Pubitemid 46574850)
    • (2007) Virology , vol.361 , Issue.2 , pp. 412-425
    • Middleton, J.K.1    Agosto, M.A.2    Severson, T.F.3    Yin, J.4    Nibert, M.L.5
  • 98
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • DOI 10.1016/S0092-8674(00)81363-X
    • Montgomery RI, Warner MS, Lum BJ, Spear PG (1996) Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87:427-436 (Pubitemid 26374317)
    • (1996) Cell , vol.87 , Issue.3 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 99
    • 0035099375 scopus 로고    scopus 로고
    • Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2
    • DOI 10.1034/j.1600-0854.2001.020206.x
    • Morris SM, Cooper JA (2001) Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2:111-123 (Pubitemid 32219864)
    • (2001) Traffic , vol.2 , Issue.2 , pp. 111-123
    • Morris, S.M.1    Cooper, J.A.2
  • 101
    • 0018077111 scopus 로고
    • Genetics of reovirus: Identification of the ds RNA segments encoding the polypeptides of the μ and σ size classes
    • Mustoe TA, Ramig RF, Sharpe AH, Fields BN (1978) Genetics of reovirus: Identification of the dsRNA segments encoding the polypeptides of the m and s size classes. Virology 89:594-604 (Pubitemid 9055907)
    • (1978) Virology , vol.89 , Issue.2 , pp. 594-604
    • Mustoe, T.A.1    Ramig, R.F.2    Sharpe, A.H.3    Fields, B.N.4
  • 102
    • 0026733619 scopus 로고
    • A carboxy-terminal fragment of protein m1/m1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration
    • Nibert ML, Fields BN (1992) A carboxy-terminal fragment of protein m1/m1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J Virol 66:6408-6418
    • (1992) J Virol , vol.66 , pp. 6408-6418
    • Nibert, M.L.1    Fields, B.N.2
  • 103
    • 0025299741 scopus 로고
    • Structure of the reovirus cell-attachment protein: A model for the domain organization of σ1
    • Nibert ML, Dermody TS, Fields BN (1990) Structure of the reovirus cell-attachment protein: A model for the domain organization of s1. J Virol 64:2976-2989 (Pubitemid 20171290)
    • (1990) Journal of Virology , vol.64 , Issue.6 , pp. 2976-2989
    • Nibert, M.L.1    Dermody, T.S.2    Fields, B.N.3
  • 104
    • 0029058860 scopus 로고
    • Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved s1 protein
    • Nibert ML, Chappell JD, Dermody TS (1995) Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved s1 protein. J Virol 69:5057-5067
    • (1995) J Virol , vol.69 , pp. 5057-5067
    • Nibert, M.L.1    Chappell, J.D.2    Dermody, T.S.3
  • 107
    • 3543115472 scopus 로고    scopus 로고
    • Putative autocleavage of outer capsid protein μ1, allowing release of myristoylated peptide μ1N during particle uncoating, is critical for cell entry by reovirus
    • DOI 10.1128/JVI.78.16.8732-8745.2004
    • Odegard AL, Chandran K, Zhang X, Parker JS, Baker TS, Nibert ML (2004) Putative autocleavage of outer capsid protein m1, allowing release of myristoylated peptide m1N during particle uncoating, is critical for cell entry by reovirus. J Virol 78:8732-8745 (Pubitemid 39025138)
    • (2004) Journal of Virology , vol.78 , Issue.16 , pp. 8732-8745
    • Odegard, A.L.1    Chandran, K.2    Zhang, X.3    Parker, J.S.L.4    Baker, T.S.5    Nibert, M.L.6
  • 108
    • 0034193309 scopus 로고    scopus 로고
    • Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin
    • DOI 10.1042/0264-6021:3470613
    • Oleinikov AV, Zhao J, Makker SP (2000) Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin. Biochem J 347:613-621 (Pubitemid 30260949)
    • (2000) Biochemical Journal , vol.347 , Issue.3 , pp. 613-621
    • Oleinikov, A.V.1    Zhao, J.2    Makker, S.P.3
  • 109
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 A resolution
    • DOI 10.1093/emboj/20.5.979
    • Olland AM, Jané-Valbuena J, Schiff LA, Nibert ML, Harrison SC (2001) Structure of the reovirus outer capsid and dsRNA-binding protein s3 at 1.8 A resolution. EMBO J 20:979-989 (Pubitemid 32186789)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 979-989
    • Olland, A.M.1    Jane-Valbuena, J.2    Schiff, L.A.3    Nibert, M.L.4    Harrison, S.C.5
  • 110
    • 20344381822 scopus 로고    scopus 로고
    • Glycoconjugate glycans as viral receptors
    • DOI 10.1080/07853890510007340
    • Olofsson S, Bergstrom T (2005) Glycoconjugate glycans as viral receptors. Ann Med 37:154-172 (Pubitemid 40780433)
    • (2005) Annals of Medicine , vol.37 , Issue.3 , pp. 154-172
    • Olofsson, S.1    Bergstrom, T.2
  • 111
    • 26444552119 scopus 로고    scopus 로고
    • Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein
    • DOI 10.1128/JVI.79.20.12714-12720.2005
    • Pager CT, Dutch RE (2005) Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J Virol 79:12714-12720 (Pubitemid 41433191)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12714-12720
    • Pager, C.T.1    Dutch, R.E.2
  • 112
    • 0024429657 scopus 로고
    • The α-anomeric form of sialic acid is the minimal receptor determinant recognized by reovirus
    • DOI 10.1016/0042-6822(89)90146-3
    • Paul RW, Choi AH, Lee PWK (1989) The a-anomeric form of sialic acid is the minimal receptor determinant recognized by reovirus. Virology 172:382-385 (Pubitemid 19221468)
    • (1989) Virology , vol.172 , Issue.1 , pp. 382-385
    • Paul, R.W.1    Choi, A.H.C.2    Lee, P.W.K.3
  • 114
    • 33748936911 scopus 로고    scopus 로고
    • Invasion of host cells by JC virus identifies a novel role for caveolae in endosomal sorting of noncaveolar ligands
    • DOI 10.1128/JVI.01086-06
    • Querbes W, O'Hara BA, Williams G, Atwood WJ (2006) Invasion of host cells by JC virus identifies a novel role for caveolae in endosomal sorting of noncaveolar ligands. J Virol 80:9402-9413 (Pubitemid 44435619)
    • (2006) Journal of Virology , vol.80 , Issue.19 , pp. 9402-9413
    • Querbes, W.1    O'Hara, B.A.2    Williams, G.3    Atwood, W.J.4
  • 115
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 A resolution
    • DOI 10.1038/35010041
    • Reinisch KM, Nibert ML, Harrison SC (2000) Structure of the reovirus core at 3.6 A resolution. Nature 404:960-967 (Pubitemid 30243583)
    • (2000) Nature , vol.404 , Issue.6781 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 116
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • DOI 10.1016/S1074-7613(00)80249-6
    • Riese RJ, Wolf PR, Bromme D, Natkin LR, Villadangos JA, Ploegh HL, Chapman HA (1996) Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4:357-366 (Pubitemid 26174051)
    • (1996) Immunity , vol.4 , Issue.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 117
    • 0027082360 scopus 로고
    • Binding of type 3 reovirus by a domain of the σ1 protein important for hemagglutination leads to infection of murine erythroleukemia cells
    • Rubin DH, Wetzel JD, Williams WV, Cohen JA, Dworkin C, Dermody TS (1992) Binding of type 3 reovirus by a domain of the s1 protein important for hemagglutination leads to infection of murine erythroleukemia cells. J Clin Invest 90:2536-2542 (Pubitemid 23010075)
    • (1992) Journal of Clinical Investigation , vol.90 , Issue.6 , pp. 2536-2542
    • Rubin, D.H.1    Wetzel, J.D.2    Williams, W.V.3    Cohen, J.A.4    Dworkin, C.5    Dermody, T.S.6
  • 118
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau QJ, Moore JP (1991) Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J Exp Med 174:407-415
    • (1991) J Exp Med , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 120
    • 34548650332 scopus 로고    scopus 로고
    • Orthoreoviruses and their replication
    • Knipe DM, Howley PM (eds), 5th edn. Lippincott Williams & Wilkins, Philadelphia
    • Schiff LA, Nibert ML, Tyler KL (2007) Orthoreoviruses and their replication. In: Knipe DM, Howley PM (eds) Fields virology, 5th edn. Lippincott Williams & Wilkins, Philadelphia, pp 1853-1915
    • (2007) Fields Virology , pp. 1853-1915
    • Schiff, L.A.1    Nibert, M.L.2    Tyler, K.L.3
  • 121
    • 0026757341 scopus 로고
    • Maturation cleavage required for infectivity of a nodavirus
    • Schneemann A, Zhong W, Gallagher TM, Rueckert RR (1992) Maturation cleavage required for infectivity of a nodavirus. J Virol 66:6728-6734
    • (1992) J Virol , vol.66 , pp. 6728-6734
    • Schneemann, A.1    Zhong, W.2    Gallagher, T.M.3    Rueckert, R.R.4
  • 122
    • 0023646021 scopus 로고
    • Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase
    • Seliger LS, Zheng K, Shatkin AJ (1987) Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase. J Biol Chem 262:16289-16293
    • (1987) J Biol Chem , vol.262 , pp. 16289-16293
    • Seliger, L.S.1    Zheng, K.2    Shatkin, A.J.3
  • 124
    • 0027177215 scopus 로고
    • Reovirus protein l3 is a poly(C)-dependent poly(G) polymerase
    • Starnes MC, Joklik WK (1993) Reovirus protein l3 is a poly(C)-dependent poly(G) polymerase. Virology 193:356-366
    • (1993) Virology , vol.193 , pp. 356-366
    • Starnes, M.C.1    Joklik, W.K.2
  • 125
    • 0037341386 scopus 로고    scopus 로고
    • Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins
    • DOI 10.1002/rmv.379
    • Stehle T, Dermody TS (2003) Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins. Rev Med Virol 13:123-132 (Pubitemid 36323675)
    • (2003) Reviews in Medical Virology , vol.13 , Issue.2 , pp. 123-132
    • Stehle, T.1    Dermody, T.S.2
  • 126
    • 3042772542 scopus 로고    scopus 로고
    • Structural similarities in the cellular receptors used by adenovirus and reovirus
    • DOI 10.1089/0882824041310621
    • Stehle T, Dermody TS (2004) Structural similarities in the cellular receptors used by adenovirus and reovirus. Viral Immunol 17:129-143 (Pubitemid 38880416)
    • (2004) Viral Immunology , vol.17 , Issue.2 , pp. 129-143
    • Stehle, T.1    Dermody, T.S.2
  • 127
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Grober A, Vey M, Angliker H, Shaw E, Thomas G, Roberts C, Klenk HD, Garten W (1992) Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J 11:2407-2414
    • (1992) EMBO J , vol.11 , pp. 2407-2414
    • Stieneke-Grober, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.D.7    Garten, W.8
  • 128
    • 33744908612 scopus 로고    scopus 로고
    • Drug evaluation: Reolysin - Wild-type reovirus as a cancer therapeutic
    • Stoeckel J, Hay JG (2006) Drug evaluation: Reolysin-wild-type reovirus as a cancer therapeutic. Curr Opin Mol Ther 8:249-260 (Pubitemid 43842396)
    • (2006) Current Opinion in Molecular Therapeutics , vol.8 , Issue.3 , pp. 249-260
    • Stoeckel, J.1    Hay, J.G.2
  • 129
    • 0025866624 scopus 로고
    • Biochemical and biophysical characterization of the reovirus cell attachment protein sigma 1: Evidence that it is a homotrimer
    • Strong JE, Leone G, Duncan R, Sharma RK, Lee PW (1991) Biochemical and biophysical characterization of the reovirus cell attachment protein sigma 1: Evidence that it is a homotrimer. Virology 184:23-32
    • (1991) Virology , vol.184 , pp. 23-32
    • Strong, J.E.1    Leone, G.2    Duncan, R.3    Sharma, R.K.4    Lee, P.W.5
  • 130
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker LJ, Nibert ML, Furlong DB, Fields BN (1987) Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J Virol 61:2351-2361 (Pubitemid 17097545)
    • (1987) Journal of Virology , vol.61 , Issue.8 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.2    Furlong, D.3    Fields, B.N.4
  • 132
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage - Structural studies of reovirus polymerase λ3
    • DOI 10.1016/S0092-8674(02)01110-8
    • Tao Y, Farsetta DL, Nibert ML, Harrison SC (2002) RNA synthesis in a cage - structural studies of reovirus polymerase l3. Cell 111:733-745 (Pubitemid 35452525)
    • (2002) Cell , vol.111 , Issue.5 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 133
    • 0020628793 scopus 로고
    • Age dependent susceptibility to reovirus type 3 encephalitis: Role of viral and host factors
    • Tardieu M, Powers ML, Weiner HL (1983) Age-dependent susceptibility to reovirus type 3 encephalitis: Role of viral and host factors. Ann Neurol 13:602-607 (Pubitemid 13103456)
    • (1983) Annals of Neurology , vol.13 , Issue.6 , pp. 602-607
    • Tardieu, M.1    Powers, M.L.2    Weiner, H.L.3
  • 135
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • DOI 10.1093/emboj/20.17.4629
    • Turk V, Turk B, Turk D (2001) Lysosomal cysteine proteases: Facts and opportunities. EMBO J 20:4629-4633 (Pubitemid 32848615)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 136
    • 0022449010 scopus 로고
    • Distinct pathways of viral spread in the host determined by reovirus S1 gene segment
    • Tyler KL, McPhee DA, Fields BN (1986) Distinct pathways of viral spread in the host determined by reovirus S1 gene segment. Science 233:770-774 (Pubitemid 16016228)
    • (1986) Science , vol.233 , Issue.4765 , pp. 770-774
    • Tyler, K.L.1    McPhee, D.A.2    Fields, B.N.3
  • 140
    • 0032893134 scopus 로고    scopus 로고
    • HIV-1 attachment: Another look
    • DOI 10.1016/S0966-842X(99)01474-2, PII S0966842X99014742
    • Ugolini S, Mondor I, Sattentau QJ (1999) HIV-1 attachment: Another look. Trends Microbiol 7:144-149 (Pubitemid 29229899)
    • (1999) Trends in Microbiology , vol.7 , Issue.4 , pp. 144-149
    • Ugolini, S.1    Mondor, I.2    Sattentau, Q.J.3
  • 141
    • 0033613385 scopus 로고    scopus 로고
    • A triple b-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • van Raaij MJ, Mitraki A, Lavigne G, Cusack S (1999) A triple b-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature 401:935-938
    • (1999) Nature , vol.401 , pp. 935-938
    • Van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 142
  • 143
    • 38849207569 scopus 로고    scopus 로고
    • Rescue of maturation-defective flock house virus infectivity with noninfectious, mature, viruslike particles
    • DOI 10.1128/JVI.02278-07
    • Walukiewicz HE, Banerjee M, Schneemann A, Johnson JE (2008) Rescue of maturationdefective flock house virus infectivity with noninfectious, mature, viruslike particles. J Virol 82:2025-2027 (Pubitemid 351206947)
    • (2008) Journal of Virology , vol.82 , Issue.4 , pp. 2025-2027
    • Walukiewicz, H.E.1    Banerjee, M.2    Schneemann, A.3    Johnson, J.E.4
  • 145
    • 0018818532 scopus 로고
    • Absolute linkage of virulence and central nervous system cell tropism of reoviruses to viral hemagglutinin
    • Weiner HL, Powers ML, Fields BN (1980) Absolute linkage of virulence and central nervous system tropism of reoviruses to viral hemagglutinin. J Infect Dis 141:609-616 (Pubitemid 10109830)
    • (1980) Journal of Infectious Diseases , vol.141 , Issue.5 , pp. 609-616
    • Weiner, H.L.1    Powers, M.L.2    Fields Fields, B.N.3
  • 146
    • 0027463283 scopus 로고
    • Isolation and genetic characterization of ethanol-resistant reovirus mutants
    • Wessner DR, Fields BN (1993) Isolation and genetic characterization of ethanol-resistant reovirus mutants. J Virol 67:2442-2447 (Pubitemid 23118837)
    • (1993) Journal of Virology , vol.67 , Issue.5 , pp. 2442-2447
    • Wessner, D.R.1    Fields, B.N.2
  • 147
    • 0031026434 scopus 로고    scopus 로고
    • Reovirus variants selected during persistent infections of L cells contain mutations in the vital S1 and S4 genes and are altered in viral disassembly
    • Wetzel JD, Wilson GJ, Baer GS, Dunnigan LR, Wright JP, Tang DSH, Dermody TS (1997) Reovirus variants selected during persistent infections of L cells contain mutations in the viral S1 and S4 genes and are altered in viral disassembly. J Virol 71:1362-1369 (Pubitemid 27030310)
    • (1997) Journal of Virology , vol.71 , Issue.2 , pp. 1362-1369
    • Wetzel, J.D.1    Wilson, G.J.2    Baer, G.S.3    Dunnigan, L.R.4    Wright, J.P.5    Tang, D.S.H.6    Dermody, T.S.7
  • 148
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein VI mediates membrane disruption following capsid disassembly
    • DOI 10.1128/JVI.79.4.1992-2000.2005
    • Wiethoff CM, Wodrich H, Gerace L, Nemerow GR (2005) Adenovirus protein VI mediates membrane disruption following capsid disassembly. J Virol 79:1992-2000 (Pubitemid 40204556)
    • (2005) Journal of Virology , vol.79 , Issue.4 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 150
    • 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
    • DOI 10.1128/JVI.76.19.9832-9843.2002
    • Wilson GJ, Nason EL, Hardy CS, Ebert DH, Wetzel JD, Prasad BVV, Dermody TS (2002) A single mutation in the carboxy terminus of reovirus outer-capsid protein s3 confers enhanced kinetics of s3 proteolysis, resistance to inhibitors of viral disassembly, and alterations in s3 structure. J Virol 76:9832-9843 (Pubitemid 35006523)
    • (2002) Journal of Virology , vol.76 , Issue.19 , pp. 9832-9843
    • Wilson, G.J.1    Nason, E.L.2    Hardy, C.S.3    Ebert, D.H.4    Wetzel, J.D.5    Prasad, B.V.V.6    Dermody, T.S.7
  • 153
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase λ3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A
    • DOI 10.1038/nsb1009
    • Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS (2003) Reovirus polymerase l3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A . Nat Struct Biol 10:1011-1018 (Pubitemid 37500493)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5
  • 154
    • 26444511104 scopus 로고    scopus 로고
    • Features of reovirus outer capsid protein μ1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 A resolution
    • DOI 10.1016/j.str.2005.07.012, PII S0969212605002716
    • Zhang X, Ji Y, Zhang L, Harrison SC, Marinescu DC, Nibert ML, Baker TS (2005) Features of reovirus outer capsid protein m1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 A resolution. Structure 13:1545-1557 (Pubitemid 41427593)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1545-1557
    • Zhang, X.1    Ji, Y.2    Zhang, L.3    Harrison, S.C.4    Marinescu, D.C.5    Nibert, M.L.6    Baker, T.S.7
  • 155
    • 33845419956 scopus 로고    scopus 로고
    • Reovirus μ1 structural rearrangements that mediate membrane penetration
    • DOI 10.1128/JVI.01343-06
    • Zhang L, Chandran K, Nibert ML, Harrison SC (2006) Reovirus m1 structural rearrangements that mediate membrane penetration. J Virol 80:12367-12376 (Pubitemid 44904387)
    • (2006) Journal of Virology , vol.80 , Issue.24 , pp. 12367-12376
    • Zhang, L.1    Chandran, K.2    Nibert, M.L.3    Harrison, S.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.