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Volumn 309, Issue , 2006, Pages 1-38

Attachment and cell entry of mammalian orthoreovirus

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; DOUBLE STRANDED RNA; JUNCTIONAL ADHESION MOLECULE A; PROTEINASE; SIALIC ACID; VIRUS PROTEIN; VIRUS RECEPTOR; BACTERIOPHAGE RECEPTOR; CELL ADHESION MOLECULE; IMMUNOGLOBULIN; JUNCTIONAL ADHESION MOLECULE A , HUMAN; JUNCTIONAL ADHESION MOLECULE-A , HUMAN; N ACETYLNEURAMINIC ACID; PEPTIDE HYDROLASE; SIGMA 1 PROTEIN, REOVIRUS;

EID: 33748120749     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/3-540-30773-7_1     Document Type: Review
Times cited : (57)

References (166)
  • 1
    • 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
    • (1994) J Virol , vol.68 , pp. 8428-8432
    • Amerongen, H.M.1    Wilson, G.A.R.2    Fields, B.N.3    Neutra, M.R.4
  • 2
    • 0035824527 scopus 로고    scopus 로고
    • Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor
    • Arrate MP, Rodriguez JM, Tran TM, Brock TA, Cunningham SA (2001) Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. J Biol Chem 276:45826-45832
    • (2001) J Biol Chem , vol.276 , pp. 45826-45832
    • Arrate, M.P.1    Rodriguez, J.M.2    Tran, T.M.3    Brock, T.A.4    Cunningham, S.A.5
  • 3
    • 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 σ3 selected during persistent infections of L cells confer resistance to protease inhibitor E64. J Virol 71:4921-4928
    • (1997) J Virol , vol.71 , pp. 4921-4928
    • Baer, G.S.1    Dermody, T.S.2
  • 4
    • 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
    • (1999) J Virol , vol.73 , pp. 9532-9543
    • Baer, G.S.1    Ebert, D.H.2    Chung, C.J.3    Erickson, A.H.4    Dermody, T.S.5
  • 5
    • 0034513771 scopus 로고    scopus 로고
    • Transmembrane proteins of tight junctions
    • Balda MS, Matter K (2000) Transmembrane proteins of tight junctions. Semin Cell Dev Biol 11:281-289
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 281-289
    • Balda, M.S.1    Matter, K.2
  • 6
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett AJ, Kembhavi AA, Brown MA, Kirschke H, Knight CG, Tamai M, Hanada K (1982) L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem J 201:189-198
    • (1982) Biochem J , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 7
    • 0035910468 scopus 로고    scopus 로고
    • Utilization of sialic acid as a coreceptor enhances reovirus attachment bymultistep adhesion strengthening
    • Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS (2001) Utilization of sialic acid as a coreceptor enhances reovirus attachment bymultistep adhesion strengthening. J Biol Chem 276:2200-2211
    • (2001) J Biol Chem , vol.276 , pp. 2200-2211
    • Barton, E.S.1    Connolly, J.L.2    Forrest, J.C.3    Chappell, J.D.4    Dermody, T.S.5
  • 10
    • 0025249289 scopus 로고
    • Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus 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
    • (1990) J Virol , vol.64 , 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
  • 11
    • 0022442854 scopus 로고
    • Identification of attenuating mutations on the reovirus type 3 S1 double-stranded RNA segment with a rapid sequencing technique
    • Bassel-Duby R, Spriggs DR, Tyler KL, Fields BN (1986) Identification of attenuating mutations on the reovirus type 3 S1 double-stranded RNA segment with a rapid sequencing technique. J Virol 60:64-67
    • (1986) J Virol , vol.60 , pp. 64-67
    • Bassel-Duby, R.1    Spriggs, D.R.2    Tyler, K.L.3    Fields, B.N.4
  • 13
    • 0039027605 scopus 로고    scopus 로고
    • Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin
    • Bazzoni G, Martinez-Estrada OM, Orsenigo F, Cordenonsi M, Citi S, Dejana E (2000) Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin. J Biol Chem 275:20520-20526
    • (2000) J Biol Chem , vol.275 , pp. 20520-20526
    • Bazzoni, G.1    Martinez-Estrada, O.M.2    Orsenigo, F.3    Cordenonsi, M.4    Citi, S.5    Dejana, E.6
  • 15
    • 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
    • (1989) J Virol , vol.63 , pp. 4676-4681
    • Bodkin, D.K.1    Nibert, M.L.2    Fields, B.N.3
  • 18
    • 0019403390 scopus 로고
    • Reovirus: Evidence for a second step in the intracellular uncoating and transcriptase activation process
    • 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
    • (1981) Virology , vol.111 , pp. 191-200
    • Borsa, J.1    Sargent, M.D.2    Lievaart, P.A.3    Copps, T.P.4
  • 19
    • 0037334521 scopus 로고    scopus 로고
    • Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells
    • Bousarghin L, Touze A, Sizaret PY, Coursaget P (2003) Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells. J Virol 77:3846-3850
    • (2003) J Virol , vol.77 , pp. 3846-3850
    • Bousarghin, L.1    Touze, A.2    Sizaret, P.Y.3    Coursaget, P.4
  • 20
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 21
    • 0020694127 scopus 로고
    • Ammonium chloride prevents lytic growth of reovirus and helps to establish persistent infection in mouse L cells
    • Canning WM, Fields BN (1983) Ammonium chloride prevents lytic growth of reovirus and helps to establish persistent infection in mouse L cells. Science 219:987-988
    • (1983) Science , vol.219 , pp. 987-988
    • Canning, W.M.1    Fields, B.N.2
  • 22
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson M (1987) Ribbon models of macromolecules. J Mol Graph 5:103-106
    • (1987) J Mol Graph , vol.5 , pp. 103-106
    • Carson, M.1
  • 24
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: A hydrophobic conformer of the reovirus membrane penetration protein μ1 mediates membrane disruption
    • Chandran K, Farsetta DL, Nibert ML (2002) Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein μ1 mediates membrane disruption. J Virol 76:9920-9933
    • (2002) J Virol , vol.76 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 25
    • 0031964230 scopus 로고    scopus 로고
    • Protease cleavage of reovirus capsidprotein 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 capsidprotein μ1/μ1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle. J Virol 762:467-475
    • (1998) J Virol , vol.762 , pp. 467-475
    • Chandran, K.1    Nibert, M.L.2
  • 26
    • 0345166984 scopus 로고    scopus 로고
    • The delta region of outer-capsid protein μ1 undergoes conformational change and release from reovirus particles during cell entry
    • Chandran K, Parker JS, Ehrlich M, Kirchhausen T, Nibert ML (2003) The delta region of outer-capsid protein μ1 undergoes conformational change and release from reovirus particles during cell entry. J Virol 77:13361-13375
    • (2003) J Virol , vol.77 , pp. 13361-13375
    • Chandran, K.1    Parker, J.S.2    Ehrlich, M.3    Kirchhausen, T.4    Nibert, M.L.5
  • 28
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman HA, Riese RJ, Shi GP (1997) Emerging roles for cysteine proteases in human biology. Annu Rev Physiol 59:63-88
    • (1997) Annu Rev Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 29
    • 0033861681 scopus 로고    scopus 로고
    • Identification of carbohydrate-binding domains in the attachment proteins of type 1 and type 3 reoviruses
    • 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
    • (2000) J Virol , vol.74 , pp. 8472-8479
    • Chappell, J.D.1    Duong, J.L.2    Wright, B.W.3    Dermody, T.S.4
  • 30
    • 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 σ1. J Virol 71:1834-1841
    • (1997) J Virol , vol.71 , pp. 1834-1841
    • Chappell, J.D.1    Gunn, V.L.2    Wetzel, J.D.3    Baer, G.S.4    Dermody, T.S.5
  • 31
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber
    • Chappell JD, Prota A, Dermody TS, Stehle T (2002) Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber. EMBO J 21:1-11
    • (2002) EMBO J , vol.21 , pp. 1-11
    • Chappell, J.D.1    Prota, A.2    Dermody, T.S.3    Stehle, T.4
  • 34
    • 0035043244 scopus 로고    scopus 로고
    • Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis
    • Connolly JL, Barton ES, Dermody TS (2001) Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis. J Virol 75:4029-4039
    • (2001) J Virol , vol.75 , pp. 4029-4039
    • Connolly, J.L.1    Barton, E.S.2    Dermody, T.S.3
  • 35
    • 0036147875 scopus 로고    scopus 로고
    • Virion disassembly is required for apoptosis induced by reovirus
    • Connolly JL, Dermody TS (2002) Virion disassembly is required for apoptosis induced by reovirus. J Virol 76:1632-1641
    • (2002) J Virol , vol.76 , pp. 1632-1641
    • Connolly, J.L.1    Dermody, T.S.2
  • 38
    • 0034749514 scopus 로고    scopus 로고
    • Calpain inhibition protects against virus-induced apoptotic myocardial injury
    • DeBiasi R, Edelstein C, Sherry B, Tyler K (2001) Calpain inhibition protects against virus-induced apoptotic myocardial injury. J Virol 75:351-361
    • (2001) J Virol , vol.75 , pp. 351-361
    • DeBiasi, R.1    Edelstein, C.2    Sherry, B.3    Tyler, K.4
  • 41
    • 0031844201 scopus 로고    scopus 로고
    • Dermody TS (1998) Molecular mechanisms of persistent infection by reovirus. In: Tyler KL, Oldstone MBA (eds), Curr Topics Micro Immunol, 233. Reoviruses, II Cytopathogenicity and pathogenesis. Springer-Verlag, Berlin Heidelberg, New York, pp 1-22
    • Dermody TS (1998) Molecular mechanisms of persistent infection by reovirus. In: Tyler KL, Oldstone MBA (eds), Curr Topics Micro Immunol, vol. 233. Reoviruses, II Cytopathogenicity and pathogenesis. Springer-Verlag, Berlin Heidelberg, New York, pp 1-22
  • 42
    • 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 σ1 region important for hemagglutination by serotype 3 reovirus strains. J Virol 64:5173-5176
    • (1990) J Virol , vol.64 , pp. 5173-5176
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 43
    • 0025134429 scopus 로고
    • Sequence diversity in S1 genes and S1 translation products of 11 serotype 3 reovirus strains
    • Dermody TS, Nibert ML, Bassel-Duby R, Fields BN (1990) Sequence diversity in S1 genes and S1 translation products of 11 serotype 3 reovirus strains. J Virol 64:4842-4850
    • (1990) J Virol , vol.64 , pp. 4842-4850
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 44
    • 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
    • (1993) J Virol , vol.67 , pp. 2055-2063
    • Dermody, T.S.1    Nibert, M.L.2    Wetzel, J.D.3    Tong, X.4    Fields, B.N.5
  • 45
    • 0021723208 scopus 로고
    • Infection of neuronal cell cultures with reovirus mimics in vitro patterns of neurotropism
    • Dichter MA, Weiner HL (1984) Infection of neuronal cell cultures with reovirus mimics in vitro patterns of neurotropism. Ann Neurol 16:603-610
    • (1984) Ann Neurol , vol.16 , pp. 603-610
    • Dichter, M.A.1    Weiner, H.L.2
  • 46
    • 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
    • (1993) J Cell Biol , vol.122 , 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
  • 47
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • 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
    • (1998) Virology , vol.245 , 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
  • 48
    • 0028088356 scopus 로고
    • Localization of two protease-sensitive regions separating distinct domains in the reovirus cell-attachment protein sigma 1
    • Duncan R, Lee PWK (1994) Localization of two protease-sensitive regions separating distinct domains in the reovirus cell-attachment protein sigma 1. Virology 203:149-152
    • (1994) Virology , vol.203 , pp. 149-152
    • Duncan, R.1    Lee, P.W.K.2
  • 49
    • 0025727528 scopus 로고
    • Conformational and functional analysis of the C-terminal globular head of the reovirus cell attachment protein
    • Duncan R, Horne D, Strong JE, Leone G, Pon RT, Yeung MC, Lee PWK (1991) Conformational and functional analysis of the C-terminal globular head of the reovirus cell attachment protein. Virology 182:810-819
    • (1991) Virology , vol.182 , pp. 810-819
    • Duncan, R.1    Horne, D.2    Strong, J.E.3    Leone, G.4    Pon, R.T.5    Yeung, M.C.6    Lee, P.W.K.7
  • 50
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • 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
    • (2002) J Biol Chem , vol.277 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 51
    • 0942265520 scopus 로고    scopus 로고
    • Cathepsin B is inhibited in mutant cells selected during persistent reovirus infection
    • Ebert DH, Kopecky-Bromberg SA, Dermody TS (2004) Cathepsin B is inhibited in mutant cells selected during persistent reovirus infection. J Biol Chem 279:3837-3851
    • (2004) J Biol Chem , vol.279 , pp. 3837-3851
    • Ebert, D.H.1    Kopecky-Bromberg, S.A.2    Dermody, T.S.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
    • 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 σ3. J Virol 75:3197-3206
    • (2001) J Virol , vol.75 , 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
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesionmolecule interactswith the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (2000) Junctional adhesionmolecule interactswith the PDZ domain-containing proteins AF-6 and ZO-1. J Biol Chem 275:27979-27988
    • (2000) J Biol Chem , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer, Z.3    Brickwedde, M.K.4    Pendl, G.G.5    Vestweber, D.6
  • 55
    • 0346025727 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs): More molecules with dual functions?
    • Ebnet K, Suzuki A, Ohno S, Vestweber D (2004) Junctional adhesion molecules (JAMs): more molecules with dual functions? J Cell Sci 117:19-29
    • (2004) J Cell Sci , vol.117 , pp. 19-29
    • Ebnet, K.1    Suzuki, A.2    Ohno, S.3    Vestweber, D.4
  • 57
    • 0019440664 scopus 로고
    • Proteolytic enhancement of rotavirus infectivity: Molecular mechanisms
    • Estes MK, Graham DY, Mason BB (1981) Proteolytic enhancement of rotavirus infectivity: molecular mechanisms. J Virol 39:879-888
    • (1981) J Virol , vol.39 , pp. 879-888
    • Estes, M.K.1    Graham, D.Y.2    Mason, B.B.3
  • 58
    • 3242794249 scopus 로고    scopus 로고
    • Peyer's patch dendritic cells process viral antigen from apoptotic epithelial cells in the intestine of reovirus-infected mice
    • 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
    • (2004) J Exp Med , vol.200 , pp. 235-245
    • Fleeton, M.1    Contractor, N.2    Leon, F.3    Wetzel, J.D.4    Dermody, T.S.5    Kelsall, B.6
  • 59
    • 0346220255 scopus 로고    scopus 로고
    • Structure-function analysis of reovirus binding to junctional adhesionmolecule 1. Implications for the mechanism of reovirus attachment
    • Forrest JC, Campbell JA, Schelling P, Stehle T, Dermody TS (2003) Structure-function analysis of reovirus binding to junctional adhesionmolecule 1. Implications for the mechanism of reovirus attachment. J Biol Chem 278:48434-48444
    • (2003) J Biol Chem , vol.278 , pp. 48434-48444
    • Forrest, J.C.1    Campbell, J.A.2    Schelling, P.3    Stehle, T.4    Dermody, T.S.5
  • 60
    • 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
    • (1990) J Virol , vol.64 , 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
  • 61
    • 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
    • (1988) J Virol , vol.62 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 62
    • 0022541361 scopus 로고
    • The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity
    • Gal S, Gottesman MM (1986) The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity. Biochem Biophys Res Commun 139:156-162
    • (1986) Biochem Biophys Res Commun , vol.139 , pp. 156-162
    • Gal, S.1    Gottesman, M.M.2
  • 63
    • 0021971028 scopus 로고
    • Processing and lysosomal localization of a glycoprotein whose secretion is transformation stimulated
    • Gal S, Willingham MC, Gottesman MM (1985) Processing and lysosomal localization of a glycoprotein whose secretion is transformation stimulated. J Cell Biol 100:535-544
    • (1985) J Cell Biol , vol.100 , pp. 535-544
    • Gal, S.1    Willingham, M.C.2    Gottesman, M.M.3
  • 64
    • 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
    • (1985) J Virol , vol.56 , pp. 356-364
    • Gentsch, J.R.1    Pacitti, A.F.2
  • 65
    • 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
  • 67
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG (1998) Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280:1618-1620
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 69
    • 0018866673 scopus 로고
    • Tumor promoters and Kirsten sarcoma virus increase synthesis of a secreted glycoprotein by regulating levels of translatable mRNA
    • Gottesman MM, Sobel ME (1980) Tumor promoters and Kirsten sarcoma virus increase synthesis of a secreted glycoprotein by regulating levels of translatable mRNA. Cell 19:449-455
    • (1980) Cell , vol.19 , pp. 449-455
    • Gottesman, M.M.1    Sobel, M.E.2
  • 70
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (2002) Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J Biol Chem 277:455-461
    • (2002) J Biol Chem , vol.277 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 71
    • 0038082242 scopus 로고    scopus 로고
    • The viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces
    • Helander A, Silvey KJ, Mantis NJ, Hutchings AB, Chandran K, Lucas WT, Nibert ML, Neutra MR (2003) The viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces. J Virol 77:7964-7977
    • (2003) J Virol , vol.77 , 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
  • 72
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
    • Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T, Tsukita S (2001) Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. J Cell Biol 154:491-497
    • (2001) J Cell Biol , vol.154 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 73
    • 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 σ3 protein: an approach for analyzing σ3 functions during virus entry. J Virol 73:2963-2973
    • (1999) J Virol , vol.73 , pp. 2963-2973
    • Jané-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
  • 74
    • 0036233299 scopus 로고    scopus 로고
    • Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma3
    • 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 sigma3. J Virol 76:5184-5197
    • (2002) J Virol , vol.76 , pp. 5184-5197
    • Jané-Valbuena, J.1    Breun, L.A.2    Schiff, L.A.3    Nibert, M.L.4
  • 75
    • 0022491811 scopus 로고
    • Genetic basis for altered pathogenesis of an immune-selected antigenic variant of reovirus type 3 Dearing
    • Kaye KM, Spriggs DR, Bassel-Duby R, Fields BN, Tyler KL (1986) Genetic basis for altered pathogenesis of an immune-selected antigenic variant of reovirus type 3 Dearing. J Virol 59:90-97
    • (1986) J Virol , vol.59 , pp. 90-97
    • Kaye, K.M.1    Spriggs, D.R.2    Bassel-Duby, R.3    Fields, B.N.4    Tyler, K.L.5
  • 76
    • 0030339827 scopus 로고    scopus 로고
    • Cellular proteases involved in the pathogenicity of human immunodeficiency and influenza viruses
    • Kido H, Towatari T, Niwa Y, Okumura Y, Beppu Y (1996) Cellular proteases involved in the pathogenicity of human immunodeficiency and influenza viruses. Adv Exp Med Biol 389:233-240
    • (1996) Adv Exp Med Biol , vol.389 , pp. 233-240
    • Kido, H.1    Towatari, T.2    Niwa, Y.3    Okumura, Y.4    Beppu, Y.5
  • 77
    • 0033617774 scopus 로고    scopus 로고
    • Cellular proteinases trigger the infectivity of the influenza A and Sendai viruses
    • Kido H, Murakami M, Oba K, Chen Y, Towatari T (1999) Cellular proteinases trigger the infectivity of the influenza A and Sendai viruses. Mol Cells 9:235-244
    • (1999) Mol Cells , vol.9 , pp. 235-244
    • Kido, H.1    Murakami, M.2    Oba, K.3    Chen, Y.4    Towatari, T.5
  • 79
    • 0024814219 scopus 로고
    • Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins
    • Kirschke H, Wiederanders B, Bromme D, Rinne A (1989) Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. Biochem J 264:467-473
    • (1989) Biochem J , vol.264 , pp. 467-473
    • Kirschke, H.1    Wiederanders, B.2    Bromme, D.3    Rinne, A.4
  • 81
    • 0032567111 scopus 로고    scopus 로고
    • No role for pepstatin-A-sensitive acidic proteinases in reovirus infections of L or MDCK cells
    • Kothandaraman S, Hebert MC, Raines RT, Nibert ML (1998) No role for pepstatin-A-sensitive acidic proteinases in reovirus infections of L or MDCK cells. Virology 251:264-272
    • (1998) Virology , vol.251 , pp. 264-272
    • Kothandaraman, S.1    Hebert, M.C.2    Raines, R.T.3    Nibert, M.L.4
  • 82
    • 0033823684 scopus 로고    scopus 로고
    • Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and do not prevent leukocyte influx into the meninges after viral or bacterial infection
    • Lechner F, Sahrbacher U, Suter T, Frei K, Brockhaus M, Koedel U, Fontana A (2000) Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and do not prevent leukocyte influx into the meninges after viral or bacterial infection. J Infect Dis 182:978-982
    • (2000) J Infect Dis , vol.182 , pp. 978-982
    • Lechner, F.1    Sahrbacher, U.2    Suter, T.3    Frei, K.4    Brockhaus, M.5    Koedel, U.6    Fontana, A.7
  • 83
    • 0019522275 scopus 로고
    • Protein σ1 is the reovirus cell attachment protein
    • Lee PW, Hayes EC, Joklik WK (1981) Protein σ1 is the reovirus cell attachment protein. Virology 108:156-163
    • (1981) Virology , vol.108 , pp. 156-163
    • Lee, P.W.1    Hayes, E.C.2    Joklik, W.K.3
  • 84
    • 0025955495 scopus 로고
    • Trimerization of the reovirus cell attachment protein (σ1) induces conformational changes in ?́1 necessary for its cell-binding function
    • Leone G, Duncan R, Lee PWK (1991) Trimerization of the reovirus cell attachment protein (σ1) induces conformational changes in ?́1 necessary for its cell-binding function. Virology 184:758-761
    • (1991) Virology , vol.184 , pp. 758-761
    • Leone, G.1    Duncan, R.2    Lee, P.W.K.3
  • 86
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, μ1, in a complex with is protector protein, σ3
    • Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC (2002) Structure of the reovirus membrane-penetration protein, μ1, in a complex with is protector protein, σ3. Cell 108:283-295
    • (2002) Cell , vol.108 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 88
    • 0026596861 scopus 로고
    • Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme
    • Mach L, Stuwe K, Hagen A, Ballaun C, Glossl J (1992) Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme. Biochem J 282:577-582
    • (1992) Biochem J , vol.282 , pp. 577-582
    • Mach, L.1    Stuwe, K.2    Hagen, A.3    Ballaun, C.4    Glossl, J.5
  • 89
    • 0036935194 scopus 로고    scopus 로고
    • Type 3 reovirus neuroinvasion after intramuscular inoculation: Direct invasion of nerve terminals and age-dependent pathogenesis
    • 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
    • (2002) Virology , vol.303 , pp. 222-231
    • Mann, M.A.1    Knipe, D.M.2    Fischbach, G.D.3    Fields, B.N.4
  • 90
    • 0023020013 scopus 로고
    • Ammonium inhibits processing and cytotoxicity of reovirus, a nonenveloped virus
    • Maratos-Flier E, Goodman MJ, Murray AH, Kahn CR (1986) Ammonium inhibits processing and cytotoxicity of reovirus, a nonenveloped virus. J Clin Invest 78:617-625
    • (1986) J Clin Invest , vol.78 , pp. 617-625
    • Maratos-Flier, E.1    Goodman, M.J.2    Murray, A.H.3    Kahn, C.R.4
  • 91
    • 0029655850 scopus 로고    scopus 로고
    • The entry of reovirus into L cells is dependent on vacuolar proton-ATPase activity
    • Martinez CG, Guinea R, Benavente J, Carrasco L (1996) The entry of reovirus into L cells is dependent on vacuolar proton-ATPase activity. J Virol 70:576-579
    • (1996) J Virol , vol.70 , pp. 576-579
    • Martinez, C.G.1    Guinea, R.2    Benavente, J.3    Carrasco, L.4
  • 93
    • 0024470378 scopus 로고
    • Interaction of lysosomal cysteine proteinases with alpha-2-macroglobulin: Conclusive evidence for the endopeptidase activities of cathepsins B and H
    • Mason RW (1989) Interaction of lysosomal cysteine proteinases with alpha-2-macroglobulin: conclusive evidence for the endopeptidase activities of cathepsins B and H. Arch Biochem Biophys 273:367-374
    • (1989) Arch Biochem Biophys , vol.273 , pp. 367-374
    • Mason, R.W.1
  • 94
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin KS, Reggio HV, Helenius A, Simons K (1982) Infectious entry pathway of influenza virus in a canine kidney cell line. J Cell Biol 91:601-613
    • (1982) J Cell Biol , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.V.2    Helenius, A.3    Simons, K.4
  • 95
    • 0020352681 scopus 로고
    • Weak bases and ionophores rapidly and reversibly raise the pH in endocytic vesicles in cultured mouse fibroblasts
    • Maxfield FR (1982) Weak bases and ionophores rapidly and reversibly raise the pH in endocytic vesicles in cultured mouse fibroblasts. J Cell Biol 95:676-681
    • (1982) J Cell Biol , vol.95 , pp. 676-681
    • Maxfield, F.R.1
  • 96
    • 0018083729 scopus 로고
    • The nature of the polypeptide encoded by each of the ten double-stranded RNA segments of reovirus type 3
    • McCrae MA, Joklik WK (1978) The nature of the polypeptide encoded by each of the ten double-stranded RNA segments of reovirus type 3. Virology 89:578-593
    • (1978) Virology , vol.89 , pp. 578-593
    • McCrae, M.A.1    Joklik, W.K.2
  • 97
    • 0026072563 scopus 로고
    • The 3-dimensional structure of reovirus obtained by cryoelectron microscopy
    • Metcalf P, Cyrklaff M, Adrian M (1991) The 3-dimensional structure of reovirus obtained by cryoelectron microscopy. EMBO J 10:3129-3136
    • (1991) EMBO J , vol.10 , pp. 3129-3136
    • Metcalf, P.1    Cyrklaff, M.2    Adrian, M.3
  • 98
    • 0028572551 scopus 로고
    • Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant chain
    • Mizuochi T, Yee ST, Kasai M, Kakiuchi T, Muno D, Kominami E (1994) Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant chain. Immunol Let 43:189-193
    • (1994) Immunol Let , vol.43 , pp. 189-193
    • Mizuochi, T.1    Yee, S.T.2    Kasai, M.3    Kakiuchi, T.4    Muno, D.5    Kominami, E.6
  • 99
    • 0025898677 scopus 로고
    • Direct spread of reovirus from the intestinal lumen to the central nervous system through vagal autonomic nerve fibers
    • Morrison LA, Sidman RL, Fields BN (1991) Direct spread of reovirus from the intestinal lumen to the central nervous system through vagal autonomic nerve fibers. Proc Natl Acad Sci U S A 88:3852-3856
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3852-3856
    • Morrison, L.A.1    Sidman, R.L.2    Fields, B.N.3
  • 100
    • 0018077111 scopus 로고
    • Genetics of reovirus: Identification of the dsRNA 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 μ and σ size classes. Virology 89:594-604
    • (1978) Virology , vol.89 , pp. 594-604
    • Mustoe, T.A.1    Ramig, R.F.2    Sharpe, A.H.3    Fields, B.N.4
  • 102
    • 0034990083 scopus 로고    scopus 로고
    • A monoclonal antibody specific for reovirus outer-capsid protein σ3 inhibits σ1-mediated hemagglutination by steric hindrance
    • Nason E, Wetzel J, Mukherjee S, Barton E, Prasad B, Dermody T (2001) A monoclonal antibody specific for reovirus outer-capsid protein σ3 inhibits σ1-mediated hemagglutination by steric hindrance. J Virol 75:6625-6634
    • (2001) J Virol , vol.75 , pp. 6625-6634
    • Nason, E.1    Wetzel, J.2    Mukherjee, S.3    Barton, E.4    Prasad, B.5    Dermody, T.6
  • 103
    • 0026733619 scopus 로고
    • A carboxy-terminal fragment of protein μ1/μ1C 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 μ1/μ1C 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
  • 104
    • 0001123624 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • Knipe DM, Howley PM eds, 4th edn. Lippincott Williams Wilkins, Philadelphia, pp
    • Nibert ML, Schiff LA (2001) Reoviruses and their replication. In: Knipe DM, Howley PM (eds) Fields virology, 4th edn. Lippincott Williams Wilkins, Philadelphia, pp 1679-1728
    • (2001) Fields virology , pp. 1679-1728
    • Nibert, M.L.1    Schiff, L.A.2
  • 105
    • 0025936096 scopus 로고
    • Mechanisms of viral pathogenesis: Distinct forms of reoviruses and their roles during replication in cells and host
    • Nibert ML, Furlong DB, Fields BN (1991) Mechanisms of viral pathogenesis: distinct forms of reoviruses and their roles during replication in cells and host. J Clin Invest 88:727-734
    • (1991) J Clin Invest , vol.88 , pp. 727-734
    • Nibert, M.L.1    Furlong, D.B.2    Fields, B.N.3
  • 106
    • 0026088718 scopus 로고
    • Mammalian reoviruses contain a myristoylated structural protein
    • Nibert ML, Schiff LA, Fields BN (1991) Mammalian reoviruses contain a myristoylated structural protein. J Virol 65:1960-1967
    • (1991) J Virol , vol.65 , pp. 1960-1967
    • Nibert, M.L.1    Schiff, L.A.2    Fields, B.N.3
  • 107
    • 0029058860 scopus 로고
    • Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved σ1 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 σ1 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
  • 108
    • 9644268149 scopus 로고    scopus 로고
    • Putative autocleavage of reovirus mu1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization
    • Nibert ML, Odegard AL, Agosto MA, Chandran K, Schiff LA (2005) Putative autocleavage of reovirus mu1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization. J Mol Biol 345:461-474
    • (2005) J Mol Biol , vol.345 , pp. 461-474
    • Nibert, M.L.1    Odegard, A.L.2    Agosto, M.A.3    Chandran, K.4    Schiff, L.A.5
  • 109
    • 0031054645 scopus 로고    scopus 로고
    • Reovirus infection and tissue injury in the mouse central nervous system are associated with apoptosis
    • Oberhaus SM, Smith RL, Clayton GH, Dermody TS, Tyler KL (1997) Reovirus infection and tissue injury in the mouse central nervous system are associated with apoptosis. J Virol 71:2100-2106
    • (1997) J Virol , vol.71 , pp. 2100-2106
    • Oberhaus, S.M.1    Smith, R.L.2    Clayton, G.H.3    Dermody, T.S.4    Tyler, K.L.5
  • 110
    • 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
    • Odegard AL, Chandran K, Zhang X, Parker JS, Baker TS, Nibert ML (2004) Putative autocleavage of outer capsid protein μ1, allowing release of myristoylated peptide μ1N during particle uncoating, is critical for cell entry by reovirus. J Virol 78:8732-8745
    • (2004) J Virol , vol.78 , pp. 8732-8745
    • Odegard, A.L.1    Chandran, K.2    Zhang, X.3    Parker, J.S.4    Baker, T.S.5    Nibert, M.L.6
  • 111
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B (1978) Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci U S A 75:3327-3331
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 112
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution
    • Olland AM, Jané-Valbuena J, Schiff LA, Nibert ML, Harrison SC (2001) Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution. EMBO J 20:979-989
    • (2001) EMBO J , vol.20 , pp. 979-989
    • Olland, A.M.1    Jané-Valbuena, J.2    Schiff, L.A.3    Nibert, M.L.4    Harrison, S.C.5
  • 113
    • 0036008013 scopus 로고    scopus 로고
    • JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes
    • Ostermann G, Weber KS, Zernecke A, Schroder A, Weber C (2002) JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes. Nat Immunol 3:151-158
    • (2002) Nat Immunol , vol.3 , pp. 151-158
    • Ostermann, G.1    Weber, K.S.2    Zernecke, A.3    Schroder, A.4    Weber, C.5
  • 114
    • 0033565947 scopus 로고    scopus 로고
    • Cutting edge: Combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells
    • Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T, Okawa K, Iwamatsu A, Kita T (1999) Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells. J Immunol 163:553-557
    • (1999) J Immunol , vol.163 , pp. 553-557
    • Ozaki, H.1    Ishii, K.2    Horiuchi, H.3    Arai, H.4    Kawamoto, T.5    Okawa, K.6    Iwamatsu, A.7    Kita, T.8
  • 115
    • 0023613970 scopus 로고
    • Glycophorin is the reovirus receptor on human erythrocytes
    • Paul RW, Lee PWK (1987) Glycophorin is the reovirus receptor on human erythrocytes. Virology 159:94-101
    • (1987) Virology , vol.159 , pp. 94-101
    • Paul, R.W.1    Lee, P.W.K.2
  • 116
    • 0024429657 scopus 로고
    • The σ-anomeric form of sialic acid is the minimal receptor determinant recognized by reovirus
    • Paul RW, Choi AH, Lee PWK (1989) The σ-anomeric form of sialic acid is the minimal receptor determinant recognized by reovirus. Virology 172:382-385
    • (1989) Virology , vol.172 , pp. 382-385
    • Paul, R.W.1    Choi, A.H.2    Lee, P.W.K.3
  • 120
    • 0000269102 scopus 로고
    • Serologic grouping of reovirus by hemagglutination- inhibition
    • Rosen L (1960) Serologic grouping of reovirus by hemagglutination- inhibition. Am J Hyg 71:242-249
    • (1960) Am J Hyg , vol.71 , pp. 242-249
    • Rosen, L.1
  • 121
    • 0026664252 scopus 로고
    • Rat procathepsin B. Proteolytic processing to the mature form in vitro
    • Rowan AD, Mason P, Mach L, Mort JS (1992) Rat procathepsin B. Proteolytic processing to the mature form in vitro. J Biol Chem 267:15993-15999
    • (1992) J Biol Chem , vol.267 , pp. 15993-15999
    • Rowan, A.D.1    Mason, P.2    Mach, L.3    Mort, J.S.4
  • 122
    • 0026859502 scopus 로고
    • Receptor utilization by reovirus type 3: Distinct binding sites on thymoma and fibroblast cell lines result in differential compartmentalization of virions
    • Rubin DH, Weiner DB, Dworkin C, Greene MI, Maul GG, Williams WV (1992) Receptor utilization by reovirus type 3: distinct binding sites on thymoma and fibroblast cell lines result in differential compartmentalization of virions. Microb Pathog 12:351-365
    • (1992) Microb Pathog , vol.12 , pp. 351-365
    • Rubin, D.H.1    Weiner, D.B.2    Dworkin, C.3    Greene, M.I.4    Maul, G.G.5    Williams, W.V.6
  • 123
    • 0027082360 scopus 로고
    • Binding of type 3 reovirus by a domain of the σ1 protein important for hemagglutination leads to infection ofmurine 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 σ1 protein important for hemagglutination leads to infection ofmurine erythroleukemia cells. J Clin Invest 90:2536-2542
    • (1992) J Clin Invest , vol.90 , 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
  • 124
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust MJ, Lakadamyali M, Zhang F, Zhuang X (2004) Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat Struct Mol Biol 11:567-573
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 125
    • 0029098591 scopus 로고
    • Microglial cathepsin B: An immunological examination of cellular and secreted species
    • Ryan RE, Sloane BF, Sameni M, Wood PL (1995) Microglial cathepsin B: an immunological examination of cellular and secreted species. J Neurochem 65:1035-1045
    • (1995) J Neurochem , vol.65 , pp. 1035-1045
    • Ryan, R.E.1    Sloane, B.F.2    Sameni, M.3    Wood, P.L.4
  • 126
    • 0000439681 scopus 로고
    • Reoviruses: A new group of respiratory and enteric viruses formerly classified as ECHO type 10 is described
    • Sabin AB (1959) Reoviruses: a new group of respiratory and enteric viruses formerly classified as ECHO type 10 is described. Science 130:1387-1389
    • (1959) Science , vol.130 , pp. 1387-1389
    • Sabin, A.B.1
  • 127
    • 0006978350 scopus 로고
    • Quantitative aspects of the spontaneous elution of influenza virus from red cells
    • Sagik B, Puck T, Levine S (1954) Quantitative aspects of the spontaneous elution of influenza virus from red cells. J Exp Med 99:251-260
    • (1954) J Exp Med , vol.99 , pp. 251-260
    • Sagik, B.1    Puck, T.2    Levine, S.3
  • 128
    • 0025223273 scopus 로고
    • Inhibitor studies indicate that active cathepsin L is probably essential to its own processing in cultured fibroblasts
    • Salminen A, Gottesman MM (1990) Inhibitor studies indicate that active cathepsin L is probably essential to its own processing in cultured fibroblasts. Biochem J 272:39-44
    • (1990) Biochem J , vol.272 , pp. 39-44
    • Salminen, A.1    Gottesman, M.M.2
  • 129
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski SB, Whittaker GR (2002) Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J Virol 76:10455-10464
    • (2002) J Virol , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 130
    • 0014627613 scopus 로고
    • Polypeptide components of virions, top component and cores of reovirus type 3
    • Smith RE, Zweerink HJ, Joklik WK (1969) Polypeptide components of virions, top component and cores of reovirus type 3. Virology 39:791-810
    • (1969) Virology , vol.39 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 132
    • 0036774827 scopus 로고    scopus 로고
    • Viral interactions with receptors in cell junctions and effects on junctional stability
    • Spear PG (2002) Viral interactions with receptors in cell junctions and effects on junctional stability. Dev Cell 3:462-464
    • (2002) Dev Cell , vol.3 , pp. 462-464
    • Spear, P.G.1
  • 133
    • 0020067849 scopus 로고
    • Attenuated reovirus type 3 strains generated by selection of haemagglutinin antigenic variants
    • Spriggs DR, Fields BN (1982) Attenuated reovirus type 3 strains generated by selection of haemagglutinin antigenic variants. Nature 297:68-70
    • (1982) Nature , vol.297 , pp. 68-70
    • Spriggs, D.R.1    Fields, B.N.2
  • 134
    • 0020568283 scopus 로고
    • Hemagglutinin variants of reovirus type 3 have altered central nervous system tropism
    • Spriggs DR, Bronson RT, Fields BN (1983) Hemagglutinin variants of reovirus type 3 have altered central nervous system tropism. Science 220:505-507
    • (1983) Science , vol.220 , pp. 505-507
    • Spriggs, D.R.1    Bronson, R.T.2    Fields, B.N.3
  • 135
    • 0037341386 scopus 로고    scopus 로고
    • Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins
    • 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
    • (2003) Rev Med Virol , vol.13 , pp. 123-132
    • Stehle, T.1    Dermody, T.S.2
  • 136
    • 3042772542 scopus 로고    scopus 로고
    • Structural similarities in the cellular receptors used by adenovirus and reovirus
    • Stehle T, Dermody TS (2004) Structural similarities in the cellular receptors used by adenovirus and reovirus. Viral Immunol 17:129-143
    • (2004) Viral Immunol , vol.17 , pp. 129-143
    • Stehle, T.1    Dermody, T.S.2
  • 137
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny K, Allison SL, Marchler-Bauer A, Kunz C, Heinz FX (1996) Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J Virol 70:8142-8147
    • (1996) J Virol , vol.70 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 138
    • 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
  • 139
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential stepin 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 stepin the viral infectious cycle. J Virol 61:2351-2361
    • (1987) J Virol , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.L.2    Furlong, D.B.3    Fields, B.N.4
  • 140
    • 0033519211 scopus 로고    scopus 로고
    • Nectin/PRR: An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein
    • Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (1999) Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. J Cell Biol 145:539-549
    • (1999) J Cell Biol , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3    Mandai, K.4    Satoh, K.5    Satoh, A.6    Nishioka, H.7    Aoki, J.8    Nomoto, A.9    Mizoguchi, A.10    Takai, Y.11
  • 141
    • 0020065786 scopus 로고
    • Viral receptors on isolated murine and human ependymal cells
    • Tardieu M, Weiner HL (1982) Viral receptors on isolated murine and human ependymal cells. Science 215:419-421
    • (1982) Science , vol.215 , pp. 419-421
    • Tardieu, M.1    Weiner, H.L.2
  • 142
    • 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
    • (1983) Ann Neurol , vol.13 , pp. 602-607
    • Tardieu, M.1    Powers, M.L.2    Weiner, H.L.3
  • 143
    • 0027429139 scopus 로고
    • Ion channels induced in lipid bilayers by subvirion particles of the nonenveloped mammalian reoviruses
    • Tosteson MT, Nibert ML, Fields BN (1993) Ion channels induced in lipid bilayers by subvirion particles of the nonenveloped mammalian reoviruses. Proc Natl Acad Sci U S A 90:10549-10552
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10549-10552
    • Tosteson, M.T.1    Nibert, M.L.2    Fields, B.N.3
  • 144
    • 0032842426 scopus 로고    scopus 로고
    • Structural and signalling molecules come together at tight junctions
    • Tsukita S, Furuse M, Itoh M (1999) Structural and signalling molecules come together at tight junctions. Curr Opin Cell Biol 11:628-633
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 628-633
    • Tsukita, S.1    Furuse, M.2    Itoh, M.3
  • 145
    • 0026503712 scopus 로고
    • Site-directed mutagenesis of the C-terminal portion of reovirus protein σ1: Evidence for a conformation-dependent receptor binding domain
    • Turner DL, Duncan R, Lee PW (1992) Site-directed mutagenesis of the C-terminal portion of reovirus protein σ1: evidence for a conformation-dependent receptor binding domain. Virology 186:219-227
    • (1992) Virology , vol.186 , pp. 219-227
    • Turner, D.L.1    Duncan, R.2    Lee, P.W.3
  • 146
    • 0001578626 scopus 로고    scopus 로고
    • Mammalian reoviruses
    • Knipe DM, Howley PM eds, 4th edn. Lippincott Williams Wilkins, Philadelphia, pp
    • Tyler KL (2001) Mammalian reoviruses. In: Knipe DM, Howley PM (eds) Fields virology, 4th edn. Lippincott Williams Wilkins, Philadelphia, pp 1729-1945
    • (2001) Fields virology , pp. 1729-1945
    • Tyler, K.L.1
  • 147
    • 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
    • (1986) Science , vol.233 , pp. 770-774
    • Tyler, K.L.1    McPhee, D.A.2    Fields, B.N.3
  • 149
    • 0032489347 scopus 로고    scopus 로고
    • Cloning and characterization of MUPP1, a novel PDZ domain protein
    • Ullmer C, Schmuck K, Figge A, Lubbert H (1998) Cloning and characterization of MUPP1, a novel PDZ domain protein. FEBS Lett 424:63-68
    • (1998) FEBS Lett , vol.424 , pp. 63-68
    • Ullmer, C.1    Schmuck, K.2    Figge, A.3    Lubbert, H.4
  • 150
    • 0033613385 scopus 로고    scopus 로고
    • A triple β-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 β-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
  • 151
    • 0008695025 scopus 로고    scopus 로고
    • Reovirus
    • Nathanson N ed, Lippincott-Raven, New York, pp
    • Virgin HW, Tyler KL, Dermody TS (1997) Reovirus. In: Nathanson N (ed) Viral pathogenesis. Lippincott-Raven, New York, pp 669-699
    • (1997) Viral pathogenesis , pp. 669-699
    • Virgin, H.W.1    Tyler, K.L.2    Dermody, T.S.3
  • 152
    • 0032551272 scopus 로고    scopus 로고
    • A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection bymutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus
    • Warner MS, Geraghty RJ, Martinez WM, Montgomery RI, Whitbeck JC, Xu R, Eisenberg RJ, Cohen GH, Spear PG (1998) A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection bymutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus. Virology 246:179-189
    • (1998) Virology , vol.246 , pp. 179-189
    • Warner, M.S.1    Geraghty, R.J.2    Martinez, W.M.3    Montgomery, R.I.4    Whitbeck, J.C.5    Xu, R.6    Eisenberg, R.J.7    Cohen, G.H.8    Spear, P.G.9
  • 154
    • 0018893801 scopus 로고
    • Interaction of reovirus with cell surface receptors. I. Murine and human lymphocytes have a receptor for the hemagglutinin of reovirus type 3
    • Weiner HL, Ault KA, Fields BN (1980) Interaction of reovirus with cell surface receptors. I. Murine and human lymphocytes have a receptor for the hemagglutinin of reovirus type 3. J Immunol 124:2143-2148
    • (1980) J Immunol , vol.124 , pp. 2143-2148
    • Weiner, H.L.1    Ault, K.A.2    Fields, B.N.3
  • 155
    • 0018818532 scopus 로고
    • Absolute linkage of virulence and central nervous system 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
    • (1980) J Infect Dis , vol.141 , pp. 609-616
    • Weiner, H.L.1    Powers, M.L.2    Fields, B.N.3
  • 156
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W, Brown JH, Cusack S, Paulson JC, Skehel JJ, Wiley DC (1988) Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 157
    • 0031026434 scopus 로고    scopus 로고
    • Reovirus variants selected during persistent infections of L cells contain mutations in the viral 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
    • (1997) J Virol , vol.71 , 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
  • 158
    • 0033233421 scopus 로고    scopus 로고
    • Identification and characterisation of human junctional adhesion molecule (JAM)
    • Williams LA, Martin-Padura I, Dejana E, Hogg N, Simmons DL (1999) Identification and characterisation of human junctional adhesion molecule (JAM). Mol Immunol 36:1175-1188
    • (1999) Mol Immunol , vol.36 , pp. 1175-1188
    • Williams, L.A.1    Martin-Padura, I.2    Dejana, E.3    Hogg, N.4    Simmons, D.L.5
  • 159
    • 0029793807 scopus 로고    scopus 로고
    • Persistent reovirus infections of L cells select mutations in viral attachment protein σ1 that alter oligomer stability
    • Wilson GJ, Wetzel JD, Puryear W, Bassel-Duby R, Dermody TS (1996) Persistent reovirus infections of L cells select mutations in viral attachment protein σ1 that alter oligomer stability. J Virol 70:6598-6606
    • (1996) J Virol , vol.70 , pp. 6598-6606
    • Wilson, G.J.1    Wetzel, J.D.2    Puryear, W.3    Bassel-Duby, R.4    Dermody, T.S.5
  • 160
    • 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 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 σ3 confers enhanced kinetics of σ3 proteolysis, resistance to inhibitors of viral disassembly, and alterations in σ3 structure. J Virol 76:9832-9843
    • (2002) J Virol , vol.76 , 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
  • 161
    • 0014966129 scopus 로고
    • Interaction of bacteriophage T4 tail fiber components with a lipopolysaccharide fraction from Escherichia coli
    • Wilson JH, Luftig RB, Wood WB (1970) Interaction of bacteriophage T4 tail fiber components with a lipopolysaccharide fraction from Escherichia coli. J Mol Biol 51:423-434
    • (1970) J Mol Biol , vol.51 , pp. 423-434
    • Wilson, J.H.1    Luftig, R.B.2    Wood, W.B.3
  • 163
    • 0036632634 scopus 로고    scopus 로고
    • Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry
    • Yoon M, Spear PG (2002) Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry. J Virol 76:7203-7208
    • (2002) J Virol , vol.76 , pp. 7203-7208
    • Yoon, M.1    Spear, P.G.2
  • 164
    • 0034722381 scopus 로고    scopus 로고
    • Tight junction, a platform for trafficking and signaling protein complexes
    • Zahraoui A, Louvard D, Galli T (2000) Tight junction, a platform for trafficking and signaling protein complexes. J Cell Biol 151:F31-F36
    • (2000) J Cell Biol , vol.151
    • Zahraoui, A.1    Louvard, D.2    Galli, T.3


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