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Volumn 91, Issue 4, 2017, Pages

Structural insights into reovirus σ1 interactions with two neutralizing antibodies

Author keywords

Crystal structure; Fab fragments; Flow cytometry; Immune escape; Mammalian reoviruses; Monoclonal antibodies; Quaternary binding epitope; Receptor binding; Surface plasmon resonance; Virus neutralization

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; JUNCTIONAL ADHESION MOLECULE A; NEUTRALIZING ANTIBODY; INFLUENZA VIRUS HEMAGGLUTININ; PROTEIN BINDING; VIRAL PROTEIN; VIRUS ANTIBODY;

EID: 85011961621     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01621-16     Document Type: Article
Times cited : (25)

References (64)
  • 1
    • 33344479421 scopus 로고    scopus 로고
    • Antiviral antibody responses: the two extremes of a wide spectrum
    • Hangartner L, Zinkernagel RM, Hengartner H. 2006. Antiviral antibody responses: the two extremes of a wide spectrum. Nat Rev Immunol 6:231-243. https://doi.org/10.1038/nri1783.
    • (2006) Nat Rev Immunol , vol.6 , pp. 231-243
    • Hangartner, L.1    Zinkernagel, R.M.2    Hengartner, H.3
  • 2
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti D, Lanzavecchia A. 2013. Broadly neutralizing antiviral antibodies. Annu Rev Immunol 31:705-742. https://doi.org/10.1146/annurev-immunol-032712-095916.
    • (2013) Annu Rev Immunol , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 3
    • 0033053331 scopus 로고    scopus 로고
    • A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site
    • Fleury D, Barrere B, Bizebard T, Daniels RS, Skehel JJ, Knossow M. 1999. A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site. Nat Struct Biol 6:530-534. https://doi.org/10.1038/9299.
    • (1999) Nat Struct Biol , vol.6 , pp. 530-534
    • Fleury, D.1    Barrere, B.2    Bizebard, T.3    Daniels, R.S.4    Skehel, J.J.5    Knossow, M.6
  • 6
    • 0027242112 scopus 로고
    • Attachment of neutralizing antibodies stabilizes the capsid of poliovirus against uncoating
    • Wetz K. 1993. Attachment of neutralizing antibodies stabilizes the capsid of poliovirus against uncoating. Virology 192:465-472. https://doi.org/10.1006/viro.1993.1062.
    • (1993) Virology , vol.192 , pp. 465-472
    • Wetz, K.1
  • 8
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus bivalently bound antibody complex-implications for viral neutralization and antibody flexibility
    • Smith TJ, Olson NH, Cheng RH, Chase ES, Baker TS. 1993. Structure of a human rhinovirus bivalently bound antibody complex-implications for viral neutralization and antibody flexibility. Proc Natl Acad Sci U S A 90:7015-7018. https://doi.org/10.1073/pnas.90.15.7015.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7015-7018
    • Smith, T.J.1    Olson, N.H.2    Cheng, R.H.3    Chase, E.S.4    Baker, T.S.5
  • 9
    • 79952073504 scopus 로고    scopus 로고
    • Complement and viral pathogenesis
    • Stoermer KA, Morrison TE. 2011. Complement and viral pathogenesis. Virology 411:362-373. https://doi.org/10.1016/j.virol.2010.12.045.
    • (2011) Virology , vol.411 , pp. 362-373
    • Stoermer, K.A.1    Morrison, T.E.2
  • 10
    • 84937504664 scopus 로고    scopus 로고
    • Complement in therapy and disease: regulating the complement system with antibody-based therapeutics
    • Melis JPM, Strumane K, Ruuls SR, Beurskens FJ, Schuurman J, Parren PWHI. 2015. Complement in therapy and disease: regulating the complement system with antibody-based therapeutics. Mol Immunol 67: 117-130. https://doi.org/10.1016/j.molimm.2015.01.028.
    • (2015) Mol Immunol , vol.67 , pp. 117-130
    • Melis, J.P.M.1    Strumane, K.2    Ruuls, S.R.3    Beurskens, F.J.4    Schuurman, J.5    Parren, P.W.H.I.6
  • 11
    • 84945265000 scopus 로고    scopus 로고
    • TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity
    • Foss S, Watkinson R, Sandlie I, James LC, Andersen JT. 2015. TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity. Immunol Rev 268:328-339. https://doi.org/10.1111/imr.12363.
    • (2015) Immunol Rev , vol.268 , pp. 328-339
    • Foss, S.1    Watkinson, R.2    Sandlie, I.3    James, L.C.4    Andersen, J.T.5
  • 12
    • 37549036732 scopus 로고    scopus 로고
    • Fc gamma receptors as regulators of immune responses
    • Nimmerjahn F, Ravetch JV. 2008. Fc gamma receptors as regulators of immune responses. Nat Rev Immunol 8:34-47. https://doi.org/10.1038/nri2206.
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 13
    • 0036719574 scopus 로고    scopus 로고
    • Antibodies, viruses and vaccines
    • Burton DR. 2002. Antibodies, viruses and vaccines. Nat Rev Immunol 2:706-713. https://doi.org/10.1038/nri891.
    • (2002) Nat Rev Immunol , vol.2 , pp. 706-713
    • Burton, D.R.1
  • 14
    • 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. https://doi.org/10.1006/viro.2002.1699.
    • (2002) Virology , vol.303 , pp. 222-231
    • Mann, M.A.1    Knipe, D.M.2    Fischbach, G.D.3    Fields, B.N.4
  • 15
    • 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. https://doi.org/10.1002/ana.410130604.
    • (1983) Ann Neurol , vol.13 , pp. 602-607
    • Tardieu, M.1    Powers, M.L.2    Weiner, H.L.3
  • 16
    • 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. https://doi.org/10.1126/science.3016895.
    • (1986) Science , vol.233 , pp. 770-774
    • Tyler, K.L.1    McPhee, D.A.2    Fields, B.N.3
  • 17
  • 18
    • 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 cell tropism of reoviruses to viral hemagglutinin. J Infect Dis 141:609-616. https://doi.org/10.1093/infdis/141.5.609.
    • (1980) J Infect Dis , vol.141 , pp. 609-616
    • Weiner, H.L.1    Powers, M.L.2    Fields, B.N.3
  • 19
    • 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. https://doi.org/10.1073/pnas.88.9.3852.
    • (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
  • 21
    • 0020665328 scopus 로고
    • The sigma 1 protein determines the extent of spread of reovirus from the gastrointestinal tract of mice
    • Kauffman RS, Wolf JL, Finberg R, Trier JS, Fields BN. 1983. The sigma 1 protein determines the extent of spread of reovirus from the gastrointestinal tract of mice. Virology 124:403-410. https://doi.org/10.1016/0042-6822(83)90356-2.
    • (1983) Virology , vol.124 , pp. 403-410
    • Kauffman, R.S.1    Wolf, J.L.2    Finberg, R.3    Trier, J.S.4    Fields, B.N.5
  • 22
    • 0029655895 scopus 로고    scopus 로고
    • Reovirus infection in rat lungs as a model to study the pathogenesis of viral pneumonia
    • Morin MJ, Warner A, Fields BN. 1996. Reovirus infection in rat lungs as a model to study the pathogenesis of viral pneumonia. J Virol 70:541-548.
    • (1996) J Virol , vol.70 , pp. 541-548
    • Morin, M.J.1    Warner, A.2    Fields, B.N.3
  • 23
    • 80052334710 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein sigma 1 in complex with sialylated oligosaccharides
    • Reiter DM, Frierson JM, Halvorson EE, Kobayashi T, Dermody TS, Stehle T. 2011. Crystal structure of reovirus attachment protein sigma 1 in complex with sialylated oligosaccharides. PLoS Pathog 7:e1002166. https://doi.org/10.1371/journal.ppat.1002166.
    • (2011) PLoS Pathog , vol.7
    • Reiter, D.M.1    Frierson, J.M.2    Halvorson, E.E.3    Kobayashi, T.4    Dermody, T.S.5    Stehle, T.6
  • 24
    • 0025299741 scopus 로고
    • Structure of the reovirus cell-attachment protein-a model for the domain organization of sigma 1
    • Nibert ML, Dermody TS, Fields BN. 1990. Structure of the reovirus cell-attachment protein-a model for the domain organization of sigma 1. J Virol 64:2976-2989.
    • (1990) J Virol , vol.64 , pp. 2976-2989
    • Nibert, M.L.1    Dermody, T.S.2    Fields, B.N.3
  • 25
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber
    • Chappell JD, Prota AE, Dermody TS, Stehle T. 2002. Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber. EMBO J 21:1-11. https://doi.org/10.1093/emboj/21.1.1.
    • (2002) EMBO J , vol.21 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 26
    • 58149263468 scopus 로고    scopus 로고
    • Structure of reovirus sigma 1 in complex with its receptor junctional adhesion molecule-A
    • Kirchner E, Guglielmi KM, Strauss HM, Dermody TS, Stehle T. 2008. Structure of reovirus sigma 1 in complex with its receptor junctional adhesion molecule-A. PLoS Pathog 4:e1000235. https://doi.org/10.1371/journal.ppat.1000235.
    • (2008) PLoS Pathog , vol.4
    • Kirchner, E.1    Guglielmi, K.M.2    Strauss, H.M.3    Dermody, T.S.4    Stehle, T.5
  • 28
    • 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. https://doi.org/10.1016/0042-6822(87)90192-9.
    • (1987) Virology , vol.161 , pp. 245-248
    • Gentsch, J.R.1    Pacitti, A.F.2
  • 29
    • 84929648716 scopus 로고    scopus 로고
    • Structure of serotype 1 reovirus attachment protein sigma 1 in complex with junctional adhesion molecule A reveals a conserved serotype-independent binding epitope
    • Stettner E, Dietrich MH, Reiss K, Dermody TS, Stehle T. 2015. Structure of serotype 1 reovirus attachment protein sigma 1 in complex with junctional adhesion molecule A reveals a conserved serotype-independent binding epitope. J Virol 89:6136-6140. https://doi.org/10.1128/JVI.00433-15.
    • (2015) J Virol , vol.89 , pp. 6136-6140
    • Stettner, E.1    Dietrich, M.H.2    Reiss, K.3    Dermody, T.S.4    Stehle, T.5
  • 30
    • 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
  • 31
    • 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 GJ, 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. https://doi.org/10.1083/jcb.122.5.1023.
    • (1993) J Cell Biol , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.J.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 32
    • 0017709320 scopus 로고
    • Neutralization of reovirus-gene responsible for neutralization antigen
    • Weiner HL, Fields BN. 1977. Neutralization of reovirus-gene responsible for neutralization antigen. J Exp Med 146:1305-1310. https://doi.org/10.1084/jem.146.5.1305.
    • (1977) J Exp Med , vol.146 , pp. 1305-1310
    • Weiner, H.L.1    Fields, B.N.2
  • 33
    • 0020026516 scopus 로고
    • Evidence for functional domains on the reovirus type 3 hemagglutinin
    • Burstin SJ, Spriggs DR, Fields BN. 1982. Evidence for functional domains on the reovirus type 3 hemagglutinin. Virology 117:146-155. https://doi.org/10.1016/0042-6822(82)90514-1.
    • (1982) Virology , vol.117 , pp. 146-155
    • Burstin, S.J.1    Spriggs, D.R.2    Fields, B.N.3
  • 34
    • 0027151892 scopus 로고
    • Protective anti-reovirus monoclonal antibodies and their effects on viral pathogenesis
    • Tyler KL, Mann MA, Fields BN, Virgin HW. 1993. Protective anti-reovirus monoclonal antibodies and their effects on viral pathogenesis. J Virol 67:3446-3453.
    • (1993) J Virol , vol.67 , pp. 3446-3453
    • Tyler, K.L.1    Mann, M.A.2    Fields, B.N.3    Virgin, H.W.4
  • 35
    • 4544262242 scopus 로고    scopus 로고
    • Protective immunoglobulin A and G antibodies bind to overlapping intersubunit epitopes in the head domain of type 1 reovirus adhesin sigma 1
    • Helander A, Miller CL, Myers KS, Neutra MR, Nibert ML. 2004. Protective immunoglobulin A and G antibodies bind to overlapping intersubunit epitopes in the head domain of type 1 reovirus adhesin sigma 1. J Virol 78:10695-10705. https://doi.org/10.1128/JVI.78.19.10695-10705.2004.
    • (2004) J Virol , vol.78 , pp. 10695-10705
    • Helander, A.1    Miller, C.L.2    Myers, K.S.3    Neutra, M.R.4    Nibert, M.L.5
  • 36
    • 0346688633 scopus 로고    scopus 로고
    • Secretory immunoglobulin A antibodies against the sigma 1 outer capsid protein of reovirus type 1 Lang prevent infection of mouse Peyer's patches
    • Hutchings AB, Helander A, Silvey KJ, Chandran K, Lucas WT, Nibert ML, Neutra MR. 2004. Secretory immunoglobulin A antibodies against the sigma 1 outer capsid protein of reovirus type 1 Lang prevent infection of mouse Peyer's patches. J Virol 78:947-957. https://doi.org/10.1128/JVI.78.2.947-957.2004.
    • (2004) J Virol , vol.78 , pp. 947-957
    • Hutchings, A.B.1    Helander, A.2    Silvey, K.J.3    Chandran, K.4    Lucas, W.T.5    Nibert, M.L.6    Neutra, M.R.7
  • 37
    • 0024202233 scopus 로고
    • Antibody protects against lethal infection with the neurally spreading reovirus type 3 (Dearing)
    • Virgin HW, Basselduby R, Fields BN, Tyler KL. 1988. Antibody protects against lethal infection with the neurally spreading reovirus type 3 (Dearing). J Virol 62:4594-4604.
    • (1988) J Virol , vol.62 , pp. 4594-4604
    • Virgin, H.W.1    Basselduby, R.2    Fields, B.N.3    Tyler, K.L.4
  • 38
    • 0024522588 scopus 로고
    • Characterization of a common high-affinity receptor for reovirus serotypes 1 and 3 on endothelial cells
    • Verdin EM, King GL, Maratosflier E. 1989. Characterization of a common high-affinity receptor for reovirus serotypes 1 and 3 on endothelial cells. J Virol 63:1318-1325.
    • (1989) J Virol , vol.63 , pp. 1318-1325
    • Verdin, E.M.1    King, G.L.2    Maratosflier, E.3
  • 39
    • 0025719821 scopus 로고
    • Monoclonal antibodies to reovirus reveal structure-function relationships between capsid proteins and genetics of susceptibility to antibody action
    • Virgin HW, Mann MA, Fields BN, Tyler KL. 1991. Monoclonal antibodies to reovirus reveal structure-function relationships between capsid proteins and genetics of susceptibility to antibody action. J Virol 65:6772-6781.
    • (1991) J Virol , vol.65 , pp. 6772-6781
    • Virgin, H.W.1    Mann, M.A.2    Fields, B.N.3    Tyler, K.L.4
  • 40
    • 0034990083 scopus 로고    scopus 로고
    • A monoclonal antibody specific for reovirus outer-capsid protein sigma3 inhibits sigma1-mediated hemagglutination by steric hindrance
    • Nason EL, Wetzel JD, Mukherjee SK, Barton ES, Prasad BVV, Dermody TS. 2001. A monoclonal antibody specific for reovirus outer-capsid protein sigma3 inhibits sigma1-mediated hemagglutination by steric hindrance. J Virol 75:6625-6634. https://doi.org/10.1128/JVI.75.14.6625-6634.2001.
    • (2001) J Virol , vol.75 , pp. 6625-6634
    • Nason, E.L.1    Wetzel, J.D.2    Mukherjee, S.K.3    Barton, E.S.4    Prasad, B.V.V.5    Dermody, T.S.6
  • 41
    • 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
  • 42
    • 0020067849 scopus 로고
    • Attenuated reovirus type 3 strains generated by selection of hemagglutinin antigenic variants
    • Spriggs DR, Fields BN. 1982. Attenuated reovirus type 3 strains generated by selection of hemagglutinin antigenic variants. Nature 297: 68-70. https://doi.org/10.1038/297068a0.
    • (1982) Nature , vol.297 , pp. 68-70
    • Spriggs, D.R.1    Fields, B.N.2
  • 43
    • 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. https://doi.org/10.1016/0042-6822(87)90351-5.
    • (1987) Virology , vol.159 , pp. 94-101
    • Paul, R.W.1    Lee, P.W.K.2
  • 44
    • 0035910468 scopus 로고    scopus 로고
    • Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening
    • Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS. 2001. Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200-2211. https://doi.org/10.1074/jbc.M004680200.
    • (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
  • 47
    • 0038082242 scopus 로고    scopus 로고
    • The viral sigma 1 protein and glycoconjugates containing alpha 2-3-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 sigma 1 protein and glycoconjugates containing alpha 2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces. J Virol 77:7964-7977. https://doi.org/10.1128/JVI.77.14.7964-7977.2003.
    • (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
  • 48
    • 84877620734 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza viruses
    • Laursen NS, Wilson IA. 2013. Broadly neutralizing antibodies against influenza viruses. Antiviral Res 98:476-483. https://doi.org/10.1016/j.antiviral.2013.03.021.
    • (2013) Antiviral Res , vol.98 , pp. 476-483
    • Laursen, N.S.1    Wilson, I.A.2
  • 49
    • 33645750724 scopus 로고    scopus 로고
    • Alternative intermolecular contacts underlie the rotavirus VP5* two-to three-fold rearrangement
    • Yoder JD, Dormitzer PR. 2006. Alternative intermolecular contacts underlie the rotavirus VP5* two-to three-fold rearrangement. EMBO J 25:1559-1568. https://doi.org/10.1038/sj.emboj.7601034.
    • (2006) EMBO J , vol.25 , pp. 1559-1568
    • Yoder, J.D.1    Dormitzer, P.R.2
  • 50
    • 20744437415 scopus 로고    scopus 로고
    • pH-induced conformational change of the rotavirus VP4 spike: implications for cell entry and antibody neutralization
    • Pesavento JB, Crawford SE, Roberts E, Estes MK, Prasad BVV. 2005. pH-induced conformational change of the rotavirus VP4 spike: implications for cell entry and antibody neutralization. J Virol 79:8572-8580. https://doi.org/10.1128/JVI.79.13.8572-8580.2005.
    • (2005) J Virol , vol.79 , pp. 8572-8580
    • Pesavento, J.B.1    Crawford, S.E.2    Roberts, E.3    Estes, M.K.4    Prasad, B.V.V.5
  • 52
    • 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. https://doi.org/10.1016/0042-6822(69)90017-8.
    • (1969) Virology , vol.39 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 53
    • 0030999547 scopus 로고    scopus 로고
    • Mutations in reovirus outer-capsid protein sigma 3 selected during persistent infections of L cells confer resistance to protease inhibitor E64
    • Baer GS, Dermody TS. 1997. Mutations in reovirus outer-capsid protein sigma 3 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
  • 54
    • 62449289261 scopus 로고    scopus 로고
    • Antibody affinity optimization using yeast cell surface display
    • Siegel RW. 2009. Antibody affinity optimization using yeast cell surface display. Methods Mol Biol 504:351-383. https://doi.org/10.1007/978-1-60327-569-9_20.
    • (2009) Methods Mol Biol , vol.504 , pp. 351-383
    • Siegel, R.W.1
  • 55
    • 34249659981 scopus 로고    scopus 로고
    • The reovirus sigma 1 aspartic acid sandwich-a trimerization motif poised for conformational change
    • Schelling P, Guglielmi KM, Kirchner E, Paetzold B, Dermody TS, Stehle T. 2007. The reovirus sigma 1 aspartic acid sandwich-a trimerization motif poised for conformational change. J Biol Chem 282:11582-11589. https://doi.org/10.1074/jbc.M610805200.
    • (2007) J Biol Chem , vol.282 , pp. 11582-11589
    • Schelling, P.1    Guglielmi, K.M.2    Kirchner, E.3    Paetzold, B.4    Dermody, T.S.5    Stehle, T.6
  • 58
    • 0028103275 scopus 로고
    • The CCP4 suite-programs for protein crystallography
    • Bailey S. 1994. The CCP4 suite-programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763. https://doi.org/10.1107/S0907444994003112.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
    • Bailey, S.1
  • 62
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60:2126-2132. https://doi.org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 63
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60:2256-2268. https://doi.org/10.1107/S0907444904026460.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 64
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K. 2012. Linking crystallographic model and data quality. Science 336:1030-1033. https://doi.org/10.1126/science.1218231.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


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