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Volumn 89, Issue 8, 2015, Pages 4143-4157

Nectin-like interactions between poliovirus and its receptor trigger conformational changes associated with cell entry

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; NECTIN; POLIOVIRUS RECEPTOR; PROTEIN VP1; PROTEIN VP2; PROTEIN VP4; UNCLASSIFIED DRUG; CAPSID PROTEIN; CELL ADHESION MOLECULE; NECTINS; VIRUS RECEPTOR;

EID: 84925428014     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03101-14     Document Type: Article
Times cited : (87)

References (82)
  • 1
    • 0000095156 scopus 로고    scopus 로고
    • Picornaviridae: the viruses and their replication
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Lippincott/The Williams & Wilkins Co, New York, NY
    • Racaniello VR. 2001. Picornaviridae: the viruses and their replication, p 685-722. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 4th ed, vol 1. Lippincott/The Williams & Wilkins Co, New York, NY.
    • (2001) Fields virology, 4th ed, vol 1 , pp. 685-722
    • Racaniello, V.R.1
  • 2
    • 29444452870 scopus 로고    scopus 로고
    • Bioinformatic characterization of the SynCAM family of immunoglobulin-like domain-containing adhesion molecules
    • Biederer T. 2006. Bioinformatic characterization of the SynCAM family of immunoglobulin-like domain-containing adhesion molecules. Genomics 87:139-150. http://dx.doi.org/10.1016/j.ygeno.2005.08.017.
    • (2006) Genomics , vol.87 , pp. 139-150
    • Biederer, T.1
  • 3
    • 0024519677 scopus 로고
    • Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn CL, Wimmer E, Racaniello VR. 1989. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 56:855-865. http://dx.doi.org/10.1016/0092-8674(89)90690-9.
    • (1989) Cell , vol.56 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 5
    • 0034725699 scopus 로고    scopus 로고
    • Two distinct binding affinities of poliovirus for its cellular receptor
    • McDermott BM, Rux AH, Eisenberg RJ, Cohen GH, Racaniello VR. 2000. Two distinct binding affinities of poliovirus for its cellular receptor. J Biol Chem 275:23089-23096. http://dx.doi.org/10.1074/jbc.M002146200.
    • (2000) J Biol Chem , vol.275 , pp. 23089-23096
    • McDermott, B.M.1    Rux, A.H.2    Eisenberg, R.J.3    Cohen, G.H.4    Racaniello, V.R.5
  • 6
    • 0000091801 scopus 로고
    • Early interactions between poliovirus and ERK cells. Some observations on the nature and significance of the rejected particles
    • Fenwick ML, Cooper PD. 1962. Early interactions between poliovirus and ERK cells. Some observations on the nature and significance of the rejected particles. Virology 18:212-223.
    • (1962) Virology , vol.18 , pp. 212-223
    • Fenwick, M.L.1    Cooper, P.D.2
  • 7
    • 0017685815 scopus 로고
    • Studies on the in vitro uncoating of poliovirus. II. Characteristics of the membrane-modified particle
    • De Sena J, Mandel B. 1977. Studies on the in vitro uncoating of poliovirus. II. Characteristics of the membrane-modified particle. Virology 78: 554-566.
    • (1977) Virology , vol.78 , pp. 554-566
    • De Sena, J.1    Mandel, B.2
  • 8
    • 0035039737 scopus 로고    scopus 로고
    • A kinetic analysis of the effect of poliovirus receptor on viral uncoating: the receptor as a catalyst
    • Tsang SK, McDermott BM, Racaniello VR, Hogle JM. 2001. A kinetic analysis of the effect of poliovirus receptor on viral uncoating: the receptor as a catalyst. J Virol 75:4984-4989. http://dx.doi.org/10.1128/JVI.75.11.4984-4989.2001.
    • (2001) J Virol , vol.75 , pp. 4984-4989
    • Tsang, S.K.1    McDermott, B.M.2    Racaniello, V.R.3    Hogle, J.M.4
  • 9
    • 0023198719 scopus 로고
    • Myristylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M, Newman JFE, Filman D, Hogle JM, Rowlands DJ, Brown F. 1987. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature 327:482-486. http://dx.doi.org/10.1038/327482a0.
    • (1987) Nature , vol.327 , pp. 482-486
    • Chow, M.1    Newman, J.F.E.2    Filman, D.3    Hogle, J.M.4    Rowlands, D.J.5    Brown, F.6
  • 10
    • 0025273268 scopus 로고
    • Cell-induced conformational change of poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks CE, Hogle JM. 1990. Cell-induced conformational change of poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J Virol 64:1934-1945.
    • (1990) J Virol , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 11
    • 33645997366 scopus 로고    scopus 로고
    • Characterization of early steps in the poliovirus infection process: receptor-decorated liposomes induce conversion of the virus to membrane-anchored entryintermediate particles
    • Tuthill TJ, Bubeck D, Rowlands DJ, Hogle JM. 2006. Characterization of early steps in the poliovirus infection process: receptor-decorated liposomes induce conversion of the virus to membrane-anchored entryintermediate particles. J Virol 80:172-180. http://dx.doi.org/10.1128/JVI.80.1.172-180.2006.
    • (2006) J Virol , vol.80 , pp. 172-180
    • Tuthill, T.J.1    Bubeck, D.2    Rowlands, D.J.3    Hogle, J.M.4
  • 12
    • 0344942597 scopus 로고    scopus 로고
    • Genome delivery and ion channel properties are altered in VP4 mutants of poliovirus
    • 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. http://dx.doi.org/10.1128/JVI.77.9.5266-5274.2003.
    • (2003) J Virol , vol.77 , pp. 5266-5274
    • Danthi, P.1    Tosteson, M.2    Li, Q.H.3    Chow, M.4
  • 13
    • 0031060329 scopus 로고    scopus 로고
    • Characterization of the ion channels formed by poliovirus in planar lipid membranes
    • Tosteson MT, Chow M. 1997. Characterization of the ion channels formed by poliovirus in planar lipid membranes. J Virol 71:507-511.
    • (1997) J Virol , vol.71 , pp. 507-511
    • Tosteson, M.T.1    Chow, M.2
  • 14
    • 2942657388 scopus 로고    scopus 로고
    • Poliovirus binding to its receptor in lipid bilayers results in particle-specific, temperaturesensitive channels
    • Tosteson MT, Wang H, Naumov A, Chow M. 2004. Poliovirus binding to its receptor in lipid bilayers results in particle-specific, temperaturesensitive channels. J Gen Virol 85:1581-1589. http://dx.doi.org/10.1099/vir.0.19745-0.
    • (2004) J Gen Virol , vol.85 , pp. 1581-1589
    • Tosteson, M.T.1    Wang, H.2    Naumov, A.3    Chow, M.4
  • 16
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 Å resolution
    • Hogle JM, Chow M, Filman DJ. 1985. Three-dimensional structure of poliovirus at 2.9 Å resolution. Science 229:1358-1365. http://dx.doi.org/10.1126/science.2994218.
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 17
    • 0024316730 scopus 로고
    • Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus
    • Filman DJ, Syed R, Chow M, Macadam AJ, Minor PD, Hogle JM. 1989. Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. EMBO J 8:1567-1579.
    • (1989) EMBO J , vol.8 , pp. 1567-1579
    • Filman, D.J.1    Syed, R.2    Chow, M.3    Macadam, A.J.4    Minor, P.D.5    Hogle, J.M.6
  • 19
    • 0024454604 scopus 로고
    • Structural analysis of antiviral agents that interact with the capsid of human rhinoviruses
    • Badger J, Minor I, Oliveira MA, Smith TJ, Rossmann MG. 1989. Structural analysis of antiviral agents that interact with the capsid of human rhinoviruses. Proteins 6:1-19. http://dx.doi.org/10.1002/prot.340060102.
    • (1989) Proteins , vol.6 , pp. 1-19
    • Badger, J.1    Minor, I.2    Oliveira, M.A.3    Smith, T.J.4    Rossmann, M.G.5
  • 21
    • 0006344586 scopus 로고
    • Binding of the antiviral drug WIN51711 to the Sabin strain of type 3 poliovirus: structural comparison with the drug binding in rhinovirus 14
    • Hiremath CN, Grant RA, Filman DJ, Hogle JM. 1995. Binding of the antiviral drug WIN51711 to the Sabin strain of type 3 poliovirus: structural comparison with the drug binding in rhinovirus 14. Acta Crystallogr D 51:473-489. http://dx.doi.org/10.1107/S090744499401084X.
    • (1995) Acta Crystallogr D , vol.51 , pp. 473-489
    • Hiremath, C.N.1    Grant, R.A.2    Filman, D.J.3    Hogle, J.M.4
  • 22
    • 0028506672 scopus 로고
    • Structures of poliovirus complexes with antiviral drugs: implications for viral stability and drug design
    • Grant RA, Hiremath C, Filman DJ, Syed R, Andries K, Hogle JM. 1994. Structures of poliovirus complexes with antiviral drugs: implications for viral stability and drug design. Curr Biol 4:784-797.
    • (1994) Curr Biol , vol.4 , pp. 784-797
    • Grant, R.A.1    Hiremath, C.2    Filman, D.J.3    Syed, R.4    Andries, K.5    Hogle, J.M.6
  • 23
    • 0034681288 scopus 로고    scopus 로고
    • Stabilization of poliovirus by capsid-binding antiviral drugs is due to entropic effects
    • Tsang SK, Danthi P, Chow M, Hogle JM. 2000. Stabilization of poliovirus by capsid-binding antiviral drugs is due to entropic effects. J Mol Biol 296:335-340. http://dx.doi.org/10.1006/jmbi.1999.3483.
    • (2000) J Mol Biol , vol.296 , pp. 335-340
    • Tsang, S.K.1    Danthi, P.2    Chow, M.3    Hogle, J.M.4
  • 24
    • 80054008048 scopus 로고    scopus 로고
    • Cell entry: a biochemical and structural perspective
    • Ehrenfeld E, Domingo E, Roos R (ed), ASM Press, Washington, DC
    • Levy H, Bostina M, Filman DJ, Hogle JM. 2010. Cell entry: a biochemical and structural perspective, p 87-107. In Ehrenfeld E, Domingo E, Roos R (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The picornaviruses , pp. 87-107
    • Levy, H.1    Bostina, M.2    Filman, D.J.3    Hogle, J.M.4
  • 26
    • 84857488318 scopus 로고    scopus 로고
    • Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid
    • Garriga D, Pickl-Herk A, Luque D, Wruss J, Caston JR, Blaas D, Verdaguer N. 2012. Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid. PLoS Pathog 8:e1002473. http://dx.doi.org/10.1371/journal.ppat.1002473.
    • (2012) PLoS Pathog , vol.8
    • Garriga, D.1    Pickl-Herk, A.2    Luque, D.3    Wruss, J.4    Caston, J.R.5    Blaas, D.6    Verdaguer, N.7
  • 29
    • 77950852687 scopus 로고    scopus 로고
    • Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy
    • Levy HC, Bostina M, Filman DJ, Hogle JM. 2010. Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy. J Virol 84:4426-4441. http://dx.doi.org/10.1128/JVI.02393-09.
    • (2010) J Virol , vol.84 , pp. 4426-4441
    • Levy, H.C.1    Bostina, M.2    Filman, D.J.3    Hogle, J.M.4
  • 30
    • 84892469578 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction shows poliovirus 135S particles poised for membrane interaction and RNA release
    • Butan C, Filman DJ, Hogle JM. 2014. Cryo-electron microscopy reconstruction shows poliovirus 135S particles poised for membrane interaction and RNA release. J Virol 88:1758-1770. http://dx.doi.org/10.1128/JVI.01949-13.
    • (2014) J Virol , vol.88 , pp. 1758-1770
    • Butan, C.1    Filman, D.J.2    Hogle, J.M.3
  • 31
    • 78650670078 scopus 로고    scopus 로고
    • Poliovirus RNA is released from the capsid near a twofold symmetry axis
    • Bostina M, Levy H, Filman DJ, Hogle JM. 2011. Poliovirus RNA is released from the capsid near a twofold symmetry axis. J Virol 85:776-783. http://dx.doi.org/10.1128/JVI.00531-10.
    • (2011) J Virol , vol.85 , pp. 776-783
    • Bostina, M.1    Levy, H.2    Filman, D.J.3    Hogle, J.M.4
  • 33
    • 22144468063 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex
    • Bubeck D, Filman DJ, Hogle JM. 2005. Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex. Nat Struct Mol Biol 12:615-618. http://dx.doi.org/10.1038/nsmb955.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 615-618
    • Bubeck, D.1    Filman, D.J.2    Hogle, J.M.3
  • 34
    • 35148838173 scopus 로고    scopus 로고
    • Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at 30A resolution
    • Bostina M, Bubeck D, Schwartz C, Nicastro D, Filman DJ, Hogle JM. 2007. Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at 30A resolution. J Struct Biol 160:200-210. http://dx.doi.org/10.1016/j.jsb.2007.08.009.
    • (2007) J Struct Biol , vol.160 , pp. 200-210
    • Bostina, M.1    Bubeck, D.2    Schwartz, C.3    Nicastro, D.4    Filman, D.J.5    Hogle, J.M.6
  • 40
    • 84859468877 scopus 로고    scopus 로고
    • Structure of TIGIT immunoreceptor bound to poliovirus receptor reveals a cell-cell adhesion and signaling mechanism that requires cis-trans receptor clustering
    • Stengel KF, Harden-Bowles K, Yu X, Rouge L, Yin J, Comps-Agrar L, Wiesmann C, Bazan JF, Eaton DL, Grogan JL. 2012. Structure of TIGIT immunoreceptor bound to poliovirus receptor reveals a cell-cell adhesion and signaling mechanism that requires cis-trans receptor clustering. Proc Natl Acad Sci U S A 109:5399-5404. http://dx.doi.org/10.1073/pnas.1120606109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5399-5404
    • Stengel, K.F.1    Harden-Bowles, K.2    Yu, X.3    Rouge, L.4    Yin, J.5    Comps-Agrar, L.6    Wiesmann, C.7    Bazan, J.F.8    Eaton, D.L.9    Grogan, J.L.10
  • 42
    • 0019750557 scopus 로고
    • Preparation and characterization of encephalomyocarditis (EMC) virus
    • Rueckert RR, Pallansch MA. 1981. Preparation and characterization of encephalomyocarditis (EMC) virus. Methods Enzymol 78:315-325.
    • (1981) Methods Enzymol , vol.78 , pp. 315-325
    • Rueckert, R.R.1    Pallansch, M.A.2
  • 44
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li X, Mooney P, Zheng S, Booth CR, Braunfeld MB, Gubbens S, Agard DA, Cheng Y. 2013. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat Methods 10:584-590. http://dx.doi.org/10.1038/nmeth.2472.
    • (2013) Nat Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 45
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, Ludtke SJ. 2007. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157:38-46. http://dx.doi.org/10.1016/j.jsb.2006.05.009.
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 46
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH. 2012. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-530. http://dx.doi.org/10.1016/j.jsb.2012.09.006.
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 47
    • 77958193837 scopus 로고    scopus 로고
    • GPU-enabled FREALIGN: accelerating single particle 3D reconstruction and refinement in Fourier space on graphics processors
    • Li X, Grigorieff N, Cheng Y. 2010. GPU-enabled FREALIGN: accelerating single particle 3D reconstruction and refinement in Fourier space on graphics processors. J Struct Biol 172:407-412. http://dx.doi.org/10.1016/j.jsb.2010.06.010.
    • (2010) J Struct Biol , vol.172 , pp. 407-412
    • Li, X.1    Grigorieff, N.2    Cheng, Y.3
  • 48
    • 51549084591 scopus 로고    scopus 로고
    • Sharpening high resolution information in single particle electron cryomicroscopy
    • Fernandez JJ, Luque D, Caston JR, Carrascosa JL. 2008. Sharpening high resolution information in single particle electron cryomicroscopy. J Struct Biol 164:170-175. http://dx.doi.org/10.1016/j.jsb.2008.05.010.
    • (2008) J Struct Biol , vol.164 , pp. 170-175
    • Fernandez, J.J.1    Luque, D.2    Caston, J.R.3    Carrascosa, J.L.4
  • 49
    • 0035937248 scopus 로고    scopus 로고
    • Ab initio phasing of highsymmetry macromolecular complexes: successful phasing of authentic poliovirus data to 3.0 Å resolution
    • Miller ST, Hogle JM, Filman DJ. 2001. Ab initio phasing of highsymmetry macromolecular complexes: successful phasing of authentic poliovirus data to 3.0 Å resolution. J Mol Biol 307:499-512. http://dx.doi.org/10.1006/jmbi.2001.4485.
    • (2001) J Mol Biol , vol.307 , pp. 499-512
    • Miller, S.T.1    Hogle, J.M.2    Filman, D.J.3
  • 51
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N, Peitsch MC. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723. http://dx.doi.org/10.1002/elps.1150181505.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 55
    • 0030501416 scopus 로고    scopus 로고
    • A pseudo-cell based approach to efficient crystallographic refinement of viruses
    • Jacobson DH, Hogle JM, Filman DJ. 1996. A pseudo-cell based approach to efficient crystallographic refinement of viruses. Acta Crystallogr D Biol Crystallogr 52:693-711. http://dx.doi.org/10.1107/S0907444996001060.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 693-711
    • Jacobson, D.H.1    Hogle, J.M.2    Filman, D.J.3
  • 56
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • Heymann JB, Belnap DM. 2007. Bsoft: image processing and molecular modeling for electron microscopy. J Struct Biol 157:3-18. http://dx.doi.org/10.1016/j.jsb.2006.06.006.
    • (2007) J Struct Biol , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 60
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • Bubeck D, Filman DJ, Cheng N, Steven AC, Hogle JM, Belnap DM. 2005. The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J Virol 79:7745-7755. http://dx.doi.org/10.1128/JVI.79.12.7745-7755.2005.
    • (2005) J Virol , vol.79 , pp. 7745-7755
    • Bubeck, D.1    Filman, D.J.2    Cheng, N.3    Steven, A.C.4    Hogle, J.M.5    Belnap, D.M.6
  • 61
    • 0028998673 scopus 로고
    • Poliovirus variants selected on mutant receptor-expressing cells identify capsid residues that expand receptor recognition
    • Colston EM, Racaniello VR. 1995. Poliovirus variants selected on mutant receptor-expressing cells identify capsid residues that expand receptor recognition. J Virol 69:4823-4829.
    • (1995) J Virol , vol.69 , pp. 4823-4829
    • Colston, E.M.1    Racaniello, V.R.2
  • 62
    • 0028575393 scopus 로고
    • Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor
    • Colston E, Racaniello VR. 1994. Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor. EMBO J 13:5855-5862.
    • (1994) EMBO J , vol.13 , pp. 5855-5862
    • Colston, E.1    Racaniello, V.R.2
  • 63
    • 0030780583 scopus 로고    scopus 로고
    • Allele-specific adaptation of poliovirus VP1 B-C loop variants to mutant cell receptors
    • Liao S, Racaniello V. 1997. Allele-specific adaptation of poliovirus VP1 B-C loop variants to mutant cell receptors. J Virol 71:9770-9777.
    • (1997) J Virol , vol.71 , pp. 9770-9777
    • Liao, S.1    Racaniello, V.2
  • 64
    • 0029563111 scopus 로고
    • Canyon rim residues, including antigenic determinants, modulate serotype-specific binding of polioviruses to mutants of the poliovirus receptor
    • Harber J, Bernhardt G, Lu HH, Sgro JY, Wimmer E. 1995. Canyon rim residues, including antigenic determinants, modulate serotype-specific binding of polioviruses to mutants of the poliovirus receptor. Virology 214:559-570. http://dx.doi.org/10.1006/viro.1995.0067.
    • (1995) Virology , vol.214 , pp. 559-570
    • Harber, J.1    Bernhardt, G.2    Lu, H.H.3    Sgro, J.Y.4    Wimmer, E.5
  • 65
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. 1976. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr A 32:922-923. http://dx.doi.org/10.1107/S05677 39476001873.
    • (1976) Acta Crystallogr A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 66
    • 34249948004 scopus 로고    scopus 로고
    • Pocket factors are unlikely to play a major role in the life cycle of human rhinovirus
    • Katpally U, Smith TJ. 2007. Pocket factors are unlikely to play a major role in the life cycle of human rhinovirus. J Virol 81:6307-6315. http://dx.doi.org/10.1128/JVI.00441-07.
    • (2007) J Virol , vol.81 , pp. 6307-6315
    • Katpally, U.1    Smith, T.J.2
  • 67
    • 0030845915 scopus 로고    scopus 로고
    • Structural studies of poliovirus mutants that overcome receptor defects
    • Wien MW, Curry S, Filman DJ, Hogle JM. 1997. Structural studies of poliovirus mutants that overcome receptor defects. Nat Struct Biol 4:666-674. http://dx.doi.org/10.1038/nsb0897-666.
    • (1997) Nat Struct Biol , vol.4 , pp. 666-674
    • Wien, M.W.1    Curry, S.2    Filman, D.J.3    Hogle, J.M.4
  • 72
    • 0001958671 scopus 로고
    • Escape mutant analysis of a drug-binding site can be used to map functions in the rhinovirus capsid
    • Laver WG, Air GM (ed), Academic Press Inc, San Diego, CA
    • Heinz BA, Shepard DA, Rueckert RR. 1990. Escape mutant analysis of a drug-binding site can be used to map functions in the rhinovirus capsid, p 173-186. In Laver WG, Air GM (ed), Use of X-ray crystallography in the desing of antiviral agents. Academic Press Inc, San Diego, CA.
    • (1990) Use of X-ray crystallography in the desing of antiviral agents , pp. 173-186
    • Heinz, B.A.1    Shepard, D.A.2    Rueckert, R.R.3
  • 73
    • 0027412243 scopus 로고
    • WIN 52035-2 inhibits both attachment and eclipse of human rhinovirus 14
    • Shepard DA, Heinz BA, Rueckert RR. 1993. WIN 52035-2 inhibits both attachment and eclipse of human rhinovirus 14. J Virol 67:2245-2254.
    • (1993) J Virol , vol.67 , pp. 2245-2254
    • Shepard, D.A.1    Heinz, B.A.2    Rueckert, R.R.3
  • 74
    • 0034070027 scopus 로고    scopus 로고
    • An antiviral compound that blocks structural transitions of poliovirus prevents receptor binding at low temperatures
    • Dove AW, Racaniello VR. 2000. An antiviral compound that blocks structural transitions of poliovirus prevents receptor binding at low temperatures. J Virol 74:3929-3931. http://dx.doi.org/10.1128/JVI.74.8.3929-3931.2000.
    • (2000) J Virol , vol.74 , pp. 3929-3931
    • Dove, A.W.1    Racaniello, V.R.2
  • 76
    • 0027410407 scopus 로고
    • WIN 51711-dependent mutants of poliovirus type 3: evidence that virions decay after release from cells unless drug is present
    • Mosser AG, Rueckert RR. 1993. WIN 51711-dependent mutants of poliovirus type 3: evidence that virions decay after release from cells unless drug is present. J Virol 67:1246-1254.
    • (1993) J Virol , vol.67 , pp. 1246-1254
    • Mosser, A.G.1    Rueckert, R.R.2
  • 77
    • 84875520601 scopus 로고    scopus 로고
    • RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors
    • Strauss M, Levy HC, Bostina M, Filman DJ, Hogle JM. 2013. RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors. J Virol 87:3903-3914. http://dx.doi.org/10.1128/JVI.03209-12.
    • (2013) J Virol , vol.87 , pp. 3903-3914
    • Strauss, M.1    Levy, H.C.2    Bostina, M.3    Filman, D.J.4    Hogle, J.M.5
  • 79
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Li Q, Yafal AG, Lee YM-H, Hogle J, Chow M. 1994. Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature. J Virol 68:3965-3970.
    • (1994) J Virol , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.-H.3    Hogle, J.4    Chow, M.5
  • 80
    • 84861325747 scopus 로고    scopus 로고
    • Structure of the Fab-labeled "breathing" state of native poliovirus
    • Lin J, Lee LY, Roivainen M, Filman DJ, Hogle JM, Belnap DM. 2012. Structure of the Fab-labeled "breathing" state of native poliovirus. J Virol 86:5959-5962. http://dx.doi.org/10.1128/JVI.05990-11.
    • (2012) J Virol , vol.86 , pp. 5959-5962
    • Lin, J.1    Lee, L.Y.2    Roivainen, M.3    Filman, D.J.4    Hogle, J.M.5    Belnap, D.M.6
  • 81
    • 84906968501 scopus 로고    scopus 로고
    • Kinetic models for receptor-catalyzed conversion of coxsackievirus b3 to A-particles
    • Carson SD. 2014. Kinetic models for receptor-catalyzed conversion of coxsackievirus b3 to A-particles. J Virol 88:11568-11575. http://dx.doi.org/10.1128/JVI.01790-14.
    • (2014) J Virol , vol.88 , pp. 11568-11575
    • Carson, S.D.1
  • 82
    • 84899057778 scopus 로고    scopus 로고
    • Kinetic and structural analysis of coxsackievirus B3 receptor interactions and formation of the A-particle
    • Organtini LJ, Makhov AM, Conway JF, Hafenstein S, Carson SD. 2014. Kinetic and structural analysis of coxsackievirus B3 receptor interactions and formation of the A-particle. J Virol 88:5755-5765. http://dx.doi.org/10.1128/JVI.00299-14.
    • (2014) J Virol , vol.88 , pp. 5755-5765
    • Organtini, L.J.1    Makhov, A.M.2    Conway, J.F.3    Hafenstein, S.4    Carson, S.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.