메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages 253-278

Parvoviruses: Structure and infection

Author keywords

capsid structure; gene therapy; parvoviruses; pathogenicity; tissue tropism

Indexed keywords

CELL SURFACE RECEPTOR; PROTEASOME; VIRUS DNA; VIRUS PROTEIN;

EID: 84858390096     PISSN: 17460794     EISSN: 17460808     Source Type: Journal    
DOI: 10.2217/fvl.12.12     Document Type: Review
Times cited : (45)

References (245)
  • 1
    • 36249027278 scopus 로고    scopus 로고
    • Parvoviridae
    • Knipe DM, HowleyPM, Griffin DE etal. (Eds). Lippincott Williams & Wilkins, PA, USA
    • Berns KI, Parrish CR. Parvoviridae. In:Field's Virology Knipe DM, HowleyPM, Griffin DE etal. (Eds). Lippincott Williams & Wilkins, PA, USA, 2437-2478 (2007).
    • (2007) Field's Virology , pp. 2437-2478
    • Berns, K.I.1    Parrish, C.R.2
  • 2
    • 81555221014 scopus 로고    scopus 로고
    • Ninth report of the International Committee on Taxonomy of Viruses
    • King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (Eds). Elsevier, The Netherlands
    • Bergoin M, Kleinschmidt J, Almendral JM etal. Ninth report of the International Committee on Taxonomy of Viruses. In:Virus Taxonomy King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (Eds). Elsevier, The Netherlands, 405-425 (2011).
    • (2011) Virus Taxonomy , vol.405-425
    • Bergoin, M.1    Kleinschmidt, J.2    Almendral, J.M.3
  • 3
    • 80051677803 scopus 로고    scopus 로고
    • Autonomous parvovirus variation and evolution
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Parrish CR. Autonomous parvovirus variation and evolution. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 47-54 (2006).
    • (2006) Parvoviruses , pp. 47-54
    • Parrish, C.R.1
  • 4
    • 54249096633 scopus 로고    scopus 로고
    • The genus Erythrovirus
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Brown KE. The genus Erythrovirus. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 25-46 (2006).
    • (2006) Parvoviruses , pp. 25-46
    • Brown, K.E.1
  • 5
    • 85145106846 scopus 로고    scopus 로고
    • Thegenus dependovirus
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Bowles DE, Rabinowitz JE, Samulski RJ. Thegenus Dependovirus. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 15-24 (2006).
    • (2006) Parvoviruses , pp. 15-24
    • Bowles, D.E.1    Rabinowitz, J.E.2    Samulski, R.J.3
  • 6
    • 85145128502 scopus 로고    scopus 로고
    • Structure and organization of the viral genome
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Cotmore SF, Tattersall R. Structure and organization of the viral genome. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 73-94 (2006).
    • (2006) Parvoviruses , pp. 73-94
    • Cotmore, S.F.1    Tattersall, R.2
  • 7
    • 0022977990 scopus 로고
    • Complete nucleotide sequence and genome organization of bovine parvovirus
    • Chen KC, Shull BC, Moses EA, Lederman M, Stout ER, Bates RC. Complete nucleotide sequence and genome organization of bovine parvovirus. J. Virol. 60(3), 1085-1097 (1986).
    • (1986) J. Virol. , vol.60 , Issue.3 , pp. 1085-1097
    • Chen, K.C.1    Shull, B.C.2    Moses, E.A.3    Lederman, M.4    Stout, E.R.5    Bates, R.C.6
  • 8
    • 64049112433 scopus 로고    scopus 로고
    • Molecular characterization of infectious clones of the minute virus of canines reveals unique features of bocaviruses
    • Sun Y, Chen AY, Cheng F, Guan W, Johnson FB, Qiu J. Molecular characterization of infectious clones of the minute virus of canines reveals unique features of bocaviruses. J. Virol. 83(8), 3956-3967 (2009).
    • (2009) J. Virol. , vol.83 , Issue.8 , pp. 3956-3967
    • Sun, Y.1    Chen, A.Y.2    Cheng, F.3    Guan, W.4    Johnson, F.B.5    Qiu, J.6
  • 9
    • 0020559884 scopus 로고
    • Invitro and invivo studies of bovine parvovirus proteins
    • Lederman M, Bates RC, Stout ER. Invitro and invivo studies of bovine parvovirus proteins. J. Virol. 48(1), 10-17 (1983).
    • (1983) J. Virol. , vol.48 , Issue.1 , pp. 10-17
    • Lederman, M.1    Bates, R.C.2    Stout, E.R.3
  • 10
    • 0015534846 scopus 로고
    • Structural proteins of HADEN virus
    • Johnson FB, Hoggan MD. Structural proteins of HADEN virus. Virology 51(1), 129-137 (1973).
    • (1973) Virology , vol.51 , Issue.1 , pp. 129-137
    • Johnson, F.B.1    Hoggan, M.D.2
  • 11
    • 85145134354 scopus 로고    scopus 로고
    • Atomic structures of viral particles
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Chapman MS, Agbandje-McKenna M. Atomic structures of viral particles. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 107-124 (2006).
    • (2006) Parvoviruses , pp. 107-124
    • Chapman, M.S.1    Agbandje-McKenna, M.2
  • 12
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett JS, Wilcher R, Samulski RJ. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 74(6), 2777-2785 (2000).
    • (2000) J. Virol. , vol.74 , Issue.6 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 13
    • 0026524911 scopus 로고
    • Infectious entry pathway for canine parvovirus
    • Provided the first evidence that successful parvoviral infection requires trafficking through low pH endosomal compartments
    • Basak S, Turner H. Infectious entry pathway for canine parvovirus. Virology 186(2), 368-376 (1992). n Provided the first evidence that successful parvoviral infection requires trafficking through low pH endosomal compartments.
    • (1992) Virology , vol.186 , Issue.2 , pp. 368-376
    • Basak, S.1    Turner, H.2
  • 14
    • 34548250956 scopus 로고    scopus 로고
    • Parvoviral host range and cell entry mechanisms
    • Cotmore SF, Tattersall P. Parvoviral host range and cell entry mechanisms. Adv. Virus Res. 70, 183-232 (2007).
    • (2007) Adv. Virus Res. , vol.70 , pp. 183-232
    • Cotmore, S.F.1    Tattersall, P.2
  • 15
    • 0032737034 scopus 로고    scopus 로고
    • Dynamin is required for recombinant adeno-associated virus type 2 infection
    • Duan D, Li Q, Kao AW, Yue Y, Pessin JE, Engelhardt JF. Dynamin is required for recombinant adeno-associated virus type 2 infection. J. Virol. 73(12), 10371-10376 (1999).
    • (1999) J. Virol. , vol.73 , Issue.12 , pp. 10371-10376
    • Duan, D.1    Li, Q.2    Kao, A.W.3    Yue, Y.4    Pessin, J.E.5    Engelhardt, J.F.6
  • 16
    • 0033937284 scopus 로고    scopus 로고
    • Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking
    • Parker JS, Parrish CR. Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J. Virol. 74(4), 1919-1930 (2000).
    • (2000) J. Virol. , vol.74 , Issue.4 , pp. 1919-1930
    • Parker, J.S.1    Parrish, C.R.2
  • 17
    • 0035138205 scopus 로고    scopus 로고
    • Intracellular trafficking of adeno-associated virus vectors: Routing to the late endosomal compartment and proteasome degradation
    • First report of the proteasomal degradation of adeno-associated virus (AAV) during its infectious life cycle
    • Douar AM, Poulard K, Stockholm D, Danos O. Intracellular trafficking of adeno-associated virus vectors: Routing to the late endosomal compartment and proteasome degradation. J. Virol. 75(4), 1824-1833 (2001). n First report of the proteasomal degradation of adeno-associated virus (AAV) during its infectious life cycle.
    • (2001) J. Virol. , vol.75 , Issue.4 , pp. 1824-1833
    • Douar, A.M.1    Poulard, K.2    Stockholm, D.3    Danos, O.4
  • 18
    • 0035043237 scopus 로고    scopus 로고
    • Adeno-associated virus type2-mediated gene transfer: Altered endocytic processing enhances transduction efficiency in murine fibroblasts
    • Hansen J, Qing K, Srivastava A. Adeno-associated virus type2-mediated gene transfer: Altered endocytic processing enhances transduction efficiency in murine fibroblasts. J. Virol. 75(9), 4080-4090 (2001).
    • (2001) J. Virol. , vol.75 , Issue.9 , pp. 4080-4090
    • Hansen, J.1    Qing, K.2    Srivastava, A.3
  • 19
    • 0035085754 scopus 로고    scopus 로고
    • Canine and feline parvoviruses can use human or feline transferrin receptors to bind, enter, and infect cells
    • Parker JS, Murphy WJ, Wang D, O'Brien SJ, Parrish CR. Canine and feline parvoviruses can use human or feline transferrin receptors to bind, enter, and infect cells. J. Virol. 75(8), 3896-3902 (2001).
    • (2001) J. Virol. , vol.75 , Issue.8 , pp. 3896-3902
    • Parker, J.S.1    Murphy, W.J.2    Wang, D.3    O'Brien, S.J.4    Parrish, C.R.5
  • 20
    • 0036891844 scopus 로고    scopus 로고
    • Cytoplasmic trafficking of minute virus of mice: Low-pH requirement, routing to late endosomes, and proteasome interaction
    • Ros C, Burckhardt CJ, Kempf C. Cytoplasmic trafficking of minute virus of mice: Low-pH requirement, routing to late endosomes, and proteasome interaction. J. Virol. 76(24), 12634-12645 (2002).
    • (2002) J. Virol. , vol.76 , Issue.24 , pp. 12634-12645
    • Ros, C.1    Burckhardt, C.J.2    Kempf, C.3
  • 22
    • 43049089793 scopus 로고    scopus 로고
    • Theparvovirus capsid odyssey: From the cell surface to the nucleus
    • Harbison CE, Chiorini JA, Parrish CR. Theparvovirus capsid odyssey: From the cell surface to the nucleus. Trends Microbiol. 16(5), 208-214 (2008).
    • (2008) Trends Microbiol. , vol.16 , Issue.5 , pp. 208-214
    • Harbison, C.E.1    Chiorini, J.A.2    Parrish, C.R.3
  • 23
    • 70349739362 scopus 로고    scopus 로고
    • Early steps in cell infection by parvoviruses: Host-specific differences in cell receptor binding but similar endosomal trafficking
    • Harbison CE, Lyi SM, Weichert WS, Parrish CR. Early steps in cell infection by parvoviruses: Host-specific differences in cell receptor binding but similar endosomal trafficking. J. Virol. 83(20), 10504-10514 (2009).
    • (2009) J. Virol. , vol.83 , Issue.20 , pp. 10504-10514
    • Harbison, C.E.1    Lyi, S.M.2    Weichert, W.S.3    Parrish, C.R.4
  • 24
    • 2442689164 scopus 로고    scopus 로고
    • Parvovirus infection of cells by using variantsof the feline transferrin receptor altering clathrin-mediated endocytosis, membrane domain localization, and capsid-binding domains
    • Hueffer K, Palermo LM, Parrish CR. Parvovirus infection of cells by using variantsof the feline transferrin receptor altering clathrin-mediated endocytosis, membrane domain localization, and capsid-binding domains. J. Virol. 78(11), 5601-5611 (2004).
    • (2004) J. Virol. , vol.78 , Issue.11 , pp. 5601-5611
    • Hueffer, K.1    Palermo, L.M.2    Parrish, C.R.3
  • 25
    • 0036174267 scopus 로고    scopus 로고
    • Endocytosis of adeno-associated virus type 5 leads to accumulation of virus particles in the Golgi compartment
    • First description of an alternative trafficking pathway for an AAV
    • Bantel-Schaal U, Hub B, Kartenbeck J. Endocytosis of adeno-associated virus type 5 leads to accumulation of virus particles in the Golgi compartment. J. Virol. 76(5), 2340-2349 (2002). n First description of an alternative trafficking pathway for an AAV.
    • (2002) J. Virol. , vol.76 , Issue.5 , pp. 2340-2349
    • Bantel-Schaal, U.1    Hub, B.2    Kartenbeck, J.3
  • 26
    • 77954516011 scopus 로고    scopus 로고
    • Multiple pathways involved in porcine parvovirus cellular entry and trafficking toward the nucleus
    • Boisvert M, Fernandes S, Tijssen P. Multiple pathways involved in porcine parvovirus cellular entry and trafficking toward the nucleus. J. Virol. 84(15), 7782-7792 (2010).
    • (2010) J. Virol. , vol.84 , Issue.15 , pp. 7782-7792
    • Boisvert, M.1    Fernandes, S.2    Tijssen, P.3
  • 27
    • 79958061881 scopus 로고    scopus 로고
    • AAV exploits subcellular stress associated with inflammation, endoplasmic reticulum expansion, and misfolded proteins in models of cystic fibrosis
    • The role of unfolded protein response in AAV trafficking
    • Johnson JS, Gentzsch M, Zhang L etal. AAV exploits subcellular stress associated with inflammation, endoplasmic reticulum expansion, and misfolded proteins in models of cystic fibrosis. PLoS Pathog. 7(5), E1002053 (2011). n The role of unfolded protein response in AAV trafficking.
    • (2011) PLoS Pathog. , vol.7 , Issue.5
    • Johnson, J.S.1    Gentzsch, M.2    Zhang, L.3
  • 28
    • 85145123631 scopus 로고    scopus 로고
    • Correlating structure with function in the viral capsid
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Agbandje-McKenna M, Chapman, MS. Correlating structure with function in the viral capsid. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 125-140 (2006).
    • (2006) Parvoviruses , pp. 125-140
    • Agbandje-McKenna, M.1    Chapman, M.S.2
  • 29
    • 83455225659 scopus 로고    scopus 로고
    • AAV capsid structure and cell interactions
    • Detailed review of the properties and structural characteristics of AAV as it relates to its life cycle
    • Agbandje-McKenna M, Kleinschmidt J. AAV capsid structure and cell interactions. Methods Mol. Biol. 807, 47-92 (2011). nn Detailed review of the properties and structural characteristics of AAV as it relates to its life cycle.
    • (2011) Methods Mol. Biol. , vol.807 , pp. 47-92
    • Agbandje-McKenna, M.1    Kleinschmidt, J.2
  • 30
    • 0035431876 scopus 로고    scopus 로고
    • A viral phospholipase A2 is required for parvovirus infectivity
    • Described the novel finding of an essential enzyme function, PLA2, encoded within the VP1 N-terminus of parvoviruses. This VP1 unique region has since been demonstrated to be essential for infectivity
    • Zadori Z, Szelei J, Lacoste MC etal. A viral phospholipase A2 is required for parvovirus infectivity. Dev. Cell 1(2), 291-302 (2001). n Described the novel finding of an essential enzyme function, PLA2, encoded within the VP1 N-terminus of parvoviruses. This VP1 unique region has since been demonstrated to be essential for infectivity.
    • (2001) Dev. Cell , vol.1 , Issue.2 , pp. 291-302
    • Zadori, Z.1    Szelei, J.2    Lacoste, M.C.3
  • 31
    • 33750712806 scopus 로고    scopus 로고
    • Adeno-associated virus type2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus
    • Sonntag F, Bleker S, Leuchs B, Fischer R, Kleinschmidt JA. Adeno-associated virus type2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus. J. Virol. 80(22), 11040-11054 (2006).
    • (2006) J. Virol. , vol.80 , Issue.22 , pp. 11040-11054
    • Sonntag, F.1    Bleker, S.2    Leuchs, B.3    Fischer, R.4    Kleinschmidt, J.A.5
  • 32
    • 0033851104 scopus 로고    scopus 로고
    • Mutational analysis of the adeno-associated virus type 2 (AAV2) capsid gene and construction of AAV2 vectors with altered tropism
    • Wu P, Xiao W, Conlon T etal. Mutational analysis of the adeno-associated virus type 2 (AAV2) capsid gene and construction of AAV2 vectors with altered tropism. J. Virol. 74(18), 8635-8647 (2000).
    • (2000) J. Virol. , vol.74 , Issue.18 , pp. 8635-8647
    • Wu, P.1    Xiao, W.2    Conlon, T.3
  • 33
    • 33646719922 scopus 로고    scopus 로고
    • Separate basic region motifs within the adeno-associated virus capsid proteins are essential for infectivity and assembly
    • Grieger JC, Snowdy S, Samulski RJ. Separate basic region motifs within the adeno-associated virus capsid proteins are essential for infectivity and assembly. J. Virol. 80(11), 5199-5210 (2006).
    • (2006) J. Virol. , vol.80 , Issue.11 , pp. 5199-5210
    • Grieger, J.C.1    Snowdy, S.2    Samulski, R.J.3
  • 34
    • 77956627896 scopus 로고    scopus 로고
    • Mutagenesis of adeno-associated virus type2 capsid protein VP1 uncovers new roles for basic amino acids in trafficking and cell-specific transduction
    • Johnson JS, Li C, Diprimio N, Weinberg MS, McCown TJ, Samulski RJ. Mutagenesis of adeno-associated virus type2 capsid protein VP1 uncovers new roles for basic amino acids in trafficking and cell-specific transduction. J. Virol. 84(17), 8888-8902 (2010).
    • (2010) J. Virol. , vol.84 , Issue.17 , pp. 8888-8902
    • Johnson, J.S.1    Li, C.2    Diprimio, N.3    Weinberg, M.S.4    McCown, T.J.5    Samulski, R.J.6
  • 35
    • 80053386167 scopus 로고    scopus 로고
    • Structure-function analysis of receptor-binding in adeno-associated virus serotype 6 (AAV-6)
    • Xie Q, Lerch TF, Meyer NL, Chapman MS. Structure-function analysis of receptor-binding in adeno-associated virus serotype 6 (AAV-6). Virology 420(1), 10-19 (2011).
    • (2011) Virology , vol.420 , Issue.1 , pp. 10-19
    • Xie, Q.1    Lerch, T.F.2    Meyer, N.L.3    Chapman, M.S.4
  • 36
    • 78649402995 scopus 로고    scopus 로고
    • Structural characterization of the dual glycan binding adeno-associated virus serotype 6
    • Ng R, Govindasamy L, Gurda BL etal. Structural characterization of the dual glycan binding adeno-associated virus serotype 6. J. Virol. 84(24), 12945-12957 (2010).
    • (2010) J. Virol. , vol.84 , Issue.24 , pp. 12945-12957
    • Ng, R.1    Govindasamy, L.2    Gurda, B.L.3
  • 37
    • 77953285729 scopus 로고    scopus 로고
    • The structure of adeno-associated virus serotype3B (AAV-3B): Insights into receptor binding and immune evasion
    • Lerch TF, Xie Q, Chapman MS. The structure of adeno-associated virus serotype3B (AAV-3B): Insights into receptor binding and immune evasion. Virology 403(1), 26-36 (2010).
    • (2010) Virology , vol.403 , Issue.1 , pp. 26-36
    • Lerch, T.F.1    Xie, Q.2    Chapman, M.S.3
  • 38
    • 36049020398 scopus 로고    scopus 로고
    • Structure of adeno-associated virus serotype8, a gene therapy vector
    • Nam HJ, Lane MD, Padron E etal. Structure of adeno-associated virus serotype8, a gene therapy vector. J. Virol. 81(22), 12260-12271 (2007).
    • (2007) J. Virol. , vol.81 , Issue.22 , pp. 12260-12271
    • Nam, H.J.1    Lane, M.D.2    Padron, E.3
  • 39
    • 20144387791 scopus 로고    scopus 로고
    • Structure of adeno-associated virus type 4
    • Padron E, Bowman V, Kaludov N etal. Structure of adeno-associated virus type 4. J. Virol. 79(8), 5047-5058 (2005).
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 5047-5058
    • Padron, E.1    Bowman, V.2    Kaludov, N.3
  • 40
    • 1842562409 scopus 로고    scopus 로고
    • Structure of adeno-associated virus serotype 5
    • Walters RW, Agbandje-McKenna M, Bowman VD etal. Structure of adeno-associated virus serotype 5. J. Virol. 78(7), 3361-3371 (2004).
    • (2004) J. Virol. , vol.78 , Issue.7 , pp. 3361-3371
    • Walters, R.W.1    Agbandje-McKenna, M.2    Bowman, V.D.3
  • 41
    • 0036678455 scopus 로고    scopus 로고
    • The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy
    • Xie Q, Bu W, Bhatia S etal. The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy. Proc. Natl Acad. Sci. USA 99(16), 10405-10410 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.16 , pp. 10405-10410
    • Xie, Q.1    Bu, W.2    Bhatia, S.3
  • 42
    • 0032534013 scopus 로고    scopus 로고
    • Functional implications of the structure of the murine parvovirus, minute virus of mice
    • Agbandje-McKenna M, Llamas-Saiz AL, Wang F, Tattersall P, Rossmann MG. Functional implications of the structure of the murine parvovirus, minute virus of mice. Structure 6(11), 1369-1381 (1998).
    • (1998) Structure , vol.6 , Issue.11 , pp. 1369-1381
    • Agbandje-McKenna, M.1    Llamas-Saiz, A.L.2    Wang, F.3    Tattersall, P.4    Rossmann, M.G.5
  • 44
    • 0343966477 scopus 로고
    • Determination and refinement of the canine parvovirus empty-capsid structure
    • Wu H, Keller W, Rossmann MG. Determination and refinement of the canine parvovirus empty-capsid structure. Acta Crystallogr. D Biol. Crystallogr. 49(Pt6), 572-579 (1993).
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , Issue.PART 6 , pp. 572-579
    • Wu, H.1    Keller, W.2    Rossmann, M.G.3
  • 45
    • 17444405970 scopus 로고    scopus 로고
    • Structure determination of feline panleukopenia virus empty particles. Proteins 16(2), 155-171 (1993). 46. Kronenberg S, Bottcher B, Von Der Lieth CW, Bleker S, Kleinschmidt JA. A conformational change in the adeno-associated virus type2 capsid leads to the exposure of hidden VP1 N termini
    • Agbandje M, McKenna R, Rossmann MG, Strassheim ML, Parrish CR. Structure determination of feline panleukopenia virus empty particles. Proteins 16(2), 155-171 (1993).
    • (2005) J. Virol. , vol.79 , Issue.9 , pp. 5296-5303
    • Agbandje, M.1    McKenna, R.2    Rossmann, M.G.3    Strassheim, M.L.4    Parrish, C.R.5
  • 46
    • 17444405970 scopus 로고    scopus 로고
    • A conformational change in the adeno-associated virus type2 capsid leads to the exposure of hidden VP1 N termini
    • Kronenberg S, Bottcher B, Von Der Lieth CW, Bleker S, Kleinschmidt JA. A conformational change in the adeno-associated virus type2 capsid leads to the exposure of hidden VP1 N termini. J. Virol. 79(9), 5296-5303 (2005).
    • (2005) J. Virol. , vol.79 , Issue.9 , pp. 5296-5303
    • Kronenberg, S.1    Bottcher, B.2    Von Der Lieth, C.W.3    Bleker, S.4    Kleinschmidt, J.A.5
  • 47
    • 0034747267 scopus 로고    scopus 로고
    • Electron cryo-microscopy and image reconstruction of adeno-associated virus type2 empty capsids
    • Kronenberg S, Kleinschmidt JA, Bottcher B. Electron cryo-microscopy and image reconstruction of adeno-associated virus type2 empty capsids. EMBO Rep. 2(11), 997-1002 (2001).
    • (2001) EMBO Rep. , vol.2 , Issue.11 , pp. 997-1002
    • Kronenberg, S.1    Kleinschmidt, J.A.2    Bottcher, B.3
  • 48
    • 0032768489 scopus 로고    scopus 로고
    • Three-dimensional structure of Aleutian mink disease parvovirus: Implications for disease pathogenicity
    • McKenna R, Olson NH, Chipman PR etal. Three-dimensional structure of Aleutian mink disease parvovirus: Implications for disease pathogenicity. J. Virol. 73(8), 6882-6891 (1999).
    • (1999) J. Virol. , vol.73 , Issue.8 , pp. 6882-6891
    • McKenna, R.1    Olson, N.H.2    Chipman, P.R.3
  • 49
    • 33751210120 scopus 로고    scopus 로고
    • Structurally mapping the diverse phenotypeof adeno-associated virus serotype 4
    • Began the description of the regions of the AAV capsid that vary between the serotypes and began the functional annotation of these regions. They play essential roles in cell recognition, determine the serotype transduction efficiency and are the determinants of antigenic reactivity
    • Govindasamy L, Padron E, McKenna R etal. Structurally mapping the diverse phenotypeof adeno-associated virus serotype 4. J. Virol. 80(23), 11556-11570 (2006). n Began the description of the regions of the AAV capsid that vary between the serotypes and began the functional annotation of these regions. They play essential roles in cell recognition, determine the serotype transduction efficiency and are the determinants of antigenic reactivity.
    • (2006) J. Virol. , vol.80 , Issue.23 , pp. 11556-11570
    • Govindasamy, L.1    Padron, E.2    McKenna, R.3
  • 50
    • 0036304301 scopus 로고    scopus 로고
    • The structure of porcine parvovirus: Comparison with related viruses
    • Simpson AA, Hebert B, Sullivan GM etal. The structure of porcine parvovirus: Comparison with related viruses. J. Mol. Biol. 315(5), 1189-1198 (2002).
    • (2002) J. Mol. Biol. , vol.315 , Issue.5 , pp. 1189-1198
    • Simpson, A.A.1    Hebert, B.2    Sullivan, G.M.3
  • 51
    • 77952704829 scopus 로고    scopus 로고
    • Human bocavirus capsid structure: Insights into the structural repertoire of the parvoviridae
    • Gurda BL, Parent KN, Bladek H etal. Human bocavirus capsid structure: Insights into the structural repertoire of the parvoviridae. J. Virol. 84(12), 5880-5889 (2010).
    • (2010) J. Virol. , vol.84 , Issue.12 , pp. 5880-5889
    • Gurda, B.L.1    Parent, K.N.2    Bladek, H.3
  • 53
    • 47749093965 scopus 로고    scopus 로고
    • Visualization of the externalized VP2 N termini of infectious human parvovirus B19
    • Kaufmann B, Chipman PR, Kostyuchenko VA, Modrow S, Rossmann MG. Visualization of the externalized VP2 N termini of infectious human parvovirus B19. J. Virol. 82(15), 7306-7312 (2008).
    • (2008) J. Virol. , vol.82 , Issue.15 , pp. 7306-7312
    • Kaufmann, B.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Modrow, S.4    Rossmann, M.G.5
  • 54
    • 0025774451 scopus 로고
    • Thethree-dimensional structure of canine parvovirus and its functional implications
    • The first crystal structure solved for a member of Parvoviridae family at 3.25-Å resolution by the heavy atom phasing method, which provided the first starting model for the structure determination of other members
    • Tsao J, Chapman MS, Agbandje M etal. Thethree-dimensional structure of canine parvovirus and its functional implications. Science 251(5000), 1456-1464 (1991). n The first crystal structure solved for a member of Parvoviridae family at 3.25-Å resolution by the heavy atom phasing method, which provided the first starting model for the structure determination of other members.
    • (1991) Science , vol.251 , Issue.5000 , pp. 1456-1464
    • Tsao, J.1    Chapman, M.S.2    Agbandje, M.3
  • 55
    • 81255179983 scopus 로고    scopus 로고
    • The assembly-activating protein promotes capsid assembly of different adeno-associated virus serotypes
    • Sonntag F, Kother K, Schmidt K etal. The assembly-activating protein promotes capsid assembly of different adeno-associated virus serotypes. J. Virol. 85(23), 12686-12697 (2011).
    • (2011) J. Virol. , vol.85 , Issue.23 , pp. 12686-12697
    • Sonntag, F.1    Kother, K.2    Schmidt, K.3
  • 56
    • 0013914098 scopus 로고
    • Studies of small DNA viruses found in various adenovirus preparations: Physical, biological, and immunological characteristics
    • Hoggan MD, Blacklow NR, Rowe WP. Studies of small DNA viruses found in various adenovirus preparations: Physical, biological, and immunological characteristics. Proc. Natl Acad. Sci. USA 55(6), 1467-1474 (1966).
    • (1966) Proc. Natl Acad. Sci. USA , vol.55 , Issue.6 , pp. 1467-1474
    • Hoggan, M.D.1    Blacklow, N.R.2    Rowe, W.P.3
  • 57
    • 0001592496 scopus 로고
    • Adenovirus-associated defective virus particles
    • Atchison RW, Casto BC, Hammon WM. Adenovirus-associated defective virus particles. Science 149(3685), 754-756 (1965).
    • (1965) Science , vol.149 , Issue.3685 , pp. 754-756
    • Atchison, R.W.1    Casto, B.C.2    Hammon, W.M.3
  • 58
    • 59749091653 scopus 로고    scopus 로고
    • Adeno-associated virus vectors and biology of gene delivery
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Carter BJ. Adeno-associated virus vectors and biology of gene delivery. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 497-498 (2006).
    • (2006) Parvoviruses , pp. 497-498
    • Carter, B.J.1
  • 59
    • 44049094771 scopus 로고    scopus 로고
    • Clinical gene therapy using recombinant adeno-associated virus vectors
    • Mueller C, Flotte TR. Clinical gene therapy using recombinant adeno-associated virus vectors. Gene Ther. 15(11), 858-863 (2008).
    • (2008) Gene Ther. , vol.15 , Issue.11 , pp. 858-863
    • Mueller, C.1    Flotte, T.R.2
  • 60
    • 54249126862 scopus 로고    scopus 로고
    • Gene therapy using adeno-associated virus vectors
    • Daya S, Berns KI. Gene therapy using adeno-associated virus vectors. Clin. Microbiol. Rev. 21(4), 583-593 (2008).
    • (2008) Clin. Microbiol. Rev. , vol.21 , Issue.4 , pp. 583-593
    • Daya, S.1    Berns, K.I.2
  • 61
    • 36749033228 scopus 로고    scopus 로고
    • The state of the art of adeno-associated virus-based vectors in gene therapy
    • Coura Rdos S, Nardi NB. The state of the art of adeno-associated virus-based vectors in gene therapy. Virol. J. 4, 99 (2007).
    • (2007) Virol. J. , vol.4 , pp. 99
    • Coura Rdos, S.1    Nardi, N.B.2
  • 62
    • 84855161388 scopus 로고    scopus 로고
    • Adenovirus-associated virus vector-mediated gene transfer in hemophilia B
    • Nathwani AC, Tuddenham EGD, Rangarajan S etal. Adenovirus-associated virus vector-mediated gene transfer in hemophilia B. N. Engl. J. Med. 365(25), 2357-2365 (2011).
    • (2011) N. Engl. J. Med. , vol.365 , Issue.25 , pp. 2357-2365
    • Nathwani, A.C.1    Tuddenham, E.G.D.2    Rangarajan, S.3
  • 63
    • 83455219474 scopus 로고    scopus 로고
    • Adeno-associated virus mediated gene therapy for retinal degenerative diseases
    • Stieger K, Cronin T, Bennett J, Rolling F. Adeno-associated virus mediated gene therapy for retinal degenerative diseases. Methods Mol. Biol. 807, 179-218 (2011).
    • (2011) Methods Mol. Biol. , vol.807 , pp. 179-218
    • Stieger, K.1    Cronin, T.2    Bennett, J.3    Rolling, F.4
  • 64
    • 71549132206 scopus 로고    scopus 로고
    • Adeno-associated viral vectors and their redirection to cell-type specific receptors
    • Michelfelder S, Trepel M. Adeno-associated viral vectors and their redirection to cell-type specific receptors. Adv. Genet. 67, 29-60 (2009).
    • (2009) Adv. Genet. , vol.67 , pp. 29-60
    • Michelfelder, S.1    Trepel, M.2
  • 65
    • 77954976233 scopus 로고    scopus 로고
    • Prevalence of serum IgG and neutralizing factors against adeno-associated virus (AAV) types 1, 2, 5, 6, 8, and 9 in the healthy population: Implications for gene therapy using AAV vectors
    • Boutin S, Monteilhet V, Veron P etal. Prevalence of serum IgG and neutralizing factors against adeno-associated virus (AAV) types 1, 2, 5, 6, 8, and 9 in the healthy population: Implications for gene therapy using AAV vectors. Hum. Gene Ther. 21(6), 704-712 (2010).
    • (2010) Hum. Gene Ther. , vol.21 , Issue.6 , pp. 704-712
    • Boutin, S.1    Monteilhet, V.2    Veron, P.3
  • 66
    • 2642512201 scopus 로고    scopus 로고
    • Clades of adeno-associated viruses are widely disseminated in human tissues
    • Gao G, Vandenberghe LH, Alvira MR etal. Clades of adeno-associated viruses are widely disseminated in human tissues. J. Virol. 78(12), 6381-6388 (2004).
    • (2004) J. Virol. , vol.78 , Issue.12 , pp. 6381-6388
    • Gao, G.1    Vandenberghe, L.H.2    Alvira, M.R.3
  • 67
    • 1842527048 scopus 로고    scopus 로고
    • Identification of adeno-associated virus contamination in cell and virus stocks by PCR
    • Katano H, Afione S, Schmidt M, Chiorini JA. Identification of adeno-associated virus contamination in cell and virus stocks by PCR. Biotechniques 36(4), 676-680 (2004).
    • (2004) Biotechniques , vol.36 , Issue.4 , pp. 676-680
    • Katano, H.1    Afione, S.2    Schmidt, M.3    Chiorini, J.A.4
  • 68
    • 33750982385 scopus 로고    scopus 로고
    • Molecular characterization of caprine adeno-associated virus (AAV-Go.1) reveals striking similarity to human AAV5
    • Qiu J, Cheng F, Pintel D. Molecular characterization of caprine adeno-associated virus (AAV-Go.1) reveals striking similarity to human AAV5. Virology 356(1-2), 208-216 (2006).
    • (2006) Virology , vol.356 , Issue.1-2 , pp. 208-216
    • Qiu, J.1    Cheng, F.2    Pintel, D.3
  • 69
    • 29744466489 scopus 로고    scopus 로고
    • Novel caprine adeno-associated virus (AAV) capsid (AAV-Go.1) is closely related to the primate AAV-5 and has unique tropism and neutralization properties
    • Arbetman AE, Lochrie M, Zhou S etal. Novel caprine adeno-associated virus (AAV) capsid (AAV-Go.1) is closely related to the primate AAV-5 and has unique tropism and neutralization properties. J. Virol. 79(24), 15238-15245 (2005).
    • (2005) J. Virol. , vol.79 , Issue.24 , pp. 15238-15245
    • Arbetman, A.E.1    Lochrie, M.2    Zhou, S.3
  • 70
    • 33747874648 scopus 로고    scopus 로고
    • Adeno-associated virus (AAV) capsid genes isolated from rat and mouse liver genomic DNA define two new AAV species distantly related to AAV-5
    • Lochrie MA, Tatsuno GP, Arbetman AE etal. Adeno-associated virus (AAV) capsid genes isolated from rat and mouse liver genomic DNA define two new AAV species distantly related to AAV-5. Virology 353(1), 68-82 (2006).
    • (2006) Virology , vol.353 , Issue.1 , pp. 68-82
    • Lochrie, M.A.1    Tatsuno, G.P.2    Arbetman, A.E.3
  • 71
    • 0030140957 scopus 로고    scopus 로고
    • Coinfection of a bearded dragon, Pogona vitticeps, with adenovirus-and dependovirus-like viruses
    • Jacobson ER, Kopit W, Kennedy FA, Funk RS. Coinfection of a bearded dragon, Pogona vitticeps, with adenovirus-and dependovirus-like viruses. Vet. Pathol. 33(3), 343-346 (1996).
    • (1996) Vet. Pathol. , vol.33 , Issue.3 , pp. 343-346
    • Jacobson, E.R.1    Kopit, W.2    Kennedy, F.A.3    Funk, R.S.4
  • 72
    • 44349170706 scopus 로고    scopus 로고
    • Analysis of AAV serotypes 1-9 mediated gene expression and tropism in mice after systemic injection
    • Zincarelli C, Soltys S, Rengo G, Rabinowitz JE. Analysis of AAV serotypes 1-9 mediated gene expression and tropism in mice after systemic injection. Mol. Ther. 16(6), 1073-1080 (2008).
    • (2008) Mol. Ther. , vol.16 , Issue.6 , pp. 1073-1080
    • Zincarelli, C.1    Soltys, S.2    Rengo, G.3    Rabinowitz, J.E.4
  • 73
    • 35348836681 scopus 로고    scopus 로고
    • Comparative biology of rAAV transduction in ferret, pig and human airway epithelia
    • Liu X, Luo M, Guo C, Yan Z, Wang Y, Engelhardt JF. Comparative biology of rAAV transduction in ferret, pig and human airway epithelia. Gene Ther. 14(21), 1543-1548 (2007).
    • (2007) Gene Ther. , vol.14 , Issue.21 , pp. 1543-1548
    • Liu, X.1    Luo, M.2    Guo, C.3    Yan, Z.4    Wang, Y.5    Engelhardt, J.F.6
  • 74
    • 62549150024 scopus 로고    scopus 로고
    • Transduction efficiencies of novel AAV vectors in mouse airway epithelium invivo and human ciliated airway epithelium invitro
    • Limberis MP, Vandenberghe LH, Zhang L, Pickles RJ, Wilson JM. Transduction efficiencies of novel AAV vectors in mouse airway epithelium invivo and human ciliated airway epithelium invitro. Mol. Ther. 17(2), 294-301 (2009).
    • (2009) Mol. Ther. , vol.17 , Issue.2 , pp. 294-301
    • Limberis, M.P.1    Vandenberghe, L.H.2    Zhang, L.3    Pickles, R.J.4    Wilson, J.M.5
  • 75
    • 73849130017 scopus 로고    scopus 로고
    • Generation of novel AAV variants by directed evolution for improved CFTR delivery to human ciliated airway epithelium
    • Li W, Zhang L, Johnson JS etal. Generation of novel AAV variants by directed evolution for improved CFTR delivery to human ciliated airway epithelium. Mol. Ther. 17(12), 2067-2077 (2009).
    • (2009) Mol. Ther. , vol.17 , Issue.12 , pp. 2067-2077
    • Li, W.1    Zhang, L.2    Johnson, J.S.3
  • 76
    • 33748945422 scopus 로고    scopus 로고
    • The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9
    • Akache B, Grimm D, Pandey K, Yant SR, Xu H, Kay MA. The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9. J. Virol. 80(19), 9831-9836 (2006).
    • (2006) J. Virol. , vol.80 , Issue.19 , pp. 9831-9836
    • Akache, B.1    Grimm, D.2    Pandey, K.3    Yant, S.R.4    Xu, H.5    Kay, M.A.6
  • 77
    • 79957918498 scopus 로고    scopus 로고
    • The AAV9 receptor and its modification to improve invivo lung gene transfer in mice
    • Bell CL, Vandenberghe LH, Bell P etal. The AAV9 receptor and its modification to improve invivo lung gene transfer in mice. J. Clin. Invest. 121(6), 2427-2435 (2011).
    • (2011) J. Clin. Invest. , vol.121 , Issue.6 , pp. 2427-2435
    • Bell, C.L.1    Vandenberghe, L.H.2    Bell, P.3
  • 78
    • 0142105497 scopus 로고    scopus 로고
    • Identification of PDGFR as a receptor for AAV-5 transduction
    • Di Pasquale G, Davidson BL, Stein CS etal. Identification of PDGFR as a receptor for AAV-5 transduction. Nat. Med. 9(10), 1306-1312 (2003).
    • (2003) Nat. Med. , vol.9 , Issue.10 , pp. 1306-1312
    • Di Pasquale, G.1    Davidson, B.L.2    Stein, C.S.3
  • 79
    • 77949757540 scopus 로고    scopus 로고
    • BAAV transcytosis requires an interaction with beta-1-4 linked-glucosamine and gp96
    • Di Pasquale G, Kaludov N, Agbandje-McKenna M, Chiorini JA. BAAV transcytosis requires an interaction with beta-1-4 linked-glucosamine and gp96. PLoS One 5(3), E9336 (2010).
    • (2010) PLoS One , vol.5 , Issue.3
    • Di Pasquale, G.1    Kaludov, N.2    Agbandje-McKenna, M.3    Chiorini, J.A.4
  • 80
    • 10644225886 scopus 로고    scopus 로고
    • Enhanced sialic acid-dependent endocytosis explains the increased efficiency of infection of airway epithelia by a novel adeno-associated virus. J. Virol. 85(17), 9023-9030 (2011). 81. Kashiwakura Y, Tamayose K, Iwabuchi K etal. Hepatocyte growth factor receptor is a coreceptor for adeno-associated virus type 2 infection
    • Dickey DD, Excoffon KJ, Koerber JT etal. Enhanced sialic acid-dependent endocytosis explains the increased efficiency of infection of airway epithelia by a novel adeno-associated virus. J. Virol. 85(17), 9023-9030 (2011).
    • (2005) J. Virol. , vol.79 , Issue.1 , pp. 609-614
    • Dickey, D.D.1    Excoffon, K.J.2    Koerber, J.T.3
  • 81
    • 10644225886 scopus 로고    scopus 로고
    • Hepatocyte growth factor receptor is a coreceptor for adeno-associated virus type 2 infection
    • Kashiwakura Y, Tamayose K, Iwabuchi K etal. Hepatocyte growth factor receptor is a coreceptor for adeno-associated virus type 2 infection. J. Virol. 79(1), 609-614 (2005).
    • (2005) J. Virol. , vol.79 , Issue.1 , pp. 609-614
    • Kashiwakura, Y.1    Tamayose, K.2    Iwabuchi, K.3
  • 82
    • 78650105132 scopus 로고    scopus 로고
    • Human hepatocyte growth factor receptor is a cellular coreceptor for adeno-associated virus serotype 3
    • Ling C, Lu Y, Kalsi JK etal. Human hepatocyte growth factor receptor is a cellular coreceptor for adeno-associated virus serotype 3. Hum. Gene Ther. 21(12), 1741-1747 (2010).
    • (2010) Hum. Gene Ther. , vol.21 , Issue.12 , pp. 1741-1747
    • Ling, C.1    Lu, Y.2    Kalsi, J.K.3
  • 83
    • 0033010884 scopus 로고    scopus 로고
    • Human fibroblast growth factor receptor 1 is a co-receptor for infection by adeno-associated virus 2
    • Qing K, Mah C, Hansen J, Zhou S, Dwarki V, Srivastava A. Human fibroblast growth factor receptor 1 is a co-receptor for infection by adeno-associated virus 2. Nat. Med. 5(1), 71-77 (1999).
    • (1999) Nat. Med. , vol.5 , Issue.1 , pp. 71-77
    • Qing, K.1    Mah, C.2    Hansen, J.3    Zhou, S.4    Dwarki, V.5    Srivastava, A.6
  • 84
    • 30744440945 scopus 로고    scopus 로고
    • Adeno-associated virus types 5 and 6 use distinct receptors for cell entry
    • Seiler MP, Miller AD, Zabner J, Halbert CL. Adeno-associated virus types 5 and 6 use distinct receptors for cell entry. Hum. Gene Ther. 17(1), 10-19 (2006).
    • (2006) Hum. Gene Ther. , vol.17 , Issue.1 , pp. 10-19
    • Seiler, M.P.1    Miller, A.D.2    Zabner, J.3    Halbert, C.L.4
  • 85
    • 79953857433 scopus 로고    scopus 로고
    • Terminal N-linked galactose is the primary receptor for adeno-associated virus 9
    • Shen S, Bryant KD, Brown SM, Randell SH, Asokan A. Terminal N-linked galactose is the primary receptor for adeno-associated virus 9. J. Biol. Chem. 286(15), 13532-13540 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.15 , pp. 13532-13540
    • Shen, S.1    Bryant, K.D.2    Brown, S.M.3    Randell, S.H.4    Asokan, A.5
  • 86
    • 0032589751 scopus 로고    scopus 로고
    • AlphaVbeta5 integrin: A co-receptor for adeno-associated virus type2 infection
    • Summerford C, Bartlett JS, Samulski RJ. AlphaVbeta5 integrin: A co-receptor for adeno-associated virus type2 infection. Nat. Med. 5(1), 78-82 (1999).
    • (1999) Nat. Med. , vol.5 , Issue.1 , pp. 78-82
    • Summerford, C.1    Bartlett, J.S.2    Samulski, R.J.3
  • 87
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions
    • Identification of heparan sulfate proteoglycan as AAV2 receptor, which is now used as a purification reagent
    • Summerford C, Samulski RJ. Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions. J. Virol. 72(2), 1438-1445 (1998). n Identification of heparan sulfate proteoglycan as AAV2 receptor, which is now used as a purification reagent.
    • (1998) J. Virol. , vol.72 , Issue.2 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 88
    • 0035827546 scopus 로고    scopus 로고
    • Binding of adeno-associated virus type5 to 2,3-linked sialic acid is required for gene transfer
    • Walters RW, Yi SM, Keshavjee S etal. Binding of adeno-associated virus type5 to 2,3-linked sialic acid is required for gene transfer. J. Biol. Chem. 276(23), 20610-20616 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.23 , pp. 20610-20616
    • Walters, R.W.1    Yi, S.M.2    Keshavjee, S.3
  • 90
    • 33748501920 scopus 로고    scopus 로고
    • Alpha2,3 and alpha2,6 N-linked sialic acids facilitate efficient binding and transduction by adeno-associated virus types 1 and 6
    • Wu Z, Miller E, Agbandje-McKenna M, Samulski RJ. Alpha2,3 and alpha2,6 N-linked sialic acids facilitate efficient binding and transduction by adeno-associated virus types 1 and 6. J. Virol. 80(18), 9093-9103 (2006).
    • (2006) J. Virol. , vol.80 , Issue.18 , pp. 9093-9103
    • Wu, Z.1    Miller, E.2    Agbandje-McKenna, M.3    Samulski, R.J.4
  • 91
    • 33750722840 scopus 로고    scopus 로고
    • Single amino acid changes can influence titer, heparin binding, and tissue tropism in different adeno-associated virus serotypes
    • Wu Z, Asokan A, Grieger JC, Govindasamy L, Agbandje-McKenna M, Samulski RJ. Single amino acid changes can influence titer, heparin binding, and tissue tropism in different adeno-associated virus serotypes. J. Virol. 80(22), 11393-11397 (2006).
    • (2006) J. Virol. , vol.80 , Issue.22 , pp. 11393-11397
    • Wu, Z.1    Asokan, A.2    Grieger, J.C.3    Govindasamy, L.4    Agbandje-McKenna, M.5    Samulski, R.J.6
  • 92
    • 33748494015 scopus 로고    scopus 로고
    • Adeno-associated virus type2 contains an integrin alpha5beta1 binding domain essential for viral cell entry
    • Asokan A, Hamra JB, Govindasamy L, Agbandje-McKenna M, Samulski RJ. Adeno-associated virus type2 contains an integrin alpha5beta1 binding domain essential for viral cell entry. J. Virol. 80(18), 8961-8969 (2006).
    • (2006) J. Virol. , vol.80 , Issue.18 , pp. 8961-8969
    • Asokan, A.1    Hamra, J.B.2    Govindasamy, L.3    Agbandje-McKenna, M.4    Samulski, R.J.5
  • 93
    • 0034957168 scopus 로고    scopus 로고
    • Adeno-associated virus serotype4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity
    • Kaludov N, Brown KE, Walters RW, Zabner J, Chiorini JA. Adeno-associated virus serotype4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity. J. Virol. 75(15), 6884-6893 (2001).
    • (2001) J. Virol. , vol.75 , Issue.15 , pp. 6884-6893
    • Kaludov, N.1    Brown, K.E.2    Walters, R.W.3    Zabner, J.4    Chiorini, J.A.5
  • 94
    • 20544445216 scopus 로고    scopus 로고
    • Attachment of bovine parvovirus to O-linked alpha 2,3 neuraminic acid on glycophorin A
    • Blackburn SD, Cline SE, Hemming JP, Johnson FB. Attachment of bovine parvovirus to O-linked alpha 2,3 neuraminic acid on glycophorin A. Arch. Virol. 150(7), 1477-1484 (2005).
    • (2005) Arch. Virol. , vol.150 , Issue.7 , pp. 1477-1484
    • Blackburn, S.D.1    Cline, S.E.2    Hemming, J.P.3    Johnson, F.B.4
  • 95
    • 60949103263 scopus 로고    scopus 로고
    • Adeno-associated virus-2 and its primary cellular receptor -cryo-EM structure of a heparin complex
    • O'Donnell J, Taylor KA, Chapman MS. Adeno-associated virus-2 and its primary cellular receptor -cryo-EM structure of a heparin complex. Virology 385(2), 434-443 (2009).
    • (2009) Virology , vol.385 , Issue.2 , pp. 434-443
    • O'Donnell, J.1    Taylor, K.A.2    Chapman, M.S.3
  • 96
    • 59149090531 scopus 로고    scopus 로고
    • Heparin binding induces conformational changes in adeno-associated virus serotype 2
    • Levy HC, Bowman VD, Govindasamy L etal. Heparin binding induces conformational changes in adeno-associated virus serotype 2. J. Struct. Biol. 165(3), 146-156 (2009).
    • (2009) J. Struct. Biol. , vol.165 , Issue.3 , pp. 146-156
    • Levy, H.C.1    Bowman, V.D.2    Govindasamy, L.3
  • 97
    • 33646723883 scopus 로고    scopus 로고
    • Gangliosides are essential for bovine adeno-associated virus entry
    • Schmidt M, Chiorini JA. Gangliosides are essential for bovine adeno-associated virus entry. J. Virol. 80(11), 5516-5522 (2006).
    • (2006) J. Virol. , vol.80 , Issue.11 , pp. 5516-5522
    • Schmidt, M.1    Chiorini, J.A.2
  • 98
    • 0038618725 scopus 로고    scopus 로고
    • Identification of amino acid residues in the capsid proteins of adeno-associated virus type2 that contribute to heparan sulfate proteoglycan binding
    • Opie SR, Warrington KH Jr, Agbandje-McKenna M, Zolotukhin S, Muzyczka N. Identification of amino acid residues in the capsid proteins of adeno-associated virus type2 that contribute to heparan sulfate proteoglycan binding. J. Virol. 77(12), 6995-7006 (2003).
    • (2003) J. Virol. , vol.77 , Issue.12 , pp. 6995-7006
    • Opie, S.R.1    Warrington Jr., K.H.2    Agbandje-McKenna, M.3    Zolotukhin, S.4    Muzyczka, N.5
  • 99
    • 0141454787 scopus 로고    scopus 로고
    • Identification of a heparin-binding motif on adeno-associated virus type2 capsids
    • Kern A, Schmidt K, Leder C etal. Identification of a heparin-binding motif on adeno-associated virus type2 capsids. J. Virol. 77(20), 11072-11081 (2003).
    • (2003) J. Virol. , vol.77 , Issue.20 , pp. 11072-11081
    • Kern, A.1    Schmidt, K.2    Leder, C.3
  • 100
    • 62649174755 scopus 로고    scopus 로고
    • Directed evolution of adeno-associated virus to an infectious respiratory virus
    • Excoffon KJ, Koerber JT, Dickey DD etal. Directed evolution of adeno-associated virus to an infectious respiratory virus. Proc. NatlAcad. Sci. USA 106(10), 3865-3870 (2009).
    • (2009) Proc. NatlAcad. Sci. USA , vol.106 , Issue.10 , pp. 3865-3870
    • Excoffon, K.J.1    Koerber, J.T.2    Dickey, D.D.3
  • 101
    • 33645840118 scopus 로고    scopus 로고
    • Attachment of adeno-associated virus type3H to fibroblast growth factor receptor1
    • Blackburn SD, Steadman RA, Johnson FB. Attachment of adeno-associated virus type3H to fibroblast growth factor receptor1. Arch. Virol. 151(3), 617-623 (2006).
    • (2006) Arch. Virol. , vol.151 , Issue.3 , pp. 617-623
    • Blackburn, S.D.1    Steadman, R.A.2    Johnson, F.B.3
  • 102
    • 84856953535 scopus 로고    scopus 로고
    • Successful target cell transduction of capsid-engineered rAAV vectors requires clathrin-dependent endocytosis
    • doi:10.1038/gt.2011.78 ( Epub ahead of print
    • Uhrig S, Coutelle O, Wiehe T, Perabo L, Hallek M, Buning H. Successful target cell transduction of capsid-engineered rAAV vectors requires clathrin-dependent endocytosis. Gene Ther. doi:10.1038/gt.2011.78 (2011) (Epub ahead of print).
    • (2011) Gene Ther.
    • Uhrig, S.1    Coutelle, O.2    Wiehe, T.3    Perabo, L.4    Hallek, M.5    Buning, H.6
  • 103
    • 0034091579 scopus 로고    scopus 로고
    • Endosomal processing limits gene transfer to polarized airway epithelia by adeno-associated virus
    • Duan D, Yue Y, Yan Z, Yang J, Engelhardt JF. Endosomal processing limits gene transfer to polarized airway epithelia by adeno-associated virus. J. Clin. Invest. 105(11), 1573-1587 (2000).
    • (2000) J. Clin. Invest. , vol.105 , Issue.11 , pp. 1573-1587
    • Duan, D.1    Yue, Y.2    Yan, Z.3    Yang, J.4    Engelhardt, J.F.5
  • 104
    • 78649447518 scopus 로고    scopus 로고
    • Intrinsic phospholipase A2 activity of adeno-associated virus is involved in endosomal escape of incoming particles
    • Stahnke S, Lux K, Uhrig S etal. Intrinsic phospholipase A2 activity of adeno-associated virus is involved in endosomal escape of incoming particles. Virology 409(1), 77-83 (2011).
    • (2011) Virology , vol.409 , Issue.1 , pp. 77-83
    • Stahnke, S.1    Lux, K.2    Uhrig, S.3
  • 105
    • 13444310872 scopus 로고    scopus 로고
    • Mutational analysis of narrow pores at the fivefold symmetry axes of adeno-associated virus type2 capsids reveals a dual role in genome packaging and activation of phospholipase A2 activity
    • Bleker S, Sonntag F, Kleinschmidt JA. Mutational analysis of narrow pores at the fivefold symmetry axes of adeno-associated virus type2 capsids reveals a dual role in genome packaging and activation of phospholipase A2 activity. J. Virol. 79(4), 2528-2540 (2005).
    • (2005) J. Virol. , vol.79 , Issue.4 , pp. 2528-2540
    • Bleker, S.1    Sonntag, F.2    Kleinschmidt, J.A.3
  • 106
    • 62749116843 scopus 로고    scopus 로고
    • Adeno-associated virus type 5 exploits two different entry pathways in human embryo fibroblasts
    • Bantel-Schaal U, Braspenning-Wesch I, Kartenbeck J. Adeno-associated virus type 5 exploits two different entry pathways in human embryo fibroblasts. J. Gen. Virol. 90(Pt2), 317-322 (2009).
    • (2009) J. Gen. Virol. , vol.90 , Issue.PART 2 , pp. 317-322
    • Bantel-Schaal, U.1    Braspenning-Wesch, I.2    Kartenbeck, J.3
  • 107
    • 80655142508 scopus 로고    scopus 로고
    • Structural studies of adeno-associated virus serotype8 capsid transitions associated with endosomal trafficking
    • Structural insights into low pH-mediated capsid conformation transitions that likely prime the AAV capsid for subsequent events in trafficking and uncoating in the host nucleus
    • Nam HJ, Gurda BL, McKenna R etal. Structural studies of adeno-associated virus serotype8 capsid transitions associated with endosomal trafficking. J. Virol. 85(22), 11791-11799 (2011). n Structural insights into low pH-mediated capsid conformation transitions that likely prime the AAV capsid for subsequent events in trafficking and uncoating in the host nucleus.
    • (2011) J. Virol. , vol.85 , Issue.22 , pp. 11791-11799
    • Nam, H.J.1    Gurda, B.L.2    McKenna, R.3
  • 109
    • 30844451241 scopus 로고    scopus 로고
    • Parvovirus uncoating invitro reveals a mechanism of DNA release without capsid disassembly and striking differences in encapsidated DNA stability
    • Ros C, Baltzer C, Mani B, Kempf C. Parvovirus uncoating invitro reveals a mechanism of DNA release without capsid disassembly and striking differences in encapsidated DNA stability. Virology 345(1), 137-147 (2006).
    • (2006) Virology , vol.345 , Issue.1 , pp. 137-147
    • Ros, C.1    Baltzer, C.2    Mani, B.3    Kempf, C.4
  • 110
    • 54549096772 scopus 로고    scopus 로고
    • Tyrosine-phosphorylation of AAV2 vectors and its consequences on viral intracellular trafficking and transgene expression
    • Zhong L, Li B, Jayandharan G etal. Tyrosine-phosphorylation of AAV2 vectors and its consequences on viral intracellular trafficking and transgene expression. Virology 381(2), 194-202 (2008).
    • (2008) Virology , vol.381 , Issue.2 , pp. 194-202
    • Zhong, L.1    Li, B.2    Jayandharan, G.3
  • 111
    • 45549090635 scopus 로고    scopus 로고
    • Next generation of adeno-associated virus 2 vectors: Point mutations in tyrosines lead to high-efficiency transduction at lower doses
    • Zhong L, Li B, Mah CS etal. Next generation of adeno-associated virus 2 vectors: Point mutations in tyrosines lead to high-efficiency transduction at lower doses. Proc. Natl Acad. Sci. USA 105(22), 7827-7832 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.22 , pp. 7827-7832
    • Zhong, L.1    Li, B.2    Mah, C.S.3
  • 112
    • 0036828086 scopus 로고    scopus 로고
    • Adenovirus-facilitated nuclear translocation of adeno-associated virus type 2
    • Xiao W, Warrington KH Jr, Hearing P, Hughes J, Muzyczka N. Adenovirus-facilitated nuclear translocation of adeno-associated virus type 2. J. Virol. 76(22), 11505-11517 (2002).
    • (2002) J. Virol. , vol.76 , Issue.22 , pp. 11505-11517
    • Xiao, W.1    Warrington Jr., K.H.2    Hearing, P.3    Hughes, J.4    Muzyczka, N.5
  • 113
    • 0034759535 scopus 로고    scopus 로고
    • Infection of purified nuclei by adeno-associated virus 2
    • Hansen J, Qing K, Srivastava A. Infection of purified nuclei by adeno-associated virus 2. Mol. Ther. 4(4), 289-296 (2001).
    • (2001) Mol. Ther. , vol.4 , Issue.4 , pp. 289-296
    • Hansen, J.1    Qing, K.2    Srivastava, A.3
  • 114
    • 62749167014 scopus 로고    scopus 로고
    • Endocytosis and nuclear trafficking of adeno-associated virus type2 are controlled by rac1 and phosphatidylinositol-3 kinase activation. J. Virol. 74(19), 9184-9196 (2000). 115. Johnson JS, Samulski RJ. Enhancement of adeno-associated virus infection by mobilizing capsids into and out of the nucleolus
    • Sanlioglu S, Benson PK, Yang J, Atkinson EM, Reynolds T, Engelhardt JF. Endocytosis and nuclear trafficking of adeno-associated virus type2 are controlled by rac1 and phosphatidylinositol-3 kinase activation. J. Virol. 74(19), 9184-9196 (2000).
    • (2009) J. Virol. , vol.83 , Issue.6 , pp. 2632-2644
    • Sanlioglu, S.1    Benson, P.K.2    Yang, J.3    Atkinson, E.M.4    Reynolds, T.5    Engelhardt, J.F.6
  • 115
    • 62749167014 scopus 로고    scopus 로고
    • Enhancement of adeno-associated virus infection by mobilizing capsids into and out of the nucleolus
    • Johnson JS, Samulski RJ. Enhancement of adeno-associated virus infection by mobilizing capsids into and out of the nucleolus. J. Virol. 83(6), 2632-2644 (2009).
    • (2009) J. Virol. , vol.83 , Issue.6 , pp. 2632-2644
    • Johnson, J.S.1    Samulski, R.J.2
  • 116
    • 24644509652 scopus 로고    scopus 로고
    • Green fluorescent protein-tagged adeno-associated virus particles allow the study of cytosolic and nuclear trafficking
    • Lux K, Goerlitz N, Schlemminger S etal. Green fluorescent protein-tagged adeno-associated virus particles allow the study of cytosolic and nuclear trafficking. J. Virol. 79(18), 11776-11787 (2005).
    • (2005) J. Virol. , vol.79 , Issue.18 , pp. 11776-11787
    • Lux, K.1    Goerlitz, N.2    Schlemminger, S.3
  • 117
    • 85145146199 scopus 로고    scopus 로고
    • A rolling-hairpin strategy: Basic mechanism of DNA replication in the parvoviruses
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Cotmore SF, Tattersall R. A rolling-hairpin strategy: Basic mechanism of DNA replication in the parvoviruses. In:Parvoviruses. Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 171-188 (2006).
    • (2006) Parvoviruses , pp. 171-188
    • Cotmore, S.F.1    Tattersall, R.2
  • 118
    • 0030846525 scopus 로고    scopus 로고
    • Mutational analysis of the adeno-associated virus type2 Rep68 protein helicase motifs
    • Walker SL, Wonderling RS, Owens RA. Mutational analysis of the adeno-associated virus type2 Rep68 protein helicase motifs. J. Virol. 71(9), 6996-7004 (1997).
    • (1997) J. Virol. , vol.71 , Issue.9 , pp. 6996-7004
    • Walker, S.L.1    Wonderling, R.S.2    Owens, R.A.3
  • 119
    • 0026659844 scopus 로고
    • Analysis of mutations in adeno-associated virus Rep protein invivo and invitro
    • Mccarty DM, Ni TH, Muzyczka N. Analysis of mutations in adeno-associated virus Rep protein invivo and invitro. J. Virol. 66(7), 4050-4057 (1992).
    • (1992) J. Virol. , vol.66 , Issue.7 , pp. 4050-4057
    • Mccarty, D.M.1    Ni, T.H.2    Muzyczka, N.3
  • 120
    • 0025218471 scopus 로고
    • Mutation of a consensus purine nucleotide binding site in the adeno-associated virus rep gene generates a dominant negative phenotype for DNA replication
    • Chejanovsky N, Carter BJ. Mutation of a consensus purine nucleotide binding site in the adeno-associated virus rep gene generates a dominant negative phenotype for DNA replication. J. Virol. 64(4), 1764-1770 (1990).
    • (1990) J. Virol. , vol.64 , Issue.4 , pp. 1764-1770
    • Chejanovsky, N.1    Carter, B.J.2
  • 121
    • 0035875669 scopus 로고    scopus 로고
    • DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids
    • King JA, Dubielzig R, Grimm D, Kleinschmidt JA. DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids. EMBO J. 20(12), 3282-3291 (2001).
    • (2001) EMBO J. , vol.20 , Issue.12 , pp. 3282-3291
    • King, J.A.1    Dubielzig, R.2    Grimm, D.3    Kleinschmidt, J.A.4
  • 123
    • 0032826095 scopus 로고    scopus 로고
    • Adeno-associated virus type2 protein interactions: Formation of pre-encapsidation complexes
    • Dubielzig R, King JA, Weger S, Kern A, Kleinschmidt JA. Adeno-associated virus type2 protein interactions: Formation of pre-encapsidation complexes. J. Virol. 73(11), 8989-8998 (1999).
    • (1999) J. Virol. , vol.73 , Issue.11 , pp. 8989-8998
    • Dubielzig, R.1    King, J.A.2    Weger, S.3    Kern, A.4    Kleinschmidt, J.A.5
  • 124
    • 30344435922 scopus 로고    scopus 로고
    • Impact of capsid conformation and Rep-capsid interactions on adeno-associated virus type 2 genome packaging
    • Bleker S, Pawlita M, Kleinschmidt JA. Impact of capsid conformation and Rep-capsid interactions on adeno-associated virus type 2 genome packaging. J. Virol. 80(2), 810-820 (2006).
    • (2006) J. Virol. , vol.80 , Issue.2 , pp. 810-820
    • Bleker, S.1    Pawlita, M.2    Kleinschmidt, J.A.3
  • 125
    • 77953439661 scopus 로고    scopus 로고
    • A viral assembly factor promotes AAV2 capsid formation in the nucleolus
    • Reports the discovery of an assembly-activating protein that is essential for capsid assembly
    • Sonntag F, Schmidt K, Kleinschmidt JA. A viral assembly factor promotes AAV2 capsid formation in the nucleolus. Proc. Natl Acad. Sci. USA 107(22), 10220-10225 (2010). n Reports the discovery of an assembly-activating protein that is essential for capsid assembly.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.22 , pp. 10220-10225
    • Sonntag, F.1    Schmidt, K.2    Kleinschmidt, J.A.3
  • 127
    • 0024442216 scopus 로고
    • Mutagenesis of an AUG codon in the adeno-associated virus rep gene: Effects on viral DNA replication
    • Chejanovsky N, Carter BJ. Mutagenesis of an AUG codon in the adeno-associated virus rep gene: Effects on viral DNA replication. Virology 173(1), 120-128 (1989).
    • (1989) Virology , vol.173 , Issue.1 , pp. 120-128
    • Chejanovsky, N.1    Carter, B.J.2
  • 128
  • 129
    • 0027476207 scopus 로고
    • Identification of a DNA-binding domain in the amino terminus of adeno-associated virus Rep proteins
    • Owens RA, Weitzman MD, Kyostio SR, Carter BJ. Identification of a DNA-binding domain in the amino terminus of adeno-associated virus Rep proteins. J. Virol. 67(2), 997-1005 (1993).
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 997-1005
    • Owens, R.A.1    Weitzman, M.D.2    Kyostio, S.R.3    Carter, B.J.4
  • 130
    • 0027241589 scopus 로고
    • Analysis of the terminal repeat binding abilities of mutant adeno-associated virus replication proteins
    • Yang Q, Trempe JP. Analysis of the terminal repeat binding abilities of mutant adeno-associated virus replication proteins. J. Virol. 67(7), 4442-4447 (1993).
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 4442-4447
    • Yang, Q.1    Trempe, J.P.2
  • 131
    • 0028290387 scopus 로고
    • Identification of linear DNA sequences that specifically bind the adeno-associated virus Rep protein
    • Mccarty DM, Pereira DJ, Zolotukhin I, Zhou X, Ryan JH, Muzyczka N. Identification of linear DNA sequences that specifically bind the adeno-associated virus Rep protein. J. Virol. 68(8), 4988-4997 (1994).
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 4988-4997
    • Mccarty, D.M.1    Pereira, D.J.2    Zolotukhin, I.3    Zhou, X.4    Ryan, J.H.5    Muzyczka, N.6
  • 132
    • 0038475876 scopus 로고    scopus 로고
    • Identification of active site residues of the adeno-associated virus type2 Rep endonuclease
    • Yoon-Robarts M, Linden RM. Identification of active site residues of the adeno-associated virus type2 Rep endonuclease. J. Biol. Chem. 278(7), 4912-4918 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 4912-4918
    • Yoon-Robarts, M.1    Linden, R.M.2
  • 135
    • 33947218846 scopus 로고    scopus 로고
    • Immune responses to AAV capsid: Are mice not humans after all?
    • Herzog RW. Immune responses to AAV capsid: Are mice not humans after all? Mol. Ther. 15(4), 649-650 (2007).
    • (2007) Mol. Ther. , vol.15 , Issue.4 , pp. 649-650
    • Herzog, R.W.1
  • 136
    • 28444491760 scopus 로고    scopus 로고
    • Identification of mouse AAV capsid-specific CD8+ T cell epitopes
    • Sabatino DE, Mingozzi F, Hui DJ etal. Identification of mouse AAV capsid-specific CD8+ T cell epitopes. Mol. Ther. 12(6), 1023-1033 (2005).
    • (2005) Mol. Ther. , vol.12 , Issue.6 , pp. 1023-1033
    • Sabatino, D.E.1    Mingozzi, F.2    Hui, D.J.3
  • 137
    • 73249136916 scopus 로고    scopus 로고
    • Identification of the murine AAVrh32.33 capsid-specific CD8+ T cell epitopes
    • Mays LE, Wilson JM. Identification of the murine AAVrh32.33 capsid-specific CD8+ T cell epitopes. J. Gene Med. 11(12), 1095-1102 (2009).
    • (2009) J. Gene Med. , vol.11 , Issue.12 , pp. 1095-1102
    • Mays, L.E.1    Wilson, J.M.2
  • 138
    • 67449093069 scopus 로고    scopus 로고
    • Cytotoxic-T-lymphocyte-mediated elimination of target cells transduced with engineered adeno-associated virus type 2 vector invivo
    • Li C, Hirsch M, Diprimio N etal. Cytotoxic-T-lymphocyte-mediated elimination of target cells transduced with engineered adeno-associated virus type 2 vector invivo. J. Virol. 83(13), 6817-6824 (2009).
    • (2009) J. Virol. , vol.83 , Issue.13 , pp. 6817-6824
    • Li, C.1    Hirsch, M.2    Diprimio, N.3
  • 139
    • 33644820684 scopus 로고    scopus 로고
    • Successful transduction of liver in hemophilia by AAV-Factor IX and limitations imposed by the host immune response
    • Manno CS, Pierce GF, Arruda VR etal. Successful transduction of liver in hemophilia by AAV-Factor IX and limitations imposed by the host immune response. Nat. Med. 12(3), 342-347 (2006).
    • (2006) Nat. Med. , vol.12 , Issue.3 , pp. 342-347
    • Manno, C.S.1    Pierce, G.F.2    Arruda, V.R.3
  • 140
    • 44049083209 scopus 로고    scopus 로고
    • Immunity to adeno-associated virus vectors in animals and humans: A continued challenge
    • Zaiss AK, Muruve DA. Immunity to adeno-associated virus vectors in animals and humans: A continued challenge. Gene Ther. 15(11), 808-816 (2008).
    • (2008) Gene Ther. , vol.15 , Issue.11 , pp. 808-816
    • Zaiss, A.K.1    Muruve, D.A.2
  • 141
    • 0033808531 scopus 로고    scopus 로고
    • Monoclonal antibodies against the adeno-associated virus type2 (AAV-2) capsid: Epitope mapping and identification of capsid domains involved in AAV-2-cell interaction and neutralization of AAV-2 infection
    • This antibody epitope mapping study identified immunodominant AAV2 capsid regions and provided reagents that have impacted the field with respect to further immunological studies of AAVs
    • Wobus CE, Hugle-Dorr B, Girod A, Petersen G, Hallek M, Kleinschmidt JA. Monoclonal antibodies against the adeno-associated virus type2 (AAV-2) capsid: Epitope mapping and identification of capsid domains involved in AAV-2-cell interaction and neutralization of AAV-2 infection. J. Virol. 74(19), 9281-9293 (2000). n This antibody epitope mapping study identified immunodominant AAV2 capsid regions and provided reagents that have impacted the field with respect to further immunological studies of AAVs.
    • (2000) J. Virol. , vol.74 , Issue.19 , pp. 9281-9293
    • Wobus, C.E.1    Hugle-Dorr, B.2    Girod, A.3    Petersen, G.4    Hallek, M.5    Kleinschmidt, J.A.6
  • 142
    • 30344450073 scopus 로고    scopus 로고
    • Mutations on the external surfaces of adeno-associated virus type2 capsids that affect transduction and neutralization
    • An exhaustive mutagenesis study of AAV2 capsid surface-exposed residues to elucidate the role played by the capsid in various steps of viral life cycle, including receptor attachment and antibody recogntion
    • Lochrie MA, Tatsuno GP, Christie B etal. Mutations on the external surfaces of adeno-associated virus type2 capsids that affect transduction and neutralization. J. Virol. 80(2), 821-834 (2006). n An exhaustive mutagenesis study of AAV2 capsid surface-exposed residues to elucidate the role played by the capsid in various steps of viral life cycle, including receptor attachment and antibody recogntion.
    • (2006) J. Virol. , vol.80 , Issue.2 , pp. 821-834
    • Lochrie, M.A.1    Tatsuno, G.P.2    Christie, B.3
  • 143
    • 33846593292 scopus 로고    scopus 로고
    • Development of AAV serotype-specific ELISAs using novel monoclonal antibodies
    • Kuck D, Kern A, Kleinschmidt JA. Development of AAV serotype-specific ELISAs using novel monoclonal antibodies. J. Virol. Methods 140(1-2), 17-24 (2007).
    • (2007) J. Virol. Methods , vol.140 , Issue.1-2 , pp. 17-24
    • Kuck, D.1    Kern, A.2    Kleinschmidt, J.A.3
  • 144
    • 84855919646 scopus 로고    scopus 로고
    • Examining the cross-reactivity and neutralization mechanisms of a panel of monoclonal antibodies against adeno-associated virus serotypes 1 and 5
    • Harbison CE, Weichert WS, Gurda BL, Chiorini JA, Agbandje-McKenna M, Parrish CR. Examining the cross-reactivity and neutralization mechanisms of a panel of monoclonal antibodies against adeno-associated virus serotypes 1 and 5. J. Gen. Virol. 93(Pt2), 347-355 (2012).
    • (2012) J. Gen. Virol. , vol.93 , Issue.PART 2 , pp. 347-355
    • Harbison, C.E.1    Weichert, W.S.2    Gurda, B.L.3    Chiorini, J.A.4    Agbandje-McKenna, M.5    Parrish, C.R.6
  • 145
    • 85145137869 scopus 로고    scopus 로고
    • The parvovirus life cycle: An introduction to molecular interactions important for infection
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Weitzman MD. The parvovirus life cycle: An introduction to molecular interactions important for infection. In:Parvoviruses Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 143-156 (2006).
    • (2006) Parvoviruses , pp. 143-156
    • Weitzman, M.D.1
  • 146
    • 85145131507 scopus 로고    scopus 로고
    • The evolution of parvovirus taxonomy
    • Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK
    • Tattersall P. The evolution of parvovirus taxonomy. In:Parvoviruses. Kerr JR, Cotmore SF, Bloom ME, Linden RM, Parrish CR (Eds). Hodder Arnold, UK, 5-14 (2006).
    • (2006) Parvoviruses , pp. 5-14
    • Tattersall, P.1
  • 148
    • 0034765428 scopus 로고    scopus 로고
    • Aleutian mink disease parvovirus infection of K562 cells is antibody-dependent and is mediated via an Fc(gamma)RII receptor. Arch. Virol. 142(2), 363-373 (1997). 149. Bloom ME, Best SM, Hayes SF etal. Identification of Aleutian mink disease parvovirus capsid sequences mediating antibody-dependent enhancement of infection, virus neutralization, and immune complex formation
    • Dworak LJ, Wolfinbarger JB, Bloom ME. Aleutian mink disease parvovirus infection of K562 cells is antibody-dependent and is mediated via an Fc(gamma)RII receptor. Arch. Virol. 142(2), 363-373 (1997).
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 11116-11127
    • Dworak, L.J.1    Wolfinbarger, J.B.2    Bloom, M.E.3
  • 149
    • 0034765428 scopus 로고    scopus 로고
    • Identification of Aleutian mink disease parvovirus capsid sequences mediating antibody-dependent enhancement of infection, virus neutralization, and immune complex formation
    • Bloom ME, Best SM, Hayes SF etal. Identification of Aleutian mink disease parvovirus capsid sequences mediating antibody-dependent enhancement of infection, virus neutralization, and immune complex formation. J. Virol. 75(22), 11116-11127 (2001).
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 11116-11127
    • Bloom, M.E.1    Best, S.M.2    Hayes, S.F.3
  • 150
    • 33846805819 scopus 로고    scopus 로고
    • Dengue virus (DENV) antibody-dependent enhancement of infection upregulates the production of anti-inflammatory cytokines, but suppresses anti-DENV free radical and pro-inflammatory cytokine production, in THP-1 cells
    • Chareonsirisuthigul T, Kalayanarooj S, Ubol S. Dengue virus (DENV) antibody-dependent enhancement of infection upregulates the production of anti-inflammatory cytokines, but suppresses anti-DENV free radical and pro-inflammatory cytokine production, in THP-1 cells. J. Gen. Virol. 88(Pt 2), 365-375 (2007).
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 2 , pp. 365-375
    • Chareonsirisuthigul, T.1    Kalayanarooj, S.2    Ubol, S.3
  • 151
    • 30844465052 scopus 로고    scopus 로고
    • Human parvovirus B19 infection of monocytic cell line U937 and antibody-dependent enhancement
    • Munakata Y, Kato I, Saito T, Kodera T, Ishii KK, Sasaki T. Human parvovirus B19 infection of monocytic cell line U937 and antibody-dependent enhancement. Virology 345(1), 251-257 (2006).
    • (2006) Virology , vol.345 , Issue.1 , pp. 251-257
    • Munakata, Y.1    Kato, I.2    Saito, T.3    Kodera, T.4    Ishii, K.K.5    Sasaki, T.6
  • 152
    • 56349123240 scopus 로고    scopus 로고
    • Animal bocaviruses: A brief review
    • Manteufel J, Truyen U. Animal bocaviruses: A brief review. Intervirology 51(5), 328-334 (2008).
    • (2008) Intervirology , vol.51 , Issue.5 , pp. 328-334
    • Manteufel, J.1    Truyen, U.2
  • 153
    • 37449017209 scopus 로고    scopus 로고
    • Human bocavirus
    • Allander T. Human bocavirus. J. Clin. Virol. 41(1), 29-33 (2008).
    • (2008) J. Clin. Virol. , vol.41 , Issue.1 , pp. 29-33
    • Allander, T.1
  • 154
    • 33947417652 scopus 로고    scopus 로고
    • Human bocavirus and acute wheezing in children
    • Allander T, Jartti T, Gupta S etal. Human bocavirus and acute wheezing in children. Clin. Infect. Dis. 44(7), 904-910 (2007).
    • (2007) Clin. Infect. Dis. , vol.44 , Issue.7 , pp. 904-910
    • Allander, T.1    Jartti, T.2    Gupta, S.3
  • 159
    • 74149089599 scopus 로고    scopus 로고
    • Newly recognized bocaviruses (HBoV, HBoV2) in children and adults with gastrointestinal illness in the United States
    • Chow BD, Ou Z, Esper FP. Newly recognized bocaviruses (HBoV, HBoV2) in children and adults with gastrointestinal illness in the United States. J. Clin. Virol. 47(2), 143-147 (2010).
    • (2010) J. Clin. Virol. , vol.47 , Issue.2 , pp. 143-147
    • Chow, B.D.1    Ou, Z.2    Esper, F.P.3
  • 160
    • 0020597640 scopus 로고
    • Human parvovirus, the cause of erythema infectiosum (fifth disease)?
    • Anderson MJ, Jones SE, Fisher-Hoch SP etal. Human parvovirus, the cause of erythema infectiosum (fifth disease)? Lancet 1(8338), 1378 (1983).
    • (1983) Lancet , vol.1 , Issue.8338 , pp. 1378
    • Anderson, M.J.1    Jones, S.E.2    Fisher-Hoch, S.P.3
  • 161
    • 0025618085 scopus 로고
    • Hydrops fetalis from B19 parvovirus infection
    • Katz VL, Chescheir NC, Bethea M. Hydrops fetalis from B19 parvovirus infection. J. Perinatol. 10(4), 366-368 (1990).
    • (1990) J. Perinatol. , vol.10 , Issue.4 , pp. 366-368
    • Katz, V.L.1    Chescheir, N.C.2    Bethea, M.3
  • 162
    • 0000754018 scopus 로고    scopus 로고
    • Infection with parvovirus B19
    • Naides SJ. Infection with Parvovirus B19. Curr. Infect. Dis. Rep. 1(3), 273-278 (1999).
    • (1999) Curr. Infect. Dis. Rep. , vol.1 , Issue.3 , pp. 273-278
    • Naides, S.J.1
  • 163
    • 0742316143 scopus 로고    scopus 로고
    • Epidemiology of human parvovirus B19 in children with sickle cell disease
    • Smith-Whitley K, Zhao H, Hodinka RL etal. Epidemiology of human parvovirus B19 in children with sickle cell disease. Blood 103(2), 422-427 (2004).
    • (2004) Blood , vol.103 , Issue.2 , pp. 422-427
    • Smith-Whitley, K.1    Zhao, H.2    Hodinka, R.L.3
  • 165
    • 0034732160 scopus 로고    scopus 로고
    • Rhesus and pig-tailed macaque parvoviruses: Identification of two new members of the erythrovirus genus in monkeys
    • Green SW, Malkovska I, O'Sullivan MG, Brown KE. Rhesus and pig-tailed macaque parvoviruses: Identification of two new members of the erythrovirus genus in monkeys. Virology 269(1), 105-112 (2000).
    • (2000) Virology , vol.269 , Issue.1 , pp. 105-112
    • Green, S.W.1    Malkovska, I.2    O'Sullivan, M.G.3    Brown, K.E.4
  • 166
    • 0033019497 scopus 로고    scopus 로고
    • Severe leukopenia and dysregulated erythropoiesis in SCID mice persistently infected with the parvovirus minute virus of mice
    • Segovia JC, Gallego JM, Bueren JA, Almendral JM. Severe leukopenia and dysregulated erythropoiesis in SCID mice persistently infected with the parvovirus minute virus of mice. J. Virol. 73(3), 1774-1784 (1999).
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 1774-1784
    • Segovia, J.C.1    Gallego, J.M.2    Bueren, J.A.3    Almendral, J.M.4
  • 167
    • 0022445383 scopus 로고
    • Pathogenicity of fibroblast-and lymphocyte-specific variants of minute virus of mice
    • Kimsey PB, Engers HD, Hirt B, Jongeneel CV. Pathogenicity of fibroblast-and lymphocyte-specific variants of minute virus of mice. J. Virol. 59(1), 8-13 (1986).
    • (1986) J. Virol. , vol.59 , Issue.1 , pp. 8-13
    • Kimsey, P.B.1    Engers, H.D.2    Hirt, B.3    Jongeneel, C.V.4
  • 168
    • 0020523002 scopus 로고
    • Reciprocal productive and restrictive virus-cell interactions of immunosuppressive and prototype strains of minute virus of mice
    • Tattersall P, Bratton J. Reciprocal productive and restrictive virus-cell interactions of immunosuppressive and prototype strains of minute virus of mice. J. Virol. 46(3), 944-955 (1983).
    • (1983) J. Virol. , vol.46 , Issue.3 , pp. 944-955
    • Tattersall, P.1    Bratton, J.2
  • 169
    • 0026000601 scopus 로고
    • Initiation of transcription from the minute virus of mice P4 promoter is stimulated in rat cells expressing a c-Ha-ras oncogene
    • Spegelaere P, Van Hille B, Spruyt N, Faisst S, Cornelis JJ, Rommelaere J. Initiation of transcription from the minute virus of mice P4 promoter is stimulated in rat cells expressing a c-Ha-ras oncogene. J. Virol. 65(9), 4919-4928 (1991).
    • (1991) J. Virol. , vol.65 , Issue.9 , pp. 4919-4928
    • Spegelaere, P.1    Van Hille, B.2    Spruyt, N.3    Faisst, S.4    Cornelis, J.J.5    Rommelaere, J.6
  • 170
    • 79958076967 scopus 로고    scopus 로고
    • The parvoviral capsid controls an intracellular phase of infection essential for efficient killing of stepwise-transformed human fibroblasts
    • Paglino J, Tattersall P. The parvoviral capsid controls an intracellular phase of infection essential for efficient killing of stepwise-transformed human fibroblasts. Virology 416(1-2), 32-41 (2011).
    • (2011) Virology , vol.416 , Issue.1-2 , pp. 32-41
    • Paglino, J.1    Tattersall, P.2
  • 171
    • 33746396481 scopus 로고    scopus 로고
    • Oncolytic murine autonomous parvovirus, a candidate vector for glioma gene therapy, is innocuous to normal and immunocompetent mouse glial cells
    • Abschuetz A, Kehl T, Geibig R, Leuchs B, Rommelaere J, Regnier-Vigouroux A. Oncolytic murine autonomous parvovirus, a candidate vector for glioma gene therapy, is innocuous to normal and immunocompetent mouse glial cells. Cell Tissue Res. 325(3), 423-436 (2006).
    • (2006) Cell Tissue Res. , vol.325 , Issue.3 , pp. 423-436
    • Abschuetz, A.1    Kehl, T.2    Geibig, R.3    Leuchs, B.4    Rommelaere, J.5    Regnier-Vigouroux, A.6
  • 172
    • 23844475355 scopus 로고    scopus 로고
    • Structural determinants of tissue tropism and invivo pathogenicity for the parvovirus minute virus of mice
    • Kontou M, Govindasamy L, Nam HJ etal. Structural determinants of tissue tropism and invivo pathogenicity for the parvovirus minute virus of mice. J. Virol. 79(17), 10931-10943 (2005).
    • (2005) J. Virol. , vol.79 , Issue.17 , pp. 10931-10943
    • Kontou, M.1    Govindasamy, L.2    Nam, H.J.3
  • 173
    • 0345196538 scopus 로고    scopus 로고
    • Identification of a cell surface protein from Crandell feline kidney cells that specifically binds Aleutian mink disease parvovirus
    • Fox JM, Bloom ME. Identification of a cell surface protein from Crandell feline kidney cells that specifically binds Aleutian mink disease parvovirus. J. Virol. 73(5), 3835-3842 (1999).
    • (1999) J. Virol. , vol.73 , Issue.5 , pp. 3835-3842
    • Fox, J.M.1    Bloom, M.E.2
  • 174
    • 0031692540 scopus 로고    scopus 로고
    • Binding of bovine parvovirus to erythrocyte membrane sialylglycoproteins
    • Thacker TC, Johnson FB. Binding of bovine parvovirus to erythrocyte membrane sialylglycoproteins. J. Gen. Virol. 79(Pt9), 2163-2169 (1998).
    • (1998) J. Gen. Virol. , vol.79 , Issue.PART 9 , pp. 2163-2169
    • Thacker, T.C.1    Johnson, F.B.2
  • 175
    • 0027686846 scopus 로고
    • Erythrocyte P antigen: Cellular receptor for B19 parvovirus
    • Brown KE, Anderson SM, Young NS. Erythrocyte P antigen: Cellular receptor for B19 parvovirus. Science 262(5130), 114-117 (1993).
    • (1993) Science , vol.262 , Issue.5130 , pp. 114-117
    • Brown, K.E.1    Anderson, S.M.2    Young, N.S.3
  • 176
    • 0345257726 scopus 로고    scopus 로고
    • Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19: Requirement of functional activation of beta1 integrin for viral entry
    • Weigel-Kelley KA, Yoder MC, Srivastava A. Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19: Requirement of functional activation of beta1 integrin for viral entry. Blood 102(12), 3927-3933 (2003).
    • (2003) Blood , vol.102 , Issue.12 , pp. 3927-3933
    • Weigel-Kelley, K.A.1    Yoder, M.C.2    Srivastava, A.3
  • 177
    • 27744600086 scopus 로고    scopus 로고
    • Ku80 autoantigen as a cellular coreceptor for human parvovirus B19 infection
    • Munakata Y, Saito-Ito T, Kumura-Ishii K etal. Ku80 autoantigen as a cellular coreceptor for human parvovirus B19 infection. Blood 106(10), 3449-3456 (2005).
    • (2005) Blood , vol.106 , Issue.10 , pp. 3449-3456
    • Munakata, Y.1    Saito-Ito, T.2    Kumura-Ishii, K.3
  • 178
    • 0023065751 scopus 로고
    • The autonomously replicating parvoviruses of vertebrates
    • The first comprehensive review on the autonomous parvoviruses
    • Cotmore SF, Tattersall P. The autonomously replicating parvoviruses of vertebrates. Adv. Virus Res. 33, 91-174 (1987). n The first comprehensive review on the autonomous parvoviruses.
    • (1987) Adv. Virus Res. , vol.33 , pp. 91-174
    • Cotmore, S.F.1    Tattersall, P.2
  • 179
    • 2542615352 scopus 로고    scopus 로고
    • Molecular mechanism for cancer-associated induction of sialyl Lewis X and sialyl Lewis A expression -The Warburg effect revisited
    • Kannagi R. Molecular mechanism for cancer-associated induction of sialyl Lewis X and sialyl Lewis A expression -the Warburg effect revisited. Glycoconj. J. 20(5), 353-364 (2004).
    • (2004) Glycoconj. J. , vol.20 , Issue.5 , pp. 353-364
    • Kannagi, R.1
  • 180
    • 33748753267 scopus 로고    scopus 로고
    • Identification of the sialic acid structures recognized by minute virus of mice and the role of binding affinity in virulence adaptation
    • Nam HJ, Gurda-Whitaker B, Gan WY etal. Identification of the sialic acid structures recognized by minute virus of mice and the role of binding affinity in virulence adaptation. J. Biol. Chem. 281(35), 25670-25677 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.35 , pp. 25670-25677
    • Nam, H.J.1    Gurda-Whitaker, B.2    Gan, W.Y.3
  • 181
    • 0034685781 scopus 로고    scopus 로고
    • Frequent occurrence of pre-existing alpha 2 ->8-linked disialic and oligosialic acids with chain lengths up to 7 Sia residues in mammalian brain glycoproteins. Prevalence revealed by highly sensitive chemical methods and anti-di-oligo-and poly-Sia antibodies specific for defined chain lengths
    • Sato C, Fukuoka H, Ohta K etal. Frequent occurrence of pre-existing alpha 2 ->8-linked disialic and oligosialic acids with chain lengths up to 7 Sia residues in mammalian brain glycoproteins. Prevalence revealed by highly sensitive chemical methods and anti-di-, oligo-, and poly-Sia antibodies specific for defined chain lengths. J. Biol. Chem. 275(20), 15422-15431 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.20 , pp. 15422-15431
    • Sato, C.1    Fukuoka, H.2    Ohta, K.3
  • 182
    • 0037302252 scopus 로고    scopus 로고
    • The natural host range shift and subsequent evolution of canine parvovirus resulted from virus-specific binding to the canine transferrin receptor
    • Hueffer K, Parker JS, Weichert WS, Geisel RE, Sgro JY, Parrish CR. The natural host range shift and subsequent evolution of canine parvovirus resulted from virus-specific binding to the canine transferrin receptor. J. Virol. 77(3), 1718-1726 (2003).
    • (2003) J. Virol. , vol.77 , Issue.3 , pp. 1718-1726
    • Hueffer, K.1    Parker, J.S.2    Weichert, W.S.3    Geisel, R.E.4    Sgro, J.Y.5    Parrish, C.R.6
  • 183
    • 0026796009 scopus 로고
    • Mutations adjacent to the dimple of the canine parvovirus capsid structure affect sialic acid binding
    • Barbis DP, Chang SF, Parrish CR. Mutations adjacent to the dimple of the canine parvovirus capsid structure affect sialic acid binding. Virology 191(1), 301-308 (1992).
    • (1992) Virology , vol.191 , Issue.1 , pp. 301-308
    • Barbis, D.P.1    Chang, S.F.2    Parrish, C.R.3
  • 184
    • 0023758549 scopus 로고
    • Nucleotide sequence and genomic organization of Aleutian mink disease parvovirus (ADV): Sequence comparisons between a nonpathogenic and a pathogenic strain of ADV
    • Bloom ME, Alexandersen S, Perryman S, Lechner D, Wolfinbarger JB. Nucleotide sequence and genomic organization of Aleutian mink disease parvovirus (ADV): Sequence comparisons between a nonpathogenic and a pathogenic strain of ADV. J. Virol. 62(8), 2903-2915 (1988).
    • (1988) J. Virol. , vol.62 , Issue.8 , pp. 2903-2915
    • Bloom, M.E.1    Alexandersen, S.2    Perryman, S.3    Lechner, D.4    Wolfinbarger, J.B.5
  • 185
    • 0242331722 scopus 로고    scopus 로고
    • Effect of a valine residue at codon 352 of the VP2 capsid protein on invivo replication and pathogenesis of Aleutian disease parvovirus in mink. Am. J. Vet. Res. 62(10), 1658-1663 (2001). 186. Govindasamy L, Hueffer K, Parrish CR, Agbandje-McKenna M. Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants
    • Stevenson MA, Fox JM, Wolfinbarger JB, Bloom ME. Effect of a valine residue at codon 352 of the VP2 capsid protein on invivo replication and pathogenesis of Aleutian disease parvovirus in mink. Am. J. Vet. Res. 62(10), 1658-1663 (2001).
    • (2003) J. Virol. , vol.77 , Issue.22 , pp. 12211-12221
    • Stevenson, M.A.1    Fox, J.M.2    Wolfinbarger, J.B.3    Bloom, M.E.4
  • 186
    • 0242331722 scopus 로고    scopus 로고
    • Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants
    • Govindasamy L, Hueffer K, Parrish CR, Agbandje-McKenna M. Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants. J. Virol. 77(22), 12211-12221 (2003).
    • (2003) J. Virol. , vol.77 , Issue.22 , pp. 12211-12221
    • Govindasamy, L.1    Hueffer, K.2    Parrish, C.R.3    Agbandje-McKenna, M.4
  • 187
    • 0141570405 scopus 로고    scopus 로고
    • Combinations of two capsid regions controlling canine host range determine canine transferrin receptor binding by canine and feline parvoviruses
    • Hueffer K, Govindasamy L, Agbandje-McKenna M, Parrish CR. Combinations of two capsid regions controlling canine host range determine canine transferrin receptor binding by canine and feline parvoviruses. J. Virol. 77(18), 10099-10105 (2003).
    • (2003) J. Virol. , vol.77 , Issue.18 , pp. 10099-10105
    • Hueffer, K.1    Govindasamy, L.2    Agbandje-McKenna, M.3    Parrish, C.R.4
  • 188
    • 34249861814 scopus 로고    scopus 로고
    • Asymmetric binding of transferrin receptor to parvovirus capsids
    • Hafenstein S, Palermo LM, Kostyuchenko VA etal. Asymmetric binding of transferrin receptor to parvovirus capsids. Proc. Natl Acad. Sci. USA 104(16), 6585-6589 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.16 , pp. 6585-6589
    • Hafenstein, S.1    Palermo, L.M.2    Kostyuchenko, V.A.3
  • 189
    • 0029847931 scopus 로고    scopus 로고
    • Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor
    • First cryoreconstruction study that enabled the visualization of a capsid-receptor interaction
    • Chipman PR, Agbandje-McKenna M, Kajigaya S etal. Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor. Proc. Natl Acad. Sci. USA 93(15), 7502-7506 (1996). n First cryoreconstruction study that enabled the visualization of a capsid-receptor interaction.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.15 , pp. 7502-7506
    • Chipman, P.R.1    Agbandje-McKenna, M.2    Kajigaya, S.3
  • 191
    • 30644456924 scopus 로고    scopus 로고
    • Host-selected amino acid changes at the sialic acid binding pocket of the parvovirus capsid modulate cell binding affinity and determine virulence
    • First crystal structure of parvovirus-receptor complex identifying a sialic acid binding pocket
    • Lopez-Bueno A, Rubio MP, Bryant N, McKenna R, Agbandje-McKenna M, Almendral JM. Host-selected amino acid changes at the sialic acid binding pocket of the parvovirus capsid modulate cell binding affinity and determine virulence. J. Virol. 80(3), 1563-1573 (2006). n First crystal structure of parvovirus-receptor complex identifying a sialic acid binding pocket.
    • (2006) J. Virol. , vol.80 , Issue.3 , pp. 1563-1573
    • Lopez-Bueno, A.1    Rubio, M.P.2    Bryant, N.3    McKenna, R.4    Agbandje-McKenna, M.5    Almendral, J.M.6
  • 192
    • 28044448698 scopus 로고    scopus 로고
    • Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry
    • Farr GA, Zhang LG, Tattersall P. Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry. Proc. Natl Acad. Sci. USA 102(47), 17148-17153 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.47 , pp. 17148-17153
    • Farr, G.A.1    Zhang, L.G.2    Tattersall, P.3
  • 193
    • 30344459715 scopus 로고    scopus 로고
    • Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome
    • Mani B, Baltzer C, Valle N, Almendral JM, Kempf C, Ros C. Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome. J. Virol. 80(2), 1015-1024 (2006).
    • (2006) J. Virol. , vol.80 , Issue.2 , pp. 1015-1024
    • Mani, B.1    Baltzer, C.2    Valle, N.3    Almendral, J.M.4    Kempf, C.5    Ros, C.6
  • 194
    • 33645994480 scopus 로고    scopus 로고
    • VP2 cleavage and the leucine ring at the base of the fivefold cylinder control pH-dependent externalization of both the VP1 N terminus and the genome of minute virus of mice
    • Farr GA, Cotmore SF, Tattersall P. VP2 cleavage and the leucine ring at the base of the fivefold cylinder control pH-dependent externalization of both the VP1 N terminus and the genome of minute virus of mice. J. Virol. 80(1), 161-171 (2006).
    • (2006) J. Virol. , vol.80 , Issue.1 , pp. 161-171
    • Farr, G.A.1    Cotmore, S.F.2    Tattersall, P.3
  • 195
    • 2942624232 scopus 로고    scopus 로고
    • A conserved leucine that constricts the pore through the capsid fivefold cylinder plays a central role in parvoviral infection
    • Farr GA, Tattersall P. A conserved leucine that constricts the pore through the capsid fivefold cylinder plays a central role in parvoviral infection. Virology 323(2), 243-256 (2004).
    • (2004) Virology , vol.323 , Issue.2 , pp. 243-256
    • Farr, G.A.1    Tattersall, P.2
  • 196
    • 0026681197 scopus 로고
    • Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface
    • Rosenfeld SJ, Yoshimoto K, Kajigaya S etal. Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface. J. Clin. Invest. 89(6), 2023-2029 (1992).
    • (1992) J. Clin. Invest. , vol.89 , Issue.6 , pp. 2023-2029
    • Rosenfeld, S.J.1    Yoshimoto, K.2    Kajigaya, S.3
  • 197
    • 33845389502 scopus 로고    scopus 로고
    • Conformational changes in the VP1-unique region of native human parvovirus B19 lead to exposure of internal sequences that play a role in virus neutralization and infectivity
    • Ros C, Gerber M, Kempf C. Conformational changes in the VP1-unique region of native human parvovirus B19 lead to exposure of internal sequences that play a role in virus neutralization and infectivity. J. Virol. 80(24), 12017-12024 (2006).
    • (2006) J. Virol. , vol.80 , Issue.24 , pp. 12017-12024
    • Ros, C.1    Gerber, M.2    Kempf, C.3
  • 198
    • 3042594845 scopus 로고    scopus 로고
    • Different susceptibility of B19 virus and mice minute virus to low pH treatment
    • Boschetti N, Niederhauser I, Kempf C, Stuhler A, Lower J, Blumel J. Different susceptibility of B19 virus and mice minute virus to low pH treatment. Transfusion 44(7), 1079-1086 (2004).
    • (2004) Transfusion , vol.44 , Issue.7 , pp. 1079-1086
    • Boschetti, N.1    Niederhauser, I.2    Kempf, C.3    Stuhler, A.4    Lower, J.5    Blumel, J.6
  • 199
    • 0036171821 scopus 로고    scopus 로고
    • Ubiquitination of both adeno-associated virus type2 and 5 capsid proteins affects the transduction efficiency of recombinant vectors
    • Yan Z, Zak R, Luxton GW, Ritchie TC, Bantel-Schaal U, Engelhardt JF. Ubiquitination of both adeno-associated virus type2 and 5 capsid proteins affects the transduction efficiency of recombinant vectors. J. Virol. 76(5), 2043-2053 (2002).
    • (2002) J. Virol. , vol.76 , Issue.5 , pp. 2043-2053
    • Yan, Z.1    Zak, R.2    Luxton, G.W.3    Ritchie, T.C.4    Bantel-Schaal, U.5    Engelhardt, J.F.6
  • 200
    • 2942752307 scopus 로고    scopus 로고
    • The ubiquitin-proteasome machinery is essential for nuclear translocation of incoming minute virus of mice
    • Ros C, Kempf C. The ubiquitin-proteasome machinery is essential for nuclear translocation of incoming minute virus of mice. Virology 324(2), 350-360 (2004).
    • (2004) Virology , vol.324 , Issue.2 , pp. 350-360
    • Ros, C.1    Kempf, C.2
  • 201
    • 0141632830 scopus 로고    scopus 로고
    • Exploitation of microtubule cytoskeleton and dynein during parvoviral traffic toward the nucleus
    • Suikkanen S, Aaltonen T, Nevalainen M etal. Exploitation of microtubule cytoskeleton and dynein during parvoviral traffic toward the nucleus. J. Virol. 77(19), 10270-10279 (2003).
    • (2003) J. Virol. , vol.77 , Issue.19 , pp. 10270-10279
    • Suikkanen, S.1    Aaltonen, T.2    Nevalainen, M.3
  • 202
    • 0036633929 scopus 로고    scopus 로고
    • Complementary roles of multiple nuclear targeting signals in the capsid proteins of the parvovirus minute virus of mice during assembly and onset of infection
    • Lombardo E, Ramirez JC, Garcia J, Almendral JM. Complementary roles of multiple nuclear targeting signals in the capsid proteins of the parvovirus minute virus of mice during assembly and onset of infection. J. Virol. 76(14), 7049-7059 (2002).
    • (2002) J. Virol. , vol.76 , Issue.14 , pp. 7049-7059
    • Lombardo, E.1    Ramirez, J.C.2    Garcia, J.3    Almendral, J.M.4
  • 203
    • 0036149891 scopus 로고    scopus 로고
    • The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection
    • Vihinen-Ranta M, Wang D, Weichert WS, Parrish CR. The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection. J. Virol. 76(4), 1884-1891 (2002).
    • (2002) J. Virol. , vol.76 , Issue.4 , pp. 1884-1891
    • Vihinen-Ranta, M.1    Wang, D.2    Weichert, W.S.3    Parrish, C.R.4
  • 204
    • 79955440194 scopus 로고    scopus 로고
    • Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle
    • Cohen S, Marr AK, Garcin P, Pante N. Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle. J. Virol. 85(10), 4863-4874 (2011).
    • (2011) J. Virol. , vol.85 , Issue.10 , pp. 4863-4874
    • Cohen, S.1    Marr, A.K.2    Garcin, P.3    Pante, N.4
  • 205
    • 33750279611 scopus 로고    scopus 로고
    • Parvoviral nuclear import: Bypassing the host nuclear-transport machinery
    • Cohen S, Behzad AR, Carroll JB, Pante N. Parvoviral nuclear import: Bypassing the host nuclear-transport machinery. J. Gen. Virol. 87(Pt11), 3209-3213 (2006).
    • (2006) J. Gen. Virol. , vol.87 , Issue.PART 11 , pp. 3209-3213
    • Cohen, S.1    Behzad, A.R.2    Carroll, J.B.3    Pante, N.4
  • 206
    • 28044462666 scopus 로고    scopus 로고
    • Pushing the envelope: Microinjection of minute virus of mice into Xenopus oocytes causes damage to the nuclear envelope
    • Cohen S, Pante N. Pushing the envelope: Microinjection of minute virus of mice into Xenopus oocytes causes damage to the nuclear envelope. J. Gen. Virol. 86(Pt 12), 3243-3252 (2005).
    • (2005) J. Gen. Virol. , vol.86 , Issue.PART 12 , pp. 3243-3252
    • Cohen, S.1    Pante, N.2
  • 207
    • 75449093577 scopus 로고    scopus 로고
    • Depletion of virion-associated divalent cations induces parvovirus minute virus of mice to eject its genome in a 3'-to-5' direction from an otherwise intact viral particle
    • Cotmore SF, Hafenstein S, Tattersall P. Depletion of virion-associated divalent cations induces parvovirus minute virus of mice to eject its genome in a 3'-to-5' direction from an otherwise intact viral particle. J. Virol. 84(4), 1945-1956 (2010).
    • (2010) J. Virol. , vol.84 , Issue.4 , pp. 1945-1956
    • Cotmore, S.F.1    Hafenstein, S.2    Tattersall, P.3
  • 208
    • 0033080393 scopus 로고    scopus 로고
    • Controlled conformational transitions in the MVM virion expose the VP1 N-terminus and viral genome without particle disassembly
    • Cotmore SF, D'Abramo AM Jr, Ticknor CM, Tattersall P. Controlled conformational transitions in the MVM virion expose the VP1 N-terminus and viral genome without particle disassembly. Virology 254(1), 169-181 (1999).
    • (1999) Virology , vol.254 , Issue.1 , pp. 169-181
    • Cotmore, S.F.1    D'Abramo Jr., A.M.2    Ticknor, C.M.3    Tattersall, P.4
  • 209
    • 0028855554 scopus 로고
    • Non-structural proteins of autonomous parvoviruses: From cellular effects to molecular mechanisms
    • Vanacker J-M, Rommelaere J. Non-structural proteins of autonomous parvoviruses: From cellular effects to molecular mechanisms. Semin. Virol. 6, 291-297 (1995).
    • (1995) Semin. Virol. , vol.6 , pp. 291-297
    • Vanacker, J.-M.1    Rommelaere, J.2
  • 210
    • 0030993261 scopus 로고    scopus 로고
    • The NS2 polypeptide of parvovirus MVM is required for capsid assembly in murine cells
    • Cotmore SF, D'Abramo AM Jr, Carbonell LF, Bratton J, Tattersall P. The NS2 polypeptide of parvovirus MVM is required for capsid assembly in murine cells. Virology 231(2), 267-280 (1997).
    • (1997) Virology , vol.231 , Issue.2 , pp. 267-280
    • Cotmore, S.F.1    D'Abramo Jr., A.M.2    Carbonell, L.F.3    Bratton, J.4    Tattersall, P.5
  • 211
    • 0036784610 scopus 로고    scopus 로고
    • The NS2 proteins of parvovirus minute virus of mice are required for efficient nuclear egress of progeny virions in mouse cells
    • Eichwald V, Daeffler L, Klein M, Rommelaere J, Salome N. The NS2 proteins of parvovirus minute virus of mice are required for efficient nuclear egress of progeny virions in mouse cells. J. Virol. 76(20), 10307-10319 (2002).
    • (2002) J. Virol. , vol.76 , Issue.20 , pp. 10307-10319
    • Eichwald, V.1    Daeffler, L.2    Klein, M.3    Rommelaere, J.4    Salome, N.5
  • 212
    • 0027397055 scopus 로고
    • NS2 is required for efficient translation of viral mRNA in minute virus of mice-infected murine cells
    • Naeger LK, Salome N, Pintel DJ. NS2 is required for efficient translation of viral mRNA in minute virus of mice-infected murine cells. J. Virol. 67(2), 1034-1043 (1993).
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 1034-1043
    • Naeger, L.K.1    Salome, N.2    Pintel, D.J.3
  • 213
    • 0027328283 scopus 로고
    • MVM(p) NS-2 protein expression is required with NS-1 for maximal cytotoxicity in human transformed cells
    • Legrand C, Rommelaere J, Caillet-Fauquet P. MVM(p) NS-2 protein expression is required with NS-1 for maximal cytotoxicity in human transformed cells. Virology 195(1), 149-155 (1993).
    • (1993) Virology , vol.195 , Issue.1 , pp. 149-155
    • Legrand, C.1    Rommelaere, J.2    Caillet-Fauquet, P.3
  • 214
    • 85080844666 scopus 로고    scopus 로고
    • Parvovirus DNA replication. Cold Spring Harbor Lab. 799-813 (1996). 215. Riolobos L, Reguera J, Mateu MG, Almendral JM. Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid
    • Cotmore SF, Tattersall P. Parvovirus DNA replication. Cold Spring Harbor Lab. 799-813 (1996).
    • (2006) J. Mol. Biol. , vol.357 , Issue.3 , pp. 1026-1038
    • Cotmore, S.F.1    Tattersall, P.2
  • 215
    • 33644943804 scopus 로고    scopus 로고
    • Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid
    • Riolobos L, Reguera J, Mateu MG, Almendral JM. Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid. J. Mol. Biol. 357(3), 1026-1038 (2006).
    • (2006) J. Mol. Biol. , vol.357 , Issue.3 , pp. 1026-1038
    • Riolobos, L.1    Reguera, J.2    Mateu, M.G.3    Almendral, J.M.4
  • 216
    • 17644446136 scopus 로고    scopus 로고
    • A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly
    • Lombardo E, Ramirez JC, Agbandje-McKenna M, Almendral JM. A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly. J. Virol. 74(8), 3804-3814 (2000).
    • (2000) J. Virol. , vol.74 , Issue.8 , pp. 3804-3814
    • Lombardo, E.1    Ramirez, J.C.2    Agbandje-McKenna, M.3    Almendral, J.M.4
  • 217
    • 0024409384 scopus 로고
    • A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles
    • Cotmore SF, Tattersall P. A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles. J. Virol. 63(9), 3902-3911 (1989).
    • (1989) J. Virol. , vol.63 , Issue.9 , pp. 3902-3911
    • Cotmore, S.F.1    Tattersall, P.2
  • 218
    • 24044442560 scopus 로고
    • Functional relevance of amino acid residues involved in interactions with ordered nucleic acid in a spherical virus. J. Biol. Chem. 280(18), 17969-17977 (2005). 219. Chen KC, Shull BC, Lederman M, Stout ER, Bates RC. Analysis of the termini of the DNA of bovine parvovirus: Demonstration of sequence inversion at the left terminus and its implication for the replication model
    • Reguera J, Grueso E, Carreira A, Sanchez-Martinez C, Almendral JM, Mateu MG. Functional relevance of amino acid residues involved in interactions with ordered nucleic acid in a spherical virus. J. Biol. Chem. 280(18), 17969-17977 (2005).
    • (1988) J. Virol. , vol.62 , Issue.10 , pp. 3807-3813
    • Reguera, J.1    Grueso, E.2    Carreira, A.3    Sanchez-Martinez, C.4    Almendral, J.M.5    Mateu, M.G.6
  • 219
    • 0023737289 scopus 로고
    • Analysis of the termini of the DNA of bovine parvovirus: Demonstration of sequence inversion at the left terminus and its implication for the replication model
    • Chen KC, Shull BC, Lederman M, Stout ER, Bates RC. Analysis of the termini of the DNA of bovine parvovirus: Demonstration of sequence inversion at the left terminus and its implication for the replication model. J. Virol. 62(10), 3807-3813 (1988).
    • (1988) J. Virol. , vol.62 , Issue.10 , pp. 3807-3813
    • Chen, K.C.1    Shull, B.C.2    Lederman, M.3    Stout, E.R.4    Bates, R.C.5
  • 220
    • 18044384804 scopus 로고    scopus 로고
    • Encapsidation of minute virus of mice DNA: Aspects of the translocation mechanism revealed by the structure of partially packaged genomes
    • Cotmore SF, Tattersall P. Encapsidation of minute virus of mice DNA: Aspects of the translocation mechanism revealed by the structure of partially packaged genomes. Virology 336(1), 100-112 (2005).
    • (2005) Virology , vol.336 , Issue.1 , pp. 100-112
    • Cotmore, S.F.1    Tattersall, P.2
  • 221
    • 13444259762 scopus 로고    scopus 로고
    • Genome packaging sense is controlled by the efficiency of the nick site in the right-end replication origin of parvoviruses minute virus of mice and LuIII
    • Cotmore SF, Tattersall P. Genome packaging sense is controlled by the efficiency of the nick site in the right-end replication origin of parvoviruses minute virus of mice and LuIII. J. Virol. 79(4), 2287-2300 (2005).
    • (2005) J. Virol. , vol.79 , Issue.4 , pp. 2287-2300
    • Cotmore, S.F.1    Tattersall, P.2
  • 222
    • 84855937996 scopus 로고    scopus 로고
    • Mutations at the base of the icosahedral five-fold cylinders of minute virus of mice induce 3'-to-5' genome uncoating and critically impair entry functions
    • Cotmore SF, Tattersall P. Mutations at the base of the icosahedral five-fold cylinders of minute virus of mice induce 3'-to-5' genome uncoating and critically impair entry functions. J. Virol. 86(1), 69-80 (2012).
    • (2012) J. Virol. , vol.86 , Issue.1 , pp. 69-80
    • Cotmore, S.F.1    Tattersall, P.2
  • 223
    • 79955438650 scopus 로고    scopus 로고
    • Structure of a packaging-defective mutant of minute virus of mice indicates that the genome is packaged via a pore at a 5-fold axis
    • Plevka P, Hafenstein S, Li L etal. Structure of a packaging-defective mutant of minute virus of mice indicates that the genome is packaged via a pore at a 5-fold axis. J. Virol. 85(10), 4822-4827 (2011).
    • (2011) J. Virol. , vol.85 , Issue.10 , pp. 4822-4827
    • Plevka, P.1    Hafenstein, S.2    Li, L.3
  • 224
    • 10644233763 scopus 로고    scopus 로고
    • The infectivity and lytic activity of minute virus of mice wild-type and derived vector particles are strikingly different
    • Lang SI, Boelz S, Stroh-Dege AY, Rommelaere J, Dinsart C, Cornelis JJ. The infectivity and lytic activity of minute virus of mice wild-type and derived vector particles are strikingly different. J. Virol. 79(1), 289-298 (2005).
    • (2005) J. Virol. , vol.79 , Issue.1 , pp. 289-298
    • Lang, S.I.1    Boelz, S.2    Stroh-Dege, A.Y.3    Rommelaere, J.4    Dinsart, C.5    Cornelis, J.J.6
  • 225
    • 0033166316 scopus 로고    scopus 로고
    • Cis requirements for the efficient production of recombinant DNA vectors based on autonomous parvoviruses
    • Kestler J, Neeb B, Struyf S etal. cis requirements for the efficient production of recombinant DNA vectors based on autonomous parvoviruses. Hum. Gene Ther. 10(10), 1619-1632 (1999).
    • (1999) Hum. Gene Ther. , vol.10 , Issue.10 , pp. 1619-1632
    • Kestler, J.1    Neeb, B.2    Struyf, S.3
  • 226
    • 0034469913 scopus 로고    scopus 로고
    • Phosphorylation status of the parvovirus minute virus of mice particle: Mapping and biological relevance of the major phosphorylation sites
    • Maroto B, Ramirez JC, Almendral JM. Phosphorylation status of the parvovirus minute virus of mice particle: Mapping and biological relevance of the major phosphorylation sites. J. Virol. 74(23), 10892-10902 (2000).
    • (2000) J. Virol. , vol.74 , Issue.23 , pp. 10892-10902
    • Maroto, B.1    Ramirez, J.C.2    Almendral, J.M.3
  • 227
    • 4544361834 scopus 로고    scopus 로고
    • Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface
    • Maroto B, Valle N, Saffrich R, Almendral JM. Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface. J. Virol. 78(19), 10685-10694 (2004).
    • (2004) J. Virol. , vol.78 , Issue.19 , pp. 10685-10694
    • Maroto, B.1    Valle, N.2    Saffrich, R.3    Almendral, J.M.4
  • 228
    • 0034652534 scopus 로고    scopus 로고
    • Biochemical and physical characterization of parvovirus minute virus of mice virus-like particles
    • Hernando E, Llamas-Saiz AL, Foces-Foces C etal. Biochemical and physical characterization of parvovirus minute virus of mice virus-like particles. Virology 267(2), 299-309 (2000).
    • (2000) Virology , vol.267 , Issue.2 , pp. 299-309
    • Hernando, E.1    Llamas-Saiz, A.L.2    Foces-Foces, C.3
  • 229
    • 0027487957 scopus 로고
    • Aleutian mink disease parvovirus infection of mink macrophages and human macrophage cell line U937: Demonstration of antibody-dependent enhancement of infection
    • Kanno H, Wolfinbarger JB, Bloom ME. Aleutian mink disease parvovirus infection of mink macrophages and human macrophage cell line U937: Demonstration of antibody-dependent enhancement of infection. J. Virol. 67(12), 7017-7024 (1993).
    • (1993) J. Virol. , vol.67 , Issue.12 , pp. 7017-7024
    • Kanno, H.1    Wolfinbarger, J.B.2    Bloom, M.E.3
  • 230
    • 0031748963 scopus 로고    scopus 로고
    • Vaccination with Aleutian mink disease parvovirus (AMDV) capsid proteins enhances disease, while vaccination with the major non-structural AMDV protein causes partial protection from disease
    • Aasted B, Alexandersen S, Christensen J. Vaccination with Aleutian mink disease parvovirus (AMDV) capsid proteins enhances disease, while vaccination with the major non-structural AMDV protein causes partial protection from disease. Vaccine 16(11-12), 1158-1165 (1998).
    • (1998) Vaccine , vol.16 , Issue.11-12 , pp. 1158-1165
    • Aasted, B.1    Alexandersen, S.2    Christensen, J.3
  • 231
    • 0031060515 scopus 로고    scopus 로고
    • Expression of Aleutian mink disease parvovirus capsid proteins in defined segments: Localization of immunoreactive sites and neutralizing epitopes to specific regions
    • Bloom ME, Martin DA, Oie KL etal. Expression of Aleutian mink disease parvovirus capsid proteins in defined segments: Localization of immunoreactive sites and neutralizing epitopes to specific regions. J. Virol. 71(1), 705-714 (1997).
    • (1997) J. Virol. , vol.71 , Issue.1 , pp. 705-714
    • Bloom, M.E.1    Martin, D.A.2    Oie, K.L.3
  • 232
    • 0015373802 scopus 로고
    • The pathogenesis of Aleutian disease of mink. II. Enhancement of tissue lesions following the administration of a killed virus vaccine or passive antibody
    • Porter DD, Larsen AE, Porter HG. The pathogenesis of Aleutian disease of mink. II. Enhancement of tissue lesions following the administration of a killed virus vaccine or passive antibody. J. Immunol. 109(1), 1-7 (1972).
    • (1972) J. Immunol. , vol.109 , Issue.1 , pp. 1-7
    • Porter, D.D.1    Larsen, A.E.2    Porter, H.G.3
  • 233
    • 0025990896 scopus 로고
    • Identification and mapping of neutralizing epitopes of human parvovirus B19 by using human antibodies
    • Sato H, Hirata J, Kuroda N, Shiraki H, Maeda Y, Okochi K. Identification and mapping of neutralizing epitopes of human parvovirus B19 by using human antibodies. J. Virol. 65(10), 5485-5490 (1991).
    • (1991) J. Virol. , vol.65 , Issue.10 , pp. 5485-5490
    • Sato, H.1    Hirata, J.2    Kuroda, N.3    Shiraki, H.4    Maeda, Y.5    Okochi, K.6
  • 234
    • 0026029619 scopus 로고
    • Identification of the region including the epitope for a monoclonal antibody which can neutralize human parvovirus B19
    • Sato H, Hirata J, Furukawa M etal. Identification of the region including the epitope for a monoclonal antibody which can neutralize human parvovirus B19. J. Virol. 65(4), 1667-1672 (1991).
    • (1991) J. Virol. , vol.65 , Issue.4 , pp. 1667-1672
    • Sato, H.1    Hirata, J.2    Furukawa, M.3
  • 235
    • 0026787952 scopus 로고
    • Haemagglutination by parvovirus B19
    • Brown KE, Cohen BJ. Haemagglutination by parvovirus B19. J. Gen. Virol. 73(Pt8), 2147-2149 (1992).
    • (1992) J. Gen. Virol. , vol.73 , Issue.PART 8 , pp. 2147-2149
    • Brown, K.E.1    Cohen, B.J.2
  • 236
    • 0027153992 scopus 로고
    • Neutralizing linear epitopes of B19 parvovirus cluster in the VP1unique and VP1-VP2 junction regions
    • Saikawa T, Anderson S, Momoeda M, Kajigaya S, Young NS. Neutralizing linear epitopes of B19 parvovirus cluster in the VP1unique and VP1-VP2 junction regions. J. Virol. 67(6), 3004-3009 (1993).
    • (1993) J. Virol. , vol.67 , Issue.6 , pp. 3004-3009
    • Saikawa, T.1    Anderson, S.2    Momoeda, M.3    Kajigaya, S.4    Young, N.S.5
  • 237
    • 0037321701 scopus 로고    scopus 로고
    • High mutant frequency in populations of a DNA virus allows evasion from antibody therapy in an immunodeficient host
    • Lopez-Bueno A, Mateu MG, Almendral JM. High mutant frequency in populations of a DNA virus allows evasion from antibody therapy in an immunodeficient host. J. Virol. 77(4), 2701-2708 (2003).
    • (2003) J. Virol. , vol.77 , Issue.4 , pp. 2701-2708
    • Lopez-Bueno, A.1    Mateu, M.G.2    Almendral, J.M.3
  • 238
    • 35348922312 scopus 로고    scopus 로고
    • Minute virus of mice, a parvovirus, in complex with the Fab fragment of a neutralizing monoclonal antibody
    • Kaufmann B, Lopez-Bueno A, Mateu MG etal. Minute virus of mice, a parvovirus, in complex with the Fab fragment of a neutralizing monoclonal antibody. J. Virol. 81(18), 9851-9858 (2007).
    • (2007) J. Virol. , vol.81 , Issue.18 , pp. 9851-9858
    • Kaufmann, B.1    Lopez-Bueno, A.2    Mateu, M.G.3
  • 239
    • 79551658540 scopus 로고    scopus 로고
    • Femtosecond x-ray protein nanocrystallography
    • Chapman HN, Fromme P, Barty A etal. Femtosecond x-ray protein nanocrystallography. Nature 470(7332), 73-77 (2011).
    • (2011) Nature , vol.470 , Issue.7332 , pp. 73-77
    • Chapman, H.N.1    Fromme, P.2    Barty, A.3
  • 240
    • 79551667263 scopus 로고    scopus 로고
    • Single mimivirus particles intercepted and imaged with an x-ray laser
    • Seibert MM, Ekeberg T, Maia FR etal. Single mimivirus particles intercepted and imaged with an x-ray laser. Nature 470(7332), 78-81 (2011).
    • (2011) Nature , vol.470 , Issue.7332 , pp. 78-81
    • Seibert, M.M.1    Ekeberg, T.2    Maia, F.R.3
  • 241
    • 79955867558 scopus 로고    scopus 로고
    • Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses
    • Yu X, Ge P, Jiang J, Atanasov I, Zhou ZH. Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses. Structure 19(5), 652-661 (2011).
    • (2011) Structure , vol.19 , Issue.5 , pp. 652-661
    • Yu, X.1    Ge, P.2    Jiang, J.3    Atanasov, I.4    Zhou, Z.H.5
  • 242
    • 73449134082 scopus 로고    scopus 로고
    • Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography
    • Peng L, Ryazantsev S, Sun R, Zhou ZH. Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography. Structure 18(1), 47-58 (2010).
    • (2010) Structure , vol.18 , Issue.1 , pp. 47-58
    • Peng, L.1    Ryazantsev, S.2    Sun, R.3    Zhou, Z.H.4
  • 244
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera -A visualization system for exploratory research and analysis
    • Pettersen EF, Goddard TD, Huang CC etal. UCSF Chimera -a visualization system for exploratory research and analysis. J. Comput. Chem. 25(13), 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3
  • 245
    • 34248172479 scopus 로고    scopus 로고
    • Interpretation of electron density with stereographic roadmap projections
    • Xiao C, Rossmann MG. Interpretation of electron density with stereographic roadmap projections. J. Struct. Biol. 158(2), 182-187 (2007).
    • (2007) J. Struct. Biol. , vol.158 , Issue.2 , pp. 182-187
    • Xiao, C.1    Rossmann, M.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.