메뉴 건너뛰기




Volumn 6, Issue 7, 2014, Pages 2899-2937

Coat as a dagger: The use of capsid proteins to perforate membranes during non-enveloped DNA viruses trafficking

Author keywords

Adenovirus; Capsid protein; Cell entry; Coat protein; Endosome escape; Membrane perforation; Papillomavirus; Parvovirus; Polyomavirus; Trafficking; Viroporins; Viruses

Indexed keywords

CAPSID PROTEIN; PHOSPHOLIPASE A2; PROTEIN VI; PROTEIN VP1; PROTEIN VP2; PROTEIN VP3; SERINE PROTEINASE INHIBITOR; SORTING NEXIN 17; UNCLASSIFIED DRUG; PROTEIN BINDING; VIRUS RECEPTOR;

EID: 84904977774     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v6072899     Document Type: Review
Times cited : (14)

References (235)
  • 1
    • 84890544306 scopus 로고    scopus 로고
    • Concepts of papillomavirus entry into host cells
    • Day, P.M.; Schelhaas, M. Concepts of papillomavirus entry into host cells. Curr. Opin. Virol. 2014, 4, 24-31.
    • (2014) Curr. Opin. Virol. , vol.4 , pp. 24-31
    • Day, P.M.1    Schelhaas, M.2
  • 2
    • 84867881070 scopus 로고    scopus 로고
    • Principlesof polyoma-and papillomavirus uncoating
    • Cerqueira, C.; Schelhaas, M. Principlesof polyoma-and papillomavirus uncoating. Med. Microbiol. Immunol. 2012, 201, 427-436.
    • (2012) Med. Microbiol. Immunol. , vol.201 , pp. 427-436
    • Cerqueira, C.1    Schelhaas, M.2
  • 3
    • 67649422214 scopus 로고    scopus 로고
    • Dna-tumor virus entry-from plasma membrane to the nucleus
    • Puntener, D.; Greber, U.F. Dna-tumor virus entry-from plasma membrane to the nucleus. Semin. Cell Dev. Biol. 2009, 20, 631-642.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 631-642
    • Puntener, D.1    Greber, U.F.2
  • 4
    • 84899010486 scopus 로고    scopus 로고
    • Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics
    • Benevento, M.; Di Palma, S.; Snijder, J.; Moyer, C.L.; Reddy, V.S.; Nemerow, G.R.; Heck, A.J. Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics. J. Biol. Chem. 2014, 289, 11421-11430.
    • (2014) J. Biol. Chem. , vol.289 , pp. 11421-11430
    • Benevento, M.1    Di Palma, S.2    Snijder, J.3    Moyer, C.L.4    Reddy, V.S.5    Nemerow, G.R.6    Heck, A.J.7
  • 5
    • 0027166647 scopus 로고
    • Integrin-alpha-v-beta-3 and integrinalpha-v-beta-5 promote adenovirus internalization but not virus attachment
    • Wickham, T.J.; Mathias, P.; Cheresh, D.A.; Nemerow, G.R. Integrin-alpha-v-beta-3 and integrinalpha-v-beta-5 promote adenovirus internalization but not virus attachment. Cell 1993, 73, 309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 6
    • 0028086074 scopus 로고
    • Multiple adenovirus serotypes use alpha-v integrins for infection
    • Mathias, P.; Wickham, T.; Moore, M.; Nemerow, G. Multiple adenovirus serotypes use alpha-v integrins for infection. J. Virol. 1994, 68, 6811-6814.
    • (1994) J. Virol. , vol.68 , pp. 6811-6814
    • Mathias, P.1    Wickham, T.2    Moore, M.3    Nemerow, G.4
  • 7
    • 0028987384 scopus 로고
    • Up-regulation of integrins alpha-v-beta-3 and alpha-vbeta-5 on human monocytes and t-lymphocytes facilitates adenovirus-mediated gene delivery
    • Huang, S.A.; Endo, R.I.; Nemerow, G.R. Up-regulation of integrins alpha-v-beta-3 and alpha-vbeta-5 on human monocytes and t-lymphocytes facilitates adenovirus-mediated gene delivery. J. Virol. 1995, 69, 2257-2263.
    • (1995) J. Virol. , vol.69 , pp. 2257-2263
    • Huang, S.A.1    Endo, R.I.2    Nemerow, G.R.3
  • 8
    • 0030610717 scopus 로고    scopus 로고
    • Integrin alpha 5 beta 1-mediated adenovirus infection is enhanced by the integrin-activating antibody ts2/16
    • Davison, E.; Diaz, R.M.; Hart, I.R.; Santis, G.; Marshall, J.F. Integrin alpha 5 beta 1-mediated adenovirus infection is enhanced by the integrin-activating antibody ts2/16. J. Virol. 1997, 71, 6204-6207.
    • (1997) J. Virol. , vol.71 , pp. 6204-6207
    • Davison, E.1    Diaz, R.M.2    Hart, I.R.3    Santis, G.4    Marshall, J.F.5
  • 9
    • 0032883208 scopus 로고    scopus 로고
    • Role of alpha(v) integrins in adenovirus cell entry and gene delivery
    • Nemerow, G.R.; Stewart, P.L. Role of alpha(v) integrins in adenovirus cell entry and gene delivery. Microbiol. Mol. Biol. Rev. 1999, 63, 725-734.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 725-734
    • Nemerow, G.R.1    Stewart, P.L.2
  • 10
    • 0031950120 scopus 로고    scopus 로고
    • Adenovirus internalization and infection require dynamin
    • Wang, K.N.; Huang, S.; Kapoor-Munshi, A.; Nemerow, G. Adenovirus internalization and infection require dynamin. J. Virol. 1998, 72, 3455-3458.
    • (1998) J. Virol. , vol.72 , pp. 3455-3458
    • Wang, K.N.1    Huang, S.2    Kapoor-Munshi, A.3    Nemerow, G.4
  • 12
    • 70449378795 scopus 로고    scopus 로고
    • Genetic reconstitution of the human adenovirus type 2 temperature-sensitive 1 mutant defective in endosomal escape
    • Imelli, N.; Ruzsics, Z.; Puntener, D.; Gastaldelli, M.; Greber, U.F. Genetic reconstitution of the human adenovirus type 2 temperature-sensitive 1 mutant defective in endosomal escape. Virol. J. 2009, 6, 174.
    • (2009) Virol. J. , vol.6 , pp. 174
    • Imelli, N.1    Ruzsics, Z.2    Puntener, D.3    Gastaldelli, M.4    Greber, U.F.5
  • 13
    • 0037119944 scopus 로고    scopus 로고
    • Adenovirus triggers macropinocytosis and endosomalleakage together withits clathrin-mediated uptake
    • Meier, O.; Boucke, K.; Hammer, S.V.; Keller, S.; Stidwill, R.P.; Hemmi, S.; Greber, U.F. Adenovirus triggers macropinocytosis and endosomalleakage together withits clathrin-mediated uptake. J. Cell Biol. 2002, 158, 1119-1131.
    • (2002) J. Cell Biol. , vol.158 , pp. 1119-1131
    • Meier, O.1    Boucke, K.2    Hammer, S.V.3    Keller, S.4    Stidwill, R.P.5    Hemmi, S.6    Greber, U.F.7
  • 15
    • 80051887181 scopus 로고    scopus 로고
    • Drifting motions of the adenovirus receptor car and immobile integrins initiate virus uncoating and membrane lytic protein exposure
    • Burckhardt, C.J.; Suomalainen, M.; Schoenenberger, P.; Boucke, K.; Hemmi, S.; Greber, U.F. Drifting motions of the adenovirus receptor car and immobile integrins initiate virus uncoating and membrane lytic protein exposure. Cell Host Microbe 2011, 10, 105-117.
    • (2011) Cell Host Microbe , vol.10 , pp. 105-117
    • Burckhardt, C.J.1    Suomalainen, M.2    Schoenenberger, P.3    Boucke, K.4    Hemmi, S.5    Greber, U.F.6
  • 16
    • 0033942486 scopus 로고    scopus 로고
    • The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol
    • Nakano, M.Y.; Boucke, K.; Suomalainen, M.; Stidwill, R.P.; Greber, U.F. The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol. J. Virol. 2000, 74, 7085-7095.
    • (2000) J. Virol. , vol.74 , pp. 7085-7095
    • Nakano, M.Y.1    Boucke, K.2    Suomalainen, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 17
    • 4444290419 scopus 로고    scopus 로고
    • Genome size and structure determine efficiency ofpostinternalization steps and gene transfer of capsid-modified adenovirus vectors in a cell-type-specific manner
    • Shayakhmetov, D.M.; Li, Z.Y.; Gaggar, A.; Gharwan, H.; Ternovoi, V.; Sandig, V.; Lieber, A. Genome size and structure determine efficiency ofpostinternalization steps and gene transfer of capsid-modified adenovirus vectors in a cell-type-specific manner. J. Virol. 2004, 78, 10009-10022.
    • (2004) J. Virol. , vol.78 , pp. 10009-10022
    • Shayakhmetov, D.M.1    Li, Z.Y.2    Gaggar, A.3    Gharwan, H.4    Ternovoi, V.5    Sandig, V.6    Lieber, A.7
  • 18
    • 11144242192 scopus 로고    scopus 로고
    • Deletion of penton rgd motifs affects the efficiency of both the internalization and the endosorne escape of viral particles containing adenovirus serotype 5 or 35 fiber knobs
    • Shayakhmetov, D.M.; Eberly, A.M.; Li, Z.Y.; Lieber, A. Deletion of penton rgd motifs affects the efficiency of both the internalization and the endosorne escape of viral particles containing adenovirus serotype 5 or 35 fiber knobs. J. Virol. 2005, 79, 1053-1061.
    • (2005) J. Virol. , vol.79 , pp. 1053-1061
    • Shayakhmetov, D.M.1    Eberly, A.M.2    Li, Z.Y.3    Lieber, A.4
  • 19
    • 0035154757 scopus 로고    scopus 로고
    • Adenovirus serotype 7 retention in a late endosomal compartment prior to cytosol escape is modulated by fiber protein
    • Miyazawa, N.; Crystal, R.G.; Leopold, P.L. Adenovirus serotype 7 retention in a late endosomal compartment prior to cytosol escape is modulated by fiber protein. J. Virol. 2001, 75, 1387-1400.
    • (2001) J. Virol. , vol.75 , pp. 1387-1400
    • Miyazawa, N.1    Crystal, R.G.2    Leopold, P.L.3
  • 20
    • 0033039503 scopus 로고    scopus 로고
    • Fiber swap between adenovirus subgroups b and c alters intracellular trafficking of adenovirus gene transfer vectors
    • Miyazawa, N.; Leopold, P.L.; Hackett, N.R.; Ferris, B.; Worgall, S.; Falck-Pedersen, E.; Crystal, R.G. Fiber swap between adenovirus subgroups b and c alters intracellular trafficking of adenovirus gene transfer vectors. J. Virol. 1999, 73, 6056-6065.
    • (1999) J. Virol. , vol.73 , pp. 6056-6065
    • Miyazawa, N.1    Leopold, P.L.2    Hackett, N.R.3    Ferris, B.4    Worgall, S.5    Falck-Pedersen, E.6    Crystal, R.G.7
  • 21
    • 4143085883 scopus 로고    scopus 로고
    • Adenovirus type-5 entry and disassemblyfollowed in living cells by fret, fluorescence anisotropy, and flim
    • Martin-Fernandez, M.; Longshaw, S.V.; Kirby, I.; Santis, G.; Tobin, M.J.; Clarke, D.T.; Jones, G.R. Adenovirus type-5 entry and disassemblyfollowed in living cells by fret, fluorescence anisotropy, and flim. Biophys. J. 2004, 87, 1316-1327.
    • (2004) Biophys. J. , vol.87 , pp. 1316-1327
    • Martin-Fernandez, M.1    Longshaw, S.V.2    Kirby, I.3    Santis, G.4    Tobin, M.J.5    Clarke, D.T.6    Jones, G.R.7
  • 22
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus-2 during entry into cells
    • Greber, U.F.; Willetts, M.; Webster, P.; Helenius, A. Stepwise dismantling of adenovirus-2 during entry into cells. Cell 1993, 75, 477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 23
    • 33846937818 scopus 로고    scopus 로고
    • Pu.1 redirects adenovirus to lysosomes in alveolar macrophages, uncoupling internalization from infection
    • Carey, B.; Staudt, M.K.; Bonaminio, D.; van der Loo, J.C.M.; Trapnell, B.C. Pu.1 redirects adenovirus to lysosomes in alveolar macrophages, uncoupling internalization from infection. J. Immunol. 2007, 178, 2440-2447.
    • (2007) J. Immunol. , vol.178 , pp. 2440-2447
    • Carey, B.1    Staudt, M.K.2    Bonaminio, D.3    van der Loo, J.C.M.4    Trapnell, B.C.5
  • 24
    • 33744478689 scopus 로고    scopus 로고
    • Photochemical treatment with endosomally localized photosensitizers enhances the number of adenoviruses in the nucleus
    • Engesaeter, B.O.; Tveito, S.; Bonsted, A.; Engebraaten, O.; Berg, K.; Maelandsmo, G.M. Photochemical treatment with endosomally localized photosensitizers enhances the number of adenoviruses in the nucleus. J. Gene Med. 2006, 8, 707-718.
    • (2006) J. Gene Med. , vol.8 , pp. 707-718
    • Engesaeter, B.O.1    Tveito, S.2    Bonsted, A.3    Engebraaten, O.4    Berg, K.5    Maelandsmo, G.M.6
  • 25
    • 84869028713 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of adenovirus membrane rupture and endosomal escape
    • Maier, O.; Marvin, S.A.; Wodrich, H.; Campbell, E.M.; Wiethoff, C.M. Spatiotemporal dynamics of adenovirus membrane rupture and endosomal escape. J. Virol. 2012, 86, 10821-10828.
    • (2012) J. Virol. , vol.86 , pp. 10821-10828
    • Maier, O.1    Marvin, S.A.2    Wodrich, H.3    Campbell, E.M.4    Wiethoff, C.M.5
  • 26
    • 56149117291 scopus 로고    scopus 로고
    • Infectious adenovirus type 2 transport through early but not late endosomes
    • Gastaldelli, M.; Imelli, N.; Boucke, K.; Amstutz, B.; Meier, O.; Greber, U.F. Infectious adenovirus type 2 transport through early but not late endosomes. Traffic 2008, 9, 2265-2278.
    • (2008) Traffic , vol.9 , pp. 2265-2278
    • Gastaldelli, M.1    Imelli, N.2    Boucke, K.3    Amstutz, B.4    Meier, O.5    Greber, U.F.6
  • 27
    • 0014605507 scopus 로고
    • Structure and development of viruses as observed in electron microscope. 10. Entry and uncoating of adenovirus
    • Morgan, C.; Rosenkra, H.S.; Mednis, B. Structure and development of viruses as observed in electron microscope. 10. Entry and uncoating of adenovirus. J. Virol. 1969, 4, 777-796.
    • (1969) J. Virol. , vol.4 , pp. 777-796
    • Morgan, C.1    Rosenkra, H.S.2    Mednis, B.3
  • 28
    • 0028107276 scopus 로고
    • Adenovirus-dependent release of choline from plasma-membrane vesicles at an acidic ph is mediated by the penton base protein
    • Seth, P. Adenovirus-dependent release of choline from plasma-membrane vesicles at an acidic ph is mediated by the penton base protein. J. Virol. 1994, 68, 1204-1206.
    • (1994) J. Virol. , vol.68 , pp. 1204-1206
    • Seth, P.1
  • 29
    • 0029154615 scopus 로고
    • Virus-mediated release of endosomal content in-vitro-Different behavior of adenovirus and rhinovirus serotype-2
    • Prchla, E.; Plank, C.; Wagner, E.; Blaas, D.; Fuchs, R. Virus-mediated release of endosomal content in-vitro-Different behavior of adenovirus and rhinovirus serotype-2. J. Cell Biol. 1995, 131, 111-123.
    • (1995) J. Cell Biol. , vol.131 , pp. 111-123
    • Prchla, E.1    Plank, C.2    Wagner, E.3    Blaas, D.4    Fuchs, R.5
  • 30
    • 84886031698 scopus 로고    scopus 로고
    • A direct and versatile assay measuring membrane penetration of adenovirus in single cells
    • Suomalainen, M.; Luisoni, S.; Boucke, K.; Bianchi, S.; Engel, D.A.; Greber, U.F. A direct and versatile assay measuring membrane penetration of adenovirus in single cells. J. Virol. 2013, 87, 12367-12379.
    • (2013) J. Virol. , vol.87 , pp. 12367-12379
    • Suomalainen, M.1    Luisoni, S.2    Boucke, K.3    Bianchi, S.4    Engel, D.A.5    Greber, U.F.6
  • 31
    • 28044448698 scopus 로고    scopus 로고
    • Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry
    • Farr, G.A.; Zhang, L.G.; Tattersall, P. Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry. Proc. Natl. Acad. Sci. USA 2005, 102, 17148-17153.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17148-17153
    • Farr, G.A.1    Zhang, L.G.2    Tattersall, P.3
  • 32
    • 84870689285 scopus 로고    scopus 로고
    • Reduced infectivity of adenovirus type 5 particles and degradation of entering viral genomes associated with incompleteprocessing of the preterminal protein
    • Kato, S.E.; Chahal, J.S.; Flint, S.J. Reduced infectivity of adenovirus type 5 particles and degradation of entering viral genomes associated with incompleteprocessing of the preterminal protein. J. Virol. 2012, 86, 13554-13565.
    • (2012) J. Virol. , vol.86 , pp. 13554-13565
    • Kato, S.E.1    Chahal, J.S.2    Flint, S.J.3
  • 33
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein vi mediates membrane disruption following capsid disassembly
    • Wiethoff, C.M.; Wodrich, H.; Gerace, L.; Nemerow, G.R. Adenovirus protein vi mediates membrane disruption following capsid disassembly. J. Virol. 2005, 79, 1992-2000.
    • (2005) J. Virol. , vol.79 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 34
    • 0029983628 scopus 로고    scopus 로고
    • The role of the adenovirus protease in virus entry into cells
    • Greber, U.F.; Webster, P.; Weber, J.; Helenius, A. The role of the adenovirus protease in virus entry into cells. EMBO J. 1996, 15, 1766-1777.
    • (1996) EMBO J. , vol.15 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 35
    • 0346243942 scopus 로고    scopus 로고
    • Switch from capsid protein import to adenovirus assembly by cleavage of nucleartransport signals
    • Wodrich, H.; Guan, T.L.; Cingolani, G.; Von Seggern, D.; Nemerow, G.; Gerace, L. Switch from capsid protein import to adenovirus assembly by cleavage of nucleartransport signals. EMBO J. 2003, 22, 6245-6255.
    • (2003) EMBO J. , vol.22 , pp. 6245-6255
    • Wodrich, H.1    Guan, T.L.2    Cingolani, G.3    Von Seggern, D.4    Nemerow, G.5    Gerace, L.6
  • 36
    • 84904987597 scopus 로고
    • The structure of the adenovirus capsid
    • Van Oostrum, J.; Burnett, R.M. The structure of the adenovirus capsid. Biophys. J. 1985, 47, 394A-394A.
    • (1985) Biophys. J. , vol.47
    • Van Oostrum, J.1    Burnett, R.M.2
  • 38
    • 19444365975 scopus 로고    scopus 로고
    • Cryoem structure at 9 angstrom resolution of an adenovirus vector targeted to hematopoietic cells
    • Saban, S.D.; Nepomuceno, R.R.; Gritton, L.D.; Nemerow, G.R.; Stewart, P.L. Cryoem structure at 9 angstrom resolution of an adenovirus vector targeted to hematopoietic cells. J. Mol. Biol. 2005, 349, 526-537.
    • (2005) J. Mol. Biol. , vol.349 , pp. 526-537
    • Saban, S.D.1    Nepomuceno, R.R.2    Gritton, L.D.3    Nemerow, G.R.4    Stewart, P.L.5
  • 39
    • 67650912075 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of adenovirus type 2 temperature-sensitive mutant 1 reveals insight into the cell entry defect
    • Silvestry, M.; Lindert, S.; Smith, J.G.; Maier, O.; Wiethoff, C.M.; Nemerow, G.R.; Stewart, P.L. Cryo-electron microscopy structure of adenovirus type 2 temperature-sensitive mutant 1 reveals insight into the cell entry defect. J. Virol. 2009, 83, 7375-7383.
    • (2009) J. Virol. , vol.83 , pp. 7375-7383
    • Silvestry, M.1    Lindert, S.2    Smith, J.G.3    Maier, O.4    Wiethoff, C.M.5    Nemerow, G.R.6    Stewart, P.L.7
  • 40
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-em reveals interactions among protein networks
    • Liu, H.R.; Jin, L.; Koh, S.B.S.; Atanasov, I.; Schein, S.; Wu, L.; Zhou, Z.H. Atomic structure of human adenovirus by cryo-em reveals interactions among protein networks. Science 2010, 329, 1038-1043.
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.R.1    Jin, L.2    Koh, S.B.S.3    Atanasov, I.4    Schein, S.5    Wu, L.6    Zhou, Z.H.7
  • 41
    • 0027390796 scopus 로고
    • Viral-dna and a viral peptide can act as cofactors of adenovirus virion proteinase activity
    • Mangel, W.F.; McGrath, W.J.; Toledo, D.L.; Anderson, C.W. Viral-dna and a viral peptide can act as cofactors of adenovirus virion proteinase activity. Nature 1993, 361, 274-275.
    • (1993) Nature , vol.361 , pp. 274-275
    • Mangel, W.F.1    McGrath, W.J.2    Toledo, D.L.3    Anderson, C.W.4
  • 43
    • 79952419255 scopus 로고    scopus 로고
    • Functional genetic and biophysical analyses of membranedisruption by human adenovirus
    • Moyer, C.L.; Wiethoff, C.M.; Maier, O.; Smith, J.G.; Nemerow, G.R. Functional genetic and biophysical analyses of membranedisruption by human adenovirus. J. Virol. 2011, 85, 2631-2641.
    • (2011) J. Virol. , vol.85 , pp. 2631-2641
    • Moyer, C.L.1    Wiethoff, C.M.2    Maier, O.3    Smith, J.G.4    Nemerow, G.R.5
  • 44
    • 84860585580 scopus 로고    scopus 로고
    • Disulfide-bond formation by a single cysteine mutation in adenovirus protein vi impairs capsid release and membrane lysis
    • Moyer, C.L.; Nemerow, G.R. Disulfide-bond formation by a single cysteine mutation in adenovirus protein vi impairs capsid release and membrane lysis. Virology 2012, 428, 41-47.
    • (2012) Virology , vol.428 , pp. 41-47
    • Moyer, C.L.1    Nemerow, G.R.2
  • 45
    • 77952577600 scopus 로고    scopus 로고
    • An n-terminal domain of adenovirus protein vi fragments membranes by inducing positive membrane curvature
    • Maier, O.; Galan, D.L.; Wodrich, H.; Wiethoff, C.M. An n-terminal domain of adenovirus protein vi fragments membranes by inducing positive membrane curvature. Virology 2010, 402, 11-19.
    • (2010) Virology , vol.402 , pp. 11-19
    • Maier, O.1    Galan, D.L.2    Wodrich, H.3    Wiethoff, C.M.4
  • 46
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz, T. Defensins: Antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 2003, 3, 710-720.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 710-720
    • Ganz, T.1
  • 47
    • 77950470139 scopus 로고    scopus 로고
    • Direct evidence from single-cell analysis that human alpha-defensins block adenovirus uncoating to neutralize infection
    • Nguyen, E.K.; Nemerow, G.R.; Smith, J.G. Direct evidence from single-cell analysis that human alpha-defensins block adenovirus uncoating to neutralize infection. J. Virol. 2010, 84, 4041-4049.
    • (2010) J. Virol. , vol.84 , pp. 4041-4049
    • Nguyen, E.K.1    Nemerow, G.R.2    Smith, J.G.3
  • 48
    • 77954682175 scopus 로고    scopus 로고
    • Insight into the mechanisms of adenovirus capsid disassembly from studies of defensin neutralization
    • Smith, J.G.; Silvestry, M.; Lindert, S.; Lu, W.Y.; Nemerow, G.R.; Stewart, P.L. Insight into the mechanisms of adenovirus capsid disassembly from studies of defensin neutralization. PLoS Pathog. 2010, 6, e1000959
    • (2010) PLoS Pathog. , vol.6
    • Smith, J.G.1    Silvestry, M.2    Lindert, S.3    Lu, W.Y.4    Nemerow, G.R.5    Stewart, P.L.6
  • 49
    • 84876441987 scopus 로고    scopus 로고
    • An intrinsically disordered region of the adenovirus capsid is implicated in neutralization by human alpha defensin 5
    • Flatt, J.W.; Kim, R.; Smith, J.G.; Nemerow, G.R.; Stewart, P.L. An intrinsically disordered region of the adenovirus capsid is implicated in neutralization by human alpha defensin 5. PLoS One 2013, 8, e61571.
    • (2013) PLoS One , vol.8
    • Flatt, J.W.1    Kim, R.2    Smith, J.G.3    Nemerow, G.R.4    Stewart, P.L.5
  • 50
  • 51
    • 75149142941 scopus 로고    scopus 로고
    • Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit
    • Bremner, K.H.; Scherer, J.; Yi, J.L.; Vershinin, M.; Gross, S.P.; Vallee, R.B. Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit. Cell Host Microbe 2009, 6, 523-535.
    • (2009) Cell Host Microbe , vol.6 , pp. 523-535
    • Bremner, K.H.1    Scherer, J.2    Yi, J.L.3    Vershinin, M.4    Gross, S.P.5    Vallee, R.B.6
  • 52
    • 0035868714 scopus 로고    scopus 로고
    • Adenovirus-activated pka and p38/mapk pathways boost microtubule-mediated nuclear targeting of virus
    • Suomalainen, M.; Nakano, M.Y.; Boucke, K.; Keller, S.; Greber, U.F. Adenovirus-activated pka and p38/mapk pathways boost microtubule-mediated nuclear targeting of virus. EMBO J. 2001, 20, 1310-1319.
    • (2001) EMBO J. , vol.20 , pp. 1310-1319
    • Suomalainen, M.1    Nakano, M.Y.2    Boucke, K.3    Keller, S.4    Greber, U.F.5
  • 53
    • 0039174260 scopus 로고    scopus 로고
    • Nuclear import adenovirus dna in vitro involves the nuclear protein import pathway and hsc70
    • Saphire, A.C.S.; Guan, T.L.; Schirmer, E.C.; Nemerow, G.R.; Gerace, L. Nuclear import adenovirus dna in vitro involves the nuclear protein import pathway and hsc70. J. Biol. Chem. 2000, 275, 4298-4304.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4298-4304
    • Saphire, A.C.S.1    Guan, T.L.2    Schirmer, E.C.3    Nemerow, G.R.4    Gerace, L.5
  • 54
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus dna involves the nuclear pore complex receptor can/nup214 and histone h1
    • Trotman, L.C.; Mosberger, N.; Fornerod, M.; Stidwill, R.P.; Greber, U.F. Import of adenovirus dna involves the nuclear pore complex receptor can/nup214 and histone h1. Nat. Cell Biol. 2001, 3, 1092-1100.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 55
    • 34548561643 scopus 로고    scopus 로고
    • A role for transportin in the nuclear import of adenovirus core proteins and dna
    • Hindley, C.E.; Lawrence, F.J.; Matthews, D.A. A role for transportin in the nuclear import of adenovirus core proteins and dna. Traffic 2007, 8, 1313-1322.
    • (2007) Traffic , vol.8 , pp. 1313-1322
    • Hindley, C.E.1    Lawrence, F.J.2    Matthews, D.A.3
  • 56
    • 19644366017 scopus 로고    scopus 로고
    • Nuclear targeting of adenovirus type 2 requires crm1-mediated nuclear export
    • Strunze, S.; Trotman, L.C.; Boucke, K.; Greber, U.F. Nuclear targeting of adenovirus type 2 requires crm1-mediated nuclear export. Mol. Biol. Cell 2005, 16, 2999-3009.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2999-3009
    • Strunze, S.1    Trotman, L.C.2    Boucke, K.3    Greber, U.F.4
  • 57
    • 0023218357 scopus 로고
    • Characterization of capsid and noncapsid proteins of b19 parvovirus propagated in human erythroid bone-marrow cell-cultures
    • Ozawa, K.; Young, N. Characterization of capsid and noncapsid proteins of b19 parvovirus propagated in human erythroid bone-marrow cell-cultures. J. Virol. 1987, 61, 2627-2630.
    • (1987) J. Virol. , vol.61 , pp. 2627-2630
    • Ozawa, K.1    Young, N.2
  • 58
    • 0017107506 scopus 로고
    • 3 structural polypeptides coded for by minute virus of mice, a parvovirus
    • Tattersall, P.; Cawte, P.J.; Shatkin, A.J.; Ward, D.C. 3 structural polypeptides coded for by minute virus of mice, a parvovirus. J. Virol. 1976, 20, 273-289.
    • (1976) J. Virol. , vol.20 , pp. 273-289
    • Tattersall, P.1    Cawte, P.J.2    Shatkin, A.J.3    Ward, D.C.4
  • 59
    • 0023065751 scopus 로고
    • The autonomously replicating parvoviruses of vertebrates
    • Cotmore, S.F.; Tattersall, P. The autonomously replicating parvoviruses of vertebrates. Adv. Virus Res. 1987, 33, 91-174.
    • (1987) Adv. Virus Res. , vol.33 , pp. 91-174
    • Cotmore, S.F.1    Tattersall, P.2
  • 60
    • 0020460257 scopus 로고
    • Canineparvovirus-A biochemical and ultrastructural characterization
    • Paradiso, P.R.; Rhode, S.L.; Singer, II. Canineparvovirus-A biochemical and ultrastructural characterization. J. Gen. Virol. 1982, 62, 113-125.
    • (1982) J. Gen. Virol. , vol.62 , pp. 113-125
    • Paradiso, P.R.1    Rhode, S.L.2    Singer, I.I.3
  • 61
    • 0015156647 scopus 로고
    • Structural proteins ofadenovirus-associated viruses
    • Rose, J.A.; Maizel, J.V.; Inman, J.K.; Shatkin, A.J. Structural proteins ofadenovirus-associated viruses. J. Virol. 1971, 8, 766-770.
    • (1971) J. Virol. , vol.8 , pp. 766-770
    • Rose, J.A.1    Maizel, J.V.2    Inman, J.K.3    Shatkin, A.J.4
  • 62
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett, J.S.; Wilcher, R.; Samulski, R.J. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 2000, 74, 2777-2785.
    • (2000) J. Virol. , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 63
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions
    • Summerford, C.; Samulski, R.J. Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions. J. Virol. 1998, 72, 1438-1445.
    • (1998) J. Virol. , vol.72 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 64
    • 0035085754 scopus 로고    scopus 로고
    • Canine and feline parvoviruses can use human or feline transferrin receptors to bind, enter, and infect cells
    • Parker, J.S.L.; Murphy, W.J.; Wang, D.; O'Brien, S.J.; Parrish, C.R. Canine and feline parvoviruses can use human or feline transferrin receptors to bind, enter, and infect cells. J. Virol. 2001, 75, 3896-3902.
    • (2001) J. Virol. , vol.75 , pp. 3896-3902
    • Parker, J.S.L.1    Murphy, W.J.2    Wang, D.3    O'Brien, S.J.4    Parrish, C.R.5
  • 65
    • 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, J.S.L.; Weichert, W.S.; Geisel, R.E.; Sgro, J.Y.; Parrish, C.R. The natural host range shift and subsequent evolution of canine parvovirus resulted from virus-specific binding to the canine transferrin receptor. J. Virol. 2003, 77, 1718-1726.
    • (2003) J. Virol. , vol.77 , pp. 1718-1726
    • Hueffer, K.1    Parker, J.S.L.2    Weichert, W.S.3    Geisel, R.E.4    Sgro, J.Y.5    Parrish, C.R.6
  • 67
    • 0027686846 scopus 로고
    • Erythrocyte-p antigen-Cellular receptor for b19 parvovirus
    • Brown, K.E.; Anderson, S.M.; Young, N.S. Erythrocyte-p antigen-Cellular receptor for b19 parvovirus. Science 1993, 262, 114-117.
    • (1993) Science , vol.262 , pp. 114-117
    • Brown, K.E.1    Anderson, S.M.2    Young, N.S.3
  • 69
    • 0345257726 scopus 로고    scopus 로고
    • Alpha 5 beta 1 integrin as a cellular coreceptor for human parvovirus b19: Requirement of functional activation of beta 1 integrin for viral entry
    • Weigel-Kelley, K.A.; Yoder, M.C.; Srivastava, A. Alpha 5 beta 1 integrin as a cellular coreceptor for human parvovirus b19: Requirement of functional activation of beta 1 integrin for viral entry. Blood 2003, 102, 3927-3933.
    • (2003) Blood , vol.102 , pp. 3927-3933
    • Weigel-Kelley, K.A.1    Yoder, M.C.2    Srivastava, A.3
  • 70
    • 0032737034 scopus 로고    scopus 로고
    • Dynamin is required for recombinant adeno-associatedvirus type 2 infection
    • Duan, D.S.; Li, Q.; Kao, A.W.; Yue, Y.P.; Pessin, J.E.; Engelhardt, J.F. Dynamin is required for recombinant adeno-associatedvirus type 2 infection. J. Virol. 1999, 73, 10371-10376.
    • (1999) J. Virol. , vol.73 , pp. 10371-10376
    • Duan, D.S.1    Li, Q.2    Kao, A.W.3    Yue, Y.P.4    Pessin, J.E.5    Engelhardt, J.F.6
  • 71
    • 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, J.S.L.; Parrish, C.R. Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J. Virol. 2000, 74, 1919-1930.
    • (2000) J. Virol. , vol.74 , pp. 1919-1930
    • Parker, J.S.L.1    Parrish, C.R.2
  • 72
    • 0036174267 scopus 로고    scopus 로고
    • Endocytosis of adeno-associated virus type 5 leads to accumulation of virus particles in the golgi compartment
    • 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. 2002, 76, 2340-2349.
    • (2002) J. Virol. , vol.76 , pp. 2340-2349
    • Bantel-Schaal, U.1    Hub, B.2    Kartenbeck, J.3
  • 74
    • 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. 2009, 90, 317-322.
    • (2009) J. Gen. Virol. , vol.90 , pp. 317-322
    • Bantel-Schaal, U.1    Braspenning-Wesch, I.2    Kartenbeck, J.3
  • 75
    • 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. 2010, 84, 7782-7792.
    • (2010) J. Virol. , vol.84 , pp. 7782-7792
    • Boisvert, M.1    Fernandes, S.2    Tijssen, P.3
  • 78
    • 0034000922 scopus 로고    scopus 로고
    • Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport
    • Vihinen-Ranta, M.; Yuan, W.; Parrish, C.R. Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport. J. Virol. 2000, 74, 4853-4859.
    • (2000) J. Virol. , vol.74 , pp. 4853-4859
    • Vihinen-Ranta, M.1    Yuan, W.2    Parrish, C.R.3
  • 80
    • 0033799367 scopus 로고    scopus 로고
    • Endocytosis and nuclear trafficking of adeno-associated virus type 2 are controlled by rac1 and phosphatidylinositol-3 kinase activation
    • Sanlioglu, S.; Benson, P.K.; Yang, J.S.; Atkinson, E.M.; Reynolds, T.; Engelhardt, J.F. Endocytosis and nuclear trafficking of adeno-associated virus type 2 are controlled by rac1 and phosphatidylinositol-3 kinase activation. J. Virol. 2000, 74, 9184-9196.
    • (2000) J. Virol. , vol.74 , pp. 9184-9196
    • Sanlioglu, S.1    Benson, P.K.2    Yang, J.S.3    Atkinson, E.M.4    Reynolds, T.5    Engelhardt, J.F.6
  • 81
    • 38949202609 scopus 로고    scopus 로고
    • Sphingomyelin induces structural alteration in canine parvovirus capsid
    • Pakkanen, K.; Karttunen, J.; Virtanen, S.; Vuento, M. Sphingomyelin induces structural alteration in canine parvovirus capsid. Virus Res. 2008, 132, 187-191.
    • (2008) Virus Res. , vol.132 , pp. 187-191
    • Pakkanen, K.1    Karttunen, J.2    Virtanen, S.3    Vuento, M.4
  • 82
    • 30344459715 scopus 로고    scopus 로고
    • Low ph-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the vp1n-terminal sequence (n-vp1), n-vp2 cleavage, and uncoating of the fulllength genome
    • Mani, B.; Baltzer, C.; Valle, N.; Almendral, J.M.; Kempf, C.; Ros, C. Low ph-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the vp1n-terminal sequence (n-vp1), n-vp2 cleavage, and uncoating of the fulllength genome. J. Virol. 2006, 80, 1015-1024.
    • (2006) J. Virol. , vol.80 , pp. 1015-1024
    • Mani, B.1    Baltzer, C.2    Valle, N.3    Almendral, J.M.4    Kempf, C.5    Ros, C.6
  • 83
    • 30844451241 scopus 로고    scopus 로고
    • Parvovirus uncoating in vitro 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 in vitro reveals a mechanism of dna release without capsid disassembly and striking differences in encapsidated dna stability. Virology 2006, 345, 137-147.
    • (2006) Virology , vol.345 , pp. 137-147
    • Ros, C.1    Baltzer, C.2    Mani, B.3    Kempf, C.4
  • 85
    • 33750712806 scopus 로고    scopus 로고
    • Adeno-associated virus type 2 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, J.A. Adeno-associated virus type 2 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. 2006, 80, 11040-11054.
    • (2006) J. Virol. , vol.80 , pp. 11040-11054
    • Sonntag, F.1    Bleker, S.2    Leuchs, B.3    Fischer, R.4    Kleinschmidt, J.A.5
  • 86
    • 33645994480 scopus 로고    scopus 로고
    • Vp2 cleavage and the leucine ring at the base of the fivefold cylinder control ph-dpendent externalization of both the vp1 n terminus and the genome of minute virus of mice
    • Farr, G.A.; Cotmore, S.F.; Tattersall, P. Vp2 cleavage and the leucine ring at the base of the fivefold cylinder control ph-dpendent externalization of both the vp1 n terminus and the genome of minute virus of mice. J. Virol. 2006, 80, 161-171.
    • (2006) J. Virol. , vol.80 , pp. 161-171
    • Farr, G.A.1    Cotmore, S.F.2    Tattersall, P.3
  • 87
    • 0032505630 scopus 로고    scopus 로고
    • Assaying for structural variation in the parvovirus capsid and its role in infection
    • Weichert, W.S.; Parker, J.S.L.; Wahid, A.T.M.; Chang, S.F.; Meier, E.; Parrish, C.R. Assaying for structural variation in the parvovirus capsid and its role in infection. Virology 1998, 250, 106-117.
    • (1998) Virology , vol.250 , pp. 106-117
    • Weichert, W.S.1    Parker, J.S.L.2    Wahid, A.T.M.3    Chang, S.F.4    Meier, E.5    Parrish, C.R.6
  • 88
    • 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, S.F.; 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. 2010, 84, 1945-1956.
    • (2010) J. Virol. , vol.84 , pp. 1945-1956
    • Cotmore, S.F.1    Hafenstein, S.2    Tattersall, P.3
  • 89
    • 84905024566 scopus 로고    scopus 로고
    • The vp1n-terminal sequence of canine parvovirus is important for efficient cell infection
    • Vihinen-Ranta, M.; Yuan, W.; Weichert, W.; Vuento, M.; Parrish, C.R. The vp1n-terminal sequence of canine parvovirus is important for efficient cell infection. Mol. Biol. Cell 2000, 11, 291A-291A.
    • (2000) Mol. Biol. Cell , vol.11
    • Vihinen-Ranta, M.1    Yuan, W.2    Weichert, W.3    Vuento, M.4    Parrish, C.R.5
  • 90
    • 0036149891 scopus 로고    scopus 로고
    • The vp1n-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection
    • Vihinen-Ranta, M.; Wang, D.; Weichert, W.S.; Parrish, C.R. The vp1n-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection. J. Virol. 2002, 76, 1884-1891.
    • (2002) J. Virol. , vol.76 , pp. 1884-1891
    • Vihinen-Ranta, M.1    Wang, D.2    Weichert, W.S.3    Parrish, C.R.4
  • 91
    • 2942624232 scopus 로고    scopus 로고
    • A conserved leucine that constricts the pore through the capsid fivefold cylinder plays a central rolein parvoviral infection
    • Farr, G.A.; Tattersall, P. A conserved leucine that constricts the pore through the capsid fivefold cylinder plays a central rolein parvoviral infection. Virology 2004, 323, 243-256.
    • (2004) Virology , vol.323 , pp. 243-256
    • Farr, G.A.1    Tattersall, P.2
  • 92
    • 0033080393 scopus 로고    scopus 로고
    • Controlled conformational transitions in the mvm virion expose the vp1 n-terminus and viral genome without particle disassembly
    • Cotmore, S.F.; D'Abramo, A.M.; Ticknor, C.M.; Tattersall, P. Controlled conformational transitions in the mvm virion expose the vp1 n-terminus and viral genome without particle disassembly. Virology 1999, 254, 169-181.
    • (1999) Virology , vol.254 , pp. 169-181
    • Cotmore, S.F.1    D'Abramo, A.M.2    Ticknor, C.M.3    Tattersall, P.4
  • 93
    • 33846324384 scopus 로고    scopus 로고
    • A twohybrid screen identifies cathepsins b and l as uncoating factors for adeno-associated virus 2 and 8
    • Akache, B.; Grimm, D.; Shen, X.; Fuess, S.; Yant, S.R.; Glazer, D.S.; Park, J.; Kay, M.A. A twohybrid screen identifies cathepsins b and l as uncoating factors for adeno-associated virus 2 and 8. Mol. Ther. 2007, 15, 330-339.
    • (2007) Mol. Ther. , vol.15 , pp. 330-339
    • Akache, B.1    Grimm, D.2    Shen, X.3    Fuess, S.4    Yant, S.R.5    Glazer, D.S.6    Park, J.7    Kay, M.A.8
  • 95
    • 0036246727 scopus 로고    scopus 로고
    • The vp1 capsid protein of adeno-associatedvirus type 2 is carrying a phospholipase a2 domain required for virus infectivity
    • Girod, A.; Wobus, C.E.; Zadori, Z.; Ried, M.; Leike, K.; Tijssen, P.; Kleinschmidt, J.A.; Hallek, M. The vp1 capsid protein of adeno-associatedvirus type 2 is carrying a phospholipase a2 domain required for virus infectivity. J. Gen. Virol. 2002, 83, 973-978.
    • (2002) J. Gen. Virol. , vol.83 , pp. 973-978
    • Girod, A.1    Wobus, C.E.2    Zadori, Z.3    Ried, M.4    Leike, K.5    Tijssen, P.6    Kleinschmidt, J.A.7    Hallek, M.8
  • 96
    • 0031464535 scopus 로고    scopus 로고
    • Characterization of a nuclear localization signal of canine parvovirus capsid proteins
    • VihinenRanta, M.; Kakkola, L.; Kalela, A.; Vilja, P.; Vuento, M. Characterization of a nuclear localization signal of canine parvovirus capsid proteins. Eur. J. Biochem. 1997, 250, 389-394.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 389-394
    • VihinenRanta, M.1    Kakkola, L.2    Kalela, A.3    Vilja, P.4    Vuento, M.5
  • 99
    • 32044453585 scopus 로고    scopus 로고
    • Activation of synoviocytes by the secreted phospholipase a(2) motif in the vp1-unique region of parvovirus b19 minor capsid protein
    • Lu, J.; Zhi, N.; Wong, S.; Brown, K.E. Activation of synoviocytes by the secreted phospholipase a(2) motif in the vp1-unique region of parvovirus b19 minor capsid protein. J. Infect. Dis. 2006, 193, 582-590.
    • (2006) J. Infect. Dis. , vol.193 , pp. 582-590
    • Lu, J.1    Zhi, N.2    Wong, S.3    Brown, K.E.4
  • 100
    • 0242636439 scopus 로고    scopus 로고
    • Recent advances inmolecular biology and physiology of the prostaglandin e-2-biosynthetic pathway
    • Murakami, M.; Kudo, I. Recent advances inmolecular biology and physiology of the prostaglandin e-2-biosynthetic pathway. Prog. Lipid Res. 2004, 43, 3-35.
    • (2004) Prog. Lipid Res. , vol.43 , pp. 3-35
    • Murakami, M.1    Kudo, I.2
  • 102
    • 78649447518 scopus 로고    scopus 로고
    • Intrinsic phospholipase a2 activity ofadeno-associated virus is involved in endosomal escape of incoming particles
    • Stahnke, S.; Lux, K.; Uhrig, S.; Kreppel, F.; Hosel, M.; Coutelle, O.; Ogris, M.; Hallek, M.; Buning, H. Intrinsic phospholipase a2 activity ofadeno-associated virus is involved in endosomal escape of incoming particles. Virology 2011, 409, 77-83.
    • (2011) Virology , vol.409 , pp. 77-83
    • Stahnke, S.1    Lux, K.2    Uhrig, S.3    Kreppel, F.4    Hosel, M.5    Coutelle, O.6    Ogris, M.7    Hallek, M.8    Buning, H.9
  • 104
    • 84876196584 scopus 로고    scopus 로고
    • The determinants for the enzyme activity of human parvovirus b19 phospholipase a2 (pla2) and its influence on cultured cells
    • Deng, X.F.; Dong, Y.M.; Yi, Q.H.; Huang, Y.; Zhao, D.; Yang, Y.B.; Tijssen, P.; Qiu, J.M.; Liu, K.Y.; Li, Y. The determinants for the enzyme activity of human parvovirus b19 phospholipase a2 (pla2) and its influence on cultured cells. PLoS One 2013, 8, e61440.
    • (2013) PLoS One , vol.8
    • Deng, X.F.1    Dong, Y.M.2    Yi, Q.H.3    Huang, Y.4    Zhao, D.5    Yang, Y.B.6    Tijssen, P.7    Qiu, J.M.8    Liu, K.Y.9    Li, Y.10
  • 106
    • 56449098532 scopus 로고    scopus 로고
    • Interaction ofparvovirus b19 with humanerythrocytes alters virus structure and cell membrane integrity
    • Bonsch, C.; Kempf, C.; Ros, C. Interaction ofparvovirus b19 with humanerythrocytes alters virus structure and cell membrane integrity. J. Virol. 2008, 82, 11784-11791.
    • (2008) J. Virol. , vol.82 , pp. 11784-11791
    • Bonsch, C.1    Kempf, C.2    Ros, C.3
  • 107
    • 33750684707 scopus 로고    scopus 로고
    • Phospholipase a2 activity-dependent stimulation of ca2+ entry by human parvovirus b19 capsid protein vp1
    • Lupescu, A.; Bock, C.T.; Lang, P.A.; Aberle, S.; Kaiser, H.; Kandolf, R.; Lang, F. Phospholipase a2 activity-dependent stimulation of ca2+ entry by human parvovirus b19 capsid protein vp1. J. Virol. 2006, 80, 11370-11380.
    • (2006) J. Virol. , vol.80 , pp. 11370-11380
    • Lupescu, A.1    Bock, C.T.2    Lang, P.A.3    Aberle, S.4    Kaiser, H.5    Kandolf, R.6    Lang, F.7
  • 110
    • 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.; Perabo, L.; Goldnau, D.; Endell, J.; Leike, K.; Kofler, D.M.; Finke, S.; Hallek, M.; et al. Green fluorescent protein-tagged adeno-associated virus particles allow the study of cytosolic and nuclear trafficking. J. Virol. 2005, 79, 11776-11787.
    • (2005) J. Virol. , vol.79 , pp. 11776-11787
    • Lux, K.1    Goerlitz, N.2    Schlemminger, S.3    Perabo, L.4    Goldnau, D.5    Endell, J.6    Leike, K.7    Kofler, D.M.8    Finke, S.9    Hallek, M.10
  • 111
    • 33750279611 scopus 로고    scopus 로고
    • Parvoviral nuclear import: Bypassing the host nuclear-transport machinery
    • Cohen, S.; Behzad, A.R.; Carroll, J.B.; Pante, N. Parvoviral nuclear import: Bypassing the host nuclear-transport machinery. J. Gen. Virol. 2006, 87, 3209-3213.
    • (2006) J. Gen. Virol. , vol.87 , pp. 3209-3213
    • Cohen, S.1    Behzad, A.R.2    Carroll, J.B.3    Pante, N.4
  • 112
    • 79955440194 scopus 로고    scopus 로고
    • Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle
    • Cohen, S.; Marr, A.K.; Garcin, P.; Pante, N. Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle. J. Virol. 2011, 85, 4863-4874.
    • (2011) J. Virol. , vol.85 , pp. 4863-4874
    • Cohen, S.1    Marr, A.K.2    Garcin, P.3    Pante, N.4
  • 113
    • 0034759535 scopus 로고    scopus 로고
    • Infection ofpurified nuclei by adeno-associated virus 2
    • Hansen, J.; Qing, K.; Srivastava, A. Infection ofpurified nuclei by adeno-associated virus 2. Mol. Ther. 2001, 4, 289-296.
    • (2001) Mol. Ther. , vol.4 , pp. 289-296
    • Hansen, J.1    Qing, K.2    Srivastava, A.3
  • 114
    • 84905034292 scopus 로고    scopus 로고
    • Adeno-associated virus utilizes host cell nuclear import machinery to enter the nucleus
    • Nicolson, S.C.; Samulski, R.J. Adeno-associated virus utilizes host cell nuclear import machinery to enter the nucleus. Mol. Ther. 2013, 21, S30-S30.
    • (2013) Mol. Ther. , vol.21
    • Nicolson, S.C.1    Samulski, R.J.2
  • 115
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses-Analysis by cryoelectron microscopy and 3-dimensional image-reconstruction
    • Baker, T.S.; Newcomb, W.W.; Olson, N.H.; Cowsert, L.M.; Olson, C.; Brown, J.C. Structures of bovine and human papillomaviruses-Analysis by cryoelectron microscopy and 3-dimensional image-reconstruction. Biophys. J. 1991, 60, 1445-1456.
    • (1991) Biophys. J. , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 116
    • 0035156505 scopus 로고    scopus 로고
    • Human papillomavirus infection requires cell surface heparan sulfate
    • Giroglou, T.; Florin, L.; Schafer, F.; Streeck, R.E.; Sapp, M. Human papillomavirus infection requires cell surface heparan sulfate. J. Virol. 2001, 75, 1565-1570.
    • (2001) J. Virol. , vol.75 , pp. 1565-1570
    • Giroglou, T.1    Florin, L.2    Schafer, F.3    Streeck, R.E.4    Sapp, M.5
  • 117
    • 0033605153 scopus 로고    scopus 로고
    • The l1 major capsid protein of human papillomavirus type 11 recombinant viruslike particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes
    • Joyce, J.G.; Tung, J.S.; Przysiecki, C.T.; Cook, J.C.; Lehman, E.D.; Sands, J.A.; Jansens, K.U.; Keller, P.M. The l1 major capsid protein of human papillomavirus type 11 recombinant viruslike particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes. J. Biol. Chem. 1999, 274, 5810-5822.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5810-5822
    • Joyce, J.G.1    Tung, J.S.2    Przysiecki, C.T.3    Cook, J.C.4    Lehman, E.D.5    Sands, J.A.6    Jansens, K.U.7    Keller, P.M.8
  • 119
    • 31944439998 scopus 로고    scopus 로고
    • Cleavage of the papillomavirus minor capsid protein, l2, at a furin consensus site is necessary for infection
    • Richards, R.M.; Lowy, D.R.; Schiller, J.T.; Day, P.M. Cleavage of the papillomavirus minor capsid protein, l2, at a furin consensus site is necessary for infection. Proc. Natl. Acad. Sci. USA 2006, 103, 1522-1527.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1522-1527
    • Richards, R.M.1    Lowy, D.R.2    Schiller, J.T.3    Day, P.M.4
  • 120
    • 84900456204 scopus 로고    scopus 로고
    • A vaccine of l2 epitope repeats fused with a modified igg1 fc induced cross-neutralizing antibodies and protective immunity against divergent human papillomavirus types
    • Chen, X.; Liu, H.; Zhang, T.; Liu, Y.; Xie, X.; Wang, Z.; Xu, X. A vaccine of l2 epitope repeats fused with a modified igg1 fc induced cross-neutralizing antibodies and protective immunity against divergent human papillomavirus types. PLoS One 2014, 9, e95448.
    • (2014) PLoS One , vol.9
    • Chen, X.1    Liu, H.2    Zhang, T.3    Liu, Y.4    Xie, X.5    Wang, Z.6    Xu, X.7
  • 121
    • 70049114748 scopus 로고    scopus 로고
    • Target cell cyclophilins facilitate human papillomavirus type 16 infection
    • Bienkowska-Haba, M.; Patel, H.D.; Sapp, M. Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog. 2009, 5, e1000524.
    • (2009) PLoS Pathog. , vol.5
    • Bienkowska-Haba, M.1    Patel, H.D.2    Sapp, M.3
  • 122
    • 73949127173 scopus 로고    scopus 로고
    • The initial steps leading to papillomavirus infection occur on the basementmembrane prior to cell surface binding
    • Kines, R.C.; Thompson, C.D.; Lowy, D.R.; Schiller, J.T.; Day, P.M. The initial steps leading to papillomavirus infection occur on the basementmembrane prior to cell surface binding. Proc. Natl. Acad. Sci. USA 2009, 106, 20458-20463.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20458-20463
    • Kines, R.C.1    Thompson, C.D.2    Lowy, D.R.3    Schiller, J.T.4    Day, P.M.5
  • 124
    • 45749150395 scopus 로고    scopus 로고
    • Bovine papillomavirus type 1: From clathrin to caveolin
    • Laniosz, V.; Holthusen, K.A.; Meneses, P.I. Bovine papillomavirus type 1: From clathrin to caveolin. J. Virol. 2008, 82, 6288-6298.
    • (2008) J. Virol. , vol.82 , pp. 6288-6298
    • Laniosz, V.1    Holthusen, K.A.2    Meneses, P.I.3
  • 125
    • 35348849085 scopus 로고    scopus 로고
    • Human papillomavirus type 31 uses a caveolin 1-and dynamin 2-mediated entry pathway for infection of human keratinocytes
    • Smith, J.L.; Campos, S.K.; Ozbun, M.A. Human papillomavirus type 31 uses a caveolin 1-and dynamin 2-mediated entry pathway for infection of human keratinocytes. J. Virol. 2007, 81, 9922-9931.
    • (2007) J. Virol. , vol.81 , pp. 9922-9931
    • Smith, J.L.1    Campos, S.K.2    Ozbun, M.A.3
  • 126
    • 0037334521 scopus 로고    scopus 로고
    • Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells
    • Bousarghin, L.; Touze, A.; Sizaret, P.Y.; Coursaget, P. Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells. J. Virol. 2003, 77, 3846-3850.
    • (2003) J. Virol. , vol.77 , pp. 3846-3850
    • Bousarghin, L.1    Touze, A.2    Sizaret, P.Y.3    Coursaget, P.4
  • 127
    • 0037347091 scopus 로고    scopus 로고
    • Papillomaviruses infect cells via a clathrin-dependent pathway
    • Day, P.M.; Lowy, D.R.; Schiller, J.T. Papillomaviruses infect cells via a clathrin-dependent pathway. Virology 2003, 307, 1-11.
    • (2003) Virology , vol.307 , pp. 1-11
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 128
    • 53749105515 scopus 로고    scopus 로고
    • Clathrin-and caveolin-independent entry of human papillomavirus type 16-involvement of tetraspaninenriched microdomains (tems)
    • Spoden, G.; Freitag, K.; Husmann, M.; Boller, K.; Sapp, M.; Lambert, C.; Florin, L. Clathrin-and caveolin-independent entry of human papillomavirus type 16-involvement of tetraspaninenriched microdomains (tems). PLoS One 2008, 3, e3313.
    • (2008) PLoS One , vol.3
    • Spoden, G.1    Freitag, K.2    Husmann, M.3    Boller, K.4    Sapp, M.5    Lambert, C.6    Florin, L.7
  • 132
    • 18744365783 scopus 로고    scopus 로고
    • Interaction of tsnare syntaxin 18 with the papillomavirus minor capsid protein mediates infection
    • Bossis, L.; Roden, R.B.S.; Gambhira, R.; Yang, R.; Tagaya, M.; Howley, P.A.; Meneses, P.I. Interaction of tsnare syntaxin 18 with the papillomavirus minor capsid protein mediates infection. J. Virol. 2005, 79, 6723-6731.
    • (2005) J. Virol. , vol.79 , pp. 6723-6731
    • Bossis, L.1    Roden, R.B.S.2    Gambhira, R.3    Yang, R.4    Tagaya, M.5    Howley, P.A.6    Meneses, P.I.7
  • 133
    • 67749120150 scopus 로고    scopus 로고
    • Human papillomavirus type 16 infection of human keratinocytes requires clathrin and caveolin-1 and is brefeldin a sensitive
    • Laniosz, V.; Dabydeen, S.A.; Havens, M.A.; Meneses, P.I. Human papillomavirus type 16 infection of human keratinocytes requires clathrin and caveolin-1 and is brefeldin a sensitive. J. Virol. 2009, 83, 8221-8232.
    • (2009) J. Virol. , vol.83 , pp. 8221-8232
    • Laniosz, V.1    Dabydeen, S.A.2    Havens, M.A.3    Meneses, P.I.4
  • 135
    • 84861413246 scopus 로고    scopus 로고
    • Opposing effects of bacitracin on human papillomavirus type 16 infection: Enhancement of binding and entry and inhibition of endosomal penetration
    • Campos, S.K.; Chapman, J.A.; Deymier, M.J.; Bronnimann, M.P.; Ozbun, M.A. Opposing effects of bacitracin on human papillomavirus type 16 infection: Enhancement of binding and entry and inhibition of endosomal penetration. J. Virol. 2012, 86, 4169-4181.
    • (2012) J. Virol. , vol.86 , pp. 4169-4181
    • Campos, S.K.1    Chapman, J.A.2    Deymier, M.J.3    Bronnimann, M.P.4    Ozbun, M.A.5
  • 136
    • 0036432779 scopus 로고    scopus 로고
    • Analysisof the infectious entry pathway of human papillomavirus type 33 pseudovirions
    • Selinka, H.C.; Giroglou, T.; Sapp, M. Analysisof the infectious entry pathway of human papillomavirus type 33 pseudovirions. Virology 2002, 299, 279-287.
    • (2002) Virology , vol.299 , pp. 279-287
    • Selinka, H.C.1    Giroglou, T.2    Sapp, M.3
  • 137
    • 68749122026 scopus 로고    scopus 로고
    • The role ofnh(4)cl and cysteineproteases in human papillomavirus type 16 infection
    • Dabydeen, S.A.; Meneses, P.I. The role ofnh(4)cl and cysteineproteases in human papillomavirus type 16 infection. Virol. J. 2009, 6, 109.
    • (2009) Virol. J. , vol.6 , pp. 109
    • Dabydeen, S.A.1    Meneses, P.I.2
  • 139
    • 0345599173 scopus 로고    scopus 로고
    • Further evidence that papillomavirus capsids exist intwo distinct conformations
    • Selinka, H.C.; Giroglou, T.; Nowak, T.; Christensen, N.D.; Sapp, M. Further evidence that papillomavirus capsids exist intwo distinct conformations. J. Virol. 2003, 77, 12961-12967.
    • (2003) J. Virol. , vol.77 , pp. 12961-12967
    • Selinka, H.C.1    Giroglou, T.2    Nowak, T.3    Christensen, N.D.4    Sapp, M.5
  • 140
    • 0037384987 scopus 로고    scopus 로고
    • Interactions between papillomavirus l1 and l2 capsid proteins
    • Finnen, R.L.; Erickson, K.D.; Chen, X.J.S.; Garcea, R.L. Interactions between papillomavirus l1 and l2 capsid proteins. J. Virol. 2003, 77, 4818-4826.
    • (2003) J. Virol. , vol.77 , pp. 4818-4826
    • Finnen, R.L.1    Erickson, K.D.2    Chen, X.J.S.3    Garcea, R.L.4
  • 142
    • 0030931283 scopus 로고    scopus 로고
    • Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 angstrom resolution
    • Trus, B.L.; Roden, R.B.S.; Greenstone, H.L.; Vrhel, M.; Schiller, J.T.; Booy, F.P. Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 angstrom resolution. Nat. Struct. Biol. 1997, 4, 413-420.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 413-420
    • Trus, B.L.1    Roden, R.B.S.2    Greenstone, H.L.3    Vrhel, M.4    Schiller, J.T.5    Booy, F.P.6
  • 143
    • 0031579249 scopus 로고    scopus 로고
    • Sequence close to the n-terminus of l2 protein is displayed on the surface of bovine papillomavirus type 1 virions
    • Liu, W.J.; Gissmann, L.; Sun, X.Y.; Kanjanahaluethai, A.; Muller, M.; Doorbar, J.; Zhou, J. Sequence close to the n-terminus of l2 protein is displayed on the surface of bovine papillomavirus type 1 virions. Virology 1997, 227, 474-483.
    • (1997) Virology , vol.227 , pp. 474-483
    • Liu, W.J.1    Gissmann, L.2    Sun, X.Y.3    Kanjanahaluethai, A.4    Muller, M.5    Doorbar, J.6    Zhou, J.7
  • 144
    • 33846337051 scopus 로고    scopus 로고
    • Neutralization of hpv16, 18, 31, and 58 pseudovirions with antisera induced by immunizing rabbits with synthetic peptides representing segments of the hpv 16 minor capsid protein l2 surface region
    • Kondo, K.; Ishii, Y.; Ochi, H.; Matsumoto, T.; Yoshikawa, H.; Kanda, T. Neutralization of hpv16, 18, 31, and 58 pseudovirions with antisera induced by immunizing rabbits with synthetic peptides representing segments of the hpv 16 minor capsid protein l2 surface region. Virology 2007, 358, 266-272.
    • (2007) Virology , vol.358 , pp. 266-272
    • Kondo, K.1    Ishii, Y.2    Ochi, H.3    Matsumoto, T.4    Yoshikawa, H.5    Kanda, T.6
  • 145
    • 84855205694 scopus 로고    scopus 로고
    • The high risk hpv16 l2 minor capsid protein has multiple transport signals that mediate its nucleocytoplasmic traffic
    • Mamoor, S.; Onder, Z.; Karanam, B.; Kwak, K.; Bordeaux, J.; Crosby, L.; Roden, R.B.S.; Moroianu, J. The high risk hpv16 l2 minor capsid protein has multiple transport signals that mediate its nucleocytoplasmic traffic. Virology 2012, 422, 413-424.
    • (2012) Virology , vol.422 , pp. 413-424
    • Mamoor, S.1    Onder, Z.2    Karanam, B.3    Kwak, K.4    Bordeaux, J.5    Crosby, L.6    Roden, R.B.S.7    Moroianu, J.8
  • 146
    • 7644237129 scopus 로고    scopus 로고
    • The l2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors
    • Darshan, M.S.; Lucchi, J.; Harding, E.; Moroianu, J. The l2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors. J. Virol. 2004, 78, 12179-12188.
    • (2004) J. Virol. , vol.78 , pp. 12179-12188
    • Darshan, M.S.1    Lucchi, J.2    Harding, E.3    Moroianu, J.4
  • 147
    • 10044234323 scopus 로고    scopus 로고
    • The positively charged termini of l2 minor capsid protein required for bovine papillomavirus infection function separately in nuclear import and dna binding
    • Fay, A.; Yutzy, W.H.; Roden, R.B.S.; Moroianu, J. The positively charged termini of l2 minor capsid protein required for bovine papillomavirus infection function separately in nuclear import and dna binding. J. Virol. 2004, 78, 13447-13454.
    • (2004) J. Virol. , vol.78 , pp. 13447-13454
    • Fay, A.1    Yutzy, W.H.2    Roden, R.B.S.3    Moroianu, J.4
  • 148
    • 0028120905 scopus 로고
    • Interaction of human papillomavirus (hpv) type-16 capsid proteins with hpv dna requires an intact l2 n-terminal sequence
    • Zhou, J.; Sun, X.Y.; Louis, K.; Frazer, I.H. Interaction of human papillomavirus (hpv) type-16 capsid proteins with hpv dna requires an intact l2 n-terminal sequence. J. Virol. 1994, 68, 619-625.
    • (1994) J. Virol. , vol.68 , pp. 619-625
    • Zhou, J.1    Sun, X.Y.2    Louis, K.3    Frazer, I.H.4
  • 149
    • 0035130055 scopus 로고    scopus 로고
    • Human papillomavirus type 16 minor capsid protein l2 n-terminal region containing a common neutralization epitopebinds to the cell surface and enters the cytoplasm
    • Kawana, Y.; Kawana, K.; Yoshikawa, H.; Taketani, Y.; Yoshiike, K.; Kanda, T. Human papillomavirus type 16 minor capsid protein l2 n-terminal region containing a common neutralization epitopebinds to the cell surface and enters the cytoplasm. J. Virol. 2001, 75, 2331-2336.
    • (2001) J. Virol. , vol.75 , pp. 2331-2336
    • Kawana, Y.1    Kawana, K.2    Yoshikawa, H.3    Taketani, Y.4    Yoshiike, K.5    Kanda, T.6
  • 151
    • 0037333367 scopus 로고    scopus 로고
    • Cell surface-binding motifs of l2 that facilitate papillomavirus infection
    • Yang, R.C.; Day, P.M.; Yutzy, W.H.; Lin, K.Y.; Hung, C.F.; Roden, R.B.S. Cell surface-binding motifs of l2 that facilitate papillomavirus infection. J. Virol. 2003, 77, 3531-3541.
    • (2003) J. Virol. , vol.77 , pp. 3531-3541
    • Yang, R.C.1    Day, P.M.2    Yutzy, W.H.3    Lin, K.Y.4    Hung, C.F.5    Roden, R.B.S.6
  • 152
    • 15244344245 scopus 로고    scopus 로고
    • The minorcapsid protein l2 contributes to two steps in the human papillomavirus type 31 life cycle
    • Holmgren, S.C.; Patterson, N.A.; Ozbun, M.A.; Lambert, P.F. The minorcapsid protein l2 contributes to two steps in the human papillomavirus type 31 life cycle. J. Virol. 2005, 79, 3938-3948.
    • (2005) J. Virol. , vol.79 , pp. 3938-3948
    • Holmgren, S.C.1    Patterson, N.A.2    Ozbun, M.A.3    Lambert, P.F.4
  • 153
    • 0034790812 scopus 로고    scopus 로고
    • Positively charged termini of the l2 minor capsid protein are necessary for papillomavirus infection
    • Roden, R.B.S.; Day, P.M.; Bronzo, B.K.; Yutzy, W.H.; Yang, Y.Q.; Lowy, D.R.; Schiller, J.T. Positively charged termini of the l2 minor capsid protein are necessary for papillomavirus infection. J. Virol. 2001, 75, 10493-10497.
    • (2001) J. Virol. , vol.75 , pp. 10493-10497
    • Roden, R.B.S.1    Day, P.M.2    Bronzo, B.K.3    Yutzy, W.H.4    Yang, Y.Q.5    Lowy, D.R.6    Schiller, J.T.7
  • 154
    • 30344481121 scopus 로고    scopus 로고
    • A membrane-destabilizing peptide incapsid protein l2 is required for egress of papillomavirus genomes from endosomes
    • Kamper, N.; Day, P.M.; Nowak, T.; Selinka, H.C.; Florin, L.; Bolscher, J.; Hilbig, L.; Schiller, J.T.; Sapp, M. A membrane-destabilizing peptide incapsid protein l2 is required for egress of papillomavirus genomes from endosomes. J. Virol. 2006, 80, 759-768.
    • (2006) J. Virol. , vol.80 , pp. 759-768
    • Kamper, N.1    Day, P.M.2    Nowak, T.3    Selinka, H.C.4    Florin, L.5    Bolscher, J.6    Hilbig, L.7    Schiller, J.T.8    Sapp, M.9
  • 155
    • 84887212439 scopus 로고    scopus 로고
    • Two highly conserved cysteine residues in hpv16 l2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytes
    • Campos, S.K.; Ozbun, M.A. Two highly conserved cysteine residues in hpv16 l2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytes. PLoS One 2009, 4, e4463.
    • (2009) PLoS One , vol.4
    • Campos, S.K.1    Ozbun, M.A.2
  • 156
    • 72449124661 scopus 로고    scopus 로고
    • Role of l2 cysteines in papillomavirus infection and neutralization
    • Gambhira, R.; Jagu, S.; Karanam, B.; Day, P.M.; Roden, R. Role of l2 cysteines in papillomavirus infection and neutralization. Virol. J. 2009, 6, 176.
    • (2009) Virol. J. , vol.6 , pp. 176
    • Gambhira, R.1    Jagu, S.2    Karanam, B.3    Day, P.M.4    Roden, R.5
  • 157
    • 84871986425 scopus 로고    scopus 로고
    • A transmembrane domain and gxxxg motifs within l2 are essential for papillomavirus infection
    • Bronnimann, M.P.; Chapman, J.A.; Park, C.K.; Campos, S.K. A transmembrane domain and gxxxg motifs within l2 are essential for papillomavirus infection. J. Virol. 2013, 87, 464-473.
    • (2013) J. Virol. , vol.87 , pp. 464-473
    • Bronnimann, M.P.1    Chapman, J.A.2    Park, C.K.3    Campos, S.K.4
  • 158
    • 84755161558 scopus 로고    scopus 로고
    • Inhibition of nuclear entry of hpv16 pseudovirus-packaged dna by an anti-hpv16 l2neutralizing antibody
    • Ishii, Y.; Tanaka, K.; Kondo, K.; Takeuchi, T.; Mori, S.; Kanda, T. Inhibition of nuclear entry of hpv16 pseudovirus-packaged dna by an anti-hpv16 l2neutralizing antibody. Virology 2010, 406, 181-188.
    • (2010) Virology , vol.406 , pp. 181-188
    • Ishii, Y.1    Tanaka, K.2    Kondo, K.3    Takeuchi, T.4    Mori, S.5    Kanda, T.6
  • 159
    • 84856808484 scopus 로고    scopus 로고
    • Human papillomavirus l2 facilitates viral escape from lateendosomes via sorting nexin 17
    • Marusic, M.B.; Ozbun, M.A.; Campos, S.K.; Myers, M.P.; Banks, L. Human papillomavirus l2 facilitates viral escape from lateendosomes via sorting nexin 17. Traffic 2012, 13, 455-467.
    • (2012) Traffic , vol.13 , pp. 455-467
    • Marusic, M.B.1    Ozbun, M.A.2    Campos, S.K.3    Myers, M.P.4    Banks, L.5
  • 160
    • 84871940100 scopus 로고    scopus 로고
    • Snx17 facilitates infection with diverse papillomavirus types
    • Bergant, M.; Banks, L. Snx17 facilitates infection with diverse papillomavirus types. J. Virol. 2013, 87, 1270-1273.
    • (2013) J. Virol. , vol.87 , pp. 1270-1273
    • Bergant, M.1    Banks, L.2
  • 161
    • 34447292801 scopus 로고    scopus 로고
    • Bovine papillomavirus type 1 infection is mediated by snare syntaxin 18
    • Laniosz, V.; Nguyen, K.C.; Meneses, P.I. Bovine papillomavirus type 1 infection is mediated by snare syntaxin 18. J. Virol. 2007, 81, 7435-7448.
    • (2007) J. Virol. , vol.81 , pp. 7435-7448
    • Laniosz, V.1    Nguyen, K.C.2    Meneses, P.I.3
  • 163
    • 0035836374 scopus 로고    scopus 로고
    • Association of bovine papillomavirus type 1 with microtubules
    • Liu, W.J.; Qi, Y.M.; Zhao, K.N.; Liu, Y.H.; Liu, X.S.; Frazer, I.H. Association of bovine papillomavirus type 1 with microtubules. Virology 2001, 282, 237-244.
    • (2001) Virology , vol.282 , pp. 237-244
    • Liu, W.J.1    Qi, Y.M.2    Zhao, K.N.3    Liu, Y.H.4    Liu, X.S.5    Frazer, I.H.6
  • 164
    • 0028811410 scopus 로고
    • Early phase in the infection of cultured-cells with papillomavirus virions
    • Zhou, J.; Gissmann, L.; Zentgraf, H.; Muller, H.; Picken, M.; Muller, M. Early phase in the infection of cultured-cells with papillomavirus virions. Virology 1995, 214, 167-176.
    • (1995) Virology , vol.214 , pp. 167-176
    • Zhou, J.1    Gissmann, L.2    Zentgraf, H.3    Muller, H.4    Picken, M.5    Muller, M.6
  • 165
    • 33745251121 scopus 로고    scopus 로고
    • Identification of a dynein interacting domain in the papillomavirus minor capsid protein l2
    • Florin, L.; Becker, K.A.; Lambert, C.; Nowak, T.; Sapp, C.; Strand, D.; Streeck, R.E.; Sapp, M. Identification of a dynein interacting domain in the papillomavirus minor capsid protein l2. J. Virol. 2006, 80, 6691-6696.
    • (2006) J. Virol. , vol.80 , pp. 6691-6696
    • Florin, L.1    Becker, K.A.2    Lambert, C.3    Nowak, T.4    Sapp, C.5    Strand, D.6    Streeck, R.E.7    Sapp, M.8
  • 166
    • 78650282789 scopus 로고    scopus 로고
    • Identification of the dynein light chains required for human papillomavirus infection
    • Schneider, M.A.; Spoden, G.A.; Florin, L.; Lambert, C. Identification of the dynein light chains required for human papillomavirus infection. Cell. Microbiol. 2011, 13, 32-46.
    • (2011) Cell. Microbiol. , vol.13 , pp. 32-46
    • Schneider, M.A.1    Spoden, G.A.2    Florin, L.3    Lambert, C.4
  • 167
    • 4644352291 scopus 로고    scopus 로고
    • Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (pml) expression
    • Day, P.M.; Baker, C.C.; Lowy, D.R.; Schiller, J.T. Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (pml) expression. Proc. Natl. Acad. Sci. USA 2004, 101, 14252-14257.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14252-14257
    • Day, P.M.1    Baker, C.C.2    Lowy, D.R.3    Schiller, J.T.4
  • 168
    • 84866170686 scopus 로고    scopus 로고
    • Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein l1 from the l2/dna complex following virus entry
    • Bienkowska-Haba, M.; Williams, C.; Kim, S.M.; Garcea, R.L.; Sapp, M. Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein l1 from the l2/dna complex following virus entry. J. Virol. 2012, 86, 9875-9887.
    • (2012) J. Virol. , vol.86 , pp. 9875-9887
    • Bienkowska-Haba, M.1    Williams, C.2    Kim, S.M.3    Garcea, R.L.4    Sapp, M.5
  • 169
    • 84860330708 scopus 로고    scopus 로고
    • Ldp12, a novel cell-permeablepeptide derived from l1 capsid protein of the human papillomavirus
    • Lee, J.E.; Lim, H.J. Ldp12, a novel cell-permeablepeptide derived from l1 capsid protein of the human papillomavirus. Mol. Biol. Rep. 2012, 39, 1079-1086.
    • (2012) Mol. Biol. Rep. , vol.39 , pp. 1079-1086
    • Lee, J.E.1    Lim, H.J.2
  • 171
    • 0028306047 scopus 로고
    • Interactions among the major and minor coat proteins of polyomavirus
    • Barouch, D.H.; Harrison, S.C. Interactions among the major and minor coat proteins of polyomavirus. J. Virol. 1994, 68, 3982-3989.
    • (1994) J. Virol. , vol.68 , pp. 3982-3989
    • Barouch, D.H.1    Harrison, S.C.2
  • 172
    • 0032526711 scopus 로고    scopus 로고
    • Interaction of polyomavirus internal protein vp2 with the major capsid protein vp1 and implications for participation of vp2 in viral entry
    • Chen, X.J.S.; Stehle, T.; Harrison, S.C. Interaction of polyomavirus internal protein vp2 with the major capsid protein vp1 and implications for participation of vp2 in viral entry. EMBO J. 1998, 17, 3233-3240.
    • (1998) EMBO J. , vol.17 , pp. 3233-3240
    • Chen, X.J.S.1    Stehle, T.2    Harrison, S.C.3
  • 173
    • 0023113683 scopus 로고
    • Myristic acid is coupled to a structural protein of polyoma-virus and sv40
    • Streuli, C.H.; Griffin, B.E. Myristic acid is coupled to a structural protein of polyoma-virus and sv40. Nature 1987, 326, 619-622.
    • (1987) Nature , vol.326 , pp. 619-622
    • Streuli, C.H.1    Griffin, B.E.2
  • 174
    • 0001488319 scopus 로고
    • A filterable agent, recovered fromak leukemic extracts, causing salivary gland carcinomas in c3h mice
    • Gross, L. A filterable agent, recovered fromak leukemic extracts, causing salivary gland carcinomas in c3h mice. Proc. Soc. Exp. Biol. Med. 1953, 83, 414-421.
    • (1953) Proc. Soc. Exp. Biol. Med. , vol.83 , pp. 414-421
    • Gross, L.1
  • 175
    • 84873720583 scopus 로고    scopus 로고
    • Human polyomaviruses in disease and cancer
    • Dalianis, T.; Hirsch, H.H. Human polyomaviruses in disease and cancer. Virology 2013, 437, 63-72.
    • (2013) Virology , vol.437 , pp. 63-72
    • Dalianis, T.1    Hirsch, H.H.2
  • 176
    • 39749113080 scopus 로고    scopus 로고
    • Clonal integration of a polyomavirus in human merkel cell carcinoma
    • Feng, H.C.; Shuda, M.; Chang, Y.; Moore, P.S. Clonal integration of a polyomavirus in human merkel cell carcinoma. Science 2008, 319, 1096-1100.
    • (2008) Science , vol.319 , pp. 1096-1100
    • Feng, H.C.1    Shuda, M.2    Chang, Y.3    Moore, P.S.4
  • 178
    • 77956794231 scopus 로고    scopus 로고
    • Lipids and proteins act in opposing manners to regulate polyomavirus infection
    • Qian, M.D.; Tsai, B. Lipids and proteins act in opposing manners to regulate polyomavirus infection. J. Virol. 2010, 84, 9840-9852.
    • (2010) J. Virol. , vol.84 , pp. 9840-9852
    • Qian, M.D.1    Tsai, B.2
  • 179
    • 31144470194 scopus 로고    scopus 로고
    • Identification of gangliosides gd1b and gt1b as receptors for bk virus
    • Low, J.A.; Magnuson, B.; Tsai, B.; Imperiale, M.J. Identification of gangliosides gd1b and gt1b as receptors for bk virus. J. Virol. 2006, 80, 1361-1366.
    • (2006) J. Virol. , vol.80 , pp. 1361-1366
    • Low, J.A.1    Magnuson, B.2    Tsai, B.3    Imperiale, M.J.4
  • 181
    • 4744347077 scopus 로고    scopus 로고
    • Conformational changes of murine polyomavirus capsid proteins induced by sialicacid binding
    • Cavaldesi, M.; Caruso, M.; Sthandier, O.; Amati, P.; Garcia, M.I. Conformational changes of murine polyomavirus capsid proteins induced by sialicacid binding. J. Biol. Chem. 2004, 279, 41573-41579.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41573-41579
    • Cavaldesi, M.1    Caruso, M.2    Sthandier, O.3    Amati, P.4    Garcia, M.I.5
  • 182
    • 67650912077 scopus 로고    scopus 로고
    • A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection
    • Qian, M.D.; Cai, D.W.; Verhey, K.J.; Tsai, B. A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog. 2009, 5, e1000465.
    • (2009) PLoS Pathog. , vol.5
    • Qian, M.D.1    Cai, D.W.2    Verhey, K.J.3    Tsai, B.4
  • 183
    • 0033968050 scopus 로고    scopus 로고
    • Jc virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis
    • Pho, M.T.; Ashok, A.; Atwood, W.J. Jc virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis. J. Virol. 2000, 74, 2288-2292.
    • (2000) J. Virol. , vol.74 , pp. 2288-2292
    • Pho, M.T.1    Ashok, A.2    Atwood, W.J.3
  • 184
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolinenriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H.A.; Chen, Y.Z.; Norkin, L.C. Bound simian virus 40 translocates to caveolinenriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol. Biol. Cell 1996, 7, 1825-1834.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.Z.2    Norkin, L.C.3
  • 185
    • 0034755553 scopus 로고    scopus 로고
    • Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial vp1 pseudocapsids toward cell nuclei
    • Richterova, Z.; Liebl, D.; Horak, M.; Palkova, Z.; Stokrova, J.; Hozak, P.; Korb, J.; Forstova, J. Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial vp1 pseudocapsids toward cell nuclei. J. Virol. 2001, 75, 10880-10891.
    • (2001) J. Virol. , vol.75 , pp. 10880-10891
    • Richterova, Z.1    Liebl, D.2    Horak, M.3    Palkova, Z.4    Stokrova, J.5    Hozak, P.6    Korb, J.7    Forstova, J.8
  • 186
    • 6344219974 scopus 로고    scopus 로고
    • Infection of vero cells by bk virus is dependent on caveolae
    • Eash, S.; Querbes, W.; Atwood, W.J. Infection of vero cells by bk virus is dependent on caveolae. J. Virol. 2004, 78, 11583-11590.
    • (2004) J. Virol. , vol.78 , pp. 11583-11590
    • Eash, S.1    Querbes, W.2    Atwood, W.J.3
  • 187
    • 0037321752 scopus 로고    scopus 로고
    • Cell penetration and trafficking of polyomavirus
    • Gilbert, J.M.; Goldberg, I.G.; Benjamin, T.L. Cell penetration and trafficking of polyomavirus. J. Virol. 2003, 77, 2615-2622.
    • (2003) J. Virol. , vol.77 , pp. 2615-2622
    • Gilbert, J.M.1    Goldberg, I.G.2    Benjamin, T.L.3
  • 188
    • 0037227696 scopus 로고    scopus 로고
    • Contrasting roles of endosomal ph and the cytoskeleton in infection of human glial cells by jc virus and simian virus 40
    • Ashok, A.; Atwood, W.J. Contrasting roles of endosomal ph and the cytoskeleton in infection of human glial cells by jc virus and simian virus 40. J. Virol. 2003, 77, 1347-1356.
    • (2003) J. Virol. , vol.77 , pp. 1347-1356
    • Ashok, A.1    Atwood, W.J.2
  • 189
    • 38649102147 scopus 로고    scopus 로고
    • Intracellular trafficking pathway of bk virus in human renal proximal tubular epithelial cells
    • Moriyama, T.; Sorokin, A. Intracellular trafficking pathway of bk virus in human renal proximal tubular epithelial cells. Virology 2008, 371, 336-349.
    • (2008) Virology , vol.371 , pp. 336-349
    • Moriyama, T.1    Sorokin, A.2
  • 190
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the er
    • Pelkmans, L.; Kartenbeck, J.; Helenius, A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the er. Nat. Cell Biol. 2001, 3, 473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 191
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin-and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • Damm, E.M.; Pelkmans, L.; Kartenbeck, J.; Mezzacasa, A.; Kurzckalia, T.; Helenius, A. Clathrin-and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae. J. Cell Biol. 2005, 168, 477-488.
    • (2005) J. Cell Biol. , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzckalia, T.5    Helenius, A.6
  • 192
    • 33646204681 scopus 로고    scopus 로고
    • Mouse polyomavirus enters early endosomes, requires their acidic ph for productive infection, and meets transferrin cargo in rab11-positive endosomes
    • Liebl, D.; Difato, F.; Hornikova, L.; Mannova, P.; Strokrova, J.; Forstova, J. Mouse polyomavirus enters early endosomes, requires their acidic ph for productive infection, and meets transferrin cargo in rab11-positive endosomes. J. Virol. 2006, 80, 4610-4622.
    • (2006) J. Virol. , vol.80 , pp. 4610-4622
    • Liebl, D.1    Difato, F.2    Hornikova, L.3    Mannova, P.4    Strokrova, J.5    Forstova, J.6
  • 193
    • 0037303397 scopus 로고    scopus 로고
    • Mouse polyomavirus utilizes recycling endosomes for a traffic pathway independent of copi vesicle transport
    • Mannova, P.; Forstova, J. Mouse polyomavirus utilizes recycling endosomes for a traffic pathway independent of copi vesicle transport. J. Virol. 2003, 77, 1672-1681.
    • (2003) J. Virol. , vol.77 , pp. 1672-1681
    • Mannova, P.1    Forstova, J.2
  • 194
    • 7744246474 scopus 로고    scopus 로고
    • Uptake pathway of polyomavirus via ganglioside gd1a
    • Gilbert, J.; Benjamin, T. Uptake pathway of polyomavirus via ganglioside gd1a. J. Virol. 2004, 78, 12259-12267.
    • (2004) J. Virol. , vol.78 , pp. 12259-12267
    • Gilbert, J.1    Benjamin, T.2
  • 195
    • 0036000023 scopus 로고    scopus 로고
    • Inhibitors of cop-mediated transport and cholera toxin action inhibit simian virus 40 infection
    • Richards, A.A.; Stang, E.; Pepperkok, R.; Parton, R.G. Inhibitors of cop-mediated transport and cholera toxin action inhibit simian virus 40 infection. Mol. Biol. Cell 2002, 13, 1750-1764.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1750-1764
    • Richards, A.A.1    Stang, E.2    Pepperkok, R.3    Parton, R.G.4
  • 196
    • 0036233218 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 is followed by brefeldin a-sensitive transport to the endoplasmic reticulum, where the virus disassembles
    • Norkin, L.C.; Anderson, H.A.; Wolfrom, S.A.; Oppenheim, A. Caveolar endocytosis of simian virus 40 is followed by brefeldin a-sensitive transport to the endoplasmic reticulum, where the virus disassembles. J. Virol. 2002, 76, 5156-5166.
    • (2002) J. Virol. , vol.76 , pp. 5156-5166
    • Norkin, L.C.1    Anderson, H.A.2    Wolfrom, S.A.3    Oppenheim, A.4
  • 197
    • 22444431627 scopus 로고    scopus 로고
    • The caveolae-mediatedsv40 entry pathway bypasses the golgi complex en route to the endoplasmic reticulum
    • Norkin, L.C.; Kuksin, D. The caveolae-mediatedsv40 entry pathway bypasses the golgi complex en route to the endoplasmic reticulum. Virol. J. 2005, 2, 38.
    • (2005) Virol. J. , vol.2 , pp. 38
    • Norkin, L.C.1    Kuksin, D.2
  • 198
    • 84901022652 scopus 로고    scopus 로고
    • Involvement of microtubular network and its motors in productive endocytictrafficking of mouse polyomavirus
    • Zila, V.; Difato, F.; Klimova, L.; Huerfano, S.; Forstova, J. Involvement of microtubular network and its motors in productive endocytictrafficking of mouse polyomavirus. PLoS One 2014, 9, e96922.
    • (2014) PLoS One , vol.9
    • Zila, V.1    Difato, F.2    Klimova, L.3    Huerfano, S.4    Forstova, J.5
  • 199
    • 79551714334 scopus 로고    scopus 로고
    • A pdi family network acts distinctly and coordinately with erp29 to facilitate polyomavirus infection
    • Walczak, C.P.; Tsai, B. A pdi family network acts distinctly and coordinately with erp29 to facilitate polyomavirus infection. J. Virol. 2011, 85, 2386-2396.
    • (2011) J. Virol. , vol.85 , pp. 2386-2396
    • Walczak, C.P.1    Tsai, B.2
  • 200
    • 35548992416 scopus 로고    scopus 로고
    • Simian virus 40 depends on er protein folding and quality control factors for entry into host cells
    • Schelhaas, M.; Malmstrom, J.; Pelkmans, L.; Haugstetter, J.; Ellgaard, L.; Grunewald, K.; Helenius, A. Simian virus 40 depends on er protein folding and quality control factors for entry into host cells. Cell 2007, 131, 516-529.
    • (2007) Cell , vol.131 , pp. 516-529
    • Schelhaas, M.1    Malmstrom, J.2    Pelkmans, L.3    Haugstetter, J.4    Ellgaard, L.5    Grunewald, K.6    Helenius, A.7
  • 201
    • 33750310094 scopus 로고    scopus 로고
    • Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus
    • Gilbert, J.; Ou, W.; Silver, J.; Benjamin, T. Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus. J. Virol. 2006, 80, 10868-10870.
    • (2006) J. Virol. , vol.80 , pp. 10868-10870
    • Gilbert, J.1    Ou, W.2    Silver, J.3    Benjamin, T.4
  • 204
    • 33748658449 scopus 로고    scopus 로고
    • Murine polyomavirus requires the endoplasmic reticulum protein derlin-2 to initiate infection
    • Lilley, B.N.; Gilbert, J.M.; Ploegh, H.L.; Benjamin, T.L. Murine polyomavirus requires the endoplasmic reticulum protein derlin-2 to initiate infection. J. Virol. 2006, 80, 8739-8744.
    • (2006) J. Virol. , vol.80 , pp. 8739-8744
    • Lilley, B.N.1    Gilbert, J.M.2    Ploegh, H.L.3    Benjamin, T.L.4
  • 205
    • 84881255147 scopus 로고    scopus 로고
    • Role of cell-type-specific endoplasmic reticulumassociated degradation in polyomavirus trafficking
    • Bennett, S.M.; Jiang, M.; Imperiale, M.J. Role of cell-type-specific endoplasmic reticulumassociated degradation in polyomavirus trafficking. J. Virol. 2013, 87, 8843-8852.
    • (2013) J. Virol. , vol.87 , pp. 8843-8852
    • Bennett, S.M.1    Jiang, M.2    Imperiale, M.J.3
  • 206
    • 0035816403 scopus 로고    scopus 로고
    • Disulfide bonds stabilize jc virus capsid-like structure by protecting calcium ions from chelation
    • Chen, P.L.; Wang, M.L.; Ou, W.C.; Lii, C.K.; Chen, L.S.; Chang, D.C. Disulfide bonds stabilize jc virus capsid-like structure by protecting calcium ions from chelation. FEBS Lett. 2001, 500, 109-113.
    • (2001) FEBS Lett. , vol.500 , pp. 109-113
    • Chen, P.L.1    Wang, M.L.2    Ou, W.C.3    Lii, C.K.4    Chen, L.S.5    Chang, D.C.6
  • 207
    • 0030839256 scopus 로고    scopus 로고
    • High-resolution structure of a polyomavirus vp1-oligosaccharide complex: Implications for assembly and receptor binding
    • Stehle, T.; Harrison, S.C. High-resolution structure of a polyomavirus vp1-oligosaccharide complex: Implications for assembly and receptor binding. EMBO J. 1997, 16, 5139-5148.
    • (1997) EMBO J. , vol.16 , pp. 5139-5148
    • Stehle, T.1    Harrison, S.C.2
  • 208
    • 0034905983 scopus 로고    scopus 로고
    • Cys(9), cys(104) and cys(207) of simian virus 40 vp1 are essential for infectious virion formation in cv-1 celss
    • Gharakhanian, E.; Fasching, C.L.; Orlando, S.J.; Perez, A.R. Cys(9), cys(104) and cys(207) of simian virus 40 vp1 are essential for infectious virion formation in cv-1 celss. J. Gen. Virol. 2001, 82, 1935-1939.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1935-1939
    • Gharakhanian, E.1    Fasching, C.L.2    Orlando, S.J.3    Perez, A.R.4
  • 209
    • 0022549499 scopus 로고
    • Self-assembly of purified polyomavirus capsid protein-vp1
    • Salunke, D.M.; Caspar, D.L.D.; Garcea, R.L. Self-assembly of purified polyomavirus capsid protein-vp1. Cell 1986, 46, 895-904.
    • (1986) Cell , vol.46 , pp. 895-904
    • Salunke, D.M.1    Caspar, D.L.D.2    Garcea, R.L.3
  • 210
    • 33845655873 scopus 로고    scopus 로고
    • Sv40vp2 and vp3 insertion into er membranes is controlled by the capsid protein vp1: Implications for dna translocation out of the er
    • Daniels, R.; Rusan, N.M.; Wadsworth, P.; Hebert, D.N. Sv40vp2 and vp3 insertion into er membranes is controlled by the capsid protein vp1: Implications for dna translocation out of the er. Mol. Cell 2006, 24, 955-966.
    • (2006) Mol. Cell , vol.24 , pp. 955-966
    • Daniels, R.1    Rusan, N.M.2    Wadsworth, P.3    Hebert, D.N.4
  • 211
    • 0042668487 scopus 로고    scopus 로고
    • The simian virus 40 minor structural protein vp3, but not vp2, is essential for infectious virion formation
    • Gharakhanian, E.; Munoz, L.; Mayorca, L. The simian virus 40 minor structural protein vp3, but not vp2, is essential for infectious virion formation. J. Gen. Virol. 2003, 84, 2111-2116.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2111-2116
    • Gharakhanian, E.1    Munoz, L.2    Mayorca, L.3
  • 212
    • 80053386878 scopus 로고    scopus 로고
    • In vitro reconstitution of sv40 particles that are composed of vp1/2/3 capsid proteins and nucleosomal dna and direct efficient gene transfer
    • Enomoto, T.; Kukimoto, I.; Kawano, M.A.; Yamaguchi, Y.; Berk, A.J.; Handa, H. In vitro reconstitution of sv40 particles that are composed of vp1/2/3 capsid proteins and nucleosomal dna and direct efficient gene transfer. Virology 2011, 420, 1-9.
    • (2011) Virology , vol.420 , pp. 1-9
    • Enomoto, T.1    Kukimoto, I.2    Kawano, M.A.3    Yamaguchi, Y.4    Berk, A.J.5    Handa, H.6
  • 213
    • 34247139824 scopus 로고    scopus 로고
    • Minor capsid proteins of simian virus 40 are dispensable for nucleocapsid assembly and cell entry but are required for nuclear entry of the viral genome
    • Nakanishi, A.; Itoh, N.; Li, P.P.; Handa, H.; Liddington, R.C.; Kasamatsu, H. Minor capsid proteins of simian virus 40 are dispensable for nucleocapsid assembly and cell entry but are required for nuclear entry of the viral genome. J. Virol. 2007, 81, 3778-3785.
    • (2007) J. Virol. , vol.81 , pp. 3778-3785
    • Nakanishi, A.1    Itoh, N.2    Li, P.P.3    Handa, H.4    Liddington, R.C.5    Kasamatsu, H.6
  • 214
    • 0030584127 scopus 로고    scopus 로고
    • Crystal structures ofmurine polyomavirus in complex with straightchain and branched-chain sialyloligosaccharide receptor fragments
    • Stehle, T.; Harrison, S.C. Crystal structures ofmurine polyomavirus in complex with straightchain and branched-chain sialyloligosaccharide receptor fragments. Structure 1996, 4, 183-194.
    • (1996) Structure , vol.4 , pp. 183-194
    • Stehle, T.1    Harrison, S.C.2
  • 215
    • 42449139527 scopus 로고    scopus 로고
    • Structural basis of gm1 ganglioside recognition by simian virus 40
    • Neu, U.; Woellner, K.; Gauglitz, G.; Stehle, T. Structural basis of gm1 ganglioside recognition by simian virus 40. Proc. Natl. Acad. Sci. USA 2008, 105, 5219-5224.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5219-5224
    • Neu, U.1    Woellner, K.2    Gauglitz, G.3    Stehle, T.4
  • 216
    • 79958051219 scopus 로고    scopus 로고
    • A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol
    • Inoue, T.; Tsai, B. A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol. PLoS Pathog. 2011, 7, e1002037.
    • (2011) PLoS Pathog. , vol.7
    • Inoue, T.1    Tsai, B.2
  • 218
    • 0027250628 scopus 로고
    • Expression of the polyomavirus vp2 and vp3 proteins in insect cells-Coexpression with the major capsid protein vp1 alters vp2/vp3 subcellular-localization
    • Delos, S.E.; Montross, L.; Moreland, R.B.; Garcea, R.L. Expression of the polyomavirus vp2 and vp3 proteins in insect cells-Coexpression with the major capsid protein vp1 alters vp2/vp3 subcellular-localization. Virology 1993, 194, 393-398.
    • (1993) Virology , vol.194 , pp. 393-398
    • Delos, S.E.1    Montross, L.2    Moreland, R.B.3    Garcea, R.L.4
  • 219
    • 76349121992 scopus 로고    scopus 로고
    • Minor capsid proteins of mouse polyomavirus are inducers of apoptosis when produced individually but are only moderate contributors to cell death during the late phase of viral infection
    • Huerfano, S.; Zila, V.; Boura, E.; Spanielova, H.; Stokrova, J.; Forstova, J. Minor capsid proteins of mouse polyomavirus are inducers of apoptosis when produced individually but are only moderate contributors to cell death during the late phase of viral infection. FEBS J. 2010, 277, 1270-1283.
    • (2010) FEBS J. , vol.277 , pp. 1270-1283
    • Huerfano, S.1    Zila, V.2    Boura, E.3    Spanielova, H.4    Stokrova, J.5    Forstova, J.6
  • 220
    • 84873808430 scopus 로고    scopus 로고
    • The viroporin activity of the minor structural proteins vp2 and vp3 is required for sv40 propagation
    • Giorda, K.M.; Raghava, S.; Zhang, M.W.; Hebert, D.N. The viroporin activity of the minor structural proteins vp2 and vp3 is required for sv40 propagation. J. Biol. Chem. 2013, 288, 2510-2520.
    • (2013) J. Biol. Chem. , vol.288 , pp. 2510-2520
    • Giorda, K.M.1    Raghava, S.2    Zhang, M.W.3    Hebert, D.N.4
  • 221
    • 84878646453 scopus 로고    scopus 로고
    • Sv40 late protein vp4 forms toroidal pores to disruptmembranes for viral release
    • Raghava, S.; Giorda, K.M.; Romano, F.B.; Heuck, A.P.; Hebert, D.N. Sv40 late protein vp4 forms toroidal pores to disruptmembranes for viral release. Biochemistry 2013, 52, 3939-3948.
    • (2013) Biochemistry , vol.52 , pp. 3939-3948
    • Raghava, S.1    Giorda, K.M.2    Romano, F.B.3    Heuck, A.P.4    Hebert, D.N.5
  • 222
    • 34547618859 scopus 로고    scopus 로고
    • A very late viral protein triggers the lytic release of sv40
    • Daniels, R.; Sadowicz, D.; Hebert, D.N. A very late viral protein triggers the lytic release of sv40. PLoS Pathog. 2007, 3, 928-938.
    • (2007) PLoS Pathog. , vol.3 , pp. 928-938
    • Daniels, R.1    Sadowicz, D.2    Hebert, D.N.3
  • 224
    • 0028152979 scopus 로고
    • Expression and purification of recombinant polyomavirus vp2 protein and its interactions with polyomavirus proteins
    • Cai, X.Y.; Chang, D.C.; Rottinghaus, S.; Consigli, R.A. Expression and purification of recombinant polyomavirus vp2 protein and its interactions with polyomavirus proteins. J. Virol. 1994, 68, 7609-7613.
    • (1994) J. Virol. , vol.68 , pp. 7609-7613
    • Cai, X.Y.1    Chang, D.C.2    Rottinghaus, S.3    Consigli, R.A.4
  • 226
    • 84883349000 scopus 로고    scopus 로고
    • The merkelcell polyomavirus minor capsid protein
    • Schowalter, R.M.; Buck, C.B. The merkelcell polyomavirus minor capsid protein. PLoS Pathog. 2013, 9, e1003558.
    • (2013) PLoS Pathog. , vol.9
    • Schowalter, R.M.1    Buck, C.B.2
  • 227
    • 26944450514 scopus 로고    scopus 로고
    • Erp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • Magnuson, B.; Rainey, E.K.; Benjamin, T.; Baryshev, M.; Mkrtchian, S.; Tsai, B. Erp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol. Cell 2005, 20, 289-300.
    • (2005) Mol. Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3    Baryshev, M.4    Mkrtchian, S.5    Tsai, B.6
  • 229
    • 84897416878 scopus 로고    scopus 로고
    • A cytosolic chaperone complexes with dynamic membrane j-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum
    • Walczak, C.P.; Ravindran, M.S.; Inoue, T.; Tsai, B. A cytosolic chaperone complexes with dynamic membrane j-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum. PLoS Pathog 2014, 10, e1004007.
    • (2014) PLoS Pathog , vol.10
    • Walczak, C.P.1    Ravindran, M.S.2    Inoue, T.3    Tsai, B.4
  • 230
    • 0036720837 scopus 로고    scopus 로고
    • Interaction of the vp3 nuclear localization signal with the importin alpha-2/beta heterodimer directs nuclear entry of infecting simian virus 40
    • Nakanishi, A.; Shum, D.; Morioka, H.; Otsuka, E.; Kasamatsu, H. Interaction of the vp3 nuclear localization signal with the importin alpha-2/beta heterodimer directs nuclear entry of infecting simian virus 40. J. Virol. 2002, 76, 9368-9377.
    • (2002) J. Virol. , vol.76 , pp. 9368-9377
    • Nakanishi, A.1    Shum, D.2    Morioka, H.3    Otsuka, E.4    Kasamatsu, H.5
  • 231
    • 33846829982 scopus 로고    scopus 로고
    • Molecular dissection of nuclear entry-competent sv40 during infection
    • Nakanishi, A.; Li, P.P.; Qu, Q.M.; Jafri, Q.H.; Kasamatsu, H. Molecular dissection of nuclear entry-competent sv40 during infection. Virus Res. 2007, 124, 226-230.
    • (2007) Virus Res. , vol.124 , pp. 226-230
    • Nakanishi, A.1    Li, P.P.2    Qu, Q.M.3    Jafri, Q.H.4    Kasamatsu, H.5
  • 232
    • 84864820752 scopus 로고    scopus 로고
    • Disassociation of the sv40 genome from capsid proteins prior to nuclear entry
    • Kuksin, D.; Norkin, L.C. Disassociation of the sv40 genome from capsid proteins prior to nuclear entry. Virol. J. 2012, 9, 158.
    • (2012) Virol. J. , vol.9 , pp. 158
    • Kuksin, D.1    Norkin, L.C.2
  • 233
    • 0014823393 scopus 로고
    • Morphological aspects of uptake ofsimian-virus-40 by permissive cells
    • Hummeler, K.; Tomassin, N.; Sokol, F. Morphological aspects of uptake ofsimian-virus-40 by permissive cells. J. Virol. 1970, 6, 87-93.
    • (1970) J. Virol. , vol.6 , pp. 87-93
    • Hummeler, K.1    Tomassin, N.2    Sokol, F.3
  • 234
    • 0017084285 scopus 로고
    • Early events in polyoma-virus infection-attachment, penetration, and nuclear entry
    • Mackay, R.L.; Consigli, R.A. Early events in polyoma-virus infection-attachment, penetration, and nuclear entry. J. Virol. 1976, 19, 620-636.
    • (1976) J. Virol. , vol.19 , pp. 620-636
    • McKay, R.L.1    Consigli, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.