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Volumn 8, Issue 4, 2012, Pages

Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CAVEOLIN 1; CHOLESTEROL; CLATHRIN; DYNAMIN; FLOTILLIN 1; P21 ACTIVATED KINASE 1; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; CAVEOLIN; P21 ACTIVATED KINASE; PAK1 PROTEIN, HUMAN; SODIUM PROTON EXCHANGE PROTEIN;

EID: 84861207605     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002657     Document Type: Article
Times cited : (229)

References (82)
  • 1
    • 2942618208 scopus 로고    scopus 로고
    • Pathogenesis of human papillomaviruses in differentiating epithelia
    • Longworth MS, Laimins LA, (2004) Pathogenesis of human papillomaviruses in differentiating epithelia. Microbiol Mol Biol Rev 68: 362-372.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 362-372
    • Longworth, M.S.1    Laimins, L.A.2
  • 2
    • 59349098016 scopus 로고    scopus 로고
    • Structure, attachment and entry of polyoma- and papillomaviruses
    • Sapp M, Day PM, (2009) Structure, attachment and entry of polyoma- and papillomaviruses. Virology 384: 400-409.
    • (2009) Virology , vol.384 , pp. 400-409
    • Sapp, M.1    Day, P.M.2
  • 3
    • 34447122482 scopus 로고    scopus 로고
    • Genital transmission of HPV in a mouse model is potentiated by nonoxynol-9 and inhibited by carrageenan
    • Roberts JN, Buck CB, Thompson CD, Kines R, Bernardo M, et al. (2007) Genital transmission of HPV in a mouse model is potentiated by nonoxynol-9 and inhibited by carrageenan. Nat Med 13: 857-861.
    • (2007) Nat Med , vol.13 , pp. 857-861
    • Roberts, J.N.1    Buck, C.B.2    Thompson, C.D.3    Kines, R.4    Bernardo, M.5
  • 4
    • 51649111041 scopus 로고    scopus 로고
    • HPV16 and BPV1 infection can be blocked by the dynamin inhibitor dynasore
    • Abban CY, Bradbury NA, Meneses PI, (2008) HPV16 and BPV1 infection can be blocked by the dynamin inhibitor dynasore. Am J Ther 15: 304-311.
    • (2008) Am J Ther , vol.15 , pp. 304-311
    • Abban, C.Y.1    Bradbury, N.A.2    Meneses, P.I.3
  • 5
    • 0037334521 scopus 로고    scopus 로고
    • Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells
    • Bousarghin L, Touze A, Sizaret PY, Coursaget P, (2003) Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells. J Virol 77: 3846-3850.
    • (2003) J Virol , vol.77 , pp. 3846-3850
    • Bousarghin, L.1    Touze, A.2    Sizaret, P.Y.3    Coursaget, P.4
  • 6
    • 0037347091 scopus 로고    scopus 로고
    • Papillomaviruses infect cells via a clathrin-dependent pathway
    • Day PM, Lowy DR, Schiller JT, (2003) Papillomaviruses infect cells via a clathrin-dependent pathway. Virology 307: 1-11.
    • (2003) Virology , vol.307 , pp. 1-11
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 7
    • 53049094647 scopus 로고    scopus 로고
    • Human papillomavirus type 16 entry: retrograde cell surface transport along actin-rich protrusions
    • Schelhaas M, Ewers H, Rajamaki ML, Day PM, Schiller JT, et al. (2008) Human papillomavirus type 16 entry: retrograde cell surface transport along actin-rich protrusions. PLoS Pathog 4: e1000148.
    • (2008) PLoS Pathog , vol.4
    • Schelhaas, M.1    Ewers, H.2    Rajamaki, M.L.3    Day, P.M.4    Schiller, J.T.5
  • 8
    • 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 JL, Campos SK, Ozbun MA, (2007) Human papillomavirus type 31 uses a caveolin 1- and dynamin 2-mediated entry pathway for infection of human keratinocytes. J Virol 81: 9922-9931.
    • (2007) J Virol , vol.81 , pp. 9922-9931
    • Smith, J.L.1    Campos, S.K.2    Ozbun, M.A.3
  • 9
    • 53749105515 scopus 로고    scopus 로고
    • Clathrin- and caveolin-independent entry of human papillomavirus type 16-involvement of tetraspanin-enriched microdomains (TEMs)
    • Spoden G, Freitag K, Husmann M, Boller K, Sapp M, et al. (2008) Clathrin- and caveolin-independent entry of human papillomavirus type 16-involvement of tetraspanin-enriched microdomains (TEMs). PLoS One 3: e3313.
    • (2008) PLoS One , vol.3
    • Spoden, G.1    Freitag, K.2    Husmann, M.3    Boller, K.4    Sapp, M.5
  • 12
    • 0035899891 scopus 로고    scopus 로고
    • Gene transfer using human papillomavirus pseudovirions varies according to virus genotype and requires cell surface heparan sulfate
    • Combita AL, Touze A, Bousarghin L, Sizaret PY, Munoz N, et al. (2001) Gene transfer using human papillomavirus pseudovirions varies according to virus genotype and requires cell surface heparan sulfate. FEMS Microbiol Lett 204: 183-188.
    • (2001) FEMS Microbiol Lett , vol.204 , pp. 183-188
    • Combita, A.L.1    Touze, A.2    Bousarghin, L.3    Sizaret, P.Y.4    Munoz, N.5
  • 13
    • 0035156505 scopus 로고    scopus 로고
    • Human papillomavirus infection requires cell surface heparan sulfate
    • Giroglou T, Florin L, Schafer F, Streeck RE, Sapp M, (2001) Human papillomavirus infection requires cell surface heparan sulfate. J Virol 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
  • 14
    • 60049100934 scopus 로고    scopus 로고
    • Role of heparan sulfate in attachment to and infection of the murine female genital tract by human papillomavirus
    • Johnson KM, Kines RC, Roberts JN, Lowy DR, Schiller JT, et al. (2009) Role of heparan sulfate in attachment to and infection of the murine female genital tract by human papillomavirus. J Virol 83: 2067-2074.
    • (2009) J Virol , vol.83 , pp. 2067-2074
    • Johnson, K.M.1    Kines, R.C.2    Roberts, J.N.3    Lowy, D.R.4    Schiller, J.T.5
  • 15
    • 33748499815 scopus 로고    scopus 로고
    • Keratinocyte-secreted laminin 5 can function as a transient receptor for human papillomaviruses by binding virions and transferring them to adjacent cells
    • Culp TD, Budgeon LR, Marinkovich MP, Meneguzzi G, Christensen ND, (2006) Keratinocyte-secreted laminin 5 can function as a transient receptor for human papillomaviruses by binding virions and transferring them to adjacent cells. J Virol 80: 8940-8950.
    • (2006) J Virol , vol.80 , pp. 8940-8950
    • Culp, T.D.1    Budgeon, L.R.2    Marinkovich, M.P.3    Meneguzzi, G.4    Christensen, N.D.5
  • 16
    • 70049114748 scopus 로고    scopus 로고
    • Target cell cyclophilins facilitate human papillomavirus type 16 infection
    • Bienkowska-Haba M, Patel HD, Sapp M, (2009) Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog 5: e1000524.
    • (2009) PLoS Pathog , vol.5
    • Bienkowska-Haba, M.1    Patel, H.D.2    Sapp, M.3
  • 17
    • 31944439998 scopus 로고    scopus 로고
    • Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection
    • Richards RM, Lowy DR, Schiller JT, Day PM, (2006) Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection. Proc Natl Acad Sci U S A 103: 1522-1527.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 1522-1527
    • Richards, R.M.1    Lowy, D.R.2    Schiller, J.T.3    Day, P.M.4
  • 18
    • 42449153250 scopus 로고    scopus 로고
    • Mechanisms of human papillomavirus type 16 neutralization by l2 cross-neutralizing and l1 type-specific antibodies
    • Day PM, Gambhira R, Roden RB, Lowy DR, Schiller JT, (2008) Mechanisms of human papillomavirus type 16 neutralization by l2 cross-neutralizing and l1 type-specific antibodies. J Virol 82: 4638-4646.
    • (2008) J Virol , vol.82 , pp. 4638-4646
    • Day, P.M.1    Gambhira, R.2    Roden, R.B.3    Lowy, D.R.4    Schiller, J.T.5
  • 19
    • 57349115458 scopus 로고    scopus 로고
    • Heparan sulfate-independent cell binding and infection with furin-precleaved papillomavirus capsids
    • Day PM, Lowy DR, Schiller JT, (2008) Heparan sulfate-independent cell binding and infection with furin-precleaved papillomavirus capsids. J Virol 82: 12565-12568.
    • (2008) J Virol , vol.82 , pp. 12565-12568
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 20
    • 73949127173 scopus 로고    scopus 로고
    • The initial steps leading to papillomavirus infection occur on the basement membrane prior to cell surface binding
    • Kines RC, Thompson CD, Lowy DR, Schiller JT, Day PM, (2009) The initial steps leading to papillomavirus infection occur on the basement membrane prior to cell surface binding. Proc Natl Acad Sci U S A 106: 20458-20463.
    • (2009) Proc Natl Acad Sci U S A , 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
  • 21
    • 35148819635 scopus 로고    scopus 로고
    • Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus
    • Selinka HC, Florin L, Patel HD, Freitag K, Schmidtke M, et al. (2007) Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus. J Virol 81: 10970-10980.
    • (2007) J Virol , vol.81 , pp. 10970-10980
    • Selinka, H.C.1    Florin, L.2    Patel, H.D.3    Freitag, K.4    Schmidtke, M.5
  • 22
    • 33847685344 scopus 로고    scopus 로고
    • Mechanisms regulating expression of the HPV 31 L1 and L2 capsid proteins and pseudovirion entry
    • Hindmarsh PL, Laimins LA, (2007) Mechanisms regulating expression of the HPV 31 L1 and L2 capsid proteins and pseudovirion entry. Virol J 4: 19.
    • (2007) Virol J , vol.4 , pp. 19
    • Hindmarsh, P.L.1    Laimins, L.A.2
  • 23
    • 0036432779 scopus 로고    scopus 로고
    • Analysis of the infectious entry pathway of human papillomavirus type 33 pseudovirions
    • Selinka HC, Giroglou T, Sapp M, (2002) Analysis of the infectious entry pathway of human papillomavirus type 33 pseudovirions. Virology 299: 279-287.
    • (2002) Virology , vol.299 , pp. 279-287
    • Selinka, H.C.1    Giroglou, T.2    Sapp, M.3
  • 24
    • 1242315658 scopus 로고    scopus 로고
    • Kinetics of in vitro adsorption and entry of papillomavirus virions
    • Culp TD, Christensen ND, (2004) Kinetics of in vitro adsorption and entry of papillomavirus virions. Virology 319: 152-161.
    • (2004) Virology , vol.319 , pp. 152-161
    • Culp, T.D.1    Christensen, N.D.2
  • 25
    • 79959959890 scopus 로고    scopus 로고
    • Single-particle tracking as a quantitative microscopy-based approach to unravel cell entry mechanisms of viruses and pharmaceutical nanoparticles
    • Ruthardt N, Lamb DC, Brauchle C, (2011) Single-particle tracking as a quantitative microscopy-based approach to unravel cell entry mechanisms of viruses and pharmaceutical nanoparticles. Mol Ther 19: 1199-1211.
    • (2011) Mol Ther , vol.19 , pp. 1199-1211
    • Ruthardt, N.1    Lamb, D.C.2    Brauchle, C.3
  • 26
    • 73549093632 scopus 로고    scopus 로고
    • Virus movements on the plasma membrane support infection and transmission between cells
    • Burckhardt CJ, Greber UF, (2009) Virus movements on the plasma membrane support infection and transmission between cells. PLoS Pathog 5: e1000621.
    • (2009) PLoS Pathog , vol.5
    • Burckhardt, C.J.1    Greber, U.F.2
  • 27
    • 33645019359 scopus 로고    scopus 로고
    • Human papillomaviruses bind a basal extracellular matrix component secreted by keratinocytes which is distinct from a membrane-associated receptor
    • Culp TD, Budgeon LR, Christensen ND, (2006) Human papillomaviruses bind a basal extracellular matrix component secreted by keratinocytes which is distinct from a membrane-associated receptor. Virology 347: 147-159.
    • (2006) Virology , vol.347 , pp. 147-159
    • Culp, T.D.1    Budgeon, L.R.2    Christensen, N.D.3
  • 28
    • 79953718772 scopus 로고    scopus 로고
    • A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis
    • Taylor MJ, Perrais D, Merrifield CJ, (2011) A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis. PLoS Biol 9: e1000604.
    • (2011) PLoS Biol , vol.9
    • Taylor, M.J.1    Perrais, D.2    Merrifield, C.J.3
  • 29
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield CJ, Feldman ME, Wan L, Almers W, (2002) Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat Cell Biol 4: 691-698.
    • (2002) Nat Cell Biol , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 30
    • 0032541402 scopus 로고    scopus 로고
    • The clathrin endocytic pathway in viral infection
    • DeTulleo L, Kirchhausen T, (1998) The clathrin endocytic pathway in viral infection. EMBO J 17: 4585-4593.
    • (1998) EMBO J , vol.17 , pp. 4585-4593
    • DeTulleo, L.1    Kirchhausen, T.2
  • 31
    • 0023669065 scopus 로고
    • Inhibition of endocytosis by anti-clathrin antibodies
    • Doxsey SJ, Brodsky FM, Blank GS, Helenius A, (1987) Inhibition of endocytosis by anti-clathrin antibodies. Cell 50: 453-463.
    • (1987) Cell , vol.50 , pp. 453-463
    • Doxsey, S.J.1    Brodsky, F.M.2    Blank, G.S.3    Helenius, A.4
  • 32
    • 0019256559 scopus 로고
    • Adsorptive endocytosis of Semliki Forest virus
    • Marsh M, Helenius A, (1980) Adsorptive endocytosis of Semliki Forest virus. J Mol Biol 142: 439-454.
    • (1980) J Mol Biol , vol.142 , pp. 439-454
    • Marsh, M.1    Helenius, A.2
  • 33
    • 0036298810 scopus 로고    scopus 로고
    • Dissecting virus entry via endocytosis
    • Sieczkarski SB, Whittaker GR, (2002) Dissecting virus entry via endocytosis. J Gen Virol 83: 1535-1545.
    • (2002) J Gen Virol , vol.83 , pp. 1535-1545
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 34
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae
    • Damm EM, Pelkmans L, Kartenbeck J, Mezzacasa A, Kurzchalia T, et al. (2005) Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J Cell Biol 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    Kurzchalia, T.5
  • 35
    • 79955436301 scopus 로고    scopus 로고
    • Role of endosomes in simian virus 40 entry and infection
    • Engel S, Heger T, Mancini R, Herzog F, Kartenbeck J, et al. (2011) Role of endosomes in simian virus 40 entry and infection. J Virol 85: 4198-4211.
    • (2011) J Virol , vol.85 , pp. 4198-4211
    • Engel, S.1    Heger, T.2    Mancini, R.3    Herzog, F.4    Kartenbeck, J.5
  • 36
    • 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, (2001) Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 3: 473-483.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 37
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest virus from acidic prelysosomal vacuoles
    • Marsh M, Bolzau E, Helenius A, (1983) Penetration of Semliki Forest virus from acidic prelysosomal vacuoles. Cell 32: 931-940.
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 38
    • 69449096573 scopus 로고    scopus 로고
    • Molecular mechanisms of clathrin-independent endocytosis
    • Hansen CG, Nichols BJ, (2009) Molecular mechanisms of clathrin-independent endocytosis. J Cell Sci 122: 1713-1721.
    • (2009) J Cell Sci , vol.122 , pp. 1713-1721
    • Hansen, C.G.1    Nichols, B.J.2
  • 39
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • Glebov OO, Bright NA, Nichols BJ, (2006) Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat Cell Biol 8: 46-54.
    • (2006) Nat Cell Biol , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 40
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • Pelkmans L, Burli T, Zerial M, Helenius A, (2004) Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic. Cell 118: 767-780.
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Burli, T.2    Zerial, M.3    Helenius, A.4
  • 43
    • 0038485582 scopus 로고    scopus 로고
    • Interaction of L2 with beta-actin directs intracellular transport of papillomavirus and infection
    • Yang R, Yutzy WHt, Viscidi RP, Roden RB, (2003) Interaction of L2 with beta-actin directs intracellular transport of papillomavirus and infection. J Biol Chem 278: 12546-12553.
    • (2003) J Biol Chem , vol.278 , pp. 12546-12553
    • Yang, R.1    Yutzy, W.H.2    Viscidi, R.P.3    Roden, R.B.4
  • 44
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J, Helenius A, (2009) Virus entry by macropinocytosis. Nat Cell Biol 11: 510-520.
    • (2009) Nat Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 46
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A, (2008) Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320: 531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 47
    • 77952710490 scopus 로고    scopus 로고
    • Vaccinia virus strains use distinct forms of macropinocytosis for host-cell entry
    • Mercer J, Knebel S, Schmidt FI, Crouse J, Burkard C, et al. (2010) Vaccinia virus strains use distinct forms of macropinocytosis for host-cell entry. Proc Natl Acad Sci U S A 107: 9346-9351.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9346-9351
    • Mercer, J.1    Knebel, S.2    Schmidt, F.I.3    Crouse, J.4    Burkard, C.5
  • 48
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
    • Brown FD, Rozelle AL, Yin HL, Balla T, Donaldson JG, (2001) Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic. J Cell Biol 154: 1007-1017.
    • (2001) J Cell Biol , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 49
    • 3342977736 scopus 로고    scopus 로고
    • Characterization of a nonclathrin endocytic pathway: membrane cargo and lipid requirements
    • Naslavsky N, Weigert R, Donaldson JG, (2004) Characterization of a nonclathrin endocytic pathway: membrane cargo and lipid requirements. Mol Biol Cell 15: 3542-3552.
    • (2004) Mol Biol Cell , vol.15 , pp. 3542-3552
    • Naslavsky, N.1    Weigert, R.2    Donaldson, J.G.3
  • 50
    • 0033601075 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation
    • Honda A, Nogami M, Yokozeki T, Yamazaki M, Nakamura H, et al. (1999) Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. Cell 99: 521-532.
    • (1999) Cell , vol.99 , pp. 521-532
    • Honda, A.1    Nogami, M.2    Yokozeki, T.3    Yamazaki, M.4    Nakamura, H.5
  • 51
    • 78249252059 scopus 로고    scopus 로고
    • Come in and take your coat off - how host cells provide endocytosis for virus entry
    • Schelhaas M, (2010) Come in and take your coat off - how host cells provide endocytosis for virus entry. Cell Microbiol 12: 1378-1388.
    • (2010) Cell Microbiol , vol.12 , pp. 1378-1388
    • Schelhaas, M.1
  • 52
    • 0033605153 scopus 로고    scopus 로고
    • The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes
    • Joyce JG, Tung JS, Przysiecki CT, Cook JC, Lehman ED, et al. (1999) The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes. J Biol Chem 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
  • 53
    • 52649120857 scopus 로고    scopus 로고
    • Caveolin-1-dependent infectious entry of human papillomavirus type 31 in human keratinocytes proceeds to the endosomal pathway for pH-dependent uncoating
    • Smith JL, Campos SK, Wandinger-Ness A, Ozbun MA, (2008) Caveolin-1-dependent infectious entry of human papillomavirus type 31 in human keratinocytes proceeds to the endosomal pathway for pH-dependent uncoating. J Virol 82: 9505-9512.
    • (2008) J Virol , vol.82 , pp. 9505-9512
    • Smith, J.L.1    Campos, S.K.2    Wandinger-Ness, A.3    Ozbun, M.A.4
  • 54
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B, (1978) Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci U S A 75: 3327-3331.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 55
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • Sieczkarski SB, Whittaker GR, (2003) Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Traffic 4: 333-343.
    • (2003) Traffic , vol.4 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 56
    • 4644352291 scopus 로고    scopus 로고
    • Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression
    • Day PM, Baker CC, Lowy DR, Schiller JT, (2004) Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression. Proc Natl Acad Sci U S A 101: 14252-14257.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 14252-14257
    • Day, P.M.1    Baker, C.C.2    Lowy, D.R.3    Schiller, J.T.4
  • 57
    • 58149390171 scopus 로고    scopus 로고
    • Host cell factors and functions involved in vesicular stomatitis virus entry
    • Johannsdottir HK, Mancini R, Kartenbeck J, Amato L, Helenius A, (2009) Host cell factors and functions involved in vesicular stomatitis virus entry. J Virol 83: 440-453.
    • (2009) J Virol , vol.83 , pp. 440-453
    • Johannsdottir, H.K.1    Mancini, R.2    Kartenbeck, J.3    Amato, L.4    Helenius, A.5
  • 58
    • 0024844490 scopus 로고
    • Endocytosis of simian virus 40 into the endoplasmic reticulum
    • Kartenbeck J, Stukenbrok H, Helenius A, (1989) Endocytosis of simian virus 40 into the endoplasmic reticulum. J Cell Biol 109: 2721-2729.
    • (1989) J Cell Biol , vol.109 , pp. 2721-2729
    • Kartenbeck, J.1    Stukenbrok, H.2    Helenius, A.3
  • 59
    • 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, et al. (2007) Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 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
  • 60
    • 0029025421 scopus 로고
    • Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells
    • Volpers C, Unckell F, Schirmacher P, Streeck RE, Sapp M, (1995) Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells. J Virol 69: 3258-3264.
    • (1995) J Virol , vol.69 , pp. 3258-3264
    • Volpers, C.1    Unckell, F.2    Schirmacher, P.3    Streeck, R.E.4    Sapp, M.5
  • 61
    • 77954230704 scopus 로고    scopus 로고
    • A major role for the minor capsid protein of human papillomavirus type 16 in immune escape
    • Fahey LM, Raff AB, Da Silva DM, Kast WM, (2009) A major role for the minor capsid protein of human papillomavirus type 16 in immune escape. J Immunol 183: 6151-6156.
    • (2009) J Immunol , vol.183 , pp. 6151-6156
    • Fahey, L.M.1    Raff, A.B.2    Da Silva, D.M.3    Kast, W.M.4
  • 62
    • 33747067917 scopus 로고    scopus 로고
    • Papillomavirus virus-like particles activate the PI3-kinase pathway via alpha-6 beta-4 integrin upon binding
    • Fothergill T, McMillan NA, (2006) Papillomavirus virus-like particles activate the PI3-kinase pathway via alpha-6 beta-4 integrin upon binding. Virology 352: 319-328.
    • (2006) Virology , vol.352 , pp. 319-328
    • Fothergill, T.1    McMillan, N.A.2
  • 63
    • 77953291134 scopus 로고    scopus 로고
    • Usage of heparan sulfate, integrins, and FAK in HPV16 infection
    • Abban CY, Meneses PI, (2010) Usage of heparan sulfate, integrins, and FAK in HPV16 infection. Virology 403: 1-16.
    • (2010) Virology , vol.403 , pp. 1-16
    • Abban, C.Y.1    Meneses, P.I.2
  • 64
    • 0018749038 scopus 로고
    • Chlorpromazine inhibits phagocytosis and exocytosis in rabbit polymorphonuclear leukocytes
    • Elferink JG, (1979) Chlorpromazine inhibits phagocytosis and exocytosis in rabbit polymorphonuclear leukocytes. Biochem Pharmacol 28: 965-968.
    • (1979) Biochem Pharmacol , vol.28 , pp. 965-968
    • Elferink, J.G.1
  • 65
    • 0023754229 scopus 로고
    • Calmodulin antagonists inhibit the phagocytic activity of cultured Kupffer cells
    • Watanabe S, Hirose M, Miyazaki A, Tomono M, Takeuchi M, et al. (1988) Calmodulin antagonists inhibit the phagocytic activity of cultured Kupffer cells. Lab Invest 59: 214-218.
    • (1988) Lab Invest , vol.59 , pp. 214-218
    • Watanabe, S.1    Hirose, M.2    Miyazaki, A.3    Tomono, M.4    Takeuchi, M.5
  • 66
    • 0019853722 scopus 로고
    • Differential effects of calmodulin antagonists on phospholipases A2 and C in thrombin-stimulated platelets
    • Walenga RW, Opas EE, Feinstein MB, (1981) Differential effects of calmodulin antagonists on phospholipases A2 and C in thrombin-stimulated platelets. J Biol Chem 256: 12523-12528.
    • (1981) J Biol Chem , vol.256 , pp. 12523-12528
    • Walenga, R.W.1    Opas, E.E.2    Feinstein, M.B.3
  • 67
    • 0033783042 scopus 로고    scopus 로고
    • Constitutive macropinocytosis in oncogene-transformed fibroblasts depends on sequential permanent activation of phosphoinositide 3-kinase and phospholipase C
    • Amyere M, Payrastre B, Krause U, Van Der Smissen P, Veithen A, et al. (2000) Constitutive macropinocytosis in oncogene-transformed fibroblasts depends on sequential permanent activation of phosphoinositide 3-kinase and phospholipase C. Mol Biol Cell 11: 3453-3467.
    • (2000) Mol Biol Cell , vol.11 , pp. 3453-3467
    • Amyere, M.1    Payrastre, B.2    Krause, U.3    van der Smissen, P.4    Veithen, A.5
  • 68
    • 0028924439 scopus 로고
    • Benzyl alcohol differently affects fluid phase endocytosis and exocytosis in renal epithelial cells
    • Giocondi MC, Mamdouh Z, Le Grimellec C, (1995) Benzyl alcohol differently affects fluid phase endocytosis and exocytosis in renal epithelial cells. Biochim Biophys Acta 1234: 197-202.
    • (1995) Biochim Biophys Acta , vol.1234 , pp. 197-202
    • Giocondi, M.C.1    Mamdouh, Z.2    Le Grimellec, C.3
  • 69
    • 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 SA, Havens MA, Meneses PI, (2009) Human papillomavirus type 16 infection of human keratinocytes requires clathrin and caveolin-1 and is brefeldin a sensitive. J Virol 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
  • 70
    • 63049113263 scopus 로고    scopus 로고
    • Defining macropinocytosis
    • Kerr MC, Teasdale RD, (2009) Defining macropinocytosis. Traffic 10: 364-371.
    • (2009) Traffic , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 71
    • 84856808484 scopus 로고    scopus 로고
    • Human Papillomavirus L2 facilitates viral escape from late endosomes via Sorting Nexin 17
    • Marusic MB, Ozbun MA, Campos SK, Myers MP, Banks L, (2011) Human Papillomavirus L2 facilitates viral escape from late endosomes via Sorting Nexin 17. Traffic 13: 455-67.
    • (2011) 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
  • 72
    • 68749122026 scopus 로고    scopus 로고
    • The role of NH4Cl and cysteine proteases in Human Papillomavirus type 16 infection
    • Dabydeen SA, Meneses PI, (2009) The role of NH4Cl and cysteine proteases in Human Papillomavirus type 16 infection. Virol J 6: 109.
    • (2009) Virol J , vol.6 , pp. 109
    • Dabydeen, S.A.1    Meneses, P.I.2
  • 73
    • 30344481121 scopus 로고    scopus 로고
    • A membrane-destabilizing peptide in capsid protein L2 is required for egress of papillomavirus genomes from endosomes
    • Kamper N, Day PM, Nowak T, Selinka HC, Florin L, et al. (2006) A membrane-destabilizing peptide in capsid protein L2 is required for egress of papillomavirus genomes from endosomes. J Virol 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
  • 74
    • 78650282789 scopus 로고    scopus 로고
    • Identification of the dynein light chains required for human papillomavirus infection
    • Schneider MA, Spoden GA, Florin L, Lambert C, (2011) Identification of the dynein light chains required for human papillomavirus infection. Cell Microbiol 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
  • 75
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin KS, Reggio H, Helenius A, Simons K, (1981) Infectious entry pathway of influenza virus in a canine kidney cell line. J Cell Biol 91: 601-613.
    • (1981) J Cell Biol , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 76
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust MJ, Lakadamyali M, Zhang F, Zhuang X, (2004) Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat Struct Mol Biol 11: 567-573.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 77
    • 79953273232 scopus 로고    scopus 로고
    • Dissection of the influenza A virus endocytic routes reveals macropinocytosis as an alternative entry pathway
    • de Vries E, Tscherne DM, Wienholts MJ, Cobos-Jimenez V, Scholte F, et al. (2011) Dissection of the influenza A virus endocytic routes reveals macropinocytosis as an alternative entry pathway. PLoS Pathog 7: e1001329.
    • (2011) PLoS Pathog , vol.7
    • de Vries, E.1    Tscherne, D.M.2    Wienholts, M.J.3    Cobos-Jimenez, V.4    Scholte, F.5
  • 78
    • 41949113636 scopus 로고    scopus 로고
    • A Raft-derived, Pak1-regulated entry participates in alpha2beta1 integrin-dependent sorting to caveosomes
    • Karjalainen M, Kakkonen E, Upla P, Paloranta H, Kankaanpaa P, et al. (2008) A Raft-derived, Pak1-regulated entry participates in alpha2beta1 integrin-dependent sorting to caveosomes. Mol Biol Cell 19: 2857-2869.
    • (2008) Mol Biol Cell , vol.19 , pp. 2857-2869
    • Karjalainen, M.1    Kakkonen, E.2    Upla, P.3    Paloranta, H.4    Kankaanpaa, P.5
  • 79
    • 47749126117 scopus 로고    scopus 로고
    • Lymphocytic choriomeningitis virus uses a novel endocytic pathway for infectious entry via late endosomes
    • Quirin K, Eschli B, Scheu I, Poort L, Kartenbeck J, et al. (2008) Lymphocytic choriomeningitis virus uses a novel endocytic pathway for infectious entry via late endosomes. Virology 378: 21-33.
    • (2008) Virology , vol.378 , pp. 21-33
    • Quirin, K.1    Eschli, B.2    Scheu, I.3    Poort, L.4    Kartenbeck, J.5
  • 81
    • 78149333191 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
    • Eierhoff T, Hrincius ER, Rescher U, Ludwig S, Ehrhardt C, (2010) The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog 6: e1001099.
    • (2010) PLoS Pathog , vol.6
    • Eierhoff, T.1    Hrincius, E.R.2    Rescher, U.3    Ludwig, S.4    Ehrhardt, C.5
  • 82
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and Quantitative Measurement of Protein-Protein Colocalization in Live Cells
    • Costes SV, Daelemans D, Cho EH, Dobbin Z, Pavlakis G, et al. (2004) Automatic and Quantitative Measurement of Protein-Protein Colocalization in Live Cells. Biophys J 86: 3993-4003.
    • (2004) Biophys J , vol.86 , pp. 3993-4003
    • Costes, S.V.1    Daelemans, D.2    Cho, E.H.3    Dobbin, Z.4    Pavlakis, G.5


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