메뉴 건너뛰기




Volumn 12, Issue 1, 2012, Pages 4-17

Tetraspanins - gateways for infection

Author keywords

Adhesion; Infectious disease; Membrane proteins; Tetraspanins

Indexed keywords

CELL MEMBRANE PROTEIN; MEMBRANE PROTEIN; SMALL INTERFERING RNA; TETRASPANIN;

EID: 84855862367     PISSN: 18715265     EISSN: 18755852     Source Type: Journal    
DOI: 10.2174/187152612798994957     Document Type: Review
Times cited : (66)

References (217)
  • 1
    • 77957736749 scopus 로고    scopus 로고
    • The evolution of vertebrate tetraspanins: Gene loss, retention, and massive positive selection after whole genome duplications
    • Huang, S.; Tian, H.; Chen, Z.; Yu, T.; Xu, A. The evolution of vertebrate tetraspanins: gene loss, retention, and massive positive selection after whole genome duplications. BMC Evol. Biol., 2010, 10, 306.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 306
    • Huang, S.1    Tian, H.2    Chen, Z.3    Yu, T.4    Xu, A.5
  • 4
    • 0033964768 scopus 로고    scopus 로고
    • Severely reduced female fertility in CD9-deficient mice
    • Le Naour, F.; Rubinstein, E.; Jasmin, C.; Prenant, M.; Boucheix, C. Severely reduced female fertility in CD9-deficient mice. Science, 2000, 287, (5451), 319-321.
    • (2000) Science , vol.287 , Issue.5451 , pp. 319-321
    • Le Naour, F.1    Rubinstein, E.2    Jasmin, C.3    Prenant, M.4    Boucheix, C.5
  • 5
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of Tetraspanin Proteins: Modulation of CD151 Lateral Interactions, Subcellular Distribution, and Integrin-dependent Cell Morphology
    • Yang, X.; Claas, C.; Kraeft, S. K.; Chen, L. B.; Wang, Z.; Kreidberg, J. A.; Hemler, M. E. Palmitoylation of Tetraspanin Proteins: Modulation of CD151 Lateral Interactions, Subcellular Distribution, and Integrin-dependent Cell Morphology. Mol. Biol. Cell, 2002, 13(3), 767-781.
    • (2002) Mol. Biol. Cell , vol.13 , Issue.3 , pp. 767-781
    • Yang, X.1    Claas, C.2    Kraeft, S.K.3    Chen, L.B.4    Wang, Z.5    Kreidberg, J.A.6    Hemler, M.E.7
  • 6
    • 0035862964 scopus 로고    scopus 로고
    • CD81 extracellular domain 3D structure: Insight into the tetraspanin superfamily structural motifs
    • Kitadokoro, K.; Bordo, D.; Galli, G.; Petracca, R.; Falugi, F.; Abrignani, S.; Grandi, G.; Bolognesi, M. CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs. Embo J., 2001, 20, (1-2), 12-18.
    • (2001) Embo J. , vol.20 , Issue.1-2 , pp. 12-18
    • Kitadokoro, K.1    Bordo, D.2    Galli, G.3    Petracca, R.4    Falugi, F.5    Abrignani, S.6    Grandi, G.7    Bolognesi, M.8
  • 8
    • 70449703290 scopus 로고    scopus 로고
    • Defining the role of laminin-332 in carcinoma
    • Guess, C. M.; Quaranta, V. Defining the role of laminin-332 in carcinoma. Matrix Biol., 2009, 28, (8), 445-455.
    • (2009) Matrix Biol. , vol.28 , Issue.8 , pp. 445-455
    • Guess, C.M.1    Quaranta, V.2
  • 9
    • 77953064012 scopus 로고    scopus 로고
    • Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
    • Stipp, C. S. Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets. Expert Rev. Mol. Med., 2010, 12, e3.
    • (2010) Expert Rev. Mol. Med. , vol.12
    • Stipp, C.S.1
  • 12
    • 0030931136 scopus 로고    scopus 로고
    • Dominant and digenic mutations in the peripherin/RDS and ROM1 genes in retinitis pigmentosa
    • Dryja, T. P.; Hahn, L. B.; Kajiwara, K.; Berson, E. L. Dominant and digenic mutations in the peripherin/RDS and ROM1 genes in retinitis pigmentosa. Invest. Ophthalmol. Vis. Sci., 1997, 38, (10), 1972-1982.
    • (1997) Invest. Ophthalmol. Vis. Sci. , vol.38 , Issue.10 , pp. 1972-1982
    • Dryja, T.P.1    Hahn, L.B.2    Kajiwara, K.3    Berson, E.L.4
  • 14
    • 4944239350 scopus 로고    scopus 로고
    • CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin
    • Karamatic Crew, V.; Burton, N.; Kagan, A.; Green, C. A.; Levene, C.; Flinter, F.; Brady, R. L.; Daniels, G.; Anstee, D. J. CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood, 2004, 104(8), 2217-2223
    • (2004) Blood , vol.104 , Issue.8 , pp. 2217-2223
    • Karamatic Crew, V.1    Burton, N.2    Kagan, A.3    Green, C.A.4    Levene, C.5    Flinter, F.6    Brady, R.L.7    Daniels, G.8    Anstee, D.J.9
  • 16
    • 79955599124 scopus 로고    scopus 로고
    • Novel TSPAN12 mutations in patients with familial exudative vitreoretinopathy and their associated phenotypes
    • Yang, H.; Xiao, X.; Li, S.; Mai, G.; Zhang, Q. Novel TSPAN12 mutations in patients with familial exudative vitreoretinopathy and their associated phenotypes. Mol. Vis., 2011, 17, 1128-1135.
    • (2011) Mol. Vis. , vol.17 , pp. 1128-1135
    • Yang, H.1    Xiao, X.2    Li, S.3    Mai, G.4    Zhang, Q.5
  • 17
    • 70349838225 scopus 로고    scopus 로고
    • TSPAN12 regulates retinal vascular development by promoting Norrin-but not Wnt-induced FZD4/beta-catenin signaling
    • Junge, H. J.; Yang, S.; Burton, J. B.; Paes, K.; Shu, X.; French, D. M.; Costa, M.; Rice, D. S.; Ye, W., TSPAN12 regulates retinal vascular development by promoting Norrin-but not Wnt-induced FZD4/beta-catenin signaling. Cell, 2009, 139, (2), 299-311.
    • (2009) Cell , vol.139 , Issue.2 , pp. 299-311
    • Junge, H.J.1    Yang, S.2    Burton, J.B.3    Paes, K.4    Shu, X.5    French, D.M.6    Costa, M.7    Rice, D.S.8    Ye, W.9
  • 19
    • 79954586065 scopus 로고    scopus 로고
    • The effects of a CD81 null mutation on retinal pigment epithelium in mice
    • Pan, Y.; Geisert, D. F.; Orr, W. E.; Geisert, E. E. The effects of a CD81 null mutation on retinal pigment epithelium in mice. Neurochem. Res., 2011, 36, (4), 569-573.
    • (2011) Neurochem. Res. , vol.36 , Issue.4 , pp. 569-573
    • Pan, Y.1    Geisert, D.F.2    Orr, W.E.3    Geisert, E.E.4
  • 20
    • 67349263394 scopus 로고    scopus 로고
    • Trafficking and function of the tetraspanin CD63
    • Pols, M. S.; Klumperman, J. Trafficking and function of the tetraspanin CD63. Exp. Cell Res., 2009, 315, (9), 1584-1592.
    • (2009) Exp. Cell Res. , vol.315 , Issue.9 , pp. 1584-1592
    • Pols, M.S.1    Klumperman, J.2
  • 21
    • 75749138551 scopus 로고    scopus 로고
    • N-linked glycan-dependent interaction of CD63 with CXCR4 at the Golgi apparatus induces downregulation of CXCR4
    • Yoshida, T.; Ebina, H.; Koyanagi, Y. N-linked glycan-dependent interaction of CD63 with CXCR4 at the Golgi apparatus induces downregulation of CXCR4. Microbiol. Immunol., 2009, 53(11), 629-635.
    • (2009) Microbiol. Immunol. , vol.53 , Issue.11 , pp. 629-635
    • Yoshida, T.1    Ebina, H.2    Koyanagi, Y.3
  • 22
    • 54049113079 scopus 로고    scopus 로고
    • The tetraspanin CD63 is involved in granule targeting of neutrophil elastase
    • Kallquist, L.; Hansson, M.; Persson, A. M.; Janssen, H.; Calafat, J.; Tapper, H.; Olsson, I. The tetraspanin CD63 is involved in granule targeting of neutrophil elastase. Blood, 2008, 112(8), 3444-3454.
    • (2008) Blood , vol.112 , Issue.8 , pp. 3444-3454
    • Kallquist, L.1    Hansson, M.2    Persson, A.M.3    Janssen, H.4    Calafat, J.5    Tapper, H.6    Olsson, I.7
  • 23
    • 78049511240 scopus 로고    scopus 로고
    • Palmitoylationdependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes
    • Flannery, A. R.; Czibener, C.; Andrews, N. W. Palmitoylationdependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes. J. Cell Biol., 2010, 191(3), 599-613.
    • (2010) J. Cell Biol. , vol.191 , Issue.3 , pp. 599-613
    • Flannery, A.R.1    Czibener, C.2    Andrews, N.W.3
  • 24
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes--vesicular carriers for intercellular communication
    • Simons, M.; Raposo, G. Exosomes--vesicular carriers for intercellular communication. Curr. Opin. Cell Biol., 2009, 21, (4), 575-581.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , Issue.4 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 25
    • 21544453605 scopus 로고    scopus 로고
    • Exosome release by reticulocytes--an integral part of the red blood cell differentiation system
    • Blanc, L.; De Gassart, A.; Geminard, C.; Bette-Bobillo, P.; Vidal, M. Exosome release by reticulocytes--an integral part of the red blood cell differentiation system. Blood Cells Mol. Dis., 2005, 35, (1), 21-26.
    • (2005) Blood Cells Mol. Dis. , vol.35 , Issue.1 , pp. 21-26
    • Blanc, L.1    De Gassart, A.2    Geminard, C.3    Bette-Bobillo, P.4    Vidal, M.5
  • 26
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Thery, C.; Ostrowski, M.; Segura, E. Membrane vesicles as conveyors of immune responses. Nat. Rev. Immunol., 2009, 9(8), 581-593.
    • (2009) Nat. Rev. Immunol. , vol.9 , Issue.8 , pp. 581-593
    • Thery, C.1    Ostrowski, M.2    Segura, E.3
  • 27
    • 33745280126 scopus 로고    scopus 로고
    • The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans
    • Liegeois, S.; Benedetto, A.; Garnier, J. M.; Schwab, Y.; Labouesse, M. The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans. J. Cell Biol., 2006, 173(6), 949-961.
    • (2006) J. Cell Biol. , vol.173 , Issue.6 , pp. 949-961
    • Liegeois, S.1    Benedetto, A.2    Garnier, J.M.3    Schwab, Y.4    Labouesse, M.5
  • 28
    • 67249115310 scopus 로고    scopus 로고
    • Secretion of Hedgehogrelated peptides and WNT during Caenorhabditis elegans development
    • Kolotuev, I.; Apaydin, A.; Labouesse, M. Secretion of Hedgehogrelated peptides and WNT during Caenorhabditis elegans development. Traffic, 2009, 10(7), 803-810.
    • (2009) Traffic , vol.10 , Issue.7 , pp. 803-810
    • Kolotuev, I.1    Apaydin, A.2    Labouesse, M.3
  • 29
    • 33646416463 scopus 로고    scopus 로고
    • The regulation of exosome secretion: A novel function of the p53 protein
    • Yu, X.; Harris, S. L.; Levine, A. J. The regulation of exosome secretion: a novel function of the p53 protein. Cancer Res., 2006, 66(9), 4795-4801.
    • (2006) Cancer Res. , vol.66 , Issue.9 , pp. 4795-4801
    • Yu, X.1    Harris, S.L.2    Levine, A.J.3
  • 30
    • 33751199883 scopus 로고    scopus 로고
    • Exosomes: From biogenesis and secretion to biological function
    • Keller, S.; Sanderson, M. P.; Stoeck, A.; Altevogt, P. Exosomes: from biogenesis and secretion to biological function. Immunol. Lett., 2006, 107(2), 102-108.
    • (2006) Immunol. Lett. , vol.107 , Issue.2 , pp. 102-108
    • Keller, S.1    Sanderson, M.P.2    Stoeck, A.3    Altevogt, P.4
  • 32
    • 34250325547 scopus 로고    scopus 로고
    • Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes
    • Fang, Y.; Wu, N.; Gan, X.; Yan, W.; Morrell, J. C.; Gould, S. J. Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes. PLoS Biol., 2007, 5(6), e158.
    • (2007) PLoS Biol. , vol.5 , Issue.6
    • Fang, Y.1    Wu, N.2    Gan, X.3    Yan, W.4    Morrell, J.C.5    Gould, S.J.6
  • 35
    • 33846502114 scopus 로고    scopus 로고
    • Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies
    • Subra, C.; Laulagnier, K.; Perret, B.; Record, M. Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies. Biochimie, 2007, 89(2), 205-512.
    • (2007) Biochimie , vol.89 , Issue.2 , pp. 205-512
    • Subra, C.1    Laulagnier, K.2    Perret, B.3    Record, M.4
  • 36
    • 79953202918 scopus 로고    scopus 로고
    • Exosome target cell selection and the importance of exosomal tetraspanins: A hypothesis
    • Rana, S.; Zoller, M. Exosome target cell selection and the importance of exosomal tetraspanins: a hypothesis. Biochem. Soc. Trans., 2011, 39(2), 559-562.
    • (2011) Biochem. Soc. Trans. , vol.39 , Issue.2 , pp. 559-562
    • Rana, S.1    Zoller, M.2
  • 37
    • 67349263394 scopus 로고    scopus 로고
    • Trafficking and function of the tetraspanin CD63
    • Pols, M. S.; Klumperman, J. Trafficking and function of the tetraspanin CD63. Exp. Cell Res., 2009, 315(9),1584-1592
    • (2009) Exp. Cell Res. , vol.315 , Issue.9 , pp. 1584-1592
    • Pols, M.S.1    Klumperman, J.2
  • 39
    • 12344335722 scopus 로고    scopus 로고
    • Tetraspanin-Fc receptor interactions
    • Moseley, G. W. Tetraspanin-Fc receptor interactions. Platelets, 2005, 16(1), 3-12.
    • (2005) Platelets , vol.16 , Issue.1 , pp. 3-12
    • Moseley, G.W.1
  • 40
    • 0030587912 scopus 로고    scopus 로고
    • CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils
    • Skubitz, K. M.; Campbell, K. D.; Iida, J.; Skubitz, A. P. CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils. J. Immunol., 1996, 157(8), 3617-3626.
    • (1996) J. Immunol. , vol.157 , Issue.8 , pp. 3617-3626
    • Skubitz, K.M.1    Campbell, K.D.2    Iida, J.3    Skubitz, A.P.4
  • 41
    • 0035283345 scopus 로고    scopus 로고
    • CD81 and microglial activation in vitro: Proliferation, phagocytosis and nitric oxide production
    • Dijkstra, S.; Geisert, E. E. Jr.; Dijkstra, C. D.; Bar, P. R.; Joosten, E. A. CD81 and microglial activation in vitro: proliferation, phagocytosis and nitric oxide production. J. Neuroimmunol., 2001, 114(1-2), 151-159.
    • (2001) J. Neuroimmunol. , vol.114 , Issue.1-2 , pp. 151-159
    • Dijkstra, S.1    Geisert Jr., E.E.2    Dijkstra, C.D.3    Bar, P.R.4    Joosten, E.A.5
  • 42
    • 34948874257 scopus 로고    scopus 로고
    • Tetraspanin CD81 is required for the alpha v beta5-integrin-dependent particle-binding step of RPE phagocytosis
    • Chang, Y.; Finnemann, S. C. Tetraspanin CD81 is required for the alpha v beta5-integrin-dependent particle-binding step of RPE phagocytosis. J. Cell Sci., 2007, 120(Pt 17), 3053-3063.
    • (2007) J. Cell Sci. , vol.120 , Issue.PART 17 , pp. 3053-3063
    • Chang, Y.1    Finnemann, S.C.2
  • 43
    • 18744391391 scopus 로고    scopus 로고
    • Plunder and stowaways: Incorporation of cellular proteins by enveloped viruses
    • Cantin, R.; Methot, S.; Tremblay, M. J. Plunder and stowaways: incorporation of cellular proteins by enveloped viruses. J. Virol., 2005, 79(11), 6577-6587.
    • (2005) J. Virol. , vol.79 , Issue.11 , pp. 6577-6587
    • Cantin, R.1    Methot, S.2    Tremblay, M.J.3
  • 44
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The Viruses and their Replication
    • In, Knipe, D. M.; Howley, P. M. Eds. Lippincott Williams & Wilkins: Philadelphia
    • Lindenbach, B. D.; Thiel, H. J.; Rice, C. M. Flaviviridae: The Viruses and their Replication. In Fields Virology, Knipe, D. M.; Howley, P. M. Eds. Lippincott Williams & Wilkins: Philadelphia, 2007; pp 1101-1152.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 45
    • 34547094367 scopus 로고    scopus 로고
    • Hepatitis C Virus
    • In, Knipe, D. M.; Howley, P. M., Eds. Lippincott Williams & Wilkins: Philadelphia
    • Lemon, S. M.; Walker, C.; Alter, M. J.; Yi, M. Hepatitis C Virus. In Fields Virology, Knipe, D. M.; Howley, P. M., Eds. Lippincott Williams & Wilkins: Philadelphia, 2007; pp 1253-1304.
    • (2007) Fields Virology , pp. 1253-1304
    • Lemon, S.M.1    Walker, C.2    Alter, M.J.3    Yi, M.4
  • 46
    • 33747797031 scopus 로고    scopus 로고
    • Treating viral hepatitis C: Efficacy, side effects, and complications
    • Manns, M. P.; Wedemeyer, H.; Cornberg, M. Treating viral hepatitis C: efficacy, side effects, and complications. Gut, 2006, 55, (9), 1350-1359.
    • (2006) Gut , vol.55 , Issue.9 , pp. 1350-1359
    • Manns, M.P.1    Wedemeyer, H.2    Cornberg, M.3
  • 47
    • 0034775964 scopus 로고    scopus 로고
    • Biogenesis of hepatitis C virus envelope glycoproteins
    • Op De Beeck, A.; Cocquerel, L.; Dubuisson, J. Biogenesis of hepatitis C virus envelope glycoproteins. J. Gen. Virol., 2001, 82, (Pt 11), 2589-2595.
    • (2001) J. Gen. Virol. , vol.82 , Issue.PART 11 , pp. 2589-2595
    • de Beeck, O.A.1    Cocquerel, L.2    Dubuisson, J.3
  • 52
    • 77956641110 scopus 로고    scopus 로고
    • Distinct intracellular trafficking of hepatitis C virus in myeloid and plasmacytoid dendritic cells
    • Lambotin, M.; Baumert, T. F.; Barth, H. Distinct intracellular trafficking of hepatitis C virus in myeloid and plasmacytoid dendritic cells. J. Virol., 2010, 84(17), 8964-8969.
    • (2010) J. Virol. , vol.84 , Issue.17 , pp. 8964-8969
    • Lambotin, M.1    Baumert, T.F.2    Barth, H.3
  • 54
    • 78449234718 scopus 로고    scopus 로고
    • The SR-BI partner PDZK1 facilitates hepatitis C virus entry
    • Eyre, N. S.; Drummer, H. E.; Beard, M. R. The SR-BI partner PDZK1 facilitates hepatitis C virus entry. PLoS Pathog., 2010, 6, (10), e1001130
    • (2010) PLoS Pathog. , vol.6 , Issue.10
    • Eyre, N.S.1    Drummer, H.E.2    Beard, M.R.3
  • 55
    • 60149090028 scopus 로고    scopus 로고
    • Human occludin is a hepatitis C virus entry factor required for infection of mouse cells
    • Ploss, A.; Evans, M. J.; Gaysinskaya, V. A.; Panis, M.; You, H.; de Jong, Y. P.; Rice, C. M. Human occludin is a hepatitis C virus entry factor required for infection of mouse cells. Nature, 2009, 457, (7231), 882-886.
    • (2009) Nature , vol.457 , Issue.7231 , pp. 882-886
    • Ploss, A.1    Evans, M.J.2    Gaysinskaya, V.A.3    Panis, M.4    You, H.5    de Jong, Y.P.6    Rice, C.M.7
  • 57
    • 33847379511 scopus 로고    scopus 로고
    • Cytotoxic CD4+ T cells use granulysin to kill Cryptococcus neoformans, and activation of this pathway is defective in HIV patients
    • Zheng, C. F.; Ma, L. L.; Jones, G. J.; Gill, M. J.; Krensky, A. M.; Kubes, P.; Mody, C. H. Cytotoxic CD4+ T cells use granulysin to kill Cryptococcus neoformans, and activation of this pathway is defective in HIV patients. Blood, 2007, 109, (5), 2049-2057.
    • (2007) Blood , vol.109 , Issue.5 , pp. 2049-2057
    • Zheng, C.F.1    Ma, L.L.2    Jones, G.J.3    Gill, M.J.4    Krensky, A.M.5    Kubes, P.6    Mody, C.H.7
  • 58
    • 41149117446 scopus 로고    scopus 로고
    • The tight junction proteins claudin-1,-6, and-9 are entry cofactors for hepatitis C virus
    • Meertens, L.; Bertaux, C.; Cukierman, L.; Cormier, E.; Lavillette, D.; Cosset, F. L.; Dragic, T., The tight junction proteins claudin-1,-6, and-9 are entry cofactors for hepatitis C virus. J. Virol., 2008, 82(7), 3555-3560.
    • (2008) J. Virol. , vol.82 , Issue.7 , pp. 3555-3560
    • Meertens, L.1    Bertaux, C.2    Cukierman, L.3    Cormier, E.4    Lavillette, D.5    Cosset, F.L.6    Dragic, T.7
  • 59
    • 70350111336 scopus 로고    scopus 로고
    • The hepatitis C virus and its hepatic environment: A toxic but finely tuned partnership
    • Perrault, M.; Pecheur, E. I. The hepatitis C virus and its hepatic environment: a toxic but finely tuned partnership. Biochem. J., 2009, 423(3), 303-314.
    • (2009) Biochem. J. , vol.423 , Issue.3 , pp. 303-314
    • Perrault, M.1    Pecheur, E.I.2
  • 60
  • 64
    • 56949088527 scopus 로고    scopus 로고
    • EWI-2wint--a host cell factor inhibiting hepatitis C virus entry
    • Schuster, C.; Baumert, T. F. EWI-2wint--a host cell factor inhibiting hepatitis C virus entry. J. Hepatol., 2009, 50(1), 222-224.
    • (2009) J. Hepatol. , vol.50 , Issue.1 , pp. 222-224
    • Schuster, C.1    Baumert, T.F.2
  • 68
    • 74549150609 scopus 로고    scopus 로고
    • RNA interference and single particle tracking analysis of hepatitis C virus endocytosis
    • Coller, K. E.; Berger, K. L.; Heaton, N. S.; Cooper, J. D.; Yoon, R.; Randall, G. RNA interference and single particle tracking analysis of hepatitis C virus endocytosis. PLoS Pathog., 2009, 5(12), e1000702.
    • (2009) PLoS Pathog. , vol.5 , Issue.12
    • Coller, K.E.1    Berger, K.L.2    Heaton, N.S.3    Cooper, J.D.4    Yoon, R.5    Randall, G.6
  • 70
    • 77949380722 scopus 로고    scopus 로고
    • Novel function of CD81 in controlling hepatitis C virus replication
    • Zhang, Y. Y.; Zhang, B. H.; Ishii, K.; Liang, T. J. Novel function of CD81 in controlling hepatitis C virus replication. J. Virol., 2010, 84(7), 3396-3407.
    • (2010) J. Virol. , vol.84 , Issue.7 , pp. 3396-3407
    • Zhang, Y.Y.1    Zhang, B.H.2    Ishii, K.3    Liang, T.J.4
  • 74
    • 33745238967 scopus 로고    scopus 로고
    • Recombinant extracellular domains of tetraspanin proteins are potent inhibitors of the infection of macrophages by human immunodeficiency virus type 1
    • Ho, S. H.; Martin, F.; Higginbottom, A.; Partridge, L. J.; Parthasarathy, V.; Moseley, G. W.; Lopez, P.; Cheng-Mayer, C.; Monk, P. N. Recombinant extracellular domains of tetraspanin proteins are potent inhibitors of the infection of macrophages by human immunodeficiency virus type 1. J. Virol., 2006, 80(13), 6487-6496.
    • (2006) J. Virol. , vol.80 , Issue.13 , pp. 6487-6496
    • Ho, S.H.1    Martin, F.2    Higginbottom, A.3    Partridge, L.J.4    Parthasarathy, V.5    Moseley, G.W.6    Lopez, P.7    Cheng-Mayer, C.8    Monk, P.N.9
  • 76
    • 79952631349 scopus 로고    scopus 로고
    • A post-entry role for CD63 in early HIV-1 replication
    • Li, G.; Dziuba, N.; Friedrich, B.; Murray, J. L.; Ferguson, M. R. A post-entry role for CD63 in early HIV-1 replication. Virology, 2011, 412(2),315-324.
    • (2011) Virology , vol.412 , Issue.2 , pp. 315-324
    • Li, G.1    Dziuba, N.2    Friedrich, B.3    Murray, J.L.4    Ferguson, M.R.5
  • 77
    • 28844472114 scopus 로고    scopus 로고
    • Increased CXCR4-dependent HIV-1 fusion in activated T cells: Role of CD4/CXCR4 association
    • Zaitseva, M.; Romantseva, T.; Manischewitz, J.; Wang, J.; Goucher, D.; Golding, H. Increased CXCR4-dependent HIV-1 fusion in activated T cells: role of CD4/CXCR4 association. J. Leukoc. Biol., 2005, 78(6), 1306-1317.
    • (2005) J. Leukoc. Biol. , vol.78 , Issue.6 , pp. 1306-1317
    • Zaitseva, M.1    Romantseva, T.2    Manischewitz, J.3    Wang, J.4    Goucher, D.5    Golding, H.6
  • 78
    • 40449100704 scopus 로고    scopus 로고
    • A CD63 mutant inhibits Tcell tropic human immunodeficiency virus type 1 entry by disrupting CXCR4 trafficking to the plasma membrane
    • Yoshida, T.; Kawano, Y.; Sato, K.; Ando, Y.; Aoki, J.; Miura, Y.; Komano, J.; Tanaka, Y.; Koyanagi, Y. A CD63 mutant inhibits Tcell tropic human immunodeficiency virus type 1 entry by disrupting CXCR4 trafficking to the plasma membrane. Traffic, 2008, 9(4), 540-558.
    • (2008) Traffic , vol.9 , Issue.4 , pp. 540-558
    • Yoshida, T.1    Kawano, Y.2    Sato, K.3    Ando, Y.4    Aoki, J.5    Miura, Y.6    Komano, J.7    Tanaka, Y.8    Koyanagi, Y.9
  • 79
    • 78649333451 scopus 로고    scopus 로고
    • CD4 dimerization requires two cysteines in the cytoplasmic domain of the molecule and occurs in microdomains distinct from lipid rafts
    • Fournier, M.; Peyrou, M.; Bourgoin, L.; Maeder, C.; Tchou, I.; Foti, M. CD4 dimerization requires two cysteines in the cytoplasmic domain of the molecule and occurs in microdomains distinct from lipid rafts. Mol. Immunol., 2010, 47(16), 2594-2603.
    • (2010) Mol. Immunol. , vol.47 , Issue.16 , pp. 2594-2603
    • Fournier, M.1    Peyrou, M.2    Bourgoin, L.3    Maeder, C.4    Tchou, I.5    Foti, M.6
  • 80
    • 33746659382 scopus 로고    scopus 로고
    • Association between disruption of CD4 receptor dimerization and increased human immunodeficiency virus type 1 entry
    • Bourgeois, R.; Mercier, J.; Paquette-Brooks, I.; Cohen, E. A. Association between disruption of CD4 receptor dimerization and increased human immunodeficiency virus type 1 entry. Retrovirology, 2006, 3, 31.
    • (2006) Retrovirology , vol.3 , pp. 31
    • Bourgeois, R.1    Mercier, J.2    Paquette-Brooks, I.3    Cohen, E.A.4
  • 81
    • 6344258722 scopus 로고    scopus 로고
    • Endocytic host cell machinery plays a dominant role in intracellular trafficking of incoming human immunodeficiency virus type 1 in human placental trophoblasts
    • Vidricaire, G.; Imbeault, M.; Tremblay, M. J. Endocytic host cell machinery plays a dominant role in intracellular trafficking of incoming human immunodeficiency virus type 1 in human placental trophoblasts. J. Virol., 2004, 78(21), 11904-11915.
    • (2004) J. Virol. , vol.78 , Issue.21 , pp. 11904-11915
    • Vidricaire, G.1    Imbeault, M.2    Tremblay, M.J.3
  • 82
    • 34247330185 scopus 로고    scopus 로고
    • A clathrin, caveolae, and dynaminindependent endocytic pathway requiring free membrane cholesterol drives HIV-1 internalization and infection in polarized trophoblastic cells
    • Vidricaire, G.; Tremblay, M. J. A clathrin, caveolae, and dynaminindependent endocytic pathway requiring free membrane cholesterol drives HIV-1 internalization and infection in polarized trophoblastic cells. J. Mol. Biol., 2007, 368(5), 1267-1283.
    • (2007) J. Mol. Biol. , vol.368 , Issue.5 , pp. 1267-1283
    • Vidricaire, G.1    Tremblay, M.J.2
  • 84
    • 0026641320 scopus 로고
    • Modulation of cell surface molecules during HIV-1 infection of H9 cells. An immunoelectron microscopic study
    • Meerloo, T.; Parmentier, H. K.; Osterhaus, A. D.; Goudsmit, J.; Schuurman, H. J. Modulation of cell surface molecules during HIV-1 infection of H9 cells. An immunoelectron microscopic study. Aids, 1992, 6(10), 1105-1116.
    • (1992) Aids , vol.6 , Issue.10 , pp. 1105-1116
    • Meerloo, T.1    Parmentier, H.K.2    Osterhaus, A.D.3    Goudsmit, J.4    Schuurman, H.J.5
  • 85
    • 0027395736 scopus 로고
    • Host cell membrane proteins on human immunodeficiency virus type 1 after in vitro, infection of H9 cells and blood mononuclear cells. An immuno-electron microscopic study
    • Meerloo, T.; Sheikh, M. A.; Bloem, A. C.; de Ronde, A.; Schutten, M.; van Els, C. A.; Roholl, P. J.; Joling, P.; Goudsmit, J.; Schuurman, H. J. Host cell membrane proteins on human immunodeficiency virus type 1 after in vitro, infection of H9 cells and blood mononuclear cells. An immuno-electron microscopic study. J. Gen. Virol., 1993, 74(Pt 1), 129-135.
    • (1993) J. Gen. Virol. , Issue.74 PART 1 , pp. 129-135
    • Meerloo, T.1    Sheikh, M.A.2    Bloem, A.C.3    de Ronde, A.4    Schutten, M.5    van Els, C.A.6    Roholl, P.J.7    Joling, P.8    Goudsmit, J.9    Schuurman, H.J.10
  • 86
    • 0027332763 scopus 로고
    • Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV
    • Orentas, R. J.; Hildreth, J. E. Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV. AIDS Res Hum. Retroviruses, 1993, 9(11), 1157-1165.
    • (1993) AIDS Res Hum. Retroviruses , vol.9 , Issue.11 , pp. 1157-1165
    • Orentas, R.J.1    Hildreth, J.E.2
  • 87
    • 0031592609 scopus 로고    scopus 로고
    • Cell membrane vesicles are a major contaminant of gradientenriched human immunodeficiency virus type-1 preparations
    • Gluschankof, P.; Mondor, I.; Gelderblom, H. R.; Sattentau, Q. J. Cell membrane vesicles are a major contaminant of gradientenriched human immunodeficiency virus type-1 preparations. Virology, 1997, 230(1), 125-133.
    • (1997) Virology , vol.230 , Issue.1 , pp. 125-133
    • Gluschankof, P.1    Mondor, I.2    Gelderblom, H.R.3    Sattentau, Q.J.4
  • 89
    • 37849037354 scopus 로고    scopus 로고
    • Modulation of human immunodeficiency virus type 1 infectivity through incorporation of tetraspanin proteins
    • Sato, K.; Aoki, J.; Misawa, N.; Daikoku, E.; Sano, K.; Tanaka, Y.; Koyanagi, Y. Modulation of human immunodeficiency virus type 1 infectivity through incorporation of tetraspanin proteins. J. Virol., 2008, 82(2), 1021-1033.
    • (2008) J. Virol. , vol.82 , Issue.2 , pp. 1021-1033
    • Sato, K.1    Aoki, J.2    Misawa, N.3    Daikoku, E.4    Sano, K.5    Tanaka, Y.6    Koyanagi, Y.7
  • 91
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews, A.; Kramer, B.; Marsh, M. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol., 2003, 162, (3), 443-455.
    • (2003) J. Cell Biol. , vol.162 , Issue.3 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 92
    • 43249130505 scopus 로고    scopus 로고
    • CD63 is not required for production of infectious human immunodeficiency virus type 1 in human macrophages
    • Ruiz-Mateos, E.; Pelchen-Matthews, A.; Deneka, M.; Marsh, M. CD63 is not required for production of infectious human immunodeficiency virus type 1 in human macrophages. J. Virol., 2008, 82(10), 4751-4761.
    • (2008) J. Virol. , vol.82 , Issue.10 , pp. 4751-4761
    • Ruiz-Mateos, E.1    Pelchen-Matthews, A.2    Deneka, M.3    Marsh, M.4
  • 93
    • 31444453892 scopus 로고    scopus 로고
    • Immature dendritic cell-derived exosomes can mediate HIV-1 trans infection
    • Wiley, R. D.; Gummuluru, S. Immature dendritic cell-derived exosomes can mediate HIV-1 trans infection. Proc. Natl. Acad. Sci. USA, 2006, 103(3), 738-743.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.3 , pp. 738-743
    • Wiley, R.D.1    Gummuluru, S.2
  • 94
    • 34547105037 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains
    • Jolly, C.; Sattentau, Q. J. Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J. Virol., 2007, 81, (15), 7873-84.
    • (2007) J. Virol. , vol.81 , Issue.15 , pp. 7873-7884
    • Jolly, C.1    Sattentau, Q.J.2
  • 95
    • 33644927263 scopus 로고    scopus 로고
    • Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane
    • Booth, A. M.; Fang, Y.; Fallon, J. K.; Yang, J. M.; Hildreth, J. E.; Gould, S. J. Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane. J. Cell Biol., 2006, 172, (6), 923-35.
    • (2006) J. Cell Biol. , vol.172 , Issue.6 , pp. 923-935
    • Booth, A.M.1    Fang, Y.2    Fallon, J.K.3    Yang, J.M.4    Hildreth, J.E.5    Gould, S.J.6
  • 97
    • 34247529467 scopus 로고    scopus 로고
    • In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53
    • Deneka, M.; Pelchen-Matthews, A.; Byland, R.; Ruiz-Mateos, E.; Marsh, M. In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53. J. Cell Biol., 2007, 177, (2), 329-341.
    • (2007) J. Cell Biol. , vol.177 , Issue.2 , pp. 329-341
    • Deneka, M.1    Pelchen-Matthews, A.2    Byland, R.3    Ruiz-Mateos, E.4    Marsh, M.5
  • 98
    • 0347993084 scopus 로고    scopus 로고
    • Evidence that HIV budding in primary macrophages occurs through the exosome release pathway
    • Nguyen, D. G.; Booth, A.; Gould, S. J.; Hildreth, J. E. Evidence that HIV budding in primary macrophages occurs through the exosome release pathway. J. Biol. Chem., 2003, 278(52), 52347-52354.
    • (2003) J. Biol. Chem. , vol.278 , Issue.52 , pp. 52347-52354
    • Nguyen, D.G.1    Booth, A.2    Gould, S.J.3    Hildreth, J.E.4
  • 100
    • 38149040172 scopus 로고    scopus 로고
    • HIV-1 replication in dendritic cells occurs through a tetraspanin-containing compartment enriched in AP-3
    • Garcia, E.; Nikolic, D. S.; Piguet, V. HIV-1 replication in dendritic cells occurs through a tetraspanin-containing compartment enriched in AP-3. Traffic, 2008, 9(2), 200-214.
    • (2008) Traffic , vol.9 , Issue.2 , pp. 200-214
    • Garcia, E.1    Nikolic, D.S.2    Piguet, V.3
  • 102
    • 33747394451 scopus 로고    scopus 로고
    • Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1
    • Nydegger, S.; Khurana, S.; Krementsov, D. N.; Foti, M.; Thali, M. Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. J. Cell Biol., 2006, 173(5), 795-807.
    • (2006) J. Cell Biol. , vol.173 , Issue.5 , pp. 795-807
    • Nydegger, S.1    Khurana, S.2    Krementsov, D.N.3    Foti, M.4    Thali, M.5
  • 103
    • 63449114891 scopus 로고    scopus 로고
    • Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells
    • Harrist, A. V.; Ryzhova, E. V.; Harvey, T.; Gonzalez-Scarano, F. Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells. PLoS ONE, 2009, 4(3), e5020.
    • (2009) PLoS ONE , vol.4 , Issue.3
    • Harrist, A.V.1    Ryzhova, E.V.2    Harvey, T.3    Gonzalez-Scarano, F.4
  • 104
    • 78649471247 scopus 로고    scopus 로고
    • HIV-1 assembly differentially alters dynamics and partitioning of tetraspanins and raft components
    • Krementsov, D. N.; Rassam, P.; Margeat, E.; Roy, N. H.; Schneider-Schaulies, J.; Milhiet, P. E.; Thali, M. HIV-1 assembly differentially alters dynamics and partitioning of tetraspanins and raft components. Traffic, 2010, 11(11), 1401-1414.
    • (2010) Traffic , vol.11 , Issue.11 , pp. 1401-1414
    • Krementsov, D.N.1    Rassam, P.2    Margeat, E.3    Roy, N.H.4    Schneider-Schaulies, J.5    Milhiet, P.E.6    Thali, M.7
  • 105
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body
    • Ono, A.; Freed, E. O. Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body. J. Virol., 2004, 78(3), 1552-1563.
    • (2004) J. Virol. , vol.78 , Issue.3 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 106
    • 2442662800 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies
    • Lindwasser, O. W.; Resh, M. D. Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies. J. Virol., 2004, 78(11), 6013-6023.
    • (2004) J. Virol. , vol.78 , Issue.11 , pp. 6013-6023
    • Lindwasser, O.W.1    Resh, M.D.2
  • 107
    • 42449108655 scopus 로고    scopus 로고
    • Dominant negative inhibition of human immunodeficiency virus particle production by the nonmyristoylated form of gag
    • Kawada, S.; Goto, T.; Haraguchi, H.; Ono, A.; Morikawa, Y. Dominant negative inhibition of human immunodeficiency virus particle production by the nonmyristoylated form of gag. J. Virol., 2008, 82(9), 4384-4399.
    • (2008) J. Virol. , vol.82 , Issue.9 , pp. 4384-4399
    • Kawada, S.1    Goto, T.2    Haraguchi, H.3    Ono, A.4    Morikawa, Y.5
  • 108
    • 79952850905 scopus 로고    scopus 로고
    • Identification of an inhibitory budding signal that blocks the release of HIV particles and exosome/microvesicle proteins
    • Gan, X.; Gould, S. J. Identification of an inhibitory budding signal that blocks the release of HIV particles and exosome/microvesicle proteins. Mol. Biol. Cell, 2011, 22(6),817-830
    • (2011) Mol. Biol. Cell , vol.22 , Issue.6 , pp. 817-830
    • Gan, X.1    Gould, S.J.2
  • 109
    • 67650886007 scopus 로고    scopus 로고
    • Formation of syncytia is repressed by tetraspanins in human immunodeficiency virus type 1-producing cells
    • Weng, J.; Krementsov, D. N.; Khurana, S.; Roy, N. H.; Thali, M. Formation of syncytia is repressed by tetraspanins in human immunodeficiency virus type 1-producing cells. J. Virol., 2009, 83(15), 7467-7474.
    • (2009) J. Virol. , vol.83 , Issue.15 , pp. 7467-7474
    • Weng, J.1    Krementsov, D.N.2    Khurana, S.3    Roy, N.H.4    Thali, M.5
  • 112
    • 0037425564 scopus 로고    scopus 로고
    • Mortality associated with influenza and respiratory syncytial virus in the United States
    • Thompson, W. W.; Shay, D. K.; Weintraub, E.; Brammer, L.; Cox, N.; Anderson, L. J.; Fukuda, K. Mortality associated with influenza and respiratory syncytial virus in the United States. Jama, 2003, 289(2), 179-186.
    • (2003) Jama , vol.289 , Issue.2 , pp. 179-186
    • Thompson, W.W.1    Shay, D.K.2    Weintraub, E.3    Brammer, L.4    Cox, N.5    Anderson, L.J.6    Fukuda, K.7
  • 113
    • 51449086295 scopus 로고    scopus 로고
    • The biology of influenza viruses
    • Bouvier, N. M.; Palese, P. The biology of influenza viruses. Vaccine, 2008, 26(Suppl 4), D49-53.
    • (2008) Vaccine , vol.26 , Issue.SUPPL 4 , pp. 49-53
    • Bouvier, N.M.1    Palese, P.2
  • 114
    • 0000443647 scopus 로고
    • Filamentous forms associated with newly isolated influenza virus
    • Chu, C. M.; Dawson, I. M.; Elford, W. J. Filamentous forms associated with newly isolated influenza virus. Lancet, 1949, 1, (6554), 602.
    • (1949) Lancet , vol.1 , Issue.6554 , pp. 602
    • Chu, C.M.1    Dawson, I.M.2    Elford, W.J.3
  • 115
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust, M. J.; Lakadamyali, M.; Zhang, F.; Zhuang, X. Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat. Struct. Mol. Biol., 2004, 11(6), 567-573.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , Issue.6 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 116
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski, S. B.; Whittaker, G. R. Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J. Virol., 2002, 76(20), 10455-10464.
    • (2002) J. Virol. , vol.76 , Issue.20 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 117
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman, J. S.; Lamb, R. A. Influenza virus assembly and budding. Virology, 2011, 411(2), 229-236.
    • (2011) Virology , vol.411 , Issue.2 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 118
    • 26944491901 scopus 로고    scopus 로고
    • Influenza virus assembly and budding at the viral budozone
    • Schmitt, A. P.; Lamb, R. A. Influenza virus assembly and budding at the viral budozone. Adv. Virus Res., 2005, 64, 383-416.
    • (2005) Adv. Virus Res. , vol.64 , pp. 383-416
    • Schmitt, A.P.1    Lamb, R.A.2
  • 119
    • 27144533145 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly
    • Chen, B. J.; Takeda, M.; Lamb, R. A. Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly. J. Virol., 2005, 79(21), 13673-13684.
    • (2005) J. Virol. , vol.79 , Issue.21 , pp. 13673-13684
    • Chen, B.J.1    Takeda, M.2    Lamb, R.A.3
  • 120
    • 36049020378 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 and influenza virus exit via different membrane microdomains
    • Khurana, S.; Krementsov, D. N.; de Parseval, A.; Elder, J. H.; Foti, M.; Thali, M. Human immunodeficiency virus type 1 and influenza virus exit via different membrane microdomains. J. Virol., 2007, 81(22), 12630-12640.
    • (2007) J. Virol. , vol.81 , Issue.22 , pp. 12630-12640
    • Khurana, S.1    Krementsov, D.N.2    de Parseval, A.3    Elder, J.H.4    Foti, M.5    Thali, M.6
  • 124
    • 33644862821 scopus 로고    scopus 로고
    • Intracellular versus cell surface assembly of retroviral pseudotypes is determined by the cellular localization of the viral glycoprotein, its capacity to interact with Gag, and the expression of the Nef protein
    • Sandrin, V.; Cosset, F. L. Intracellular versus cell surface assembly of retroviral pseudotypes is determined by the cellular localization of the viral glycoprotein, its capacity to interact with Gag, and the expression of the Nef protein. J. Biol. Chem., 2006, 281(1), 528-542.
    • (2006) J. Biol. Chem. , vol.281 , Issue.1 , pp. 528-542
    • Sandrin, V.1    Cosset, F.L.2
  • 125
    • 79953177046 scopus 로고    scopus 로고
    • Tetraspanin functions during HIV-1 and influenza virus replication
    • Thali, M. Tetraspanin functions during HIV-1 and influenza virus replication. Biochem. Soc. Trans., 2011, 39(2), 529-531.
    • (2011) Biochem. Soc. Trans. , vol.39 , Issue.2 , pp. 529-531
    • Thali, M.1
  • 126
    • 0033526648 scopus 로고    scopus 로고
    • Human T-lymphotropic virus type I infection
    • Manns, A.; Hisada, M.; La Grenade, L. Human T-lymphotropic virus type I infection. Lancet, 1999, 353(9168), 1951-1958.
    • (1999) Lancet , vol.353 , Issue.9168 , pp. 1951-1958
    • Manns, A.1    Hisada, M.2    La Grenade, L.3
  • 127
    • 0022111287 scopus 로고
    • Viral aetiology of adult T-cell leukaemia
    • Yamamoto, N.; Hinuma, Y. Viral aetiology of adult T-cell leukaemia. J. Gen. Virol., 1985, 66(Pt 8), 1641-1660.
    • (1985) J. Gen. Virol. , vol.66 , Issue.PART 8 , pp. 1641-1660
    • Yamamoto, N.1    Hinuma, Y.2
  • 128
    • 0026537225 scopus 로고
    • Identification of membrane antigen C33 recognized by monoclonal antibodies inhibitory to human T-cell leukemia virus type 1 (HTLV-1)-induced syncytium formation: Altered glycosylation of C33 antigen in HTLV-1-positive T cells
    • Fukudome, K.; Furuse, M.; Imai, T.; Nishimura, M.; Takagi, S.; Hinuma, Y.; Yoshie, O. Identification of membrane antigen C33 recognized by monoclonal antibodies inhibitory to human T-cell leukemia virus type 1 (HTLV-1)-induced syncytium formation: altered glycosylation of C33 antigen in HTLV-1-positive T cells. J. Virol., 1992, 66(3), 1394-1401.
    • (1992) J. Virol. , vol.66 , Issue.3 , pp. 1394-1401
    • Fukudome, K.1    Furuse, M.2    Imai, T.3    Nishimura, M.4    Takagi, S.5    Hinuma, Y.6    Yoshie, O.7
  • 129
    • 0026703106 scopus 로고
    • C33 antigen recognized by monoclonal antibodies inhibitory to human T cell leukemia virus type 1-induced syncytium formation is a member of a new family of transmembrane proteins including CD9, CD37, CD53, and CD63
    • Imai, T.; Fukudome, K.; Takagi, S.; Nagira, M.; Furuse, M.; Fukuhara, N.; Nishimura, M.; Hinuma, Y.; Yoshie, O. C33 antigen recognized by monoclonal antibodies inhibitory to human T cell leukemia virus type 1-induced syncytium formation is a member of a new family of transmembrane proteins including CD9, CD37, CD53, and CD63. J. Immunol., 1992, 149(9), 2879-2886.
    • (1992) J. Immunol. , vol.149 , Issue.9 , pp. 2879-2886
    • Imai, T.1    Fukudome, K.2    Takagi, S.3    Nagira, M.4    Furuse, M.5    Fukuhara, N.6    Nishimura, M.7    Hinuma, Y.8    Yoshie, O.9
  • 130
    • 0034715523 scopus 로고    scopus 로고
    • Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission
    • Pique, C.; Lagaudriere-Gesbert, C.; Delamarre, L.; Rosenberg, A. R.; Conjeaud, H.; Dokhelar, M. C. Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission. Virology, 2000, 276(2), 455-465.
    • (2000) Virology , vol.276 , Issue.2 , pp. 455-465
    • Pique, C.1    Lagaudriere-Gesbert, C.2    Delamarre, L.3    Rosenberg, A.R.4    Conjeaud, H.5    Dokhelar, M.C.6
  • 131
    • 77649242985 scopus 로고    scopus 로고
    • Quantitative comparison of HTLV-1 and HIV-1 cell-to-cell infection with new replication dependent vectors
    • Mazurov, D.; Ilinskaya, A.; Heidecker, G.; Lloyd, P.; Derse, D. Quantitative comparison of HTLV-1 and HIV-1 cell-to-cell infection with new replication dependent vectors. PLoS Pathog., 2010, 6(2), e1000788.
    • (2010) PLoS Pathog. , vol.6 , Issue.2
    • Mazurov, D.1    Ilinskaya, A.2    Heidecker, G.3    Lloyd, P.4    Derse, D.5
  • 132
    • 32844458333 scopus 로고    scopus 로고
    • HTLV-1 Gag protein associates with CD82 tetraspanin microdomains at the plasma membrane
    • Mazurov, D.; Heidecker, G.; Derse, D. HTLV-1 Gag protein associates with CD82 tetraspanin microdomains at the plasma membrane. Virology, 2006, 346(1), 194-204.
    • (2006) Virology , vol.346 , Issue.1 , pp. 194-204
    • Mazurov, D.1    Heidecker, G.2    Derse, D.3
  • 133
    • 33646675570 scopus 로고    scopus 로고
    • Molecular biology of human papillomavirus infection and cervical cancer
    • Doorbar, J. Molecular biology of human papillomavirus infection and cervical cancer. Clin. Sci. (Lond), 2006, 110(5), 525-541.
    • (2006) Clin. Sci. (Lond) , vol.110 , Issue.5 , pp. 525-541
    • Doorbar, J.1
  • 134
    • 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(3), 1565-1570.
    • (2001) J. Virol. , vol.75 , Issue.3 , pp. 1565-1570
    • Giroglou, T.1    Florin, L.2    Schafer, F.3    Streeck, R.E.4    Sapp, M.5
  • 135
    • 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), 1-11.
    • (2003) Virology , vol.307 , Issue.1 , pp. 1-11
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 136
    • 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(10), e3313.
    • (2008) PLoS ONE , vol.3 , Issue.10
    • Spoden, G.1    Freitag, K.2    Husmann, M.3    Boller, K.4    Sapp, M.5    Lambert, C.6    Florin, L.7
  • 137
    • 78649321214 scopus 로고    scopus 로고
    • Control and elimination of porcine reproductive and respiratory syndrome virus
    • Corzo, C. A.; Mondaca, E.; Wayne, S.; Torremorell, M.; Dee, S.; Davies, P.; Morrison, R. B. Control and elimination of porcine reproductive and respiratory syndrome virus. Virus Res., 2010, 154, (1-2), 185-192.
    • (2010) Virus Res. , vol.154 , Issue.1-2 , pp. 185-192
    • Corzo, C.A.1    Mondaca, E.2    Wayne, S.3    Torremorell, M.4    Dee, S.5    Davies, P.6    Morrison, R.B.7
  • 138
    • 58149378592 scopus 로고    scopus 로고
    • Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virus
    • Van Gorp, H.; Van Breedam, W.; Delputte, P. L.; Nauwynck, H. J. Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virus. J. Gen. Virol., 2008, 89, (Pt 12), 2943-2953.
    • (2008) J. Gen. Virol. , vol.89 , Issue.PART 12 , pp. 2943-2953
    • van Gorp, H.1    Van Breedam, W.2    Delputte, P.L.3    Nauwynck, H.J.4
  • 139
    • 34447108939 scopus 로고    scopus 로고
    • Role of CD151, A tetraspanin, in porcine reproductive and respiratory syndrome virus infection
    • Shanmukhappa, K.; Kim, J. K.; Kapil, S. Role of CD151, A tetraspanin, in porcine reproductive and respiratory syndrome virus infection. Virol J., 2007, 4, 62.
    • (2007) Virol J. , vol.4 , pp. 62
    • Shanmukhappa, K.1    Kim, J.K.2    Kapil, S.3
  • 140
    • 0028875939 scopus 로고
    • A conserved motif at the 3' end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication
    • Yu, W.; Leibowitz, J. L. A conserved motif at the 3' end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication. Virology, 1995, 214(1), 128-138.
    • (1995) Virology , vol.214 , Issue.1 , pp. 128-138
    • Yu, W.1    Leibowitz, J.L.2
  • 141
  • 142
    • 0031051160 scopus 로고    scopus 로고
    • Inhibition of feline immunodeficiency virus infection by CD9 antibody operates after virus entry and is independent of virus tropism
    • Willett, B.; Hosie, M.; Shaw, A.; Neil, J. Inhibition of feline immunodeficiency virus infection by CD9 antibody operates after virus entry and is independent of virus tropism. J. Gen. Virol., 1997, 78(Pt 3), 611-618.;
    • (1997) J. Gen. Virol. , vol.78 , Issue.PART 3 , pp. 611-618
    • Willett, B.1    Hosie, M.2    Shaw, A.3    Neil, J.4
  • 143
    • 0028272314 scopus 로고
    • Identification of a putative cellular receptor for feline immunodeficiency virus as the feline homologue of CD9
    • Willett, B. J.; Hosie, M. J.; Jarrett, O.; Neil, J. C. Identification of a putative cellular receptor for feline immunodeficiency virus as the feline homologue of CD9. Immunology, 1994, 81, (2), 228-33
    • (1994) Immunology , vol.81 , Issue.2 , pp. 228-233
    • Willett, B.J.1    Hosie, M.J.2    Jarrett, O.3    Neil, J.C.4
  • 144
    • 0029053833 scopus 로고
    • cDNA cloning and eukaryotic expression of feline CD9
    • Willett, B. J.; Neil, J. C. cDNA cloning and eukaryotic expression of feline CD9. Mol. Immunol., 1995, 32(6), 417-423.
    • (1995) Mol. Immunol. , vol.32 , Issue.6 , pp. 417-423
    • Willett, B.J.1    Neil, J.C.2
  • 145
    • 0030835319 scopus 로고    scopus 로고
    • Blocking of feline immunodeficiency virus infection by a monoclonal antibody to CD9 is via inhibition of virus release rather than interference with receptor binding
    • de Parseval, A.; Lerner, D. L.; Borrow, P.; Willett, B. J.; Elder, J. H. Blocking of feline immunodeficiency virus infection by a monoclonal antibody to CD9 is via inhibition of virus release rather than interference with receptor binding. J. Virol., 1997, 71(8), 5742-5749.
    • (1997) J. Virol. , vol.71 , Issue.8 , pp. 5742-5749
    • de Parseval, A.1    Lerner, D.L.2    Borrow, P.3    Willett, B.J.4    Elder, J.H.5
  • 147
  • 148
    • 0033854377 scopus 로고    scopus 로고
    • Antibodies to CD9, a tetraspan transmembrane protein, inhibit canine distemper virus-induced cell-cell fusion but not virus-cell fusion
    • Schmid, E.; Zurbriggen, A.; Gassen, U.; Rima, B.; ter Meulen, V.; Schneider-Schaulies, J. Antibodies to CD9, a tetraspan transmembrane protein, inhibit canine distemper virus-induced cell-cell fusion but not virus-cell fusion. J. Virol., 2000, 74(16), 7554-7561.
    • (2000) J. Virol. , vol.74 , Issue.16 , pp. 7554-7561
    • Schmid, E.1    Zurbriggen, A.2    Gassen, U.3    Rima, B.4    ter Meulen, V.5    Schneider-Schaulies, J.6
  • 149
    • 33744800779 scopus 로고    scopus 로고
    • CD9-dependent regulation of Canine distemper virus-induced cell-cell fusion segregates with the extracellular domain of the haemagglutinin
    • Singethan, K.; Topfstedt, E.; Schubert, S.; Duprex, W. P.; Rima, B. K.; Schneider-Schaulies, J. CD9-dependent regulation of Canine distemper virus-induced cell-cell fusion segregates with the extracellular domain of the haemagglutinin. J. Gen. Virol., 2006, 87(Pt 6), 1635-1642.
    • (2006) J. Gen. Virol. , vol.87 , Issue.PART 6 , pp. 1635-1642
    • Singethan, K.1    Topfstedt, E.2    Schubert, S.3    Duprex, W.P.4    Rima, B.K.5    Schneider-Schaulies, J.6
  • 151
    • 3142545772 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport
    • Douglas, M. W.; Diefenbach, R. J.; Homa, F. L.; Miranda-Saksena, M.; Rixon, F. J.; Vittone, V.; Byth, K.; Cunningham, A. L. Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport. J. Biol. Chem., 2004, 279(27), 28522-28530.
    • (2004) J. Biol. Chem. , vol.279 , Issue.27 , pp. 28522-28530
    • Douglas, M.W.1    Diefenbach, R.J.2    Homa, F.L.3    Miranda-Saksena, M.4    Rixon, F.J.5    Vittone, V.6    Byth, K.7    Cunningham, A.L.8
  • 152
    • 77954508585 scopus 로고    scopus 로고
    • Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein
    • Wang, L.; Liu, L.; Che, Y.; Jiang, L.; Dong, C.; Zhang, Y.; Li, Q. Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein. Virol. J., 2010, 7, 156.
    • (2010) Virol. J. , vol.7 , pp. 156
    • Wang, L.1    Liu, L.2    Che, Y.3    Jiang, L.4    Dong, C.5    Zhang, Y.6    Li, Q.7
  • 153
    • 33847793666 scopus 로고    scopus 로고
    • CD9 promotes adeno-associated virus type 2 infection of mammary carcinoma cells with low cell surface expression of heparan sulphate proteoglycans
    • Kurzeder, C.; Koppold, B.; Sauer, G.; Pabst, S.; Kreienberg, R.; Deissler, H. CD9 promotes adeno-associated virus type 2 infection of mammary carcinoma cells with low cell surface expression of heparan sulphate proteoglycans. Int. J. Mol. Med., 2007, 19(2), 325-333.
    • (2007) Int. J. Mol. Med. , vol.19 , Issue.2 , pp. 325-333
    • Kurzeder, C.1    Koppold, B.2    Sauer, G.3    Pabst, S.4    Kreienberg, R.5    Deissler, H.6
  • 155
    • 38349107361 scopus 로고    scopus 로고
    • Identification of host proteins associated with retroviral vector particles by proteomic analysis of highly purified vector preparations
    • Segura, M. M.; Garnier, A.; Di Falco, M. R.; Whissell, G.; Meneses-Acosta, A.; Arcand, N.; Kamen, A. Identification of host proteins associated with retroviral vector particles by proteomic analysis of highly purified vector preparations. J. Virol., 2008, 82(3), 1107-1117.
    • (2008) J. Virol. , vol.82 , Issue.3 , pp. 1107-1117
    • Segura, M.M.1    Garnier, A.2    Di Falco, M.R.3    Whissell, G.4    Meneses-Acosta, A.5    Arcand, N.6    Kamen, A.7
  • 156
    • 0032560578 scopus 로고    scopus 로고
    • Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of host complement control proteins into its envelope
    • Vanderplasschen, A.; Mathew, E.; Hollinshead, M.; Sim, R. B.; Smith, G. L. Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of host complement control proteins into its envelope. Proc. Natl. Acad. Sci. USA, 1998, 95(13), 7544-7549
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.13 , pp. 7544-7549
    • Vanderplasschen, A.1    Mathew, E.2    Hollinshead, M.3    Sim, R.B.4    Smith, G.L.5
  • 157
    • 0036788088 scopus 로고    scopus 로고
    • An investigation of incorporation of cellular antigens into vaccinia virus particles
    • Krauss, O.; Hollinshead, R.; Hollinshead, M.; Smith, G. L. An investigation of incorporation of cellular antigens into vaccinia virus particles. J. Gen. Virol., 2002, 83(Pt 10), 2347-2359.
    • (2002) J. Gen. Virol. , vol.83 , Issue.PART 10 , pp. 2347-2359
    • Krauss, O.1    Hollinshead, R.2    Hollinshead, M.3    Smith, G.L.4
  • 158
    • 28844491720 scopus 로고    scopus 로고
    • Evaluation of specificity and effects of monoclonal antibodies submitted to the Eighth Human Leucocyte Differentiation Antigen Workshop on rotaviruscell attachment and entry
    • Halasz, P.; Fleming, F. E.; Coulson, B. S. Evaluation of specificity and effects of monoclonal antibodies submitted to the Eighth Human Leucocyte Differentiation Antigen Workshop on rotaviruscell attachment and entry. Cell Immunol., 2005, 236(1-2), 179-187.
    • (2005) Cell Immunol. , vol.236 , Issue.1-2 , pp. 179-187
    • Halasz, P.1    Fleming, F.E.2    Coulson, B.S.3
  • 159
    • 0030879648 scopus 로고    scopus 로고
    • Bacterial virulence in urinary tract infection
    • Svanborg, C.; Godaly, G., Bacterial virulence in urinary tract infection. Infect. Dis. Clin. N. Am., 1997, 11(3), 513-529.
    • (1997) Infect. Dis. Clin. N. Am. , vol.11 , Issue.3 , pp. 513-529
    • Svanborg, C.1    Godaly, G.2
  • 160
    • 0029796909 scopus 로고    scopus 로고
    • In vitro, binding of type 1-fimbriated Escherichia coli to uroplakins Ia and Ib: Relation to urinary tract infections
    • Wu, X. R.; Sun, T. T.; Medina, J. J. In vitro, binding of type 1-fimbriated Escherichia coli to uroplakins Ia and Ib: relation to urinary tract infections. Proc. Natl. Acad. Sci. USA, 1996, 93(18), 9630-9635.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.18 , pp. 9630-9635
    • Wu, X.R.1    Sun, T.T.2    Medina, J.J.3
  • 161
    • 0034747254 scopus 로고    scopus 로고
    • Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: Evidence from in vitro, FimH binding
    • Zhou, G.; Mo, W. J.; Sebbel, P.; Min, G.; Neubert, T. A.; Glockshuber, R.; Wu, X. R.; Sun, T. T.; Kong, X. P. Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: evidence from in vitro, FimH binding. J. Cell Sci., 2001, 114(Pt 22), 4095-4103.
    • (2001) J. Cell Sci. , vol.114 , Issue.PART 22 , pp. 4095-4103
    • Zhou, G.1    Mo, W.J.2    Sebbel, P.3    Min, G.4    Neubert, T.A.5    Glockshuber, R.6    Wu, X.R.7    Sun, T.T.8    Kong, X.P.9
  • 162
    • 33746191724 scopus 로고    scopus 로고
    • Molecular epidemiologic identification of Escherichia coli genes that are potentially involved in movement of the organism from the intestinal tract to the vagina and bladder
    • Xie, J.; Foxman, B.; Zhang, L.; Marrs, C. F. Molecular epidemiologic identification of Escherichia coli genes that are potentially involved in movement of the organism from the intestinal tract to the vagina and bladder. J. Clin. Microbiol., 2006, 44(7), 2434-2441.
    • (2006) J. Clin. Microbiol. , vol.44 , Issue.7 , pp. 2434-2441
    • Xie, J.1    Foxman, B.2    Zhang, L.3    Marrs, C.F.4
  • 163
    • 0032553579 scopus 로고    scopus 로고
    • Induction and evasion of host defenses by type 1-piliated uropathogenic Escherichia coli
    • Mulvey, M. A.; Lopez-Boado, Y. S.; Wilson, C. L.; Roth, R.; Parks, W. C.; Heuser, J.; Hultgren, S. J. Induction and evasion of host defenses by type 1-piliated uropathogenic Escherichia coli. Science, 1998, 282, (5393), 1494-1497.
    • (1998) Science , vol.282 , Issue.5393 , pp. 1494-1497
    • Mulvey, M.A.1    Lopez-Boado, Y.S.2    Wilson, C.L.3    Roth, R.4    Parks, W.C.5    Heuser, J.6    Hultgren, S.J.7
  • 164
    • 0034978222 scopus 로고    scopus 로고
    • Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection
    • Mulvey, M. A.; Schilling, J. D.; Hultgren, S. J. Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection. Infect. Immun., 2001, 69(7), 4572-4579.
    • (2001) Infect. Immun. , vol.69 , Issue.7 , pp. 4572-4579
    • Mulvey, M.A.1    Schilling, J.D.2    Hultgren, S.J.3
  • 165
    • 34249670657 scopus 로고    scopus 로고
    • Cyclic AMP-regulated exocytosis of Escherichia coli from infected bladder epithelial cells
    • Bishop, B. L.; Duncan, M. J.; Song, J.; Li, G.; Zaas, D.; Abraham, S. N. Cyclic AMP-regulated exocytosis of Escherichia coli from infected bladder epithelial cells. Nat. Med., 2007, 13(5), 625-630.
    • (2007) Nat. Med. , vol.13 , Issue.5 , pp. 625-630
    • Bishop, B.L.1    Duncan, M.J.2    Song, J.3    Li, G.4    Zaas, D.5    Abraham, S.N.6
  • 166
    • 53449094756 scopus 로고    scopus 로고
    • Listeria monocytogenes, a unique model in infection biology: An overview
    • Cossart, P.; Toledo-Arana, A. Listeria monocytogenes, a unique model in infection biology: an overview. Microbes. Infect., 2008, 10(9), 1041-1050.
    • (2008) Microbes. Infect. , vol.10 , Issue.9 , pp. 1041-1050
    • Cossart, P.1    Toledo-Arana, A.2
  • 167
    • 34548516176 scopus 로고    scopus 로고
    • Molecular mechanisms exploited by Listeria monocytogenes during host cell invasion
    • Seveau, S.; Pizarro-Cerda, J.; Cossart, P. Molecular mechanisms exploited by Listeria monocytogenes during host cell invasion. Microbes. Infect., 2007, 9(10), 1167-1175.
    • (2007) Microbes. Infect. , vol.9 , Issue.10 , pp. 1167-1175
    • Seveau, S.1    Pizarro-Cerda, J.2    Cossart, P.3
  • 168
    • 34548444206 scopus 로고    scopus 로고
    • Type II phosphatidylinositol 4-kinases promote Listeria monocytogenes entry into target cells
    • Pizarro-Cerda, J.; Payrastre, B.; Wang, Y. J.; Veiga, E.; Yin, H. L.; Cossart, P. Type II phosphatidylinositol 4-kinases promote Listeria monocytogenes entry into target cells. Cell Microbiol., 2007, 9, (10), 2381-2390.
    • (2007) Cell Microbiol. , vol.9 , Issue.10 , pp. 2381-2390
    • Pizarro-Cerda, J.1    Payrastre, B.2    Wang, Y.J.3    Veiga, E.4    Yin, H.L.5    Cossart, P.6
  • 169
    • 0034331438 scopus 로고    scopus 로고
    • Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase
    • Yauch, R. L.; Hemler, M. E. Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase. Biochem. J., 2000, 351(Pt 3), 629-637.
    • (2000) Biochem. J. , vol.351 , Issue.PART 3 , pp. 629-637
    • Yauch, R.L.1    Hemler, M.E.2
  • 171
    • 0024194130 scopus 로고
    • The intracellular life of Chlamydia
    • Schachter, J. The intracellular life of Chlamydia. Curr. Top. Microbiol. Immunol., 1988, 138, 109-139.
    • (1988) Curr. Top. Microbiol. Immunol. , vol.138 , pp. 109-139
    • Schachter, J.1
  • 172
    • 32244447356 scopus 로고    scopus 로고
    • Trafficking from CD63-positive late endocytic multivesicular bodies is essential for intracellular development of Chlamydia trachomatis
    • Beatty, W. L. Trafficking from CD63-positive late endocytic multivesicular bodies is essential for intracellular development of Chlamydia trachomatis. J. Cell Sci., 2006, 119(Pt 2), 350-359.
    • (2006) J. Cell Sci. , vol.119 , Issue.PART 2 , pp. 350-359
    • Beatty, W.L.1
  • 173
    • 46449083293 scopus 로고    scopus 로고
    • Late endocytic multivesicular bodies intersect the chlamydial inclusion in the absence of CD63
    • Beatty, W. L. Late endocytic multivesicular bodies intersect the chlamydial inclusion in the absence of CD63. Infect. Immun., 2008, 76(7), 2872-2881.
    • (2008) Infect. Immun. , vol.76 , Issue.7 , pp. 2872-2881
    • Beatty, W.L.1
  • 174
    • 11244333284 scopus 로고    scopus 로고
    • Management of meningitis
    • Tunbridge, A.; Read, R. C. Management of meningitis. Clin. Med., 2004, 4(6), 499-505.
    • (2004) Clin. Med. , vol.4 , Issue.6 , pp. 499-505
    • Tunbridge, A.1    Read, R.C.2
  • 175
    • 76849105930 scopus 로고    scopus 로고
    • Cellular and molecular biology of Neisseria meningitidis colonization and invasive disease
    • Hill, D. J.; Griffiths, N. J.; Borodina, E.; Virji, M. Cellular and molecular biology of Neisseria meningitidis colonization and invasive disease. Clin. Sci., (Lond), 2010, 118(9), 547-564.
    • (2010) Clin. Sci., (Lond) , vol.118 , Issue.9 , pp. 547-564
    • Hill, D.J.1    Griffiths, N.J.2    Borodina, E.3    Virji, M.4
  • 177
    • 0037327558 scopus 로고    scopus 로고
    • 'Small' talk: Opa proteins as mediators of Neisseria-host-cell communication
    • Hauck, C. R.; Meyer, T. F. 'Small' talk: Opa proteins as mediators of Neisseria-host-cell communication. Curr. Opin. Microbiol., 2003, 6(1), 43-49.
    • (2003) Curr. Opin. Microbiol. , vol.6 , Issue.1 , pp. 43-49
    • Hauck, C.R.1    Meyer, T.F.2
  • 178
    • 77952292205 scopus 로고    scopus 로고
    • Mechanisms of meningeal invasion by a bacterial extracellular pathogen, the example of Neisseria meningitidis
    • Join-Lambert, O.; Morand, P. C.; Carbonnelle, E.; Coureuil, M.; Bille, E.; Bourdoulous, S.; Nassif, X. Mechanisms of meningeal invasion by a bacterial extracellular pathogen, the example of Neisseria meningitidis. Prog. Neurobiol., 2010, 91(2), 130-139.
    • (2010) Prog. Neurobiol. , vol.91 , Issue.2 , pp. 130-139
    • Join-Lambert, O.1    Morand, P.C.2    Carbonnelle, E.3    Coureuil, M.4    Bille, E.5    Bourdoulous, S.6    Nassif, X.7
  • 179
    • 0030779080 scopus 로고    scopus 로고
    • Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
    • Kallstrom, H.; Liszewski, M. K.; Atkinson, J. P.; Jonsson, A. B. Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria. Mol. Microbiol., 1997, 25(4), 639-647.
    • (1997) Mol. Microbiol. , vol.25 , Issue.4 , pp. 639-647
    • Kallstrom, H.1    Liszewski, M.K.2    Atkinson, J.P.3    Jonsson, A.B.4
  • 180
    • 0034872590 scopus 로고    scopus 로고
    • Inverse relationship between pilusmediated gonococcal adherence and surface expression of the pilus receptor, CD46
    • Tobiason, D. M.; Seifert, H. S. Inverse relationship between pilusmediated gonococcal adherence and surface expression of the pilus receptor, CD46. Microbiology, 2001, 147(Pt 8), 2333-2340.
    • (2001) Microbiology , vol.147 , Issue.PART 8 , pp. 2333-2340
    • Tobiason, D.M.1    Seifert, H.S.2
  • 181
    • 0029844602 scopus 로고    scopus 로고
    • The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae
    • Virji, M.; Watt, S. M.; Barker, S.; Makepeace, K.; Doyonnas, R. The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae. Mol. Microbiol., 1996, 22, (5), 929-939.
    • (1996) Mol. Microbiol. , vol.22 , Issue.5 , pp. 929-939
    • Virji, M.1    Watt, S.M.2    Barker, S.3    Makepeace, K.4    Doyonnas, R.5
  • 182
    • 79959383500 scopus 로고    scopus 로고
    • Cooperative role for tetraspanins in adhesinmediated attachment of bacterial species to human epithelial cells
    • Green, L. R.; Monk, P. N.; Partridge, L. J.; Morris, P.; Gorringe, A. R.; Read, R. C. Cooperative role for tetraspanins in adhesinmediated attachment of bacterial species to human epithelial cells. Infect. Immun., 2011, 79(6),2241-2249.
    • (2011) Infect. Immun. , vol.79 , Issue.6 , pp. 2241-2249
    • Green, L.R.1    Monk, P.N.2    Partridge, L.J.3    Morris, P.4    Gorringe, A.R.5    Read, R.C.6
  • 183
    • 0034960729 scopus 로고    scopus 로고
    • Unusual intracellular trafficking of Salmonella typhimurium in human melanoma cells
    • Martinez-Lorenzo, M. J.; Meresse, S.; de Chastellier, C.; Gorvel, J. P. Unusual intracellular trafficking of Salmonella typhimurium in human melanoma cells. Cell Microbiol., 2001, 3(6), 407-416.
    • (2001) Cell Microbiol. , vol.3 , Issue.6 , pp. 407-416
    • Martinez-Lorenzo, M.J.1    Meresse, S.2    de Chastellier, C.3    Gorvel, J.P.4
  • 185
    • 3843126411 scopus 로고    scopus 로고
    • CD63 tetraspanin slows down cell migration and translocates to the endosomal-lysosomal-MIICs route after extracellular stimuli in human immature dendritic cells
    • Mantegazza, A. R.; Barrio, M. M.; Moutel, S.; Bover, L.; Weck, M.; Brossart, P.; Teillaud, J. L.; Mordoh, J. CD63 tetraspanin slows down cell migration and translocates to the endosomal-lysosomal-MIICs route after extracellular stimuli in human immature dendritic cells. Blood, 2004, 104, (4), 1183-1190.
    • (2004) Blood , vol.104 , Issue.4 , pp. 1183-1190
    • Mantegazza, A.R.1    Barrio, M.M.2    Moutel, S.3    Bover, L.4    Weck, M.5    Brossart, P.6    Teillaud, J.L.7    Mordoh, J.8
  • 186
    • 33750467949 scopus 로고    scopus 로고
    • Recruitment of CD63 to Cryptococcus neoformans phagosomes requires acidification
    • Artavanis-Tsakonas, K.; Love, J. C.; Ploegh, H. L.; Vyas, J. M. Recruitment of CD63 to Cryptococcus neoformans phagosomes requires acidification. Proc. Natl. Acad. Sci. USA, 2006, 103, (43), 15945-15950.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.43 , pp. 15945-15950
    • Artavanis-Tsakonas, K.1    Love, J.C.2    Ploegh, H.L.3    Vyas, J.M.4
  • 187
    • 0037022671 scopus 로고    scopus 로고
    • Replication of Cryptococcus neoformans in macrophages is accompanied by phagosomal permeabilization and accumulation of vesicles containing polysaccharide in the cytoplasm
    • Tucker, S. C.; Casadevall, A. Replication of Cryptococcus neoformans in macrophages is accompanied by phagosomal permeabilization and accumulation of vesicles containing polysaccharide in the cytoplasm. Proc. Natl. Acad. Sci. USA, 2002, 99(5), 3165-3170.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.5 , pp. 3165-3170
    • Tucker, S.C.1    Casadevall, A.2
  • 189
    • 0035144246 scopus 로고    scopus 로고
    • Association of distinct tetraspanins with MHC class II molecules at different subcellular locations in human immature dendritic cells
    • Engering, A.; Pieters, J. Association of distinct tetraspanins with MHC class II molecules at different subcellular locations in human immature dendritic cells. Int. Immunol., 2001, 13(2), 127-134.
    • (2001) Int. Immunol. , vol.13 , Issue.2 , pp. 127-134
    • Engering, A.1    Pieters, J.2
  • 191
    • 33750606979 scopus 로고    scopus 로고
    • Phagosome extrusion and host-cell survival after Cryptococcus neoformans phagocytosis by macrophages
    • Alvarez, M.; Casadevall, A. Phagosome extrusion and host-cell survival after Cryptococcus neoformans phagocytosis by macrophages. Curr. Biol., 2006, 16(21), 2161-2165.
    • (2006) Curr. Biol. , vol.16 , Issue.21 , pp. 2161-2165
    • Alvarez, M.1    Casadevall, A.2
  • 192
    • 33750604745 scopus 로고    scopus 로고
    • Expulsion of live pathogenic yeast by macrophages
    • Ma, H.; Croudace, J. E.; Lammas, D. A.; May, R. C. Expulsion of live pathogenic yeast by macrophages. Curr. Biol., 2006, 16(21), 2156-2160.
    • (2006) Curr. Biol. , vol.16 , Issue.21 , pp. 2156-2160
    • Ma, H.1    Croudace, J.E.2    Lammas, D.A.3    May, R.C.4
  • 193
    • 55049131325 scopus 로고    scopus 로고
    • Challenges facing drug development for malaria
    • Craft, J. C. Challenges facing drug development for malaria. Curr. Opin. Microbiol., 2008, 11(5), 428-433.
    • (2008) Curr. Opin. Microbiol. , vol.11 , Issue.5 , pp. 428-433
    • Craft, J.C.1
  • 194
    • 33750140518 scopus 로고    scopus 로고
    • The silent path to thousands of merozoites: The Plasmodium liver stage
    • Prudencio, M.; Rodriguez, A.; Mota, M. M. The silent path to thousands of merozoites: the Plasmodium liver stage. Nat. Rev. Microbiol., 2006, 4(11), 849-856.
    • (2006) Nat. Rev. Microbiol. , vol.4 , Issue.11 , pp. 849-856
    • Prudencio, M.1    Rodriguez, A.2    Mota, M.M.3
  • 198
    • 40349098213 scopus 로고    scopus 로고
    • Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domain
    • Yalaoui, S.; Zougbede, S.; Charrin, S.; Silvie, O.; Arduise, C.; Farhati, K.; Boucheix, C.; Mazier, D.; Rubinstein, E.; Froissard, P. Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domain. PLoS Pathog., 2008, 4(2), e1000010.
    • (2008) PLoS Pathog. , vol.4 , Issue.2
    • Yalaoui, S.1    Zougbede, S.2    Charrin, S.3    Silvie, O.4    Arduise, C.5    Farhati, K.6    Boucheix, C.7    Mazier, D.8    Rubinstein, E.9    Froissard, P.10
  • 201
    • 40649095689 scopus 로고    scopus 로고
    • Inflammatory profile of new bacterial strain exacerbations of chronic obstructive pulmonary disease
    • Sethi, S.; Wrona, C.; Eschberger, K.; Lobbins, P.; Cai, X.; Murphy, T. F. Inflammatory profile of new bacterial strain exacerbations of chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med., 2008, 177(5), 491-497.
    • (2008) Am. J. Respir. Crit. Care Med. , vol.177 , Issue.5 , pp. 491-497
    • Sethi, S.1    Wrona, C.2    Eschberger, K.3    Lobbins, P.4    Cai, X.5    Murphy, T.F.6
  • 203
    • 0032935608 scopus 로고    scopus 로고
    • The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages
    • Astarie-Dequeker, C.; N'Diaye, E. N.; Le Cabec, V.; Rittig, M. G.; Prandi, J.; Maridonneau-Parini, I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages. Infect. Immun., 1999, 67(2), 469-477.
    • (1999) Infect. Immun. , vol.67 , Issue.2 , pp. 469-477
    • Astarie-Dequeker, C.1    N'Diaye, E.N.2    Le Cabec, V.3    Rittig, M.G.4    Prandi, J.5    Maridonneau-Parini, I.6
  • 204
    • 80052050200 scopus 로고    scopus 로고
    • Importance of phagosomal functionality for growth restriction of mycobacterium tuberculosis in primary human macrophages
    • Welin, A.; Raffetseder, J.; Eklund, D.; Stendahl, O.; Lerm, M. Importance of phagosomal functionality for growth restriction of mycobacterium tuberculosis in primary human macrophages. J. Innate. Immun., 2011, 3(5),508-518
    • (2011) J. Innate. Immun. , vol.3 , Issue.5 , pp. 508-518
    • Welin, A.1    Raffetseder, J.2    Eklund, D.3    Stendahl, O.4    Lerm, M.5
  • 206
    • 33947141939 scopus 로고    scopus 로고
    • Lounging in a lysosome: The intracellular lifestyle of Coxiella burnetii
    • Voth, D. E.; Heinzen, R. A. Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii. Cell Microbiol., 2007, 9(4), 829-840.
    • (2007) Cell Microbiol. , vol.9 , Issue.4 , pp. 829-840
    • Voth, D.E.1    Heinzen, R.A.2
  • 207
    • 77955300012 scopus 로고    scopus 로고
    • Coxiella burnetii phase I and II variants replicate with similar kinetics in degradative phagolysosome-like compartments of human macrophages
    • Howe, D.; Shannon, J. G.; Winfree, S.; Dorward, D. W.; Heinzen, R. A. Coxiella burnetii phase I and II variants replicate with similar kinetics in degradative phagolysosome-like compartments of human macrophages. Infect. Immun., 2010, 78(8), 3465-3474.
    • (2010) Infect. Immun. , vol.78 , Issue.8 , pp. 3465-3474
    • Howe, D.1    Shannon, J.G.2    Winfree, S.3    Dorward, D.W.4    Heinzen, R.A.5
  • 208
    • 0037674823 scopus 로고    scopus 로고
    • Neutrophil granulocytes--Trojan horses for Leishmania major and other intracellular microbes?
    • Laskay, T.; van Zandbergen, G.; Solbach, W. Neutrophil granulocytes--Trojan horses for Leishmania major and other intracellular microbes? Trends Microbiol., 2003, 11(5), 210-214.
    • (2003) Trends Microbiol. , vol.11 , Issue.5 , pp. 210-214
    • Laskay, T.1    van Zandbergen, G.2    Solbach, W.3
  • 209
    • 78049412212 scopus 로고    scopus 로고
    • Selective fusion of azurophilic granules with Leishmania-containing phagosomes in human neutrophils
    • Mollinedo, F.; Janssen, H.; de la Iglesia-Vicente, J.; Villa-Pulgarin, J. A.; Calafat, J. Selective fusion of azurophilic granules with Leishmania-containing phagosomes in human neutrophils. J. Biol. Chem., 2010, 285(45), 34528-34536.
    • (2010) J. Biol. Chem. , vol.285 , Issue.45 , pp. 34528-34536
    • Mollinedo, F.1    Janssen, H.2    de la Iglesia-Vicente, J.3    Villa-Pulgarin, J.A.4    Calafat, J.5
  • 210
    • 70450216505 scopus 로고    scopus 로고
    • Strategies for targeting tetraspanin proteins: Potential therapeutic applications in microbial infections
    • Hassuna, N.; Monk, P. N.; Moseley, G. W.; Partridge, L. J. Strategies for targeting tetraspanin proteins: potential therapeutic applications in microbial infections. BioDrugs, 2009, 23(6), 341-359.
    • (2009) BioDrugs , vol.23 , Issue.6 , pp. 341-359
    • Hassuna, N.1    Monk, P.N.2    Moseley, G.W.3    Partridge, L.J.4
  • 217
    • 75149121861 scopus 로고    scopus 로고
    • The role of tetraspanins in the pathogenesis of infectious diseases
    • van Spriel, A. B.; Figdor, C. G. The role of tetraspanins in the pathogenesis of infectious diseases. Microbes. Infect., 2010, 12(2), 106-112.
    • (2010) Microbes. Infect. , vol.12 , Issue.2 , pp. 106-112
    • van Spriel, A.B.1    Figdor, C.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.