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Volumn 1, Issue 2, 2012, Pages 102-127

Exploitation of cellular cytoskeletons and signaling pathways for cell entry by Kaposi's sarcoma-associated herpesvirus and the closely related rhesus rhadinovirus

Author keywords

Actin; Cellular signaling; Endocytosis; Integrin; Kaposi's sarcoma associated herpesvirus (KSHV); Microtubule; Rhesus rhadinovirus (RRV); Ubiquitination; Virus entry

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; CD209 ANTIGEN; CLATHRIN; DYNEIN ADENOSINE TRIPHOSPHATASE; EARLY ENDOSOME ANTIGEN 1; EPHRIN A2; EPHRIN B2; EPHRIN RECEPTOR A2; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 15; F ACTIN; G ACTIN; GELATINASE A; GLYCOPROTEIN B; GLYCOPROTEIN L; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HEPARAN SULFATE; INTEGRIN; INTERLEUKIN 6; KINESIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; PROTEIN CDC42; PROTEIN TYROSINE KINASE; RAC1 PROTEIN; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SERUM RESPONSE FACTOR; UNINDEXED DRUG; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 84904412440     PISSN: None     EISSN: 20760817     Source Type: Journal    
DOI: 10.3390/pathogens1020102     Document Type: Review
Times cited : (7)

References (179)
  • 1
    • 0034077911 scopus 로고    scopus 로고
    • Cellular receptors for viruses: Links to tropism and pathogenesis
    • Schneider-Schaulies, J. Cellular receptors for viruses: Links to tropism and pathogenesis. J. Gen. Virol.2000, 81, 1413-1429.
    • (2000) J. Gen. Virol , vol.81 , pp. 1413-1429
    • Schneider-Schaulies, J.1
  • 2
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: Open sesame
    • Marsh, M.; Helenius, A. Virus entry: Open sesame. Cell 2006, 124, 729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 3
    • 34648828546 scopus 로고    scopus 로고
    • Molecular biology of KSHV in relation to AIDS-associated oncogenesis
    • Greene, W.; Kuhne, K.; Ye, F.; Chen, J.; Zhou, F.; Lei, X.; Gao, S.J. Molecular biology of KSHV in relation to AIDS-associated oncogenesis. Cancer Treat. Res. 2007, 133, 69-127.
    • (2007) Cancer Treat. Res , vol.133 , pp. 69-127
    • Greene, W.1    Kuhne, K.2    Ye, F.3    Chen, J.4    Zhou, F.5    Lei, X.6    Gao, S.J.7
  • 4
    • 84865483420 scopus 로고    scopus 로고
    • Kaposi's sarcoma associated herpesvirus entry into target cells
    • Chakraborty, S.; Veettil, M.V.; Chandran, B. Kaposi's sarcoma associated herpesvirus entry into target cells. Front. Microbiol. 2012, 3, 6.
    • (2012) Front. Microbiol , vol.3 , pp. 6
    • Chakraborty, S.1    Veettil, M.V.2    Chandran, B.3
  • 5
    • 77649197259 scopus 로고    scopus 로고
    • Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells
    • Chandran, B. Early events in Kaposi's sarcoma-associated herpesvirus infection of target cells. J. Virol. 2010, 84, 2188-2199.
    • (2010) J. Virol , vol.84 , pp. 2188-2199
    • Chandran, B.1
  • 6
    • 60049098650 scopus 로고    scopus 로고
    • Herpesvirus interactions with the host cytoskeleton
    • Lyman, M.G.; Enquist, L.W. Herpesvirus interactions with the host cytoskeleton. J. Virol. 2009, 83, 2058-2066.
    • (2009) J. Virol , vol.83 , pp. 2058-2066
    • Lyman, M.G.1    Enquist, L.W.2
  • 7
    • 79955667161 scopus 로고    scopus 로고
    • Actin' up: Herpesvirus interactions with rho gtpase signaling
    • Van den Broeke, C.; Favoreel, H.W. Actin' up: Herpesvirus interactions with rho gtpase signaling. Viruses 2011, 3, 278-292.
    • (2011) Viruses , vol.3 , pp. 278-292
    • Van den Broeke, C.1    Favoreel, H.W.2
  • 8
    • 79955661336 scopus 로고    scopus 로고
    • Actin in herpesvirus infection
    • Roberts, K.L.; Baines, J.D. Actin in herpesvirus infection. Viruses 2011, 3, 336-346.
    • (2011) Viruses , vol.3 , pp. 336-346
    • Roberts, K.L.1    Baines, J.D.2
  • 9
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: Component localization and mechanical coupling
    • Janmey, P.A. The cytoskeleton and cell signaling: Component localization and mechanical coupling. Physiol. Rev. 1998, 78, 763-781.
    • (1998) Physiol. Rev , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 11
    • 0025940482 scopus 로고
    • Structure and function of the endothelial cytoskeleton
    • Gottlieb, A.I.; Langille, B.L.; Wong, M.K.; Kim, D.W. Structure and function of the endothelial cytoskeleton. Lab. Invest. 1991, 65, 123-137.
    • (1991) Lab. Invest , vol.65 , pp. 123-137
    • Gottlieb, A.I.1    Langille, B.L.2    Wong, M.K.3    Kim, D.W.4
  • 12
    • 79960743030 scopus 로고    scopus 로고
    • Structural organization of the actin cytoskeleton at sites of clathrin-mediated endocytosis
    • Collins, A.; Warrington, A.; Taylor, K.A.; Svitkina, T. Structural organization of the actin cytoskeleton at sites of clathrin-mediated endocytosis. Curr. Biol. 2011, 21, 1167-1175.
    • (2011) Curr. Biol , vol.21 , pp. 1167-1175
    • Collins, A.1    Warrington, A.2    Taylor, K.A.3    Svitkina, T.4
  • 13
    • 0036228744 scopus 로고    scopus 로고
    • Intercellular adhesion, signalling and the cytoskeleton
    • Jamora, C.; Fuchs, E. Intercellular adhesion, signalling and the cytoskeleton. Nat. Cell Biol. 2002, 4, E101-108.
    • (2002) Nat. Cell Biol , vol.4
    • Jamora, C.1    Fuchs, E.2
  • 15
    • 1842862375 scopus 로고    scopus 로고
    • The role of the cytoskeleton during viral infection
    • Dohner, K.; Sodeik, B. The role of the cytoskeleton during viral infection. Curr. Top. Microbiol. Immunol. 2005, 285, 67-108.
    • (2005) Curr. Top. Microbiol. Immunol , vol.285 , pp. 67-108
    • Dohner, K.1    Sodeik, B.2
  • 16
    • 0033791649 scopus 로고    scopus 로고
    • Structural insights into microtubule function
    • Nogales, E. Structural insights into microtubule function. Annu. Rev. Biochem. 2000, 69, 277-302.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 277-302
    • Nogales, E.1
  • 17
    • 79956141898 scopus 로고    scopus 로고
    • Subversion of the actin cytoskeleton during viral infection
    • Taylor, M.P.; Koyuncu, O.O.; Enquist, L.W. Subversion of the actin cytoskeleton during viral infection. Nat. Rev. Microbiol. 2011, 9, 427-439.
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 427-439
    • Taylor, M.P.1    Koyuncu, O.O.2    Enquist, L.W.3
  • 18
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for rho gtpases: Turning on the switch
    • Schmidt, A.; Hall, A. Guanine nucleotide exchange factors for rho gtpases: Turning on the switch. Genes Dev. 2002, 16, 1587-1609.
    • (2002) Genes Dev , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 19
    • 58149330144 scopus 로고    scopus 로고
    • Regulation of cytokinesis by rho gtpase flux
    • Miller, A.L.; Bement, W.M. Regulation of cytokinesis by rho gtpase flux. Nat. Cell Biol. 2009, 11, 71-77.
    • (2009) Nat. Cell Biol , vol.11 , pp. 71-77
    • Miller, A.L.1    Bement, W.M.2
  • 20
    • 0034213327 scopus 로고    scopus 로고
    • Rho gtpases and their effector proteins
    • Bishop, A.L.; Hall, A. Rho gtpases and their effector proteins. Biochem. J. 2000, 348 Pt 2, 241-255.
    • (2000) Biochem. J , vol.348 , Issue.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 21
    • 84255195050 scopus 로고    scopus 로고
    • Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways
    • Anitei, M.; Hoflack, B. Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways. Nat. Cell Biol. 2012, 14, 11-19.
    • (2012) Nat. Cell Biol , vol.14 , pp. 11-19
    • Anitei, M.1    Hoflack, B.2
  • 22
    • 84855602576 scopus 로고    scopus 로고
    • Interplay between microtubule dynamics and intracellular organization
    • de Forges, H.; Bouissou, A.; Perez, F. Interplay between microtubule dynamics and intracellular organization. Int. J. Biochem. Cell Biol. 2012, 44, 266-274.
    • (2012) Int. J. Biochem. Cell Biol , vol.44 , pp. 266-274
    • de Forges, H.1    Bouissou, A.2    Perez, F.3
  • 23
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S.; Weber, K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 2003, 4, 938-947.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 24
    • 77957868249 scopus 로고    scopus 로고
    • Post-translational modifications of microtubules
    • Wloga, D.; Gaertig, J. Post-translational modifications of microtubules. J. Cell Sci. 2010, 123, 3447-3455.
    • (2010) J. Cell Sci , vol.123 , pp. 3447-3455
    • Wloga, D.1    Gaertig, J.2
  • 25
    • 21244468590 scopus 로고    scopus 로고
    • Viral stop-and-go along microtubules: Taking a ride with dynein and kinesins
    • Dohner, K.; Nagel, C.H.; Sodeik, B. Viral stop-and-go along microtubules: Taking a ride with dynein and kinesins. Trends Microbiol. 2005, 13, 320-327.
    • (2005) Trends Microbiol , vol.13 , pp. 320-327
    • Dohner, K.1    Nagel, C.H.2    Sodeik, B.3
  • 26
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee, M.A.; Heuser, J.E.; Vallee, R.B. An extended microtubule-binding structure within the dynein motor domain. Nature 1997, 390, 636-639.
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 27
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard, J.; Hudspeth, A.J.; Vale, R.D. Movement of microtubules by single kinesin molecules. Nature 1989, 342, 154-158.
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 28
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four aaa modules of cytoplasmic dynein
    • Kon, T.; Nishiura, M.; Ohkura, R.; Toyoshima, Y.Y.; Sutoh, K. Distinct functions of nucleotide-binding/hydrolysis sites in the four aaa modules of cytoplasmic dynein. Biochemistry 2004, 43, 11266-11274.
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.Y.4    Sutoh, K.5
  • 29
    • 79955415241 scopus 로고    scopus 로고
    • A rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza a virus viral rna
    • Amorim, M.J.; Bruce, E.A.; Read, E.K.; Foeglein, A.; Mahen, R.; Stuart, A.D.; Digard, P. A rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza a virus viral rna. J. Virol. 2011, 85, 4143-4156.
    • (2011) J. Virol , vol.85 , pp. 4143-4156
    • Amorim, M.J.1    Bruce, E.A.2    Read, E.K.3    Foeglein, A.4    Mahen, R.5    Stuart, A.D.6    Digard, P.7
  • 30
    • 77956205779 scopus 로고    scopus 로고
    • Trafficking of sendai virus nucleocapsids is mediated by intracellular vesicles
    • Chambers, R.; Takimoto, T. Trafficking of sendai virus nucleocapsids is mediated by intracellular vesicles. PLoS One 2010, 5, e10994.
    • (2010) PLoS One , vol.5
    • Chambers, R.1    Takimoto, T.2
  • 32
    • 67649598052 scopus 로고    scopus 로고
    • Intracellular transport of human immunodeficiency virus type 1 genomic rna and viral production are dependent on dynein motor function and late endosome positioning
    • Lehmann, M.; Milev, M.P.; Abrahamyan, L.; Yao, X.J.; Pante, N.; Mouland, A.J. Intracellular transport of human immunodeficiency virus type 1 genomic rna and viral production are dependent on dynein motor function and late endosome positioning. J. Biol. Chem. 2009, 284, 14572-14585.
    • (2009) J. Biol. Chem , vol.284 , pp. 14572-14585
    • Lehmann, M.1    Milev, M.P.2    Abrahamyan, L.3    Yao, X.J.4    Pante, N.5    Mouland, A.J.6
  • 35
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B.; Ebersold, M.W.; Helenius, A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 1997, 136, 1007-1021.
    • (1997) J. Cell Biol , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 37
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen, M.; Nakano, M.Y.; Keller, S.; Boucke, K.; Stidwill, R.P.; Greber, U.F. Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J. Cell Biol. 1999, 144, 657-672.
    • (1999) J. Cell Biol , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3    Boucke, K.4    Stidwill, R.P.5    Greber, U.F.6
  • 41
    • 46349083027 scopus 로고    scopus 로고
    • A gamma-herpesvirus glycoprotein complex manipulates actin to promote viral spread
    • Gill, M.B.; Edgar, R.; May, J.S.; Stevenson, P.G. A gamma-herpesvirus glycoprotein complex manipulates actin to promote viral spread. PLoS One 2008, 3, e1808.
    • (2008) PLoS One , vol.3
    • Gill, M.B.1    Edgar, R.2    May, J.S.3    Stevenson, P.G.4
  • 42
    • 77951582061 scopus 로고    scopus 로고
    • Linking actin dynamics and gene transcription to drive cellular motile functions
    • Olson, E.N.; Nordheim, A. Linking actin dynamics and gene transcription to drive cellular motile functions. Nat. Rev. Mol. Cell. Biol. 2010, 11, 353-365.
    • (2010) Nat. Rev. Mol. Cell. Biol , vol.11 , pp. 353-365
    • Olson, E.N.1    Nordheim, A.2
  • 43
    • 82755192841 scopus 로고    scopus 로고
    • Shaking the myosin family tree: Biochemical kinetics defines four types of myosin motor
    • Bloemink, M.J.; Geeves, M.A. Shaking the myosin family tree: Biochemical kinetics defines four types of myosin motor. Semin. Cell Dev. Biol. 2011, 22, 961-967.
    • (2011) Semin. Cell Dev. Biol , vol.22 , pp. 961-967
    • Bloemink, M.J.1    Geeves, M.A.2
  • 44
    • 77952934976 scopus 로고    scopus 로고
    • Structural and functional insights into the myosin motor mechanism
    • Sweeney, H.L.; Houdusse, A. Structural and functional insights into the myosin motor mechanism. Annu. Rev. Biophys. 2010, 39, 539-557.
    • (2010) Annu. Rev. Biophys , vol.39 , pp. 539-557
    • Sweeney, H.L.1    Houdusse, A.2
  • 46
    • 0034683666 scopus 로고    scopus 로고
    • Myosin vi: Roles for a minus end-directed actin motor in cells
    • Cramer, L.P. Myosin vi: Roles for a minus end-directed actin motor in cells. J. Cell. Biol. 2000, 150, F121-126.
    • (2000) J. Cell. Biol , vol.150
    • Cramer, L.P.1
  • 47
    • 32944475622 scopus 로고    scopus 로고
    • A superhighway to virus infection
    • Greber, U.F.; Way, M. A superhighway to virus infection. Cell 2006, 124, 741-754.
    • (2006) Cell , vol.124 , pp. 741-754
    • Greber, U.F.1    Way, M.2
  • 49
    • 0031663239 scopus 로고    scopus 로고
    • Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by rho family gtpases
    • Li, E.; Stupack, D.; Bokoch, G.M.; Nemerow, G.R. Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by rho family gtpases. J. Virol. 1998, 72, 8806-8812.
    • (1998) J. Virol , vol.72 , pp. 8806-8812
    • Li, E.1    Stupack, D.2    Bokoch, G.M.3    Nemerow, G.R.4
  • 50
    • 0029795964 scopus 로고    scopus 로고
    • The function of intermediate filaments in cell shape and cytoskeletal integrity
    • Goldman, R.D.; Khuon, S.; Chou, Y.H.; Opal, P.; Steinert, P.M. The function of intermediate filaments in cell shape and cytoskeletal integrity. J. Cell. Biol. 1996, 134, 971-983.
    • (1996) J. Cell. Biol , vol.134 , pp. 971-983
    • Goldman, R.D.1    Khuon, S.2    Chou, Y.H.3    Opal, P.4    Steinert, P.M.5
  • 51
    • 0033960790 scopus 로고    scopus 로고
    • Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics
    • Herrmann, H.; Aebi, U. Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr. Opin. Cell Biol. 2000, 12, 79-90.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 79-90
    • Herrmann, H.1    Aebi, U.2
  • 52
    • 18744398716 scopus 로고    scopus 로고
    • Cryo-electron microscopy of trichocyte (hard alpha-keratin) intermediate filaments reveals a low-density core
    • Watts, N.R.; Jones, L.N.; Cheng, N.; Wall, J.S.; Parry, D.A.; Steven, A.C. Cryo-electron microscopy of trichocyte (hard alpha-keratin) intermediate filaments reveals a low-density core. J. Struct. Biol. 2002, 137, 109-118.
    • (2002) J. Struct. Biol , vol.137 , pp. 109-118
    • Watts, N.R.1    Jones, L.N.2    Cheng, N.3    Wall, J.S.4    Parry, D.A.5    Steven, A.C.6
  • 53
    • 0037335755 scopus 로고    scopus 로고
    • Aebi, U. Molecular architecture of intermediate filaments
    • Strelkov, S.V.; Herrmann, H.; Aebi, U. Molecular architecture of intermediate filaments. Bioessays 2003, 25, 243-251.
    • (2003) Bioessays , vol.25 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2
  • 54
    • 0000595684 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • 3rd ed. ed.; Fields, B.N.; Knipe, D.M.; Howley, P.M., Eds.; Lippincott-Raven: Philadephia
    • Roizman, B.; Sears, E. Herpes simplex viruses and their replication. In Fundamental virology; 3rd ed. ed.; Fields, B.N.; Knipe, D.M.; Howley, P.M., Eds.; Lippincott-Raven: Philadephia, 1996; pp. 1043-1107.
    • (1996) Fundamental Virology , pp. 1043-1107
    • Roizman, B.1    Sears, E.2
  • 55
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter, T.C. Herpesvirus assembly and egress. J. Virol. 2002, 76, 1537-1547.
    • (2002) J. Virol , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 56
    • 0141632878 scopus 로고    scopus 로고
    • Herpesvirus entry: An update
    • Spear, P.G.; Longnecker, R. Herpesvirus entry: An update. J. Virol. 2003, 77, 10179-10185.
    • (2003) J. Virol , vol.77 , pp. 10179-10185
    • Spear, P.G.1    Longnecker, R.2
  • 57
    • 79960736994 scopus 로고    scopus 로고
    • Introduction to the human gamma-herpesviruses
    • Arvin, A.; Campadelli-Fiume, G.; Mocarski, E.; Moore, P.S.; Roizman, B.; Whitley, R.; Yamanishi, K., Eds.; Cambridge
    • Longnecker, R.; Neipel, F. Introduction to the human gamma-herpesviruses. In Human herpesviruses: Biology, therapy, and immunoprophylaxis; Arvin, A.; Campadelli-Fiume, G.; Mocarski, E.; Moore, P.S.; Roizman, B.; Whitley, R.; Yamanishi, K., Eds.; Cambridge, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis
    • Longnecker, R.1    Neipel, F.2
  • 58
    • 79953048485 scopus 로고    scopus 로고
    • Pathogenesis and host control of gammaherpesviruses: Lessons from the mouse
    • Barton, E.; Mandal, P.; Speck, S.H. Pathogenesis and host control of gammaherpesviruses: Lessons from the mouse. Annu. Rev. Immunol. 2011, 29, 351-397.
    • (2011) Annu. Rev. Immunol , vol.29 , pp. 351-397
    • Barton, E.1    Mandal, P.2    Speck, S.H.3
  • 59
    • 0038523775 scopus 로고    scopus 로고
    • Host range of kaposi's sarcoma-associated herpesvirus in cultured cells
    • Bechtel, J.T.; Liang, Y.; Hvidding, J.; Ganem, D. Host range of kaposi's sarcoma-associated herpesvirus in cultured cells. J. Virol. 2003, 77, 6474-6481.
    • (2003) J. Virol , vol.77 , pp. 6474-6481
    • Bechtel, J.T.1    Liang, Y.2    Hvidding, J.3    Ganem, D.4
  • 60
    • 79955465352 scopus 로고    scopus 로고
    • Viruses and human cancer: From detection to causality
    • Sarid, R.; Gao, S.J. Viruses and human cancer: From detection to causality. Cancer Lett. 2011, 305, 218-227.
    • (2011) Cancer Lett , vol.305 , pp. 218-227
    • Sarid, R.1    Gao, S.J.2
  • 61
    • 84865293571 scopus 로고    scopus 로고
    • Mechanisms of kaposi's sarcoma-associated herpesvirus latency and reactivation
    • 2011
    • Ye, F.; Lei, X.; Gao, S.J. Mechanisms of kaposi's sarcoma-associated herpesvirus latency and reactivation. Adv. Virol. 2011, 2011, pii 193860.
    • (2011) Adv. Virol , pp. 193860
    • Ye, F.1    Lei, X.2    Gao, S.J.3
  • 62
    • 78049380583 scopus 로고    scopus 로고
    • Molecular biology of kaposi's sarcoma-associated herpesvirus and related oncogenesis
    • Cai, Q.; Verma, S.C.; Lu, J.; Robertson, E.S. Molecular biology of kaposi's sarcoma-associated herpesvirus and related oncogenesis. Adv. Virus Res. 2010, 78, 87-142.
    • (2010) Adv. Virus Res , vol.78 , pp. 87-142
    • Cai, Q.1    Verma, S.C.2    Lu, J.3    Robertson, E.S.4
  • 63
    • 77958183244 scopus 로고    scopus 로고
    • Viral latency and its regulation: Lessons from the gamma-herpesviruses
    • Speck, S.H.; Ganem, D. Viral latency and its regulation: Lessons from the gamma-herpesviruses. Cell Host Microbe 2010, 8, 100-115.
    • (2010) Cell Host Microbe , vol.8 , pp. 100-115
    • Speck, S.H.1    Ganem, D.2
  • 64
    • 77957121811 scopus 로고    scopus 로고
    • Kaposi's sarcoma and its associated herpesvirus
    • Mesri, E.A.; Cesarman, E.; Boshoff, C. Kaposi's sarcoma and its associated herpesvirus. Nat. Rev. Cancer 2010, 10, 707-719.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 707-719
    • Mesri, E.A.1    Cesarman, E.2    Boshoff, C.3
  • 65
    • 0038654366 scopus 로고    scopus 로고
    • Aids-related malignancies
    • Scadden, D.T. Aids-related malignancies. Annu. Rev. Med. 2003, 54, 285-303.
    • (2003) Annu. Rev. Med , vol.54 , pp. 285-303
    • Scadden, D.T.1
  • 67
    • 0032975917 scopus 로고    scopus 로고
    • Sequence and genomic analysis of a rhesus macaque rhadinovirus with similarity to kaposi's sarcoma-associated herpesvirus/human herpesvirus 8
    • Searles, R.P.; Bergquam, E.P.; Axthelm, M.K.; Wong, S.W. Sequence and genomic analysis of a rhesus macaque rhadinovirus with similarity to kaposi's sarcoma-associated herpesvirus/human herpesvirus 8. J. Virol. 1999, 73, 3040-3053.
    • (1999) J. Virol , vol.73 , pp. 3040-3053
    • Searles, R.P.1    Bergquam, E.P.2    Axthelm, M.K.3    Wong, S.W.4
  • 68
    • 0033588879 scopus 로고    scopus 로고
    • Induction of b cell hyperplasia in simian immunodeficiency virus-infected rhesus macaques with the simian homologue of kaposi's sarcoma-associated herpesvirus
    • Wong, S.W.; Bergquam, E.P.; Swanson, R.M.; Lee, F.W.; Shiigi, S.M.; Avery, N.A.; Fanton, J.W.; Axthelm, M.K. Induction of b cell hyperplasia in simian immunodeficiency virus-infected rhesus macaques with the simian homologue of kaposi's sarcoma-associated herpesvirus. J. Exp. Med. 1999, 190, 827-840.
    • (1999) J. Exp. Med , vol.190 , pp. 827-840
    • Wong, S.W.1    Bergquam, E.P.2    Swanson, R.M.3    Lee, F.W.4    Shiigi, S.M.5    Avery, N.A.6    Fanton, J.W.7    Axthelm, M.K.8
  • 69
    • 58149169170 scopus 로고    scopus 로고
    • Rhesus macaque rhadinovirus-associated non-hodgkin lymphoma: Animal model for KSHV-associated malignancies
    • Orzechowska, B.U.; Powers, M.F.; Sprague, J.; Li, H.; Yen, B.; Searles, R.P.; Axthelm, M.K.; Wong, S.W. Rhesus macaque rhadinovirus-associated non-hodgkin lymphoma: Animal model for KSHV-associated malignancies. Blood 2008, 112, 4227-4234.
    • (2008) Blood , vol.112 , pp. 4227-4234
    • Orzechowska, B.U.1    Powers, M.F.2    Sprague, J.3    Li, H.4    Yen, B.5    Searles, R.P.6    Axthelm, M.K.7    Wong, S.W.8
  • 70
    • 48149108390 scopus 로고    scopus 로고
    • Designing an effective aids vaccine: Strategies and current status
    • Coutsinos, Z.; Absi, Z.; Henin, Y.; Guillet, J.G.; Launay, O. Designing an effective aids vaccine: Strategies and current status. Rev. Med. Interne. 2008, 29, 632-641.
    • (2008) Rev. Med. Interne , vol.29 , pp. 632-641
    • Coutsinos, Z.1    Absi, Z.2    Henin, Y.3    Guillet, J.G.4    Launay, O.5
  • 71
    • 1842612607 scopus 로고    scopus 로고
    • Virus entry: Molecular mechanisms and biomedical applications
    • Dimitrov, D.S. Virus entry: Molecular mechanisms and biomedical applications. Nat. Rev. Microbiol. 2004, 2, 109-122.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 109-122
    • Dimitrov, D.S.1
  • 72
    • 44749091723 scopus 로고    scopus 로고
    • Entry of herpesviruses into mammalian cells
    • Heldwein, E.E.; Krummenacher, C. Entry of herpesviruses into mammalian cells. Cell. Mol. Life Sci. 2008, 65, 1653-1668.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 1653-1668
    • Heldwein, E.E.1    Krummenacher, C.2
  • 73
    • 0023037932 scopus 로고
    • Oligomerization of herpes simplex virus glycoprotein b
    • Claesson-Welsh, L.; Spear, P.G. Oligomerization of herpes simplex virus glycoprotein b. J. Virol. 1986, 60, 803-806.
    • (1986) J. Virol , vol.60 , pp. 803-806
    • Claesson-Welsh, L.1    Spear, P.G.2
  • 74
    • 0036226223 scopus 로고    scopus 로고
    • Human herpesvirus 8 glycoprotein b (gb), gh, and gl can mediate cell fusion
    • Pertel, P.E. Human herpesvirus 8 glycoprotein b (gb), gh, and gl can mediate cell fusion. J. Virol. 2002, 76, 4390-4400.
    • (2002) J. Virol , vol.76 , pp. 4390-4400
    • Pertel, P.E.1
  • 76
    • 0033568369 scopus 로고    scopus 로고
    • Characterization of human herpesvirus-8 k8.1a/b glycoproteins by monoclonal antibodies
    • Zhu, L.; Puri, V.; Chandran, B. Characterization of human herpesvirus-8 k8.1a/b glycoproteins by monoclonal antibodies. Virology 1999, 262, 237-249.
    • (1999) Virology , vol.262 , pp. 237-249
    • Zhu, L.1    Puri, V.2    Chandran, B.3
  • 77
    • 79960390398 scopus 로고    scopus 로고
    • Rhesus monkey rhadinovirus orf57 induces gh and gl glycoprotein expression through posttranscriptional accumulation of target mrnas
    • Shin, Y.C.; Desrosiers, R.C. Rhesus monkey rhadinovirus orf57 induces gh and gl glycoprotein expression through posttranscriptional accumulation of target mrnas. J. Virol. 2011, 85, 7810-7817.
    • (2011) J. Virol , vol.85 , pp. 7810-7817
    • Shin, Y.C.1    Desrosiers, R.C.2
  • 78
    • 47049084010 scopus 로고    scopus 로고
    • Extreme dependence of gh and gl expression on orf57 and association with highly unusual codon usage in rhesus monkey rhadinovirus
    • Bilello, J.P.; Morgan, J.S.; Desrosiers, R.C. Extreme dependence of gh and gl expression on orf57 and association with highly unusual codon usage in rhesus monkey rhadinovirus. J. Virol. 2008, 82, 7231-7237.
    • (2008) J. Virol , vol.82 , pp. 7231-7237
    • Bilello, J.P.1    Morgan, J.S.2    Desrosiers, R.C.3
  • 79
    • 0034099096 scopus 로고    scopus 로고
    • The primary sequence of rhesus monkey rhadinovirus isolate 26-95: Sequence similarities to kaposi's sarcoma-associated herpesvirus and rhesus monkey rhadinovirus isolate 17577
    • Alexander, L.; Denekamp, L.; Knapp, A.; Auerbach, M.R.; Damania, B.; Desrosiers, R.C. The primary sequence of rhesus monkey rhadinovirus isolate 26-95: Sequence similarities to kaposi's sarcoma-associated herpesvirus and rhesus monkey rhadinovirus isolate 17577. J. Virol. 2000, 74, 3388-3398.
    • (2000) J. Virol , vol.74 , pp. 3388-3398
    • Alexander, L.1    Denekamp, L.2    Knapp, A.3    Auerbach, M.R.4    Damania, B.5    Desrosiers, R.C.6
  • 81
    • 34547110512 scopus 로고    scopus 로고
    • Epstein-barr virus entry
    • Hutt-Fletcher, L.M. Epstein-barr virus entry. J. Virol. 2007, 81, 7825-7832.
    • (2007) J. Virol , vol.81 , pp. 7825-7832
    • Hutt-Fletcher, L.M.1
  • 82
  • 84
    • 79953199052 scopus 로고    scopus 로고
    • How does cellular heparan sulfate function in viral pathogenicity?
    • Zhu, W.; Li, J.; Liang, G. How does cellular heparan sulfate function in viral pathogenicity? Biomed. Environ. Sci. 2011, 24, 81-87.
    • (2011) Biomed. Environ. Sci , vol.24 , pp. 81-87
    • Zhu, W.1    Li, J.2    Liang, G.3
  • 85
    • 0034883314 scopus 로고    scopus 로고
    • Herpesviruses and heparan sulfate: An intimate relationship in aid of viral entry
    • Shukla, D.; Spear, P.G. Herpesviruses and heparan sulfate: An intimate relationship in aid of viral entry. J. Clin. Invest. 2001, 108, 503-510.
    • (2001) J. Clin. Invest , vol.108 , pp. 503-510
    • Shukla, D.1    Spear, P.G.2
  • 86
    • 0024497174 scopus 로고
    • Initial interaction of herpes simplex virus with cells is binding to heparan sulfate
    • WuDunn, D.; Spear, P.G. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J. Virol. 1989, 63, 52-58.
    • (1989) J. Virol , vol.63 , pp. 52-58
    • Wudunn, D.1    Spear, P.G.2
  • 87
    • 0026551062 scopus 로고
    • Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans
    • Shieh, M.T.; WuDunn, D.; Montgomery, R.I.; Esko, J.D.; Spear, P.G. Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J. Cell Biol. 1992, 116, 1273-1281.
    • (1992) J. Cell Biol , vol.116 , pp. 1273-1281
    • Shieh, M.T.1    Wudunn, D.2    Montgomery, R.I.3    Esko, J.D.4    Spear, P.G.5
  • 89
    • 58049209246 scopus 로고    scopus 로고
    • The importance of heparan sulfate in herpesvirus infection
    • O'Donnell, C.D.; Shukla, D. The importance of heparan sulfate in herpesvirus infection. Virol. Sin. 2008, 23, 383-393.
    • (2008) Virol. Sin , vol.23 , pp. 383-393
    • O'Donnell, C.D.1    Shukla, D.2
  • 90
    • 0035811148 scopus 로고    scopus 로고
    • Human herpesvirus 8 envelope-associated glycoprotein b interacts with heparan sulfate-like moieties
    • Akula, S.M.; Pramod, N.P.; Wang, F.Z.; Chandran, B. Human herpesvirus 8 envelope-associated glycoprotein b interacts with heparan sulfate-like moieties. Virology 2001, 284, 235-249.
    • (2001) Virology , vol.284 , pp. 235-249
    • Akula, S.M.1    Pramod, N.P.2    Wang, F.Z.3    Chandran, B.4
  • 91
    • 0035836376 scopus 로고    scopus 로고
    • Human herpesvirus 8 interaction with target cells involves heparan sulfate
    • Akula, S.M.; Wang, F.Z.; Vieira, J.; Chandran, B. Human herpesvirus 8 interaction with target cells involves heparan sulfate. Virology 2001, 282, 245-255.
    • (2001) Virology , vol.282 , pp. 245-255
    • Akula, S.M.1    Wang, F.Z.2    Vieira, J.3    Chandran, B.4
  • 92
    • 58149382621 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus gh/gl: Glycoprotein export and interaction with cellular receptors
    • Hahn, A.; Birkmann, A.; Wies, E.; Dorer, D.; Mahr, K.; Sturzl, M.; Titgemeyer, F.; Neipel, F. Kaposi's sarcoma-associated herpesvirus gh/gl: Glycoprotein export and interaction with cellular receptors. J. Virol. 2009, 83, 396-407.
    • (2009) J. Virol , vol.83 , pp. 396-407
    • Hahn, A.1    Birkmann, A.2    Wies, E.3    Dorer, D.4    Mahr, K.5    Sturzl, M.6    Titgemeyer, F.7    Neipel, F.8
  • 93
    • 0034902748 scopus 로고    scopus 로고
    • Human herpesvirus 8 envelope glycoprotein K8.1a interaction with the target cells involves heparan sulfate
    • Wang, F.Z.; Akula, S.M.; Pramod, N.P.; Zeng, L.; Chandran, B. Human herpesvirus 8 envelope glycoprotein K8.1a interaction with the target cells involves heparan sulfate. J. Virol. 2001, 75, 7517-7527.
    • (2001) J. Virol , vol.75 , pp. 7517-7527
    • Wang, F.Z.1    Akula, S.M.2    Pramod, N.P.3    Zeng, L.4    Chandran, B.5
  • 94
    • 0035159830 scopus 로고    scopus 로고
    • Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1
    • Birkmann, A.; Mahr, K.; Ensser, A.; Yaguboglu, S.; Titgemeyer, F.; Fleckenstein, B.; Neipel, F. Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1. J. Virol. 2001, 75, 11583-11593.
    • (2001) J. Virol , vol.75 , pp. 11583-11593
    • Birkmann, A.1    Mahr, K.2    Ensser, A.3    Yaguboglu, S.4    Titgemeyer, F.5    Fleckenstein, B.6    Neipel, F.7
  • 95
    • 2642581527 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus glycoprotein K8.1 is dispensable for virus entry
    • Luna, R.E.; Zhou, F.; Baghian, A.; Chouljenko, V.; Forghani, B.; Gao, S.J.; Kousoulas, K.G. Kaposi's sarcoma-associated herpesvirus glycoprotein K8.1 is dispensable for virus entry. J. Virol. 2004, 78, 6389-6398.
    • (2004) J. Virol , vol.78 , pp. 6389-6398
    • Luna, R.E.1    Zhou, F.2    Baghian, A.3    Chouljenko, V.4    Forghani, B.5    Gao, S.J.6    Kousoulas, K.G.7
  • 96
    • 78049495027 scopus 로고    scopus 로고
    • Rhesus rhadinovirus infection of rhesus fibroblasts occurs through clathrin-mediated endocytosis
    • Zhang, W.; Zhou, F.; Greene, W.; Gao, S.J. Rhesus rhadinovirus infection of rhesus fibroblasts occurs through clathrin-mediated endocytosis. J. Virol. 2010, 84, 11709-11717.
    • (2010) J. Virol , vol.84 , pp. 11709-11717
    • Zhang, W.1    Zhou, F.2    Greene, W.3    Gao, S.J.4
  • 97
    • 83655162842 scopus 로고    scopus 로고
    • The cell biology of receptor-mediated virus entry
    • Grove, J.; Marsh, M. The cell biology of receptor-mediated virus entry. J. Cell Biol. 2011, 195, 1071-1082.
    • (2011) J. Cell Biol , vol.195 , pp. 1071-1082
    • Grove, J.1    Marsh, M.2
  • 99
    • 0037227929 scopus 로고    scopus 로고
    • Differential n-linked glycosylation of human immunodeficiency virus and ebola virus envelope glycoproteins modulates interactions with dc-sign and dc-signr
    • Lin, G.; Simmons, G.; Pohlmann, S.; Baribaud, F.; Ni, H.; Leslie, G.J.; Haggarty, B.S.; Bates, P.; Weissman, D.; Hoxie, J.A.; Doms, R.W. Differential n-linked glycosylation of human immunodeficiency virus and ebola virus envelope glycoproteins modulates interactions with dc-sign and dc-signr. J. Virol. 2003, 77, 1337-1346.
    • (2003) J. Virol , vol.77 , pp. 1337-1346
    • Lin, G.1    Simmons, G.2    Pohlmann, S.3    Baribaud, F.4    Ni, H.5    Leslie, G.J.6    Haggarty, B.S.7    Bates, P.8    Weissman, D.9    Hoxie, J.A.10    Doms, R.W.11
  • 100
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins dc-sign and l-sign mediate cellular entry by ebola virus in cis and in trans
    • Alvarez, C.P.; Lasala, F.; Carrillo, J.; Muniz, O.; Corbi, A.L.; Delgado, R. C-type lectins dc-sign and l-sign mediate cellular entry by ebola virus in cis and in trans. J. Virol. 2002, 76, 6841-6844.
    • (2002) J. Virol , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1    Lasala, F.2    Carrillo, J.3    Muniz, O.4    Corbi, A.L.5    Delgado, R.6
  • 103
    • 0036172314 scopus 로고    scopus 로고
    • Dc-sign-mediated internalization of hiv is required for trans-enhancement of t cell infection
    • Kwon, D.S.; Gregorio, G.; Bitton, N.; Hendrickson, W.A.; Littman, D.R. Dc-sign-mediated internalization of hiv is required for trans-enhancement of t cell infection. Immunity 2002, 16, 135-144.
    • (2002) Immunity , vol.16 , pp. 135-144
    • Kwon, D.S.1    Gregorio, G.2    Bitton, N.3    Hendrickson, W.A.4    Littman, D.R.5
  • 104
    • 77956181131 scopus 로고    scopus 로고
    • Characterization of entry and infection of monocytic thp-1 cells by Kaposi's sarcoma associated herpesvirus (KSHV): Role of heparan sulfate, dc-sign, integrins and signaling
    • Kerur, N.; Veettil, M.V.; Sharma-Walia, N.; Sadagopan, S.; Bottero, V.; Paul, A.G.; Chandran, B. Characterization of entry and infection of monocytic thp-1 cells by Kaposi's sarcoma associated herpesvirus (KSHV): Role of heparan sulfate, dc-sign, integrins and signaling. Virology 2010, 406, 103-116.
    • (2010) Virology , vol.406 , pp. 103-116
    • Kerur, N.1    Veettil, M.V.2    Sharma-Walia, N.3    Sadagopan, S.4    Bottero, V.5    Paul, A.G.6    Chandran, B.7
  • 105
    • 43249086082 scopus 로고    scopus 로고
    • Human herpesvirus 8 infects and replicates in primary cultures of activated b lymphocytes through dc-sign
    • Rappocciolo, G.; Hensler, H.R.; Jais, M.; Reinhart, T.A.; Pegu, A.; Jenkins, F.J.; Rinaldo, C.R. Human herpesvirus 8 infects and replicates in primary cultures of activated b lymphocytes through dc-sign. J. Virol. 2008, 82, 4793-4806.
    • (2008) J. Virol , vol.82 , pp. 4793-4806
    • Rappocciolo, G.1    Hensler, H.R.2    Jais, M.3    Reinhart, T.A.4    Pegu, A.5    Jenkins, F.J.6    Rinaldo, C.R.7
  • 107
    • 57349181494 scopus 로고    scopus 로고
    • Lack of heparan sulfate expression in b-cell lines: Implications for kaposi's sarcoma-associated herpesvirus and murine gammaherpesvirus 68 infections
    • Jarousse, N.; Chandran, B.; Coscoy, L. Lack of heparan sulfate expression in b-cell lines: Implications for kaposi's sarcoma-associated herpesvirus and murine gammaherpesvirus 68 infections. J. Virol. 2008, 82, 12591-12597.
    • (2008) J. Virol , vol.82 , pp. 12591-12597
    • Jarousse, N.1    Chandran, B.2    Coscoy, L.3
  • 108
    • 84862924585 scopus 로고    scopus 로고
    • Reconstruction of integrin activation
    • Ye, F.; Kim, C.; Ginsberg, M.H. Reconstruction of integrin activation. Blood 2012, 119, 26-33.
    • (2012) Blood , vol.119 , pp. 26-33
    • Ye, F.1    Kim, C.2    Ginsberg, M.H.3
  • 109
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F.G.; Ruoslahti, E. Integrin signaling. Science 1999, 285, 1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 110
    • 36049006185 scopus 로고    scopus 로고
    • Cell integrins: Commonly used receptors for diverse viral pathogens
    • Stewart, P.L.; Nemerow, G.R. Cell integrins: Commonly used receptors for diverse viral pathogens. Trends Microbiol. 2007, 15, 500-507.
    • (2007) Trends Microbiol , vol.15 , pp. 500-507
    • Stewart, P.L.1    Nemerow, G.R.2
  • 111
    • 0036008473 scopus 로고    scopus 로고
    • Integrin alpha3beta1 (cd 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells
    • Akula, S.M.; Pramod, N.P.; Wang, F.Z.; Chandran, B. Integrin alpha3beta1 (cd 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells. Cell 2002, 108, 407-419.
    • (2002) Cell , vol.108 , pp. 407-419
    • Akula, S.M.1    Pramod, N.P.2    Wang, F.Z.3    Chandran, B.4
  • 114
    • 0037369082 scopus 로고    scopus 로고
    • Human herpesvirus 8 envelope glycoprotein b mediates cell adhesion via its rgd sequence
    • Wang, F.Z.; Akula, S.M.; Sharma-Walia, N.; Zeng, L.; Chandran, B. Human herpesvirus 8 envelope glycoprotein b mediates cell adhesion via its rgd sequence. J. Virol. 2003, 77, 3131-3147.
    • (2003) J. Virol , vol.77 , pp. 3131-3147
    • Wang, F.Z.1    Akula, S.M.2    Sharma-Walia, N.3    Zeng, L.4    Chandran, B.5
  • 115
    • 57349163515 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus forms a multimolecular complex of integrins (alphavbeta5, alphavbeta3, and alpha3beta1) and cd98-xct during infection of human dermal microvascular endothelial cells, and cd98-xct is essential for the postentry stage of infection
    • Veettil, M.V.; Sadagopan, S.; Sharma-Walia, N.; Wang, F.Z.; Raghu, H.; Varga, L.; Chandran, B. Kaposi's sarcoma-associated herpesvirus forms a multimolecular complex of integrins (alphavbeta5, alphavbeta3, and alpha3beta1) and cd98-xct during infection of human dermal microvascular endothelial cells, and cd98-xct is essential for the postentry stage of infection. J. Virol. 2008, 82, 12126-12144.
    • (2008) J. Virol , vol.82 , pp. 12126-12144
    • Veettil, M.V.1    Sadagopan, S.2    Sharma-Walia, N.3    Wang, F.Z.4    Raghu, H.5    Varga, L.6    Chandran, B.7
  • 116
    • 0038758763 scopus 로고    scopus 로고
    • Characterization of entry mechanisms of human herpesvirus 8 by using an rta-dependent reporter cell line
    • Inoue, N.; Winter, J.; Lal, R.B.; Offermann, M.K.; Koyano, S. Characterization of entry mechanisms of human herpesvirus 8 by using an rta-dependent reporter cell line. J. Virol. 2003, 77, 8147-8152.
    • (2003) J. Virol , vol.77 , pp. 8147-8152
    • Inoue, N.1    Winter, J.2    Lal, R.B.3    Offermann, M.K.4    Koyano, S.5
  • 117
    • 33748957350 scopus 로고    scopus 로고
    • Broad target cell selectivity of kaposi's sarcoma-associated herpesvirus glycoprotein-mediated cell fusion and virion entry
    • Kaleeba, J.A.; Berger, E.A. Broad target cell selectivity of kaposi's sarcoma-associated herpesvirus glycoprotein-mediated cell fusion and virion entry. Virology 2006, 354, 7-14.
    • (2006) Virology , vol.354 , pp. 7-14
    • Kaleeba, J.A.1    Berger, E.A.2
  • 118
    • 38349134847 scopus 로고    scopus 로고
    • Integrin alphavbeta3 binds to the rgd motif of glycoprotein b of kaposi's sarcoma-associated herpesvirus and functions as an rgd-dependent entry receptor
    • Garrigues, H.J.; Rubinchikova, Y.E.; Dipersio, C.M.; Rose, T.M. Integrin alphavbeta3 binds to the rgd motif of glycoprotein b of kaposi's sarcoma-associated herpesvirus and functions as an rgd-dependent entry receptor. J. Virol. 2008, 82, 1570-1580.
    • (2008) J. Virol , vol.82 , pp. 1570-1580
    • Garrigues, H.J.1    Rubinchikova, Y.E.2    Dipersio, C.M.3    Rose, T.M.4
  • 119
    • 0032532104 scopus 로고    scopus 로고
    • Modulation of rgd sequence motifs regulates disintegrin recognition of alphaiib beta3 and alpha5 beta1 integrin complexes. Replacement of elegantin alanine-50 with proline, n-terminal to the rgd sequence, diminishes recognition of the alpha5 beta1 complex with restoration induced by mn2+ cation
    • Rahman, S.; Aitken, A.; Flynn, G.; Formstone, C.; Savidge, G.F. Modulation of rgd sequence motifs regulates disintegrin recognition of alphaiib beta3 and alpha5 beta1 integrin complexes. Replacement of elegantin alanine-50 with proline, n-terminal to the rgd sequence, diminishes recognition of the alpha5 beta1 complex with restoration induced by mn2+ cation. Biochem. J. 1998, 335 (Pt2), 247-257.
    • (1998) Biochem. J , vol.335 , Issue.2 , pp. 247-257
    • Rahman, S.1    Aitken, A.2    Flynn, G.3    Formstone, C.4    Savidge, G.F.5
  • 121
    • 41149084179 scopus 로고    scopus 로고
    • Eph-ephrin bidirectional signaling in physiology and disease
    • Pasquale, E.B. Eph-ephrin bidirectional signaling in physiology and disease. Cell 2008, 133, 38-52.
    • (2008) Cell , vol.133 , pp. 38-52
    • Pasquale, E.B.1
  • 122
    • 0036785161 scopus 로고    scopus 로고
    • Diverse roles for the eph family of receptor tyrosine kinases in carcinogenesis
    • Nakamoto, M.; Bergemann, A.D. Diverse roles for the eph family of receptor tyrosine kinases in carcinogenesis. Microsc. Res. Tech. 2002, 59, 58-67.
    • (2002) Microsc. Res. Tech , vol.59 , pp. 58-67
    • Nakamoto, M.1    Bergemann, A.D.2
  • 123
    • 0033970865 scopus 로고    scopus 로고
    • A splice variant of human ephrin-a4 encodes a soluble molecule that is secreted by activated human b lymphocytes
    • Aasheim, H.C.; Munthe, E.; Funderud, S.; Smeland, E.B.; Beiske, K.; Logtenberg, T. A splice variant of human ephrin-a4 encodes a soluble molecule that is secreted by activated human b lymphocytes. Blood 2000, 95, 221-230.
    • (2000) Blood , vol.95 , pp. 221-230
    • Aasheim, H.C.1    Munthe, E.2    Funderud, S.3    Smeland, E.B.4    Beiske, K.5    Logtenberg, T.6
  • 124
    • 0035984168 scopus 로고    scopus 로고
    • Characterization of gamma2-human herpesvirus-8 glycoproteins gh and gl
    • Naranatt, P.P.; Akula, S.M.; Chandran, B. Characterization of gamma2-human herpesvirus-8 glycoproteins gh and gl. Arch. Virol. 2002, 147, 1349-1370.
    • (2002) Arch. Virol , vol.147 , pp. 1349-1370
    • Naranatt, P.P.1    Akula, S.M.2    Chandran, B.3
  • 125
    • 84860832684 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus interacts with ephrina2 receptor to amplify signaling essential for productive infection
    • Chakraborty, S.; Veettil, M.V.; Bottero, V.; Chandran, B. Kaposi's sarcoma-associated herpesvirus interacts with ephrina2 receptor to amplify signaling essential for productive infection. Proc. Natl. Acad. Sci. USA 2012, 109, E1163-1172.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Chakraborty, S.1    Veettil, M.V.2    Bottero, V.3    Chandran, B.4
  • 126
    • 84863969631 scopus 로고    scopus 로고
    • Cancer angiogenesis induced by kaposi's sarcoma-associated herpesvirus is mediated by ezh2
    • He, M.; Zhang, W.; Bakken, T.; Schutten, M.; Toth, Z.; Jung, J.U.; Gill, P.; Cannon, M.; Gao, S.J. Cancer angiogenesis induced by kaposi's sarcoma-associated herpesvirus is mediated by ezh2. Cancer Res. 2012, 72, 3582-3592.
    • (2012) Cancer Res , vol.72 , pp. 3582-3592
    • He, M.1    Zhang, W.2    Bakken, T.3    Schutten, M.4    Toth, Z.5    Jung, J.U.6    Gill, P.7    Cannon, M.8    Gao, S.J.9
  • 127
    • 0020026263 scopus 로고
    • Induction of maturation in cultured human monocytic leukemia cells by a phorbol diester
    • Tsuchiya, S.; Kobayashi, Y.; Goto, Y.; Okumura, H.; Nakae, S.; Konno, T.; Tada, K. Induction of maturation in cultured human monocytic leukemia cells by a phorbol diester. Cancer Res. 1982, 42, 1530-1536.
    • (1982) Cancer Res , vol.42 , pp. 1530-1536
    • Tsuchiya, S.1    Kobayashi, Y.2    Goto, Y.3    Okumura, H.4    Nakae, S.5    Konno, T.6    Tada, K.7
  • 128
    • 42949126711 scopus 로고    scopus 로고
    • The x(c)- cystine/glutamate antiporter: A potential target for therapy of cancer and other diseases
    • Lo, M.; Wang, Y.Z.; Gout, P.W. The x(c)- cystine/glutamate antiporter: A potential target for therapy of cancer and other diseases. J. Cell Physiol. 2008, 215, 593-602.
    • (2008) J. Cell Physiol , vol.215 , pp. 593-602
    • Lo, M.1    Wang, Y.Z.2    Gout, P.W.3
  • 129
    • 33645468403 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus fusion-entry receptor: Cystine transporter xCT
    • Kaleeba, J.A.; Berger, E.A. Kaposi's sarcoma-associated herpesvirus fusion-entry receptor: Cystine transporter xCT. Science 2006, 311, 1921-1924.
    • (2006) Science , vol.311 , pp. 1921-1924
    • Kaleeba, J.A.1    Berger, E.A.2
  • 130
    • 0036298810 scopus 로고    scopus 로고
    • Dissecting virus entry via endocytosis
    • Sieczkarski, S.B.; Whittaker, G.R. Dissecting virus entry via endocytosis. J. Gen. Virol. 2002, 83, 1535-1545.
    • (2002) J. Gen. Virol , vol.83 , pp. 1535-1545
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 131
    • 0021325510 scopus 로고
    • Early events in the infection of human b lymphocytes by epstein-barr virus: The internalization process
    • Nemerow, G.R.; Cooper, N.R. Early events in the infection of human b lymphocytes by epstein-barr virus: The internalization process. Virology 1984, 132, 186-198.
    • (1984) Virology , vol.132 , pp. 186-198
    • Nemerow, G.R.1    Cooper, N.R.2
  • 132
    • 0026696312 scopus 로고
    • Epstein-barr virus enters b cells and epithelial cells by different routes
    • Miller, N.; Hutt-Fletcher, L.M. Epstein-barr virus enters b cells and epithelial cells by different routes. J. Virol. 1992, 66, 3409-3414.
    • (1992) J. Virol , vol.66 , pp. 3409-3414
    • Miller, N.1    Hutt-Fletcher, L.M.2
  • 134
    • 0017658303 scopus 로고
    • Replication of epstein-barr virus: Ultrastructural and immunofluorescent studies of p3hr1-superinfected raji cells
    • Seigneurin, J.M.; Vuillaume, M.; Lenoir, G.; De-The, G. Replication of epstein-barr virus: Ultrastructural and immunofluorescent studies of p3hr1-superinfected raji cells. J. Virol. 1977, 24, 836-845.
    • (1977) J. Virol , vol.24 , pp. 836-845
    • Seigneurin, J.M.1    Vuillaume, M.2    Lenoir, G.3    De-The, G.4
  • 135
    • 0038082194 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) infection of human fibroblast cells occurs through endocytosis
    • Akula, S.M.; Naranatt, P.P.; Walia, N.S.; Wang, F.Z.; Fegley, B.; Chandran, B. Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) infection of human fibroblast cells occurs through endocytosis. J. Virol. 2003, 77, 7978-7990.
    • (2003) J. Virol , vol.77 , pp. 7978-7990
    • Akula, S.M.1    Naranatt, P.P.2    Walia, N.S.3    Wang, F.Z.4    Fegley, B.5    Chandran, B.6
  • 136
    • 70049116403 scopus 로고    scopus 로고
    • Actin dynamics regulate multiple endosomal steps during kaposi's sarcoma-associated herpesvirus entry and trafficking in endothelial cells
    • Greene, W.; Gao, S.J. Actin dynamics regulate multiple endosomal steps during kaposi's sarcoma-associated herpesvirus entry and trafficking in endothelial cells. PLoS Pathog. 2009, 5, e1000512.
    • (2009) PLoS Pathog , vol.5
    • Greene, W.1    Gao, S.J.2
  • 137
    • 65349165676 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells
    • Raghu, H.; Sharma-Walia, N.; Veettil, M.V.; Sadagopan, S.; Chandran, B. Kaposi's sarcoma-associated herpesvirus utilizes an actin polymerization-dependent macropinocytic pathway to enter human dermal microvascular endothelial and human umbilical vein endothelial cells. J. Virol. 2009, 83, 4895-4911.
    • (2009) J. Virol , vol.83 , pp. 4895-4911
    • Raghu, H.1    Sharma-Walia, N.2    Veettil, M.V.3    Sadagopan, S.4    Chandran, B.5
  • 138
    • 33847131016 scopus 로고    scopus 로고
    • Virus trafficking - learning from single-virus tracking
    • Brandenburg, B.; Zhuang, X. Virus trafficking - learning from single-virus tracking. Nat. Rev. Microbiol. 2007, 5, 197-208.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 197-208
    • Brandenburg, B.1    Zhuang, X.2
  • 139
    • 0036437319 scopus 로고    scopus 로고
    • Break ins and break outs: Viral interactions with the cytoskeleton of mammalian cells
    • Smith, G.A.; Enquist, L.W. Break ins and break outs: Viral interactions with the cytoskeleton of mammalian cells. Annu. Rev. Cell Dev. Biol. 2002, 18, 135-161.
    • (2002) Annu. Rev. Cell Dev. Biol , vol.18 , pp. 135-161
    • Smith, G.A.1    Enquist, L.W.2
  • 140
    • 84863703068 scopus 로고    scopus 로고
    • The ubiquitin/proteasome system mediates entry and endosomal trafficking of kaposi's sarcoma-associated herpesvirus in endothelial cells
    • Greene, W.; Zhang, W.; He, M.; Witt, C.; Ye, F.; Gao, S.J. The ubiquitin/proteasome system mediates entry and endosomal trafficking of kaposi's sarcoma-associated herpesvirus in endothelial cells. PLoS Pathog. 2012, 8, e1002703.
    • (2012) PLoS Pathog , vol.8
    • Greene, W.1    Zhang, W.2    He, M.3    Witt, C.4    Ye, F.5    Gao, S.J.6
  • 141
    • 84862955208 scopus 로고    scopus 로고
    • Microtubule- and dynein-dependent nuclear trafficking of rhesus rhadinovirus in rhesus fibroblasts
    • Zhang, W.; Greene, W.; Gao, S.J. Microtubule- and dynein-dependent nuclear trafficking of rhesus rhadinovirus in rhesus fibroblasts. J. Virol. 2012, 86, 599-604.
    • (2012) J. Virol , vol.86 , pp. 599-604
    • Zhang, W.1    Greene, W.2    Gao, S.J.3
  • 142
    • 0033052332 scopus 로고    scopus 로고
    • Inhibition of clathrin-coated pit assembly by an eps15 mutant
    • Benmerah, A.; Bayrou, M.; Cerf-Bensussan, N.; Dautry-Varsat, A. Inhibition of clathrin-coated pit assembly by an eps15 mutant. J. Cell Sci. 1999, 112 (Pt 9), 1303-1311.
    • (1999) J. Cell Sci , vol.112 , Issue.9 , pp. 1303-1311
    • Benmerah, A.1    Bayrou, M.2    Cerf-Bensussan, N.3    Dautry-Varsat, A.4
  • 144
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via rhoa-gtp-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt, P.P.; Krishnan, H.H.; Smith, M.S.; Chandran, B. Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via rhoa-gtp-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J. Virol. 2005, 79, 1191-1206.
    • (2005) J. Virol , vol.79 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 145
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J.K.; Echeverri, C.J.; Nilsson, T.; Vallee, R.B. Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 1997, 139, 469-484.
    • (1997) J. Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 146
    • 80051887181 scopus 로고    scopus 로고
    • Drifting motions of the adenovirus receptor car and immobile integrins initiate virus uncoating and membrane lytic protein exposure
    • Burckhardt, C.J.; Suomalainen, M.; Schoenenberger, P.; Boucke, K.; Hemmi, S.; Greber, U.F. Drifting motions of the adenovirus receptor car and immobile integrins initiate virus uncoating and membrane lytic protein exposure. Cell Host Microbe 2011, 10, 105-117.
    • (2011) Cell Host Microbe , vol.10 , pp. 105-117
    • Burckhardt, C.J.1    Suomalainen, M.2    Schoenenberger, P.3    Boucke, K.4    Hemmi, S.5    Greber, U.F.6
  • 147
    • 33644775671 scopus 로고    scopus 로고
    • Myosin ii functions in actin-bundle turnover in neuronal growth cones
    • Medeiros, N.A.; Burnette, D.T.; Forscher, P. Myosin ii functions in actin-bundle turnover in neuronal growth cones. Nat. Cell Biol. 2006, 8, 215-226.
    • (2006) Nat. Cell Biol , vol.8 , pp. 215-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 148
    • 22944446447 scopus 로고    scopus 로고
    • Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells
    • Lehmann, M.J.; Sherer, N.M.; Marks, C.B.; Pypaert, M.; Mothes, W. Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells. J. Cell Biol. 2005, 170, 317-325.
    • (2005) J. Cell Biol , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3    Pypaert, M.4    Mothes, W.5
  • 151
    • 70349275248 scopus 로고    scopus 로고
    • Impact of rac1 and cdc42 signaling during early herpes simplex virus type 1 infection of keratinocytes
    • Petermann, P.; Haase, I.; Knebel-Morsdorf, D. Impact of rac1 and cdc42 signaling during early herpes simplex virus type 1 infection of keratinocytes. J. Virol. 2009, 83, 9759-9772.
    • (2009) J. Virol , vol.83 , pp. 9759-9772
    • Petermann, P.1    Haase, I.2    Knebel-Morsdorf, D.3
  • 152
    • 33751414583 scopus 로고    scopus 로고
    • Early herpes simplex virus type 1 infection is dependent on regulated rac1/cdc42 signalling in epithelial mdckii cells
    • Hoppe, S.; Schelhaas, M.; Jaeger, V.; Liebig, T.; Petermann, P.; Knebel-Morsdorf, D. Early herpes simplex virus type 1 infection is dependent on regulated rac1/cdc42 signalling in epithelial mdckii cells. J. Gen. Virol. 2006, 87, 3483-3494.
    • (2006) J. Gen. Virol , vol.87 , pp. 3483-3494
    • Hoppe, S.1    Schelhaas, M.2    Jaeger, V.3    Liebig, T.4    Petermann, P.5    Knebel-Morsdorf, D.6
  • 153
    • 0026100907 scopus 로고
    • Penetration of cells by herpes simplex virus does not require a low ph-dependent endocytic pathway
    • Wittels, M.; Spear, P.G. Penetration of cells by herpes simplex virus does not require a low ph-dependent endocytic pathway. Virus Res. 1991, 18, 271-290.
    • (1991) Virus Res , vol.18 , pp. 271-290
    • Wittels, M.1    Spear, P.G.2
  • 154
    • 84855980522 scopus 로고    scopus 로고
    • Important but differential roles for actin in trafficking of epstein-barr virus in b cells and epithelial cells
    • Valencia, S.M.; Hutt-Fletcher, L.M. Important but differential roles for actin in trafficking of epstein-barr virus in b cells and epithelial cells. J. Virol. 2012, 86, 2-10.
    • (2012) J. Virol , vol.86 , pp. 2-10
    • Valencia, S.M.1    Hutt-Fletcher, L.M.2
  • 155
    • 0022762880 scopus 로고
    • Cytoskeletal disruption during human cytomegalovirus infection of human lung fibroblasts
    • Jones, N.L.; Lewis, J.C.; Kilpatrick, B.A. Cytoskeletal disruption during human cytomegalovirus infection of human lung fibroblasts. Eur. J. Cell Biol. 1986, 41, 304-312.
    • (1986) Eur. J. Cell Biol , vol.41 , pp. 304-312
    • Jones, N.L.1    Lewis, J.C.2    Kilpatrick, B.A.3
  • 156
    • 31144442190 scopus 로고    scopus 로고
    • Focal adhesion kinase is critical for entry of kaposi's sarcoma-associated herpesvirus into target cells
    • Krishnan, H.H.; Sharma-Walia, N.; Streblow, D.N.; Naranatt, P.P.; Chandran, B. Focal adhesion kinase is critical for entry of kaposi's sarcoma-associated herpesvirus into target cells. J. Virol. 2006, 80, 1167-1180.
    • (2006) J. Virol , vol.80 , pp. 1167-1180
    • Krishnan, H.H.1    Sharma-Walia, N.2    Streblow, D.N.3    Naranatt, P.P.4    Chandran, B.5
  • 157
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M.; Burridge, K. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 1996, 133, 1403-1415.
    • (1996) J. Cell Biol , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 158
    • 0037225685 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus induces the phosphatidylinositol 3-kinase-pkc-zeta-mek-erk signaling pathway in target cells early during infection: Implications for infectivity
    • Naranatt, P.P.; Akula, S.M.; Zien, C.A.; Krishnan, H.H.; Chandran, B. Kaposi's sarcoma-associated herpesvirus induces the phosphatidylinositol 3-kinase-pkc-zeta-mek-erk signaling pathway in target cells early during infection: Implications for infectivity. J. Virol. 2003, 77, 1524-1539.
    • (2003) J. Virol , vol.77 , pp. 1524-1539
    • Naranatt, P.P.1    Akula, S.M.2    Zien, C.A.3    Krishnan, H.H.4    Chandran, B.5
  • 159
    • 1842536029 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 envelope glycoprotein gb induces the integrin-dependent focal adhesion kinase-src-phosphatidylinositol 3-kinase-rho gtpase signal pathways and cytoskeletal rearrangements
    • Sharma-Walia, N.; Naranatt, P.P.; Krishnan, H.H.; Zeng, L.; Chandran, B. Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 envelope glycoprotein gb induces the integrin-dependent focal adhesion kinase-src-phosphatidylinositol 3-kinase-rho gtpase signal pathways and cytoskeletal rearrangements. J. Virol. 2004, 78, 4207-4223.
    • (2004) J. Virol , vol.78 , pp. 4207-4223
    • Sharma-Walia, N.1    Naranatt, P.P.2    Krishnan, H.H.3    Zeng, L.4    Chandran, B.5
  • 160
    • 33751245144 scopus 로고    scopus 로고
    • Rhoa-gtpase facilitates entry of kaposi's sarcoma-associated herpesvirus into adherent target cells in a src-dependent manner
    • Veettil, M.V.; Sharma-Walia, N.; Sadagopan, S.; Raghu, H.; Sivakumar, R.; Naranatt, P.P.; Chandran, B. Rhoa-gtpase facilitates entry of kaposi's sarcoma-associated herpesvirus into adherent target cells in a src-dependent manner. J. Virol. 2006, 80, 11432-11446.
    • (2006) J. Virol , vol.80 , pp. 11432-11446
    • Veettil, M.V.1    Sharma-Walia, N.2    Sadagopan, S.3    Raghu, H.4    Sivakumar, R.5    Naranatt, P.P.6    Chandran, B.7
  • 161
    • 0033525759 scopus 로고    scopus 로고
    • Egf receptor signaling stimulates src kinase phosphorylation of clathrin, influencing clathrin redistribution and egf uptake
    • Wilde, A.; Beattie, E.C.; Lem, L.; Riethof, D.A.; Liu, S.H.; Mobley, W.C.; Soriano, P.; Brodsky, F.M. Egf receptor signaling stimulates src kinase phosphorylation of clathrin, influencing clathrin redistribution and egf uptake. Cell 1999, 96, 677-687.
    • (1999) Cell , vol.96 , pp. 677-687
    • Wilde, A.1    Beattie, E.C.2    Lem, L.3    Riethof, D.A.4    Liu, S.H.5    Mobley, W.C.6    Soriano, P.7    Brodsky, F.M.8
  • 163
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S.L. Clathrin-coated vesicle formation and protein sorting: An integrated process. Annu. Rev. Biochem. 1997, 66, 511-548.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 165
    • 12844265252 scopus 로고    scopus 로고
    • A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • Yarar, D.; Waterman-Storer, C.M.; Schmid, S.L. A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Mol. Biol. Cell 2005, 16, 964-975.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 964-975
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 166
  • 167
    • 78651237433 scopus 로고    scopus 로고
    • Interaction of c-cbl with myosin iia regulates bleb associated macropinocytosis of kaposi's sarcoma-associated herpesvirus
    • Valiya Veettil, M.; Sadagopan, S.; Kerur, N.; Chakraborty, S.; Chandran, B. Interaction of c-cbl with myosin iia regulates bleb associated macropinocytosis of kaposi's sarcoma-associated herpesvirus. PLoS Pathog. 2010, 6, e1001238.
    • (2010) PLoS Pathog , vol.6
    • Valiya Veettil, M.1    Sadagopan, S.2    Kerur, N.3    Chakraborty, S.4    Chandran, B.5
  • 168
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer, J.; Helenius, A. Virus entry by macropinocytosis. Nat. Cell Biol. 2009, 11, 510-520.
    • (2009) Nat. Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 169
    • 81255200343 scopus 로고    scopus 로고
    • C-cbl-mediated selective virus-receptor translocations into lipid rafts regulate productive kaposi's sarcoma-associated herpesvirus infection in endothelial cells
    • Chakraborty, S.; ValiyaVeettil, M.; Sadagopan, S.; Paudel, N.; Chandran, B. C-cbl-mediated selective virus-receptor translocations into lipid rafts regulate productive kaposi's sarcoma-associated herpesvirus infection in endothelial cells. J. Virol. 2011, 85, 12410-12430.
    • (2011) J. Virol , vol.85 , pp. 12410-12430
    • Chakraborty, S.1    Valiyaveettil, M.2    Sadagopan, S.3    Paudel, N.4    Chandran, B.5
  • 170
    • 79956299299 scopus 로고    scopus 로고
    • Receptor sorting within endosomal trafficking pathway is facilitated by dynamic actin filaments
    • Ohashi, E.; Tanabe, K.; Henmi, Y.; Mesaki, K.; Kobayashi, Y.; Takei, K. Receptor sorting within endosomal trafficking pathway is facilitated by dynamic actin filaments. PLoS One 2011, 6, e19942.
    • (2011) PLoS One , vol.6
    • Ohashi, E.1    Tanabe, K.2    Henmi, Y.3    Mesaki, K.4    Kobayashi, Y.5    Takei, K.6
  • 171
    • 79955828987 scopus 로고    scopus 로고
    • Molecular mechanisms of ubiquitin-dependent membrane traffic
    • Hurley, J.H.; Stenmark, H. Molecular mechanisms of ubiquitin-dependent membrane traffic. Annu. Rev. Biophys. 2011, 40, 119-142.
    • (2011) Annu. Rev. Biophys , vol.40 , pp. 119-142
    • Hurley, J.H.1    Stenmark, H.2
  • 172
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell. Biol. 2001, 2, 195-201.
    • (2001) Nat. Rev. Mol. Cell. Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 173
    • 33646747652 scopus 로고    scopus 로고
    • Modulation of Kaposi's sarcoma-associated herpesvirus infection and replication by mek/erk, jnk, and p38 multiple mitogen-activated protein kinase pathways during primary infection
    • Pan, H.; Xie, J.; Ye, F.; Gao, S.J. Modulation of Kaposi's sarcoma-associated herpesvirus infection and replication by mek/erk, jnk, and p38 multiple mitogen-activated protein kinase pathways during primary infection. J. Virol. 2006, 80, 5371-5382.
    • (2006) J. Virol , vol.80 , pp. 5371-5382
    • Pan, H.1    Xie, J.2    Ye, F.3    Gao, S.J.4
  • 174
    • 23244461927 scopus 로고    scopus 로고
    • Erk1/2 and mek1/2 induced by Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) early during infection of target cells are essential for expression of viral genes and for establishment of infection
    • Sharma-Walia, N.; Krishnan, H.H.; Naranatt, P.P.; Zeng, L.; Smith, M.S.; Chandran, B. Erk1/2 and mek1/2 induced by Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) early during infection of target cells are essential for expression of viral genes and for establishment of infection. J. Virol. 2005, 79, 10308-10329.
    • (2005) J. Virol , vol.79 , pp. 10308-10329
    • Sharma-Walia, N.1    Krishnan, H.H.2    Naranatt, P.P.3    Zeng, L.4    Smith, M.S.5    Chandran, B.6
  • 175
    • 29744457034 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus induction of ap-1 and interleukin 6 during primary infection mediated by multiple mitogen-activated protein kinase pathways
    • Xie, J.; Pan, H.; Yoo, S.; Gao, S.J. Kaposi's sarcoma-associated herpesvirus induction of ap-1 and interleukin 6 during primary infection mediated by multiple mitogen-activated protein kinase pathways. J. Virol. 2005, 79, 15027-15037.
    • (2005) J. Virol , vol.79 , pp. 15027-15037
    • Xie, J.1    Pan, H.2    Yoo, S.3    Gao, S.J.4
  • 176
    • 34250811336 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus infection promotes invasion of primary human umbilical vein endothelial cells by inducing matrix metalloproteinases
    • Qian, L.W.; Xie, J.; Ye, F.; Gao, S.J. Kaposi's sarcoma-associated herpesvirus infection promotes invasion of primary human umbilical vein endothelial cells by inducing matrix metalloproteinases. J. Virol. 2007, 81, 7001-7010.
    • (2007) J. Virol , vol.81 , pp. 7001-7010
    • Qian, L.W.1    Xie, J.2    Ye, F.3    Gao, S.J.4
  • 177
    • 34247117937 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus promotes angiogenesis by inducing angiopoietin-2 expression via ap-1 and ets1
    • Ye, F.C.; Blackbourn, D.J.; Mengel, M.; Xie, J.P.; Qian, L.W.; Greene, W.; Yeh, I.T.; Graham, D.; Gao, S.J. Kaposi's sarcoma-associated herpesvirus promotes angiogenesis by inducing angiopoietin-2 expression via ap-1 and ets1. J. Virol. 2007, 81, 3980-3991.
    • (2007) J. Virol , vol.81 , pp. 3980-3991
    • Ye, F.C.1    Blackbourn, D.J.2    Mengel, M.3    Xie, J.P.4    Qian, L.W.5    Greene, W.6    Yeh, I.T.7    Graham, D.8    Gao, S.J.9
  • 178
    • 56449122995 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus disrupts adherens junctions and increases endothelial permeability by inducing degradation of ve-cadherin
    • Qian, L.W.; Greene, W.; Ye, F.; Gao, S.J. Kaposi's sarcoma-associated herpesvirus disrupts adherens junctions and increases endothelial permeability by inducing degradation of ve-cadherin. J. Virol. 2008, 82, 11902-11912.
    • (2008) J. Virol , vol.82 , pp. 11902-11912
    • Qian, L.W.1    Greene, W.2    Ye, F.3    Gao, S.J.4
  • 179
    • 0036632634 scopus 로고    scopus 로고
    • Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry
    • Yoon, M.; Spear, P.G. Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry. J. Virol. 2002, 76, 7203-7208.
    • (2002) J. Virol , vol.76 , pp. 7203-7208
    • Yoon, M.1    Spear, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.