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Volumn 3, Issue 7, 2011, Pages 1015-1040

Herpesviruses and intermediate filaments: Close encounters with the third type

Author keywords

Cytomegalovirus; Cytoskeleton; Epstein barr virus; Herpes simplex virus; Herpesvirus; Infection; Intermediate filament; Kaposi's sarcoma associated herpesvirus; Varicella zoster virus

Indexed keywords

ALPHA INTERNEXIN; DESMIN; FILENSIN; GLIAL FIBRILLARY ACIDIC PROTEIN; INTERMEDIATE FILAMENT PROTEIN; KERATIN; LAMIN A; LAMIN B; LAMIN B1; LAMIN B2; LAMIN C; LAMIN C1; LAMIN C2; NESTIN; NEUROFILAMENT H PROTEIN; NEUROFILAMENT L PROTEIN; NEUROFILAMENT M PROTEIN; NEUROFILAMENT PROTEIN; PERIPHERIN; PHAKININ; SYNCOILIN; SYNEMIN ALPHA; SYNEMIN BETA; UNCLASSIFIED DRUG; VIMENTIN;

EID: 79960782143     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v3071015     Document Type: Review
Times cited : (16)

References (203)
  • 1
    • 68849114844 scopus 로고    scopus 로고
    • Dysfunctions of neuronal and glial intermediate filaments in disease
    • Liem, R.K.; Messing, A. Dysfunctions of neuronal and glial intermediate filaments in disease. J. Clin. Invest. 2009, 119, 1814-1824.
    • (2009) J. Clin. Invest , vol.119 , pp. 1814-1824
    • Liem, R.K.1    Messing, A.2
  • 3
    • 68849112456 scopus 로고    scopus 로고
    • Intermediate filaments: Primary determinants of cell architecture and plasticity
    • Herrmann, H.; Strelkov, S.V.; Burkhard, P.; Aebi, U. Intermediate filaments: Primary determinants of cell architecture and plasticity. J. Clin. Invest. 2009, 119, 1772-1783.
    • (2009) J. Clin. Invest , vol.119 , pp. 1772-1783
    • Herrmann, H.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4
  • 4
    • 68849106856 scopus 로고    scopus 로고
    • IF-pathies: A broad spectrum of intermediate filament-associated diseases
    • Omary, M.B. IF-pathies: A broad spectrum of intermediate filament-associated diseases. J. Clin. Invest. 2009, 119, 1756-1762.
    • (2009) J. Clin. Invest , vol.119 , pp. 1756-1762
    • Omary, M.B.1
  • 5
  • 7
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm
    • Kim, S.; Coulombe, P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 2007, 21, 1581-1597.
    • (2007) Genes Dev , vol.21 , pp. 1581-1597
    • Kim, S.1    Coulombe, P.A.2
  • 8
    • 37849013303 scopus 로고    scopus 로고
    • Intermediate filament assembly: Dynamics to disease
    • Godsel, L.M.; Hobbs, R.P.; Green, K.J. Intermediate filament assembly: Dynamics to disease. Trends Cell Biol. 2008, 18, 28-37.
    • (2008) Trends Cell Biol , vol.18 , pp. 28-37
    • Godsel, L.M.1    Hobbs, R.P.2    Green, K.J.3
  • 9
    • 0034687247 scopus 로고    scopus 로고
    • Cellular regulation of actin network assembly
    • Amann, K.J.; Pollard, T.D. Cellular regulation of actin network assembly. Curr. Biol. 2000, 10, R728-R730.
    • (2000) Curr. Biol , vol.10
    • Amann, K.J.1    Pollard, T.D.2
  • 10
    • 0019782697 scopus 로고
    • Microtubule treadmills-Possible molecular machinery
    • Margolis, R.L.; Wilson, L. Microtubule treadmills-Possible molecular machinery. Nature 1981, 293, 705-711.
    • (1981) Nature , vol.293 , pp. 705-711
    • Margolis, R.L.1    Wilson, L.2
  • 11
    • 0037335755 scopus 로고    scopus 로고
    • 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    Aebi, U.3
  • 13
    • 33745873555 scopus 로고    scopus 로고
    • Heads and tails of intermediate filament phosphorylation: Multiple sites and functional insights
    • Omary, M.B.; Ku, N.O.; Tao, G.Z.; Toivola, D.M.; Liao, J. Heads and tails of intermediate filament phosphorylation: Multiple sites and functional insights. Trends Biochem. Sci. 2006, 31, 383-394.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 383-394
    • Omary, M.B.1    Ku, N.O.2    Tao, G.Z.3    Toivola, D.M.4    Liao, J.5
  • 15
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds
    • Herrmann, H.; Aebi, U. Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu. Rev. Biochem. 2004, 73, 749-789.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 17
    • 0032487522 scopus 로고    scopus 로고
    • Rapid movements of vimentin on microtubule tracks: Kinesin-dependent assembly of intermediate filament networks
    • Prahlad, V.; Yoon, M.; Moir, R.D.; Vale, R.D.; Goldman, R.D. Rapid movements of vimentin on microtubule tracks: Kinesin-dependent assembly of intermediate filament networks. J. Cell Biol. 1998, 143, 159-170.
    • (1998) J. Cell Biol , vol.143 , pp. 159-170
    • Prahlad, V.1    Yoon, M.2    Moir, R.D.3    Vale, R.D.4    Goldman, R.D.5
  • 18
    • 0032949408 scopus 로고    scopus 로고
    • Intermediate filaments in motion: Observations of intermediate filaments in cells using green fluorescent protein-vimentin
    • Martys, J.L.; Ho, C.L.; Liem, R.K.; Gundersen, G.G. Intermediate filaments in motion: Observations of intermediate filaments in cells using green fluorescent protein-vimentin. Mol. Biol. Cell 1999, 10, 1289-1295.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1289-1295
    • Martys, J.L.1    Ho, C.L.2    Liem, R.K.3    Gundersen, G.G.4
  • 19
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • Yabe, J.T.; Pimenta, A.; Shea, T.B. Kinesin-mediated transport of neurofilament protein oligomers in growing axons. J. Cell Sci. 1999, 112, 3799-3814.
    • (1999) J. Cell Sci , vol.112 , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3
  • 20
    • 33646257802 scopus 로고    scopus 로고
    • Dynein mediates retrograde neurofilament transport within axons and anterograde delivery of NFs from perikarya into axons: Regulation by multiple phosphorylation events
    • Motil, J.; Chan, W.K.; Dubey, M.; Chaudhury, P.; Pimenta, A.; Chylinski, T.M.; Ortiz, D.T.; Shea, T.B. Dynein mediates retrograde neurofilament transport within axons and anterograde delivery of NFs from perikarya into axons: Regulation by multiple phosphorylation events. Cell Motil. Cytoskeleton 2006, 63, 266-286.
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 266-286
    • Motil, J.1    Chan, W.K.2    Dubey, M.3    Chaudhury, P.4    Pimenta, A.5    Chylinski, T.M.6    Ortiz, D.T.7    Shea, T.B.8
  • 21
    • 0033783031 scopus 로고    scopus 로고
    • Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin
    • Shah, J.V.; Flanagan, L.A.; Janmey, P.A.; Leterrier, J.F. Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin. Mol. Biol. Cell 2000, 11, 3495-3508.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3495-3508
    • Shah, J.V.1    Flanagan, L.A.2    Janmey, P.A.3    Leterrier, J.F.4
  • 22
    • 0038010428 scopus 로고    scopus 로고
    • Rapid transport of neural intermediate filament protein
    • Helfand, B.T.; Loomis, P.; Yoon, M.; Goldman, R.D. Rapid transport of neural intermediate filament protein. J. Cell Sci. 2003, 116, 2345-2359.
    • (2003) J. Cell Sci , vol.116 , pp. 2345-2359
    • Helfand, B.T.1    Loomis, P.2    Yoon, M.3    Goldman, R.D.4
  • 23
    • 0015181351 scopus 로고
    • The role of three cytoplasmic fibers in BHK-21 cell motility. I. Microtubules and the effects of colchicine
    • Goldman, R.D. The role of three cytoplasmic fibers in BHK-21 cell motility. I. Microtubules and the effects of colchicine. J. Cell Biol. 1971, 51, 752-762.
    • (1971) J. Cell Biol , vol.51 , pp. 752-762
    • Goldman, R.D.1
  • 24
    • 1842381834 scopus 로고
    • Different intermediate-sized filaments distinguished by immunofluorescence microscopy
    • Franke, W.W.; Schmid, E.; Osborn, M.; Weber, K. Different intermediate-sized filaments distinguished by immunofluorescence microscopy. Proc. Natl. Acad. Sci. U. S. A. 1978, 75, 5034-5038.
    • (1978) Proc. Natl. Acad. Sci. U. S. A , vol.75 , pp. 5034-5038
    • Franke, W.W.1    Schmid, E.2    Osborn, M.3    Weber, K.4
  • 25
    • 0025142635 scopus 로고
    • Cytoskeletal dynamics in rabbit synovial fibroblasts: I. Effects of acrylamide on intermediate filaments and microfilaments
    • Aggeler, J.; Seely, K. Cytoskeletal dynamics in rabbit synovial fibroblasts: I. Effects of acrylamide on intermediate filaments and microfilaments. Cell Motil. Cytoskeleton 1990, 16, 110-120.
    • (1990) Cell Motil. Cytoskeleton , vol.16 , pp. 110-120
    • Aggeler, J.1    Seely, K.2
  • 26
    • 0019885815 scopus 로고
    • Intermediate filaments in 3T3 cells collapse after intracellular injection of a monoclonal anti-intermediate filament antibody
    • Klymkowsky, M.W. Intermediate filaments in 3T3 cells collapse after intracellular injection of a monoclonal anti-intermediate filament antibody. Nature 1981, 291, 249-251.
    • (1981) Nature , vol.291 , pp. 249-251
    • Klymkowsky, M.W.1
  • 27
    • 0019436188 scopus 로고
    • Disruption of the in vivo distribution of the intermediate filaments in fibroblasts through the microinjection of a specific monoclonal antibody
    • Lin, J.J.; Feramisco, J.R. Disruption of the in vivo distribution of the intermediate filaments in fibroblasts through the microinjection of a specific monoclonal antibody. Cell 1981, 24, 185-193.
    • (1981) Cell , vol.24 , pp. 185-193
    • Lin, J.J.1    Feramisco, J.R.2
  • 28
    • 0019804382 scopus 로고
    • Coiling of intermediate filaments induced by microinjection of a vimentin-specific antibody does not interfere with locomotion and mitosis
    • Gawlitta, W.; Osborn, M.; Weber, K. Coiling of intermediate filaments induced by microinjection of a vimentin-specific antibody does not interfere with locomotion and mitosis. Eur. J. Cell Biol. 1981, 26, 83-90.
    • (1981) Eur. J. Cell Biol , vol.26 , pp. 83-90
    • Gawlitta, W.1    Osborn, M.2    Weber, K.3
  • 29
    • 27744556965 scopus 로고    scopus 로고
    • Cellular integrity plus: Organelle-related and protein-targeting functions of intermediate filaments
    • Toivola, D.M.; Tao, G.Z.; Habtezion, A.; Liao, J.; Omary, M.B. Cellular integrity plus: Organelle-related and protein-targeting functions of intermediate filaments. Trends Cell Biol. 2005, 15, 608-617.
    • (2005) Trends Cell Biol , vol.15 , pp. 608-617
    • Toivola, D.M.1    Tao, G.Z.2    Habtezion, A.3    Liao, J.4    Omary, M.B.5
  • 30
    • 34248182865 scopus 로고    scopus 로고
    • Intermediate filaments as signaling platforms
    • Pallari, H.M.; Eriksson, J.E. Intermediate filaments as signaling platforms. Sci. STKE 2006, 2006, p e53.
    • (2006) Sci. STKE 2006
    • Pallari, H.M.1    Eriksson, J.E.2
  • 31
    • 0028361169 scopus 로고
    • The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW-13 cells
    • Sarria, A.J.; Lieber, J.G.; Nordeen, S.K.; Evans, R.M. The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW-13 cells. J. Cell Sci. 1994, 107, 1593-1607.
    • (1994) J. Cell Sci , vol.107 , pp. 1593-1607
    • Sarria, A.J.1    Lieber, J.G.2    Nordeen, S.K.3    Evans, R.M.4
  • 34
    • 84929285686 scopus 로고    scopus 로고
    • Comparative virion structures of human herpesviruses
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press: Cambridge, UK
    • Liu, F.; Hong Zhou, Z. Comparative virion structures of human 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 University Press: Cambridge, UK, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy and Immunoprophylaxis
    • Liu, F.1    Hong Zhou, Z.2
  • 35
    • 27744524532 scopus 로고    scopus 로고
    • Herpes simplex virus and varicella-zoster virus: Why do these human alphaherpesviruses behave so differently from one another?
    • Mori, I.; Nishiyama, Y. Herpes simplex virus and varicella-zoster virus: Why do these human alphaherpesviruses behave so differently from one another? Rev. Med. Virol. 2005, 15, 393-406.
    • (2005) Rev. Med. Virol , vol.15 , pp. 393-406
    • Mori, I.1    Nishiyama, Y.2
  • 36
    • 84929292550 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses into the cell
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press: Cambridge, UK
    • Campadelli-Fiume, G.; Menotti, L. Entry of alphaherpesviruses into the cell. 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 University Press: Cambridge, UK, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy and Immunoprophylaxis
    • Campadelli-Fiume, G.1    Menotti, L.2
  • 39
    • 0028907911 scopus 로고
    • Fibroblasts, epithelial cells, endothelial cells and smooth muscle cells are major targets of human cytomegalovirus infection in lung and gastrointestinal tissues
    • Sinzger, C.; Grefte, A.; Plachter, B.; Gouw, A.S.; The, T.H.; Jahn, G. Fibroblasts, epithelial cells, endothelial cells and smooth muscle cells are major targets of human cytomegalovirus infection in lung and gastrointestinal tissues. J. Gen. Virol. 1995, 76, 741-750.
    • (1995) J. Gen. Virol , vol.76 , pp. 741-750
    • Sinzger, C.1    Grefte, A.2    Plachter, B.3    Gouw, A.S.4    The, T.H.5    Jahn, G.6
  • 40
    • 0036252650 scopus 로고    scopus 로고
    • Human cytomegalovirus as a direct pathogen: Correlation of multiorgan involvement and cell distribution with clinical and pathological findings in a case of congenital inclusion disease
    • Bissinger, A.L.; Sinzger, C.; Kaiserling, E.; Jahn, G. Human cytomegalovirus as a direct pathogen: correlation of multiorgan involvement and cell distribution with clinical and pathological findings in a case of congenital inclusion disease. J. Med. Virol. 2002, 67, 200-206.
    • (2002) J. Med. Virol , vol.67 , pp. 200-206
    • Bissinger, A.L.1    Sinzger, C.2    Kaiserling, E.3    Jahn, G.4
  • 41
    • 65349092347 scopus 로고    scopus 로고
    • Dendritic cells in cytomegalovirus infection: Viral evasion and host countermeasures
    • Rolle, A.; Olweus, J. Dendritic cells in cytomegalovirus infection: Viral evasion and host countermeasures. Apmis 2009, 117, 413-426.
    • (2009) Apmis , vol.117 , pp. 413-426
    • Rolle, A.1    Olweus, J.2
  • 42
    • 57049147613 scopus 로고    scopus 로고
    • Manipulation of dendritic cell functions by human cytomegalovirus
    • Sinclair, J. Manipulation of dendritic cell functions by human cytomegalovirus. Expert Rev. Mol. Med. 2008, 10, e35.
    • (2008) Expert Rev. Mol. Med , vol.10
    • Sinclair, J.1
  • 44
    • 72949114077 scopus 로고    scopus 로고
    • Endothelial cells in human cytomegalovirus infection: One host cell out of many or a crucial target for virus spread?
    • Adler, B.; Sinzger, C. Endothelial cells in human cytomegalovirus infection: One host cell out of many or a crucial target for virus spread? Thromb. Haemost. 2009, 102, 1057-1063.
    • (2009) Thromb. Haemost , vol.102 , pp. 1057-1063
    • Adler, B.1    Sinzger, C.2
  • 45
  • 46
    • 39149113788 scopus 로고    scopus 로고
    • Human cytomegalovirus: Latency and reactivation in the myeloid lineage
    • Sinclair, J. Human cytomegalovirus: Latency and reactivation in the myeloid lineage. J. Clin. Virol. 2008, 41, 180-185.
    • (2008) J. Clin. Virol , vol.41 , pp. 180-185
    • Sinclair, J.1
  • 47
    • 12844286068 scopus 로고    scopus 로고
    • Update on human herpesvirus 6 biology, clinical features, and therapy
    • De Bolle, L.; Naesens, L.; de Clercq, E. Update on human herpesvirus 6 biology, clinical features, and therapy. Clin. Microbiol. Rev. 2005, 18, 217-245.
    • (2005) Clin. Microbiol. Rev , vol.18 , pp. 217-245
    • de Bolle, L.1    Naesens, L.2    de Clercq, E.3
  • 48
    • 66749103177 scopus 로고    scopus 로고
    • Recent topics related to human herpesvirus 6 cell tropism
    • Mori, Y. Recent topics related to human herpesvirus 6 cell tropism. Cell. Microbiol. 2009, 11, 1001-1006.
    • (2009) Cell. Microbiol , vol.11 , pp. 1001-1006
    • Mori, Y.1
  • 49
    • 84890663904 scopus 로고    scopus 로고
    • HHV-6A, 6B, and 7: Immunobiology and host response
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press: Cambridge, UK
    • Wang, F.-Z.; Pellett, P.E. HHV-6A, 6B, and 7: Immunobiology and host response. 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 University Press: Cambridge, UK, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy and Immunoprophylaxis
    • Wang, F.-Z.1    Pellett, P.E.2
  • 50
    • 35348962397 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus
    • 5th ed.; Knipe, D., Howley, P., Griffin, D., Lamb, R., Martin, M., Roizman, B., Straus, S., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA
    • Ganem, D. Kaposi's sarcoma-associated herpesvirus. In Fields Virology, 5th ed.; Knipe, D., Howley, P., Griffin, D., Lamb, R., Martin, M., Roizman, B., Straus, S., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA, 2007; pp. 2875-2888.
    • (2007) Fields Virology , pp. 2875-2888
    • Ganem, D.1
  • 51
    • 79960792025 scopus 로고    scopus 로고
    • Gammaherpesviruses entry and early events during infection
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press: Cambridge, UK
    • Chandran, B.; Hutt-Fletcher, L. Gammaherpesviruses entry and early events during infection. 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 University Press: Cambridge, UK, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy and Immunoprophylaxis
    • Chandran, B.1    Hutt-Fletcher, L.2
  • 52
    • 84929272699 scopus 로고    scopus 로고
    • Comparative analysis of herpesvirus-common proteins
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press: Cambridge, UK
    • Mocarski, E.S. Comparative analysis of herpesvirus-common proteins. 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 University Press: Cambridge, UK, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy and Immunoprophylaxis
    • Mocarski, E.S.1
  • 54
    • 0036776337 scopus 로고    scopus 로고
    • Intact microtubules support adenovirus and herpes simplex virus infections
    • Mabit, H.; Nakano, M.Y.; Prank, U.; Saam, B.; Dohner, K.; Sodeik, B.; Greber, U.F. Intact microtubules support adenovirus and herpes simplex virus infections. J. Virol. 2002, 76, 9962-9971.
    • (2002) J. Virol , vol.76 , pp. 9962-9971
    • Mabit, H.1    Nakano, M.Y.2    Prank, U.3    Saam, B.4    Dohner, K.5    Sodeik, B.6    Greber, U.F.7
  • 55
    • 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
  • 56
    • 0017123619 scopus 로고
    • Keratinization of the oral epithelium
    • Adams, D. Keratinization of the oral epithelium. Ann. R. Coll. Surg. Engl. 1976, 58, 351-358.
    • (1976) Ann. R. Coll. Surg. Engl , vol.58 , pp. 351-358
    • Adams, D.1
  • 59
    • 35649005443 scopus 로고    scopus 로고
    • The surface protein Srr-1 of Streptococcus agalactiae binds human keratin 4 and promotes adherence to epithelial HEp-2 cells
    • Samen, U.; Eikmanns, B.J.; Reinscheid, D.J.; Borges, F. The surface protein Srr-1 of Streptococcus agalactiae binds human keratin 4 and promotes adherence to epithelial HEp-2 cells. Infect. Immun. 2007, 75, 5405-5414.
    • (2007) Infect. Immun , vol.75 , pp. 5405-5414
    • Samen, U.1    Eikmanns, B.J.2    Reinscheid, D.J.3    Borges, F.4
  • 60
    • 0037040012 scopus 로고    scopus 로고
    • Identification of cytokeratins as accessory mediators of Salmonella entry into eukaryotic cells
    • Carlson, S.A.; Omary, M.B.; Jones, B.D. Identification of cytokeratins as accessory mediators of Salmonella entry into eukaryotic cells. Life Sci. 2002, 70, 1415-1426.
    • (2002) Life Sci , vol.70 , pp. 1415-1426
    • Carlson, S.A.1    Omary, M.B.2    Jones, B.D.3
  • 61
    • 0034019163 scopus 로고    scopus 로고
    • Group B streptococci and other gram-positive cocci bind to cytokeratin 8
    • Tamura, G.S.; Nittayajarn, A. Group B streptococci and other gram-positive cocci bind to cytokeratin 8. Infect. Immun. 2000, 68, 2129-2134.
    • (2000) Infect. Immun , vol.68 , pp. 2129-2134
    • Tamura, G.S.1    Nittayajarn, A.2
  • 62
    • 30344482571 scopus 로고    scopus 로고
    • Defining the cellular target(s) of porcine reproductive and respiratory syndrome virus blocking monoclonal antibody 7G10
    • Kim, J.K.; Fahad, A.M.; Shanmukhappa, K.; Kapil, S. Defining the cellular target(s) of porcine reproductive and respiratory syndrome virus blocking monoclonal antibody 7G10. J. Virol. 2006, 80, 689-696.
    • (2006) J. Virol , vol.80 , pp. 689-696
    • Kim, J.K.1    Fahad, A.M.2    Shanmukhappa, K.3    Kapil, S.4
  • 63
    • 0029991762 scopus 로고    scopus 로고
    • Anti-idiotypic antibody to the V3 domain of gp120 binds to vimentin: A possible role of intermediate filaments in the early steps of HIV-1 infection cycle
    • Thomas, E.K.; Connelly, R.J.; Pennathur, S.; Dubrovsky, L.; Haffar, O.K.; Bukrinsky, M.I. Anti-idiotypic antibody to the V3 domain of gp120 binds to vimentin: A possible role of intermediate filaments in the early steps of HIV-1 infection cycle. Viral. Immunol. 1996, 9, 73-87.
    • (1996) Viral. Immunol , vol.9 , pp. 73-87
    • Thomas, E.K.1    Connelly, R.J.2    Pennathur, S.3    Dubrovsky, L.4    Haffar, O.K.5    Bukrinsky, M.I.6
  • 65
    • 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
  • 66
    • 0021323966 scopus 로고
    • Pathogenesis of herpes simplex labialis: Excretion of virus in the oral cavity
    • Spruance, S.L. Pathogenesis of herpes simplex labialis: Excretion of virus in the oral cavity. J. Clin. Microbiol. 1984, 19, 675-679.
    • (1984) J. Clin. Microbiol , vol.19 , pp. 675-679
    • Spruance, S.L.1
  • 67
    • 0030906208 scopus 로고    scopus 로고
    • Infection and replication of herpes simplex virus type 1 in an organotypic epithelial culture system
    • Visalli, R.J.; Courtney, R.J.; Meyers, C. Infection and replication of herpes simplex virus type 1 in an organotypic epithelial culture system. Virology 1997, 230, 236-243.
    • (1997) Virology , vol.230 , pp. 236-243
    • Visalli, R.J.1    Courtney, R.J.2    Meyers, C.3
  • 68
    • 30344435010 scopus 로고    scopus 로고
    • Human cytomegalovirus entry into epithelial and endothelial cells depends on genes UL128 to UL150 and occurs by endocytosis and low-pH fusion
    • Ryckman, B.J.; Jarvis, M.A.; Drummond, D.D.; Nelson, J.A.; Johnson, D.C. Human cytomegalovirus entry into epithelial and endothelial cells depends on genes UL128 to UL150 and occurs by endocytosis and low-pH fusion. J. Virol. 2006, 80, 710-722.
    • (2006) J. Virol , vol.80 , pp. 710-722
    • Ryckman, B.J.1    Jarvis, M.A.2    Drummond, D.D.3    Nelson, J.A.4    Johnson, D.C.5
  • 69
    • 37349028312 scopus 로고    scopus 로고
    • Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that mediates entry into epithelial and endothelial cells
    • Ryckman, B.J.; Rainish, B.L.; Chase, M.C.; Borton, J.A.; Nelson, J.A.; Jarvis, M.A.; Johnson, D.C. Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that mediates entry into epithelial and endothelial cells. J. Virol. 2008, 82, 60-70.
    • (2008) J. Virol , vol.82 , pp. 60-70
    • Ryckman, B.J.1    Rainish, B.L.2    Chase, M.C.3    Borton, J.A.4    Nelson, J.A.5    Jarvis, M.A.6    Johnson, D.C.7
  • 70
    • 39149093012 scopus 로고    scopus 로고
    • Entry route of HCMV into endothelial cells
    • Sinzger, C. Entry route of HCMV into endothelial cells. J. Clin. Virol. 2008, 41, 174-179.
    • (2008) J. Clin. Virol , vol.41 , pp. 174-179
    • Sinzger, C.1
  • 71
    • 35148875988 scopus 로고    scopus 로고
    • Cytomegalovirus UL131-128 products promote gB conformational transition and gB-gH interaction during entry into endothelial cells
    • Patrone, M.; Secchi, M.; Bonaparte, E.; Milanesi, G.; Gallina, A. Cytomegalovirus UL131-128 products promote gB conformational transition and gB-gH interaction during entry into endothelial cells. J. Virol. 2007, 81, 11479-11488.
    • (2007) J. Virol , vol.81 , pp. 11479-11488
    • Patrone, M.1    Secchi, M.2    Bonaparte, E.3    Milanesi, G.4    Gallina, A.5
  • 72
    • 29144522907 scopus 로고    scopus 로고
    • Human cytomegalovirus virion protein complex required for epithelial and endothelial cell tropism
    • Wang, D.; Shenk, T. Human cytomegalovirus virion protein complex required for epithelial and endothelial cell tropism. Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 18153-18158.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 18153-18158
    • Wang, D.1    Shenk, T.2
  • 73
    • 23244466315 scopus 로고    scopus 로고
    • Human cytomegalovirus UL131 open reading frame is required for epithelial cell tropism
    • Wang, D.; Shenk, T. Human cytomegalovirus UL131 open reading frame is required for epithelial cell tropism. J. Virol. 2005, 79, 10330-10338.
    • (2005) J. Virol , vol.79 , pp. 10330-10338
    • Wang, D.1    Shenk, T.2
  • 74
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • Nicola, A.V.; McEvoy, A.M.; Straus, S.E. Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J. Virol. 2003, 77, 5324-5332.
    • (2003) J. Virol , vol.77 , pp. 5324-5332
    • Nicola, A.V.1    McEvoy, A.M.2    Straus, S.E.3
  • 75
    • 3142719117 scopus 로고    scopus 로고
    • Cellular and viral requirements for rapid endocytic entry of herpes simplex virus
    • Nicola, A.V.; Straus, S.E. Cellular and viral requirements for rapid endocytic entry of herpes simplex virus. J. Virol. 2004, 78, 7508-7517.
    • (2004) J. Virol , vol.78 , pp. 7508-7517
    • Nicola, A.V.1    Straus, S.E.2
  • 76
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway
    • Nicola, A.V.; Hou, J.; Major, E.O.; Straus, S.E. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J. Virol. 2005, 79, 7609-7616.
    • (2005) J. Virol , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3    Straus, S.E.4
  • 77
    • 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
  • 78
    • 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
  • 80
    • 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
  • 81
    • 0020315826 scopus 로고
    • Actin distribution and synthesis in human fibroblasts infected by cytomegalovirus
    • Losse, D.; Lauer, R.; Weder, D.; Radsak, K. Actin distribution and synthesis in human fibroblasts infected by cytomegalovirus. Arch. Virol. 1982, 71, 353-359.
    • (1982) Arch. Virol , vol.71 , pp. 353-359
    • Losse, D.1    Lauer, R.2    Weder, D.3    Radsak, K.4
  • 82
    • 77953315624 scopus 로고    scopus 로고
    • RASCAL is a new human cytomegalovirus-encoded protein that localizes to the nuclear lamina and in cytoplasmic vesicles at late times postinfection
    • Miller, M.S.; Furlong, W.E.; Pennell, L.; Geadah, M.; Hertel, L. RASCAL is a new human cytomegalovirus-encoded protein that localizes to the nuclear lamina and in cytoplasmic vesicles at late times postinfection. J. Virol. 2010, 84, 6483-6496.
    • (2010) J. Virol , vol.84 , pp. 6483-6496
    • Miller, M.S.1    Furlong, W.E.2    Pennell, L.3    Geadah, M.4    Hertel, L.5
  • 83
    • 67650424329 scopus 로고    scopus 로고
    • Onset of human cytomegalovirus replication in fibroblasts requires the presence of an intact vimentin cytoskeleton
    • Miller, M.S.; Hertel, L. Onset of human cytomegalovirus replication in fibroblasts requires the presence of an intact vimentin cytoskeleton. J. Virol. 2009, 83, 7015-7028.
    • (2009) J. Virol , vol.83 , pp. 7015-7028
    • Miller, M.S.1    Hertel, L.2
  • 84
    • 0022658383 scopus 로고
    • Organization of cytoskeleton elements during herpes simplex virus type 1 infection of human fibroblasts: An immunofluorescence study
    • Norrild, B.; Lehto, V.P.; Virtanen, I. Organization of cytoskeleton elements during herpes simplex virus type 1 infection of human fibroblasts: An immunofluorescence study. J. Gen. Virol. 1986, 67, 97-105.
    • (1986) J. Gen. Virol , vol.67 , pp. 97-105
    • Norrild, B.1    Lehto, V.P.2    Virtanen, I.3
  • 85
    • 0023097012 scopus 로고
    • Microtubules and intermediate filaments of herpes simplex virus infected cells
    • Dienes, H.P.; Hiller, G.; Muller, S.; Falke, D. Microtubules and intermediate filaments of herpes simplex virus infected cells. Arch. Virol. 1987, 94, 15-28.
    • (1987) Arch. Virol , vol.94 , pp. 15-28
    • Dienes, H.P.1    Hiller, G.2    Muller, S.3    Falke, D.4
  • 86
    • 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. 2008, 83, 2058-2066.
    • (2008) J. Virol , vol.83 , pp. 2058-2066
    • Lyman, M.G.1    Enquist, L.W.2
  • 87
    • 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
  • 88
    • 0032832371 scopus 로고    scopus 로고
    • Equine herpes virus type 1 (EHV-1) infection induces alterations in the cytoskeleton of vero cells but not apoptosis
    • Walter, I.; Nowotny, N. Equine herpes virus type 1 (EHV-1) infection induces alterations in the cytoskeleton of vero cells but not apoptosis. Arch. Virol. 1999, 144, 1827-1836.
    • (1999) Arch. Virol , vol.144 , pp. 1827-1836
    • Walter, I.1    Nowotny, N.2
  • 89
    • 20944433146 scopus 로고    scopus 로고
    • Varicella-zoster virus infection influences expression and organization of actin and alpha-tubulin but does not affect lamin A and vimentin
    • Kuhn, M.; Desloges, N.; Rahaus, M.; Wolff, M.H. Varicella-zoster virus infection influences expression and organization of actin and alpha-tubulin but does not affect lamin A and vimentin. Intervirology 2005, 48, 312-320.
    • (2005) Intervirology , vol.48 , pp. 312-320
    • Kuhn, M.1    Desloges, N.2    Rahaus, M.3    Wolff, M.H.4
  • 90
    • 0026787140 scopus 로고
    • Human cytomegalovirus penetrates host cells by pH-independent fusion at the cell surface
    • Compton, T.; Nepomuceno, R.R.; Nowlin, D.M. Human cytomegalovirus penetrates host cells by pH-independent fusion at the cell surface. Virology 1992, 191, 387-395.
    • (1992) Virology , vol.191 , pp. 387-395
    • Compton, T.1    Nepomuceno, R.R.2    Nowlin, D.M.3
  • 91
    • 34249682108 scopus 로고    scopus 로고
    • Novel functions of vimentin in cell adhesion, migration, and signaling
    • Ivaska, J.; Pallari, H.M.; Nevo, J.; Eriksson, J.E. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp. Cell Res. 2007, 313, 2050-2062.
    • (2007) Exp. Cell Res , vol.313 , pp. 2050-2062
    • Ivaska, J.1    Pallari, H.M.2    Nevo, J.3    Eriksson, J.E.4
  • 92
    • 27844444696 scopus 로고    scopus 로고
    • PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility
    • Ivaska, J.; Vuoriluoto, K.; Huovinen, T.; Izawa, I.; Inagaki, M.; Parker, P.J. PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility. EMBO J. 2005, 24, 3834-3845.
    • (2005) EMBO J , vol.24 , pp. 3834-3845
    • Ivaska, J.1    Vuoriluoto, K.2    Huovinen, T.3    Izawa, I.4    Inagaki, M.5    Parker, P.J.6
  • 93
    • 7444256550 scopus 로고    scopus 로고
    • Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain
    • Feire, A.L.; Koss, H.; Compton, T. Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain. Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 15470-15475.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 15470-15475
    • Feire, A.L.1    Koss, H.2    Compton, T.3
  • 94
    • 18844442068 scopus 로고    scopus 로고
    • Integrin alphavbeta3 is a coreceptor for human cytomegalovirus
    • Wang, X.; Huang, D.Y.; Huong, S.M.; Huang, E.S. Integrin alphavbeta3 is a coreceptor for human cytomegalovirus. Nat. Med. 2005, 11, 515-521.
    • (2005) Nat. Med , vol.11 , pp. 515-521
    • Wang, X.1    Huang, D.Y.2    Huong, S.M.3    Huang, E.S.4
  • 96
    • 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
  • 97
    • 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
  • 98
    • 73949091055 scopus 로고    scopus 로고
    • Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8
    • Chesnokova, L.S.; Nishimura, S.L.; Hutt-Fletcher, L.M. Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8. Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 20464-20469.
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 20464-20469
    • Chesnokova, L.S.1    Nishimura, S.L.2    Hutt-Fletcher, L.M.3
  • 99
    • 0020261964 scopus 로고
    • The intracellular movement of endocytic vesicles in cultured granulosa cells
    • Herman, B.; Albertini, D.F. The intracellular movement of endocytic vesicles in cultured granulosa cells. Cell Motil. 1982, 2, 583-597.
    • (1982) Cell Motil , vol.2 , pp. 583-597
    • Herman, B.1    Albertini, D.F.2
  • 101
    • 17444383492 scopus 로고    scopus 로고
    • Intermediate filaments and vesicular membrane traffic: The odd couple's first dance?
    • Styers, M.L.; Kowalczyk, A.P.; Faundez, V. Intermediate filaments and vesicular membrane traffic: the odd couple's first dance? Traffic 2005, 6, 359-365.
    • (2005) Traffic , vol.6 , pp. 359-365
    • Styers, M.L.1    Kowalczyk, A.P.2    Faundez, V.3
  • 102
    • 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
  • 103
    • 9444239263 scopus 로고    scopus 로고
    • The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton
    • Styers, M.L.; Salazar, G.; Love, R.; Peden, A.A.; Kowalczyk, A.P.; Faundez, V. The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton. Mol. Biol. Cell 2004, 15, 5369-5382.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5369-5382
    • Styers, M.L.1    Salazar, G.2    Love, R.3    Peden, A.A.4    Kowalczyk, A.P.5    Faundez, V.6
  • 104
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson, M.S. Adaptable adaptors for coated vesicles. Trends Cell Biol. 2004, 14, 167-174.
    • (2004) Trends Cell Biol , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 105
    • 0032126699 scopus 로고    scopus 로고
    • Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes, and synaptic vesicles
    • Kantheti, P.; Qiao, X.; Diaz, M.E.; Peden, A.A.; Meyer, G.E.; Carskadon, S.L.; Kapfhamer, D.; Sufalko, D.; Robinson, M.S.; Noebels, J.L., et al. Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes, and synaptic vesicles. Neuron 1998, 21, 111-122.
    • (1998) Neuron , vol.21 , pp. 111-122
    • Kantheti, P.1    Qiao, X.2    Diaz, M.E.3    Peden, A.A.4    Meyer, G.E.5    Carskadon, S.L.6    Kapfhamer, D.7    Sufalko, D.8    Robinson, M.S.9    Noebels, J.L.10
  • 106
  • 107
    • 0036086313 scopus 로고    scopus 로고
    • The ClC-3 chloride channel promotes acidification of lysosomes in CHO-K1 and Huh-7 cells
    • Li, X.; Wang, T.; Zhao, Z.; Weinman, S.A. The ClC-3 chloride channel promotes acidification of lysosomes in CHO-K1 and Huh-7 cells. Am. J. Physiol. Cell Physiol. 2002, 282, C1483-C1491.
    • (2002) Am. J. Physiol. Cell Physiol , vol.282
    • Li, X.1    Wang, T.2    Zhao, Z.3    Weinman, S.A.4
  • 108
    • 77449095180 scopus 로고    scopus 로고
    • The ClC-3 Cl-/H+ antiporter becomes uncoupled at low extracellular pH
    • Matsuda, J.J.; Filali, M.S.; Collins, M.M.; Volk, K.A.; Lamb, F.S. The ClC-3 Cl-/H+ antiporter becomes uncoupled at low extracellular pH. J. Biol. Chem. 2010, 285, 2569-2579.
    • (2010) J. Biol. Chem , vol.285 , pp. 2569-2579
    • Matsuda, J.J.1    Filali, M.S.2    Collins, M.M.3    Volk, K.A.4    Lamb, F.S.5
  • 109
    • 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
  • 110
    • 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
  • 112
    • 59749086561 scopus 로고    scopus 로고
    • The unfolded protein response and autophagy: Herpesviruses rule
    • Lee, D.Y.; Lee, J.; Sugden, B. The unfolded protein response and autophagy: Herpesviruses rule! J. Virol. 2009, 83, 1168-1172.
    • (2009) J. Virol , vol.83 , pp. 1168-1172
    • Lee, D.Y.1    Lee, J.2    Sugden, B.3
  • 113
    • 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
  • 114
    • 3142642871 scopus 로고    scopus 로고
    • Bidirectional transport along microtubules
    • Welte, M.A. Bidirectional transport along microtubules. Curr. Biol. 2004, 14, R525-R537.
    • (2004) Curr. Biol , vol.14
    • Welte, M.A.1
  • 115
    • 34548818532 scopus 로고    scopus 로고
    • A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
    • Salpingidou, G.; Smertenko, A.; Hausmanowa-Petrucewicz, I.; Hussey, P.J.; Hutchison, C.J. A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J. Cell Biol. 2007, 178, 897-904.
    • (2007) J. Cell Biol , vol.178 , pp. 897-904
    • Salpingidou, G.1    Smertenko, A.2    Hausmanowa-Petrucewicz, I.3    Hussey, P.J.4    Hutchison, C.J.5
  • 117
    • 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
  • 118
    • 73449134082 scopus 로고    scopus 로고
    • Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography
    • Peng, L.; Ryazantsev, S.; Sun, R.; Zhou, Z.H. Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography. Structure 2010, 18, 47-58.
    • (2010) Structure , vol.18 , pp. 47-58
    • Peng, L.1    Ryazantsev, S.2    Sun, R.3    Zhou, Z.H.4
  • 119
    • 0034091334 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 entry into host cells: Reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro
    • Ojala, P.M.; Sodeik, B.; Ebersold, M.W.; Kutay, U.; Helenius, A. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol. Cell Biol. 2000, 20, 4922-4931.
    • (2000) Mol. Cell Biol , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3    Kutay, U.4    Helenius, A.5
  • 121
    • 59649092592 scopus 로고    scopus 로고
    • Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment
    • Copeland, A.M.; Newcomb, W.W.; Brown, J.C. Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment. J. Virol. 2009, 83, 1660-1668.
    • (2009) J. Virol , vol.83 , pp. 1660-1668
    • Copeland, A.M.1    Newcomb, W.W.2    Brown, J.C.3
  • 122
    • 0026021706 scopus 로고
    • Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments
    • Djabali, K.; Portier, M.M.; Gros, F.; Blobel, G.; Georgatos, S.D. Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments. Cell 1991, 64, 109-121.
    • (1991) Cell , vol.64 , pp. 109-121
    • Djabali, K.1    Portier, M.M.2    Gros, F.3    Blobel, G.4    Georgatos, S.D.5
  • 123
    • 0023371437 scopus 로고
    • Lamin B constitutes an intermediate filament attachment site at the nuclear envelope
    • Georgatos, S.D.; Blobel, G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J. Cell Biol. 1987, 105, 117-125.
    • (1987) J. Cell Biol , vol.105 , pp. 117-125
    • Georgatos, S.D.1    Blobel, G.2
  • 124
    • 0023430563 scopus 로고
    • Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: Evidence for a conserved site-specificity in intermediate filament-membrane interactions
    • Georgatos, S.D.; Weber, K.; Geisler, N.; Blobel, G. Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc. Natl. Acad. Sci. U. S. A. 1987, 84, 6780-6784.
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 6780-6784
    • Georgatos, S.D.1    Weber, K.2    Geisler, N.3    Blobel, G.4
  • 125
    • 0020162216 scopus 로고
    • The nuclear matrix: Three-dimensional architecture and protein composition
    • Capco, D.G.; Wan, K.M.; Penman, S. The nuclear matrix: Three-dimensional architecture and protein composition. Cell 1982, 29, 847-858.
    • (1982) Cell , vol.29 , pp. 847-858
    • Capco, D.G.1    Wan, K.M.2    Penman, S.3
  • 126
    • 0023075406 scopus 로고
    • Connections of intermediate filaments with the nuclear lamina and the cell periphery
    • Katsuma, Y.; Swierenga, S.H.; Marceau, N.; French, S.W. Connections of intermediate filaments with the nuclear lamina and the cell periphery. Biol. Cell 1987, 59, 193-203.
    • (1987) Biol. Cell , vol.59 , pp. 193-203
    • Katsuma, Y.1    Swierenga, S.H.2    Marceau, N.3    French, S.W.4
  • 127
    • 0023953897 scopus 로고
    • Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes
    • Carmo-Fonseca, M.; Cidadao, A.J.; David-Ferreira, J.F. Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes. Eur. J. Cell Biol. 1988, 45, 282-290.
    • (1988) Eur. J. Cell Biol , vol.45 , pp. 282-290
    • Carmo-Fonseca, M.1    Cidadao, A.J.2    David-Ferreira, J.F.3
  • 129
    • 34547918327 scopus 로고    scopus 로고
    • Communication between the cytoskeleton and the nuclear envelope to position the nucleus
    • Starr, D.A. Communication between the cytoskeleton and the nuclear envelope to position the nucleus. Mol. Biosyst. 2007, 3, 583-589.
    • (2007) Mol. Biosyst , vol.3 , pp. 583-589
    • Starr, D.A.1
  • 130
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • Starr, D.A.; Fridolfsson, H.N. Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu. Rev. Cell Dev. Biol. 2010, 26, 421-444.
    • (2010) Annu. Rev. Cell Dev. Biol , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 131
    • 0031017220 scopus 로고    scopus 로고
    • Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure
    • Maniotis, A.J.; Chen, C.S.; Ingber, D.E. Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc. Natl. Acad. Sci. U. S. A. 1997, 94, 849-854.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 849-854
    • Maniotis, A.J.1    Chen, C.S.2    Ingber, D.E.3
  • 132
    • 0029460729 scopus 로고
    • Intermediate filaments and gene regulation
    • Traub, P. Intermediate filaments and gene regulation. Physiol. Chem. Phys. Med. NMR 1995, 27, 377-400.
    • (1995) Physiol. Chem. Phys. Med. NMR , vol.27 , pp. 377-400
    • Traub, P.1
  • 133
    • 33847410610 scopus 로고    scopus 로고
    • Gene silencing at the nuclear periphery
    • Shaklai, S.; Amariglio, N.; Rechavi, G.; Simon, A.J. Gene silencing at the nuclear periphery. FEBS J. 2007, 274, 1383-1392.
    • (2007) FEBS J , vol.274 , pp. 1383-1392
    • Shaklai, S.1    Amariglio, N.2    Rechavi, G.3    Simon, A.J.4
  • 134
    • 61849178739 scopus 로고    scopus 로고
    • A-type nuclear lamins act as transcriptional repressors when targeted to promoters
    • Lee, D.C.; Welton, K.L.; Smith, E.D.; Kennedy, B.K. A-type nuclear lamins act as transcriptional repressors when targeted to promoters. Exp. Cell Res. 2009, 315, 996-1007.
    • (2009) Exp. Cell Res , vol.315 , pp. 996-1007
    • Lee, D.C.1    Welton, K.L.2    Smith, E.D.3    Kennedy, B.K.4
  • 135
    • 26444589253 scopus 로고    scopus 로고
    • The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
    • Somech, R.; Shaklai, S.; Geller, O.; Amariglio, N.; Simon, A.J.; Rechavi, G.; Gal-Yam, E.N. The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J. Cell Sci. 2005, 118, 4017-4025.
    • (2005) J. Cell Sci , vol.118 , pp. 4017-4025
    • Somech, R.1    Shaklai, S.2    Geller, O.3    Amariglio, N.4    Simon, A.J.5    Rechavi, G.6    Gal-Yam, E.N.7
  • 137
    • 75749085178 scopus 로고    scopus 로고
    • Chromatinisation of herpesvirus genomes
    • Paulus, C.; Nitzsche, A.; Nevels, M. Chromatinisation of herpesvirus genomes. Rev. Med. Virol. 2010, 20, 34-50.
    • (2010) Rev. Med. Virol , vol.20 , pp. 34-50
    • Paulus, C.1    Nitzsche, A.2    Nevels, M.3
  • 138
    • 44949265263 scopus 로고    scopus 로고
    • Role for A-type lamins in herpesviral DNA targeting and heterochromatin modulation
    • Silva, L.; Cliffe, A.; Chang, L.; Knipe, D.M. Role for A-type lamins in herpesviral DNA targeting and heterochromatin modulation. PLoS Pathog. 2008, 4, e1000071.
    • (2008) PLoS Pathog , vol.4
    • Silva, L.1    Cliffe, A.2    Chang, L.3    Knipe, D.M.4
  • 140
    • 26444621444 scopus 로고    scopus 로고
    • Gene expression analysis in mice with elevated glial fibrillary acidic protein and Rosenthal fibers reveals a stress response followed by glial activation and neuronal dysfunction
    • Hagemann, T.L.; Gaeta, S.A.; Smith, M.A.; Johnson, D.A.; Johnson, J.A.; Messing, A. Gene expression analysis in mice with elevated glial fibrillary acidic protein and Rosenthal fibers reveals a stress response followed by glial activation and neuronal dysfunction. Hum. Mol. Genet. 2005, 14, 2443-2458.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2443-2458
    • Hagemann, T.L.1    Gaeta, S.A.2    Smith, M.A.3    Johnson, D.A.4    Johnson, J.A.5    Messing, A.6
  • 141
    • 0028197466 scopus 로고
    • Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin
    • Li, H.; Choudhary, S.K.; Milner, D.J.; Munir, M.I.; Kuisk, I.R.; Capetanaki, Y. Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin. J. Cell Biol. 1994, 124, 827-841.
    • (1994) J. Cell Biol , vol.124 , pp. 827-841
    • Li, H.1    Choudhary, S.K.2    Milner, D.J.3    Munir, M.I.4    Kuisk, I.R.5    Capetanaki, Y.6
  • 142
    • 0037225772 scopus 로고    scopus 로고
    • Microarray analysis of host cell gene transcription in response to varicella-zoster virus infection of human T cells and fibroblasts in vitro and SCIDhu skin xenografts in vivo
    • Jones, J.O.; Arvin, A.M. Microarray analysis of host cell gene transcription in response to varicella-zoster virus infection of human T cells and fibroblasts in vitro and SCIDhu skin xenografts in vivo. J. Virol. 2003, 77, 1268-1280.
    • (2003) J. Virol , vol.77 , pp. 1268-1280
    • Jones, J.O.1    Arvin, A.M.2
  • 143
    • 0037790986 scopus 로고    scopus 로고
    • Susceptibility of immature and mature Langerhans cell-type dendritic cells to infection and immunomodulation by human cytomegalovirus
    • Hertel, L.; Lacaille, V.G.; Strobl, H.; Mellins, E.D.; Mocarski, E.S. Susceptibility of immature and mature Langerhans cell-type dendritic cells to infection and immunomodulation by human cytomegalovirus. J. Virol. 2003, 77, 7563-7574.
    • (2003) J. Virol , vol.77 , pp. 7563-7574
    • Hertel, L.1    Lacaille, V.G.2    Strobl, H.3    Mellins, E.D.4    Mocarski, E.S.5
  • 144
    • 77949356639 scopus 로고    scopus 로고
    • Human cytomegalovirus infection causes premature and abnormal differentiation of human neural progenitor cells
    • Luo, M.H.; Hannemann, H.; Kulkarni, A.S.; Schwartz, P.H.; O'Dowd, J.M.; Fortunato, E.A. Human cytomegalovirus infection causes premature and abnormal differentiation of human neural progenitor cells. J. Virol. 2010, 84, 3528-3541.
    • (2010) J. Virol , vol.84 , pp. 3528-3541
    • Luo, M.H.1    Hannemann, H.2    Kulkarni, A.S.3    Schwartz, P.H.4    O'Dowd, J.M.5    Fortunato, E.A.6
  • 147
    • 0142085695 scopus 로고    scopus 로고
    • Upregulation of the truncated basic hair keratin 1(hHb1-DeltaN) in carcinoma cells by Epstein-Barr virus (EBV)
    • Nishikawa, J.; Kiss, C.; Imai, S.; Takada, K.; Okita, K.; Klein, G.; Szekely, L. Upregulation of the truncated basic hair keratin 1(hHb1-DeltaN) in carcinoma cells by Epstein-Barr virus (EBV). Int. J. Cancer 2003, 107, 597-602.
    • (2003) Int. J. Cancer , vol.107 , pp. 597-602
    • Nishikawa, J.1    Kiss, C.2    Imai, S.3    Takada, K.4    Okita, K.5    Klein, G.6    Szekely, L.7
  • 148
    • 0024336625 scopus 로고
    • Epstein-Barr virus latent infection membrane protein increases vimentin expression in human B-cell lines
    • Birkenbach, M.; Liebowitz, D.; Wang, F.; Sample, J.; Kieff, E. Epstein-Barr virus latent infection membrane protein increases vimentin expression in human B-cell lines. J. Virol. 1989, 63, 4079-4084.
    • (1989) J. Virol , vol.63 , pp. 4079-4084
    • Birkenbach, M.1    Liebowitz, D.2    Wang, F.3    Sample, J.4    Kieff, E.5
  • 149
    • 0027456839 scopus 로고
    • Epstein-Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells
    • Allday, M.J.; Crawford, D.H.; Thomas, J.A. Epstein-Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells. J. Gen. Virol. 1993, 74, 361-369.
    • (1993) J. Gen. Virol , vol.74 , pp. 361-369
    • Allday, M.J.1    Crawford, D.H.2    Thomas, J.A.3
  • 150
    • 0027991790 scopus 로고
    • Modulation of vimentin, the CD40 activation antigen and Burkitt's lymphoma antigen (CD77) by the Epstein-Barr virus nuclear antigen EBNA-4
    • Silins, S.L.; Sculley, T.B. Modulation of vimentin, the CD40 activation antigen and Burkitt's lymphoma antigen (CD77) by the Epstein-Barr virus nuclear antigen EBNA-4. Virology 1994, 202, 16-24.
    • (1994) Virology , vol.202 , pp. 16-24
    • Silins, S.L.1    Sculley, T.B.2
  • 151
    • 1842457780 scopus 로고    scopus 로고
    • Transcriptional response of a common permissive cell type to infection by two diverse alphaherpesviruses
    • Ray, N.; Enquist, L.W. Transcriptional response of a common permissive cell type to infection by two diverse alphaherpesviruses. J. Virol. 2004, 78, 3489-3501.
    • (2004) J. Virol , vol.78 , pp. 3489-3501
    • Ray, N.1    Enquist, L.W.2
  • 152
    • 0037168545 scopus 로고    scopus 로고
    • The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene
    • Taddeo, B.; Esclatine, A.; Roizman, B. The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene. Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 17031-17036.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 17031-17036
    • Taddeo, B.1    Esclatine, A.2    Roizman, B.3
  • 154
    • 77953302554 scopus 로고    scopus 로고
    • Escape of herpesviruses from the nucleus
    • Lee, C.P.; Chen, M.R. Escape of herpesviruses from the nucleus. Rev. Med. Virol. 2010, 20, 214-230.
    • (2010) Rev. Med. Virol , vol.20 , pp. 214-230
    • Lee, C.P.1    Chen, M.R.2
  • 155
    • 84929284235 scopus 로고    scopus 로고
    • Maturation and egress
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press: Cambridge, UK
    • Britt, B. Maturation and egress. 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 University Press: Cambridge, UK, 2007.
    • (2007) Human Herpesviruses: Biology, Therapy and Immunoprophylaxis
    • Britt, B.1
  • 157
    • 0034892692 scopus 로고    scopus 로고
    • Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection
    • Scott, E.S.; O'Hare, P. Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection. J. Virol. 2001, 75, 8818-8830.
    • (2001) J. Virol , vol.75 , pp. 8818-8830
    • Scott, E.S.1    O'Hare, P.2
  • 158
    • 33645961583 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B
    • Park, R.; Baines, J.D. Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B. J. Virol. 2006, 80, 494-504.
    • (2006) J. Virol , vol.80 , pp. 494-504
    • Park, R.1    Baines, J.D.2
  • 159
    • 2442697760 scopus 로고    scopus 로고
    • Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34
    • Reynolds, A.E.; Liang, L.; Baines, J.D. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34. J. Virol. 2004, 78, 5564-5575.
    • (2004) J. Virol , vol.78 , pp. 5564-5575
    • Reynolds, A.E.1    Liang, L.2    Baines, J.D.3
  • 160
    • 2442719000 scopus 로고    scopus 로고
    • Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late maturation of viral replication compartments to the nuclear periphery
    • Simpson-Holley, M.; Baines, J.; Roller, R.; Knipe, D.M. Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late maturation of viral replication compartments to the nuclear periphery. J. Virol. 2004, 78, 5591-5600.
    • (2004) J. Virol , vol.78 , pp. 5591-5600
    • Simpson-Holley, M.1    Baines, J.2    Roller, R.3    Knipe, D.M.4
  • 161
    • 34247642597 scopus 로고    scopus 로고
    • Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein
    • Morris, J.B.; Hofemeister, H.; O'Hare, P. Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein. J. Virol. 2007, 81, 4429-4437.
    • (2007) J. Virol , vol.81 , pp. 4429-4437
    • Morris, J.B.1    Hofemeister, H.2    O'Hare, P.3
  • 162
    • 34648822335 scopus 로고    scopus 로고
    • Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3
    • Leach, N.; Bjerke, S.L.; Christensen, D.K.; Bouchard, J.M.; Mou, F.; Park, R.; Baines, J.; Haraguchi, T.; Roller, R.J. Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3. J. Virol. 2007, 81, 10792-10803.
    • (2007) J. Virol , vol.81 , pp. 10792-10803
    • Leach, N.1    Bjerke, S.L.2    Christensen, D.K.3    Bouchard, J.M.4    Mou, F.5    Park, R.6    Baines, J.7    Haraguchi, T.8    Roller, R.J.9
  • 163
    • 34249939914 scopus 로고    scopus 로고
    • US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells
    • Mou, F.; Forest, T.; Baines, J.D. US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells. J. Virol. 2007, 81, 6459-6470.
    • (2007) J. Virol , vol.81 , pp. 6459-6470
    • Mou, F.1    Forest, T.2    Baines, J.D.3
  • 164
    • 69249222501 scopus 로고    scopus 로고
    • Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins
    • Cano-Monreal, G.L.; Wylie, K.M.; Cao, F.; Tavis, J.E.; Morrison, L.A. Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins. Virology 2009, 392, 137-147.
    • (2009) Virology , vol.392 , pp. 137-147
    • Cano-Monreal, G.L.1    Wylie, K.M.2    Cao, F.3    Tavis, J.E.4    Morrison, L.A.5
  • 165
    • 0034989005 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 UL34 protein requires UL31 protein for its relocation to the internal nuclear membrane in transfected cells
    • Yamauchi, Y.; Shiba, C.; Goshima, F.; Nawa, A.; Murata, T.; Nishiyama, Y. Herpes simplex virus type 2 UL34 protein requires UL31 protein for its relocation to the internal nuclear membrane in transfected cells. J. Gen. Virol. 2001, 82, 1423-1428.
    • (2001) J. Gen. Virol , vol.82 , pp. 1423-1428
    • Yamauchi, Y.1    Shiba, C.2    Goshima, F.3    Nawa, A.4    Murata, T.5    Nishiyama, Y.6
  • 166
    • 26444466028 scopus 로고    scopus 로고
    • Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection
    • Simpson-Holley, M.; Colgrove, R.C.; Nalepa, G.; Harper, J.W.; Knipe, D.M. Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection. J. Virol. 2005, 79, 12840-12851.
    • (2005) J. Virol , vol.79 , pp. 12840-12851
    • Simpson-Holley, M.1    Colgrove, R.C.2    Nalepa, G.3    Harper, J.W.4    Knipe, D.M.5
  • 167
    • 33646018621 scopus 로고    scopus 로고
    • Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress
    • Bjerke, S.L.; Roller, R.J. Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress. Virology 2006, 347, 261-276.
    • (2006) Virology , vol.347 , pp. 261-276
    • Bjerke, S.L.1    Roller, R.J.2
  • 168
    • 31144450021 scopus 로고    scopus 로고
    • Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31
    • Kato, A.; Yamamoto, M.; Ohno, T.; Tanaka, M.; Sata, T.; Nishiyama, Y.; Kawaguchi, Y. Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31. J. Virol. 2006, 80, 1476-1486.
    • (2006) J. Virol , vol.80 , pp. 1476-1486
    • Kato, A.1    Yamamoto, M.2    Ohno, T.3    Tanaka, M.4    Sata, T.5    Nishiyama, Y.6    Kawaguchi, Y.7
  • 169
    • 77956186490 scopus 로고    scopus 로고
    • Significance of host cell kinases in herpes simplex virus type 1 egress and lamin-associated protein disassembly from the nuclear lamina
    • Leach, N.R.; Roller, R.J. Significance of host cell kinases in herpes simplex virus type 1 egress and lamin-associated protein disassembly from the nuclear lamina. Virology 2010, 406, 127-137.
    • (2010) Virology , vol.406 , pp. 127-137
    • Leach, N.R.1    Roller, R.J.2
  • 170
    • 49149090155 scopus 로고    scopus 로고
    • Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane
    • Mou, F.; Wills, E.G.; Park, R.; Baines, J.D. Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane. J. Virol. 2008, 82, 8094-8104.
    • (2008) J. Virol , vol.82 , pp. 8094-8104
    • Mou, F.1    Wills, E.G.2    Park, R.3    Baines, J.D.4
  • 171
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: Many faces, many functions
    • Schirmer, E.C.; Foisner, R. Proteins that associate with lamins: Many faces, many functions. Exp. Cell Res. 2007, 313, 2167-2179.
    • (2007) Exp. Cell Res , vol.313 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 172
    • 41649097238 scopus 로고    scopus 로고
    • Nuclear lamins: Major factors in the structural organization and function of the nucleus and chromatin
    • Dechat, T.; Pfleghaar, K.; Sengupta, K.; Shimi, T.; Shumaker, D.K.; Solimando, L.; Goldman, R.D. Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin. Genes Dev. 2008, 22, 832-853.
    • (2008) Genes Dev , vol.22 , pp. 832-853
    • Dechat, T.1    Pfleghaar, K.2    Sengupta, K.3    Shimi, T.4    Shumaker, D.K.5    Solimando, L.6    Goldman, R.D.7
  • 174
    • 0347698385 scopus 로고
    • Mouse cytomegalovirus infection. An electron microscopic study of hepatic parenchymal cells
    • Ruebner, B.H.; Miyai, K.; Slusser, R.J.; Wedemeyer, P.; Medearis, D.N., Jr. Mouse cytomegalovirus infection. An electron microscopic study of hepatic parenchymal cells. Am. J. Pathol. 1964, 44, 799-821.
    • (1964) Am. J. Pathol , vol.44 , pp. 799-821
    • Ruebner, B.H.1    Miyai, K.2    Slusser, R.J.3    Wedemeyer, P.4    Medearis Jr., D.N.5
  • 175
    • 0021714650 scopus 로고
    • An ultrastructural investigation of cytomegalovirus replication in murine hepatocytes
    • Papadimitriou, J.M.; Shellam, G.R.; Robertson, T.A. An ultrastructural investigation of cytomegalovirus replication in murine hepatocytes. J. Gen. Virol. 1984, 65, 1979-1990.
    • (1984) J. Gen. Virol , vol.65 , pp. 1979-1990
    • Papadimitriou, J.M.1    Shellam, G.R.2    Robertson, T.A.3
  • 176
    • 0033656912 scopus 로고    scopus 로고
    • Human bone marrow fibroblasts infected by cytomegalovirus: Ultrastructural observations
    • Gilloteaux, J.; Nassiri, M.R. Human bone marrow fibroblasts infected by cytomegalovirus: ultrastructural observations. J. Submicrosc. Cytol. Pathol. 2000, 32, 17-45.
    • (2000) J. Submicrosc. Cytol. Pathol , vol.32 , pp. 17-45
    • Gilloteaux, J.1    Nassiri, M.R.2
  • 177
    • 0023833210 scopus 로고
    • Human cytomegalovirus morphogenesis: An ultrastructural study of the late cytoplasmic phases
    • Severi, B.; Landini, M.P.; Govoni, E. Human cytomegalovirus morphogenesis: an ultrastructural study of the late cytoplasmic phases. Arch. Virol. 1988, 98, 51-64.
    • (1988) Arch. Virol , vol.98 , pp. 51-64
    • Severi, B.1    Landini, M.P.2    Govoni, E.3
  • 178
    • 33947399237 scopus 로고    scopus 로고
    • Cytomegalovirus primary envelopment occurs at large infoldings of the inner nuclear membrane
    • Buser, C.; Walther, P.; Mertens, T.; Michel, D. Cytomegalovirus primary envelopment occurs at large infoldings of the inner nuclear membrane. J. Virol. 2007, 81, 3042-3048.
    • (2007) J. Virol , vol.81 , pp. 3042-3048
    • Buser, C.1    Walther, P.2    Mertens, T.3    Michel, D.4
  • 179
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi, W.; Haas, J.; Wagner, M.; Krohne, G.; Koszinowski, U.H. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 2002, 297, 854-857.
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 180
    • 63449129336 scopus 로고    scopus 로고
    • Cytomegaloviral proteins that associate with the nuclear lamina: Components of a postulated nuclear egress complex
    • Milbradt, J.; Auerochs, S.; Sticht, H.; Marschall, M. Cytomegaloviral proteins that associate with the nuclear lamina: Components of a postulated nuclear egress complex. J. Gen. Virol. 2009, 90, 579-590.
    • (2009) J. Gen. Virol , vol.90 , pp. 579-590
    • Milbradt, J.1    Auerochs, S.2    Sticht, H.3    Marschall, M.4
  • 181
    • 77951577056 scopus 로고    scopus 로고
    • Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirus
    • Milbradt, J.; Webel, R.; Auerochs, S.; Sticht, H.; Marschall, M. Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirus. J. Biol. Chem. 2010, 285, 13979-13989.
    • (2010) J. Biol. Chem , vol.285 , pp. 13979-13989
    • Milbradt, J.1    Webel, R.2    Auerochs, S.3    Sticht, H.4    Marschall, M.5
  • 183
    • 0024514339 scopus 로고
    • Alteration of nuclear lamina protein in human fibroblasts infected with cytomegalovirus (HCMV)
    • Radsak, K.; Schneider, D.; Jost, E.; Brucher, K.H. Alteration of nuclear lamina protein in human fibroblasts infected with cytomegalovirus (HCMV). Arch. Virol. 1989, 105, 103-112.
    • (1989) Arch. Virol , vol.105 , pp. 103-112
    • Radsak, K.1    Schneider, D.2    Jost, E.3    Brucher, K.H.4
  • 184
    • 42449130222 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina during human cytomegalovirus infection: Role of the viral proteins pUL50 and pUL53
    • Camozzi, D.; Pignatelli, S.; Valvo, C.; Lattanzi, G.; Capanni, C.; dal Monte, P.; Landini, M.P. Remodelling of the nuclear lamina during human cytomegalovirus infection: Role of the viral proteins pUL50 and pUL53. J. Gen. Virol. 2008, 89, 731-740.
    • (2008) J. Gen. Virol , vol.89 , pp. 731-740
    • Camozzi, D.1    Pignatelli, S.2    Valvo, C.3    Lattanzi, G.4    Capanni, C.5    dal Monte, P.6    Landini, M.P.7
  • 186
    • 35048861785 scopus 로고    scopus 로고
    • Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C
    • Milbradt, J.; Auerochs, S.; Marschall, M. Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C. J. Gen. Virol. 2007, 88, 2642-2650.
    • (2007) J. Gen. Virol , vol.88 , pp. 2642-2650
    • Milbradt, J.1    Auerochs, S.2    Marschall, M.3
  • 187
    • 67650911368 scopus 로고    scopus 로고
    • Function of human cytomegalovirus UL97 kinase in viral infection and its inhibition by maribavir
    • Prichard, M.N. Function of human cytomegalovirus UL97 kinase in viral infection and its inhibition by maribavir. Rev. Med. Virol. 2009, 19, 215-229.
    • (2009) Rev. Med. Virol , vol.19 , pp. 215-229
    • Prichard, M.N.1
  • 188
    • 0041837470 scopus 로고    scopus 로고
    • Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2
    • Kawaguchi, Y.; Kato, K. Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2. Rev. Med. Virol. 2003, 13, 331-340.
    • (2003) Rev. Med. Virol , vol.13 , pp. 331-340
    • Kawaguchi, Y.1    Kato, K.2
  • 189
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M.; Nakagawa, J.; Doree, M.; Labbe, J.C.; Nigg, E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 1990, 61, 591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 190
    • 6344270058 scopus 로고    scopus 로고
    • Global analysis of host cell gene expression late during cytomegalovirus infection reveals extensive dysregulation of cell cycle gene expression and induction of Pseudomitosis independent of US28 function
    • Hertel, L.; Mocarski, E.S. Global analysis of host cell gene expression late during cytomegalovirus infection reveals extensive dysregulation of cell cycle gene expression and induction of Pseudomitosis independent of US28 function. J. Virol. 2004, 78, 11988-12011.
    • (2004) J. Virol , vol.78 , pp. 11988-12011
    • Hertel, L.1    Mocarski, E.S.2
  • 191
    • 33846597192 scopus 로고    scopus 로고
    • Viral and cell cycle-regulated kinases in cytomegalovirus-induced pseudomitosis and replication
    • Hertel, L.; Chou, S.; Mocarski, E.S. Viral and cell cycle-regulated kinases in cytomegalovirus-induced pseudomitosis and replication. PLoS Pathog. 2007, 3, e6.
    • (2007) PLoS Pathog , vol.3
    • Hertel, L.1    Chou, S.2    Mocarski, E.S.3
  • 192
    • 0024501607 scopus 로고
    • Localization of Epstein-Barr virus envelope glycoproteins on the inner nuclear membrane of virus-producing cells
    • Torrisi, M.R.; Cirone, M.; Pavan, A.; Zompetta, C.; Barile, G.; Frati, L.; Faggioni, A. Localization of Epstein-Barr virus envelope glycoproteins on the inner nuclear membrane of virus-producing cells. J. Virol. 1989, 63, 828-832.
    • (1989) J. Virol , vol.63 , pp. 828-832
    • Torrisi, M.R.1    Cirone, M.2    Pavan, A.3    Zompetta, C.4    Barile, G.5    Frati, L.6    Faggioni, A.7
  • 195
    • 20044393307 scopus 로고    scopus 로고
    • Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: Interactions with BFRF1 and with the nuclear lamina
    • Gonnella, R.; Farina, A.; Santarelli, R.; Raffa, S.; Feederle, R.; Bei, R.; Granato, M.; Modesti, A.; Frati, L.; Delecluse, H.J., et al. Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: Interactions with BFRF1 and with the nuclear lamina. J. Virol. 2005, 79, 3713-3727.
    • (2005) J. Virol , vol.79 , pp. 3713-3727
    • Gonnella, R.1    Farina, A.2    Santarelli, R.3    Raffa, S.4    Feederle, R.5    Bei, R.6    Granato, M.7    Modesti, A.8    Frati, L.9    Delecluse, H.J.10
  • 196
    • 56449106108 scopus 로고    scopus 로고
    • Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production
    • Lee, C.P.; Huang, Y.H.; Lin, S.F.; Chang, Y.; Chang, Y.H.; Takada, K.; Chen, M.R. Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production. J. Virol. 2008, 82, 11913-11926.
    • (2008) J. Virol , vol.82 , pp. 11913-11926
    • Lee, C.P.1    Huang, Y.H.2    Lin, S.F.3    Chang, Y.4    Chang, Y.H.5    Takada, K.6    Chen, M.R.7
  • 200
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • Milner, D.J.; Mavroidis, M.; Weisleder, N.; Capetanaki, Y. Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J. Cell Biol. 2000, 150, 1283-1298.
    • (2000) J. Cell Biol , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanaki, Y.4
  • 202
    • 34249723830 scopus 로고    scopus 로고
    • Structural and regulatory functions of keratins
    • Magin, T.M.; Vijayaraj, P.; Leube, R.E. Structural and regulatory functions of keratins. Exp. Cell Res. 2007, 313, 2021-2032.
    • (2007) Exp. Cell Res , vol.313 , pp. 2021-2032
    • Magin, T.M.1    Vijayaraj, P.2    Leube, R.E.3
  • 203
    • 67749116432 scopus 로고    scopus 로고
    • The nucleoprotein of lymphocytic choriomeningitis virus facilitates spread of persistent infection through stabilization of the keratin network
    • Labudova, M.; Tomaskova, J.; Skultety, L.; Pastorek, J.; Pastorekova, S. The nucleoprotein of lymphocytic choriomeningitis virus facilitates spread of persistent infection through stabilization of the keratin network. J. Virol. 2009, 83, 7842-7849.
    • (2009) J. Virol , vol.83 , pp. 7842-7849
    • Labudova, M.1    Tomaskova, J.2    Skultety, L.3    Pastorek, J.4    Pastorekova, S.5


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