메뉴 건너뛰기




Volumn 3, Issue 7, 2011, Pages 941-981

Peripheral tissues, alphaherpesviruses and the cytoskeleton in neuronal infections

Author keywords

Alphaherpesvirus; Cytoskeleton; Neuroinvasion; Virus transport

Indexed keywords

ACTIN; KINESIN; MOLECULAR MOTOR; MYOSIN; TUBULIN; VIRUS DNA; VIRUS PROTEIN;

EID: 79960816793     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v3070941     Document Type: Review
Times cited : (30)

References (317)
  • 1
    • 78149254592 scopus 로고    scopus 로고
    • A neurotropic herpesvirus infecting the gastropod, abalone, shares ancestry with oyster herpesvirus and a herpesvirus associated with the amphioxus genome
    • Savin, K.W.; Cocks, B.G.; Wong, F.; Sawbridge, T.; Cogan, N.; Savage, D.; Warner, S. A neurotropic herpesvirus infecting the gastropod, abalone, shares ancestry with oyster herpesvirus and a herpesvirus associated with the amphioxus genome. Virol. J. 2010, 7, 308.
    • (2010) Virol. J , vol.7 , pp. 308
    • Savin, K.W.1    Cocks, B.G.2    Wong, F.3    Sawbridge, T.4    Cogan, N.5    Savage, D.6    Warner, S.7
  • 2
    • 67349232384 scopus 로고    scopus 로고
    • Ostreid herpes virus 1 infection in families of the Pacific oyster, Crassostrea gigas, during a summer mortality outbreak: Differences in viral DNA detection and quantification using real-time PCR
    • Sauvage, C.; Pepin, J.F.; Lapegue, S.; Boudry, P.; Renault, T. Ostreid herpes virus 1 infection in families of the Pacific oyster, Crassostrea gigas, during a summer mortality outbreak: Differences in viral DNA detection and quantification using real-time PCR. Virus Res. 2009, 142, 181-187.
    • (2009) Virus Res , vol.142 , pp. 181-187
    • Sauvage, C.1    Pepin, J.F.2    Lapegue, S.3    Boudry, P.4    Renault, T.5
  • 6
    • 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
  • 7
    • 33644822448 scopus 로고    scopus 로고
    • Viral interactions with the cytoskeleton: A hitchhiker's guide to the cell
    • Radtke, K.; Dohner, K.; Sodeik, B. Viral interactions with the cytoskeleton: A hitchhiker's guide to the cell. Cell. Microbiol. 2006, 8, 387-400.
    • (2006) Cell. Microbiol , vol.8 , pp. 387-400
    • Radtke, K.1    Dohner, K.2    Sodeik, B.3
  • 8
    • 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
  • 9
    • 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
  • 10
    • 77955597073 scopus 로고    scopus 로고
    • A hitchhiker's guide to the nervous system: The complex journey of viruses and toxins
    • Salinas, S.; Schiavo, G.; Kremer, E.J. A hitchhiker's guide to the nervous system: The complex journey of viruses and toxins. Nat. Rev. Microbiol. 2010, 8, 645-655.
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 645-655
    • Salinas, S.1    Schiavo, G.2    Kremer, E.J.A.3
  • 11
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • Fields, B.N., Knipe, D.M., Howley, P.M., Griffin, D.E., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA
    • Roizman, B.; Knipe, D.M. Herpes simplex viruses and their replication. In Fields Virology; Fields, B.N., Knipe, D.M., Howley, P.M., Griffin, D.E., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA, 2001; Volume 2, pp. 2399-2459.
    • (2001) Fields Virology , vol.2 , pp. 2399-2459
    • Roizman, B.1    Knipe, D.M.2
  • 13
    • 77952883755 scopus 로고    scopus 로고
    • Herpesvirus systematics
    • Davison, A.J. Herpesvirus systematics. Vet. Microbiol. 2010, 143, 52-69.
    • (2010) Vet. Microbiol , vol.143 , pp. 52-69
    • Davison, A.J.1
  • 14
    • 0001142642 scopus 로고    scopus 로고
    • The family Herpesviridae: A brief introduction
    • Fields, B.N., Knipe, D.M., Howley, P.M., Griffin, D.E., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA
    • Roizman, B.; Pellett, P.E. The family Herpesviridae: A brief introduction. In Fields virology; Fields, B.N., Knipe, D.M., Howley, P.M., Griffin, D.E., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA, 2001; Volume 2, pp. 2381-2397.
    • (2001) Fields Virology , vol.2 , pp. 2381-2397
    • Roizman, B.1    Pellett, P.E.2
  • 15
    • 0026484602 scopus 로고
    • The family Herpesviridae: An update
    • The Herpesvirus Study Group of the International Committee on Taxonomy of Viruses
    • Roizman, B.; Desrosiers, R.C.; Fleckenstein, B.; Lopez, C.; Minson, A.C.; Studdert, M.J. The family Herpesviridae: An update. The Herpesvirus Study Group of the International Committee on Taxonomy of Viruses. Arch. Virol. 1992, 123, 425-449.
    • (1992) Arch. Virol , vol.123 , pp. 425-449
    • Roizman, B.1    Desrosiers, R.C.2    Fleckenstein, B.3    Lopez, C.4    Minson, A.C.5    Studdert, M.J.6
  • 16
    • 0000314691 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • Fields, B.N., Knipe, D.M., Howley, P.M., Eds.; Lippincott-Raven Publishers: Philadelphia, PA, USA
    • Whitley, R.J. Herpes simplex viruses. In Fields Virology; Fields, B.N., Knipe, D.M., Howley, P.M., Eds.; Lippincott-Raven Publishers: Philadelphia, PA, USA, 1996; Volume 2, pp. 2297-2342.
    • (1996) Fields Virology , vol.2 , pp. 2297-2342
    • Whitley, R.J.1
  • 17
    • 84929263033 scopus 로고    scopus 로고
    • Clinical and pathological aspects of EBV and KSHV infection
    • Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K., Eds.; Cambridge University Press, Cambridge, UK, Chapter 50
    • Ambinder, R.F.; Cesarman, E. Clinical and pathological aspects of EBV and KSHV 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; Chapter 50.
    • (2007) Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis
    • Ambinder, R.F.1    Cesarman, E.2
  • 18
    • 73949113906 scopus 로고    scopus 로고
    • Herpesviruses-A zoonotic threat?
    • Tischer, B.K.; Osterrieder, N. Herpesviruses-A zoonotic threat? Vet. Microbiol. 2010, 140, 266-270.
    • (2010) Vet Microbiol , vol.140 , pp. 266-270
    • Tischer, B.K.1    Osterrieder, N.2
  • 19
    • 0020578881 scopus 로고
    • Characterization of Marek's disease virus-infected lymphocytes: Discrimination between cytolytically and latently infected cells
    • Shek, W.R.; Calnek, B.W.; Schat, K.A.; Chen, C.H. Characterization of Marek's disease virus-infected lymphocytes: Discrimination between cytolytically and latently infected cells. J. Natl. Cancer Inst. 1983, 70, 485-491.
    • (1983) J. Natl. Cancer Inst , vol.70 , pp. 485-491
    • Shek, W.R.1    Calnek, B.W.2    Schat, K.A.3    Chen, C.H.4
  • 20
    • 0019522792 scopus 로고
    • Marek's disease as a model for the Landry--Guillain--Barre syndrome: Latent viral infection in nonneuronal cells accompanied by specific immune responses to peripheral nerve and myelin
    • Pepose, J.S.; Stevens, J.G.; Cook, M.L.; Lampert, P.W. Marek's disease as a model for the Landry--Guillain--Barre syndrome: Latent viral infection in nonneuronal cells accompanied by specific immune responses to peripheral nerve and myelin. Am. J. Pathol. 1981, 103, 309-320.
    • (1981) Am. J. Pathol , vol.103 , pp. 309-320
    • Pepose, J.S.1    Stevens, J.G.2    Cook, M.L.3    Lampert, P.W.4
  • 21
    • 0026629867 scopus 로고
    • Demonstration of sites of latency of infectious laryngotracheitis virus using the polymerase chain reaction
    • Williams, R.A.; Bennett, M.; Bradbury, J.M.; Gaskell, R.M.; Jones, R.C.; Jordan, F.T. Demonstration of sites of latency of infectious laryngotracheitis virus using the polymerase chain reaction. J. Gen. Virol. 1992, 73, 2415-2420.
    • (1992) J. Gen. Virol , vol.73 , pp. 2415-2420
    • Williams, R.A.1    Bennett, M.2    Bradbury, J.M.3    Gaskell, R.M.4    Jones, R.C.5    Jordan, F.T.6
  • 22
    • 0035171263 scopus 로고    scopus 로고
    • Herpes simplex virus epidemiology and ocular importance
    • Liesegang, T.J. Herpes simplex virus epidemiology and ocular importance. Cornea 2001, 20, 1-13.
    • (2001) Cornea , vol.20 , pp. 1-13
    • Liesegang, T.J.1
  • 23
    • 0022526807 scopus 로고
    • Autonomic nervous system involvement in experimental genital infection by herpes simplex virus type 2
    • Sanjuan, N.A.; Lascano, E.F. Autonomic nervous system involvement in experimental genital infection by herpes simplex virus type 2. Arch. Virol. 1986, 91, 329-339.
    • (1986) Arch. Virol , vol.91 , pp. 329-339
    • Sanjuan, N.A.1    Lascano, E.F.2
  • 24
    • 0036288016 scopus 로고    scopus 로고
    • Detection of herpes simplex virus type 1 in human ciliary ganglia
    • Bustos, D.E.; Atherton, S.S. Detection of herpes simplex virus type 1 in human ciliary ganglia. Invest. Ophthalmol. Vis. Sci. 2002, 43, 2244-2249.
    • (2002) Invest. Ophthalmol. Vis. Sci , vol.43 , pp. 2244-2249
    • Bustos, D.E.1    Atherton, S.S.2
  • 26
    • 26444577541 scopus 로고    scopus 로고
    • Herpes simplex virus infections in neonates and early childhood
    • Kimberlin, D.W. Herpes simplex virus infections in neonates and early childhood. Semin. Pediatr. Infect. Dis. 2005, 16, 271-281.
    • (2005) Semin. Pediatr. Infect. Dis , vol.16 , pp. 271-281
    • Kimberlin, D.W.1
  • 27
    • 0037434062 scopus 로고    scopus 로고
    • Acyclovir-resistant genital herpes among persons attending sexually transmitted disease and human immunodeficiency virus clinics
    • Reyes, M.; Shaik, N.S.; Graber, J.M.; Nisenbaum, R.; Wetherall, N.T.; Fukuda, K.; Reeves, W.C. Acyclovir-resistant genital herpes among persons attending sexually transmitted disease and human immunodeficiency virus clinics. Arch. Intern. Med. 2003, 163, 76-80.
    • (2003) Arch. Intern. Med , vol.163 , pp. 76-80
    • Reyes, M.1    Shaik, N.S.2    Graber, J.M.3    Nisenbaum, R.4    Wetherall, N.T.5    Fukuda, K.6    Reeves, W.C.7
  • 28
    • 0037244124 scopus 로고    scopus 로고
    • Herpes simplex virus resistance to acyclovir and penciclovir after two decades of antiviral therapy
    • Bacon, T.H.; Levin, M.J.; Leary, J.J.; Sarisky, R.T.; Sutton, D. Herpes simplex virus resistance to acyclovir and penciclovir after two decades of antiviral therapy. Clin. Microbiol. Rev. 2003, 16, 114-128.
    • (2003) Clin. Microbiol. Rev , vol.16 , pp. 114-128
    • Bacon, T.H.1    Levin, M.J.2    Leary, J.J.3    Sarisky, R.T.4    Sutton, D.5
  • 29
    • 13944264636 scopus 로고    scopus 로고
    • Varicella-Zoster virus pathogenesis and immunobiology: New concepts emerging from investigations with the SCIDhu mouse model
    • Ku, C.C.; Besser, J.; Abendroth, A.; Grose, C.; Arvin, A.M. Varicella-Zoster virus pathogenesis and immunobiology: New concepts emerging from investigations with the SCIDhu mouse model. J. Virol. 2005, 79, 2651-2658.
    • (2005) J. Virol , vol.79 , pp. 2651-2658
    • Ku, C.C.1    Besser, J.2    Abendroth, A.3    Grose, C.4    Arvin, A.M.5
  • 30
    • 0023759968 scopus 로고
    • Airborne transmission of nosocomial varicella from localized zoster
    • Josephson, A.; Gombert, M.E. Airborne transmission of nosocomial varicella from localized zoster. J. Infect. Dis. 1988, 158, 238-241.
    • (1988) J. Infect. Dis , vol.158 , pp. 238-241
    • Josephson, A.1    Gombert, M.E.2
  • 31
    • 35248835968 scopus 로고    scopus 로고
    • The neurotropic herpes viruses: Herpes simplex and varicella-zoster
    • Steiner, I.; Kennedy, P.G.; Pachner, A.R. The neurotropic herpes viruses: Herpes simplex and varicella-zoster. Lancet Neurol. 2007, 6, 1015-1028.
    • (2007) Lancet Neurol , vol.6 , pp. 1015-1028
    • Steiner, I.1    Kennedy, P.G.2    Pachner, A.R.3
  • 32
    • 0022921063 scopus 로고
    • CNS diseases associated with varicella zoster virus and herpes simplex virus infection
    • Barnes, D.W.; Whitley, R.J. CNS diseases associated with varicella zoster virus and herpes simplex virus infection. Pathogenesis and current therapy. Neurol. Clin. 1986, 4, 265-283.
    • (1986) Pathogenesis and current therapy. Neurol Clin , vol.4 , pp. 265-283
    • Barnes, D.W.1    Whitley, R.J.2
  • 34
    • 79960759349 scopus 로고    scopus 로고
    • 6th ed.; Cann, C., Ed.; Lippincott Williams & Wilkins: Baltimore, MD, USA
    • Jones, C.A.; Hunt, R.D.; King, N.W. Veterinary Pathology, 6th ed.; Cann, C., Ed.; Lippincott Williams & Wilkins: Baltimore, MD, USA, 1997; pp. 217-234.
    • (1997) Veterinary Pathology , pp. 217-234
    • Jones, C.A.1    Hunt, R.D.2    King, N.W.3
  • 37
    • 0026599626 scopus 로고
    • Biology of B virus in macaque and human hosts: A review
    • Weigler, B.J. Biology of B virus in macaque and human hosts: A review. Clin. Infect. Dis. 1992, 14, 555-567.
    • (1992) Clin. Infect. Dis , vol.14 , pp. 555-567
    • Weigler, B.J.1
  • 39
    • 0032247683 scopus 로고    scopus 로고
    • Infection and spread of alphaherpesviruses in the nervous system
    • Enquist, L.W.; Husak, P.J.; Banfield, B.W.; Smith, G.A. Infection and spread of alphaherpesviruses in the nervous system. Adv. Virus Res. 1998, 51, 237-347.
    • (1998) Adv. Virus Res , vol.51 , pp. 237-347
    • Enquist, L.W.1    Husak, P.J.2    Banfield, B.W.3    Smith, G.A.4
  • 40
    • 24944433231 scopus 로고    scopus 로고
    • Molecular biology of pseudorabies virus: Impact on neurovirology and veterinary medicine
    • Pomeranz, L.E.; Reynolds, A.E.; Hengartner, C.J. Molecular biology of pseudorabies virus: Impact on neurovirology and veterinary medicine. Microbiol. Mol. Biol. Rev. 2005, 69, 462-500.
    • (2005) Microbiol. Mol. Biol. Rev , vol.69 , pp. 462-500
    • Pomeranz, L.E.1    Reynolds, A.E.2    Hengartner, C.J.3
  • 41
    • 0025361892 scopus 로고
    • Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture
    • Dotti, C.G.; Simons, K. Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture. Cell 1990, 62, 63-72.
    • (1990) Cell , vol.62 , pp. 63-72
    • Dotti, C.G.1    Simons, K.2
  • 42
    • 0026017320 scopus 로고
    • Polarized sorting of glypiated proteins in hippocampal neurons
    • Dotti, C.G.; Parton, R.G.; Simons, K. Polarized sorting of glypiated proteins in hippocampal neurons. Nature 1991, 349, 158-161.
    • (1991) Nature , vol.349 , pp. 158-161
    • Dotti, C.G.1    Parton, R.G.2    Simons, K.3
  • 44
    • 0030245731 scopus 로고    scopus 로고
    • A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins
    • Fannon, A.M.; Colman, D.R. A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins. Neuron 1996, 17, 423-434.
    • (1996) Neuron , vol.17 , pp. 423-434
    • Fannon, A.M.1    Colman, D.R.2
  • 47
    • 0033938994 scopus 로고    scopus 로고
    • Recurring views on the structure and function of the cytoskeleton: A 300-year epic
    • Frixione, E. Recurring views on the structure and function of the cytoskeleton: A 300-year epic. Cell Motil. Cytoskeleton 2000, 46, 73-94.
    • (2000) Cell Motil. Cytoskeleton , vol.46 , pp. 73-94
    • Frixione, E.1
  • 48
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard, T.D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 1986, 103, 2747-2754.
    • (1986) J. Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 49
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R.D.; Heuser, J.A.; Pollard, T.D. The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 6181-6186.
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 50
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: Matching assembly factors with cellular structures
    • Chhabra, E.S.; Higgs, H.N. The many faces of actin: Matching assembly factors with cellular structures. Nat. Cell Biol. 2007, 9, 1110-1121.
    • (2007) Nat. Cell Biol , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 51
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo, L. Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu. Rev. Cell Dev. Biol. 2002, 18, 601-635.
    • (2002) Annu. Rev. Cell Dev. Biol , vol.18 , pp. 601-635
    • Luo, L.1
  • 52
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 1994, 10, 31-54.
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 31-54
    • Hall, A.1
  • 53
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N.; Hall, A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 1997, 9, 86-92.
    • (1997) Curr. Opin. Cell Biol , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 54
    • 77956663124 scopus 로고    scopus 로고
    • Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation
    • Zhang, F.; Saha, S.; Shabalina, S.A.; Kashina, A. Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. Science 2010, 329, 1534-1537.
    • (2010) Science , vol.329 , pp. 1534-1537
    • Zhang, F.1    Saha, S.2    Shabalina, S.A.3    Kashina, A.4
  • 55
    • 0036678475 scopus 로고    scopus 로고
    • Association of PI-3 kinase with PAK1 leads to actin phosphorylation and cytoskeletal reorganization
    • Papakonstanti, E.A.; Stournaras, C. Association of PI-3 kinase with PAK1 leads to actin phosphorylation and cytoskeletal reorganization. Mol. Biol. Cell 2002, 13, 2946-2962.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2946-2962
    • Papakonstanti, E.A.1    Stournaras, C.2
  • 57
    • 52049116495 scopus 로고    scopus 로고
    • Actin motors that drive formation and disassembly of epithelial apical junctions
    • Ivanov, A.I. Actin motors that drive formation and disassembly of epithelial apical junctions. Front. Biosci. 2008, 13, 6662-6681.
    • (2008) Front. Biosci , vol.13 , pp. 6662-6681
    • Ivanov, A.I.1
  • 58
    • 67349086281 scopus 로고    scopus 로고
    • The trip of the tip: Understanding the growth cone machinery
    • Lowery, L.A.; Van Vactor, D. The trip of the tip: Understanding the growth cone machinery. Nat. Rev. Mol. Cell Biol. 2009, 10, 332-343.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 332-343
    • Lowery, L.A.1    van Vactor, D.2
  • 59
    • 0027461117 scopus 로고
    • Cytoplasmic segregation and cytoskeletal organization in the electric catfish giant electromotoneuron with special reference to the axon hillock region
    • Braun, N.; Schikorski, T.; Zimmermann, H. Cytoplasmic segregation and cytoskeletal organization in the electric catfish giant electromotoneuron with special reference to the axon hillock region. Neuroscience 1993, 52, 745-756.
    • (1993) Neuroscience , vol.52 , pp. 745-756
    • Braun, N.1    Schikorski, T.2    Zimmermann, H.3
  • 60
    • 23244440196 scopus 로고    scopus 로고
    • The actin cytoskeleton: Integrating form and function at the synapse
    • Dillon, C.; Goda, Y. The actin cytoskeleton: Integrating form and function at the synapse. Annu. Rev. Neurosci. 2005, 28, 25-55.
    • (2005) Annu. Rev. Neurosci , vol.28 , pp. 25-55
    • Dillon, C.1    Goda, Y.2
  • 61
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: An overview
    • Wade, R.H. On and around microtubules: An overview. Mol. Biotechnol. 2009, 43, 177-191.
    • (2009) Mol. Biotechnol , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 62
    • 33847776094 scopus 로고    scopus 로고
    • Microtubule-organizing centres: A re-evaluation
    • Luders, J.; Stearns, T. Microtubule-organizing centres: A re-evaluation. Nat. Rev. Mol. Cell Biol. 2007, 8, 161-167.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 161-167
    • Luders, J.1    Stearns, T.2
  • 63
    • 33751191831 scopus 로고    scopus 로고
    • Generation of noncentrosomal microtubule arrays
    • Bartolini, F.; Gundersen, G.G. Generation of noncentrosomal microtubule arrays. J. Cell Sci. 2006, 119, 4155-4163.
    • (2006) J. Cell Sci , vol.119 , pp. 4155-4163
    • Bartolini, F.1    Gundersen, G.G.2
  • 64
    • 0742289586 scopus 로고    scopus 로고
    • Microtubule organization and function in epithelial cells
    • Musch, A. Microtubule organization and function in epithelial cells. Traffic 2004, 5, 1-9.
    • (2004) Traffic , vol.5 , pp. 1-9
    • Musch, A.1
  • 65
    • 56349123945 scopus 로고    scopus 로고
    • Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts
    • Meng, W.; Mushika, Y.; Ichii, T.; Takeichi, M. Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts. Cell 2008, 135, 948-959.
    • (2008) Cell , vol.135 , pp. 948-959
    • Meng, W.1    Mushika, Y.2    Ichii, T.3    Takeichi, M.4
  • 66
    • 0029874167 scopus 로고    scopus 로고
    • Centripetal transport of herpes simplex virus in human retinal pigment epithelial cells in vitro
    • Topp, K.S.; Bisla, K.; Saks, N.D.; Lavail, J.H. Centripetal transport of herpes simplex virus in human retinal pigment epithelial cells in vitro. Neuroscience 1996, 71, 1133-1144.
    • (1996) Neuroscience , vol.71 , pp. 1133-1144
    • Topp, K.S.1    Bisla, K.2    Saks, N.D.3    Lavail, J.H.4
  • 67
    • 72149120574 scopus 로고    scopus 로고
    • The microtubule network and neuronal morphogenesis: Dynamic and coordinated orchestration through multiple players
    • Poulain, F.E.; Sobel, A. The microtubule network and neuronal morphogenesis: Dynamic and coordinated orchestration through multiple players. Mol. Cell. Neurosci. 2010, 43, 15-32.
    • (2010) Mol. Cell. Neurosci , vol.43 , pp. 15-32
    • Poulain, F.E.1    Sobel, A.2
  • 68
    • 0028069394 scopus 로고
    • Microtubule polarity in the peripheral processes of trigeminal ganglion cells: Relevance for the retrograde transport of herpes simplex virus
    • Topp, K.S.; Meade, L.B.; LaVail, J.H. Microtubule polarity in the peripheral processes of trigeminal ganglion cells: Relevance for the retrograde transport of herpes simplex virus. J. Neurosci. 1994, 14, 318-325.
    • (1994) J. Neurosci , vol.14 , pp. 318-325
    • Topp, K.S.1    Meade, L.B.2    Lavail, J.H.3
  • 69
    • 34247606028 scopus 로고    scopus 로고
    • Myosin at work: Motor adaptations for a variety of cellular functions
    • O'Connell, C.B.; Tyska, M.J.; Mooseker, M.S. Myosin at work: Motor adaptations for a variety of cellular functions. Biochim. Biophys. Acta 2007, 1773, 615-630.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 615-630
    • O'Connell, C.B.1    Tyska, M.J.2    Mooseker, M.S.3
  • 70
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • De La Cruz, E.M.; Ostap, E.M. Relating biochemistry and function in the myosin superfamily. Curr. Opin. Cell Biol. 2004, 16, 61-67.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 61-67
    • de la Cruz, E.M.1    Ostap, E.M.2
  • 71
    • 0032489872 scopus 로고    scopus 로고
    • Cell crawling: First the motor, now the transmission
    • Heidemann, S.R.; Buxbaum, R.E. Cell crawling: First the motor, now the transmission. J. Cell Biol. 1998, 141, 1-4.
    • (1998) J. Cell Biol , vol.141 , pp. 1-4
    • Heidemann, S.R.1    Buxbaum, R.E.2
  • 72
    • 77954237525 scopus 로고    scopus 로고
    • Unconventional processive mechanics of non-muscle myosin IIB
    • Norstrom, M.F.; Smithback, P.A.; Rock, R.S. Unconventional processive mechanics of non-muscle myosin IIB. J. Biol. Chem. 2010, 285, 26326-26334.
    • (2010) J. Biol. Chem , vol.285 , pp. 26326-26334
    • Norstrom, M.F.1    Smithback, P.A.2    Rock, R.S.3
  • 74
    • 1642448472 scopus 로고    scopus 로고
    • Functional divergence of human cytoplasmic myosin II: Kinetic characterization of the non-muscle IIA isoform
    • Kovacs, M.; Wang, F.; Hu, A.; Zhang, Y.; Sellers, J.R. Functional divergence of human cytoplasmic myosin II: Kinetic characterization of the non-muscle IIA isoform. J. Biol. Chem. 2003, 278, 38132-38140.
    • (2003) J. Biol. Chem , vol.278 , pp. 38132-38140
    • Kovacs, M.1    Wang, F.2    Hu, A.3    Zhang, Y.4    Sellers, J.R.5
  • 76
    • 0032410805 scopus 로고    scopus 로고
    • The case for a common ancestor: Kinesin and myosin motor proteins and G proteins
    • Kull, F.J.; Vale, R.D.; Fletterick, R.J. The case for a common ancestor: Kinesin and myosin motor proteins and G proteins. J. Muscle Res. Cell Motil. 1998, 19, 877-886.
    • (1998) J. Muscle Res. Cell Motil , vol.19 , pp. 877-886
    • Kull, F.J.1    Vale, R.D.2    Fletterick, R.J.3
  • 78
    • 24344465919 scopus 로고    scopus 로고
    • Analysis of the kinesin superfamily: Insights into structure and function
    • Miki, H.; Okada, Y.; Hirokawa, N. Analysis of the kinesin superfamily: Insights into structure and function. Trends Cell Biol. 2005, 15, 467-476.
    • (2005) Trends Cell Biol , vol.15 , pp. 467-476
    • Miki, H.1    Okada, Y.2    Hirokawa, N.3
  • 81
    • 0037462770 scopus 로고    scopus 로고
    • Characterization of the movement of the kinesin motor KIF1A in living cultured neurons
    • Lee, J.R.; Shin, H.; Ko, J.; Choi, J.; Lee, H.; Kim, E. Characterization of the movement of the kinesin motor KIF1A in living cultured neurons. J. Biol. Chem. 2003, 278, 2624-2629.
    • (2003) J. Biol. Chem , vol.278 , pp. 2624-2629
    • Lee, J.R.1    Shin, H.2    Ko, J.3    Choi, J.4    Lee, H.5    Kim, E.6
  • 82
    • 55549134618 scopus 로고    scopus 로고
    • KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD
    • Niwa, S.; Tanaka, Y.; Hirokawa, N. KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD. Nat. Cell Biol. 2008, 10, 1269-1279.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1269-1279
    • Niwa, S.1    Tanaka, Y.2    Hirokawa, N.3
  • 83
    • 0030939131 scopus 로고    scopus 로고
    • KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles
    • Saito, N.; Okada, Y.; Noda, Y.; Kinoshita, Y.; Kondo, S.; Hirokawa, N. KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles. Neuron 1997, 18, 425-438.
    • (1997) Neuron , vol.18 , pp. 425-438
    • Saito, N.1    Okada, Y.2    Noda, Y.3    Kinoshita, Y.4    Kondo, S.5    Hirokawa, N.6
  • 84
    • 0035132691 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of mouse C-terminal kinesin motor KifC3
    • Yang, Z.; Xia, C.; Roberts, E.A.; Bush, K.; Nigam, S.K.; Goldstein, L.S. Molecular cloning and functional analysis of mouse C-terminal kinesin motor KifC3. Mol. Cell Biol. 2001, 21, 765-770.
    • (2001) Mol. Cell Biol , vol.21 , pp. 765-770
    • Yang, Z.1    Xia, C.2    Roberts, E.A.3    Bush, K.4    Nigam, S.K.5    Goldstein, L.S.6
  • 85
    • 0030888785 scopus 로고    scopus 로고
    • Characterization of KIFC2, a neuronal kinesin superfamily member in mouse
    • Hanlon, D.W.; Yang, Z.; Goldstein, L.S. Characterization of KIFC2, a neuronal kinesin superfamily member in mouse. Neuron 1997, 18, 439-451.
    • (1997) Neuron , vol.18 , pp. 439-451
    • Hanlon, D.W.1    Yang, Z.2    Goldstein, L.S.3
  • 86
    • 78951491641 scopus 로고    scopus 로고
    • The kinesin superfamily protein KIF17 is regulated by the same transcription factor (NRF-1) as its cargo NR2B in neurons
    • Dhar, S.S.; Wong-Riley, M.T. The kinesin superfamily protein KIF17 is regulated by the same transcription factor (NRF-1) as its cargo NR2B in neurons. Biochim. Biophys. Acta 2011, 1813, 403-411.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 403-411
    • Dhar, S.S.1    Wong-Riley, M.T.2
  • 87
    • 36249016834 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a molecular adaptor between the neurospecific KIF3C kinesin and dendritic RNA granules
    • Davidovic, L.; Jaglin, X.H.; Lepagnol-Bestel, A.M.; Tremblay, S.; Simonneau, M.; Bardoni, B.; Khandjian, E.W. The fragile X mental retardation protein is a molecular adaptor between the neurospecific KIF3C kinesin and dendritic RNA granules. Hum. Mol. Genet. 2007, 16, 3047-3058.
    • (2007) Hum. Mol. Genet , vol.16 , pp. 3047-3058
    • Davidovic, L.1    Jaglin, X.H.2    Lepagnol-Bestel, A.M.3    Tremblay, S.4    Simonneau, M.5    Bardoni, B.6    Khandjian, E.W.7
  • 89
    • 33751572018 scopus 로고    scopus 로고
    • Cargo selection by specific kinesin light chain 1 isoforms
    • Wozniak, M.J.; Allan, V.J. Cargo selection by specific kinesin light chain 1 isoforms. EMBO J. 2006, 25, 5457-5468.
    • (2006) EMBO J , vol.25 , pp. 5457-5468
    • Wozniak, M.J.1    Allan, V.J.2
  • 90
    • 0035954436 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport
    • Tai, A.W.; Chuang, J.Z.; Sung, C.H. Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport. J. Cell Biol. 2001, 153, 1499-1509.
    • (2001) J. Cell Biol , vol.153 , pp. 1499-1509
    • Tai, A.W.1    Chuang, J.Z.2    Sung, C.H.3
  • 91
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King, S.J.; Schroer, T.A. Dynactin increases the processivity of the cytoplasmic dynein motor. Nat. Cell Biol. 2000, 2, 20-24.
    • (2000) Nat. Cell Biol , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 96
    • 33749015997 scopus 로고    scopus 로고
    • Microtubule motors at the intersection of trafficking and transport
    • Caviston, J.P.; Holzbaur, E.L. Microtubule motors at the intersection of trafficking and transport. Trends Cell Biol. 2006, 16, 530-537.
    • (2006) Trends Cell Biol , vol.16 , pp. 530-537
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 97
    • 0034046190 scopus 로고    scopus 로고
    • Luminal and basolateral membrane transport of glutathione in isolated perfused S(1), S(2), and S(3) segments of the rabbit proximal tubule
    • Parks, L.D.; Zalups, R.K.; Barfuss, D.W. Luminal and basolateral membrane transport of glutathione in isolated perfused S(1), S(2), and S(3) segments of the rabbit proximal tubule. J. Am. Soc. Nephrol. 2000, 11, 1008-1015.
    • (2000) J. Am. Soc. Nephrol , vol.11 , pp. 1008-1015
    • Parks, L.D.1    Zalups, R.K.2    Barfuss, D.W.3
  • 98
    • 0030984076 scopus 로고    scopus 로고
    • Kinesin- and myosin-driven steps of vesicle recruitment for Ca2+-regulated exocytosis
    • Bi, G.Q.; Morris, R.L.; Liao, G.; Alderton, J.M.; Scholey, J.M.; Steinhardt, R.A. Kinesin- and myosin-driven steps of vesicle recruitment for Ca2+-regulated exocytosis. J. Cell Biol. 1997, 138, 999-1008.
    • (1997) J. Cell Biol , vol.138 , pp. 999-1008
    • Bi, G.Q.1    Morris, R.L.2    Liao, G.3    Alderton, J.M.4    Scholey, J.M.5    Steinhardt, R.A.6
  • 99
    • 0034169041 scopus 로고    scopus 로고
    • Vesicular transport as a new paradigm in short-term regulation of transepithelial transport
    • Park, C.S.; Leem, C.H.; Jang, Y.J.; Shim, Y.H. Vesicular transport as a new paradigm in short-term regulation of transepithelial transport. J. Korean Med. Sci. 2000, 15, 123-132.
    • (2000) J. Korean Med. Sci , vol.15 , pp. 123-132
    • Park, C.S.1    Leem, C.H.2    Jang, Y.J.3    Shim, Y.H.4
  • 100
    • 0035812652 scopus 로고    scopus 로고
    • Dynamics and cooperativity of microtubule decoration by the motor protein kinesin
    • Vilfan, A.; Frey, E.; Schwabl, F.; Thormahlen, M.; Song, Y.H.; Mandelkow, E. Dynamics and cooperativity of microtubule decoration by the motor protein kinesin. J. Mol. Biol. 2001, 312, 1011-1026.
    • (2001) J. Mol. Biol , vol.312 , pp. 1011-1026
    • Vilfan, A.1    Frey, E.2    Schwabl, F.3    Thormahlen, M.4    Song, Y.H.5    Mandelkow, E.6
  • 101
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
    • Kural, C.; Kim, H.; Syed, S.; Goshima, G.; Gelfand, V.I.; Selvin, P.R. Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement? Science 2005, 308, 1469-1472.
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1    Kim, H.2    Syed, S.3    Goshima, G.4    Gelfand, V.I.5    Selvin, P.R.6
  • 102
    • 14744280774 scopus 로고    scopus 로고
    • Long-range cooperative binding of kinesin to a microtubule in the presence of ATP
    • Muto, E.; Sakai, H.; Kaseda, K. Long-range cooperative binding of kinesin to a microtubule in the presence of ATP. J. Cell Biol. 2005, 168, 691-696.
    • (2005) J. Cell Biol , vol.168 , pp. 691-696
    • Muto, E.1    Sakai, H.2    Kaseda, K.3
  • 103
    • 0029757282 scopus 로고    scopus 로고
    • Binding sites on microtubules of kinesin motors of the same or opposite polarity
    • Song, H.; Endow, S.A. Binding sites on microtubules of kinesin motors of the same or opposite polarity. Biochemistry 1996, 35, 11203-11209.
    • (1996) Biochemistry , vol.35 , pp. 11203-11209
    • Song, H.1    Endow, S.A.2
  • 105
  • 106
    • 0035104723 scopus 로고    scopus 로고
    • Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids
    • Muresan, V.; Stankewich, M.C.; Steffen, W.; Morrow, J.S.; Holzbaur, E.L.; Schnapp, B.J. Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids. Mol. Cell 2001, 7, 173-183.
    • (2001) Mol. Cell , vol.7 , pp. 173-183
    • Muresan, V.1    Stankewich, M.C.2    Steffen, W.3    Morrow, J.S.4    Holzbaur, E.L.5    Schnapp, B.J.6
  • 108
    • 0037447054 scopus 로고    scopus 로고
    • Dynactin: Coordinating motors with opposite inclinations
    • Gross, S.P. Dynactin: coordinating motors with opposite inclinations. Curr. Biol. 2003, 13, R320-R322.
    • (2003) Curr. Biol , vol.13
    • Gross, S.P.1
  • 111
    • 2342640469 scopus 로고    scopus 로고
    • A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity
    • Ligon, L.A.; Tokito, M.; Finklestein, J.M.; Grossman, F.E.; Holzbaur, E.L. A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity. J. Biol. Chem. 2004, 279, 19201-19208.
    • (2004) J. Biol. Chem , vol.279 , pp. 19201-19208
    • Ligon, L.A.1    Tokito, M.2    Finklestein, J.M.3    Grossman, F.E.4    Holzbaur, E.L.5
  • 112
    • 77955057326 scopus 로고    scopus 로고
    • Linking molecular motors to membrane cargo
    • Akhmanova, A.; Hammer, J.A., Linking molecular motors to membrane cargo. Curr. Opin. Cell Biol. 2010, 22, 479-487.
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 479-487
    • Akhmanova, A.1    Hammer, J.A.2
  • 113
    • 70350446761 scopus 로고    scopus 로고
    • Traffic control: Regulation of kinesin motors
    • Verhey, K.J.; Hammond, J.W. Traffic control: Regulation of kinesin motors. Nat. Rev. Mol. Cell Biol. 2009, 10, 765-777.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 765-777
    • Verhey, K.J.1    Hammond, J.W.2
  • 114
    • 0030921711 scopus 로고    scopus 로고
    • Brain myosin is a synaptic vesicle-associated motor protein: Evidence for a Ca2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • Prekeris, R.; Terrian, D.M. Brain myosin V is a synaptic vesicle-associated motor protein: Evidence for a Ca2+-dependent interaction with the synaptobrevin-synaptophysin complex. J. Cell Biol. 1997, 137, 1589-1601.
    • (1997) J. Cell Biol , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 116
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • Hoppe, T.; Cassata, G.; Barral, J.M.; Springer, W.; Hutagalung, A.H.; Epstein, H.F.; Baumeister, R. Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans. Cell 2004, 118, 337-349.
    • (2004) Cell , vol.118 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6    Baumeister, R.7
  • 118
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode, B.L.; Drubin, D.G.; Barnes, G. Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 2000, 12, 63-71.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 119
    • 0028236443 scopus 로고
    • Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B
    • Herold, B.C.; Visalli, R.J.; Susmarski, N.; Brandt, C.R.; Spear, P.G. Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B. J. Gen. Virol. 1994, 75, 1211-1222.
    • (1994) J. Gen. Virol , vol.75 , pp. 1211-1222
    • Herold, B.C.1    Visalli, R.J.2    Susmarski, N.3    Brandt, C.R.4    Spear, P.G.5
  • 120
    • 0026026623 scopus 로고
    • Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity
    • Herold, B.C.; WuDunn, D.; Soltys, N.; Spear, P.G. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 1991, 65, 1090-1098.
    • (1991) J. Virol , vol.65 , pp. 1090-1098
    • Herold, B.C.1    Wudunn, D.2    Soltys, N.3    Spear, P.G.4
  • 121
    • 0026308922 scopus 로고
    • Involvement of glycoprotein C (gC) in adsorption of herpes simplex virus type 1 (HSV-1) to the cell
    • Svennerholm, B.; Jeansson, S.; Vahlne, A.; Lycke, E. Involvement of glycoprotein C (gC) in adsorption of herpes simplex virus type 1 (HSV-1) to the cell. Arch. Virol. 1991, 120, 273-279.
    • (1991) Arch. Virol , vol.120 , pp. 273-279
    • Svennerholm, B.1    Jeansson, S.2    Vahlne, A.3    Lycke, E.4
  • 122
    • 55249089044 scopus 로고    scopus 로고
    • Structural rearrangement within an enveloped virus upon binding to the host cell
    • Meckes, D.G., Jr.; Wills, J.W. Structural rearrangement within an enveloped virus upon binding to the host cell. J. Virol. 2008, 82, 10429-10435.
    • (2008) J. Virol , vol.82 , pp. 10429-10435
    • Meckes Jr., D.G.1    Wills, J.W.2
  • 123
    • 0037345386 scopus 로고    scopus 로고
    • A role for glycoprotein C in pseudorabies virus entry that is independent of virus attachment to heparan sulfate and which involves the actin cytoskeleton
    • Rue, C.A.; Ryan, P. A role for glycoprotein C in pseudorabies virus entry that is independent of virus attachment to heparan sulfate and which involves the actin cytoskeleton. Virology 2003, 307, 12-21.
    • (2003) Virology , vol.307 , pp. 12-21
    • Rue, C.A.1    Ryan, P.2
  • 126
    • 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
  • 127
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C.D.; Hall, A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 128
    • 78650070161 scopus 로고    scopus 로고
    • Phosphoinositide 3 kinase signalling may affect multiple steps during herpes simplex virus type-1 entry
    • Tiwari, V.; Shukla, D. Phosphoinositide 3 kinase signalling may affect multiple steps during herpes simplex virus type-1 entry. J. Gen. Virol. 2010, 91, 3002-3009.
    • (2010) J. Gen. Virol , vol.91 , pp. 3002-3009
    • Tiwari, V.1    Shukla, D.2
  • 129
    • 0037184967 scopus 로고    scopus 로고
    • Trans-interactions of nectins induce formation of filopodia and Lamellipodia through the respective activation of Cdc42 and Rac small G proteins
    • Kawakatsu, T.; Shimizu, K.; Honda, T.; Fukuhara, T.; Hoshino, T.; Takai, Y. Trans-interactions of nectins induce formation of filopodia and Lamellipodia through the respective activation of Cdc42 and Rac small G proteins. J. Biol. Chem. 2002, 277, 50749-50755.
    • (2002) J. Biol. Chem , vol.277 , pp. 50749-50755
    • Kawakatsu, T.1    Shimizu, K.2    Honda, T.3    Fukuhara, T.4    Hoshino, T.5    Takai, Y.6
  • 130
    • 14444271574 scopus 로고    scopus 로고
    • Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction
    • Mandai, K.; Nakanishi, H.; Satoh, A.; Obaishi, H.; Wada, M.; Nishioka, H.; Itoh, M.; Mizoguchi, A.; Aoki, T.; Fujimoto, T., et al. Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction. J. Cell Biol. 1997, 139, 517-528.
    • (1997) J. Cell Biol , vol.139 , pp. 517-528
    • Mandai, K.1    Nakanishi, H.2    Satoh, A.3    Obaishi, H.4    Wada, M.5    Nishioka, H.6    Itoh, M.7    Mizoguchi, A.8    Aoki, T.9    Fujimoto, T.10
  • 131
    • 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
  • 132
    • 0015302546 scopus 로고
    • Proteins specified by herpes simplex virus. VI. Viral proteins in the plasma membrane
    • Heine, J.W.; Spear, P.G.; Roizman, B. Proteins specified by herpes simplex virus. VI. Viral proteins in the plasma membrane. J. Virol. 1972, 9, 431-439.
    • (1972) J. Virol , vol.9 , pp. 431-439
    • Heine, J.W.1    Spear, P.G.2    Roizman, B.3
  • 133
    • 77956643036 scopus 로고    scopus 로고
    • Virus cell-to-cell transmission
    • Mothes, W.; Sherer, N.M.; Jin, J.; Zhong, P. Virus cell-to-cell transmission. J. Virol. 2010, 84, 8360-8368.
    • (2010) J. Virol , vol.84 , pp. 8360-8368
    • Mothes, W.1    Sherer, N.M.2    Jin, J.3    Zhong, P.4
  • 134
    • 66149103595 scopus 로고    scopus 로고
    • The virological synapse facilitates herpes simplex virus entry into T cells
    • Aubert, M.; Yoon, M.; Sloan, D.D.; Spear, P.G.; Jerome, K.R. The virological synapse facilitates herpes simplex virus entry into T cells. J. Virol. 2009, 83, 6171-6183.
    • (2009) J. Virol , vol.83 , pp. 6171-6183
    • Aubert, M.1    Yoon, M.2    Sloan, D.D.3    Spear, P.G.4    Jerome, K.R.5
  • 136
    • 0022521899 scopus 로고
    • Pseudorabies virus gene encoding glycoprotein gIII is not essential for growth in tissue culture
    • Robbins, A.K.; Whealy, M.E.; Watson, R.J.; Enquist, L.W. Pseudorabies virus gene encoding glycoprotein gIII is not essential for growth in tissue culture. J. Virol. 1986, 59, 635-645.
    • (1986) J. Virol , vol.59 , pp. 635-645
    • Robbins, A.K.1    Whealy, M.E.2    Watson, R.J.3    Enquist, L.W.4
  • 137
    • 0030589196 scopus 로고    scopus 로고
    • The UL 16 gene product of herpes simplex virus 1 is a virion protein that colocalizes with intranuclear capsid proteins
    • Nalwanga, D.; Rempel, S.; Roizman, B.; Baines, J.D. The UL 16 gene product of herpes simplex virus 1 is a virion protein that colocalizes with intranuclear capsid proteins. Virology 1996, 226, 236-242.
    • (1996) Virology , vol.226 , pp. 236-242
    • Nalwanga, D.1    Rempel, S.2    Roizman, B.3    Baines, J.D.4
  • 138
    • 0031746910 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins B and C, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread
    • Laquerre, S.; Argnani, R.; Anderson, D.B.; Zucchini, S.; Manservigi, R.; Glorioso, J.C. Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins B and C, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread. J. Virol. 1998, 72, 6119-6130.
    • (1998) J. Virol , vol.72 , pp. 6119-6130
    • Laquerre, S.1    Argnani, R.2    Anderson, D.B.3    Zucchini, S.4    Manservigi, R.5    Glorioso, J.C.6
  • 139
    • 0020666899 scopus 로고
    • Antigenic variants of herpes simplex virus selected with glycoprotein-specific monoclonal antibodies
    • Holland, T.C.; Marlin, S.D.; Levine, M.; Glorioso, J. Antigenic variants of herpes simplex virus selected with glycoprotein-specific monoclonal antibodies. J. Virol. 1983, 45, 672-682.
    • (1983) J. Virol , vol.45 , pp. 672-682
    • Holland, T.C.1    Marlin, S.D.2    Levine, M.3    Glorioso, J.4
  • 140
    • 0018355420 scopus 로고
    • Molecular genetics of herpes simplex virus. II. Mapping of the major viral glycoproteins and of the genetic loci specifying the social behavior of infected cells
    • Ruyechan, W.T.; Morse, L.S.; Knipe, D.M.; Roizman, B. Molecular genetics of herpes simplex virus. II. Mapping of the major viral glycoproteins and of the genetic loci specifying the social behavior of infected cells. J. Virol. 1979, 29, 677-697.
    • (1979) J. Virol , vol.29 , pp. 677-697
    • Ruyechan, W.T.1    Morse, L.S.2    Knipe, D.M.3    Roizman, B.4
  • 141
    • 0026053928 scopus 로고
    • The open reading frames UL3, UL4, UL10, and UL16 are dispensable for the replication of herpes simplex virus 1 in cell culture
    • Baines, J.D.; Roizman, B. The open reading frames UL3, UL4, UL10, and UL16 are dispensable for the replication of herpes simplex virus 1 in cell culture. J. Virol. 1991, 65, 938-944.
    • (1991) J. Virol , vol.65 , pp. 938-944
    • Baines, J.D.1    Roizman, B.2
  • 142
    • 0021808063 scopus 로고
    • Inhibition of herpes simplex virus type 1 penetration by cytochalasins B and D
    • Rosenthal, K.S.; Perez, R.; Hodnichak, C. Inhibition of herpes simplex virus type 1 penetration by cytochalasins B and D. J. Gen. Virol. 1985, 66, 1601-1605.
    • (1985) J. Gen. Virol , vol.66 , pp. 1601-1605
    • Rosenthal, K.S.1    Perez, R.2    Hodnichak, C.3
  • 143
    • 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
  • 144
    • 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
  • 145
    • 0023772685 scopus 로고
    • Herpes simplex virus infection of the human sensory neuron. An electron microscopy study
    • Lycke, E.; Hamark, B.; Johansson, M.; Krotochwil, A.; Lycke, J.; Svennerholm, B. Herpes simplex virus infection of the human sensory neuron. An electron microscopy study. Arch. Virol. 1988, 101, 87-104.
    • (1988) Arch. Virol , vol.101 , pp. 87-104
    • Lycke, E.1    Hamark, B.2    Johansson, M.3    Krotochwil, A.4    Lycke, J.5    Svennerholm, B.6
  • 146
    • 48749114826 scopus 로고    scopus 로고
    • Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry
    • Maurer, U.E.; Sodeik, B.; Grunewald, K. Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry. Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 10559-10564.
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grunewald, K.3
  • 147
    • 18744382150 scopus 로고    scopus 로고
    • Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1
    • Milne, R.S.; Nicola, A.V.; Whitbeck, J.C.; Eisenberg, R.J.; Cohen, G.H. Glycoprotein D receptor-dependent, low-pH-independent endocytic entry of herpes simplex virus type 1. J. Virol. 2005, 79, 6655-6663.
    • (2005) J. Virol , vol.79 , pp. 6655-6663
    • Milne, R.S.1    Nicola, A.V.2    Whitbeck, J.C.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 148
    • 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
  • 149
    • 0027473609 scopus 로고
    • Envelope glycoprotein gp50 of pseudorabies virus is essential for virus entry but is not required for viral spread in mice
    • Peeters, B.; Pol, J.; Gielkens, A.; Moormann, R. Envelope glycoprotein gp50 of pseudorabies virus is essential for virus entry but is not required for viral spread in mice. J. Virol. 1993, 67, 170-177.
    • (1993) J. Virol , vol.67 , pp. 170-177
    • Peeters, B.1    Pol, J.2    Gielkens, A.3    Moormann, R.4
  • 150
    • 0025165552 scopus 로고
    • Evolutionary relationships of virion glycoprotein genes in the S regions of alphaherpesvirus genomes
    • McGeoch, D.J. Evolutionary relationships of virion glycoprotein genes in the S regions of alphaherpesvirus genomes. J. Gen. Virol. 1990, 71, 2361-2367.
    • (1990) J. Gen. Virol , vol.71 , pp. 2361-2367
    • McGeoch, D.J.1
  • 151
    • 0027534495 scopus 로고
    • Glycoprotein gp50-negative pseudorabies virus: A novel approach toward a nonspreading live herpesvirus vaccine
    • Heffner, S.; Kovacs, F.; Klupp, B.G.; Mettenleiter, T.C. Glycoprotein gp50-negative pseudorabies virus: A novel approach toward a nonspreading live herpesvirus vaccine. J. Virol. 1993, 67, 1529-1537.
    • (1993) J. Virol , vol.67 , pp. 1529-1537
    • Heffner, S.1    Kovacs, F.2    Klupp, B.G.3    Mettenleiter, T.C.4
  • 152
    • 0028819214 scopus 로고
    • Role of glycoprotein gD in the adhesion of pseudorabies virus infected cells and subsequent cell-associated virus spread
    • Hanssens, F.P.; Nauwynck, H.J.; Mettenlieter, T.C. Role of glycoprotein gD in the adhesion of pseudorabies virus infected cells and subsequent cell-associated virus spread. Arch. Virol. 1995, 140, 1855-1862.
    • (1995) Arch. Virol , vol.140 , pp. 1855-1862
    • Hanssens, F.P.1    Nauwynck, H.J.2    Mettenlieter, T.C.3
  • 153
    • 60249087808 scopus 로고    scopus 로고
    • HSV-1 infection through inhibitory receptor, PILRalpha
    • Satoh, T.; Arase, H. HSV-1 infection through inhibitory receptor, PILRalpha. Uirusu 2008, 58, 27-36.
    • (2008) Uirusu , vol.58 , pp. 27-36
    • Satoh, T.1    Arase, H.2
  • 156
    • 0034254317 scopus 로고    scopus 로고
    • FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells
    • Fournier, N.; Chalus, L.; Durand, I.; Garcia, E.; Pin, J.J.; Churakova, T.; Patel, S.; Zlot, C.; Gorman, D.; Zurawski, S, et al. FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells. J. Immunol. 2000, 165, 1197-1209.
    • (2000) J. Immunol , vol.165 , pp. 1197-1209
    • Fournier, N.1    Chalus, L.2    Durand, I.3    Garcia, E.4    Pin, J.J.5    Churakova, T.6    Patel, S.7    Zlot, C.8    Gorman, D.9    Zurawski, S.10
  • 157
    • 34248189845 scopus 로고    scopus 로고
    • Comparative analysis of the paired immunoglobulin-like receptor (PILR) locus in six mammalian genomes: Duplication, conversion, and the birth of new genes
    • Wilson, M.D.; Cheung, J.; Martindale, D.W.; Scherer, S.W.; Koop, B.F. Comparative analysis of the paired immunoglobulin-like receptor (PILR) locus in six mammalian genomes: Duplication, conversion, and the birth of new genes. Physiol. Genom. 2006, 27, 201-218.
    • (2006) Physiol. Genom , vol.27 , pp. 201-218
    • Wilson, M.D.1    Cheung, J.2    Martindale, D.W.3    Scherer, S.W.4    Koop, B.F.5
  • 158
    • 66849099168 scopus 로고    scopus 로고
    • Role of nectin-1, HVEM, and PILR-alpha in HSV-2 entry into human retinal pigment epithelial cells
    • Shukla, S.Y.; Singh, Y.K.; Shukla, D. Role of nectin-1, HVEM, and PILR-alpha in HSV-2 entry into human retinal pigment epithelial cells. Invest. Ophthalmol. Vis. Sci. 2009, 50, 2878-2887.
    • (2009) Invest. Ophthalmol. Vis. Sci , vol.50 , pp. 2878-2887
    • Shukla, S.Y.1    Singh, Y.K.2    Shukla, D.3
  • 159
    • 53049094647 scopus 로고    scopus 로고
    • Human papillomavirus type 16 entry: Retrograde cell surface transport along actin-rich protrusions
    • Schelhaas, M.; Ewers, H.; Rajamaki, M.L.; Day, P.M.; Schiller, J.T.; Helenius, A. Human papillomavirus type 16 entry: Retrograde cell surface transport along actin-rich protrusions. PLoS Pathog. 2008, 4, e1000148.
    • (2008) PLoS Pathog , vol.4
    • Schelhaas, M.1    Ewers, H.2    Rajamaki, M.L.3    Day, P.M.4    Schiller, J.T.5    Helenius, A.6
  • 162
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T.; Chen, X.Q.; Manser, E.; Lim, L. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell Biol. 1996, 16, 5313-5327.
    • (1996) Mol. Cell Biol , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 163
    • 0033864069 scopus 로고    scopus 로고
    • Y-27632, an inhibitor of rho-associated protein kinase, suppresses tumor cell invasion via regulation of focal adhesion and focal adhesion kinase
    • Imamura, F.; Mukai, M.; Ayaki, M.; Akedo, H. Y-27632, an inhibitor of rho-associated protein kinase, suppresses tumor cell invasion via regulation of focal adhesion and focal adhesion kinase. Jpn. J. Cancer Res. 2000, 91, 811-816.
    • (2000) Jpn. J. Cancer Res , vol.91 , pp. 811-816
    • Imamura, F.1    Mukai, M.2    Ayaki, M.3    Akedo, H.4
  • 164
    • 24744464366 scopus 로고    scopus 로고
    • Focal adhesion kinase plays a pivotal role in herpes simplex virus entry
    • Cheshenko, N.; Liu, W.; Satlin, L.M.; Herold, B.C. Focal adhesion kinase plays a pivotal role in herpes simplex virus entry. J. Biol. Chem. 2005, 280, 31116-31125.
    • (2005) J. Biol. Chem , vol.280 , pp. 31116-31125
    • Cheshenko, N.1    Liu, W.2    Satlin, L.M.3    Herold, B.C.4
  • 165
    • 35148822681 scopus 로고    scopus 로고
    • Equine herpesvirus 1 enters cells by two different pathways, and infection requires the activation of the cellular kinase ROCK1
    • Frampton, A.R., Jr.; Stolz, D.B.; Uchida, H.; Goins, W.F.; Cohen, J.B.; Glorioso, J.C. Equine herpesvirus 1 enters cells by two different pathways, and infection requires the activation of the cellular kinase ROCK1. J. Virol. 2007, 81, 10879-10889.
    • (2007) J. Virol , vol.81 , pp. 10879-10889
    • Frampton Jr., A.R.1    Stolz, D.B.2    Uchida, H.3    Goins, W.F.4    Cohen, J.B.5    Glorioso, J.C.6
  • 166
    • 70349795535 scopus 로고    scopus 로고
    • Infectious entry of equine herpesvirus-1 into host cells through different endocytic pathways
    • Hasebe, R.; Sasaki, M.; Sawa, H.; Wada, R.; Umemura, T.; Kimura, T. Infectious entry of equine herpesvirus-1 into host cells through different endocytic pathways. Virology 2009, 393, 198-209.
    • (2009) Virology , vol.393 , pp. 198-209
    • Hasebe, R.1    Sasaki, M.2    Sawa, H.3    Wada, R.4    Umemura, T.5    Kimura, T.6
  • 167
    • 0037113074 scopus 로고    scopus 로고
    • Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton
    • Mundy, D.I.; Machleidt, T.; Ying, Y.S.; Anderson, R.G.; Bloom, G.S. Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton. J. Cell Sci. 2002, 115, 4327-4339.
    • (2002) J. Cell Sci , vol.115 , pp. 4327-4339
    • Mundy, D.I.1    Machleidt, T.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 168
  • 169
    • 33750728629 scopus 로고    scopus 로고
    • Two modes of herpesvirus trafficking in neurons: Membrane acquisition directs motion
    • Antinone, S.E.; Smith, G.A. Two modes of herpesvirus trafficking in neurons: Membrane acquisition directs motion. J. Virol. 2006, 80, 11235-11240.
    • (2006) J. Virol , vol.80 , pp. 11235-11240
    • Antinone, S.E.1    Smith, G.A.2
  • 170
    • 0024400607 scopus 로고
    • Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration
    • Fuller, A.O.; Santos, R.E.; Spear, P.G. Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration. J. Virol. 1989, 63, 3435-3443.
    • (1989) J. Virol , vol.63 , pp. 3435-3443
    • Fuller, A.O.1    Santos, R.E.2    Spear, P.G.3
  • 171
    • 0023388477 scopus 로고
    • Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface
    • Fuller, A.O.; Spear, P.G. Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface. Proc. Natl. Acad. Sci. U. S. A. 1987, 84, 5454-5458.
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 5454-5458
    • Fuller, A.O.1    Spear, P.G.2
  • 172
    • 0021320804 scopus 로고
    • Uptake and transport of herpes simplex virus in neurites of rat dorsal root ganglia cells in culture
    • Lycke, E.; Kristensson, K.; Svennerholm, B.; Vahlne, A.; Ziegler, R. Uptake and transport of herpes simplex virus in neurites of rat dorsal root ganglia cells in culture. J. Gen. Virol. 1984, 65, 55-64.
    • (1984) J. Gen. Virol , vol.65 , pp. 55-64
    • Lycke, E.1    Kristensson, K.2    Svennerholm, B.3    Vahlne, A.4    Ziegler, R.5
  • 173
    • 0014281593 scopus 로고
    • Electron microscopy of herpes simplex virus
    • Morgan, C.; Rose, H.M.; Mednis, B. Electron microscopy of herpes simplex virus. I. Entry. J. Virol. 1968, 2, 507-516.
    • (1968) I. Entry. J. Virol , vol.2 , pp. 507-516
    • Morgan, C.1    Rose, H.M.2    Mednis, B.3
  • 174
    • 0016293618 scopus 로고
    • Herpes simplex virus and human cytomegalovirus replication in WI-38 cells. II. An ultrastructural study of viral penetration
    • Smith, J.D.; de Harven, E. Herpes simplex virus and human cytomegalovirus replication in WI-38 cells. II. An ultrastructural study of viral penetration. J. Virol. 1974, 14, 945-956.
    • (1974) J. Virol , vol.14 , pp. 945-956
    • Smith, J.D.1    de Harven, E.2
  • 175
    • 13944272582 scopus 로고    scopus 로고
    • Entry of pseudorabies virus: An immunogold-labeling study
    • Granzow, H.; Klupp, B.G.; Mettenleiter, T.C. Entry of pseudorabies virus: An immunogold-labeling study. J. Virol. 2005, 79, 3200-3205.
    • (2005) J. Virol , vol.79 , pp. 3200-3205
    • Granzow, H.1    Klupp, B.G.2    Mettenleiter, T.C.3
  • 176
    • 17644404401 scopus 로고    scopus 로고
    • Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins
    • Luxton, G.W.; Haverlock, S.; Coller, K.E.; Antinone, S.E.; Pincetic, A.; Smith, G.A. Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins. Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 5832-5837.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 5832-5837
    • Luxton, G.W.1    Haverlock, S.2    Coller, K.E.3    Antinone, S.E.4    Pincetic, A.5    Smith, G.A.6
  • 177
    • 73949125038 scopus 로고    scopus 로고
    • Retrograde axon transport of herpes simplex virus and pseudorabies virus: A live-cell comparative analysis
    • Antinone, S.E.; Smith, G.A. Retrograde axon transport of herpes simplex virus and pseudorabies virus: a live-cell comparative analysis. J. Virol. 2010, 84, 1504-1512.
    • (2010) J. Virol , vol.84 , pp. 1504-1512
    • Antinone, S.E.1    Smith, G.A.2
  • 178
    • 49749129617 scopus 로고    scopus 로고
    • Two viral kinases are required for sustained long distance axon transport of a neuroinvasive herpesvirus
    • Coller, K.E.; Smith, G.A. Two viral kinases are required for sustained long distance axon transport of a neuroinvasive herpesvirus. Traffic 2008, 9, 1458-1470.
    • (2008) Traffic , vol.9 , pp. 1458-1470
    • Coller, K.E.1    Smith, G.A.2
  • 179
    • 0022531958 scopus 로고
    • Neuritic transport of herpes simplex virus in rat sensory neurons in vitro. Effects of substances interacting with microtubular function and axonal flow [nocodazole, taxol and erythro-9-3-(2-hydroxynonyl)adenine]
    • Kristensson, K.; Lycke, E.; Roytta, M.; Svennerholm, B.; Vahlne, A. Neuritic transport of herpes simplex virus in rat sensory neurons in vitro. Effects of substances interacting with microtubular function and axonal flow [nocodazole, taxol and erythro-9-3-(2-hydroxynonyl)adenine]. J. Gen. Virol. 1986, 67, 2023-2028.
    • (1986) J. Gen. Virol , vol.67 , pp. 2023-2028
    • Kristensson, K.1    Lycke, E.2    Roytta, M.3    Svennerholm, B.4    Vahlne, A.5
  • 180
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao, R.; Antony, C.; Dotti, C.; Karsenti, E.; Stelzer, E.H.; Simons, K. The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 1989, 109, 2817-2832.
    • (1989) J. Cell Biol , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.5    Simons, K.6
  • 181
    • 0024094695 scopus 로고
    • The unusual microtubule polarity in teleost retinal pigment epithelial cells
    • Troutt, L.L.; Burnside, B. The unusual microtubule polarity in teleost retinal pigment epithelial cells. J. Cell Biol. 1988, 107, 1461-1464.
    • (1988) J. Cell Biol , vol.107 , pp. 1461-1464
    • Troutt, L.L.1    Burnside, B.2
  • 182
    • 0024521070 scopus 로고
    • Microtubule polarities indicate that nucleation and capture of microtubules occurs at cell surfaces in Drosophila
    • Mogensen, M.M.; Tucker, J.B.; Stebbings, H. Microtubule polarities indicate that nucleation and capture of microtubules occurs at cell surfaces in Drosophila. J. Cell Biol. 1989, 108, 1445-1452.
    • (1989) J. Cell Biol , vol.108 , pp. 1445-1452
    • Mogensen, M.M.1    Tucker, J.B.2    Stebbings, H.3
  • 183
    • 1842843639 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection of polarized epithelial cells requires microtubules and access to receptors present at cell-cell contact sites
    • Marozin, S.; Prank, U.; Sodeik, B. Herpes simplex virus type 1 infection of polarized epithelial cells requires microtubules and access to receptors present at cell-cell contact sites. J. Gen. Virol. 2004, 85, 775-786.
    • (2004) J. Gen. Virol , vol.85 , pp. 775-786
    • Marozin, S.1    Prank, U.2    Sodeik, B.3
  • 184
    • 67650480904 scopus 로고    scopus 로고
    • Propagation of swine hemagglutinating encephalomyelitis virus and pseudorabies virus in dorsal root ganglia cells
    • Hara, Y.; Hasebe, R.; Sunden, Y.; Ochiai, K.; Honda, E.; Sakoda, Y.; Umemura, T. Propagation of swine hemagglutinating encephalomyelitis virus and pseudorabies virus in dorsal root ganglia cells. J. Vet. Med. Sci. 2009, 71, 595-601.
    • (2009) J. Vet. Med. Sci , vol.71 , pp. 595-601
    • Hara, Y.1    Hasebe, R.2    Sunden, Y.3    Ochiai, K.4    Honda, E.5    Sakoda, Y.6    Umemura, T.7
  • 186
    • 8644272418 scopus 로고    scopus 로고
    • Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axons
    • Smith, G.A.; Pomeranz, L.; Gross, S.P.; Enquist, L.W. Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axons. Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 16034-16039.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 16034-16039
    • Smith, G.A.1    Pomeranz, L.2    Gross, S.P.3    Enquist, L.W.4
  • 187
    • 77957652501 scopus 로고    scopus 로고
    • Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures
    • Radtke, K.; Kieneke, D.; Wolfstein, A.; Michael, K.; Steffen, W.; Scholz, T.; Karger, A.; Sodeik, B. Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog. 2010, 6, e1000991.
    • (2010) PLoS Pathog , vol.6
    • Radtke, K.1    Kieneke, D.2    Wolfstein, A.3    Michael, K.4    Steffen, W.5    Scholz, T.6    Karger, A.7    Sodeik, B.8
  • 188
    • 19644366017 scopus 로고    scopus 로고
    • Nuclear targeting of adenovirus type 2 requires CRM1-mediated nuclear export
    • Strunze, S.; Trotman, L.C.; Boucke, K.; Greber, U.F. Nuclear targeting of adenovirus type 2 requires CRM1-mediated nuclear export. Mol. Biol. Cell 2005, 16, 2999-3009.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2999-3009
    • Strunze, S.1    Trotman, L.C.2    Boucke, K.3    Greber, U.F.4
  • 189
    • 14744294752 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 membrane protein UL56 associates with the kinesin motor protein KIF1A
    • Koshizuka, T.; Kawaguchi, Y.; Nishiyama, Y. Herpes simplex virus type 2 membrane protein UL56 associates with the kinesin motor protein KIF1A. J. Gen. Virol. 2005, 86, 527-533.
    • (2005) J. Gen. Virol , vol.86 , pp. 527-533
    • Koshizuka, T.1    Kawaguchi, Y.2    Nishiyama, Y.3
  • 190
    • 3142545772 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport
    • Douglas, M.W.; Diefenbach, R.J.; Homa, F.L.; Miranda-Saksena, M.; Rixon, F.J.; Vittone, V.; Byth, K.; Cunningham, A.L. Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport. J. Biol. Chem. 2004, 279, 28522-28530.
    • (2004) J. Biol. Chem , vol.279 , pp. 28522-28530
    • Douglas, M.W.1    Diefenbach, R.J.2    Homa, F.L.3    Miranda-Saksena, M.4    Rixon, F.J.5    Vittone, V.6    Byth, K.7    Cunningham, A.L.8
  • 191
    • 0033962923 scopus 로고    scopus 로고
    • The herpes simplex virus 1 U(L)34 protein interacts with a cytoplasmic dynein intermediate chain and targets nuclear membrane
    • Ye, G.J.; Vaughan, K.T.; Vallee, R.B.; Roizman, B. The herpes simplex virus 1 U(L)34 protein interacts with a cytoplasmic dynein intermediate chain and targets nuclear membrane. J. Virol. 2000, 74, 1355-1363.
    • (2000) J. Virol , vol.74 , pp. 1355-1363
    • Ye, G.J.1    Vaughan, K.T.2    Vallee, R.B.3    Roizman, B.4
  • 193
    • 0028783737 scopus 로고
    • Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: Structural authenticity and localization of VP26
    • Trus, B.L.; Homa, F.L.; Booy, F.P.; Newcomb, W.W.; Thomsen, D.R.; Cheng, N.; Brown, J.C.; Steven, A.C. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26. J. Virol. 1995, 69, 7362-7366.
    • (1995) J. Virol , vol.69 , pp. 7362-7366
    • Trus, B.L.1    Homa, F.L.2    Booy, F.P.3    Newcomb, W.W.4    Thomsen, D.R.5    Cheng, N.6    Brown, J.C.7    Steven, A.C.8
  • 194
    • 0028804828 scopus 로고
    • Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids
    • Zhou, Z.H.; He, J.; Jakana, J.; Tatman, J.D.; Rixon, F.J.; Chiu, W. Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids. Nat. Struct. Biol. 1995, 2, 1026-1030.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 1026-1030
    • Zhou, Z.H.1    He, J.2    Jakana, J.3    Tatman, J.D.4    Rixon, F.J.5    Chiu, W.6
  • 195
    • 32944467134 scopus 로고    scopus 로고
    • The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro
    • Wolfstein, A.; Nagel, C.H.; Radtke, K.; Dohner, K.; Allan, V.J.; Sodeik, B. The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro. Traffic 2006, 7, 227-237.
    • (2006) Traffic , vol.7 , pp. 227-237
    • Wolfstein, A.1    Nagel, C.H.2    Radtke, K.3    Dohner, K.4    Allan, V.J.5    Sodeik, B.6
  • 196
    • 17344386043 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 VP26 is not essential for replication in cell culture but influences production of infectious virus in the nervous system of infected mice
    • Desai, P.; DeLuca, N.A.; Person, S. Herpes simplex virus type 1 VP26 is not essential for replication in cell culture but influences production of infectious virus in the nervous system of infected mice. Virology 1998, 247, 115-124.
    • (1998) Virology , vol.247 , pp. 115-124
    • Desai, P.1    Deluca, N.A.2    Person, S.3
  • 197
    • 33646750547 scopus 로고    scopus 로고
    • The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus
    • Antinone, S.E.; Shubeita, G.T.; Coller, K.E.; Lee, J.I.; Haverlock-Moyns, S.; Gross, S.P.; Smith, G.A. The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus. J. Virol. 2006, 80, 5494-5498.
    • (2006) J. Virol , vol.80 , pp. 5494-5498
    • Antinone, S.E.1    Shubeita, G.T.2    Coller, K.E.3    Lee, J.I.4    Haverlock-Moyns, S.5    Gross, S.P.6    Smith, G.A.7
  • 198
    • 33746853425 scopus 로고    scopus 로고
    • Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26
    • Dohner, K.; Radtke, K.; Schmidt, S.; Sodeik, B. Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26. J. Virol. 2006, 80, 8211-8224.
    • (2006) J. Virol , vol.80 , pp. 8211-8224
    • Dohner, K.1    Radtke, K.2    Schmidt, S.3    Sodeik, B.4
  • 199
    • 0020701819 scopus 로고
    • Molecular genetics of herpes simplex virus. VIII. further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle
    • Batterson, W.; Furlong, D.; Roizman, B. Molecular genetics of herpes simplex virus. VIII. further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle. J. Virol. 1983, 45, 397-407.
    • (1983) J. Virol , vol.45 , pp. 397-407
    • Batterson, W.1    Furlong, D.2    Roizman, B.3
  • 200
    • 41149126620 scopus 로고    scopus 로고
    • Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus
    • Jovasevic, V.; Liang, L.; Roizman, B. Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus. J. Virol. 2008, 82, 3311-3319.
    • (2008) J. Virol , vol.82 , pp. 3311-3319
    • Jovasevic, V.1    Liang, L.2    Roizman, B.3
  • 201
    • 0034466764 scopus 로고    scopus 로고
    • A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells
    • Desai, P.J. A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells. J. Virol. 2000, 74, 11608-11618.
    • (2000) J. Virol , vol.74 , pp. 11608-11618
    • Desai, P.J.1
  • 202
    • 6344219960 scopus 로고    scopus 로고
    • Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein
    • Fuchs, W.; Klupp, B.G.; Granzow, H.; Mettenleiter, T.C. Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein. J. Virol. 2004, 78, 11879-11889.
    • (2004) J. Virol , vol.78 , pp. 11879-11889
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Mettenleiter, T.C.4
  • 203
    • 70350516473 scopus 로고    scopus 로고
    • Characterization of the herpes simplex virus (HSV)-1 tegument protein VP1-2 during infection with the HSV temperature-sensitive mutant tsB7
    • Abaitua, F.; Souto, R.N.; Browne, H.; Daikoku, T.; O'Hare, P. Characterization of the herpes simplex virus (HSV)-1 tegument protein VP1-2 during infection with the HSV temperature-sensitive mutant tsB7. J. Gen. Virol. 2009, 90, 2353-2363.
    • (2009) J. Gen. Virol , vol.90 , pp. 2353-2363
    • Abaitua, F.1    Souto, R.N.2    Browne, H.3    Daikoku, T.4    O'Hare, P.5
  • 205
    • 35448946916 scopus 로고    scopus 로고
    • The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins
    • Coller, K.E.; Lee, J.I.; Ueda, A.; Smith, G.A. The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. J. Virol. 2007, 81, 11790-11797.
    • (2007) J. Virol , vol.81 , pp. 11790-11797
    • Coller, K.E.1    Lee, J.I.2    Ueda, A.3    Smith, G.A.4
  • 206
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25
    • Pasdeloup, D.; Blondel, D.; Isidro, A.L.; Rixon, F.J. Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J. Virol. 2009, 83, 6610-6623.
    • (2009) J. Virol , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3    Rixon, F.J.4
  • 208
    • 0036191216 scopus 로고    scopus 로고
    • Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein
    • Klupp, B.G.; Fuchs, W.; Granzow, H.; Nixdorf, R.; Mettenleiter, T.C. Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein. J. Virol. 2002, 76, 3065-3071.
    • (2002) J. Virol , vol.76 , pp. 3065-3071
    • Klupp, B.G.1    Fuchs, W.2    Granzow, H.3    Nixdorf, R.4    Mettenleiter, T.C.5
  • 209
    • 73949127977 scopus 로고    scopus 로고
    • The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2)
    • Ko, D.H.; Cunningham, A.L.; Diefenbach, R.J. The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2). J. Virol. 2010, 84, 1397-1405.
    • (2010) J. Virol , vol.84 , pp. 1397-1405
    • Ko, D.H.1    Cunningham, A.L.2    Diefenbach, R.J.3
  • 210
    • 0026787060 scopus 로고
    • Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1
    • McNabb, D.S.; Courtney, R.J. Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1. Virology 1992, 190, 221-232.
    • (1992) Virology , vol.190 , pp. 221-232
    • McNabb, D.S.1    Courtney, R.J.2
  • 211
    • 0345471494 scopus 로고    scopus 로고
    • Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions
    • Zhou, Z.H.; Chen, D.H.; Jakana, J.; Rixon, F.J.; Chiu, W. Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. J. Virol. 1999, 73, 3210-3218.
    • (1999) J. Virol , vol.73 , pp. 3210-3218
    • Zhou, Z.H.1    Chen, D.H.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5
  • 212
    • 0015427631 scopus 로고
    • Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2
    • Gibson, W.; Roizman, B. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J. Virol. 1972, 10, 1044-1052.
    • (1972) J. Virol , vol.10 , pp. 1044-1052
    • Gibson, W.1    Roizman, B.2
  • 213
    • 0020214102 scopus 로고
    • Morphological components of herpesvirus. IV. Ultrastructural features of the envelope and tegument
    • Vernon, S.K.; Lawrence, W.C.; Long, C.A.; Rubin, B.A.; Sheffield, J.B. Morphological components of herpesvirus. IV. Ultrastructural features of the envelope and tegument. J. Ultrastruct. Res. 1982, 81, 163-171.
    • (1982) J. Ultrastruct. Res , vol.81 , pp. 163-171
    • Vernon, S.K.1    Lawrence, W.C.2    Long, C.A.3    Rubin, B.A.4    Sheffield, J.B.5
  • 214
    • 67849102088 scopus 로고    scopus 로고
    • Phenotypic similarities and differences between UL37-deleted pseudorabies virus and herpes simplex virus type 1
    • Leege, T.; Granzow, H.; Fuchs, W.; Klupp, B.G.; Mettenleiter, T.C. Phenotypic similarities and differences between UL37-deleted pseudorabies virus and herpes simplex virus type 1. J. Gen. Virol. 2009, 90, 1560-1568.
    • (2009) J. Gen. Virol , vol.90 , pp. 1560-1568
    • Leege, T.1    Granzow, H.2    Fuchs, W.3    Klupp, B.G.4    Mettenleiter, T.C.5
  • 215
    • 0034849764 scopus 로고    scopus 로고
    • Pseudorabies virus UL37 gene product is involved in secondary envelopment
    • Klupp, B.G.; Granzow, H.; Mundt, E.; Mettenleiter, T.C. Pseudorabies virus UL37 gene product is involved in secondary envelopment. J. Virol. 2001, 75, 8927-8936.
    • (2001) J. Virol , vol.75 , pp. 8927-8936
    • Klupp, B.G.1    Granzow, H.2    Mundt, E.3    Mettenleiter, T.C.4
  • 216
    • 32944480977 scopus 로고    scopus 로고
    • The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport
    • Luxton, G.W.; Lee, J.I.; Haverlock-Moyns, S.; Schober, J.M.; Smith, G.A. The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport. J. Virol. 2006, 80, 201-209.
    • (2006) J. Virol , vol.80 , pp. 201-209
    • Luxton, G.W.1    Lee, J.I.2    Haverlock-Moyns, S.3    Schober, J.M.4    Smith, G.A.5
  • 217
    • 0034785814 scopus 로고    scopus 로고
    • A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation
    • Desai, P.; Sexton, G.L.; McCaffery, J.M.; Person, S. A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation. J. Virol. 2001, 75, 10259-10271.
    • (2001) J. Virol , vol.75 , pp. 10259-10271
    • Desai, P.1    Sexton, G.L.2    McCaffery, J.M.3    Person, S.A.4
  • 218
    • 63149186260 scopus 로고    scopus 로고
    • Translocation of incoming pseudorabies virus capsids to the cell nucleus is delayed in the absence of tegument protein pUL37
    • Krautwald, M.; Fuchs, W.; Klupp, B.G.; Mettenleiter, T.C. Translocation of incoming pseudorabies virus capsids to the cell nucleus is delayed in the absence of tegument protein pUL37. J. Virol. 2009, 83, 3389-3396.
    • (2009) J. Virol , vol.83 , pp. 3389-3396
    • Krautwald, M.1    Fuchs, W.2    Klupp, B.G.3    Mettenleiter, T.C.4
  • 219
    • 58149393193 scopus 로고    scopus 로고
    • Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1
    • Roberts, A.P.; Abaitua, F.; O'Hare, P.; McNab, D.; Rixon, F.J.; Pasdeloup, D. Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1. J. Virol. 2009, 83, 105-116.
    • (2009) J. Virol , vol.83 , pp. 105-116
    • Roberts, A.P.1    Abaitua, F.2    O'Hare, P.3    McNab, D.4    Rixon, F.J.5    Pasdeloup, D.6
  • 220
    • 17344368861 scopus 로고    scopus 로고
    • Active intranuclear movement of herpesvirus capsids
    • Forest, T.; Barnard, S.; Baines, J.D. Active intranuclear movement of herpesvirus capsids. Nat. Cell Biol. 2005, 7, 429-431.
    • (2005) Nat. Cell Biol , vol.7 , pp. 429-431
    • Forest, T.1    Barnard, S.2    Baines, J.D.3
  • 221
    • 33947368648 scopus 로고    scopus 로고
    • Electron tomography of nascent herpes simplex virus virions
    • Baines, J.D.; Hsieh, C.E.; Wills, E.; Mannella, C.; Marko, M. Electron tomography of nascent herpes simplex virus virions. J. Virol. 2007, 81, 2726-2735.
    • (2007) J. Virol , vol.81 , pp. 2726-2735
    • Baines, J.D.1    Hsieh, C.E.2    Wills, E.3    Mannella, C.4    Marko, M.5
  • 223
    • 31144448686 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses
    • Mettenleiter, T.C.; Minson, T. Egress of alphaherpesviruses. J. Virol. 2006, 80, 1610-1611;
    • (2006) J. Virol , vol.80 , pp. 1610-1611
    • Mettenleiter, T.C.1    Minson, T.2
  • 224
    • 33745267085 scopus 로고    scopus 로고
    • The egress of herpesviruses from cells: The unanswered questions
    • Campadelli-Fiume, G.; Roizman, B. The egress of herpesviruses from cells: The unanswered questions. J. Virol. 2006, 80, 6716-6717; author replies 6717-6719.
    • (2006) J. Virol , vol.80 , pp. 6716-6717
    • Campadelli-Fiume, G.1    Roizman, B.2
  • 227
    • 0036278491 scopus 로고    scopus 로고
    • The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions
    • Fuchs, W.; Granzow, H.; Klupp, B.G.; Kopp, M.; Mettenleiter, T.C. The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions. J. Virol. 2002, 76, 6729-6742.
    • (2002) J. Virol , vol.76 , pp. 6729-6742
    • Fuchs, W.1    Granzow, H.2    Klupp, B.G.3    Kopp, M.4    Mettenleiter, T.C.5
  • 228
    • 49049113021 scopus 로고    scopus 로고
    • Identification of structural protein-protein interactions of herpes simplex virus type 1
    • Lee, J.H.; Vittone, V.; Diefenbach, E.; Cunningham, A.L.; Diefenbach, R.J. Identification of structural protein-protein interactions of herpes simplex virus type 1. Virology 2008, 378, 347-354.
    • (2008) Virology , vol.378 , pp. 347-354
    • Lee, J.H.1    Vittone, V.2    Diefenbach, E.3    Cunningham, A.L.4    Diefenbach, R.J.5
  • 229
    • 0142092454 scopus 로고    scopus 로고
    • Binding partners for the UL11 tegument protein of herpes simplex virus type 1
    • Loomis, J.S.; Courtney, R.J.; Wills, J.W. Binding partners for the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 2003, 77, 11417-11424.
    • (2003) J. Virol , vol.77 , pp. 11417-11424
    • Loomis, J.S.1    Courtney, R.J.2    Wills, J.W.3
  • 230
    • 0026614607 scopus 로고
    • The pseudorabies virus homology of the herpes simplex virus UL21 gene product is a capsid protein which is involved in capsid maturation
    • de Wind, N.; Wagenaar, F.; Pol, J.; Kimman, T.; Berns, A. The pseudorabies virus homology of the herpes simplex virus UL21 gene product is a capsid protein which is involved in capsid maturation. J. Virol. 1992, 66, 7096-7103.
    • (1992) J. Virol , vol.66 , pp. 7096-7103
    • de Wind, N.1    Wagenaar, F.2    Pol, J.3    Kimman, T.4    Berns, A.5
  • 231
    • 13744250797 scopus 로고    scopus 로고
    • Complex formation between the UL16 and UL21 tegument proteins of pseudorabies virus
    • Klupp, B.G.; Bottcher, S.; Granzow, H.; Kopp, M.; Mettenleiter, T.C. Complex formation between the UL16 and UL21 tegument proteins of pseudorabies virus. J. Virol. 2005, 79, 1510-1522.
    • (2005) J. Virol , vol.79 , pp. 1510-1522
    • Klupp, B.G.1    Bottcher, S.2    Granzow, H.3    Kopp, M.4    Mettenleiter, T.C.5
  • 232
    • 77954508585 scopus 로고    scopus 로고
    • Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein
    • Wang, L.; Liu, L.; Che, Y.; Jiang, L.; Dong, C.; Zhang, Y.; Li, Q. Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein. Virol. J. 2010, 7, 156.
    • (2010) Virol. J , vol.7 , pp. 156
    • Wang, L.1    Liu, L.2    Che, Y.3    Jiang, L.4    Dong, C.5    Zhang, Y.6    Li, Q.7
  • 234
    • 55549112567 scopus 로고    scopus 로고
    • Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures
    • Desai, P.; Sexton, G.L.; Huang, E.; Person, S. Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures. J. Virol. 2008, 82, 11354-11361.
    • (2008) J. Virol , vol.82 , pp. 11354-11361
    • Desai, P.1    Sexton, G.L.2    Huang, E.3    Person, S.4
  • 235
    • 0035158723 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread
    • Johnson, D.C.; Webb, M.; Wisner, T.W.; Brunetti, C. Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread. J. Virol. 2001, 75, 821-833.
    • (2001) J. Virol , vol.75 , pp. 821-833
    • Johnson, D.C.1    Webb, M.2    Wisner, T.W.3    Brunetti, C.4
  • 236
    • 0035138826 scopus 로고    scopus 로고
    • Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions
    • McMillan, T.N.; Johnson, D.C. Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions. J. Virol. 2001, 75, 1928-1940.
    • (2001) J. Virol , vol.75 , pp. 1928-1940
    • McMillan, T.N.1    Johnson, D.C.2
  • 237
    • 43949089146 scopus 로고    scopus 로고
    • Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1
    • Sugimoto, K.; Uema, M.; Sagara, H.; Tanaka, M.; Sata, T.; Hashimoto, Y.; Kawaguchi, Y. Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1. J. Virol. 2008, 82, 5198-5211.
    • (2008) J. Virol , vol.82 , pp. 5198-5211
    • Sugimoto, K.1    Uema, M.2    Sagara, H.3    Tanaka, M.4    Sata, T.5    Hashimoto, Y.6    Kawaguchi, Y.7
  • 238
    • 0028857923 scopus 로고
    • Redistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis
    • Avitabile, E.; Di Gaeta, S.; Torrisi, M.R.; Ward, P.L.; Roizman, B.; Campadelli-Fiume, G. Redistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis. J. Virol. 1995, 69, 7472-7482.
    • (1995) J. Virol , vol.69 , pp. 7472-7482
    • Avitabile, E.1    di Gaeta, S.2    Torrisi, M.R.3    Ward, P.L.4    Roizman, B.5    Campadelli-Fiume, G.6
  • 239
    • 0027511479 scopus 로고
    • Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1
    • Campadelli, G.; Brandimarti, R.; Di Lazzaro, C.; Ward, P.L.; Roizman, B.; Torrisi, M.R. Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1. Proc. Natl. Acad. Sci. U. S. A. 1993, 90, 2798-2802.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 2798-2802
    • Campadelli, G.1    Brandimarti, R.2    di Lazzaro, C.3    Ward, P.L.4    Roizman, B.5    Torrisi, M.R.6
  • 240
    • 65349120570 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 glycoprotein E mediates retrograde spread from epithelial cells to neurites
    • McGraw, H.M.; Friedman, H.M. Herpes simplex virus type 1 glycoprotein E mediates retrograde spread from epithelial cells to neurites. J. Virol. 2009, 83, 4791-4799.
    • (2009) J. Virol , vol.83 , pp. 4791-4799
    • McGraw, H.M.1    Friedman, H.M.2
  • 241
    • 67649891816 scopus 로고    scopus 로고
    • Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane
    • Remillard-Labrosse, G.; Mihai, C.; Duron, J.; Guay, G.; Lippe, R. Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane. Traffic 2009, 10, 1074-1083.
    • (2009) Traffic , vol.10 , pp. 1074-1083
    • Remillard-Labrosse, G.1    Mihai, C.2    Duron, J.3    Guay, G.4    Lippe, R.5
  • 242
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl, M.; Maeda, Y.; Colanzi, A.; Ayala, I.; Van Lint, J.; Malhotra, V. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell 2001, 104, 409-420.
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    van Lint, J.5    Malhotra, V.6
  • 245
    • 33646168140 scopus 로고    scopus 로고
    • Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro
    • Lee, G.E.; Murray, J.W.; Wolkoff, A.W.; Wilson, D.W. Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro. J. Virol. 2006, 80, 4264-4275.
    • (2006) J. Virol , vol.80 , pp. 4264-4275
    • Lee, G.E.1    Murray, J.W.2    Wolkoff, A.W.3    Wilson, D.W.4
  • 246
    • 47749138960 scopus 로고    scopus 로고
    • UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules
    • Shanda, S.K.; Wilson, D.W. UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules. J. Virol. 2008, 82, 7388-7394.
    • (2008) J. Virol , vol.82 , pp. 7388-7394
    • Shanda, S.K.1    Wilson, D.W.2
  • 247
    • 0026100629 scopus 로고
    • Identification and characterization of a novel non-infectious herpes simplex virus-related particle
    • Szilagyi, J.F.; Cunningham, C. Identification and characterization of a novel non-infectious herpes simplex virus-related particle. J. Gen. Virol. 1991, 72, 661-668.
    • (1991) J. Gen. Virol , vol.72 , pp. 661-668
    • Szilagyi, J.F.1    Cunningham, C.2
  • 250
    • 0041387510 scopus 로고    scopus 로고
    • Association of the herpes simplex virus type 1 Us11 gene product with the cellular kinesin light-chain-related protein PAT1 results in the redistribution of both polypeptides
    • Benboudjema, L.; Mulvey, M.; Gao, Y.; Pimplikar, S.W.; Mohr, I. Association of the herpes simplex virus type 1 Us11 gene product with the cellular kinesin light-chain-related protein PAT1 results in the redistribution of both polypeptides. J. Virol. 2003, 77, 9192-9203.
    • (2003) J. Virol , vol.77 , pp. 9192-9203
    • Benboudjema, L.1    Mulvey, M.2    Gao, Y.3    Pimplikar, S.W.4    Mohr, I.5
  • 251
    • 0036278489 scopus 로고    scopus 로고
    • Identification and characterization of the UL56 gene product of herpes simplex virus type 2
    • Koshizuka, T.; Goshima, F.; Takakuwa, H.; Nozawa, N.; Daikoku, T.; Koiwai, O.; Nishiyama, Y. Identification and characterization of the UL56 gene product of herpes simplex virus type 2. J. Virol. 2002, 76, 6718-6728.
    • (2002) J. Virol , vol.76 , pp. 6718-6728
    • Koshizuka, T.1    Goshima, F.2    Takakuwa, H.3    Nozawa, N.4    Daikoku, T.5    Koiwai, O.6    Nishiyama, Y.7
  • 252
    • 0025914790 scopus 로고
    • Elimination of UL56 gene by insertion of LacZ cassette between nucleotide position 116030 to 121753 of the herpes simplex virus type 1 genome abrogates intraperitoneal pathogenicity in tree shrews and mice
    • Rosen-Wolff, A.; Lamade, W.; Berkowitz, C.; Becker, Y.; Darai, G. Elimination of UL56 gene by insertion of LacZ cassette between nucleotide position 116030 to 121753 of the herpes simplex virus type 1 genome abrogates intraperitoneal pathogenicity in tree shrews and mice. Virus Res. 1991, 20, 205-221.
    • (1991) Virus Res , vol.20 , pp. 205-221
    • Rosen-Wolff, A.1    Lamade, W.2    Berkowitz, C.3    Becker, Y.4    Darai, G.5
  • 253
    • 0036124578 scopus 로고    scopus 로고
    • Evidence of a role for nonmuscle myosin II in herpes simplex virus type 1 egress
    • van Leeuwen, H.; Elliott, G.; O'Hare, P. Evidence of a role for nonmuscle myosin II in herpes simplex virus type 1 egress. J. Virol. 2002, 76, 3471-3481.
    • (2002) J. Virol , vol.76 , pp. 3471-3481
    • van Leeuwen, H.1    Elliott, G.2    O'Hare, P.3
  • 254
    • 77956845138 scopus 로고    scopus 로고
    • Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins
    • Roberts, K.L.; Baines, J.D. Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins. J. Virol. 2010, 84, 9889-9896.
    • (2010) J. Virol , vol.84 , pp. 9889-9896
    • Roberts, K.L.1    Baines, J.D.2
  • 255
    • 33751396164 scopus 로고    scopus 로고
    • Protein sorting in the synaptic vesicle life cycle
    • Bonanomi, D.; Benfenati, F.; Valtorta, F. Protein sorting in the synaptic vesicle life cycle. Prog. Neurobiol. 2006, 80, 177-217.
    • (2006) Prog. Neurobiol , vol.80 , pp. 177-217
    • Bonanomi, D.1    Benfenati, F.2    Valtorta, F.3
  • 256
    • 0035921429 scopus 로고    scopus 로고
    • A conserved alpha-herpesvirus protein necessary for axonal localization of viral membrane proteins
    • Tomishima, M.J.; Enquist, L.W. A conserved alpha-herpesvirus protein necessary for axonal localization of viral membrane proteins. J. Cell Biol. 2001, 154, 741-752.
    • (2001) J. Cell Biol , vol.154 , pp. 741-752
    • Tomishima, M.J.1    Enquist, L.W.2
  • 257
    • 35148896264 scopus 로고    scopus 로고
    • Pseudorabies virus Us9 directs axonal sorting of viral capsids
    • Lyman, M.G.; Feierbach, B.; Curanovic, D.; Bisher, M.; Enquist, L.W. Pseudorabies virus Us9 directs axonal sorting of viral capsids. J. Virol. 2007, 81, 11363-11371.
    • (2007) J. Virol , vol.81 , pp. 11363-11371
    • Lyman, M.G.1    Feierbach, B.2    Curanovic, D.3    Bisher, M.4    Enquist, L.W.5
  • 258
    • 67650465605 scopus 로고    scopus 로고
    • Comparison of the pseudorabies virus Us9 protein with homologs from other veterinary and human alphaherpesviruses
    • Lyman, M.G.; Kemp, C.D.; Taylor, M.P.; Enquist, L.W. Comparison of the pseudorabies virus Us9 protein with homologs from other veterinary and human alphaherpesviruses. J. Virol. 2009, 83, 6978-6986.
    • (2009) J. Virol , vol.83 , pp. 6978-6986
    • Lyman, M.G.1    Kemp, C.D.2    Taylor, M.P.3    Enquist, L.W.4
  • 259
    • 35548989378 scopus 로고    scopus 로고
    • Herpes simplex virus protein UL11 but not UL51 is associated with lipid rafts
    • Koshizuka, T.; Kawaguchi, Y.; Nozawa, N.; Mori, I.; Nishiyama, Y. Herpes simplex virus protein UL11 but not UL51 is associated with lipid rafts. Virus Genes 2007, 35, 571-575.
    • (2007) Virus Genes , vol.35 , pp. 571-575
    • Koshizuka, T.1    Kawaguchi, Y.2    Nozawa, N.3    Mori, I.4    Nishiyama, Y.5
  • 260
    • 44949099369 scopus 로고    scopus 로고
    • Targeting of pseudorabies virus structural proteins to axons requires association of the viral Us9 protein with lipid rafts
    • Lyman, M.G.; Curanovic, D.; Enquist, L.W. Targeting of pseudorabies virus structural proteins to axons requires association of the viral Us9 protein with lipid rafts. PLoS Pathog. 2008, 4, e1000065.
    • (2008) PLoS Pathog , vol.4
    • Lyman, M.G.1    Curanovic, D.2    Enquist, L.W.3
  • 261
    • 0015581906 scopus 로고
    • Pathogenesis of herpetic neuritis and ganglionitis in mice: Evidence for intra-axonal transport of infection
    • Cook, M.L.; Stevens, J.G. Pathogenesis of herpetic neuritis and ganglionitis in mice: evidence for intra-axonal transport of infection. Infect. Immun. 1973, 7, 272-288.
    • (1973) Infect. Immun , vol.7 , pp. 272-288
    • Cook, M.L.1    Stevens, J.G.2
  • 262
    • 0015357221 scopus 로고
    • Intra-axonal location of herpes simplex virus particles
    • Hill, T.J.; Field, H.J.; Roome, A.P. Intra-axonal location of herpes simplex virus particles. J. Gen. Virol. 1972, 15, 233-235.
    • (1972) J. Gen. Virol , vol.15 , pp. 233-235
    • Hill, T.J.1    Field, H.J.2    Roome, A.P.3
  • 263
    • 0015952473 scopus 로고
    • Study on the propagation of Herpes simplex virus (type 2) into the brain after intraocular injection
    • Kristensson, K.; Ghetti, B.; Wisniewski, H.M. Study on the propagation of Herpes simplex virus (type 2) into the brain after intraocular injection. Brain Res. 1974, 69, 189-201.
    • (1974) Brain Res , vol.69 , pp. 189-201
    • Kristensson, K.1    Ghetti, B.2    Wisniewski, H.M.3
  • 264
    • 0030760743 scopus 로고    scopus 로고
    • Factors that contribute to the transneuronal spread of herpes simplex virus
    • LaVail, J.H.; Topp, K.S.; Giblin, P.A.; Garner, J.A. Factors that contribute to the transneuronal spread of herpes simplex virus. J. Neurosci. Res. 1997, 49, 485-496.
    • (1997) J. Neurosci. Res , vol.49 , pp. 485-496
    • Lavail, J.H.1    Topp, K.S.2    Giblin, P.A.3    Garner, J.A.4
  • 265
    • 0028285180 scopus 로고
    • Axonal transport of herpes simplex virions to epidermal cells: Evidence for a specialized mode of virus transport and assembly
    • Penfold, M.E.; Armati, P.; Cunningham, A.L. Axonal transport of herpes simplex virions to epidermal cells: evidence for a specialized mode of virus transport and assembly. Proc. Natl. Acad. Sci. U. S. A. 1994, 91, 6529-6533.
    • (1994) Proc. Natl. Acad. Sci. U. S. A , vol.91 , pp. 6529-6533
    • Penfold, M.E.1    Armati, P.2    Cunningham, A.L.3
  • 266
    • 0005599756 scopus 로고    scopus 로고
    • Anterograde transport of herpes simplex virus proteins in axons of peripheral human fetal neurons: An immunoelectron microscopy study
    • Holland, D.J.; Miranda-Saksena, M.; Boadle, R.A.; Armati, P.; Cunningham, A.L. Anterograde transport of herpes simplex virus proteins in axons of peripheral human fetal neurons: An immunoelectron microscopy study. J. Virol. 1999, 73, 8503-8511.
    • (1999) J. Virol , vol.73 , pp. 8503-8511
    • Holland, D.J.1    Miranda-Saksena, M.2    Boadle, R.A.3    Armati, P.4    Cunningham, A.L.5
  • 267
    • 78649438708 scopus 로고    scopus 로고
    • Ultrastructural analysis of virion formation and intraaxonal transport of herpes simplex virus type 1 in primary rat neurons
    • Negatsch, A.; Granzow, H.; Maresch, C.; Klupp, B.G.; Fuchs, W.; Teifke, J.P.; Mettenleiter, T.C. Ultrastructural analysis of virion formation and intraaxonal transport of herpes simplex virus type 1 in primary rat neurons. J. Virol. 2010, 84, 13031-13035.
    • (2010) J. Virol , vol.84 , pp. 13031-13035
    • Negatsch, A.1    Granzow, H.2    Maresch, C.3    Klupp, B.G.4    Fuchs, W.5    Teifke, J.P.6    Mettenleiter, T.C.7
  • 268
    • 78649450933 scopus 로고    scopus 로고
    • Completely assembled virus particles detected by transmission electron microscopy in proximal and mid-axons of neurons infected with herpes simplex virus type 1, herpes simplex virus type 2 and pseudorabies virus
    • Huang, J.; Lazear, H.M.; Friedman, H.M. Completely assembled virus particles detected by transmission electron microscopy in proximal and mid-axons of neurons infected with herpes simplex virus type 1, herpes simplex virus type 2 and pseudorabies virus. Virology 2011, 409, 12-16.
    • (2011) Virology , vol.409 , pp. 12-16
    • Huang, J.1    Lazear, H.M.2    Friedman, H.M.3
  • 270
    • 73949143468 scopus 로고    scopus 로고
    • Directional transneuronal spread of alpha-herpesvirus infection
    • Curanovic, D.; Enquist, L. Directional transneuronal spread of alpha-herpesvirus infection. Future Virol. 2009, 4, 591.
    • (2009) Future Virol , vol.4 , pp. 591
    • Curanovic, D.1    Enquist, L.2
  • 271
    • 79954571251 scopus 로고    scopus 로고
    • Anterograde transport of herpes simplex virus capsids in neurons by both Separate and Married mechanisms
    • Wisner, T.W.; Sugimoto, K.; Howard, P.W.; Kawaguchi, Y.; Johnson, D.C. Anterograde transport of herpes simplex virus capsids in neurons by both Separate and Married mechanisms. J. Virol. 2011, 85, 5919-5928.
    • (2011) J. Virol , vol.85 , pp. 5919-5928
    • Wisner, T.W.1    Sugimoto, K.2    Howard, P.W.3    Kawaguchi, Y.4    Johnson, D.C.5
  • 272
    • 78649434392 scopus 로고    scopus 로고
    • Resolving the assembly state of herpes simplex virus during axon transport by live-cell imaging
    • Antinone, S.E.; Zaichick, S.V.; Smith, G.A. Resolving the assembly state of herpes simplex virus during axon transport by live-cell imaging. J. Virol. 2010, 84, 13019-13030.
    • (2010) J. Virol , vol.84 , pp. 13019-13030
    • Antinone, S.E.1    Zaichick, S.V.2    Smith, G.A.3
  • 273
    • 63149090485 scopus 로고    scopus 로고
    • Herpes simplex virus utilizes the large secretory vesicle pathway for anterograde transport of tegument and envelope proteins and for viral exocytosis from growth cones of human fetal axons
    • Miranda-Saksena, M.; Boadle, R.A.; Aggarwal, A.; Tijono, B.; Rixon, F.J.; Diefenbach, R.J.; Cunningham, A.L. Herpes simplex virus utilizes the large secretory vesicle pathway for anterograde transport of tegument and envelope proteins and for viral exocytosis from growth cones of human fetal axons. J. Virol. 2009, 83, 3187-3199.
    • (2009) J. Virol , vol.83 , pp. 3187-3199
    • Miranda-Saksena, M.1    Boadle, R.A.2    Aggarwal, A.3    Tijono, B.4    Rixon, F.J.5    Diefenbach, R.J.6    Cunningham, A.L.7
  • 274
    • 0035853091 scopus 로고    scopus 로고
    • Herpesviruses use bidirectional fast-axonal transport to spread in sensory neurons
    • Smith, G.A.; Gross, S.P.; Enquist, L.W. Herpesviruses use bidirectional fast-axonal transport to spread in sensory neurons. Proc. Natl. Acad. Sci. U. S. A. 2001, 98, 3466-3470.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 3466-3470
    • Smith, G.A.1    Gross, S.P.2    Enquist, L.W.3
  • 275
    • 79751493269 scopus 로고    scopus 로고
    • Calculation of the anterograde velocity of varicella-zoster virions in a human sciatic nerve during shingles
    • Tannous, R.; Grose, C. Calculation of the anterograde velocity of varicella-zoster virions in a human sciatic nerve during shingles. J. Infect. Dis. 2011, 203, 324-326.
    • (2011) J. Infect. Dis , vol.203 , pp. 324-326
    • Tannous, R.1    Grose, C.2
  • 276
    • 73949107300 scopus 로고    scopus 로고
    • Multi-targeted neuroprotection by the HSV-2 gene ICP10PK includes robust bystander activity through PI3-K/Akt and/or MEK/ERK-dependent neuronal release of vascular endothelial growth factor and fractalkine
    • Laing, J.M.; Smith, C.C.; Aurelian, L. Multi-targeted neuroprotection by the HSV-2 gene ICP10PK includes robust bystander activity through PI3-K/Akt and/or MEK/ERK-dependent neuronal release of vascular endothelial growth factor and fractalkine. J. Neurochem. 2010, 112, 662-676.
    • (2010) J. Neurochem , vol.112 , pp. 662-676
    • Laing, J.M.1    Smith, C.C.2    Aurelian, L.3
  • 277
    • 8744251609 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta and the regulation of axon growth
    • Goold, R.G.; Gordon-Weeks, P.R. Glycogen synthase kinase 3beta and the regulation of axon growth. Biochem. Soc. Trans. 2004, 32, 809-811.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 809-811
    • Goold, R.G.1    Gordon-Weeks, P.R.2
  • 278
    • 33646806089 scopus 로고    scopus 로고
    • The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon
    • Ada-Nguema, A.S.; Xenias, H.; Hofman, J.M.; Wiggins, C.H.; Sheetz, M.P.; Keely, P.J. The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon. J. Cell Sci. 2006, 119, 1307-1319.
    • (2006) J. Cell Sci , vol.119 , pp. 1307-1319
    • Ada-Nguema, A.S.1    Xenias, H.2    Hofman, J.M.3    Wiggins, C.H.4    Sheetz, M.P.5    Keely, P.J.6
  • 280
    • 0041707652 scopus 로고    scopus 로고
    • Pseudorabies virus US3 protein kinase mediates actin stress fiber breakdown
    • Van Minnebruggen, G.; Favoreel, H.W.; Jacobs, L.; Nauwynck, H.J. Pseudorabies virus US3 protein kinase mediates actin stress fiber breakdown. J. Virol. 2003, 77, 9074-9080.
    • (2003) J. Virol , vol.77 , pp. 9074-9080
    • van Minnebruggen, G.1    Favoreel, H.W.2    Jacobs, L.3    Nauwynck, H.J.4
  • 281
    • 77955015590 scopus 로고    scopus 로고
    • Subcellular localization of the alphaherpesvirus serine/threonine kinase Us3 as a determinant of Us3 function
    • Finnen, R.L.; Banfield, B.W. Subcellular localization of the alphaherpesvirus serine/threonine kinase Us3 as a determinant of Us3 function. Virulence 2010, 1, 291-294.
    • (2010) Virulence , vol.1 , pp. 291-294
    • Finnen, R.L.1    Banfield, B.W.2
  • 282
    • 73949121101 scopus 로고    scopus 로고
    • Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3
    • Finnen, R.L.; Roy, B.B.; Zhang, H.; Banfield, B.W. Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3. Virology 2010, 397, 23-33.
    • (2010) Virology , vol.397 , pp. 23-33
    • Finnen, R.L.1    Roy, B.B.2    Zhang, H.3    Banfield, B.W.4
  • 283
    • 0034487382 scopus 로고    scopus 로고
    • Expression of herpes simplex virus type 2 US3 affects the Cdc42/Rac pathway and attenuates c-Jun N-terminal kinase activation
    • Murata, T.; Goshima, F.; Daikoku, T.; Takakuwa, H.; Nishiyama, Y. Expression of herpes simplex virus type 2 US3 affects the Cdc42/Rac pathway and attenuates c-Jun N-terminal kinase activation. Genes Cells 2000, 5, 1017-1027.
    • (2000) Genes Cells , vol.5 , pp. 1017-1027
    • Murata, T.1    Goshima, F.2    Daikoku, T.3    Takakuwa, H.4    Nishiyama, Y.5
  • 284
    • 77952883239 scopus 로고    scopus 로고
    • Point mutations in BHV-1 Us3 gene abolish its ability to induce cytoskeletal changes in various cell types
    • Brzozowska, A.; Rychlowski, M.; Lipinska, A.D.; Bienkowska-Szewczyk, K. Point mutations in BHV-1 Us3 gene abolish its ability to induce cytoskeletal changes in various cell types. Vet. Microbiol. 2010, 143, 8-13.
    • (2010) Vet. Microbiol , vol.143 , pp. 8-13
    • Brzozowska, A.1    Rychlowski, M.2    Lipinska, A.D.3    Bienkowska-Szewczyk, K.4
  • 285
    • 21144450684 scopus 로고    scopus 로고
    • Cytoskeletal rearrangements and cell extensions induced by the US3 kinase of an alphaherpesvirus are associated with enhanced spread
    • Favoreel, H.W.; Van Minnebruggen, G.; Adriaensen, D.; Nauwynck, H.J. Cytoskeletal rearrangements and cell extensions induced by the US3 kinase of an alphaherpesvirus are associated with enhanced spread. Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 8990-8995.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 8990-8995
    • Favoreel, H.W.1    van Minnebruggen, G.2    Adriaensen, D.3    Nauwynck, H.J.4
  • 286
    • 0027983813 scopus 로고
    • Inactivation of glycoprotein gE and thymidine kinase or the US3-encoded protein kinase synergistically decreases in vivo replication of pseudorabies virus and the induction of protective immunity
    • Kimman, T.G.; De Wind, N.; De Bruin, T.; de Visser, Y.; Voermans, J. Inactivation of glycoprotein gE and thymidine kinase or the US3-encoded protein kinase synergistically decreases in vivo replication of pseudorabies virus and the induction of protective immunity. Virology 1994, 205, 511-518.
    • (1994) Virology , vol.205 , pp. 511-518
    • Kimman, T.G.1    de Wind, N.2    de Bruin, T.3    de Visser, Y.4    Voermans, J.5
  • 287
    • 0026548412 scopus 로고
    • Contribution of single genes within the unique short region of Aujeszky's disease virus (suid herpesvirus type 1) to virulence, pathogenesis and immunogenicity
    • Kimman, T.G.; de Wind, N.; Oei-Lie, N.; Pol, J.M.; Berns, A.J.; Gielkens, A.L. Contribution of single genes within the unique short region of Aujeszky's disease virus (suid herpesvirus type 1) to virulence, pathogenesis and immunogenicity. J. Gen. Virol. 1992, 73, 243-251.
    • (1992) J. Gen. Virol , vol.73 , pp. 243-251
    • Kimman, T.G.1    de Wind, N.2    Oei-Lie, N.3    Pol, J.M.4    Berns, A.J.5    Gielkens, A.L.6
  • 288
    • 33745284607 scopus 로고    scopus 로고
    • Role of pseudorabies virus Us3 protein kinase during neuronal infection
    • Olsen, L.M.; Ch'ng, T.H.; Card, J.P.; Enquist, L.W. Role of pseudorabies virus Us3 protein kinase during neuronal infection. J. Virol. 2006, 80, 6387-6398.
    • (2006) J. Virol , vol.80 , pp. 6387-6398
    • Olsen, L.M.1    Ch'ng, T.H.2    Card, J.P.3    Enquist, L.W.4
  • 289
    • 0242416181 scopus 로고    scopus 로고
    • The US3 protein kinase of herpes simplex virus attenuates the activation of the c-Jun N-terminal protein kinase signal transduction pathway in infected piriform cortex neurons of C57BL/6 mice
    • Mori, I.; Goshima, F.; Koshizuka, T.; Koide, N.; Sugiyama, T.; Yoshida, T.; Yokochi, T.; Kimura, Y.; Nishiyama, Y. The US3 protein kinase of herpes simplex virus attenuates the activation of the c-Jun N-terminal protein kinase signal transduction pathway in infected piriform cortex neurons of C57BL/6 mice. Neurosci. Lett. 2003, 351, 201-205.
    • (2003) Neurosci. Lett , vol.351 , pp. 201-205
    • Mori, I.1    Goshima, F.2    Koshizuka, T.3    Koide, N.4    Sugiyama, T.5    Yoshida, T.6    Yokochi, T.7    Kimura, Y.8    Nishiyama, Y.9
  • 290
    • 33746458854 scopus 로고    scopus 로고
    • Herpes simplex virus US3 protein kinase regulates virus-induced apoptosis in olfactory and vomeronasal chemosensory neurons in vivo
    • Mori, I.; Goshima, F.; Watanabe, D.; Ito, H.; Koide, N.; Yoshida, T.; Liu, B.; Kimura, Y.; Yokochi, T.; Nishiyama, Y. Herpes simplex virus US3 protein kinase regulates virus-induced apoptosis in olfactory and vomeronasal chemosensory neurons in vivo. Microbes Infect. 2006, 8, 1806-1812.
    • (2006) Microbes Infect , vol.8 , pp. 1806-1812
    • Mori, I.1    Goshima, F.2    Watanabe, D.3    Ito, H.4    Koide, N.5    Yoshida, T.6    Liu, B.7    Kimura, Y.8    Yokochi, T.9    Nishiyama, Y.10
  • 291
    • 0027330327 scopus 로고
    • The pathogenicity of a US3 protein kinase-deficient mutant of herpes simplex virus type 2 in mice
    • Kurachi, R.; Daikoku, T.; Tsurumi, T.; Maeno, K.; Nishiyama, Y.; Kurata, T. The pathogenicity of a US3 protein kinase-deficient mutant of herpes simplex virus type 2 in mice. Arch. Virol. 1993, 133, 259-273.
    • (1993) Arch. Virol , vol.133 , pp. 259-273
    • Kurachi, R.1    Daikoku, T.2    Tsurumi, T.3    Maeno, K.4    Nishiyama, Y.5    Kurata, T.6
  • 292
    • 0026802405 scopus 로고
    • Construction of a US3 lacZ insertion mutant of herpes simplex virus type 2 and characterization of its phenotype in vitro and in vivo
    • Nishiyama, Y.; Yamada, Y.; Kurachi, R.; Daikoku, T. Construction of a US3 lacZ insertion mutant of herpes simplex virus type 2 and characterization of its phenotype in vitro and in vivo. Virology 1992, 190, 256-268.
    • (1992) Virology , vol.190 , pp. 256-268
    • Nishiyama, Y.1    Yamada, Y.2    Kurachi, R.3    Daikoku, T.4
  • 293
    • 33845653234 scopus 로고    scopus 로고
    • Uses for JNK: The many and varied substrates of the c-Jun N-terminal kinases
    • Bogoyevitch, M.A.; Kobe, B. Uses for JNK: The many and varied substrates of the c-Jun N-terminal kinases. Microbiol. Mol. Biol. Rev. 2006, 70, 1061-1095.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 1061-1095
    • Bogoyevitch, M.A.1    Kobe, B.2
  • 295
    • 78650581104 scopus 로고    scopus 로고
    • Role of group A p21-activated kinases in the anti-apoptotic activity of the pseudorabies virus US3 protein kinase
    • Van den Broeke, C.; Radu, M.; Nauwynck, H.J.; Chernoff, J.; Favoreel, H.W. Role of group A p21-activated kinases in the anti-apoptotic activity of the pseudorabies virus US3 protein kinase. Virus Res. 2011, 155, 376-380.
    • (2011) Virus Res , vol.155 , pp. 376-380
    • van den Broeke, C.1    Radu, M.2    Nauwynck, H.J.3    Chernoff, J.4    Favoreel, H.W.5
  • 296
    • 0034766941 scopus 로고    scopus 로고
    • Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation
    • Geiss, B.J.; Tavis, J.E.; Metzger, L.M.; Leib, D.A.; Morrison, L.A. Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation. J. Virol. 2001, 75, 10721-10729.
    • (2001) J. Virol , vol.75 , pp. 10721-10729
    • Geiss, B.J.1    Tavis, J.E.2    Metzger, L.M.3    Leib, D.A.4    Morrison, L.A.5
  • 297
    • 77951031475 scopus 로고    scopus 로고
    • Bovine herpesvirus-1 US3 protein kinase: Critical residues and involvement in the phosphorylation of VP22
    • Labiuk, S.L.; Lobanov, V.; Lawman, Z.; Snider, M.; Babiuk, L.A.; van Drunen Littel-van den Hurk, S. Bovine herpesvirus-1 US3 protein kinase: Critical residues and involvement in the phosphorylation of VP22. J. Gen. Virol. 2010, 91, 1117-1126.
    • (2010) J. Gen. Virol , vol.91 , pp. 1117-1126
    • Labiuk, S.L.1    Lobanov, V.2    Lawman, Z.3    Snider, M.4    Babiuk, L.A.5    van Littel, D.6    van den Hurk, S.7
  • 298
    • 0030560984 scopus 로고    scopus 로고
    • Phosphorylation of the herpes simplex virus type 1 tegument protein VP22
    • Elliott, G.; O'Reilly, D.; O'Hare, P. Phosphorylation of the herpes simplex virus type 1 tegument protein VP22. Virology 1996, 226, 140-145.
    • (1996) Virology , vol.226 , pp. 140-145
    • Elliott, G.1    O'Reilly, D.2    O'Hare, P.3
  • 299
    • 0031901219 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules
    • Elliott, G.; O'Hare, P. Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules. J. Virol. 1998, 72, 6448-6455.
    • (1998) J. Virol , vol.72 , pp. 6448-6455
    • Elliott, G.1    O'Hare, P.2
  • 300
    • 0036238503 scopus 로고    scopus 로고
    • Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding
    • Martin, A.; O'Hare, P.; McLauchlan, J.; Elliott, G. Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding. J. Virol. 2002, 76, 4961-4970.
    • (2002) J. Virol , vol.76 , pp. 4961-4970
    • Martin, A.1    O'Hare, P.2    McLauchlan, J.3    Elliott, G.4
  • 302
    • 54949149816 scopus 로고    scopus 로고
    • Microtubule acetylation through HDAC6 inhibition results in increased transfection efficiency
    • Vaughan, E.E.; Geiger, R.C.; Miller, A.M.; Loh-Marley, P.L.; Suzuki, T.; Miyata, N.; Dean, D.A. Microtubule acetylation through HDAC6 inhibition results in increased transfection efficiency. Mol. Ther. 2008, 16, 1841-1847.
    • (2008) Mol. Ther , vol.16 , pp. 1841-1847
    • Vaughan, E.E.1    Geiger, R.C.2    Miller, A.M.3    Loh-Marley, P.L.4    Suzuki, T.5    Miyata, N.6    Dean, D.A.7
  • 303
    • 0034014715 scopus 로고    scopus 로고
    • Distinctions between bovine herpesvirus 1 and herpes simplex virus type 1 VP22 tegument protein subcellular associations
    • Harms, J.S.; Ren, X.; Oliveira, S.C.; Splitter, G.A. Distinctions between bovine herpesvirus 1 and herpes simplex virus type 1 VP22 tegument protein subcellular associations. J. Virol. 2000, 74, 3301-3312.
    • (2000) J. Virol , vol.74 , pp. 3301-3312
    • Harms, J.S.1    Ren, X.2    Oliveira, S.C.3    Splitter, G.A.4
  • 305
    • 0033154929 scopus 로고    scopus 로고
    • Intercellular spread of GFP-VP22
    • Aints, A.; Dilber, M.S.; Smith, C.I. Intercellular spread of GFP-VP22. J. Gene Med. 1999, 1, 275-279.
    • (1999) J. Gene Med , vol.1 , pp. 275-279
    • Aints, A.1    Dilber, M.S.2    Smith, C.I.3
  • 306
    • 0032896455 scopus 로고    scopus 로고
    • Intercellular delivery of thymidine kinase prodrug activating enzyme by the herpes simplex virus protein, VP22
    • Dilber, M.S.; Phelan, A.; Aints, A.; Mohamed, A.J.; Elliott, G.; Smith, C.I.; O'Hare, P. Intercellular delivery of thymidine kinase prodrug activating enzyme by the herpes simplex virus protein, VP22. Gene Ther. 1999, 6, 12-21.
    • (1999) Gene Ther , vol.6 , pp. 12-21
    • Dilber, M.S.1    Phelan, A.2    Aints, A.3    Mohamed, A.J.4    Elliott, G.5    Smith, C.I.6    O'Hare, P.7
  • 307
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott, G.; O'Hare, P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 1997, 88, 223-233.
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 308
    • 0037062508 scopus 로고    scopus 로고
    • Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection
    • Sciortino, M.T.; Taddeo, B.; Poon, A.P.; Mastino, A.; Roizman, B. Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection. Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 8318-8323.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 8318-8323
    • Sciortino, M.T.1    Taddeo, B.2    Poon, A.P.3    Mastino, A.4    Roizman, B.5
  • 309
    • 33645958290 scopus 로고    scopus 로고
    • Intercellular trafficking of the major tegument protein VP22 of bovine herpesvirus-1 and its application to improve a DNA vaccine
    • Zheng, C.F.; Brownlie, R.; Huang, D.Y.; Babiuk, L.A.; van Drunen Littel-van den Hurk, S. Intercellular trafficking of the major tegument protein VP22 of bovine herpesvirus-1 and its application to improve a DNA vaccine. Arch. Virol. 2006, 151, 985-993.
    • (2006) Arch. Virol , vol.151 , pp. 985-993
    • Zheng, C.F.1    Brownlie, R.2    Huang, D.Y.3    Babiuk, L.A.4    van Drunen, L.H.5
  • 311
    • 0038190872 scopus 로고    scopus 로고
    • HSV-1 VP22 augments adenoviral gene transfer to CNS neurons in the retina and striatum in vivo
    • Kretz, A.; Wybranietz, W.A.; Hermening, S.; Lauer, U.M.; Isenmann, S. HSV-1 VP22 augments adenoviral gene transfer to CNS neurons in the retina and striatum in vivo. Mol. Ther. 2003, 7, 659-669.
    • (2003) Mol. Ther , vol.7 , pp. 659-669
    • Kretz, A.1    Wybranietz, W.A.2    Hermening, S.3    Lauer, U.M.4    Isenmann, S.5
  • 312
    • 0036138814 scopus 로고    scopus 로고
    • The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents
    • del Rio, T.; Werner, H.C.; Enquist, L.W. The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents. J. Virol. 2002, 76, 774-782.
    • (2002) J. Virol , vol.76 , pp. 774-782
    • del Rio, T.1    Werner, H.C.2    Enquist, L.W.3
  • 313
    • 33748652681 scopus 로고    scopus 로고
    • Characterization of a UL49-null mutant: VP22 of herpes simplex virus type 1 facilitates viral spread in cultured cells and the mouse cornea
    • Duffy, C.; Lavail, J.H.; Tauscher, A.N.; Wills, E.G.; Blaho, J.A.; Baines, J.D. Characterization of a UL49-null mutant: VP22 of herpes simplex virus type 1 facilitates viral spread in cultured cells and the mouse cornea. J. Virol. 2006, 80, 8664-8675.
    • (2006) J. Virol , vol.80 , pp. 8664-8675
    • Duffy, C.1    Lavail, J.H.2    Tauscher, A.N.3    Wills, E.G.4    Blaho, J.A.5    Baines, J.D.6
  • 314
    • 77955207838 scopus 로고    scopus 로고
    • ICP0 dismantles microtubule networks in herpes simplex virus-infected cells
    • Liu, M.; Schmidt, E.E.; Halford, W.P. ICP0 dismantles microtubule networks in herpes simplex virus-infected cells. PLoS ONE 2010, 5, e10975.
    • (2010) PLoS ONE , vol.5
    • Liu, M.1    Schmidt, E.E.2    Halford, W.P.3
  • 315
    • 48249132077 scopus 로고    scopus 로고
    • Interactions of the HSV-1 UL25 capsid protein with cellular-associated protein with cellular microtubule-associated protein
    • Guo, L.; Zhang, Y.; Che, Y.; Wu, W.; Li, W.; Wang, L.; Liao, Y.; Liu, L.; Li, Q. Interactions of the HSV-1 UL25 capsid protein with cellular microtubule-associated protein. Virologica Sinica 2008, 23, 211-217.
    • (2008) Virologica Sinica , vol.23 , pp. 211-217
    • Guo, L.1    Zhang, Y.2    Che, Y.3    Wu, W.4    Li, W.5    Wang, L.6    Liao, Y.7    Liu, L.8    Li, Q.9
  • 316
    • 0035183978 scopus 로고    scopus 로고
    • Herpes simplex virus encodes a virion-associated protein which promotes long cellular processes in over-expressing cells
    • Takakuwa, H.; Goshima, F.; Koshizuka, T.; Murata, T.; Daikoku, T.; Nishiyama, Y. Herpes simplex virus encodes a virion-associated protein which promotes long cellular processes in over-expressing cells. Genes Cells 2001, 6, 955-966.
    • (2001) Genes Cells , vol.6 , pp. 955-966
    • Takakuwa, H.1    Goshima, F.2    Koshizuka, T.3    Murata, T.4    Daikoku, T.5    Nishiyama, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.