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Volumn 415, Issue 2, 2011, Pages 114-121

PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1

Author keywords

Cytoskeleton; ERM proteins; Microtubules; Moesin; PDZD8; Viral infection

Indexed keywords

MOESIN; PDZD8 PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 79957785375     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.04.006     Document Type: Article
Times cited : (21)

References (55)
  • 1
    • 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(12):7472-7482.
    • (1995) J. Virol. , vol.69 , Issue.12 , 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
  • 3
    • 0035807711 scopus 로고    scopus 로고
    • Assessment of the subcellular localization of the herpes simplex virus structural protein VP22 in the absence of other viral gene products
    • Blouin A., Blaho J.A. Assessment of the subcellular localization of the herpes simplex virus structural protein VP22 in the absence of other viral gene products. Virus Res. 2001, 81(1-2):57-68.
    • (2001) Virus Res. , vol.81 , Issue.1-2 , pp. 57-68
    • Blouin, A.1    Blaho, J.A.2
  • 4
    • 0035656829 scopus 로고    scopus 로고
    • Polarity and developmental regulation of two PDZ proteins in the retinal pigment epithelium
    • Bonilha V.L., Rodriguez-Boulan E. Polarity and developmental regulation of two PDZ proteins in the retinal pigment epithelium. Invest. Ophthalmol. Vis. Sci. 2001, 42(13):3274-3282.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , Issue.13 , pp. 3274-3282
    • Bonilha, V.L.1    Rodriguez-Boulan, E.2
  • 5
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho K.O., Hunt C.A., Kennedy M.B. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 1992, 9(5):929-942.
    • (1992) Neuron , vol.9 , Issue.5 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 7
    • 0023097012 scopus 로고
    • Microtubules and intermediate filaments of herpes simplex virus infected cells
    • Dienes H.P., Hiller G., Müller S., Falke D. Microtubules and intermediate filaments of herpes simplex virus infected cells. Arch. Virol. 1987, 94(1-2):15-28.
    • (1987) Arch. Virol. , vol.94 , Issue.1-2 , pp. 15-28
    • Dienes, H.P.1    Hiller, G.2    Müller, S.3    Falke, D.4
  • 9
    • 0017849068 scopus 로고
    • Involvement of microtubules in cytopathic effects of animal viruses: early proteins of adenovirus and herpesvirus inhibit formation of microtubular paracrystals in HeLa-S3 cells
    • Ebina T., Satake M., Ishida N. Involvement of microtubules in cytopathic effects of animal viruses: early proteins of adenovirus and herpesvirus inhibit formation of microtubular paracrystals in HeLa-S3 cells. J. Gen. Virol. 1978, 38(3):535-548.
    • (1978) J. Gen. Virol. , vol.38 , Issue.3 , pp. 535-548
    • Ebina, T.1    Satake, M.2    Ishida, N.3
  • 10
    • 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(8):6448-6455.
    • (1998) J. Virol. , vol.72 , Issue.8 , pp. 6448-6455
    • Elliott, G.1    O'Hare, P.2
  • 11
    • 0033180348 scopus 로고    scopus 로고
    • Protein modules as organizers of membrane structure
    • Fanning A.S., Anderson J.M. Protein modules as organizers of membrane structure. Curr. Opin. Cell Biol. 1999, 11(4):432-439.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , Issue.4 , pp. 432-439
    • Fanning, A.S.1    Anderson, J.M.2
  • 13
    • 58549092371 scopus 로고    scopus 로고
    • Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density
    • Feng W., Zhang M. Organization and dynamics of PDZ-domain-related supramodules in the postsynaptic density. Nat. Rev. Neurosci. 2009, 10(2):87-99.
    • (2009) Nat. Rev. Neurosci. , vol.10 , Issue.2 , pp. 87-99
    • Feng, W.1    Zhang, M.2
  • 14
    • 34247516852 scopus 로고    scopus 로고
    • ERM proteins in epithelial cell organization and functions
    • Fievet B., Louvard D., Arpin M. ERM proteins in epithelial cell organization and functions. Biochim. Biophys. Acta 2007, 1773(5):653-660.
    • (2007) Biochim. Biophys. Acta , vol.1773 , Issue.5 , pp. 653-660
    • Fievet, B.1    Louvard, D.2    Arpin, M.3
  • 16
    • 32944475622 scopus 로고    scopus 로고
    • A superhighway to virus infection
    • Greber U.F., Way M. A superhighway to virus infection. Cell 2006, 124(4):741-754.
    • (2006) Cell , vol.124 , Issue.4 , pp. 741-754
    • Greber, U.F.1    Way, M.2
  • 17
    • 42449159718 scopus 로고    scopus 로고
    • The ERM family member ezrin regulates stable microtubule formation and retroviral infection
    • Haedicke J., de los Santos K., Mott C., Goff S.P., Naghavi M.H. The ERM family member ezrin regulates stable microtubule formation and retroviral infection. J. Virol. 2008, 82:4665-4670.
    • (2008) J. Virol. , vol.82 , pp. 4665-4670
    • Haedicke, J.1    de los Santos, K.2    Mott, C.3    Goff, S.P.4    Naghavi, M.H.5
  • 18
    • 0029791770 scopus 로고    scopus 로고
    • Studies to show that with podophyllotoxin the early replicative stages of herpes simplex virus type 1 depend upon functional cytoplasmic microtubules
    • Hammonds T.R., Denyer S.P., Jackson D.E., Irving W.L. Studies to show that with podophyllotoxin the early replicative stages of herpes simplex virus type 1 depend upon functional cytoplasmic microtubules. J. Med. Microbiol. 1996, 45(3):167-172.
    • (1996) J. Med. Microbiol. , vol.45 , Issue.3 , pp. 167-172
    • Hammonds, T.R.1    Denyer, S.P.2    Jackson, D.E.3    Irving, W.L.4
  • 19
    • 0019805013 scopus 로고
    • Microtubules and microfilaments in HSV-infected rabbit-kidney cells
    • Heeg U., Haase W., Brauer D., Falke D. Microtubules and microfilaments in HSV-infected rabbit-kidney cells. Arch. Virol. 1981, 70(3):233-246.
    • (1981) Arch. Virol. , vol.70 , Issue.3 , pp. 233-246
    • Heeg, U.1    Haase, W.2    Brauer, D.3    Falke, D.4
  • 20
    • 77956636731 scopus 로고    scopus 로고
    • PDZD8 is a novel Gag-interacting factor that promotes retroviral infection
    • Henning M.S., Morham S.G., Goff S.P., Naghavi M.H. PDZD8 is a novel Gag-interacting factor that promotes retroviral infection. J. Virol. 2010, 84(17):8990-8995.
    • (2010) J. Virol. , vol.84 , Issue.17 , pp. 8990-8995
    • Henning, M.S.1    Morham, S.G.2    Goff, S.P.3    Naghavi, M.H.4
  • 21
    • 0029115575 scopus 로고
    • Establishment of human microglial cell lines after transfection of primary cultures of embryonic microglial cells with the SV40 large T antigen
    • Janabi N., Peudenier S., Heron B., Ng K.H., Tardieu M. Establishment of human microglial cell lines after transfection of primary cultures of embryonic microglial cells with the SV40 large T antigen. Neurosci. Lett. 1995, 195(2):105-108.
    • (1995) Neurosci. Lett. , vol.195 , Issue.2 , pp. 105-108
    • Janabi, N.1    Peudenier, S.2    Heron, B.3    Ng, K.H.4    Tardieu, M.5
  • 22
    • 67449089190 scopus 로고    scopus 로고
    • The hepatitis E virus open reading frame 3 product interacts with microtubules and interferes with their dynamics
    • Kannan H., Fan S., Patel D., Bossis I., Zhang Y.J. The hepatitis E virus open reading frame 3 product interacts with microtubules and interferes with their dynamics. J. Virol. 2009, 83(13):6375-6382.
    • (2009) J. Virol. , vol.83 , Issue.13 , pp. 6375-6382
    • Kannan, H.1    Fan, S.2    Patel, D.3    Bossis, I.4    Zhang, Y.J.5
  • 23
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • Kennedy M.B. Origin of PDZ (DHR, GLGF) domains. Trends Biochem. Sci. 1995, 20(9):350.
    • (1995) Trends Biochem. Sci. , vol.20 , Issue.9 , pp. 350
    • Kennedy, M.B.1
  • 24
    • 0034881153 scopus 로고    scopus 로고
    • Microtubule reorganization during herpes simplex virus type 1 infection facilitates the nuclear localization of VP22, a major virion tegument protein
    • Kotsakis A., Pomeranz L.E., Blouin A., Blaho J.A. Microtubule reorganization during herpes simplex virus type 1 infection facilitates the nuclear localization of VP22, a major virion tegument protein. J. Virol. 2001, 75(18):8697-8711.
    • (2001) J. Virol. , vol.75 , Issue.18 , pp. 8697-8711
    • Kotsakis, A.1    Pomeranz, L.E.2    Blouin, A.3    Blaho, J.A.4
  • 25
    • 0034597128 scopus 로고    scopus 로고
    • Dishevelled-1 regulates microtubule stability: a new function mediated by glycogen synthase kinase-3beta
    • Krylova O., Messenger M.J., Salinas P.C. Dishevelled-1 regulates microtubule stability: a new function mediated by glycogen synthase kinase-3beta. J. Cell Biol. 2000, 151(1):83-94.
    • (2000) J. Cell Biol. , vol.151 , Issue.1 , pp. 83-94
    • Krylova, O.1    Messenger, M.J.2    Salinas, P.C.3
  • 26
    • 77951763488 scopus 로고    scopus 로고
    • A regulated complex of the scaffolding proteins PDZK1 and EBP50 with ezrin contribute to microvillar organization
    • LaLonde D.P., Garbett D., Bretscher A. A regulated complex of the scaffolding proteins PDZK1 and EBP50 with ezrin contribute to microvillar organization. Mol. Biol. Cell 2010, 21(9):1519-1529.
    • (2010) Mol. Biol. Cell , vol.21 , Issue.9 , pp. 1519-1529
    • LaLonde, D.P.1    Garbett, D.2    Bretscher, A.3
  • 27
    • 0038205871 scopus 로고    scopus 로고
    • Role of PDZ domain-containing proteins and ERM proteins in regulation of renal function and dysfunction
    • Levi M. Role of PDZ domain-containing proteins and ERM proteins in regulation of renal function and dysfunction. J. Am. Soc. Nephrol. 2003, 14(7):1949-1951.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , Issue.7 , pp. 1949-1951
    • Levi, M.1
  • 28
    • 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(6):e10975.
    • (2010) PLoS One , vol.5 , Issue.6
    • Liu, M.1    Schmidt, E.E.2    Halford, W.P.3
  • 29
    • 0029846832 scopus 로고    scopus 로고
    • Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain
    • Lue R.A., Brandin E., Chan E.P., Branton D. Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain. J. Cell Biol. 1996, 135(4):1125-1137.
    • (1996) J. Cell Biol. , vol.135 , Issue.4 , pp. 1125-1137
    • Lue, R.A.1    Brandin, E.2    Chan, E.P.3    Branton, D.4
  • 30
    • 0029851093 scopus 로고    scopus 로고
    • Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton
    • Marfatia S.M., Morais Cabral J.H., Lin L., Hough C., Bryant P.J., Stolz L., Chishti A.H. Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton. J. Cell Biol. 1996, 135(3):753-766.
    • (1996) J. Cell Biol. , vol.135 , Issue.3 , pp. 753-766
    • Marfatia, S.M.1    Morais Cabral, J.H.2    Lin, L.3    Hough, C.4    Bryant, P.J.5    Stolz, L.6    Chishti, A.H.7
  • 32
    • 53749092892 scopus 로고    scopus 로고
    • Efficient quiescent infection of normal human diploid fibroblasts with wild-type herpes simplex virus type 1
    • McMahon R., Walsh D. Efficient quiescent infection of normal human diploid fibroblasts with wild-type herpes simplex virus type 1. J. Virol. 2008, 82(20):10218-10230.
    • (2008) J. Virol. , vol.82 , Issue.20 , pp. 10218-10230
    • McMahon, R.1    Walsh, D.2
  • 33
    • 33846496911 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC) protein regulates epithelial cell migration and morphogenesis via PDZ domain-based interactions with plasma membranes
    • Mimori-Kiyosue Y., Matsui C., Sasaki H., Tsukita S. Adenomatous polyposis coli (APC) protein regulates epithelial cell migration and morphogenesis via PDZ domain-based interactions with plasma membranes. Genes Cells 2007, 12(2):219-233.
    • (2007) Genes Cells , vol.12 , Issue.2 , pp. 219-233
    • Mimori-Kiyosue, Y.1    Matsui, C.2    Sasaki, H.3    Tsukita, S.4
  • 34
    • 18244397937 scopus 로고    scopus 로고
    • Overexpression of fasciculation and elongation protein zeta-1 (FEZ1) induces a post-entry block to retroviruses in cultured cells
    • Naghavi M.H., Hatziioannou T., Gao G., Goff S.P. Overexpression of fasciculation and elongation protein zeta-1 (FEZ1) induces a post-entry block to retroviruses in cultured cells. Genes Dev. 2005, 19(9):1105-1115.
    • (2005) Genes Dev. , vol.19 , Issue.9 , pp. 1105-1115
    • Naghavi, M.H.1    Hatziioannou, T.2    Gao, G.3    Goff, S.P.4
  • 36
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt P.P., Krishnan H.H., Smith M.S., Chandran B. Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J. Virol. 2005, 79(2):1191-1206.
    • (2005) J. Virol. , vol.79 , Issue.2 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 37
    • 0032775897 scopus 로고    scopus 로고
    • Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection
    • Pomeranz L.E., Blaho J.A. Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J. Virol. 1999, 73(8):6769-6781.
    • (1999) J. Virol. , vol.73 , Issue.8 , pp. 6769-6781
    • Pomeranz, L.E.1    Blaho, J.A.2
  • 38
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: targeting signalling molecules to sub-membranous sites
    • Ponting C.P., Phillips C., Davies K.E., Blake D.J. PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays 1997, 19(6):469-479.
    • (1997) Bioessays , vol.19 , Issue.6 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 39
    • 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(3):387-400.
    • (2006) Cell. Microbiol. , vol.8 , Issue.3 , pp. 387-400
    • Radtke, K.1    Dohner, K.2    Sodeik, B.3
  • 40
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • Lippincott, Williams and Wilkins, D.M. Knipe, P.M. Howley (Eds.)
    • Roizman B., Knipe D.M., Whitley R.J. Herpes simplex viruses. Fields Virology 2007, Lippincott, Williams and Wilkins. 5th edition ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2007) Fields Virology
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 41
    • 1842536029 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 envelope glycoprotein gB induces the integrin-dependent focal adhesion kinase-Src-phosphatidylinositol 3-kinase-rho GTPase signal pathways and cytoskeletal rearrangements
    • Sharma-Walia N., Naranatt P.P., Krishnan H.H., Zeng L., Chandran B. Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 envelope glycoprotein gB induces the integrin-dependent focal adhesion kinase-Src-phosphatidylinositol 3-kinase-rho GTPase signal pathways and cytoskeletal rearrangements. J. Virol. 2004, 78(8):4207-4223.
    • (2004) J. Virol. , vol.78 , Issue.8 , pp. 4207-4223
    • Sharma-Walia, N.1    Naranatt, P.P.2    Krishnan, H.H.3    Zeng, L.4    Chandran, B.5
  • 42
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M., Sala C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 2001, 24:1-29.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 43
    • 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(11):955-966.
    • (2001) Genes Cells , vol.6 , Issue.11 , pp. 955-966
    • Takakuwa, H.1    Goshima, F.2    Koshizuka, T.3    Murata, T.4    Daikoku, T.5    Nishiyama, Y.6
  • 44
    • 0037240318 scopus 로고    scopus 로고
    • Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF)
    • Terawaki S., Maesaki R., Okada K., Hakoshima T. Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF). Acta Crystallogr. D Biol. Crystallogr. 2003, 59(Pt 1):177-179.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , Issue.PT 1 , pp. 177-179
    • Terawaki, S.1    Maesaki, R.2    Okada, K.3    Hakoshima, T.4
  • 45
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita S., Yonemura S. Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 1999, 274(49):34507-34510.
    • (1999) J. Biol. Chem. , vol.274 , Issue.49 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 47
    • 1842831274 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells
    • Walsh D., Mohr I. Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells. Genes Dev. 2004, 18(6):660-672.
    • (2004) Genes Dev. , vol.18 , Issue.6 , pp. 660-672
    • Walsh, D.1    Mohr, I.2
  • 48
    • 32644444260 scopus 로고    scopus 로고
    • Assembly of an active translation initiation factor complex by a viral protein
    • Walsh D., Mohr I. Assembly of an active translation initiation factor complex by a viral protein. Genes Dev. 2006, 20(4):461-472.
    • (2006) Genes Dev. , vol.20 , Issue.4 , pp. 461-472
    • Walsh, D.1    Mohr, I.2
  • 49
    • 35448990549 scopus 로고    scopus 로고
    • The contributions of microtubule stability and dynamic instability to adenovirus nuclear localization efficiency
    • Warren J.C., Cassimeris L. The contributions of microtubule stability and dynamic instability to adenovirus nuclear localization efficiency. Cell Motil. Cytoskeleton 2007, 64(9):675-689.
    • (2007) Cell Motil. Cytoskeleton , vol.64 , Issue.9 , pp. 675-689
    • Warren, J.C.1    Cassimeris, L.2
  • 50
    • 33746658599 scopus 로고    scopus 로고
    • Infection with replication-deficient adenovirus induces changes in the dynamic instability of host cell microtubules
    • Warren J.C., Rutkowski A., Cassimeris L. Infection with replication-deficient adenovirus induces changes in the dynamic instability of host cell microtubules. Mol. Biol. Cell 2006, 17(8):3557-3568.
    • (2006) Mol. Biol. Cell , vol.17 , Issue.8 , pp. 3557-3568
    • Warren, J.C.1    Rutkowski, A.2    Cassimeris, L.3
  • 51
    • 3142642871 scopus 로고    scopus 로고
    • Bidirectional transport along microtubules
    • Welte M.A. Bidirectional transport along microtubules. Curr. Biol. 2004, 14(13):R525-R537.
    • (2004) Curr. Biol. , vol.14 , Issue.13
    • Welte, M.A.1
  • 53
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S., Weber K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 2003, 4(12):938-947.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.12 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 54
    • 34250900288 scopus 로고    scopus 로고
    • Microtubule-mediated and microtubule-independent transport of adenovirus type 5 in HEK293 cells
    • Yea C., Dembowy J., Pacione L., Brown M. Microtubule-mediated and microtubule-independent transport of adenovirus type 5 in HEK293 cells. J. Virol. 2007, 81(13):6899-6908.
    • (2007) J. Virol. , vol.81 , Issue.13 , pp. 6899-6908
    • Yea, C.1    Dembowy, J.2    Pacione, L.3    Brown, M.4
  • 55
    • 16244412942 scopus 로고    scopus 로고
    • Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import
    • Yedowitz J.C., Kotsakis A., Schlegel E.F., Blaho J.A. Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import. J. Virol. 2005, 79(8):4730-4743.
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 4730-4743
    • Yedowitz, J.C.1    Kotsakis, A.2    Schlegel, E.F.3    Blaho, J.A.4


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