메뉴 건너뛰기




Volumn 78, Issue 12, 2004, Pages 6360-6369

Novel nuclear herniations induced by nuclear localization of a viral protein

Author keywords

[No Author keywords available]

Indexed keywords

LAMIN; PROTEIN OMEGA1S; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 2642520334     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.12.6360-6369.2004     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0026318583 scopus 로고
    • Biosynthesis of reovirus-specified polypeptides: Expression of reovirus S1-encoded sigma 1NS protein in transfected and infected cells as measured with serotype specific polyclonal antibody
    • Belli, B. A., and C. E. Samuel. 1991. Biosynthesis of reovirus-specified polypeptides: expression of reovirus S1-encoded sigma 1NS protein in transfected and infected cells as measured with serotype specific polyclonal antibody. Virology 185:698-709.
    • (1991) Virology , vol.185 , pp. 698-709
    • Belli, B.A.1    Samuel, C.E.2
  • 3
    • 0027944460 scopus 로고
    • nup1 mutants exhibit pleiotropic defects in nuclear pore complex function
    • Bogerd, A. M., J. A. Hoffman, D. C. Amberg, G. R. Fink, and L. I. Davis. 1994. nup1 mutants exhibit pleiotropic defects in nuclear pore complex function. J. Cell Biol. 127:319-332.
    • (1994) J. Cell Biol. , vol.127 , pp. 319-332
    • Bogerd, A.M.1    Hoffman, J.A.2    Amberg, D.C.3    Fink, G.R.4    Davis, L.I.5
  • 4
    • 0038381462 scopus 로고    scopus 로고
    • Two distinct phases of virus-induced NF-kappaB-regulation enhance TRAIL-mediated apoptosis in virus-infected cells
    • Clarke, P., S. M. Meintzer, L. Moffitt, and K. L. Tyler. 2003. Two distinct phases of virus-induced NF-kappaB-regulation enhance TRAIL-mediated apoptosis in virus-infected cells. J. Biol. Chem. 278:18092-18100.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18092-18100
    • Clarke, P.1    Meintzer, S.M.2    Moffitt, L.3    Tyler, K.L.4
  • 5
    • 0035164662 scopus 로고    scopus 로고
    • Reovirus infection activates JNK and the JNK-dependent transcription factor c-Jun
    • Clarke, P., S. M. Meintzer, C. Widmann, G. L. Johnson, and K. L. Tyler. 2001. Reovirus infection activates JNK and the JNK-dependent transcription factor c-Jun. J. Virol. 75:11275-11283.
    • (2001) J. Virol. , vol.75 , pp. 11275-11283
    • Clarke, P.1    Meintzer, S.M.2    Widmann, C.3    Johnson, G.L.4    Tyler, K.L.5
  • 7
    • 0036358297 scopus 로고    scopus 로고
    • Structures of importins
    • K. Weis (ed.). Springer-Verlag, Heidelberg, Germany
    • Conti, E. 2002. Structures of importins, p. 93-113. In K. Weis (ed.), Nuclear transport. Springer-Verlag, Heidelberg, Germany.
    • (2002) Nuclear Transport , pp. 93-113
    • Conti, E.1
  • 9
    • 0041707779 scopus 로고    scopus 로고
    • Reovirus-induced alteration in expression of apoptosis and DNA repair genes with potential roles in viral pathogenesis
    • DeBiasi, R. L., P. Clarke, S. Meintzer, R. Jotte, B. K. Kleinschmidt-Demasters, G. L. Johnson, and K. L. Tyler. 2003. Reovirus-induced alteration in expression of apoptosis and DNA repair genes with potential roles in viral pathogenesis. J. Virol. 77:8934-8947.
    • (2003) J. Virol. , vol.77 , pp. 8934-8947
    • DeBiasi, R.L.1    Clarke, P.2    Meintzer, S.3    Jotte, R.4    Kleinschmidt-Demasters, B.K.5    Johnson, G.L.6    Tyler, K.L.7
  • 11
    • 0025134429 scopus 로고
    • Sequence diversity in S1 genes and S1 translation products of 11 serotype 3 reovirus strains
    • Dermody, T. S., M. L. Nibert, R. Bassel-Duby, and B. N. Fields. 1990. Sequence diversity in S1 genes and S1 translation products of 11 serotype 3 reovirus strains. J. Virol. 64:4842-4850.
    • (1990) J. Virol. , vol.64 , pp. 4842-4850
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 12
    • 0037154838 scopus 로고    scopus 로고
    • Role of nucleoporin induction in releasing an mRNA nuclear export block
    • Enninga, J., D. E. Levy, G. Blobel, and B. M. Fontoura. 2002. Role of nucleoporin induction in releasing an mRNA nuclear export block. Science 295:1523-1525.
    • (2002) Science , vol.295 , pp. 1523-1525
    • Enninga, J.1    Levy, D.E.2    Blobel, G.3    Fontoura, B.M.4
  • 13
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • Favreau, C., E. Duboselard, C. Ostlund, C. Vigouroux, J. Capeau, M. Wehnert, D. Higuet, H. J. Worman, J. C. Courvalin, and B. Buendia. 2003. Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell Res. 282:14-23.
    • (2003) Exp. Cell Res. , vol.282 , pp. 14-23
    • Favreau, C.1    Duboselard, E.2    Ostlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6    Higuet, D.7    Worman, H.J.8    Courvalin, J.C.9    Buendia, B.10
  • 14
    • 0028008470 scopus 로고
    • Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport
    • Fortes, P., A. Beloso, and J. Ortin. 1994. Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport. EMBO J. 13:704-712.
    • (1994) EMBO J. , vol.13 , pp. 704-712
    • Fortes, P.1    Beloso, A.2    Ortin, J.3
  • 16
    • 0025005766 scopus 로고
    • Lamins A and C bind and assemble at the surface of mitotic chromosomes
    • Glass, J. R., and L. Gerace. 1990. Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111:1047-1057.
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1057
    • Glass, J.R.1    Gerace, L.2
  • 17
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleocytoplasmic trafficking and nuclear pore complex composition
    • Gustin, K. E., and P. Sarnow. 2001. Effects of poliovirus infection on nucleocytoplasmic trafficking and nuclear pore complex composition. EMBO J. 20:240-249.
    • (2001) EMBO J. , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 18
    • 0036337963 scopus 로고    scopus 로고
    • Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus
    • Gustin, K. E., and P. Sarnow. 2002. Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J. Virol. 76:8787-8796.
    • (2002) J. Virol. , vol.76 , pp. 8787-8796
    • Gustin, K.E.1    Sarnow, P.2
  • 20
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison, C. J. 2002. Lamins: building blocks or regulators of gene expression? Nat. Rev. Mol. Cell Biol. 3:848-858.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 21
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae
    • Lenz-Bohme, B., J. Wismar, S. Fuchs, R. Reifegerste, E. Buchner, H. Betz, and B. Schmitt. 1997. Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae. J. Cell Biol. 137:1001-1016.
    • (1997) J. Cell Biol. , vol.137 , pp. 1001-1016
    • Lenz-Bohme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6    Schmitt, B.7
  • 22
    • 0037470055 scopus 로고    scopus 로고
    • Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus functionally interacts with heterochromatin protein 1
    • Lim, C., D. Lee, T. Seo, C. Choi, and J. Choe. 2003. Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus functionally interacts with heterochromatin protein 1. J. Biol. Chem. 278:7397-7405.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7397-7405
    • Lim, C.1    Lee, D.2    Seo, T.3    Choi, C.4    Choe, J.5
  • 23
    • 0033749567 scopus 로고    scopus 로고
    • Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes
    • Liu, J., T. R. Ben Shahar, D. Riemer, M. Treinin, P. Spann, K. Weber, A. Fire, and Y. Gruenbaum. 2000. Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol. Biol. Cell. 11:3937-3947.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Ben Shahar, T.R.2    Riemer, D.3    Treinin, M.4    Spann, P.5    Weber, K.6    Fire, A.7    Gruenbaum, Y.8
  • 24
    • 0035201307 scopus 로고    scopus 로고
    • The structure and function of nuclear lamins: Implications for disease
    • Moir, R. D., and T. P. Spann. 2001. The structure and function of nuclear lamins: implications for disease. Cell Mol. Life Sci. 58:1748-1757.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1748-1757
    • Moir, R.D.1    Spann, T.P.2
  • 25
    • 0034640884 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization blocks the elongation phase of DNA replication
    • Moir, R. D., T. P. Spann, H. Herrmann, and R. D. Goldman. 2000. Disruption of nuclear lamin organization blocks the elongation phase of DNA replication. J. Cell Biol. 149:1179-1192.
    • (2000) J. Cell Biol. , vol.149 , pp. 1179-1192
    • Moir, R.D.1    Spann, T.P.2    Herrmann, H.3    Goldman, R.D.4
  • 26
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi, W., J. Haas, M. Wagner, G. Krohne, and U. H. Koszinowski. 2002. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 297:854-857.
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 27
    • 0035902446 scopus 로고    scopus 로고
    • Multiple vesiculoviral matrix proteins inhibit both nuclear export and import
    • Petersen, J. M., L. S. Her, and J. E. Dahlberg. 2001. Multiple vesiculoviral matrix proteins inhibit both nuclear export and import. Proc. Natl. Acad. Sci. USA 98:8590-8595.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8590-8595
    • Petersen, J.M.1    Her, L.S.2    Dahlberg, J.E.3
  • 28
    • 0033761842 scopus 로고    scopus 로고
    • The matrix protein of vesicular stomatitis virus inhibits nucleocytoplasmic transport when it is in the nucleus and associated with nuclear pore complexes
    • Petersen, J. M., L. S. Her, V. Varvel, E. Lund, and J. E. Dahlberg. 2000. The matrix protein of vesicular stomatitis virus inhibits nucleocytoplasmic transport when it is in the nucleus and associated with nuclear pore complexes. Mol. Cell. Biol. 20:8590-8601.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8590-8601
    • Petersen, J.M.1    Her, L.S.2    Varvel, V.3    Lund, E.4    Dahlberg, J.E.5
  • 29
    • 0033163714 scopus 로고    scopus 로고
    • Four-dimensional control of the cell cycle
    • Pines, J. 1999. Four-dimensional control of the cell cycle. Nat. Cell Biol. 1:E73-E79.
    • (1999) Nat. Cell Biol. , vol.1
    • Pines, J.1
  • 31
    • 0034742597 scopus 로고    scopus 로고
    • 2)/M phase cell cycle arrest is associated with inhibition of p34 (cdc2)
    • 2)/M phase cell cycle arrest is associated with inhibition of p34 (cdc2). J. Virol. 75:7429-7434.
    • (2001) J. Virol. , vol.75 , pp. 7429-7434
    • Poggioli, G.J.1    Dermody, T.S.2    Tyler, K.L.3
  • 33
    • 0032504065 scopus 로고    scopus 로고
    • Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents
    • Poon, B., K. Grovit-Ferbas, S. A. Stewart, and I. S. Chen. 1998. Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents. Science 281:266-269.
    • (1998) Science , vol.281 , pp. 266-269
    • Poon, B.1    Grovit-Ferbas, K.2    Stewart, S.A.3    Chen, I.S.4
  • 34
    • 0031707093 scopus 로고    scopus 로고
    • Reovirus growth in cell culture does not require the full complement of viral proteins: Identification of a α1s-null mutant
    • Rodgers, S. E., J. L. Connolly, J. D. Chappell, and T. S. Dermody. 1998. Reovirus growth in cell culture does not require the full complement of viral proteins: identification of a α1s-null mutant. J. Virol. 72:8597-8604.
    • (1998) J. Virol. , vol.72 , pp. 8597-8604
    • Rodgers, S.E.1    Connolly, J.L.2    Chappell, J.D.3    Dermody, T.S.4
  • 35
    • 0037405246 scopus 로고    scopus 로고
    • Recruitment of Tat to heterochromatin protein HP1 via interaction with CTIP2 inhibits human immunodeficiency virus type 1 replication in microglial cells
    • Rohr, O., D. Lecestre, S. Chasserot-Golaz, C. Marban, D. Avram, D. Aunis, M. Leid, and E. Schaeffer. 2003. Recruitment of Tat to heterochromatin protein HP1 via interaction with CTIP2 inhibits human immunodeficiency virus type 1 replication in microglial cells. J. Virol. 77:5415-5427.
    • (2003) J. Virol. , vol.77 , pp. 5415-5427
    • Rohr, O.1    Lecestre, D.2    Chasserot-Golaz, S.3    Marban, C.4    Avram, D.5    Aunis, D.6    Leid, M.7    Schaeffer, E.8
  • 36
    • 0035972145 scopus 로고    scopus 로고
    • Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization
    • Schirmer, E. C., T. Guan, and L. Gerace. 2001. Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J. Cell Biol. 153:479-489.
    • (2001) J. Cell Biol. , vol.153 , pp. 479-489
    • Schirmer, E.C.1    Guan, T.2    Gerace, L.3
  • 37
    • 0034892692 scopus 로고    scopus 로고
    • Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection
    • Scott, E. S., and P. O'Hare. 2001. Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection. J. Virol. 75:8818-8830.
    • (2001) J. Virol. , vol.75 , pp. 8818-8830
    • Scott, E.S.1    O'Hare, P.2
  • 38
    • 0035155641 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling by human immunodeficiency virus type 1 Vpr
    • Sherman, M. P., C. M. de Noronha, M. I. Heusch, S. Greene, and W. C. Greene. 2001. Nucleocytoplasmic shuttling by human immunodeficiency virus type 1 Vpr. J. Virol. 75:1522-1532.
    • (2001) J. Virol. , vol.75 , pp. 1522-1532
    • Sherman, M.P.1    De Noronha, C.M.2    Heusch, M.I.3    Greene, S.4    Greene, W.C.5
  • 39
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • Stuurman, N., S. Heins, and U. Aebi. 1998. Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 122:42-66.
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 41
    • 0028826078 scopus 로고
    • Differences in the capacity of reovirus strains to induce apoptosis are determined by the viral attachment protein sigma 1
    • Tyler, K. L., M. K. Squier, S. E. Rodgers, B. E. Schneider, S. M. Oberhaus, T. A. Grdina, J. J. Cohen, and T. S. Dermody. 1995. Differences in the capacity of reovirus strains to induce apoptosis are determined by the viral attachment protein sigma 1. J. Virol. 69:6972-6979.
    • (1995) J. Virol. , vol.69 , pp. 6972-6979
    • Tyler, K.L.1    Squier, M.K.2    Rodgers, S.E.3    Schneider, B.E.4    Oberhaus, S.M.5    Grdina, T.A.6    Cohen, J.J.7    Dermody, T.S.8
  • 42
    • 0035691915 scopus 로고    scopus 로고
    • Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene
    • Vigouroux, C., M. Auclair, E. Dubosclard, M. Pouchelet, J. Capeau, J. C. Courvalin, and B. Buendia. 2001. Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene. J. Cell Sci. 114:4459-4468.
    • (2001) J. Cell Sci. , vol.114 , pp. 4459-4468
    • Vigouroux, C.1    Auclair, M.2    Dubosclard, E.3    Pouchelet, M.4    Capeau, J.5    Courvalin, J.C.6    Buendia, B.7
  • 43
    • 0028233485 scopus 로고
    • NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure
    • Wente, S. R., and G. Blobel. 1994. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J. Cell Biol. 125:955-969.
    • (1994) J. Cell Biol. , vol.125 , pp. 955-969
    • Wente, S.R.1    Blobel, G.2
  • 44
    • 0034849496 scopus 로고    scopus 로고
    • Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division
    • Wurm, T., H. Chen, T. Hodgson, P. Britton, G. Brooks, and J. A. Hiscox. 2001. Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division. J. Virol. 75:9345-9356.
    • (2001) J. Virol. , vol.75 , pp. 9345-9356
    • Wurm, T.1    Chen, H.2    Hodgson, T.3    Britton, P.4    Brooks, G.5    Hiscox, J.A.6
  • 45
    • 0032888954 scopus 로고    scopus 로고
    • Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1
    • Zolotukhin, A. S., and B. K. Felber. 1999. Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev. J. Virol. 73:120-127.
    • (1999) Rev. J. Virol. , vol.73 , pp. 120-127
    • Zolotukhin, A.S.1    Felber, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.