메뉴 건너뛰기




Volumn 77, Issue 16, 2003, Pages 9052-9068

Redistribution of cyclophilin A to viral factories during vaccinia virus infection and its incorporation into mature particles

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN A; CYCLOSPORIN A; VIROSOME;

EID: 0042208090     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.16.9052-9068.2003     Document Type: Article
Times cited : (74)

References (58)
  • 1
    • 0242528876 scopus 로고    scopus 로고
    • Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase
    • Arevalo-Rodriguez, M., M. E. Cardenas, X. Wu, S. D. Hanes, and J. Heitman. 2000. Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 19:3739-3749.
    • (2000) EMBO J. , vol.19 , pp. 3739-3749
    • Arevalo-Rodriguez, M.1    Cardenas, M.E.2    Wu, X.3    Hanes, S.D.4    Heitman, J.5
  • 2
    • 0030727448 scopus 로고    scopus 로고
    • Preferential virosomal location of under-phosphorylated H5R protein synthesized in vaccinia virus-infected cells
    • Beaud, G., and R. Beaud. 1997. Preferential virosomal location of under-phosphorylated H5R protein synthesized in vaccinia virus-infected cells. J. Gen. Virol. 78:3297-3302.
    • (1997) J. Gen. Virol. , vol.78 , pp. 3297-3302
    • Beaud, G.1    Beaud, R.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0035930607 scopus 로고    scopus 로고
    • Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles
    • Brown, C. R., D. Y. Cui, G. G. Hung, and H. L. Chiang. 2001. Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles. J. Biol. Chem. 276:48017-48026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48017-48026
    • Brown, C.R.1    Cui, D.Y.2    Hung, G.G.3    Chiang, H.L.4
  • 6
    • 0033544878 scopus 로고    scopus 로고
    • Transcription factor YY1 is a vaccinia virus late promoter activator
    • Broyles, S. S., X. Liu, M. Zhu, and M. Kremer. 1999. Transcription factor YY1 is a vaccinia virus late promoter activator. J. Biol. Chem. 274:35662-35667.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35662-35667
    • Broyles, S.S.1    Liu, X.2    Zhu, M.3    Kremer, M.4
  • 7
    • 0033155422 scopus 로고    scopus 로고
    • Distribution of cytoskeletal structures and organelles of the host cell during evolution of the intracellular parasitism by Trypanosoma cruzi
    • Carvalho, T. M., A. G. Ferreira, E. S. Coimbra, C. T. Rosestolato, and W. De Souza. 1999. Distribution of cytoskeletal structures and organelles of the host cell during evolution of the intracellular parasitism by Trypanosoma cruzi. J. Submicrosc. Cytol. Pathol. 31:325-333.
    • (1999) J. Submicrosc. Cytol. Pathol. , vol.31 , pp. 325-333
    • Carvalho, T.M.1    Ferreira, A.G.2    Coimbra, E.S.3    Rosestolato, C.T.4    De Souza, W.5
  • 8
    • 0029948529 scopus 로고    scopus 로고
    • Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization
    • Colgan, J., H. E. Yuan, E. K. Franke, and J. Luban. 1996. Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization. J. Virol. 70:4299-4310.
    • (1996) J. Virol. , vol.70 , pp. 4299-4310
    • Colgan, J.1    Yuan, H.E.2    Franke, E.K.3    Luban, J.4
  • 9
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley, N. J., E. K. Baker, M. A. Stamnes, and C. S. Zuker. 1991. The cyclophilin homolog ninaA is required in the secretory pathway. Cell 67:255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 11
    • 0028866712 scopus 로고
    • Actin-based motility of vaccinia virus
    • Cudmore, S., P. Cossart, G. Griffiths, and M. Way. 1995. Actin-based motility of vaccinia virus. Nature 378:636-638.
    • (1995) Nature , vol.378 , pp. 636-638
    • Cudmore, S.1    Cossart, P.2    Griffiths, G.3    Way, M.4
  • 12
    • 0033854259 scopus 로고    scopus 로고
    • Characterization of the vaccinia virus H3L envelope protein: Topology and posttranslational membrane insertion via the C-terminal hydrophobic tail
    • da Fonseca, F. G., E. J. Wolffe, A. Weisberg, and B. Moss. 2000. Characterization of the vaccinia virus H3L envelope protein: topology and posttranslational membrane insertion via the C-terminal hydrophobic tail. J. Virol. 74:7508-7517.
    • (2000) J. Virol. , vol.74 , pp. 7508-7517
    • Da Fonseca, F.G.1    Wolffe, E.J.2    Weisberg, A.3    Moss, B.4
  • 13
    • 0000332478 scopus 로고
    • The development of vaccinia virus in Earle's strain L cells as examined by electron microscopy
    • Dales, S., and L. Siminovitch. 1961. The development of vaccinia virus in Earle's strain L cells as examined by electron microscopy. J. Biophys. Biochem. Cytol. 10:475-503.
    • (1961) J. Biophys. Biochem. Cytol. , vol.10 , pp. 475-503
    • Dales, S.1    Siminovitch, L.2
  • 14
    • 0034715790 scopus 로고    scopus 로고
    • An emergent poxvirus from humans and cattle in Rio de Janeiro State: Cantagalo virus may derive from Brazilian smallpox vaccine
    • Damaso, C. R., J. J. Esposito, R. C. Condit, and N. Moussatché. 2000. An emergent poxvirus from humans and cattle in Rio de Janeiro State: Cantagalo virus may derive from Brazilian smallpox vaccine. Virology 277:439-449.
    • (2000) Virology , vol.277 , pp. 439-449
    • Damaso, C.R.1    Esposito, J.J.2    Condit, R.C.3    Moussatché, N.4
  • 15
    • 0027947038 scopus 로고
    • Cyclosporin A inhibits vaccinia virus replication in vitro
    • Damaso, C. R., and S. J. Keller. 1994. Cyclosporin A inhibits vaccinia virus replication in vitro. Arch. Virol. 134:303-319.
    • (1994) Arch. Virol. , vol.134 , pp. 303-319
    • Damaso, C.R.1    Keller, S.J.2
  • 16
    • 0031975724 scopus 로고    scopus 로고
    • Inhibition of vaccinia virus replication by cyclosporin A analogues correlates with their affinity for cellular cyclophilins
    • Damaso, C. R., and N. Moussatché. 1998. Inhibition of vaccinia virus replication by cyclosporin A analogues correlates with their affinity for cellular cyclophilins. J. Gen. Virol. 79:339-346.
    • (1998) J. Gen. Virol. , vol.79 , pp. 339-346
    • Damaso, C.R.1    Moussatché, N.2
  • 17
    • 0026450538 scopus 로고
    • Protein synthesis in vaccinia virus-infected cells. I. Effect of hypertonic shock recovery
    • Damaso, C. R., and N. Moussatché. 1992. Protein synthesis in vaccinia virus-infected cells. I. Effect of hypertonic shock recovery. Arch. Virol. 123: 295-308.
    • (1992) Arch. Virol. , vol.123 , pp. 295-308
    • Damaso, C.R.1    Moussatché, N.2
  • 18
    • 0036385915 scopus 로고    scopus 로고
    • Azathioprine inhibits vaccinia virus replication in both BSC-40 and RAG cell lines acting on different stages of virus cycle
    • Damaso, C. R., M. F. Oliveira, S. M. Massarani, and N. Moussatché. 2002. Azathioprine inhibits vaccinia virus replication in both BSC-40 and RAG cell lines acting on different stages of virus cycle. Virology 300:79-91.
    • (2002) Virology , vol.300 , pp. 79-91
    • Damaso, C.R.1    Oliveira, M.F.2    Massarani, S.M.3    Moussatché, N.4
  • 19
    • 0000404916 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerases - An overview of the cyclophilin. FKBP and parvulin families
    • M.-J. Gething (ed.), Oxford University Press, Oxford, England
    • Dolinski, K., and J. Heitman. 1997. Peptidyl-prolyl isomerases - an overview of the cyclophilin, FKBP and parvulin families, p. 359-369. In M.-J. Gething (ed.), Guidebook to molecular chaperones and protein-folding catalysts. Oxford University Press, Oxford, England.
    • (1997) Guidebook to Molecular Chaperones and Protein-Folding Catalysts , pp. 359-369
    • Dolinski, K.1    Heitman, J.2
  • 20
    • 0018192230 scopus 로고
    • Replication of vaccinia DNA in mouse L cells. IV. Protein synthesis and viral DNA replication
    • Esteban, M., and J. A. Holowczak. 1978. Replication of vaccinia DNA in mouse L cells. IV. Protein synthesis and viral DNA replication. Virology 86:376-390.
    • (1978) Virology , vol.86 , pp. 376-390
    • Esteban, M.1    Holowczak, J.A.2
  • 21
    • 0028066730 scopus 로고
    • Rearrangement of intermediate filament network of BHK-21 cells infected with vaccinia virus
    • Ferreira, L. R., N. Moussatché, and V. Moura Neto. 1994. Rearrangement of intermediate filament network of BHK-21 cells infected with vaccinia virus. Arch. Virol. 138:273-285.
    • (1994) Arch. Virol. , vol.138 , pp. 273-285
    • Ferreira, L.R.1    Moussatché, N.2    Moura Neto, V.3
  • 22
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G., B. Wittmann-Liebold, K. Lang, T. Kiefhaber, and F. X. Schmid. 1989. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337:476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 23
    • 0031951650 scopus 로고    scopus 로고
    • p53 and RPA are sequestered in viral replication centers in the nuclei of cells infected with human cytomegalovirus
    • Fortunato, E. A., and D. H. Spector. 1998. p53 and RPA are sequestered in viral replication centers in the nuclei of cells infected with human cytomegalovirus. J. Virol. 72:2033-2039.
    • (1998) J. Virol. , vol.72 , pp. 2033-2039
    • Fortunato, E.A.1    Spector, D.H.2
  • 24
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E. K., H. E. Yuan, and J. Luban. 1994. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372:359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.2    Luban, J.3
  • 25
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgard, P. O., N. Bergenhem, B. H. Jonsson, M. Svensson, and U. Carlsson. 1992. Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 258:466-468.
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgard, P.O.1    Bergenhem, N.2    Jonsson, B.H.3    Svensson, M.4    Carlsson, U.5
  • 26
    • 0041925439 scopus 로고    scopus 로고
    • In vitro assembly properties of wild-type and cyclophilin-binding defective human immunodeficiency virus capsid proteins in the presence and absence of cyclophilin A
    • Grättinger, M., H. Hohenberg, D. Thomas, T. Wilk, B. Müller, and H. G. Kräusslich. 1999. In vitro assembly properties of wild-type and cyclophilin-binding defective human immunodeficiency virus capsid proteins in the presence and absence of cyclophilin A. Virology 257:247-260.
    • (1999) Virology , vol.257 , pp. 247-260
    • Grättinger, M.1    Hohenberg, H.2    Thomas, D.3    Wilk, T.4    Müller, B.5    Kräusslich, H.G.6
  • 27
    • 0034755323 scopus 로고    scopus 로고
    • Structure and assembly of intracellular mature vaccinia virus: Isolated-particle analysis
    • Griffiths, G., R. Wepf, T. Wendt, J. K. Locker, M. Cyrklaff, and N. Roos. 2001. Structure and assembly of intracellular mature vaccinia virus: isolated-particle analysis. J. Virol. 75:11034-11055.
    • (2001) J. Virol. , vol.75 , pp. 11034-11055
    • Griffiths, G.1    Wepf, R.2    Wendt, T.3    Locker, J.K.4    Cyrklaff, M.5    Roos, N.6
  • 30
    • 0024520356 scopus 로고
    • Detailed phenotypic characterization of five temperature-sensitive mutants in the 22-and 147-kilodalton subunits of vaccinia virus DNA-dependent RNA polymerase
    • Hooda-Dhingra, U., C. L. Thompson, and R. C. Condit. 1989. Detailed phenotypic characterization of five temperature-sensitive mutants in the 22-and 147-kilodalton subunits of vaccinia virus DNA-dependent RNA polymerase. J. Virol. 63:714-729.
    • (1989) J. Virol. , vol.63 , pp. 714-729
    • Hooda-Dhingra, U.1    Thompson, C.L.2    Condit, R.C.3
  • 31
    • 0036470544 scopus 로고    scopus 로고
    • A cyclophilin functions in pre-mRNA splicing
    • Horowitz, D. S., E. J. Lee, S. A. Mabon, and T. Misteli. 2002. A cyclophilin functions in pre-mRNA splicing. EMBO J. 21:470-480.
    • (2002) EMBO J. , vol.21 , pp. 470-480
    • Horowitz, D.S.1    Lee, E.J.2    Mabon, S.A.3    Misteli, T.4
  • 32
    • 0036149214 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
    • Hung, J. J., C. S. Chung, and W. Chang. 2002. Molecular chaperone Hsp90 is important for vaccinia virus growth in cells. J. Virol. 76:1379-1390.
    • (2002) J. Virol. , vol.76 , pp. 1379-1390
    • Hung, J.J.1    Chung, C.S.2    Chang, W.3
  • 33
    • 0026803306 scopus 로고
    • Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins
    • Jindal, S., and R. A. Young. 1992. Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins. J. Virol. 66:5357-5362.
    • (1992) J. Virol. , vol.66 , pp. 5357-5362
    • Jindal, S.1    Young, R.A.2
  • 34
    • 0001238863 scopus 로고
    • The replication and coating of vaccinia DNA
    • Joklik, W. K., and Y. Becker. 1964. The replication and coating of vaccinia DNA. J. Mol. Biol. 10:452-474.
    • (1964) J. Mol. Biol. , vol.10 , pp. 452-474
    • Joklik, W.K.1    Becker, Y.2
  • 35
    • 0027321984 scopus 로고
    • The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin
    • Kern, D., T. Drakenberg, M. Wikstrom, S. Forsen, H. Bang, and G. Fischer. 1993. The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. FEBS Lett. 323:198-202.
    • (1993) FEBS Lett. , vol.323 , pp. 198-202
    • Kern, D.1    Drakenberg, T.2    Wikstrom, M.3    Forsen, S.4    Bang, H.5    Fischer, G.6
  • 36
    • 0029085091 scopus 로고
    • Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation
    • Klappa, P., R. B. Freedman, and R. Zimmermann. 1995. Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation. Eur. J. Biochem. 232:755-764.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 755-764
    • Klappa, P.1    Freedman, R.B.2    Zimmermann, R.3
  • 37
    • 0028846647 scopus 로고
    • In situ detection of cyclosporin A: Evidence for nuclear localization of cyclosporine and cyclophilins
    • Le Hir, M., Q. Su, L. Weber, G. Woerly, A. Granelli-Piperno, and B. Ryffel. 1995. In situ detection of cyclosporin A: evidence for nuclear localization of cyclosporine and cyclophilins. Lab. Investig. 73:727-733.
    • (1995) Lab. Investig. , vol.73 , pp. 727-733
    • Le Hir, M.1    Su, Q.2    Weber, L.3    Woerly, G.4    Granelli-Piperno, A.5    Ryffel, B.6
  • 39
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban, J., K. L. Bossolt, E. K. Franke, G. V. Kalpana, and S. P. Goff. 1993. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73:1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 41
    • 0014342309 scopus 로고
    • Inhibition of HeLa cell protein synthesis by the vaccinia virion
    • Moss, B. 1968. Inhibition of HeLa cell protein synthesis by the vaccinia virion. J. Virol. 2:1028-1037.
    • (1968) J. Virol. , vol.2 , pp. 1028-1037
    • Moss, B.1
  • 42
    • 0001142643 scopus 로고    scopus 로고
    • Poxviridae: The viruses and their replication
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus. (ed.), Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Moss, B. 2001. Poxviridae: the viruses and their replication, p. 2885-2921. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus. (ed.), Fields virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 4th Ed. , pp. 2885-2921
    • Moss, B.1
  • 43
    • 0034254776 scopus 로고    scopus 로고
    • Vaccinia virus infection disrupts microtubule organization and centrosome function
    • Ploubidou, A., V. Moreau, K. Ashman, I. Reckmann, C. Gonzalez, and M. Way. 2000. Vaccinia virus infection disrupts microtubule organization and centrosome function. EMBO J. 19:3932-3944.
    • (2000) EMBO J. , vol.19 , pp. 3932-3944
    • Ploubidou, A.1    Moreau, V.2    Ashman, K.3    Reckmann, I.4    Gonzalez, C.5    Way, M.6
  • 45
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • Rassow, J., K. Mohrs, S. Koidl, I. B. Barthelmess, N. Pfanner, and M. Tropschug. 1995. Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15:2654-2662.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 46
    • 0028213927 scopus 로고
    • A cellular factor is required for transcription of vaccinia viral intermediate-stage genes
    • Rosales, R., G. Sutter, and B. Moss. 1994. A cellular factor is required for transcription of vaccinia viral intermediate-stage genes. Proc. Natl. Acad. Sci. USA 91:3794-3798.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3794-3798
    • Rosales, R.1    Sutter, G.2    Moss, B.3
  • 48
    • 0033485553 scopus 로고    scopus 로고
    • Host cyclophilin A mediates HIV-1 attachment to target cells via heparans
    • Saphire, A. C., M. D. Bobardt, and P. A. Gallay. 1999. Host cyclophilin A mediates HIV-1 attachment to target cells via heparans. EMBO J. 18:6771-6785.
    • (1999) EMBO J. , vol.18 , pp. 6771-6785
    • Saphire, A.C.1    Bobardt, M.D.2    Gallay, P.A.3
  • 49
    • 0035917897 scopus 로고    scopus 로고
    • Receptor accessory folding helper enzymes: The functional role of peptidyl prolyl cis/trans isomerases
    • Schiene-Fischer, C., and C. Yu. 2001. Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Lett. 495:1-6.
    • (2001) FEBS Lett. , vol.495 , pp. 1-6
    • Schiene-Fischer, C.1    Yu, C.2
  • 50
    • 0029132706 scopus 로고
    • Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum
    • Smith, T., L. R. Ferreira, C. Hebert, K. Norris, and J. J. Sauk. 1995. Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J. Biol. Chem. 270: 18323-18328.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18323-18328
    • Smith, T.1    Ferreira, L.R.2    Hebert, C.3    Norris, K.4    Sauk, J.J.5
  • 51
    • 0032488218 scopus 로고    scopus 로고
    • Gag protein from human immunodeficiency virus type 1 assembles in the absence of cyclophilin A
    • Streblow, D. N., M. Kitabwalla, and C. D. Pauza. 1998. Gag protein from human immunodeficiency virus type 1 assembles in the absence of cyclophilin A. Virology 252:228-234.
    • (1998) Virology , vol.252 , pp. 228-234
    • Streblow, D.N.1    Kitabwalla, M.2    Pauza, C.D.3
  • 52
    • 0034975627 scopus 로고    scopus 로고
    • Vaccinia virus A30L protein is required for association of viral membranes with dense viroplasm to form immature virions
    • Szajner, P., A. S. Weisberg, E. J. Wolffe, and B. Moss. 2001. Vaccinia virus A30L protein is required for association of viral membranes with dense viroplasm to form immature virions. J. Virol. 75:5752-5761.
    • (2001) J. Virol. , vol.75 , pp. 5752-5761
    • Szajner, P.1    Weisberg, A.S.2    Wolffe, E.J.3    Moss, B.4
  • 54
    • 0024500099 scopus 로고
    • Fine structure mapping of five temperature-sensitive mutants in the 22- and 147-kilodalton subunits of vaccinia virus DNA-dependent RNA polymerase
    • Thompson, C. L., U. Hooda-Dhingra, and R. C. Condit. 1989. Fine structure mapping of five temperature-sensitive mutants in the 22- and 147-kilodalton subunits of vaccinia virus DNA-dependent RNA polymerase. J. Virol. 63: 705-713.
    • (1989) J. Virol. , vol.63 , pp. 705-713
    • Thompson, C.L.1    Hooda-Dhingra, U.2    Condit, R.C.3
  • 55
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex: Involvement in cholesterol trafficking
    • Uittenbogaard, A., Y. Ying, and E. J. Smart. 1998. Characterization of a cytosolic heat-shock protein-caveolin chaperone complex: involvement in cholesterol trafficking. J. Biol. Chem. 273:6525-6532.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6525-6532
    • Uittenbogaard, A.1    Ying, Y.2    Smart, E.J.3
  • 56
    • 0035164017 scopus 로고    scopus 로고
    • Vaccinia virus intracellular movement is associated with microtubules and independent of actin tails
    • Ward, B. M., and B. Moss. 2001. Vaccinia virus intracellular movement is associated with microtubules and independent of actin tails. J. Virol. 75: 11651-11663.
    • (2001) J. Virol. , vol.75 , pp. 11651-11663
    • Ward, B.M.1    Moss, B.2
  • 57
    • 0033602561 scopus 로고    scopus 로고
    • Cyclophilin A incorporation is not required for human immunodeficiency virus type 1 particle maturation and does not destabilize the mature capsid
    • Wiegers, K., G. Rutter, U. Schubert, M. Grättinger, and H. G. Kräusslich. 1999. Cyclophilin A incorporation is not required for human immunodeficiency virus type 1 particle maturation and does not destabilize the mature capsid. Virology 257:261-274.
    • (1999) Virology , vol.257 , pp. 261-274
    • Wiegers, K.1    Rutter, G.2    Schubert, U.3    Grättinger, M.4    Kräusslich, H.G.5
  • 58
    • 0035798690 scopus 로고    scopus 로고
    • Vaccinia virus late transcription is activated in vitro by cellular heterogeneous nuclear ribonucleoproteins
    • Wright, C. F., B. W. Oswald, and S. Dellis. 2001. Vaccinia virus late transcription is activated in vitro by cellular heterogeneous nuclear ribonucleoproteins. J. Biol. Chem. 276:40680-40686.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40680-40686
    • Wright, C.F.1    Oswald, B.W.2    Dellis, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.