메뉴 건너뛰기




Volumn 9, Issue 9, 2009, Pages 2399-2407

Proteomics analysis of BHK-21 cells infected with a fixed strain of rabies virus

Author keywords

2 D PAGE; Proteomics; Rabies

Indexed keywords

STATHMIN; SUPEROXIDE DISMUTASE; VIMENTIN;

EID: 66249094561     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200701007     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 0003085873 scopus 로고    scopus 로고
    • Fields, B. N, Knipe, D. M, Howley, P. M, Eds, Raven Press, Philadelphia
    • Dietzschold, B., Rupprecht, C. E., Fu, Z. F., Koprowski, H., In: Fields, B. N., Knipe, D. M., Howley, P. M. (Eds.), Fields Virology, Raven Press, Philadelphia 1996, pp. 1137-1159.
    • (1996) Fields Virology , pp. 1137-1159
    • Dietzschold, B.1    Rupprecht, C.E.2    Fu, Z.F.3    Koprowski, H.4
  • 2
    • 0000249124 scopus 로고    scopus 로고
    • Human rabies: A disease of complex neuropathogenetic mechanisms and diagnostic challenges
    • Hemachudha, T., Laothamatas, J., Rupprecht, C. E., Human rabies: A disease of complex neuropathogenetic mechanisms and diagnostic challenges. Lancet Neurol. 2002, 1,101-109.
    • (2002) Lancet Neurol , vol.1 , pp. 101-109
    • Hemachudha, T.1    Laothamatas, J.2    Rupprecht, C.E.3
  • 5
    • 34247128164 scopus 로고    scopus 로고
    • Rabies-update on a global disease
    • Wyatt, J., Rabies-update on a global disease. Pediatr. Infect. Dis. J. 2007, 26, 351-352.
    • (2007) Pediatr. Infect. Dis. J , vol.26 , pp. 351-352
    • Wyatt, J.1
  • 6
    • 16244410813 scopus 로고    scopus 로고
    • Pathogenesis of rabies-Editorial
    • Jackson, A. C., Fu, Z. F., Pathogenesis of rabies-Editorial. J. Neurovirol. 2005, 11, 74-75.
    • (2005) J. Neurovirol , vol.11 , pp. 74-75
    • Jackson, A.C.1    Fu, Z.F.2
  • 8
    • 0036691009 scopus 로고    scopus 로고
    • Rabies virus is not cytolytic for rat spinal motoneurons in vitro
    • Guigoni, C., Coulon, P., Rabies virus is not cytolytic for rat spinal motoneurons in vitro. J. Neurovirol. 2002, 8, 306-317.
    • (2002) J. Neurovirol , vol.8 , pp. 306-317
    • Guigoni, C.1    Coulon, P.2
  • 9
    • 34547122855 scopus 로고    scopus 로고
    • Lethal silver-haired bat rabies virus infection can be prevented by opening the blood-brain barrier
    • Roy, A., Hooper, D. C., Lethal silver-haired bat rabies virus infection can be prevented by opening the blood-brain barrier. J. Virol. 2007, 81, 7993-7998.
    • (2007) J. Virol , vol.81 , pp. 7993-7998
    • Roy, A.1    Hooper, D.C.2
  • 10
    • 25144513480 scopus 로고    scopus 로고
    • Attenuated Rabies virus activates, while pathogenic rabies virus evades, the host innate immune responses in the Central Nervous System
    • Wang, Z. W., Sarmento, L., Wang, Y., Li, X. etal., Attenuated Rabies virus activates, while pathogenic rabies virus evades, the host innate immune responses in the Central Nervous System. J. Virol. 2005, 79, 12554-12565.
    • (2005) J. Virol , vol.79 , pp. 12554-12565
    • Wang, Z.W.1    Sarmento, L.2    Wang, Y.3    Li, X.4
  • 11
    • 16244380220 scopus 로고    scopus 로고
    • The role of immune responses in the pathogenesis of rabies
    • Hooper, D. C., The role of immune responses in the pathogenesis of rabies. J. Neurovirol. 2005, 11, 88-92.
    • (2005) J. Neurovirol , vol.11 , pp. 88-92
    • Hooper, D.C.1
  • 12
    • 0242690437 scopus 로고    scopus 로고
    • Apoptosis and rabies virus neuroinva- sion
    • Baloul, L., Lafon, M., Apoptosis and rabies virus neuroinva- sion. Biochimie 2003, 85, 777-788.
    • (2003) Biochimie , vol.85 , pp. 777-788
    • Baloul, L.1    Lafon, M.2
  • 13
    • 14144249711 scopus 로고    scopus 로고
    • Modulation of the immune response in the nervous system by rabies virus
    • Lafon, M., Modulation of the immune response in the nervous system by rabies virus. Curr. Top. Microbiol. Immunol. 2005, 289, 239-258.
    • (2005) Curr. Top. Microbiol. Immunol , vol.289 , pp. 239-258
    • Lafon, M.1
  • 14
    • 34247145818 scopus 로고    scopus 로고
    • Rabies virus matrix protein interplay with eIF3, new insights into rabies virus pathogenesis
    • Komarova, A. V., Real, E., Borman, A. M., Brocard, M. etal., Rabies virus matrix protein interplay with eIF3, new insights into rabies virus pathogenesis. Nucleic Acids Res. 2007, 35, 1522-1532.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1522-1532
    • Komarova, A.V.1    Real, E.2    Borman, A.M.3    Brocard, M.4
  • 15
    • 34249035067 scopus 로고    scopus 로고
    • Proteomic profiling reveals that rabies virus infection results in differential expression of host proteins involved in ion homeostasis and synaptic physiology in the central nervous system
    • Dhingra, V., Li, X., Liu, Y., Fu, Z. F., Proteomic profiling reveals that rabies virus infection results in differential expression of host proteins involved in ion homeostasis and synaptic physiology in the central nervous system. J. Neurovirol. 2007, 13, 107-117.
    • (2007) J. Neurovirol , vol.13 , pp. 107-117
    • Dhingra, V.1    Li, X.2    Liu, Y.3    Fu, Z.F.4
  • 16
    • 0000308692 scopus 로고
    • Fluorescent antibody staining of street and fixed rabies virus antigens
    • Goldwasser, R. A., Kissling, R. E., Fluorescent antibody staining of street and fixed rabies virus antigens. Proc. Soc. Exp. Biol. Med. 1958, 98, 219-223.
    • (1958) Proc. Soc. Exp. Biol. Med , vol.98 , pp. 219-223
    • Goldwasser, R.A.1    Kissling, R.E.2
  • 17
    • 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., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248254.
    • (1976) Anal. Biochem , vol.72 , pp. 248254
    • Bradford, M.M.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0029927505 scopus 로고    scopus 로고
    • Mass spec- trometric sequencing of proteins silver-stained polyacryl- amide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spec- trometric sequencing of proteins silver-stained polyacryl- amide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 20
    • 3042665732 scopus 로고    scopus 로고
    • Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis
    • Candiano, G., Bruschi, M., Musante, L., Santucci, L. etal., Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 2004, 25, 1327-1333.
    • (2004) Electrophoresis , vol.25 , pp. 1327-1333
    • Candiano, G.1    Bruschi, M.2    Musante, L.3    Santucci, L.4
  • 21
    • 0018968617 scopus 로고
    • Tissue culture technique for routine isolation of street strain rabies virus
    • Rudd, R. J., Trimarchi, C. V., Abelseth, M. K., Tissue culture technique for routine isolation of street strain rabies virus. J. Clin. Microbiol. 1980, 12, 590-593.
    • (1980) J. Clin. Microbiol , vol.12 , pp. 590-593
    • Rudd, R.J.1    Trimarchi, C.V.2    Abelseth, M.K.3
  • 22
    • 33646861788 scopus 로고    scopus 로고
    • Rabies virus chaperone: Identification of the phosphoprotein pep- tide that keeps nucleoprotein soluble and free from nonspecific RNA
    • Mavrakis, M., Mehouas, S., Real, E., Iseni, F. et al., Rabies virus chaperone: Identification of the phosphoprotein pep- tide that keeps nucleoprotein soluble and free from nonspecific RNA. Virology 2006, 349, 422-429.
    • (2006) Virology , vol.349 , pp. 422-429
    • Mavrakis, M.1    Mehouas, S.2    Real, E.3    Iseni, F.4
  • 23
    • 19444368893 scopus 로고    scopus 로고
    • Characterization of P gene- deficient rabies virus: Propagation, pathogenicity and anti- genicity
    • Morimoto, K., Shoji, Y., Inoue, S., Characterization of P gene- deficient rabies virus: Propagation, pathogenicity and anti- genicity. Virus Res. 2005, 111, 61-67.
    • (2005) Virus Res , vol.111 , pp. 61-67
    • Morimoto, K.1    Shoji, Y.2    Inoue, S.3
  • 24
    • 19944370132 scopus 로고    scopus 로고
    • Identification of the rabies virus alpha/beta interferon antagonist: Phosphopro- tein P interferes with phosphorylation of interferon regulatory factor 3
    • Brzozka, K., Finke, S., Conzelmann, K. K., Identification of the rabies virus alpha/beta interferon antagonist: Phosphopro- tein P interferes with phosphorylation of interferon regulatory factor 3. J. Virol. 2005, 79, 7673-7681.
    • (2005) J. Virol , vol.79 , pp. 7673-7681
    • Brzozka, K.1    Finke, S.2    Conzelmann, K.K.3
  • 25
    • 33744456994 scopus 로고    scopus 로고
    • The viral protein P interferes with IRF-3, Stat1, and PML nuclear bodies
    • Rabies viral mechanisms to escape the IFN system
    • Chelbi-Alix, M. K., Vidy, A., El Bougrini, J., Blondel, D., Rabies viral mechanisms to escape the IFN system: The viral protein P interferes with IRF-3, Stat1, and PML nuclear bodies. J. Interferon Cytokine Res. 2006, 26, 271-280.
    • (2006) J. Interferon Cytokine Res , vol.26 , pp. 271-280
    • Chelbi-Alix, M.K.1    Vidy, A.2    El Bougrini, J.3    Blondel, D.4
  • 26
    • 0033986999 scopus 로고    scopus 로고
    • The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C
    • Gupta, A. K., Blondel, D., Choudhary, S., Banerjee, A. K., The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C. J. Virol. 2000, 74, 91-98.
    • (2000) J. Virol , vol.74 , pp. 91-98
    • Gupta, A.K.1    Blondel, D.2    Choudhary, S.3    Banerjee, A.K.4
  • 27
    • 0031765540 scopus 로고    scopus 로고
    • 2. Possible relationships between the two forms of the noncatalytic subunit (P protein)
    • Studies on the rabies virus RNA polymerase
    • Takamatsu, F., Asakawa, N., Morimoto, K., Takeuchi, K. etal., Studies on the rabies virus RNA polymerase: 2. Possible relationships between the two forms of the noncatalytic subunit (P protein). Microbiol. Immunol. 1998, 42, 761-771.
    • (1998) Microbiol. Immunol , vol.42 , pp. 761-771
    • Takamatsu, F.1    Asakawa, N.2    Morimoto, K.3    Takeuchi, K.4
  • 28
    • 0036021094 scopus 로고    scopus 로고
    • 3. Two-dimensional electrophoretic analysis of the multiplicity of noncatalytic subunit (P protein)
    • Studies on the rabies virus RNA polymerase
    • Eriguchi, Y., Toriumi, H., Kawai, A., Studies on the rabies virus RNA polymerase: 3. Two-dimensional electrophoretic analysis of the multiplicity of noncatalytic subunit (P protein). Microbiol. Immunol. 2002, 46, 463-474.
    • (2002) Microbiol. Immunol , vol.46 , pp. 463-474
    • Eriguchi, Y.1    Toriumi, H.2    Kawai, A.3
  • 29
    • 34247160941 scopus 로고    scopus 로고
    • The nucleocytoplasmic rabies virus P protein counteracts interferon signaling by inhibiting both nuclear accumulation and DNA binding of STAT1
    • Vidy, A., El Bougrini, J., Chelbi-Alix, M. K., Blondel, D., The nucleocytoplasmic rabies virus P protein counteracts interferon signaling by inhibiting both nuclear accumulation and DNA binding of STAT1. J. Virol. 2007, 81, 4255-4263.
    • (2007) J. Virol , vol.81 , pp. 4255-4263
    • Vidy, A.1    El Bougrini, J.2    Chelbi-Alix, M.K.3    Blondel, D.4
  • 30
    • 10044241595 scopus 로고    scopus 로고
    • Further studies on the hyperphosphorylated form (p40) of the rabies virus nominal phosphoprotein (P)
    • Toriumi, H., Eriguchi, Y., Takamatsu, F., Kawai, A., Further studies on the hyperphosphorylated form (p40) of the rabies virus nominal phosphoprotein (P). Microbiol. Immunol. 2004, 48, 865-874.
    • (2004) Microbiol. Immunol , vol.48 , pp. 865-874
    • Toriumi, H.1    Eriguchi, Y.2    Takamatsu, F.3    Kawai, A.4
  • 31
    • 0018860240 scopus 로고
    • Rabies serogroup viruses in neuroblastoma cells: Propagation, "autointerference," and apparently random back-mutation of attenuated viruses to the virulent state
    • Clark, H. F., Rabies serogroup viruses in neuroblastoma cells: Propagation, "autointerference," and apparently random back-mutation of attenuated viruses to the virulent state. Infect. Immun. 1980, 27, 1012-1022.
    • (1980) Infect. Immun , vol.27 , pp. 1012-1022
    • Clark, H.F.1
  • 32
    • 0021133349 scopus 로고
    • Transient change of organization of vimentin filaments during mitosis as demonstrated by a monoclonal antibody
    • Franke, W. W., Grund, C., Kuhn, C., Lehto, V. P., Virtanen, I., Transient change of organization of vimentin filaments during mitosis as demonstrated by a monoclonal antibody. Exp. CellRes. 1984, 154, 567-580.
    • (1984) Exp. CellRes , vol.154 , pp. 567-580
    • Franke, W.W.1    Grund, C.2    Kuhn, C.3    Lehto, V.P.4    Virtanen, I.5
  • 33
    • 0038709375 scopus 로고    scopus 로고
    • Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis
    • Chou, Y. H., Khuon, S., Herrmann, H., Goldman, R. D., Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis. Mol. Biol. Cell 2003, 14, 1468-1478.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1468-1478
    • Chou, Y.H.1    Khuon, S.2    Herrmann, H.3    Goldman, R.D.4
  • 34
    • 24644480042 scopus 로고    scopus 로고
    • Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II
    • Stefanovic, S., Windsor, M., Nagata, K. I., Inagaki, M., Wileman, T., Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II. J. Virol. 2005, 79, 11766-11775.
    • (2005) J. Virol , vol.79 , pp. 11766-11775
    • Stefanovic, S.1    Windsor, M.2    Nagata, K.I.3    Inagaki, M.4    Wileman, T.5
  • 35
    • 0028066730 scopus 로고
    • Rearrangement of intermediate filament network of BHK-21 cells infected with vaccinia virus
    • Ferreira, L. R., Moussatche, N., Moura Neto, V., Rearrangement of intermediate filament network of BHK-21 cells infected with vaccinia virus. Arch. Virol. 1994, 138, 273-285.
    • (1994) Arch. Virol , vol.138 , pp. 273-285
    • Ferreira, L.R.1    Moussatche, N.2    Moura Neto, V.3
  • 36
    • 0023228781 scopus 로고
    • Processing of vimentin occurs during the early stages of adenovirus infection
    • Belin, M. T., Boulanger, P., Processing of vimentin occurs during the early stages of adenovirus infection. J. Virol. 1987, 61, 2559-2566.
    • (1987) J. Virol , vol.61 , pp. 2559-2566
    • Belin, M.T.1    Boulanger, P.2
  • 37
    • 0025344531 scopus 로고
    • Disruption of the actin cytoskeleton in yeast capping protein mutants
    • Amatruda, J. F., Cannon, J. F., Tatchell, K., Hug, C., Cooper, J. A., Disruption of the actin cytoskeleton in yeast capping protein mutants. Nature 1990, 344, 352-354.
    • (1990) Nature , vol.344 , pp. 352-354
    • Amatruda, J.F.1    Cannon, J.F.2    Tatchell, K.3    Hug, C.4    Cooper, J.A.5
  • 38
    • 0024421755 scopus 로고
    • Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin
    • Caldwell, J. E., Heiss, S. G., Mermall, V., Cooper, J. A., Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin. Biochemistry 1989, 28, 8506-8514.
    • (1989) Biochemistry , vol.28 , pp. 8506-8514
    • Caldwell, J.E.1    Heiss, S.G.2    Mermall, V.3    Cooper, J.A.4
  • 39
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates
    • Schafer, D. A., Korshunova, Y. O., Schroer, T. A., Cooper, J. A., Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates. J. Cell Biol. 1994, 127, 453-465.
    • (1994) J. Cell Biol , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 40
    • 0029065328 scopus 로고
    • Capping protein levels influence actin assembly and cell motility in dictyostelium
    • Hug, C., Jay, P. Y., Reddy, I., McNally, J. G. et al., Capping protein levels influence actin assembly and cell motility in dictyostelium. Cell 1995, 81, 591-600.
    • (1995) Cell , vol.81 , pp. 591-600
    • Hug, C.1    Jay, P.Y.2    Reddy, I.3    McNally, J.G.4
  • 41
    • 0001298780 scopus 로고
    • Oxygen-dependent muta- genesis in Escherichia coli lacking superoxide dismutase
    • Farr, S. B., D'Ari, R., Touati, D., Oxygen-dependent muta- genesis in Escherichia coli lacking superoxide dismutase. Proc. Natl. Acad. Sci. USA 1986, 83, 8268-8272.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8268-8272
    • Farr, S.B.1    D'Ari, R.2    Touati, D.3
  • 42
    • 0026636441 scopus 로고
    • Free radicals, antioxidants, and human disease: Where are we now?
    • Halliwell, B., Gutteridge, J. M., Cross, C. E., Free radicals, antioxidants, and human disease: Where are we now? J. Lab. Clin. Med. 1992, 119, 598-620.
    • (1992) J. Lab. Clin. Med , vol.119 , pp. 598-620
    • Halliwell, B.1    Gutteridge, J.M.2    Cross, C.E.3
  • 43
    • 0021077837 scopus 로고
    • Distinct patterns of cyto- plasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells
    • Sobel, A., Tashjian, A. H., Jr., Distinct patterns of cyto- plasmic protein phosphorylation related to regulation of synthesis and release of prolactin by GH cells. J. Biol. Chem. 1983, 258, 10312-10324.
    • (1983) J. Biol. Chem , vol.258 , pp. 10312-10324
    • Sobel, A.1    Tashjian Jr., A.H.2
  • 44
    • 7244239105 scopus 로고    scopus 로고
    • Dysregulation of stathmin, a microtubule-destabilizing protein, and up-regulation of Hsp25, Hsp27, and the anti- oxidant peroxiredoxin 6 in a mouse model of familial amyotrophic lateral sclerosis
    • Strey, C. W., Spellman, D., Stieber, A., Gonatas, J. O. et al., Dysregulation of stathmin, a microtubule-destabilizing protein, and up-regulation of Hsp25, Hsp27, and the anti- oxidant peroxiredoxin 6 in a mouse model of familial amyotrophic lateral sclerosis. Am. J. Pathol. 2004, 165, 1701-1718.
    • (2004) Am. J. Pathol , vol.165 , pp. 1701-1718
    • Strey, C.W.1    Spellman, D.2    Stieber, A.3    Gonatas, J.O.4
  • 45
    • 0034237451 scopus 로고    scopus 로고
    • Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: Evaluation by the two hybrid system
    • Tchorzewski, M., Boldyreff, B., Issinger, O., Grankowski, N., Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: Evaluation by the two hybrid system. Int. J. Biochem. Cell Biol. 2000, 32, 737-746.
    • (2000) Int. J. Biochem. Cell Biol , vol.32 , pp. 737-746
    • Tchorzewski, M.1    Boldyreff, B.2    Issinger, O.3    Grankowski, N.4
  • 46
    • 0035827659 scopus 로고    scopus 로고
    • Pivotal role of the P1 N-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity
    • Gonzalo, P., Lavergne, J. P., Reboud, J. P., Pivotal role of the P1 N-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity. J. Biol. Chem. 2001, 276, 19762-19769.
    • (2001) J. Biol. Chem , vol.276 , pp. 19762-19769
    • Gonzalo, P.1    Lavergne, J.P.2    Reboud, J.P.3
  • 47
    • 0029402485 scopus 로고
    • Proteins P1, P2, and P0, components of the eukaryotic ribo- some stalk. Newstructural and functional aspects
    • Remacha, M., Jimenez-Diaz, A., Santos, C., Briones, E. etal., Proteins P1, P2, and P0, components of the eukaryotic ribo- some stalk. Newstructural and functional aspects. Biochem. Cell Biol. 1995, 73, 959-968.
    • (1995) Biochem. Cell Biol , vol.73 , pp. 959-968
    • Remacha, M.1    Jimenez-Diaz, A.2    Santos, C.3    Briones, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.