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Volumn 390, Issue 2, 2009, Pages 356-367

Analyses of the spleen proteome of chickens infected with Marek's disease virus

Author keywords

1D LC ESI MS MS; 2D gel electrophoresis; Chicken proteome; Host response; Marek's disease virus

Indexed keywords

PROTEOME; UBIQUITIN;

EID: 67649976592     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.05.020     Document Type: Article
Times cited : (31)

References (69)
  • 1
    • 33644895114 scopus 로고    scopus 로고
    • Development of a real-time PCR assay using SYBR green chemistry for monitoring Marek's disease virus genome load in feather tips
    • Abdul-Careem M.F., Hunter B.D., Nagy E., Read L.R., Sanei B., Spencer J.L., et al. Development of a real-time PCR assay using SYBR green chemistry for monitoring Marek's disease virus genome load in feather tips. J. Virol. Methods 133 (2006) 34-40
    • (2006) J. Virol. Methods , vol.133 , pp. 34-40
    • Abdul-Careem, M.F.1    Hunter, B.D.2    Nagy, E.3    Read, L.R.4    Sanei, B.5    Spencer, J.L.6
  • 2
    • 33845198479 scopus 로고    scopus 로고
    • Cytokine gene expression patterns associated with immunization against Marek's disease in chickens
    • Abdul-Careem M.F., Hunter B.D., Parvizi P., Haghighi H.R., Thanthrige-Don N., and Sharif S. Cytokine gene expression patterns associated with immunization against Marek's disease in chickens. Vaccine 25 (2007) 424-432
    • (2007) Vaccine , vol.25 , pp. 424-432
    • Abdul-Careem, M.F.1    Hunter, B.D.2    Parvizi, P.3    Haghighi, H.R.4    Thanthrige-Don, N.5    Sharif, S.6
  • 3
    • 61649115889 scopus 로고    scopus 로고
    • Proteomic analysis reveals the actin cytoskeleton as cellular target for the human papillomavirus type 8
    • Akgül B., Zigrino P., Frith D., Hanrahan S., and Storey A. Proteomic analysis reveals the actin cytoskeleton as cellular target for the human papillomavirus type 8. Virology 386 (2009) 1-5
    • (2009) Virology , vol.386 , pp. 1-5
    • Akgül, B.1    Zigrino, P.2    Frith, D.3    Hanrahan, S.4    Storey, A.5
  • 4
    • 2942741144 scopus 로고    scopus 로고
    • Study of host-pathogen interactions to identify sustainable vaccine strategies to Marek's disease
    • Baaten B.J.G., Butter C., and Davison T.F. Study of host-pathogen interactions to identify sustainable vaccine strategies to Marek's disease. Vet. Immunol. Immunopathol. 100 (2004) 165-177
    • (2004) Vet. Immunol. Immunopathol. , vol.100 , pp. 165-177
    • Baaten, B.J.G.1    Butter, C.2    Davison, T.F.3
  • 5
    • 0034243928 scopus 로고    scopus 로고
    • A review of the development of chicken lines to resolve genes determining resistance to diseases
    • Bacon L.D., Hunt H.D., and Cheng H.H. A review of the development of chicken lines to resolve genes determining resistance to diseases. Poult. Sci. 79 (2000) 1082-1093
    • (2000) Poult. Sci. , vol.79 , pp. 1082-1093
    • Bacon, L.D.1    Hunt, H.D.2    Cheng, H.H.3
  • 6
    • 0033554655 scopus 로고    scopus 로고
    • Molecular cloning of chick UCH-6 which shares high similarity with human UCH-L3: its unusual substrate specificity and tissue distribution
    • Baek S.H., Yoo Y.J., Tanaka K., and Chung C.H. Molecular cloning of chick UCH-6 which shares high similarity with human UCH-L3: its unusual substrate specificity and tissue distribution. Biochem. Biophys. Res. Commun. 264 (1999) 235-240
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 235-240
    • Baek, S.H.1    Yoo, Y.J.2    Tanaka, K.3    Chung, C.H.4
  • 7
    • 33645449133 scopus 로고    scopus 로고
    • Marek's disease: an evolving problem
    • Davison F., and Nair V. (Eds), Biology and life cycle. Elsevier Academic Press, USA
    • Baigent S.J., and Davison F. Marek's disease: an evolving problem. In: Davison F., and Nair V. (Eds). Marek's Disease Virus (2004), Biology and life cycle. Elsevier Academic Press, USA 62-77
    • (2004) Marek's Disease Virus , pp. 62-77
    • Baigent, S.J.1    Davison, F.2
  • 8
    • 33947171543 scopus 로고    scopus 로고
    • Identification of stathmin 1 expression induced by Epstein-Barr virus in human B lymphocytes
    • Baik S.Y., Yun H.S., Lee H.J., Lee M.H., Jung S.E., Kim J.W., et al. Identification of stathmin 1 expression induced by Epstein-Barr virus in human B lymphocytes. Cell Prolif. 40 (2007) 268-281
    • (2007) Cell Prolif. , vol.40 , pp. 268-281
    • Baik, S.Y.1    Yun, H.S.2    Lee, H.J.3    Lee, M.H.4    Jung, S.E.5    Kim, J.W.6
  • 9
    • 4143117776 scopus 로고    scopus 로고
    • The transglutaminase family: an overview: minireview article
    • Beninati S., and Piacentini M. The transglutaminase family: an overview: minireview article. Amino Acids 26 (2004) 367-372
    • (2004) Amino Acids , vol.26 , pp. 367-372
    • Beninati, S.1    Piacentini, M.2
  • 10
    • 0001677717 scopus 로고
    • Controlling the false discovery rate - a practical and powerful approach to multiple testing
    • Benjamini Y., and Hochberg Y. Controlling the false discovery rate - a practical and powerful approach to multiple testing. J R Stat. Soc. series B Stat. Methodol. 57 (1995) 289-300
    • (1995) J R Stat. Soc. series B Stat. Methodol. , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 11
    • 40149102342 scopus 로고    scopus 로고
    • The 19S proteasorne ATPase Sug1 plays a critical role in regulating MHC class II transcription
    • Bhat K.P., Turner J.D., Myers S.E., Cape A.D., Ting J.P.Y., and Greer S.F. The 19S proteasorne ATPase Sug1 plays a critical role in regulating MHC class II transcription. Mol. Immunol. 45 (2008) 2214-2224
    • (2008) Mol. Immunol. , vol.45 , pp. 2214-2224
    • Bhat, K.P.1    Turner, J.D.2    Myers, S.E.3    Cape, A.D.4    Ting, J.P.Y.5    Greer, S.F.6
  • 12
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N., Lorenzo H.K., Carmona S., Laforge M., Harper F., Dumont C., et al. Cathepsin D triggers bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 278 (2003) 31401-31411
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6
  • 13
    • 0030807896 scopus 로고    scopus 로고
    • The herpes simplex virus virulence factor ICP34.5 and the cellular protein MyD116 complex with proliferating cell nuclear antigen through the 63-amino-acid domain conserved in ICP34.5, MyD116, and GADD34
    • Brown S.M., MacLean A.R., McKie E.A., and Harland J. The herpes simplex virus virulence factor ICP34.5 and the cellular protein MyD116 complex with proliferating cell nuclear antigen through the 63-amino-acid domain conserved in ICP34.5, MyD116, and GADD34. J. Virol. 71 (1997) 9442-9449
    • (1997) J. Virol. , vol.71 , pp. 9442-9449
    • Brown, S.M.1    MacLean, A.R.2    McKie, E.A.3    Harland, J.4
  • 14
    • 0030962466 scopus 로고    scopus 로고
    • Quantification of Marek's disease virus in chicken lymphocytes using the polymerase chain reaction with fluorescence detection
    • Bumstead N., Sillibourne J., Rennie M., Ross N., and Davison F. Quantification of Marek's disease virus in chicken lymphocytes using the polymerase chain reaction with fluorescence detection. J.Virol.Methods 65 (1997) 75-81
    • (1997) J.Virol.Methods , vol.65 , pp. 75-81
    • Bumstead, N.1    Sillibourne, J.2    Rennie, M.3    Ross, N.4    Davison, F.5
  • 15
    • 4043083306 scopus 로고    scopus 로고
    • Proteomics in the chicken: tools for understanding immune responses to avian diseases
    • Burgess S.C. Proteomics in the chicken: tools for understanding immune responses to avian diseases. Poult. Sci. 83 (2004) 552-573
    • (2004) Poult. Sci. , vol.83 , pp. 552-573
    • Burgess, S.C.1
  • 16
    • 34248154149 scopus 로고    scopus 로고
    • Modeling the proteome of a Marek's disease transformed cell line: a natural animal model for CD30 overexpressing lymphomas
    • Buza J.J., and Burgess S.C. Modeling the proteome of a Marek's disease transformed cell line: a natural animal model for CD30 overexpressing lymphomas. Proteomics 7 (2007) 1316-1326
    • (2007) Proteomics , vol.7 , pp. 1316-1326
    • Buza, J.J.1    Burgess, S.C.2
  • 17
    • 49849092309 scopus 로고    scopus 로고
    • + lymphocytes activated with staphylococcal enterotoxin B, and those malignantly transformed by Marek's disease virus
    • + lymphocytes activated with staphylococcal enterotoxin B, and those malignantly transformed by Marek's disease virus. J. Proteome Res. 7 (2008) 2380-2387
    • (2008) J. Proteome Res. , vol.7 , pp. 2380-2387
    • Buza, J.J.1    Burgess, S.C.2
  • 18
    • 42449130222 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina during human cytomegalovirus infection: role of the viral proteins pUL50 and pUL53
    • Camozzi D., Pignatelli S., Valvo C., Lattanzi G., Capanni C., Monte P.D., et al. Remodelling of the nuclear lamina during human cytomegalovirus infection: role of the viral proteins pUL50 and pUL53. J. Gen. Virol. 89 (2008) 731-740
    • (2008) J. Gen. Virol. , vol.89 , pp. 731-740
    • Camozzi, D.1    Pignatelli, S.2    Valvo, C.3    Lattanzi, G.4    Capanni, C.5    Monte, P.D.6
  • 19
    • 41149098534 scopus 로고    scopus 로고
    • Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation
    • Conus S., Perozzo R., Reinheckel T., Peters C., Scapozza L., Yousefi S., et al. Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation. J. Exp. Med. 205 (2008) 685-698
    • (2008) J. Exp. Med. , vol.205 , pp. 685-698
    • Conus, S.1    Perozzo, R.2    Reinheckel, T.3    Peters, C.4    Scapozza, L.5    Yousefi, S.6
  • 20
    • 53049100000 scopus 로고    scopus 로고
    • Application of saturation dye 2D-DIGE proteomics to characterize proteins modulated by oxidized low density lipoprotein treatment of human macrophages
    • Dupont A., Chwastyniak M., Beseme O., Guihot A.L., Drobecq H., Amouyel P., et al. Application of saturation dye 2D-DIGE proteomics to characterize proteins modulated by oxidized low density lipoprotein treatment of human macrophages. J. Proteome Res. 7 (2008) 3572-3582
    • (2008) J. Proteome Res. , vol.7 , pp. 3572-3582
    • Dupont, A.1    Chwastyniak, M.2    Beseme, O.3    Guihot, A.L.4    Drobecq, H.5    Amouyel, P.6
  • 21
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J.E., and Gygi S.P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4 (2007) 207-214
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 23
    • 20444363472 scopus 로고    scopus 로고
    • Transglutaminase 2 in the balance of cell death and survival
    • Fesus L., and Szondy Z. Transglutaminase 2 in the balance of cell death and survival. FEBS Lett. 579 (2005) 3297-3302
    • (2005) FEBS Lett. , vol.579 , pp. 3297-3302
    • Fesus, L.1    Szondy, Z.2
  • 26
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • Griffin T.A., Nandi D., Cruz M., Fehling H.J., Kaer L.V., Monaco J.J., et al. Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits. J. Exp. Med. 187 (1998) 97-104
    • (1998) J. Exp. Med. , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3    Fehling, H.J.4    Kaer, L.V.5    Monaco, J.J.6
  • 28
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi S.P., Rochon Y., Franza B.R., and Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol. Cell. Biol. 19 (1999) 1720-1730
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 29
    • 0042530129 scopus 로고    scopus 로고
    • The herpes simplex virus (HSV) protein ICP34.5 is a virion component that forms a DNA-binding complex with proliferating cell nuclear antigen and HSV replication proteins
    • Harland J., Dunn P., Cameron E., Conner J., and Brown S.M. The herpes simplex virus (HSV) protein ICP34.5 is a virion component that forms a DNA-binding complex with proliferating cell nuclear antigen and HSV replication proteins. J. Neurovirol. 9 (2003) 477-488
    • (2003) J. Neurovirol. , vol.9 , pp. 477-488
    • Harland, J.1    Dunn, P.2    Cameron, E.3    Conner, J.4    Brown, S.M.5
  • 30
    • 0038401122 scopus 로고    scopus 로고
    • Viral inhibition of MHC class II antigen presentation
    • Hegde N.R., Chevalier M.S., and Johnson D.C. Viral inhibition of MHC class II antigen presentation. Trends Immunol. 24 (2003) 278-285
    • (2003) Trends Immunol. , vol.24 , pp. 278-285
    • Hegde, N.R.1    Chevalier, M.S.2    Johnson, D.C.3
  • 31
    • 0029911690 scopus 로고    scopus 로고
    • Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma
    • Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B., Fujiwara T., et al. Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma. J. Exp. Med. 183 (1996) 1807-1816
    • (1996) J. Exp. Med. , vol.183 , pp. 1807-1816
    • Hisamatsu, H.1    Shimbara, N.2    Saito, Y.3    Kristensen, P.4    Hendil, K.B.5    Fujiwara, T.6
  • 32
    • 34547697884 scopus 로고    scopus 로고
    • Tissue transglutaminase and the stress response
    • Ientile R., Caccamo D., and Griffin M. Tissue transglutaminase and the stress response. Amino Acids 33 (2007) 385-394
    • (2007) Amino Acids , vol.33 , pp. 385-394
    • Ientile, R.1    Caccamo, D.2    Griffin, M.3
  • 33
    • 31844455411 scopus 로고    scopus 로고
    • Relationship between Marek's disease virus load in peripheral blood lymphocytes at various stages of infection and clinical Marek's disease in broiler chickens
    • Islam A.F.M.F., Walkden-Brown S.W., Islam A., Underwood G.J., and Groves P.J. Relationship between Marek's disease virus load in peripheral blood lymphocytes at various stages of infection and clinical Marek's disease in broiler chickens. Avian Pathol. 35 (2006) 42-48
    • (2006) Avian Pathol. , vol.35 , pp. 42-48
    • Islam, A.F.M.F.1    Walkden-Brown, S.W.2    Islam, A.3    Underwood, G.J.4    Groves, P.J.5
  • 34
    • 0016218277 scopus 로고
    • Changes in the activity of several serum enzymes in chicks with Marek's disease
    • Ivanov V., Bozukova T., and Nikolova M. Changes in the activity of several serum enzymes in chicks with Marek's disease. Vet. Med. Nauki 11 (1974) 18-24
    • (1974) Vet. Med. Nauki , vol.11 , pp. 18-24
    • Ivanov, V.1    Bozukova, T.2    Nikolova, M.3
  • 35
    • 24944437299 scopus 로고    scopus 로고
    • Quantitative analysis of severe acute respiratory syndrome (SARS)-associated coronavirus-infected cells using proteomic approaches - implications for cellular responses to virus infection
    • Jiang X.S., Tang L.Y., Dai J., Zhou H., Li S.J., Xia Q.C., et al. Quantitative analysis of severe acute respiratory syndrome (SARS)-associated coronavirus-infected cells using proteomic approaches - implications for cellular responses to virus infection. Mol. Cell. Proteomics 4 (2005) 902-913
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 902-913
    • Jiang, X.S.1    Tang, L.Y.2    Dai, J.3    Zhou, H.4    Li, S.J.5    Xia, Q.C.6
  • 36
    • 33646367913 scopus 로고    scopus 로고
    • Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B
    • Laurent-Matha V., Derocq D., Prebois C., Katunuma N., and Liaudet-Coopman E. Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B. J. Biochem. 139 (2006) 363-371
    • (2006) J. Biochem. , vol.139 , pp. 363-371
    • Laurent-Matha, V.1    Derocq, D.2    Prebois, C.3    Katunuma, N.4    Liaudet-Coopman, E.5
  • 37
    • 33644863314 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection
    • Leong W.F., and Chow V.T.K. Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell. Microbiol. 8 (2006) 565-580
    • (2006) Cell. Microbiol. , vol.8 , pp. 565-580
    • Leong, W.F.1    Chow, V.T.K.2
  • 38
    • 0344837287 scopus 로고    scopus 로고
    • Major histocompatibility complex class I is downregulated in Marek's disease virus infected chicken embryo fibroblasts and corrected by chicken interferon
    • Levy A.M., Davidson I., Burgess S.C., and Dan Heller E. Major histocompatibility complex class I is downregulated in Marek's disease virus infected chicken embryo fibroblasts and corrected by chicken interferon. Comp. Immunol. Microbiol. Infect. Dis. 26 (2003) 189-198
    • (2003) Comp. Immunol. Microbiol. Infect. Dis. , vol.26 , pp. 189-198
    • Levy, A.M.1    Davidson, I.2    Burgess, S.C.3    Dan Heller, E.4
  • 39
    • 33748760661 scopus 로고    scopus 로고
    • Expression of Marek's disease virus phosphorylated polypeptide pp38 produces splice variants and enhances metabolic activity
    • Li X.H., Jarosinski K.W., and Schat K.A. Expression of Marek's disease virus phosphorylated polypeptide pp38 produces splice variants and enhances metabolic activity. Vet. Microbiol. 117 (2006) 154-168
    • (2006) Vet. Microbiol. , vol.117 , pp. 154-168
    • Li, X.H.1    Jarosinski, K.W.2    Schat, K.A.3
  • 40
    • 34247632080 scopus 로고    scopus 로고
    • Deubiquitination in virus infection
    • Lindner H.A. Deubiquitination in virus infection. Virology 362 (2007) 245-256
    • (2007) Virology , vol.362 , pp. 245-256
    • Lindner, H.A.1
  • 41
    • 0035543327 scopus 로고    scopus 로고
    • A strategy to identify positional candidate genes conferring Marek's disease resistance by integrating DNA microarrays and genetic mapping
    • Liu H.C., Cheng H.H., Tirunagaru V., Sofer L., and Burnside J. A strategy to identify positional candidate genes conferring Marek's disease resistance by integrating DNA microarrays and genetic mapping. Anim. Genet. 32 (2001) 351-359
    • (2001) Anim. Genet. , vol.32 , pp. 351-359
    • Liu, H.C.1    Cheng, H.H.2    Tirunagaru, V.3    Sofer, L.4    Burnside, J.5
  • 42
    • 33646557327 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach to study Marek's disease virus gene expression
    • Liu H.C.S., Soderblom E.J., and Goshe M.B. A mass spectrometry-based proteomic approach to study Marek's disease virus gene expression. J. Virol. Methods 135 (2006) 66-75
    • (2006) J. Virol. Methods , vol.135 , pp. 66-75
    • Liu, H.C.S.1    Soderblom, E.J.2    Goshe, M.B.3
  • 43
    • 43549083241 scopus 로고    scopus 로고
    • Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells
    • Liu N., Song W.J., Wang P., Lee K.C., Chan W., Chen H.L., et al. Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells. Proteomics 8 (2008) 1851-1858
    • (2008) Proteomics , vol.8 , pp. 1851-1858
    • Liu, N.1    Song, W.J.2    Wang, P.3    Lee, K.C.4    Chan, W.5    Chen, H.L.6
  • 44
    • 0036828724 scopus 로고    scopus 로고
    • Probability based validation of protein identifications using a modified SEQUEST algorithm
    • MacCoss M.J., Wu C.C., and Yates J.R. Probability based validation of protein identifications using a modified SEQUEST algorithm. Anal. Chem. 74 (2002) 5593-5599
    • (2002) Anal. Chem. , vol.74 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates, J.R.3
  • 45
    • 0032979181 scopus 로고    scopus 로고
    • Stathmin interaction with HSC70 family proteins
    • Manceau V., Gavet O., Curmi P., and Sobel A. Stathmin interaction with HSC70 family proteins. Electrophoresis 20 (1999) 409-417
    • (1999) Electrophoresis , vol.20 , pp. 409-417
    • Manceau, V.1    Gavet, O.2    Curmi, P.3    Sobel, A.4
  • 47
    • 0034751349 scopus 로고    scopus 로고
    • Induction of host gene expression following infection of chicken embryo fibroblasts with oncogenic Marek's disease virus
    • Morgan R.W., Sofer L., Anderson A.S., Bernberg E.L., Cui J., and Burnside J. Induction of host gene expression following infection of chicken embryo fibroblasts with oncogenic Marek's disease virus. J. Virol. 75 (2001) 533-539
    • (2001) J. Virol. , vol.75 , pp. 533-539
    • Morgan, R.W.1    Sofer, L.2    Anderson, A.S.3    Bernberg, E.L.4    Cui, J.5    Burnside, J.6
  • 48
    • 0029618664 scopus 로고
    • Immunomodulation of peripheral T-cells in chickens infected with Marek's disease virus - involvement in immunosuppression
    • Morimura T., Hattori M., Ohashi K., Sugimoto C., and Onuma M. Immunomodulation of peripheral T-cells in chickens infected with Marek's disease virus - involvement in immunosuppression. J. Gen. Virol. 76 (1995) 2979-2985
    • (1995) J. Gen. Virol. , vol.76 , pp. 2979-2985
    • Morimura, T.1    Hattori, M.2    Ohashi, K.3    Sugimoto, C.4    Onuma, M.5
  • 49
    • 0030453929 scopus 로고    scopus 로고
    • Apoptosis and CD8-down-regulation in the thymus of chickens infected with Marek's disease virus - brief report
    • Morimura T., Ohashi K., Kon Y., Hattori M., Sugimoto C., and Onuma M. Apoptosis and CD8-down-regulation in the thymus of chickens infected with Marek's disease virus - brief report. Arch. Virol. 141 (1996) 2243-2249
    • (1996) Arch. Virol. , vol.141 , pp. 2243-2249
    • Morimura, T.1    Ohashi, K.2    Kon, Y.3    Hattori, M.4    Sugimoto, C.5    Onuma, M.6
  • 50
    • 33845970245 scopus 로고    scopus 로고
    • Dynamics of the cellular metabolome during human cytomegalovirus infection
    • Munger J., Bajad S.U., Coller H.A., Shenk T., and Rabinowitz J.D. Dynamics of the cellular metabolome during human cytomegalovirus infection. PLoS pathog. 2 (2006) 1165-1175
    • (2006) PLoS pathog. , vol.2 , pp. 1165-1175
    • Munger, J.1    Bajad, S.U.2    Coller, H.A.3    Shenk, T.4    Rabinowitz, J.D.5
  • 51
    • 29544450310 scopus 로고    scopus 로고
    • Proteomic analysis using an unfinished bacterial genome: the effects of subminimum inhibitory concentrations of antibodies on Mannheimia haemolytica virulence factor expression
    • Nanduri B., Lawrence M.L., Vanguri S., and Burgess S.C. Proteomic analysis using an unfinished bacterial genome: the effects of subminimum inhibitory concentrations of antibodies on Mannheimia haemolytica virulence factor expression. Proteomics 5 (2005) 4852-4863
    • (2005) Proteomics , vol.5 , pp. 4852-4863
    • Nanduri, B.1    Lawrence, M.L.2    Vanguri, S.3    Burgess, S.C.4
  • 52
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., and Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75 (2003) 4646-4658
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 53
    • 33846807478 scopus 로고    scopus 로고
    • Marek's disease virus up-regulates major histocompatibility complex class II cell surface expression in infected cells
    • Niikura M., Kim T., Hunt H.D., Burnside J., Morgan R.W., Dodgson J.B., et al. Marek's disease virus up-regulates major histocompatibility complex class II cell surface expression in infected cells. Virology 359 (2007) 212-219
    • (2007) Virology , vol.359 , pp. 212-219
    • Niikura, M.1    Kim, T.2    Hunt, H.D.3    Burnside, J.4    Morgan, R.W.5    Dodgson, J.B.6
  • 54
    • 11144241331 scopus 로고    scopus 로고
    • Use of DNA microarrays to monitor host response to virus and virus-derived gene therapy vectors
    • Piersanti S., Martina Y., Cherubini G., Avitabile D., and Saggio I. Use of DNA microarrays to monitor host response to virus and virus-derived gene therapy vectors. Am. J. Pharmacogenomics 4 (2004) 345-356
    • (2004) Am. J. Pharmacogenomics , vol.4 , pp. 345-356
    • Piersanti, S.1    Martina, Y.2    Cherubini, G.3    Avitabile, D.4    Saggio, I.5
  • 55
    • 55949109950 scopus 로고    scopus 로고
    • Changes in the Gallus gallus proteome induced by Marek's disease virus
    • Ramaroson M.F., Ruby J., Goshe M.B., and Liu H.C. Changes in the Gallus gallus proteome induced by Marek's disease virus. J. Proteome Res. 7 (2008) 4346-4358
    • (2008) J. Proteome Res. , vol.7 , pp. 4346-4358
    • Ramaroson, M.F.1    Ruby, J.2    Goshe, M.B.3    Liu, H.C.4
  • 56
    • 58149400656 scopus 로고    scopus 로고
    • Differential proteome expression associated with urokinase plasminogen activator receptor (uPAR) suppression in malignant epithelial cancer
    • Saldanha R.G., Xu N., Molloy M.P., Veal D.A., and Baker M.S. Differential proteome expression associated with urokinase plasminogen activator receptor (uPAR) suppression in malignant epithelial cancer. J. Proteome Res. 7 (2008) 4792-4806
    • (2008) J. Proteome Res. , vol.7 , pp. 4792-4806
    • Saldanha, R.G.1    Xu, N.2    Molloy, M.P.3    Veal, D.A.4    Baker, M.S.5
  • 57
    • 33846069309 scopus 로고    scopus 로고
    • Transcriptional analysis of host responses to Marek's disease viral infection
    • Sarson A.J., Abdul-Careem M.F., Zhou H., and Sharif S. Transcriptional analysis of host responses to Marek's disease viral infection. Viral Immunol. 19 (2006) 747-758
    • (2006) Viral Immunol. , vol.19 , pp. 747-758
    • Sarson, A.J.1    Abdul-Careem, M.F.2    Zhou, H.3    Sharif, S.4
  • 58
    • 0002580579 scopus 로고
    • Characterization of 2 highly oncogenic strains of Marek's disease virus
    • Schat K.A., Calnek B.W., and Fabricant J. Characterization of 2 highly oncogenic strains of Marek's disease virus. Avian Pathol. 11 (1982) 593-605
    • (1982) Avian Pathol. , vol.11 , pp. 593-605
    • Schat, K.A.1    Calnek, B.W.2    Fabricant, J.3
  • 59
    • 15244359449 scopus 로고    scopus 로고
    • S3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown
    • S3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown. J. Virol. 79 (2005) 3987-3997
    • (2005) J. Virol. , vol.79 , pp. 3987-3997
    • Schumacher, D.1    Tischer, B.K.2    Trapp, S.3    Osterrieder, N.4
  • 60
    • 44249105923 scopus 로고    scopus 로고
    • hi) Marek's disease lymphoma cell phenotype most closely resembles T-regulatory cells. Cancer Immunol
    • hi) Marek's disease lymphoma cell phenotype most closely resembles T-regulatory cells. Cancer Immunol. Immunother. 57 (2008) 1253-1262
    • (2008) Immunother. , vol.57 , pp. 1253-1262
    • Shack, L.A.1    Buza, J.J.2    Burgess, S.C.3
  • 61
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., and Mann M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68 (1996) 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 62
    • 0033176061 scopus 로고    scopus 로고
    • Response of embryonic chicken lymphocytes to in ovo exposure to lymphotropic viruses
    • St Hill C.A., and Sharma J.M. Response of embryonic chicken lymphocytes to in ovo exposure to lymphotropic viruses. Am. J. Vet. Res. 60 (1999) 937-941
    • (1999) Am. J. Vet. Res. , vol.60 , pp. 937-941
    • St Hill, C.A.1    Sharma, J.M.2
  • 63
    • 0033884066 scopus 로고    scopus 로고
    • Regulation of host cell translation by viruses and effects on cell function
    • Thompson S.R., and Sarnow P. Regulation of host cell translation by viruses and effects on cell function. Curr. Opin. Microbiol. 3 (2000) 366-370
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 366-370
    • Thompson, S.R.1    Sarnow, P.2
  • 64
    • 0037401872 scopus 로고    scopus 로고
    • Deubiquitinating enzymes-the importance of driving in reverse along the ubiquitin-proteasome pathway
    • Wing S.S. Deubiquitinating enzymes-the importance of driving in reverse along the ubiquitin-proteasome pathway. Int. J. Biochem. Cell Biol. 35 (2003) 590-605
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 590-605
    • Wing, S.S.1
  • 65
    • 0030936371 scopus 로고    scopus 로고
    • Increased virulence of Marek's disease virus field isolates
    • Witter R.L. Increased virulence of Marek's disease virus field isolates. Avian Dis. 41 (1997) 149-163
    • (1997) Avian Dis. , vol.41 , pp. 149-163
    • Witter, R.L.1
  • 66
    • 0034050549 scopus 로고    scopus 로고
    • Expression of cytokine genes in Marek's disease virus-infected chickens and chicken embryo fibroblast cultures
    • Xing Z., and Schat K.A. Expression of cytokine genes in Marek's disease virus-infected chickens and chicken embryo fibroblast cultures. Immunology 100 (2000) 70-76
    • (2000) Immunology , vol.100 , pp. 70-76
    • Xing, Z.1    Schat, K.A.2
  • 67
    • 33646432725 scopus 로고    scopus 로고
    • Suppressive effect of elongation factor 2 on apoptosis induced by HIV-1 viral protein R
    • Zelivianski S., Liang D., Chen M., Mirkin B.L., and Zhao R.Y. Suppressive effect of elongation factor 2 on apoptosis induced by HIV-1 viral protein R. Apoptosis 11 (2006) 377-388
    • (2006) Apoptosis , vol.11 , pp. 377-388
    • Zelivianski, S.1    Liang, D.2    Chen, M.3    Mirkin, B.L.4    Zhao, R.Y.5
  • 68
    • 17144475356 scopus 로고    scopus 로고
    • Host-pathogen interactions: a proteomic view. Expert Rev
    • Zhang C.G., Chromy B.A., and McCutchen-Maloney S.L. Host-pathogen interactions: a proteomic view. Expert Rev. Proteomics 2 (2005) 187-202
    • (2005) Proteomics , vol.2 , pp. 187-202
    • Zhang, C.G.1    Chromy, B.A.2    McCutchen-Maloney, S.L.3
  • 69
    • 41549087403 scopus 로고    scopus 로고
    • Proteomics analysis of host cells infected with infectious bursal disease virus
    • Zheng X.J., Hong L.L., Shi L.X., Guo J.Q., Sun Z., and Zhou J.Y. Proteomics analysis of host cells infected with infectious bursal disease virus. Mol. Cell. Proteomics 7 (2008) 612-625
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 612-625
    • Zheng, X.J.1    Hong, L.L.2    Shi, L.X.3    Guo, J.Q.4    Sun, Z.5    Zhou, J.Y.6


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