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Volumn 11, Issue 2, 2012, Pages 995-1008

Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals protein and pathway regulation in porcine circovirus type 2 infected PK-15 cells

Author keywords

pathway analysis; porcine circovirus type 2; quantitative proteomics; stable isotope labeling with amino acids in cell culture (SILAC)

Indexed keywords

AMINO ACID; CELL PROTEIN;

EID: 84856645718     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200755d     Document Type: Article
Times cited : (31)

References (71)
  • 1
    • 78349282668 scopus 로고    scopus 로고
    • Bronchiolitis obliterans organizing pneumonia in Swine associated with porcine circovirus type 2 infection
    • Cheng, C. C.; Lee, Y. F.; Lin, N. N.; Wu, C. L.; Tung, K. C.; Chiu, Y. T. Bronchiolitis obliterans organizing pneumonia in Swine associated with porcine circovirus type 2 infection J. Biomed. Biotechnol. 2011, 2011, 245728
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 245728
    • Cheng, C.C.1    Lee, Y.F.2    Lin, N.N.3    Wu, C.L.4    Tung, K.C.5    Chiu, Y.T.6
  • 2
    • 79952107078 scopus 로고    scopus 로고
    • Immunopathological characterization of porcine circovirus type 2 infection-associated follicular changes in inguinal lymph nodes using high-throughput tissue microarray
    • Lin, C. M.; Jeng, C. R.; Hsiao, S. H.; Liu, J. P.; Chang, C. C.; Chiou, M. T.; Tsai, Y. C.; Chia, M. Y.; Pang, V. F. Immunopathological characterization of porcine circovirus type 2 infection-associated follicular changes in inguinal lymph nodes using high-throughput tissue microarray Vet. Microbiol. 2011, 149 (1-2) 72-84
    • (2011) Vet. Microbiol. , vol.149 , Issue.1-2 , pp. 72-84
    • Lin, C.M.1    Jeng, C.R.2    Hsiao, S.H.3    Liu, J.P.4    Chang, C.C.5    Chiou, M.T.6    Tsai, Y.C.7    Chia, M.Y.8    Pang, V.F.9
  • 3
    • 49049100655 scopus 로고    scopus 로고
    • Post-weaning multisystemic wasting syndrome and other PCV2-related problems in pigs: A 12-year experience
    • Madec, F.; Rose, N.; Grasland, B.; Cariolet, R.; Jestin, A. Post-weaning multisystemic wasting syndrome and other PCV2-related problems in pigs: a 12-year experience Transbound Emerg. Dis. 2008, 55 (7) 273-83
    • (2008) Transbound Emerg. Dis. , vol.55 , Issue.7 , pp. 273-83
    • Madec, F.1    Rose, N.2    Grasland, B.3    Cariolet, R.4    Jestin, A.5
  • 4
    • 67650918303 scopus 로고    scopus 로고
    • Reproductive failure experimentally induced in sows via artificial insemination with semen spiked with porcine circovirus type 2
    • Madson, D. M.; Patterson, A. R.; Ramamoorthy, S.; Pal, N.; Meng, X. J.; Opriessnig, T. Reproductive failure experimentally induced in sows via artificial insemination with semen spiked with porcine circovirus type 2 Vet. Pathol. 2009, 46 (4) 707-16
    • (2009) Vet. Pathol. , vol.46 , Issue.4 , pp. 707-16
    • Madson, D.M.1    Patterson, A.R.2    Ramamoorthy, S.3    Pal, N.4    Meng, X.J.5    Opriessnig, T.6
  • 5
    • 2442471877 scopus 로고    scopus 로고
    • Pathogenesis of postweaning multisystemic wasting syndrome caused by Porcine circovirus 2: An immune riddle
    • Darwich, L.; Segales, J.; Mateu, E. Pathogenesis of postweaning multisystemic wasting syndrome caused by Porcine circovirus 2: An immune riddle Arch. Virol. 2004, 149 (5) 857-74
    • (2004) Arch. Virol. , vol.149 , Issue.5 , pp. 857-74
    • Darwich, L.1    Segales, J.2    Mateu, E.3
  • 6
    • 0345599153 scopus 로고    scopus 로고
    • Comparison of the structures of three circoviruses: Chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus
    • Crowther, R. A.; Berriman, J. A.; Curran, W. L.; Allan, G. M.; Todd, D. Comparison of the structures of three circoviruses: chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus J. Virol. 2003, 77 (24) 13036-41
    • (2003) J. Virol. , vol.77 , Issue.24 , pp. 13036-41
    • Crowther, R.A.1    Berriman, J.A.2    Curran, W.L.3    Allan, G.M.4    Todd, D.5
  • 7
    • 0031950374 scopus 로고    scopus 로고
    • Nucleotide sequence of porcine circovirus associated with postweaning multisystemic wasting syndrome in pigs
    • Hamel, A. L.; Lin, L. L.; Nayar, G. P. Nucleotide sequence of porcine circovirus associated with postweaning multisystemic wasting syndrome in pigs J. Virol. 1998, 72 (6) 5262-7
    • (1998) J. Virol. , vol.72 , Issue.6 , pp. 5262-7
    • Hamel, A.L.1    Lin, L.L.2    Nayar, G.P.3
  • 8
    • 0031041177 scopus 로고    scopus 로고
    • Mapping and characterization of the origin of DNA replication of porcine circovirus
    • Mankertz, A.; Persson, F.; Mankertz, J.; Blaess, G.; Buhk, H. J. Mapping and characterization of the origin of DNA replication of porcine circovirus J. Virol. 1997, 71 (3) 2562-6
    • (1997) J. Virol. , vol.71 , Issue.3 , pp. 2562-6
    • Mankertz, A.1    Persson, F.2    Mankertz, J.3    Blaess, G.4    Buhk, H.J.5
  • 9
    • 0033833402 scopus 로고    scopus 로고
    • Open reading frame 2 of porcine circovirus type 2 encodes a major capsid protein
    • Nawagitgul, P.; Morozov, I.; Bolin, S. R.; Harms, P. A.; Sorden, S. D.; Paul, P. S. Open reading frame 2 of porcine circovirus type 2 encodes a major capsid protein J. Gen. Virol. 2000, 81 (Pt 9) 2281-7
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 9 , pp. 2281-7
    • Nawagitgul, P.1    Morozov, I.2    Bolin, S.R.3    Harms, P.A.4    Sorden, S.D.5    Paul, P.S.6
  • 10
    • 77956264738 scopus 로고    scopus 로고
    • Porcine circovirus type 2 (PCV2) Cap and Rep proteins are involved in the development of cell-mediated immunity upon PCV2 infection
    • Fort, M.; Sibila, M.; Nofrarias, M.; Perez-Martin, E.; Olvera, A.; Mateu, E.; Segales, J. Porcine circovirus type 2 (PCV2) Cap and Rep proteins are involved in the development of cell-mediated immunity upon PCV2 infection Vet. Immunol. Immunopathol. 2010, 137 (3-4) 226-34
    • (2010) Vet. Immunol. Immunopathol. , vol.137 , Issue.3-4 , pp. 226-34
    • Fort, M.1    Sibila, M.2    Nofrarias, M.3    Perez-Martin, E.4    Olvera, A.5    Mateu, E.6    Segales, J.7
  • 11
    • 20744458839 scopus 로고    scopus 로고
    • Characterization of a previously unidentified viral protein in porcine circovirus type 2-infected cells and its role in virus-induced apoptosis
    • Liu, J.; Chen, I.; Kwang, J. Characterization of a previously unidentified viral protein in porcine circovirus type 2-infected cells and its role in virus-induced apoptosis J. Virol. 2005, 79 (13) 8262-74
    • (2005) J. Virol. , vol.79 , Issue.13 , pp. 8262-74
    • Liu, J.1    Chen, I.2    Kwang, J.3
  • 12
    • 78650011823 scopus 로고    scopus 로고
    • Porcine circovirus type 2 DNA influences cytoskeleton rearrangements in plasmacytoid and monocyte-derived dendritic cells
    • Balmelli, C.; Steiner, E.; Moulin, H.; Peduto, N.; Herrmann, B.; Summerfield, A.; McCullough, K. Porcine circovirus type 2 DNA influences cytoskeleton rearrangements in plasmacytoid and monocyte-derived dendritic cells Immunology 2011, 132 (1) 57-65
    • (2011) Immunology , vol.132 , Issue.1 , pp. 57-65
    • Balmelli, C.1    Steiner, E.2    Moulin, H.3    Peduto, N.4    Herrmann, B.5    Summerfield, A.6    McCullough, K.7
  • 13
    • 79951773447 scopus 로고    scopus 로고
    • Proinflammatory cytokine expression in the lung of pigs with porcine circovirus type 2-associated respiratory disease
    • Chae, J. S.; Choi, K. S. Proinflammatory cytokine expression in the lung of pigs with porcine circovirus type 2-associated respiratory disease Res. Vet. Sci. 2011, 90 (2) 321-3
    • (2011) Res. Vet. Sci. , vol.90 , Issue.2 , pp. 321-3
    • Chae, J.S.1    Choi, K.S.2
  • 14
    • 77957853200 scopus 로고    scopus 로고
    • Porcine circovirus type 2 (PCV2) induces cell proliferation, fusion, and chemokine expression in swine monocytic cells in vitro
    • Tsai, Y. C.; Jeng, C. R.; Hsiao, S. H.; Chang, H. W.; Liu, J. J.; Chang, C. C.; Lin, C. M.; Chia, M. Y.; Pang, V. F. Porcine circovirus type 2 (PCV2) induces cell proliferation, fusion, and chemokine expression in swine monocytic cells in vitro Vet. Res. 2010, 41 (5) 60
    • (2010) Vet. Res. , vol.41 , Issue.5 , pp. 60
    • Tsai, Y.C.1    Jeng, C.R.2    Hsiao, S.H.3    Chang, H.W.4    Liu, J.J.5    Chang, C.C.6    Lin, C.M.7    Chia, M.Y.8    Pang, V.F.9
  • 15
    • 0242320355 scopus 로고    scopus 로고
    • Identification of a sequence from the genome of porcine circovirus type 2 with an inhibitory effect on IFN-alpha production by porcine PBMCs
    • Hasslung, F. C.; Berg, M.; Allan, G. M.; Meehan, B. M.; McNeilly, F.; Fossum, C. Identification of a sequence from the genome of porcine circovirus type 2 with an inhibitory effect on IFN-alpha production by porcine PBMCs J. Gen. Virol. 2003, 84 (Pt 11) 2937-45
    • (2003) J. Gen. Virol. , vol.84 , Issue.PART 11 , pp. 2937-45
    • Hasslung, F.C.1    Berg, M.2    Allan, G.M.3    Meehan, B.M.4    McNeilly, F.5    Fossum, C.6
  • 16
    • 76049110438 scopus 로고    scopus 로고
    • Porcine circovirus type 2 ORF3 protein competes with p53 in binding to Pirh2 and mediates the deregulation of p53 homeostasis
    • Karuppannan, A. K.; Liu, S.; Jia, Q.; Selvaraj, M.; Kwang, J. Porcine circovirus type 2 ORF3 protein competes with p53 in binding to Pirh2 and mediates the deregulation of p53 homeostasis Virology 2010, 398 (1) 1-11
    • (2010) Virology , vol.398 , Issue.1 , pp. 1-11
    • Karuppannan, A.K.1    Liu, S.2    Jia, Q.3    Selvaraj, M.4    Kwang, J.5
  • 17
    • 66149087263 scopus 로고    scopus 로고
    • JNK and p38 mitogen-activated protein kinase pathways contribute to porcine circovirus type 2 infection
    • Wei, L.; Zhu, Z.; Wang, J.; Liu, J. JNK and p38 mitogen-activated protein kinase pathways contribute to porcine circovirus type 2 infection J. Virol. 2009, 83 (12) 6039-47
    • (2009) J. Virol. , vol.83 , Issue.12 , pp. 6039-47
    • Wei, L.1    Zhu, Z.2    Wang, J.3    Liu, J.4
  • 18
    • 61649086141 scopus 로고    scopus 로고
    • Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins
    • Finsterbusch, T.; Steinfeldt, T.; Doberstein, K.; Rodner, C.; Mankertz, A. Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins Virology 2009, 386 (1) 122-31
    • (2009) Virology , vol.386 , Issue.1 , pp. 122-31
    • Finsterbusch, T.1    Steinfeldt, T.2    Doberstein, K.3    Rodner, C.4    Mankertz, A.5
  • 19
    • 33750267397 scopus 로고    scopus 로고
    • Porcine circovirus type 2 replicase binds the capsid protein and an intermediate filament-like protein
    • Timmusk, S.; Fossum, C.; Berg, M. Porcine circovirus type 2 replicase binds the capsid protein and an intermediate filament-like protein J. Gen. Virol. 2006, 87 (Pt 11) 3215-23
    • (2006) J. Gen. Virol. , vol.87 , Issue.PART 11 , pp. 3215-23
    • Timmusk, S.1    Fossum, C.2    Berg, M.3
  • 20
    • 70449381259 scopus 로고    scopus 로고
    • Differential proteome analysis of host cells infected with porcine circovirus type 2
    • Zhang, X.; Zhou, J.; Wu, Y.; Zheng, X.; Ma, G.; Wang, Z.; Jin, Y.; He, J.; Yan, Y. Differential proteome analysis of host cells infected with porcine circovirus type 2 J. Proteome Res. 2009, 8 (11) 5111-9
    • (2009) J. Proteome Res. , vol.8 , Issue.11 , pp. 5111-9
    • Zhang, X.1    Zhou, J.2    Wu, Y.3    Zheng, X.4    Ma, G.5    Wang, Z.6    Jin, Y.7    He, J.8    Yan, Y.9
  • 21
    • 77957355995 scopus 로고    scopus 로고
    • Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells
    • Emmott, E.; Wise, H.; Loucaides, E. M.; Matthews, D. A.; Digard, P.; Hiscox, J. A. Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells J. Proteome Res. 2010, 9 (10) 5335-45
    • (2010) J. Proteome Res. , vol.9 , Issue.10 , pp. 5335-45
    • Emmott, E.1    Wise, H.2    Loucaides, E.M.3    Matthews, D.A.4    Digard, P.5    Hiscox, J.A.6
  • 22
    • 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.; Wu, J. R.; Zeng, R. 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 2005, 4 (7) 902-13
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.7 , pp. 902-13
    • Jiang, X.S.1    Tang, L.Y.2    Dai, J.3    Zhou, H.4    Li, S.J.5    Xia, Q.C.6    Wu, J.R.7    Zeng, R.8
  • 23
    • 77952878717 scopus 로고    scopus 로고
    • Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques
    • Skiba, M.; Glowinski, F.; Koczan, D.; Mettenleiter, T. C.; Karger, A. Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques Vet. Microbiol. 2010, 143 (1) 14-20
    • (2010) Vet. Microbiol. , vol.143 , Issue.1 , pp. 14-20
    • Skiba, M.1    Glowinski, F.2    Koczan, D.3    Mettenleiter, T.C.4    Karger, A.5
  • 24
    • 77956497028 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals changes in the cytoplasmic, nuclear, and nucleolar proteomes in Vero cells infected with the coronavirus infectious bronchitis virus
    • Emmott, E.; Rodgers, M. A.; Macdonald, A.; McCrory, S.; Ajuh, P.; Hiscox, J. A. Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals changes in the cytoplasmic, nuclear, and nucleolar proteomes in Vero cells infected with the coronavirus infectious bronchitis virus Mol. Cell. Proteomics 2010, 9 (9) 1920-36
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.9 , pp. 1920-36
    • Emmott, E.1    Rodgers, M.A.2    MacDonald, A.3    McCrory, S.4    Ajuh, P.5    Hiscox, J.A.6
  • 28
    • 69149098047 scopus 로고    scopus 로고
    • HIV induces both a down-regulation of IRAK-4 that impairs TLR signalling and an up-regulation of the antibiotic peptide dermcidin in monocytic cells
    • Pathak, S.; De Souza, G. A.; Salte, T.; Wiker, H. G.; Asjo, B. HIV induces both a down-regulation of IRAK-4 that impairs TLR signalling and an up-regulation of the antibiotic peptide dermcidin in monocytic cells Scand. J. Immunol. 2009, 70 (3) 264-76
    • (2009) Scand. J. Immunol. , vol.70 , Issue.3 , pp. 264-76
    • Pathak, S.1    De Souza, G.A.2    Salte, T.3    Wiker, H.G.4    Asjo, B.5
  • 29
    • 79951742026 scopus 로고    scopus 로고
    • Global identification of miR-373-regulated genes in breast cancer by quantitative proteomics
    • Yan, G. R.; Xu, S. H.; Tan, Z. L.; Liu, L.; He, Q. Y. Global identification of miR-373-regulated genes in breast cancer by quantitative proteomics Proteomics 2011, 11 (5) 912-20
    • (2011) Proteomics , vol.11 , Issue.5 , pp. 912-20
    • Yan, G.R.1    Xu, S.H.2    Tan, Z.L.3    Liu, L.4    He, Q.Y.5
  • 30
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26 (12) 1367-72
    • (2008) Nat. Biotechnol. , vol.26 , Issue.12 , pp. 1367-72
    • Cox, J.1    Mann, M.2
  • 31
    • 61349162384 scopus 로고    scopus 로고
    • Proteomic alteration of PK-15 cells after infection by classical swine fever virus
    • Sun, J.; Jiang, Y.; Shi, Z.; Yan, Y.; Guo, H.; He, F.; Tu, C. Proteomic alteration of PK-15 cells after infection by classical swine fever virus J. Proteome Res. 2008, 7 (12) 5263-9
    • (2008) J. Proteome Res. , vol.7 , Issue.12 , pp. 5263-9
    • Sun, J.1    Jiang, Y.2    Shi, Z.3    Yan, Y.4    Guo, H.5    He, F.6    Tu, C.7
  • 32
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M. Functional and quantitative proteomics using SILAC Nat. Rev. Mol. Cell. Biol. 2006, 7 (12) 952-8
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , Issue.12 , pp. 952-8
    • Mann, M.1
  • 33
    • 36148990505 scopus 로고    scopus 로고
    • The calpains: Modular designs and functional diversity
    • Croall, D. E.; Ersfeld, K. The calpains: modular designs and functional diversity Genome Biol. 2007, 8 (6) 218
    • (2007) Genome Biol. , vol.8 , Issue.6 , pp. 218
    • Croall, D.E.1    Ersfeld, K.2
  • 37
    • 0024994036 scopus 로고
    • In vitro digestion of spectrin, protein 4.1 and ankyrin by erythrocyte calcium dependent neutral protease (calpain I)
    • Boivin, P.; Galand, C.; Dhermy, D. In vitro digestion of spectrin, protein 4.1 and ankyrin by erythrocyte calcium dependent neutral protease (calpain I) Int. J. Biochem. 1990, 22 (12) 1479-89
    • (1990) Int. J. Biochem. , vol.22 , Issue.12 , pp. 1479-89
    • Boivin, P.1    Galand, C.2    Dhermy, D.3
  • 38
    • 0034524665 scopus 로고    scopus 로고
    • The pathogenic activation of calpain: A marker and mediator of cellular toxicity and disease states
    • Vanderklish, P. W.; Bahr, B. A. The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states Int. J. Exp. Pathol. 2000, 81 (5) 323-39
    • (2000) Int. J. Exp. Pathol. , vol.81 , Issue.5 , pp. 323-39
    • Vanderklish, P.W.1    Bahr, B.A.2
  • 40
    • 85047689015 scopus 로고    scopus 로고
    • Calpains can do it alone: Implications for cancer therapy
    • Guicciardi, M. E.; Gores, G. J. Calpains can do it alone: implications for cancer therapy Cancer Biol. Ther. 2003, 2 (2) 153-4
    • (2003) Cancer Biol. Ther. , vol.2 , Issue.2 , pp. 153-4
    • Guicciardi, M.E.1    Gores, G.J.2
  • 41
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni, J.; Ellerby, L. M. Calpain activation in Huntington's disease J. Neurosci. 2002, 22 (12) 4842-9
    • (2002) J. Neurosci. , vol.22 , Issue.12 , pp. 4842-9
    • Gafni, J.1    Ellerby, L.M.2
  • 42
    • 78449296170 scopus 로고    scopus 로고
    • Cleavage of Tau by calpain in Alzheimer's disease: The quest for the toxic 17 kD fragment
    • Garg, S.; Timm, T.; Mandelkow, E. M.; Mandelkow, E.; Wang, Y. Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment Neurobiol. Aging 2011, 32 (1) 1-14
    • (2011) Neurobiol. Aging , vol.32 , Issue.1 , pp. 1-14
    • Garg, S.1    Timm, T.2    Mandelkow, E.M.3    Mandelkow, E.4    Wang, Y.5
  • 43
    • 20344386015 scopus 로고    scopus 로고
    • Calpains and disease
    • Zatz, M.; Starling, A. Calpains and disease N. Engl. J. Med. 2005, 352 (23) 2413-23
    • (2005) N. Engl. J. Med. , vol.352 , Issue.23 , pp. 2413-23
    • Zatz, M.1    Starling, A.2
  • 44
    • 0036934648 scopus 로고    scopus 로고
    • Calpain activation in neurodegenerative diseases: Confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2
    • Adamec, E.; Mohan, P.; Vonsattel, J. P.; Nixon, R. A. Calpain activation in neurodegenerative diseases: confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2 Acta Neuropathol. 2002, 104 (1) 92-104
    • (2002) Acta Neuropathol. , vol.104 , Issue.1 , pp. 92-104
    • Adamec, E.1    Mohan, P.2    Vonsattel, J.P.3    Nixon, R.A.4
  • 46
    • 77953525398 scopus 로고    scopus 로고
    • Hepatitis B virus X protein upregulates expression of calpain small subunit 1 via nuclear factor-kappaB/p65 in hepatoma cells
    • Zhang, F.; Wang, Q.; Ye, L.; Feng, Y.; Zhang, X. Hepatitis B virus X protein upregulates expression of calpain small subunit 1 via nuclear factor-kappaB/p65 in hepatoma cells J. Med. Virol. 2010, 82 (6) 920-8
    • (2010) J. Med. Virol. , vol.82 , Issue.6 , pp. 920-8
    • Zhang, F.1    Wang, Q.2    Ye, L.3    Feng, Y.4    Zhang, X.5
  • 47
    • 77958566966 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Tat activates calpain proteases via the ryanodine receptor to enhance surface dopamine transporter levels and increase transporter-specific uptake and Vmax
    • Perry, S. W.; Barbieri, J.; Tong, N.; Polesskaya, O.; Pudasaini, S.; Stout, A.; Lu, R.; Kiebala, M.; Maggirwar, S. B.; Gelbard, H. A. Human immunodeficiency virus-1 Tat activates calpain proteases via the ryanodine receptor to enhance surface dopamine transporter levels and increase transporter-specific uptake and Vmax J. Neurosci. 2010, 30 (42) 14153-64
    • (2010) J. Neurosci. , vol.30 , Issue.42 , pp. 14153-64
    • Perry, S.W.1    Barbieri, J.2    Tong, N.3    Polesskaya, O.4    Pudasaini, S.5    Stout, A.6    Lu, R.7    Kiebala, M.8    Maggirwar, S.B.9    Gelbard, H.A.10
  • 48
    • 0035971091 scopus 로고    scopus 로고
    • Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: A mechanism of 'pathological apoptosis'?
    • Blomgren, K.; Zhu, C.; Wang, X.; Karlsson, J. O.; Leverin, A. L.; Bahr, B. A.; Mallard, C.; Hagberg, H. Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of 'pathological apoptosis'? J. Biol. Chem. 2001, 276 (13) 10191-8
    • (2001) J. Biol. Chem. , vol.276 , Issue.13 , pp. 10191-8
    • Blomgren, K.1    Zhu, C.2    Wang, X.3    Karlsson, J.O.4    Leverin, A.L.5    Bahr, B.A.6    Mallard, C.7    Hagberg, H.8
  • 49
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • Chua, B. T.; Guo, K.; Li, P. Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases J. Biol. Chem. 2000, 275 (7) 5131-5
    • (2000) J. Biol. Chem. , vol.275 , Issue.7 , pp. 5131-5
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 51
    • 0033568430 scopus 로고    scopus 로고
    • Implication of calpain in caspase activation during B cell clonal deletion
    • Ruiz-Vela, A.; Gonzalez, D. B. G.; Martinez-A, C. Implication of calpain in caspase activation during B cell clonal deletion EMBO J. 1999, 18 (18) 4988-98
    • (1999) EMBO J. , vol.18 , Issue.18 , pp. 4988-98
    • Ruiz-Vela, A.1    Gonzalez, D.B.G.2    Martinez-A, C.3
  • 52
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa, T.; Yuan, J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis J. Cell Biol. 2000, 150 (4) 887-94
    • (2000) J. Cell Biol. , vol.150 , Issue.4 , pp. 887-94
    • Nakagawa, T.1    Yuan, J.2
  • 53
    • 31344432567 scopus 로고    scopus 로고
    • Degraded collagen induces calpain-mediated apoptosis and destruction of the X-chromosome-linked inhibitor of apoptosis (xIAP) in human vascular smooth muscle cells
    • von Wnuck, L. K.; Keul, P.; Lucke, S.; Heusch, G.; Wohlschlaeger, J.; Baba, H. A.; Levkau, B. Degraded collagen induces calpain-mediated apoptosis and destruction of the X-chromosome-linked inhibitor of apoptosis (xIAP) in human vascular smooth muscle cells Cardiovasc. Res. 2006, 69 (3) 697-705
    • (2006) Cardiovasc. Res. , vol.69 , Issue.3 , pp. 697-705
    • Von Wnuck, L.K.1    Keul, P.2    Lucke, S.3    Heusch, G.4    Wohlschlaeger, J.5    Baba, H.A.6    Levkau, B.7
  • 54
    • 65249111703 scopus 로고    scopus 로고
    • Cardiac-specific deletion of mkk4 reveals its role in pathological hypertrophic remodeling but not in physiological cardiac growth
    • Liu, W.; Zi, M.; Jin, J.; Prehar, S.; Oceandy, D.; Kimura, T. E.; Lei, M.; Neyses, L.; Weston, A. H.; Cartwright, E. J.; Wang, X. Cardiac-specific deletion of mkk4 reveals its role in pathological hypertrophic remodeling but not in physiological cardiac growth Circ. Res. 2009, 104 (7) 905-14
    • (2009) Circ. Res. , vol.104 , Issue.7 , pp. 905-14
    • Liu, W.1    Zi, M.2    Jin, J.3    Prehar, S.4    Oceandy, D.5    Kimura, T.E.6    Lei, M.7    Neyses, L.8    Weston, A.H.9    Cartwright, E.J.10    Wang, X.11
  • 55
    • 33646365075 scopus 로고    scopus 로고
    • Regulation of Stat3 nuclear import by importin alpha5 and importin alpha7 via two different functional sequence elements
    • Ma, J.; Cao, X. Regulation of Stat3 nuclear import by importin alpha5 and importin alpha7 via two different functional sequence elements Cell Signal. 2006, 18 (8) 1117-26
    • (2006) Cell Signal. , vol.18 , Issue.8 , pp. 1117-26
    • Ma, J.1    Cao, X.2
  • 56
    • 40349113426 scopus 로고    scopus 로고
    • Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus
    • Gabriel, G.; Herwig, A.; Klenk, H. D. Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus PLoS Pathog. 2008, 4 (2) e11
    • (2008) PLoS Pathog. , vol.4 , Issue.2 , pp. 11
    • Gabriel, G.1    Herwig, A.2    Klenk, H.D.3
  • 57
    • 0031041580 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 1 forms a complex with the nuclear transporter karyopherin alpha2
    • Fischer, N.; Kremmer, E.; Lautscham, G.; Mueller-Lantzsch, N.; Grasser, F. A. Epstein-Barr virus nuclear antigen 1 forms a complex with the nuclear transporter karyopherin alpha2 J. Biol. Chem. 1997, 272 (7) 3999-4005
    • (1997) J. Biol. Chem. , vol.272 , Issue.7 , pp. 3999-4005
    • Fischer, N.1    Kremmer, E.2    Lautscham, G.3    Mueller-Lantzsch, N.4    Grasser, F.A.5
  • 58
    • 0035827596 scopus 로고    scopus 로고
    • A gamma-2 herpesvirus nucleocytoplasmic shuttle protein interacts with importin alpha 1 and alpha 5
    • Goodwin, D. J.; Whitehouse, A. A gamma-2 herpesvirus nucleocytoplasmic shuttle protein interacts with importin alpha 1 and alpha 5 J. Biol. Chem. 2001, 276 (23) 19905-12
    • (2001) J. Biol. Chem. , vol.276 , Issue.23 , pp. 19905-12
    • Goodwin, D.J.1    Whitehouse, A.2
  • 59
    • 0033567847 scopus 로고    scopus 로고
    • Nuclear import of HPV11 L1 capsid protein is mediated by karyopherin alpha2beta1 heterodimers
    • Merle, E.; Rose, R. C.; LeRoux, L.; Moroianu, J. Nuclear import of HPV11 L1 capsid protein is mediated by karyopherin alpha2beta1 heterodimers J. Cell Biochem. 1999, 74 (4) 628-37
    • (1999) J. Cell Biochem. , vol.74 , Issue.4 , pp. 628-37
    • Merle, E.1    Rose, R.C.2    Leroux, L.3    Moroianu, J.4
  • 60
    • 0031975959 scopus 로고    scopus 로고
    • HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection
    • Vodicka, M. A.; Koepp, D. M.; Silver, P. A.; Emerman, M. HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection Genes Dev. 1998, 12 (2) 175-85
    • (1998) Genes Dev. , vol.12 , Issue.2 , pp. 175-85
    • Vodicka, M.A.1    Koepp, D.M.2    Silver, P.A.3    Emerman, M.4
  • 61
    • 33845406669 scopus 로고    scopus 로고
    • Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex
    • Deng, T.; Engelhardt, O. G.; Thomas, B.; Akoulitchev, A. V.; Brownlee, G. G.; Fodor, E. Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex J. Virol. 2006, 80 (24) 11911-9
    • (2006) J. Virol. , vol.80 , Issue.24 , pp. 11911-9
    • Deng, T.1    Engelhardt, O.G.2    Thomas, B.3    Akoulitchev, A.V.4    Brownlee, G.G.5    Fodor, E.6
  • 62
    • 35348964100 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection
    • Chongsatja, P. O.; Bourchookarn, A.; Lo, C. F.; Thongboonkerd, V.; Krittanai, C. Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection Proteomics 2007, 7 (19) 3592-601
    • (2007) Proteomics , vol.7 , Issue.19 , pp. 3592-601
    • Chongsatja, P.O.1    Bourchookarn, A.2    Lo, C.F.3    Thongboonkerd, V.4    Krittanai, C.5
  • 63
    • 41549087403 scopus 로고    scopus 로고
    • Proteomics analysis of host cells infected with infectious bursal disease virus
    • Zheng, X.; Hong, L.; Shi, L.; Guo, J.; Sun, Z.; Zhou, J. Proteomics analysis of host cells infected with infectious bursal disease virus Mol. Cell. Proteomics 2008, 7 (3) 612-25
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.3 , pp. 612-25
    • Zheng, X.1    Hong, L.2    Shi, L.3    Guo, J.4    Sun, Z.5    Zhou, J.6
  • 65
    • 50849093525 scopus 로고    scopus 로고
    • Vimentin is required for dengue virus serotype 2 infection but microtubules are not necessary for this process
    • Chen, W.; Gao, N.; Wang, J. L.; Tian, Y. P.; Chen, Z. T.; An, J. Vimentin is required for dengue virus serotype 2 infection but microtubules are not necessary for this process Arch. Virol. 2008, 153 (9) 1777-81
    • (2008) Arch. Virol. , vol.153 , Issue.9 , pp. 1777-81
    • Chen, W.1    Gao, N.2    Wang, J.L.3    Tian, Y.P.4    Chen, Z.T.5    An, J.6
  • 66
    • 60649084936 scopus 로고    scopus 로고
    • AcMNPV EXON0 (AC141) which is required for the efficient egress of budded virus nucleocapsids interacts with beta-tubulin
    • Fang, M.; Nie, Y.; Theilmann, D. A. AcMNPV EXON0 (AC141) which is required for the efficient egress of budded virus nucleocapsids interacts with beta-tubulin Virology 2009, 385 (2) 496-504
    • (2009) Virology , vol.385 , Issue.2 , pp. 496-504
    • Fang, M.1    Nie, Y.2    Theilmann, D.A.3
  • 68
    • 0035203946 scopus 로고    scopus 로고
    • Induction of stress response renders human tumor cell lines resistant to curcumin-mediated apoptosis: Role of reactive oxygen intermediates
    • Khar, A.; Ali, A. M.; Pardhasaradhi, B. V.; Varalakshmi, C. H.; Anjum, R.; Kumari, A. L. Induction of stress response renders human tumor cell lines resistant to curcumin-mediated apoptosis: role of reactive oxygen intermediates Cell Stress Chaperones 2001, 6 (4) 368-76
    • (2001) Cell Stress Chaperones , vol.6 , Issue.4 , pp. 368-76
    • Khar, A.1    Ali, A.M.2    Pardhasaradhi, B.V.3    Varalakshmi, C.H.4    Anjum, R.5    Kumari, A.L.6
  • 69
    • 18744416943 scopus 로고    scopus 로고
    • Heat shock protein 90 expression in Epstein-Barr virus-infected B cells promotes gammadelta T-cell proliferation in vitro
    • Kotsiopriftis, M.; Tanner, J. E.; Alfieri, C. Heat shock protein 90 expression in Epstein-Barr virus-infected B cells promotes gammadelta T-cell proliferation in vitro J. Virol. 2005, 79 (11) 7255-61
    • (2005) J. Virol. , vol.79 , Issue.11 , pp. 7255-61
    • Kotsiopriftis, M.1    Tanner, J.E.2    Alfieri, C.3
  • 70
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • Srivastava, P. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses Annu. Rev. Immunol. 2002, 20, 395-425
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 71
    • 0034004805 scopus 로고    scopus 로고
    • Heat shock proteins, tumor immunogenicity and antigen presentation: An integrated view
    • Wells, A. D.; Malkovsky, M. Heat shock proteins, tumor immunogenicity and antigen presentation: an integrated view Immunol. Today 2000, 21 (3) 129-32
    • (2000) Immunol. Today , vol.21 , Issue.3 , pp. 129-32
    • Wells, A.D.1    Malkovsky, M.2


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