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Volumn 83, Issue 12, 2002, Pages 3055-3066

Role of G protein and protein kinase signalling in influenza virus budding in MDCK cells

Author keywords

[No Author keywords available]

Indexed keywords

3 [8 [(DIMETHYLAMINO)METHYL] 6,7,8,9 TETRAHYDROPYRIDO[1,2 A]INDOL 10 YL] 4 (1 METHYL 1H INDOL 3 YL) 1H PYRROLE 2,5 DIONE; 5,6 DICHLOROBENZIMIDAZOLE RIBOSIDE; 8 BROMO CYCLIC AMP; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; ALUMINUM FLUORIDE; CASEIN KINASE II; COMPOUND 48-80; CYCLIC AMP DEPENDENT PROTEIN KINASE; DIGITONIN; FLUORIDE SODIUM; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANYLYLIMIDODIPHOSPHATE; LYSOPHOSPHATIDYLCHOLINE; MASTOPARAN; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE; PROTEIN KINASE C; SURAMIN; WORTMANNIN;

EID: 0036937194     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/0022-1317-83-12-3055     Document Type: Review
Times cited : (39)

References (73)
  • 1
    • 0028909420 scopus 로고
    • Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation
    • Allende, J. E. & Allende, C. C. (1995). Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB Journal 9, 313-323.
    • (1995) FASEB Journal , vol.9 , pp. 313-323
    • Allende, J.E.1    Allende, C.C.2
  • 2
    • 0020323968 scopus 로고
    • Phosphorylation of the nucleoprotein of an avian influenza virus
    • Almond, J. W. & Felsenreich, V. (1982). Phosphorylation of the nucleoprotein of an avian influenza virus. Journal of General Virology 60, 295-305.
    • (1982) Journal of General Virology , vol.60 , pp. 295-305
    • Almond, J.W.1    Felsenreich, V.2
  • 3
    • 0032561327 scopus 로고    scopus 로고
    • Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues
    • Arni, S., Keilbaugh, S. A., Ostermeyer, A. G. & Brown, D. A. (1998). Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues. Journal of Biological Chemistry 273, 28478-28485.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 28478-28485
    • Arni, S.1    Keilbaugh, S.A.2    Ostermeyer, A.G.3    Brown, D.A.4
  • 4
    • 0030966390 scopus 로고    scopus 로고
    • Association of influenza virus NP and M1 proteins with cytoskeletal elements in influenza virus-infected cells
    • Avalos, R. T., Zhang, Y. & Nayak, D. P. (1997). Association of influenza virus NP and M1 proteins with cytoskeletal elements in influenza virus-infected cells. Journal of Virology 71, 2947-2958.
    • (1997) Journal of Virology , vol.71 , pp. 2947-2958
    • Avalos, R.T.1    Zhang, Y.2    Nayak, D.P.3
  • 5
    • 0033934725 scopus 로고    scopus 로고
    • Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association
    • Barman, S. & Nayak, D. P. (2000). Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association. Journal of Virology 74, 6538-6545.
    • (2000) Journal of Virology , vol.74 , pp. 6538-6545
    • Barman, S.1    Nayak, D.P.2
  • 6
    • 0034939645 scopus 로고    scopus 로고
    • Transport of viral proteins to the apical membranes and interaction of matrix proteins with glycoproteins in the assembly of influenza viruses
    • Barman, S., Ali, A., Hui, E. K.-W., Adhikary, L. & Nayak, D. P. (2001). Transport of viral proteins to the apical membranes and interaction of matrix proteins with glycoproteins in the assembly of influenza viruses. Virus Research 77, 61-69.
    • (2001) Virus Research , vol.77 , pp. 61-69
    • Barman, S.1    Ali, A.2    Hui, E.K.-W.3    Adhikary, L.4    Nayak, D.P.5
  • 8
    • 0022367326 scopus 로고
    • Fluoroaluminates activate transducin-GDP by mimicking the γ-phosphate of GTP in its binding site
    • Bigay, J., Deterre, P., Pfister, C. & Chabre, M. (1985). Fluoroaluminates activate transducin-GDP by mimicking the γ-phosphate of GTP in its binding site. FEBS Letters 191, 181-185.
    • (1985) FEBS Letters , vol.191 , pp. 181-185
    • Bigay, J.1    Deterre, P.2    Pfister, C.3    Chabre, M.4
  • 9
    • 0028900381 scopus 로고
    • Polarized exocytosis in MDCK cells is regulated by phosphorylation
    • Brewer, C. B. & Roth, M. G. (1995). Polarized exocytosis in MDCK cells is regulated by phosphorylation. Journal of Cell Science 108, 789-796.
    • (1995) Journal of Cell Science , vol.108 , pp. 789-796
    • Brewer, C.B.1    Roth, M.G.2
  • 10
    • 0033946767 scopus 로고    scopus 로고
    • The role of influenza virus M1 in nuclear export of viral RNPs
    • Bui, M., Wills, E., Helenius, A. & Whittaker, G. R. (2000). The role of influenza virus M1 in nuclear export of viral RNPs. Journal of Virology 74, 1781-1786.
    • (2000) Journal of Virology , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.2    Helenius, A.3    Whittaker, G.R.4
  • 11
    • 0035827264 scopus 로고    scopus 로고
    • Endocytosis and signaling cascades: A close encounter
    • Cavalli, V., Corti, M. & Gruenberg, J. (2001). Endocytosis and signaling cascades: a close encounter. FEBS Letters 498, 190-196.
    • (2001) FEBS Letters , vol.498 , pp. 190-196
    • Cavalli, V.1    Corti, M.2    Gruenberg, J.3
  • 12
    • 0034011765 scopus 로고    scopus 로고
    • Regulation of signal transduction by endocytosis
    • Ceresa, B. P. & Schmid, S. L. (2000). Regulation of signal transduction by endocytosis. Current Opinion in Cell Biology 12, 204-210.
    • (2000) Current Opinion in Cell Biology , vol.12 , pp. 204-210
    • Ceresa, B.P.1    Schmid, S.L.2
  • 14
    • 0021981584 scopus 로고
    • Role of guanine nucleotide regulatory binding proteins in the activation of polyphosphoinositide phosphodiesterase
    • Cockcroft, S. & Gomperts, B. D. (1985). Role of guanine nucleotide regulatory binding proteins in the activation of polyphosphoinositide phosphodiesterase. Nature 314, 534-536.
    • (1985) Nature , vol.314 , pp. 534-536
    • Cockcroft, S.1    Gomperts, B.D.2
  • 15
    • 0027185578 scopus 로고
    • Circular ruffle formation and closure lead to macropinocytosis in hepatocyte growth factor/scatter factor treated cells
    • Dowrick, P., Kenworthy, P., McCann, B. & Warn, R. (1993). Circular ruffle formation and closure lead to macropinocytosis in hepatocyte growth factor/scatter factor treated cells. European Journal of Cell Biology 61, 44-53.
    • (1993) European Journal of Cell Biology , vol.61 , pp. 44-53
    • Dowrick, P.1    Kenworthy, P.2    McCann, B.3    Warn, R.4
  • 16
    • 0028241862 scopus 로고
    • Selective regulation of apical endocytosis in polarized Madin-Darby canine kidney cells by mastoparan and cAMP
    • Eker, P., Holm, P. K., van Deurs, B. & Sandvig, K. (1994). Selective regulation of apical endocytosis in polarized Madin-Darby canine kidney cells by mastoparan and cAMP. Journal of Biological Chemistry 269, 18607-18615.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 18607-18615
    • Eker, P.1    Holm, P.K.2    van Deurs, B.3    Sandvig, K.4
  • 17
    • 0028151902 scopus 로고
    • Permeabilization of MDCK cells with cholesterol binding agents: Dependence on substratum and confluency
    • Esparís-Ogando, A., Zurzolo, C. & Rodriguez-Boulan, E. (1994). Permeabilization of MDCK cells with cholesterol binding agents: dependence on substratum and confluency. American Journal of Physiology 267, C166-C176.
    • (1994) American Journal of Physiology , vol.267
    • Esparís-Ogando, A.1    Zurzolo, C.2    Rodriguez-Boulan, E.3
  • 18
    • 0033837291 scopus 로고    scopus 로고
    • Subcellular localization of protein kinase CK2: A key to its function?
    • Faust, M. & Montenarh, M. (2000). Subcellular localization of protein kinase CK2: a key to its function? Cell and Tissue Research 301, 329-340.
    • (2000) Cell and Tissue Research , vol.301 , pp. 329-340
    • Faust, M.1    Montenarh, M.2
  • 19
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed, E. O. (2002). Viral late domains. Journal of Virology 76, 4679-4687.
    • (2002) Journal of Virology , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 21
    • 0026211749 scopus 로고
    • 2+ mobilization and prostacyclin synthesis in cultured human endothelium: Further evidence for regulation by a pertussis toxin-insensitive guanine nucleotide-binding protein
    • 2+ mobilization and prostacyclin synthesis in cultured human endothelium: further evidence for regulation by a pertussis toxin-insensitive guanine nucleotide-binding protein. American Journal of Respiratory Cell and Molecular Biology 5, 113-124.
    • (1991) American Journal of Respiratory Cell and Molecular Biology , vol.5 , pp. 113-124
    • Garcia, J.G.N.1    Dominguez, J.2    English, D.3
  • 22
    • 0035043282 scopus 로고    scopus 로고
    • Global impact of influenza virus on cellular pathways is mediated by both replication-dependent and -independent events
    • Geiss, G. K., An, M. C., Bumgarner, R. E., Hammersmark, E., Cunningham, D. & Katze, M. G. (2001). Global impact of influenza virus on cellular pathways is mediated by both replication-dependent and -independent events. Journal of Virology 75, 4321-4331.
    • (2001) Journal of Virology , vol.75 , pp. 4321-4331
    • Geiss, G.K.1    An, M.C.2    Bumgarner, R.E.3    Hammersmark, E.4    Cunningham, D.5    Katze, M.G.6
  • 25
    • 0025308076 scopus 로고
    • The phosphorylation of the integral membrane (M1) protein of influenza virus
    • Gregoriades, A., Guzman, G. G. & Paoletti, E. (1990). The phosphorylation of the integral membrane (M1) protein of influenza virus. Virus Research 16, 27-41.
    • (1990) Virus Research , vol.16 , pp. 27-41
    • Gregoriades, A.1    Guzman, G.G.2    Paoletti, E.3
  • 26
    • 0028167863 scopus 로고
    • Gsα stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A
    • Hansen, S. H. & Casanova, J. E. (1994). Gsα stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A. Journal of Cell Biology 126, 677-687.
    • (1994) Journal of Cell Biology , vol.126 , pp. 677-687
    • Hansen, S.H.1    Casanova, J.E.2
  • 27
    • 0012359643 scopus 로고    scopus 로고
    • Signal transduction pathways through heterotrimeric G proteins: Transmission of hormonal and sensory signals
    • Edited by E. J. M. Helmreich. Oxford: Oxford University Press
    • Helmreich, E. J. M. (2001). Signal transduction pathways through heterotrimeric G proteins: transmission of hormonal and sensory signals. In The Biochemistry of Cell Signalling, pp. 76-101. Edited by E. J. M. Helmreich. Oxford: Oxford University Press.
    • (2001) The Biochemistry of Cell Signalling , pp. 76-101
    • Helmreich, E.J.M.1
  • 30
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototope in its regulatory domain
    • House, C. & Kemp, B. E. (1987). Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science 238, 1726-1728.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 31
    • 0026353470 scopus 로고
    • Purification and analysis of protein kinase C isozymes
    • Huang, K.-P. & Huang, F. L. (1991). Purification and analysis of protein kinase C isozymes. Methods in Enzymology 200, 241-252.
    • (1991) Methods in Enzymology , vol.200 , pp. 241-252
    • Huang, K.-P.1    Huang, F.L.2
  • 33
    • 0035950932 scopus 로고    scopus 로고
    • Role of ATP in influenza virus budding
    • Hui, E. K.-W. & Nayak, D. P. (2001). Role of ATP in influenza virus budding. Virology 290, 329-341.
    • (2001) Virology , vol.290 , pp. 329-341
    • Hui, E.K.-W.1    Nayak, D.P.2
  • 34
    • 0026652035 scopus 로고
    • Protein kinase C activity during sphinganine potentiation of retinoic acid-induced differentiation in a human leukemia cell line (HL-60)
    • Hui, E. K.-W. & Yung, B. Y.-M. (1992). Protein kinase C activity during sphinganine potentiation of retinoic acid-induced differentiation in a human leukemia cell line (HL-60). Life Sciences 51, 415-422.
    • (1992) Life Sciences , vol.51 , pp. 415-422
    • Hui, E.K.-W.1    Yung, B.Y.-M.2
  • 35
    • 0029894049 scopus 로고    scopus 로고
    • Analysis of the role of p200-containing vesicles in post-Golgi traffic
    • Ikonen, E., Parton, R. G., Lafont, F. & Simons, K. (1996). Analysis of the role of p200-containing vesicles in post-Golgi traffic. Molecular Biology of the Cell 7, 961-974.
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 961-974
    • Ikonen, E.1    Parton, R.G.2    Lafont, F.3    Simons, K.4
  • 36
    • 0021924118 scopus 로고
    • Phosphopeptide fingerprints of nucleoproteins of various influenza A virus strains grown in different host cells
    • Kistner, O., Muller, H., Becht, H. & Scholtissek, C. (1985). Phosphopeptide fingerprints of nucleoproteins of various influenza A virus strains grown in different host cells. Journal of General Virology 66, 465-472.
    • (1985) Journal of General Virology , vol.66 , pp. 465-472
    • Kistner, O.1    Muller, H.2    Becht, H.3    Scholtissek, C.4
  • 37
    • 0024445913 scopus 로고
    • Differential phosphorylation of the nucleoprotein of influenza A viruses
    • Kistner, O., Muller, K. & Scholtissek, C. (1989). Differential phosphorylation of the nucleoprotein of influenza A viruses. Journal of General Virology 70, 2421-2431.
    • (1989) Journal of General Virology , vol.70 , pp. 2421-2431
    • Kistner, O.1    Muller, K.2    Scholtissek, C.3
  • 38
    • 0026070152 scopus 로고
    • Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/rac
    • Koch, G., Haberman, B., Mohr, C., Just, I. & Aktories, K. (1991). Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/rac. FEBS Letters 291, 336-340.
    • (1991) FEBS Letters , vol.291 , pp. 336-340
    • Koch, G.1    Haberman, B.2    Mohr, C.3    Just, I.4    Aktories, K.5
  • 39
    • 0025179326 scopus 로고
    • Inhibitory effect of protein kinase C inhibitor on the replication of influenza type A virus
    • Kurokawa, M., Ochiai, H., Nakajima, K. & Niwayama, S. (1990). Inhibitory effect of protein kinase C inhibitor on the replication of influenza type A virus. Journal of General Virology 71, 2149-2155.
    • (1990) Journal of General Virology , vol.71 , pp. 2149-2155
    • Kurokawa, M.1    Ochiai, H.2    Nakajima, K.3    Niwayama, S.4
  • 40
    • 0034972583 scopus 로고    scopus 로고
    • Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
    • Latham, T. & Galarza, J. M. (2001). Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. Journal of Virology 75, 6154-6165.
    • (2001) Journal of Virology , vol.75 , pp. 6154-6165
    • Latham, T.1    Galarza, J.M.2
  • 41
    • 0035658016 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus: The getaway driver nabbed
    • Luban, J. (2001). HIV-1 and Ebola virus: the getaway driver nabbed. Nature Medicine 7, 1278-1280.
    • (2001) Nature Medicine , vol.7 , pp. 1278-1280
    • Luban, J.1
  • 42
    • 0032828271 scopus 로고    scopus 로고
    • A fatal relationship - Influenza virus interactions with the host cell
    • Ludwig, S., Pleschka, S. & Wolff, T. (1999). A fatal relationship - influenza virus interactions with the host cell. Viral Immunology 12, 175-196.
    • (1999) Viral Immunology , vol.12 , pp. 175-196
    • Ludwig, S.1    Pleschka, S.2    Wolff, T.3
  • 43
    • 0028357354 scopus 로고
    • Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinase-1 and -2
    • Marin, O., Meggio, F. & Pinna, L. A. (1994). Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinase-1 and -2. Biochemical and Biophysical Research Communication 198, 898-905.
    • (1994) Biochemical and Biophysical Research Communication , vol.198 , pp. 898-905
    • Marin, O.1    Meggio, F.2    Pinna, L.A.3
  • 44
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin, K. & Helenius, A. (1991). Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67, 117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 46
    • 0025190182 scopus 로고
    • Direct activation of GTP-binding regulatory proteins (G-proteins) by substance P and compound 48/80
    • Mousli, M., Bronner, C., Landry, Y., Bockaert, J. & Rouot, B. (1990). Direct activation of GTP-binding regulatory proteins (G-proteins) by substance P and compound 48/80. FEBS Letters 259, 260-262.
    • (1990) FEBS Letters , vol.259 , pp. 260-262
    • Mousli, M.1    Bronner, C.2    Landry, Y.3    Bockaert, J.4    Rouot, B.5
  • 47
    • 0000756591 scopus 로고    scopus 로고
    • A look at assembly and morphogenesis of orthomyxo- and paramyxoviruses
    • Nayak, D. P. (1996). A look at assembly and morphogenesis of orthomyxo- and paramyxoviruses. ASM News 62, 411-414.
    • (1996) ASM News , vol.62 , pp. 411-414
    • Nayak, D.P.1
  • 48
    • 0002738750 scopus 로고    scopus 로고
    • Virus morphology, replication and assembly
    • Edited by C. J. Hurst. London: Academic Press
    • Nayak, D. P. (2000). Virus morphology, replication and assembly. In Viral Ecology, pp. 64-123. Edited by C. J. Hurst. London: Academic Press.
    • (2000) Viral Ecology , pp. 64-123
    • Nayak, D.P.1
  • 49
    • 0036045120 scopus 로고    scopus 로고
    • Role of lipid rafts in virus assembly and budding
    • Nayak, D. P. & Barman, S. (2002). Role of lipid rafts in virus assembly and budding. Advances in Virus Research 58, 1-28.
    • (2002) Advances in Virus Research , vol.58 , pp. 1-28
    • Nayak, D.P.1    Barman, S.2
  • 51
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann, G., Castrucci, M. R. & Kawaoka, Y. (1997). Nuclear import and export of influenza virus nucleoprotein. Journal of Virology 71, 9690-9700.
    • (1997) Journal of Virology , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 53
    • 0012462323 scopus 로고    scopus 로고
    • Role of the protein kinase C gene family in the regulation of cell function
    • Edited by M. J. Clemens. New York & London: Harwood Academic Publishers
    • Pears, C. J. (1996). Role of the protein kinase C gene family in the regulation of cell function. In Protein Phosphorylation in Cell Growth Regulation, pp. 111-133. Edited by M. J. Clemens. New York & London: Harwood Academic Publishers.
    • (1996) Protein Phosphorylation in Cell Growth Regulation , pp. 111-133
    • Pears, C.J.1
  • 54
    • 0033976989 scopus 로고    scopus 로고
    • The replication activity of influenza virus polymerase is linked to the capacity of the PA subunit to induce proteolysis
    • Perales, B., Sanz-Ezquerro, S., Gastaminza, P., Ortega, J., Santarén, J. F., Ortín, J. & Nieto, A. (2000). The replication activity of influenza virus polymerase is linked to the capacity of the PA subunit to induce proteolysis. Journal of Virology 74, 1307-1312.
    • (2000) Journal of Virology , vol.74 , pp. 1307-1312
    • Perales, B.1    Sanz-Ezquerro, S.2    Gastaminza, P.3    Ortega, J.4    Santarén J., F.5    Ortín, J.6    Nieto, A.7
  • 55
    • 0026780629 scopus 로고
    • Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1
    • Perich, J. W., Meggio, M., Reynolds, E. C., Marin, O. & Pinna, L. A. (1992). Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1. Biochemistry 31, 5893-5897.
    • (1992) Biochemistry , vol.31 , pp. 5893-5897
    • Perich, J.W.1    Meggio, M.2    Reynolds, E.C.3    Marin, O.4    Pinna, L.A.5
  • 56
    • 0019775198 scopus 로고
    • Phosphorylation of influenza virus nucleoprotein in vivo
    • Petri, T. & Dimmock, N. J. (1981). Phosphorylation of influenza virus nucleoprotein in vivo. Journal of General Virology 57, 185-190.
    • (1981) Journal of General Virology , vol.57 , pp. 185-190
    • Petri, T.1    Dimmock, N.J.2
  • 57
  • 58
    • 0027401264 scopus 로고
    • S class of heterotrimeric G protein
    • S class of heterotrimeric G protein. Nature 362, 456-458.
    • (1993) Nature , vol.362 , pp. 456-458
    • Pimplikar, S.W.1    Simons, K.2
  • 59
    • 0028364351 scopus 로고
    • Basolateral protein transport in streptolysin O-permeabilized MDCK cells
    • Pimplikar, S. W., Ikonen, E. & Simons, K. (1994). Basolateral protein transport in streptolysin O-permeabilized MDCK cells. Journal of Cell Biology 125, 1025-1035.
    • (1994) Journal of Cell Biology , vol.125 , pp. 1025-1035
    • Pimplikar, S.W.1    Ikonen, E.2    Simons, K.3
  • 60
  • 61
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: A multifunctional RNA-binding protein pivotal to virus replication
    • Portela, A. & Digard, P. (2002). The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication. Journal of General Virology 83, 723-734.
    • (2002) Journal of General Virology , vol.83 , pp. 723-734
    • Portela, A.1    Digard, P.2
  • 62
    • 0034702018 scopus 로고    scopus 로고
    • The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C
    • Reinhardt, J. & Wolff, T. (2000). The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. Veterinary Microbiology 74, 87-100.
    • (2000) Veterinary Microbiology , vol.74 , pp. 87-100
    • Reinhardt, J.1    Wolff, T.2
  • 63
    • 0025924358 scopus 로고
    • 2 protein of influenza virus is found in purified virus and phosphorylated in infected cells
    • 2 protein of influenza virus is found in purified virus and phosphorylated in infected cells. Archives of Virology 116, 69-80.
    • (1991) Archives of Virology , vol.116 , pp. 69-80
    • Richardson, J.C.1    Akkina, R.K.2
  • 64
    • 12044259376 scopus 로고
    • Membrane ruffling and signal transduction
    • Ridley, A. J. (1994). Membrane ruffling and signal transduction. BioEssays 16, 321-327.
    • (1994) BioEssays , vol.16 , pp. 321-327
    • Ridley, A.J.1
  • 65
    • 0035827310 scopus 로고    scopus 로고
    • Rho protein, PI 3-kinase and monocyte/macrophage motility
    • Ridley, A. J. (2001). Rho protein, PI 3-kinase and monocyte/macrophage motility. FEBS Letters 498, 168-171.
    • (2001) FEBS Letters , vol.498 , pp. 168-171
    • Ridley, A.J.1
  • 66
    • 0033767394 scopus 로고    scopus 로고
    • Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor
    • Root, C. N., Wills, E. G., McNair, L. L. & Whittaker, G. R. (2000). Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor. Journal of General Virology 81, 2697-2705.
    • (2000) Journal of General Virology , vol.81 , pp. 2697-2705
    • Root, C.N.1    Wills, E.G.2    McNair, L.L.3    Whittaker, G.R.4
  • 68
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., Rietveld, A., Wilk, T. & Simons, K. (1999). Influenza viruses select ordered lipid domains during budding from the plasma membrane. Journal of Biological Chemistry 274, 2038-2044.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 69
    • 0012398482 scopus 로고
    • GTP-binding proteins in plant
    • Edited by M. Zerial & L. A. Huber. Oxford: Oxford University Press
    • Terry, N., van Montagu, M. & Inze, D. (1995). GTP-binding proteins in plant. In Guidebook to Small GTPase, pp. 32-38. Edited by M. Zerial & L. A. Huber. Oxford: Oxford University Press.
    • (1995) Guidebook to Small GTPase , pp. 32-38
    • Terry, N.1    van Montagu, M.2    Inze, D.3
  • 70
    • 0026027812 scopus 로고
    • Characterisation of the influenza virus associated protein kinase and its resemblance to casein kinase II
    • Tucker, S. P., Penn, C. R. & McCauley, J. W. (1990). Characterisation of the influenza virus associated protein kinase and its resemblance to casein kinase II. Virus Research 18, 243-262.
    • (1990) Virus Research , vol.18 , pp. 243-262
    • Tucker, S.P.1    Penn, C.R.2    McCauley, J.W.3
  • 71
    • 0028321980 scopus 로고
    • Influenza A virus late mRNAs are specifically retained in the nucleus in the presence of a methyltransferase or a protein kinase inhibitor
    • Vogel, U., Kunerl, M. & Scholtissek, C. (1994). Influenza A virus late mRNAs are specifically retained in the nucleus in the presence of a methyltransferase or a protein kinase inhibitor. Virology 198, 227-233.
    • (1994) Virology , vol.198 , pp. 227-233
    • Vogel, U.1    Kunerl, M.2    Scholtissek, C.3
  • 72
    • 0028240355 scopus 로고
    • Sphinganine potentiation of dimethyl sulfoxide-induced granulocytic differentiation, increase of alkaline phosphatase activity and decrease of protein kinase C activity in a human leukemia cell line (HL-60)
    • Yung, B. Y.-M., Hsiao, T.-F., Wei, L. L.-L. & Hui, E. K.-W. (1994). Sphinganine potentiation of dimethyl sulfoxide-induced granulocytic differentiation, increase of alkaline phosphatase activity and decrease of protein kinase C activity in a human leukemia cell line (HL-60). Biochemical and Biophysical Research Communications 199, 888-896.
    • (1994) Biochemical and Biophysical Research Communications , vol.199 , pp. 888-896
    • Yung, B.Y.-M.1    Hsiao, T.-F.2    Wei, L.L.-L.3    Hui, E.K.-W.4
  • 73
    • 0033995067 scopus 로고    scopus 로고
    • Influenza virus assembly and lipid raft microdomains: A role for the cytoplasmic tails of the spike glycoproteins
    • Zhang, J., Pekosz, A. & Lamb, R. A. (2000). Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins. Journal of Virology 74, 4635-4644.
    • (2000) Journal of Virology , vol.74 , pp. 4635-4644
    • Zhang, J.1    Pekosz, A.2    Lamb, R.A.3


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