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Volumn 5, Issue MAY, 2014, Pages

Wheat germ cell-free system-based production of hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 for generation and characterization of monoclonal antibody

Author keywords

Cell free protein synthesis; Human parainfluenza virus 3; Monoclonal antibody; Proteomics

Indexed keywords

HN PROTEIN; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 84905060629     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00208     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0034715352 scopus 로고    scopus 로고
    • Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein
    • doi: 10.1006/viro.2000.0556
    • Ali, A., and Nayak, D. P. (2000). Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein. Virology 276, 289-303. doi: 10.1006/viro.2000.0556.
    • (2000) Virology , vol.276 , pp. 289-303
    • Ali, A.1    Nayak, D.P.2
  • 2
    • 44249091413 scopus 로고    scopus 로고
    • Serpins (serine protease inhibitors)
    • Chap. 21, Unit 21.7, doi: 10.1002/0471140864.ps2107s26
    • Bauman, S. J., Whinna, H. C., and Church, F. C. (2002). Serpins (serine protease inhibitors). Curr. Protoc. Protein Sci. Chap. 21, Unit 21.7. doi: 10.1002/0471140864.ps2107s26.
    • (2002) Curr. Protoc. Protein Sci.
    • Bauman, S.J.1    Whinna, H.C.2    Church, F.C.3
  • 3
    • 84866940758 scopus 로고    scopus 로고
    • Genome sequencing phylogenetic analysis of 39 human parainfluenza virus type 1 strains isolated from 1997-2010.
    • doi: 10.1371/journal.pone.0046048
    • Beck, E. T., He, J., Nelson, M. I., Bose, M. E., Fan, J., Kumar, S., et al. (2012). Genome sequencing and phylogenetic analysis of 39 human parainfluenza virus type 1 strains isolated from 1997-2010. PLoS ONE 7:e46048. doi: 10.1371/journal.pone.0046048.
    • (2012) PLoS ONE , vol.7
    • Beck, E.T.1    He, J.2    Nelson, M.I.3    Bose, M.E.4    Fan, J.5    Kumar, S.6
  • 4
    • 84877595007 scopus 로고    scopus 로고
    • Role of N-linked glycosylation of the human parainfluenza virus type 3 hemagglutinin-neuraminidase protein
    • doi: 10.1016/j.virusres.2013.03.012
    • Chu, F. L., Wen, H. L., Hou, G. H., Lin, B., Zhang, W. Q., Song, Y. Y., et al. (2013). Role of N-linked glycosylation of the human parainfluenza virus type 3 hemagglutinin-neuraminidase protein. Virus Res. 174, 137-147. doi: 10.1016/j.virusres.2013.03.012.
    • (2013) Virus Res. , vol.174 , pp. 137-147
    • Chu, F.L.1    Wen, H.L.2    Hou, G.H.3    Lin, B.4    Zhang, W.Q.5    Song, Y.Y.6
  • 5
    • 0034934133 scopus 로고    scopus 로고
    • Human parainfluenza virus-associated hospitalizations among children less than five years of age in the United States
    • doi: 10.1097/00006454-200107000-00003
    • Counihan, M. E., Shay, D. K., Holman, R. C., Lowther, S. A., and Anderson, L. J. (2001). Human parainfluenza virus-associated hospitalizations among children less than five years of age in the United States. Pediatr. Infect. Dis. J. 20, 646-653. doi: 10.1097/00006454-200107000-00003.
    • (2001) Pediatr. Infect. Dis. J. , vol.20 , pp. 646-653
    • Counihan, M.E.1    Shay, D.K.2    Holman, R.C.3    Lowther, S.A.4    Anderson, L.J.5
  • 6
    • 33644814737 scopus 로고    scopus 로고
    • Advances in genome-wide protein expression using the wheat germ cell-free system
    • doi: 10.1007/978-1-59259-948-6_11
    • Endo, Y., and Sawasaki, T. (2005). Advances in genome-wide protein expression using the wheat germ cell-free system. Methods Mol. Biol. 310, 145-167. doi: 10.1007/978-1-59259-948-6_11.
    • (2005) Methods Mol. Biol. , vol.310 , pp. 145-167
    • Endo, Y.1    Sawasaki, T.2
  • 7
    • 33746695331 scopus 로고    scopus 로고
    • Cell-free expression systems for eukaryotic protein production
    • doi: 10.1016/j.copbio.2006.06.009
    • Endo, Y., and Sawasaki, T. (2006). Cell-free expression systems for eukaryotic protein production. Curr. Opin. Biotechnol. 17, 373-380. doi: 10.1016/j.copbio.2006.06.009.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 373-380
    • Endo, Y.1    Sawasaki, T.2
  • 8
    • 0021710556 scopus 로고
    • Parainfluenza virus type 3: seasonality and risk of infection and reinfection in young children
    • doi: 10.1093/infdis/150.6.851
    • Glezen, W. P., Frank, A. L., Taber, L. H., and Kasel, J. A. (1984). Parainfluenza virus type 3: seasonality and risk of infection and reinfection in young children. J. Infect. Dis. 150, 851-857. doi: 10.1093/infdis/150.6.851.
    • (1984) J. Infect. Dis. , vol.150 , pp. 851-857
    • Glezen, W.P.1    Frank, A.L.2    Taber, L.H.3    Kasel, J.A.4
  • 9
    • 0020966735 scopus 로고
    • Monoclonal antibodies against human paramyxovirus type 3 and against SV5 virus: preparation and preliminary characterization
    • doi: 10.1099/0022-1317-64-8-1663
    • Goswami, K. K., and Russell, W. C. (1983). Monoclonal antibodies against human paramyxovirus type 3 and against SV5 virus: preparation and preliminary characterization. J. Gen. Virol. 64, 1663-1672. doi: 10.1099/0022-1317-64-8-1663.
    • (1983) J. Gen. Virol. , vol.64 , pp. 1663-1672
    • Goswami, K.K.1    Russell, W.C.2
  • 10
    • 0026637939 scopus 로고
    • Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia
    • Horvath, C. M., Paterson, R. G., Shaughnessy, M. A., Wood, R., and Lamb, R. A. (1992). Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia. J. Virol. 66, 4564-4569..
    • (1992) J. Virol. , vol.66 , pp. 4564-4569
    • Horvath, C.M.1    Paterson, R.G.2    Shaughnessy, M.A.3    Wood, R.4    Lamb, R.A.5
  • 11
    • 0026525004 scopus 로고
    • Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses
    • Hu, X. L., Ray, R., and Compans, R. W. (1992). Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses. J. Virol. 66, 1528-1534..
    • (1992) J. Virol. , vol.66 , pp. 1528-1534
    • Hu, X.L.1    Ray, R.2    Compans, R.W.3
  • 12
    • 0028884662 scopus 로고
    • Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle
    • doi: 10.1006/viro.1995.9925
    • Huberman, K., Peluso, R. W., and Moscona, A. (1995). Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle. Virology 214, 294-300. doi: 10.1006/viro.1995.9925.
    • (1995) Virology , vol.214 , pp. 294-300
    • Huberman, K.1    Peluso, R.W.2    Moscona, A.3
  • 13
    • 0029788697 scopus 로고    scopus 로고
    • Analysis of M phase-specific phosphorylation of DNA topoisomerase II
    • doi: 10.1074/jbc.271.35.21439
    • Kimura, K., Nozaki, N., Enomoto, T., Tanaka, M., and Kikuchi, A. (1996). Analysis of M phase-specific phosphorylation of DNA topoisomerase II. J. Biol. Chem. 271, 21439-21445. doi: 10.1074/jbc.271.35.21439.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21439-21445
    • Kimura, K.1    Nozaki, N.2    Enomoto, T.3    Tanaka, M.4    Kikuchi, A.5
  • 14
    • 0028043440 scopus 로고
    • Identification of the nature of modification that causes the shift of DNA topoisomerase II beta to apparent higher molecular weight forms in the M phase
    • Kimura, K., Nozaki, N., Saijo, M., Kikuchi, A., Ui, M., and Enomoto, T. (1994). Identification of the nature of modification that causes the shift of DNA topoisomerase II beta to apparent higher molecular weight forms in the M phase. J. Biol. Chem. 269, 24523-24526..
    • (1994) J. Biol. Chem. , vol.269 , pp. 24523-24526
    • Kimura, K.1    Nozaki, N.2    Saijo, M.3    Kikuchi, A.4    Ui, M.5    Enomoto, T.6
  • 15
    • 84861302576 scopus 로고    scopus 로고
    • Hsp70 protein positively regulates rabies virus infection
    • doi: 10.1128/JVI.06501-11
    • Lahaye, X., Vidy, A., Fouquet, B., and Blondel, D. (2012). Hsp70 protein positively regulates rabies virus infection. J. Virol. 86, 4743-4751. doi: 10.1128/JVI.06501-11.
    • (2012) J. Virol. , vol.86 , pp. 4743-4751
    • Lahaye, X.1    Vidy, A.2    Fouquet, B.3    Blondel, D.4
  • 16
    • 67749104678 scopus 로고    scopus 로고
    • Functional characterization of Negri bodies (NBs) in rabies virus-infected cells: evidence that NBs are sites of viral transcription and replication
    • doi: 10.1128/JVI.00554-09
    • Lahaye, X., Vidy, A., Pomier, C., Obiang, L., Harper, F., Gaudin, Y., et al. (2009). Functional characterization of Negri bodies (NBs) in rabies virus-infected cells: evidence that NBs are sites of viral transcription and replication. J. Virol. 83, 7948-7958. doi: 10.1128/JVI.00554-09.
    • (2009) J. Virol. , vol.83 , pp. 7948-7958
    • Lahaye, X.1    Vidy, A.2    Pomier, C.3    Obiang, L.4    Harper, F.5    Gaudin, Y.6
  • 17
    • 79952076763 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo.
    • doi: 10.1371/journal.pone.0016546
    • Li, G., Zhang, J., Tong, X., Liu, W., and Ye, X. (2011). Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo. PLoS ONE 6:e16546. doi: 10.1371/journal.pone.0016546.
    • (2011) PLoS ONE , vol.6
    • Li, G.1    Zhang, J.2    Tong, X.3    Liu, W.4    Ye, X.5
  • 18
    • 16444378781 scopus 로고    scopus 로고
    • Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies
    • doi: 10.1007/s10254-004-0025-5
    • Mayer, M. P. (2005). Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev. Physiol. Biochem. Pharmacol. 153, 1-46. doi: 10.1007/s10254-004-0025-5.
    • (2005) Rev. Physiol. Biochem. Pharmacol. , vol.153 , pp. 1-46
    • Mayer, M.P.1
  • 19
    • 0022353374 scopus 로고
    • Molecular cloning of a full-length cDNA encoding the hemagglutinin-neuraminidase glycoprotein of Sendai virus
    • doi: 10.1016/0014-5793(85)80885-1
    • Miura, N., Nakatani, Y., Ishiura, M., Uchida, T., and Okada, Y. (1985). Molecular cloning of a full-length cDNA encoding the hemagglutinin-neuraminidase glycoprotein of Sendai virus. FEBS Lett. 188, 112-116. doi: 10.1016/0014-5793(85)80885-1.
    • (1985) FEBS Lett. , vol.188 , pp. 112-116
    • Miura, N.1    Nakatani, Y.2    Ishiura, M.3    Uchida, T.4    Okada, Y.5
  • 20
    • 84878164106 scopus 로고    scopus 로고
    • Genotyping of mumps virus detected in Yokohama City from 1999 to 2010
    • doi: 10.7883/yoken.66.226
    • Momoki, T. S. (2013). Genotyping of mumps virus detected in Yokohama City from 1999 to 2010. Jpn. J. Infect. Dis. 66, 226-231. doi: 10.7883/yoken.66.226.
    • (2013) Jpn. J. Infect. Dis. , vol.66 , pp. 226-231
    • Momoki, T.S.1
  • 21
    • 0034909749 scopus 로고    scopus 로고
    • Human parainfluenza virus type 3 HN-receptor interaction: effect of 4-guanidino-Neu5Ac2en on a neuraminidase-deficient variant
    • doi: 10.1128/JVI.75.16.7481-7488.2001
    • Porotto, M., Greengard, O., Poltoratskaia, N., Horga, M. A., and Moscona, A. (2001). Human parainfluenza virus type 3 HN-receptor interaction: effect of 4-guanidino-Neu5Ac2en on a neuraminidase-deficient variant. J. Virol. 75, 7481-7488. doi: 10.1128/JVI.75.16.7481-7488.2001.
    • (2001) J. Virol. , vol.75 , pp. 7481-7488
    • Porotto, M.1    Greengard, O.2    Poltoratskaia, N.3    Horga, M.A.4    Moscona, A.5
  • 22
    • 84855272388 scopus 로고    scopus 로고
    • Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry
    • doi: 10.1074/jbc.M111.298059
    • Porotto, M., Palmer, S. G., Palermo, L. M., and Moscona, A. (2012). Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry. J. Biol. Chem. 287, 778-793. doi: 10.1074/jbc.M111.298059.
    • (2012) J. Biol. Chem. , vol.287 , pp. 778-793
    • Porotto, M.1    Palmer, S.G.2    Palermo, L.M.3    Moscona, A.4
  • 23
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B., and Toft, D. O. (2003). Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228, 111-133..
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 24
    • 0022542843 scopus 로고
    • Characterization of four parainfluenza virus type 3 proteins by use of monoclonal antibodies
    • doi: 10.1099/0022-1317-67-8-1531
    • Rydbeck, R., Orvell, C., Love, A., and Norrby, E. (1986). Characterization of four parainfluenza virus type 3 proteins by use of monoclonal antibodies. J. Gen. Virol. 67, 1531-1542. doi: 10.1099/0022-1317-67-8-1531.
    • (1986) J. Gen. Virol. , vol.67 , pp. 1531-1542
    • Rydbeck, R.1    Orvell, C.2    Love, A.3    Norrby, E.4
  • 25
    • 38049057933 scopus 로고    scopus 로고
    • Arabidopsis HY5 protein functions as a DNA-binding tag for purification and functional immobilization of proteins on agarose/DNA microplate
    • doi: 10.1016/j.febslet.2007.12.004
    • Sawasaki, T., Kamura, N., Matsunaga, S., Saeki, M., Tsuchimochi, M., Morishita, R., et al. (2008). Arabidopsis HY5 protein functions as a DNA-binding tag for purification and functional immobilization of proteins on agarose/DNA microplate. FEBS Lett. 582, 221-228. doi: 10.1016/j.febslet.2007.12.004.
    • (2008) FEBS Lett. , vol.582 , pp. 221-228
    • Sawasaki, T.1    Kamura, N.2    Matsunaga, S.3    Saeki, M.4    Tsuchimochi, M.5    Morishita, R.6
  • 26
    • 84858955425 scopus 로고    scopus 로고
    • Regulation of survival gene hsp70
    • doi: 10.1007/s12192-011-0290-6
    • Silver, J. T., and Noble, E. G. (2012). Regulation of survival gene hsp70. Cell Stress Chaperones 17, 1-9. doi: 10.1007/s12192-011-0290-6.
    • (2012) Cell Stress Chaperones , vol.17 , pp. 1-9
    • Silver, J.T.1    Noble, E.G.2
  • 27
    • 78650911572 scopus 로고    scopus 로고
    • A nonredundant role for mouse Serpinb3a in the induction of mucus production in asthma
    • doi: 10.1016/j.jaci.2010.10.009
    • Sivaprasad, U., Askew, D. J., Ericksen, M. B., Gibson, A. M., Stier, M. T., Brandt, E. B., et al. (2011). A nonredundant role for mouse Serpinb3a in the induction of mucus production in asthma. J. Allergy Clin. Immunol. 127, 254-261. doi: 10.1016/j.jaci.2010.10.009.
    • (2011) J. Allergy Clin. Immunol. , vol.127 , pp. 254-261
    • Sivaprasad, U.1    Askew, D.J.2    Ericksen, M.B.3    Gibson, A.M.4    Stier, M.T.5    Brandt, E.B.6
  • 28
    • 0037213262 scopus 로고    scopus 로고
    • The genome length of human parainfluenza virus type 2 follows the rule of six, and recombinant viruses recovered from non-polyhexameric-length antigenomic cDNAs contain a biased distribution of correcting mutations
    • doi: 10.1128/JVI.77.1.270-279.2003
    • Skiadopoulos, M. H., Vogel, L., Riggs, J. M., Surman, S. R., Collins, P. L., and Murphy, B. R. (2003). The genome length of human parainfluenza virus type 2 follows the rule of six, and recombinant viruses recovered from non-polyhexameric-length antigenomic cDNAs contain a biased distribution of correcting mutations. J. Virol. 77, 270-279. doi: 10.1128/JVI.77.1.270-279.2003.
    • (2003) J. Virol. , vol.77 , pp. 270-279
    • Skiadopoulos, M.H.1    Vogel, L.2    Riggs, J.M.3    Surman, S.R.4    Collins, P.L.5    Murphy, B.R.6
  • 29
    • 84876080333 scopus 로고    scopus 로고
    • Critical role of the fusion protein cytoplasmic tail sequence in parainfluenza virus assembly.
    • doi: 10.1371/journal.pone.0061281
    • Stone, R., and Takimoto, T. (2013). Critical role of the fusion protein cytoplasmic tail sequence in parainfluenza virus assembly. PLoS ONE 8:e61281. doi: 10.1371/journal.pone.0061281.
    • (2013) PLoS ONE , vol.8
    • Stone, R.1    Takimoto, T.2
  • 30
    • 0021686786 scopus 로고
    • Structural characterization of virion proteins and genomic RNA of human parainfluenza virus 3
    • Storey, D. G., Dimock, K., and Kang, C. Y. (1984). Structural characterization of virion proteins and genomic RNA of human parainfluenza virus 3. J. Virol. 52, 761-766..
    • (1984) J. Virol. , vol.52 , pp. 761-766
    • Storey, D.G.1    Dimock, K.2    Kang, C.Y.3
  • 31
    • 84869137921 scopus 로고    scopus 로고
    • Establishment of a robust dengue virus NS3-NS5 binding assay for identification of protein-protein interaction inhibitors
    • doi: 10.1016/j.antiviral.2012.09.023
    • Takahashi, H., Takahashi, C., Moreland, N. J., Chang, Y. T., Sawasaki, T., Ryo, A., et al. (2012). Establishment of a robust dengue virus NS3-NS5 binding assay for identification of protein-protein interaction inhibitors. Antiviral Res. 96, 305-314. doi: 10.1016/j.antiviral.2012.09.023.
    • (2012) Antiviral Res. , vol.96 , pp. 305-314
    • Takahashi, H.1    Takahashi, C.2    Moreland, N.J.3    Chang, Y.T.4    Sawasaki, T.5    Ryo, A.6
  • 32
    • 77952758035 scopus 로고    scopus 로고
    • The cell-free protein synthesis system from wheat germ
    • doi: 10.1007/978-1-60327-331-2_3
    • Takai, K., and Endo, Y. (2010). The cell-free protein synthesis system from wheat germ. Methods Mol. Biol. 607, 23-30. doi: 10.1007/978-1-60327-331-2_3.
    • (2010) Methods Mol. Biol. , vol.607 , pp. 23-30
    • Takai, K.1    Endo, Y.2
  • 33
    • 77950908515 scopus 로고    scopus 로고
    • The wheat-germ cell-free expression system
    • doi: 10.2174/138920110791111933
    • Takai, K., Sawasaki, T., and Endo, Y. (2010). The wheat-germ cell-free expression system. Curr. Pharm. Biotechnol. 11, 272-278. doi: 10.2174/138920110791111933.
    • (2010) Curr. Pharm. Biotechnol. , vol.11 , pp. 272-278
    • Takai, K.1    Sawasaki, T.2    Endo, Y.3
  • 34
    • 0036891868 scopus 로고    scopus 로고
    • Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion
    • doi: 10.1128/JVI.76.24.13028-13033.2002
    • Takimoto, T., Taylor, G. L., Connaris, H. C., Crennell, S. J., and Portner, A. (2002). Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion. J. Virol. 76, 13028-13033. doi: 10.1128/JVI.76.24.13028-13033.2002.
    • (2002) J. Virol. , vol.76 , pp. 13028-13033
    • Takimoto, T.1    Taylor, G.L.2    Connaris, H.C.3    Crennell, S.J.4    Portner, A.5
  • 35
    • 0021931934 scopus 로고
    • Protection of mice from wild-type Sendai virus infection by a trypsin-resistant mutant, TR-2
    • Tashiro, M., and Homma, M. (1985). Protection of mice from wild-type Sendai virus infection by a trypsin-resistant mutant, TR-2. J. Virol. 53, 228-234..
    • (1985) J. Virol. , vol.53 , pp. 228-234
    • Tashiro, M.1    Homma, M.2
  • 36
    • 0021838299 scopus 로고
    • Antigenic variation in the hemagglutinin-neuraminidase protein of human parainfluenza type 3 virus
    • doi: 10.1016/0042-6822(85)90395-2
    • van Wyke Coelingh, K. L., Winter, C., and Murphy, B. R. (1985). Antigenic variation in the hemagglutinin-neuraminidase protein of human parainfluenza type 3 virus. Virology 143, 569-582. doi: 10.1016/0042-6822(85)90395-2.
    • (1985) Virology , vol.143 , pp. 569-582
    • van Wyke Coelingh, K.L.1    Winter, C.2    Murphy, B.R.3
  • 37
    • 0021948192 scopus 로고
    • Production of monoclonal antibodies against parainfluenza 3 virus and their use in diagnosis by immunofluorescence
    • Waner, J. L., Whitehurst, N. J., Downs, T., and Graves, D. G. (1985). Production of monoclonal antibodies against parainfluenza 3 virus and their use in diagnosis by immunofluorescence. J. Clin. Microbiol. 22, 535-538..
    • (1985) J. Clin. Microbiol. , vol.22 , pp. 535-538
    • Waner, J.L.1    Whitehurst, N.J.2    Downs, T.3    Graves, D.G.4
  • 38
    • 0022341707 scopus 로고
    • Human parainfluenza virus 3: purification and characterization of subviral components, viral proteins and viral RNA
    • doi: 10.1016/0168-1702(85)90434-4
    • Wechsler, S. L., Lambert, D. M., Galinski, M. S., Heineke, B. E., and Pons, M. W. (1985). Human parainfluenza virus 3: purification and characterization of subviral components, viral proteins and viral RNA. Virus Res. 3, 339-351. doi: 10.1016/0168-1702(85)90434-4.
    • (1985) Virus Res. , vol.3 , pp. 339-351
    • Wechsler, S.L.1    Lambert, D.M.2    Galinski, M.S.3    Heineke, B.E.4    Pons, M.W.5
  • 39
    • 64149119175 scopus 로고    scopus 로고
    • Parainfluenza virus infection of young children: estimates of the population-based burden of hospitalization
    • doi: 10.1016/j.jpeds.2008.11.034
    • Weinberg, G. A., Hall, C. B., Iwane, M. K., Poehling, K. A., Edwards, K. M., Griffin, M. R., et al. (2009). Parainfluenza virus infection of young children: estimates of the population-based burden of hospitalization. J. Pediatr. 154, 694-699. doi: 10.1016/j.jpeds.2008.11.034.
    • (2009) J. Pediatr. , vol.154 , pp. 694-699
    • Weinberg, G.A.1    Hall, C.B.2    Iwane, M.K.3    Poehling, K.A.4    Edwards, K.M.5    Griffin, M.R.6
  • 40
    • 77953442031 scopus 로고    scopus 로고
    • HSP70 induced by Hantavirus infection interacts with viral nucleocapsid protein and its overexpression suppresses virus infection in Vero E6 cells
    • Yu, L., Ye, L., Zhao, R., Liu, Y.F., and Yang, S.J. (2009). HSP70 induced by Hantavirus infection interacts with viral nucleocapsid protein and its overexpression suppresses virus infection in Vero E6 cells. Am. J. Transl. Res. 1, 367-380.
    • (2009) Am. J. Transl. Res. , vol.1 , pp. 367-380
    • Yu, L.1    Ye, L.2    Zhao, R.3    Liu, Y.F.4    Yang, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.