메뉴 건너뛰기




Volumn 24, Issue 5, 2003, Pages 190-200

Quantitative multiplex real-time PCR for the sensitive detection of interferon β gene induction and viral suppression of interferon β expression

Author keywords

Coxsackievirus B3; Interferon beta; Multiplex PCR; Poly I:C transfection; Quantitative PCR

Indexed keywords

BETA INTERFERON; MESSENGER RNA; POLYCYTIDYLIC ACID; PORPHOBILINOGEN DEAMINASE;

EID: 0142164889     PISSN: 10434666     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cyto.2003.09.001     Document Type: Article
Times cited : (14)

References (49)
  • 1
    • 0034767753 scopus 로고    scopus 로고
    • Antiviral actions of interferons
    • Samuel C.E. Antiviral actions of interferons. Clin Microbiol Rev. 14:2001;778-809.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 778-809
    • Samuel, C.E.1
  • 2
    • 0034924802 scopus 로고    scopus 로고
    • Production of interferons and beta-chemokines by placental trophoblasts of HIV-1-infected women
    • Lee B.N., Hammill H., Popek E.J., Cron S., Kozinetz C., Paul M., et al. Production of interferons and beta-chemokines by placental trophoblasts of HIV-1-infected women. Infect Dis Obstet Gynecol. 9:2001;95-104.
    • (2001) Infect Dis Obstet Gynecol , vol.9 , pp. 95-104
    • Lee, B.N.1    Hammill, H.2    Popek, E.J.3    Cron, S.4    Kozinetz, C.5    Paul, M.6
  • 3
    • 0032078394 scopus 로고    scopus 로고
    • Highly sensitive detection of gene expression of an intronless gene: Amplification of mRNA, but not genomic DNA by nucleic acid sequence based amplification (NASBA)
    • Heim A., Grumbach I.M., Zeuke S., Top B. Highly sensitive detection of gene expression of an intronless gene: amplification of mRNA, but not genomic DNA by nucleic acid sequence based amplification (NASBA). Nucleic Acids Res. 26:1998;2250-2251.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2250-2251
    • Heim, A.1    Grumbach, I.M.2    Zeuke, S.3    Top, B.4
  • 4
    • 84981779372 scopus 로고
    • Zwischenmoleculare Energiewanderung und Fluoreszenz
    • Förster V.T. Zwischenmoleculare Energiewanderung und Fluoreszenz. Ann Phys (Leibzig). 1948;55-75.
    • (1948) Ann Phys (Leibzig) , pp. 55-75
    • Förster, V.T.1
  • 5
    • 0031022694 scopus 로고    scopus 로고
    • Continuous fluorescence monitoring of rapid cycle DNA amplification
    • 134-8
    • Wittwer C.T., Herrmann M.G., Moss A.A., Rasmussen R.P. Continuous fluorescence monitoring of rapid cycle DNA amplification. Biotechniques. 22:1997;130-131. 134-8.
    • (1997) Biotechniques , vol.22 , pp. 130-131
    • Wittwer, C.T.1    Herrmann, M.G.2    Moss, A.A.3    Rasmussen, R.P.4
  • 7
    • 0029881633 scopus 로고    scopus 로고
    • Recombinant interferons beta and gamma have a higher antiviral activity than interferon-alpha in coxsackievirus B3-infected carrier state cultures of human myocardial fibroblasts
    • Heim A., Stille-Seigener M., Pring-Akerblom P., Grumbach I., Brehm C., Kreuzer H., et al. Recombinant interferons beta and gamma have a higher antiviral activity than interferon-alpha in coxsackievirus B3-infected carrier state cultures of human myocardial fibroblasts. J Interferon Cytokine Res. 16:1996;283-287.
    • (1996) J Interferon Cytokine Res , vol.16 , pp. 283-287
    • Heim, A.1    Stille-Seigener, M.2    Pring-Akerblom, P.3    Grumbach, I.4    Brehm, C.5    Kreuzer, H.6
  • 8
    • 0027389221 scopus 로고
    • Degradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNA
    • Black T.L., Barber G.N., Katze M.G. Degradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNA. J Virol. 67:1993;791-800.
    • (1993) J Virol , vol.67 , pp. 791-800
    • Black, T.L.1    Barber, G.N.2    Katze, M.G.3
  • 9
    • 0024593159 scopus 로고
    • The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: Implications for translational regulation
    • Black T.L., Safer B., Hovanessian A., Katze M.G. The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation. J Virol. 63:1989;2244-2251.
    • (1989) J Virol , vol.63 , pp. 2244-2251
    • Black, T.L.1    Safer, B.2    Hovanessian, A.3    Katze, M.G.4
  • 10
    • 0034877005 scopus 로고    scopus 로고
    • Poliovirus 3A protein limits interleukin-6 (IL-6), IL-8, and beta interferon secretion during viral infection
    • Dodd D.A., Giddings T.H. Jr., Kirkegaard K. Poliovirus 3A protein limits interleukin-6 (IL-6), IL-8, and beta interferon secretion during viral infection. J Virol. 75:2001;8158-8165.
    • (2001) J Virol , vol.75 , pp. 8158-8165
    • Dodd, D.A.1    Giddings T.H., Jr.2    Kirkegaard, K.3
  • 11
    • 0030728931 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: Genetic and ultrastructural analysis
    • Doedens J.R., Giddings T.H. Jr., Kirkegaard K. Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J Virol. 71:1997;9054-9064.
    • (1997) J Virol , vol.71 , pp. 9054-9064
    • Doedens, J.R.1    Giddings T.H., Jr.2    Kirkegaard, K.3
  • 12
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex
    • Etchison D., Milburn S.C., Edery I., Sonenberg N., Hershey J.W. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J Biol Chem. 257:1982;14806-14810.
    • (1982) J Biol Chem , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 13
    • 0020045412 scopus 로고
    • Association of cap-binding protein with eucaryotic initiation factor 3 in initiation factor preparations from uninfected and poliovirus-infected HeLa cells
    • Hansen J., Etchison D., Hershey J.W., Ehrenfeld E. Association of cap-binding protein with eucaryotic initiation factor 3 in initiation factor preparations from uninfected and poliovirus-infected HeLa cells. J Virol. 42:1982;200-207.
    • (1982) J Virol , vol.42 , pp. 200-207
    • Hansen, J.1    Etchison, D.2    Hershey, J.W.3    Ehrenfeld, E.4
  • 14
    • 0032889314 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro
    • Joachims M., Van Breugel P.C., Lloyd R.E. Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro. J Virol. 73:1999;718-727.
    • (1999) J Virol , vol.73 , pp. 718-727
    • Joachims, M.1    Van Breugel, P.C.2    Lloyd, R.E.3
  • 15
    • 0034646863 scopus 로고    scopus 로고
    • Transient induction of cytokine production in human myocardial fibroblasts by coxsackievirus B3
    • Heim A., Zeuke S., Weiss S., Ruschewski W., Grumbach I.M. Transient induction of cytokine production in human myocardial fibroblasts by coxsackievirus B3. Circ Res. 86:2000;753-759.
    • (2000) Circ Res , vol.86 , pp. 753-759
    • Heim, A.1    Zeuke, S.2    Weiss, S.3    Ruschewski, W.4    Grumbach, I.M.5
  • 16
    • 0031840623 scopus 로고    scopus 로고
    • Quantitation of minimal residual disease in Philadelphia chromosome positive chronic myeloid leukaemia patients using real-time quantitative RT-PCR
    • Mensink E., van de Locht A., Schattenberg A., Linders E., Schaap N., Geurts van Kessel A., et al. Quantitation of minimal residual disease in Philadelphia chromosome positive chronic myeloid leukaemia patients using real-time quantitative RT-PCR. Br J Haematol. 102:1998;768-774.
    • (1998) Br J Haematol , vol.102 , pp. 768-774
    • Mensink, E.1    Van De Locht, A.2    Schattenberg, A.3    Linders, E.4    Schaap, N.5    Geurts Van Kessel, A.6
  • 17
    • 0002565608 scopus 로고    scopus 로고
    • Selection of hybridization probes for real-time quantification and genetic analysis
    • S. Meuer, C. Wittwer, & K. Nakagawara. Berlin, Heidelberg, New York: Springer-Verlag
    • Landt O. Selection of hybridization probes for real-time quantification and genetic analysis. Meuer S., Wittwer C., Nakagawara K. Rapid cycle real-time PCR: methods and applications. 2001;35-41 Springer-Verlag, Berlin, Heidelberg, New York.
    • (2001) Rapid cycle real-time PCR: Methods and applications , pp. 35-41
    • Landt, O.1
  • 18
    • 2442766122 scopus 로고    scopus 로고
    • Spreadsheet software for thermodynamic melting point prediction of oligonucleotide hybridization with and without mismatches
    • Schütz E., von Ahsen N. Spreadsheet software for thermodynamic melting point prediction of oligonucleotide hybridization with and without mismatches. Biotechniques. 27:1999;1218-1224.
    • (1999) Biotechniques , vol.27 , pp. 1218-1224
    • Schütz, E.1    Von Ahsen, N.2
  • 19
    • 0030585155 scopus 로고    scopus 로고
    • When two strands are better than one: The mediators and modulators of the cellular responses to double-stranded RNA
    • Jacobs B.L., Langland J.O. When two strands are better than one: the mediators and modulators of the cellular responses to double-stranded RNA. Virology. 219:1996;339-349.
    • (1996) Virology , vol.219 , pp. 339-349
    • Jacobs, B.L.1    Langland, J.O.2
  • 20
    • 0029051672 scopus 로고
    • Involvement of the double-stranded-RNA-dependent kinase PKR in interferon expression and interferon-mediated antiviral activity
    • Der S.D., Lau A.S. Involvement of the double-stranded-RNA-dependent kinase PKR in interferon expression and interferon-mediated antiviral activity. Proc Natl Acad Sci U S A. 92:1995;8841-8845.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8841-8845
    • Der, S.D.1    Lau, A.S.2
  • 21
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR: Structure and function
    • Clemens M.J., Elia A. The double-stranded RNA-dependent protein kinase PKR: structure and function. J Interferon Cytokine Res. 17:1997;503-524.
    • (1997) J Interferon Cytokine Res , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 22
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B
    • Kumar A., Haque J., Lacoste J., Hiscott J., Williams B.R. Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B. Proc Natl Acad Sci U S A. 91:1994;6288-6292.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6288-6292
    • Kumar, A.1    Haque, J.2    Lacoste, J.3    Hiscott, J.4    Williams, B.R.5
  • 23
    • 0034082457 scopus 로고    scopus 로고
    • PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex
    • Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F. PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex. Mol Cell Biol. 20:2000;4532-4542.
    • (2000) Mol Cell Biol , vol.20 , pp. 4532-4542
    • Bonnet, M.C.1    Weil, R.2    Dam, E.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 24
    • 0025361887 scopus 로고
    • Interaction of adenovirus VA RNAl with the protein kinase DAI: Nonequivalence of binding and function
    • Mellits K.H., Kostura M., Mathews M.B. Interaction of adenovirus VA RNAl with the protein kinase DAI: nonequivalence of binding and function. Cell. 61:1990;843-852.
    • (1990) Cell , vol.61 , pp. 843-852
    • Mellits, K.H.1    Kostura, M.2    Mathews, M.B.3
  • 25
    • 0025931571 scopus 로고
    • Adenovirus virus-associated RNA and translation control
    • Mathews M.B., Shenk T. Adenovirus virus-associated RNA and translation control. J Virol. 65:1991;5657-5662.
    • (1991) J Virol , vol.65 , pp. 5657-5662
    • Mathews, M.B.1    Shenk, T.2
  • 26
    • 0029910938 scopus 로고    scopus 로고
    • Regulation of the double-stranded RNA-dependent protein kinase PKR by RNAs encoded by a repeated sequence in the Epstein-Barr virus genome
    • Elia A., Laing K.G., Schofield A., Tilleray V.J., Clemens M.J. Regulation of the double-stranded RNA-dependent protein kinase PKR by RNAs encoded by a repeated sequence in the Epstein-Barr virus genome. Nucleic Acids Res. 24:1996;4471-4478.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4471-4478
    • Elia, A.1    Laing, K.G.2    Schofield, A.3    Tilleray, V.J.4    Clemens, M.J.5
  • 27
    • 0036302036 scopus 로고    scopus 로고
    • Interferon regulatory factor-1, interferon-beta, and reovirus-induced myocarditis
    • Azzam-Smoak K., Noah D.L., Stewart M.J., Blum M.A., Sherry B. Interferon regulatory factor-1, interferon-beta, and reovirus-induced myocarditis. Virology. 298:2002;20-29.
    • (2002) Virology , vol.298 , pp. 20-29
    • Azzam-Smoak, K.1    Noah, D.L.2    Stewart, M.J.3    Blum, M.A.4    Sherry, B.5
  • 28
    • 0031893220 scopus 로고    scopus 로고
    • Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation
    • Lin R., Heylbroeck C., Pitha P.M., Hiscott J. Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation. Mol Cell Biol. 18:1998;2986-2996.
    • (1998) Mol Cell Biol , vol.18 , pp. 2986-2996
    • Lin, R.1    Heylbroeck, C.2    Pitha, P.M.3    Hiscott, J.4
  • 29
    • 0032579369 scopus 로고    scopus 로고
    • Regulation of type I interferon gene expression by interferon regulatory factor-3
    • Schafer S.L., Lin R., Moore P.A., Hiscott J., Pitha P.M. Regulation of type I interferon gene expression by interferon regulatory factor-3. J Biol Chem. 273:1998;2714-2720.
    • (1998) J Biol Chem , vol.273 , pp. 2714-2720
    • Schafer, S.L.1    Lin, R.2    Moore, P.A.3    Hiscott, J.4    Pitha, P.M.5
  • 30
    • 0032481352 scopus 로고    scopus 로고
    • Direct triggering of the type I interferon system by virus infection: Activation of a transcription factor complex containing IRF-3 and CBP/p300
    • Yoneyama M., Suhara W., Fukuhara Y., Fukuda M., Nishida E., Fujita T. Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF-3 and CBP/p300. EMBO J. 17:1998;1087-1095.
    • (1998) EMBO J , vol.17 , pp. 1087-1095
    • Yoneyama, M.1    Suhara, W.2    Fukuhara, Y.3    Fukuda, M.4    Nishida, E.5    Fujita, T.6
  • 31
    • 0033257795 scopus 로고    scopus 로고
    • JNK2 and IKKbeta are required for activating the innate response to viral infection
    • Chu W.M., Ostertag D., Li Z.W., Chang L., Chen Y., Hu Y., et al. JNK2 and IKKbeta are required for activating the innate response to viral infection. Immunity. 11:1999;721-731.
    • (1999) Immunity , vol.11 , pp. 721-731
    • Chu, W.M.1    Ostertag, D.2    Li, Z.W.3    Chang, L.4    Chen, Y.5    Hu, Y.6
  • 32
    • 0034629279 scopus 로고    scopus 로고
    • Inactivation of interferon regulatory factor-1 tumor suppressor protein by HPV E7 oncoprotein. Implication for the E7-mediated immune evasion mechanism in cervical carcinogenesis
    • Park J.S., Kim E.J., Kwon H.J., Hwang E.S., Namkoong S.E., Um S.J. Inactivation of interferon regulatory factor-1 tumor suppressor protein by HPV E7 oncoprotein. Implication for the E7-mediated immune evasion mechanism in cervical carcinogenesis. J Biol Chem. 275:2000;6764-6769.
    • (2000) J Biol Chem , vol.275 , pp. 6764-6769
    • Park, J.S.1    Kim, E.J.2    Kwon, H.J.3    Hwang, E.S.4    Namkoong, S.E.5    Um, S.J.6
  • 34
    • 0036838725 scopus 로고    scopus 로고
    • The influenza A virus NS1 protein inhibits activation of Jun N-terminal kinase and AP-1 transcription factors
    • Ludwig S., Wang X., Ehrhardt C., Zheng H., Donelan N., Planz O., et al. The influenza A virus NS1 protein inhibits activation of Jun N-terminal kinase and AP-1 transcription factors. J Virol. 76:2002;11166-11171.
    • (2002) J Virol , vol.76 , pp. 11166-11171
    • Ludwig, S.1    Wang, X.2    Ehrhardt, C.3    Zheng, H.4    Donelan, N.5    Planz, O.6
  • 35
    • 0033870894 scopus 로고    scopus 로고
    • Activation of interferon regulatory factor 3 is inhibited by the influenza A virus NS1 protein
    • Talon J., Horvath C.M., Polley R., Basler C.F., Muster T., Palese P., et al. Activation of interferon regulatory factor 3 is inhibited by the influenza A virus NS1 protein. J Virol. 74:2000;7989-7996.
    • (2000) J Virol , vol.74 , pp. 7989-7996
    • Talon, J.1    Horvath, C.M.2    Polley, R.3    Basler, C.F.4    Muster, T.5    Palese, P.6
  • 36
    • 0032128003 scopus 로고    scopus 로고
    • Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity
    • Ronco L.V., Karpova A.Y., Vidal M., Howley P.M. Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity. Genes Dev. 12:1998;2061-2072.
    • (1998) Genes Dev , vol.12 , pp. 2061-2072
    • Ronco, L.V.1    Karpova, A.Y.2    Vidal, M.3    Howley, P.M.4
  • 37
    • 0034127011 scopus 로고    scopus 로고
    • Translation of NRF mRNA is mediated by highly efficient internal ribosome entry
    • Oumard A., Hennecke M., Hauser H., Nourbakhsh M. Translation of NRF mRNA is mediated by highly efficient internal ribosome entry. Mol Cell Biol. 20:2000;2755-2759.
    • (2000) Mol Cell Biol , vol.20 , pp. 2755-2759
    • Oumard, A.1    Hennecke, M.2    Hauser, H.3    Nourbakhsh, M.4
  • 38
    • 0027399391 scopus 로고
    • An improved strategy and a useful housekeeping gene for RNA analysis from formalin-fixed, paraffin-embedded tissues by PCR
    • Finke J., Fritzen R., Ternes P., Lange W., Dolken G. An improved strategy and a useful housekeeping gene for RNA analysis from formalin-fixed, paraffin-embedded tissues by PCR. Biotechniques. 14:1993;448-453.
    • (1993) Biotechniques , vol.14 , pp. 448-453
    • Finke, J.1    Fritzen, R.2    Ternes, P.3    Lange, W.4    Dolken, G.5
  • 39
    • 0023713201 scopus 로고    scopus 로고
    • Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression
    • Chretien S., Dubart A., Beaupain D., Raich N., Grandchamp B., Rosa J., et al. Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. Proc Natl Acad Sci U S A. 85:1998;6-10.
    • (1998) Proc Natl Acad Sci U S A , vol.85 , pp. 6-10
    • Chretien, S.1    Dubart, A.2    Beaupain, D.3    Raich, N.4    Grandchamp, B.5    Rosa, J.6
  • 40
    • 0036130355 scopus 로고    scopus 로고
    • Quantitative analysis of beta-actin, beta-2-microglobulin and porphobilinogen deaminase mRNA and their comparison as control transcripts for RT-PCR
    • doi: 10.1006/mcpr.2001.0392
    • Lupberger J., Kreuzer K.A., Baskaynak G., Peters U.R., le Coutre P., Schmidt C.A. Quantitative analysis of beta-actin, beta-2-microglobulin and porphobilinogen deaminase mRNA and their comparison as control transcripts for RT-PCR. Mol Cell Probes. 16:2002;25-30. [doi: 10.1006/mcpr.2001.0392].
    • (2002) Mol Cell Probes , vol.16 , pp. 25-30
    • Lupberger, J.1    Kreuzer, K.A.2    Baskaynak, G.3    Peters, U.R.4    Le Coutre, P.5    Schmidt, C.A.6
  • 41
    • 0020490012 scopus 로고
    • The human fibroblast and human immune interferon genes and their expression in homologous and heterologous cells
    • Fiers W., Remaut E., Devos R., Cheroutre H., Contreras R., Gheysen D., et al. The human fibroblast and human immune interferon genes and their expression in homologous and heterologous cells. Philos Trans R Soc Lond B Biol Sci. 299:1982;29-38.
    • (1982) Philos Trans R Soc Lond B Biol Sci , vol.299 , pp. 29-38
    • Fiers, W.1    Remaut, E.2    Devos, R.3    Cheroutre, H.4    Contreras, R.5    Gheysen, D.6
  • 42
    • 0015486829 scopus 로고
    • Production of high-titered interferon in cultures of human diploid cells
    • Havell E.A., Vilcek J. Production of high-titered interferon in cultures of human diploid cells. Antimicrob Agents Chemother. 2:1972;476-484.
    • (1972) Antimicrob Agents Chemother , vol.2 , pp. 476-484
    • Havell, E.A.1    Vilcek, J.2
  • 43
    • 0011279512 scopus 로고
    • Tfx-50 reagent: A new transfection reagent for eucaryotic cells
    • Schenborn E. Tfx-50 reagent: a new transfection reagent for eucaryotic cells. Promega Notes. 52:1995;2.
    • (1995) Promega Notes , vol.52 , pp. 2
    • Schenborn, E.1
  • 44
    • 0031698256 scopus 로고    scopus 로고
    • Induction of interferon synthesis and activation of interferon- stimulated genes by liposomal transfection reagents
    • Li X.L., Boyanapalli M., Weihua X., Kalvakolanu D.V., Hassel B.A. Induction of interferon synthesis and activation of interferon-stimulated genes by liposomal transfection reagents. J Interferon Cytokine Res. 18:1998;947-952.
    • (1998) J Interferon Cytokine Res , vol.18 , pp. 947-952
    • Li, X.L.1    Boyanapalli, M.2    Weihua, X.3    Kalvakolanu, D.V.4    Hassel, B.A.5
  • 45
    • 0035881553 scopus 로고    scopus 로고
    • Characterization of human myocardial fibroblasts immortalized by HPV16 E6-E7 genes
    • doi: 10.1006/excr.2001.5274
    • Harms W., Rothamel T., Miller K., Harste G., Grassmann M., Heim A. Characterization of human myocardial fibroblasts immortalized by HPV16 E6-E7 genes. Exp Cell Res. 268:2001;252-261. [doi: 10.1006/excr.2001.5274 ].
    • (2001) Exp Cell Res , vol.268 , pp. 252-261
    • Harms, W.1    Rothamel, T.2    Miller, K.3    Harste, G.4    Grassmann, M.5    Heim, A.6
  • 46
    • 0034665215 scopus 로고    scopus 로고
    • Attachment of coxsackievirus B3 variants to various cell lines: Mapping of phenotypic differences to capsid protein VP1
    • doi: 10.1006/viro.2000.0485
    • Schmidtke M., Selinka H.C., Heim A., Jahn B., Tonew M., Kandolf R., et al. Attachment of coxsackievirus B3 variants to various cell lines: mapping of phenotypic differences to capsid protein VP1. Virology. 275:2000;77-88. [doi: 10.1006/viro.2000.0485].
    • (2000) Virology , vol.275 , pp. 77-88
    • Schmidtke, M.1    Selinka, H.C.2    Heim, A.3    Jahn, B.4    Tonew, M.5    Kandolf, R.6
  • 47
    • 0028848531 scopus 로고
    • Cultured human myocardial fibroblasts of pediatric origin: Natural human interferon-alpha is more effective than recombinant interferon- alpha 2a in carrier-state coxsackievirus B3 replication
    • Heim A., Brehm C., Stille-Siegener M., Muller G., Hake S., Kandolf R., et al. Cultured human myocardial fibroblasts of pediatric origin: natural human interferon-alpha is more effective than recombinant interferon- alpha 2a in carrier-state coxsackievirus B3 replication. J Mol Cell Cardiol. 27:1995;2199-2208.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 2199-2208
    • Heim, A.1    Brehm, C.2    Stille-Siegener, M.3    Muller, G.4    Hake, S.5    Kandolf, R.6
  • 49
    • 0031568919 scopus 로고    scopus 로고
    • Product differentiation by analysis of DNA melting curves during the polymerase chain reaction
    • Ririe K.M., Rasmussen R.P., Wittwer C.T. Product differentiation by analysis of DNA melting curves during the polymerase chain reaction. Anal Biochem. 245:1997;154-160.
    • (1997) Anal Biochem , vol.245 , pp. 154-160
    • Ririe, K.M.1    Rasmussen, R.P.2    Wittwer, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.