메뉴 건너뛰기




Volumn 52, Issue 1, 2003, Pages 17-34

Monoclonal antibodies to elongation factor-1α inhibit in vitro translation in lysates of Sf21 cells

Author keywords

Elongation factor 1 ; Monoclonal antibodies; Protein translation; Spodoptera frugiperda

Indexed keywords

INSECTA; LEPIDOPTERA; SPODOPTERA; SPODOPTERA FRUGIPERDA;

EID: 0037208830     PISSN: 07394462     EISSN: None     Source Type: Journal    
DOI: 10.1002/arch.10061     Document Type: Article
Times cited : (4)

References (60)
  • 1
    • 0026750776 scopus 로고
    • Prolongation of skin allograft survival in mice by didemnin B
    • Alfrey EJ, Zukoski CF, Montgomery DW. 1992. Prolongation of skin allograft survival in mice by didemnin B. Transplantation 54:188-189.
    • (1992) Transplantation , vol.54 , pp. 188-189
    • Alfrey, E.J.1    Zukoski, C.F.2    Montgomery, D.W.3
  • 2
    • 0030044484 scopus 로고    scopus 로고
    • Inhibition of signaling from Type 1 receptor tyrosine kinases via intracellular expression of single-chain antibodies
    • Beerli RR, Wels W, Hynes NE. 1996. Inhibition of signaling from Type 1 receptor tyrosine kinases via intracellular expression of single-chain antibodies. Breast Cancer Res Treat 38:11-17.
    • (1996) Breast Cancer Res Treat , vol.38 , pp. 11-17
    • Beerli, R.R.1    Wels, W.2    Hynes, N.E.3
  • 3
    • 0018330752 scopus 로고
    • 35S]methionine for studying the biosynthesis of the polypeptides of mouse liver endoplasmic reticulum membrane fractions in vivo
    • 35S]methionine for studying the biosynthesis of the polypeptides of mouse liver endoplasmic reticulum membrane fractions in vivo. Can J Biochem 57:625-638.
    • (1979) Can J Biochem , vol.57 , pp. 625-638
    • Behar-Bannelier, M.1    Sharma, R.N.2    Murray, R.K.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0343035661 scopus 로고    scopus 로고
    • A TNF receptor antagonistic scFv, which is not secreted in mammalian cells, is expressed as a soluble mono- and bivalent scFv derivative in insect cells
    • Brocks B, Rode HJ, Klein M, Gerlach E, Dubel S, Little M, Pfizenmaier K, Moosmayer D. 1997. A TNF receptor antagonistic scFv, which is not secreted in mammalian cells, is expressed as a soluble mono- and bivalent scFv derivative in insect cells. Immunotechnology 3:173-184.
    • (1997) Immunotechnology , vol.3 , pp. 173-184
    • Brocks, B.1    Rode, H.J.2    Klein, M.3    Gerlach, E.4    Dubel, S.5    Little, M.6    Pfizenmaier, K.7    Moosmayer, D.8
  • 7
    • 2342472276 scopus 로고    scopus 로고
    • Affinity measurements by band shift and competition ELISA
    • Kontermann, R, Dübel S, editors. New York: Springer-Verlag
    • Bumke MA, Neri D. 2001. Affinity measurements by band shift and competition ELISA. In: Kontermann, R, Dübel S, editors. Antibody engineering. New York: Springer-Verlag. p 395-396.
    • (2001) Antibody Engineering , pp. 395-396
    • Bumke, M.A.1    Neri, D.2
  • 8
    • 0006050973 scopus 로고
    • Monoclonal antibody technology: The production and characterization of rodent and human hybridomas
    • Burdon RH, van Knippenberg PH, editors. New York: Elsevier Science Publishing Company, Inc.
    • Campbell AM. 1984. Monoclonal antibody technology: the production and characterization of rodent and human hybridomas. In: Burdon RH, van Knippenberg PH, editors. Laboratory techniques in biochemistry and molecular biology, vol. 13. New York: Elsevier Science Publishing Company, Inc. p 158-160.
    • (1984) Laboratory Techniques in Biochemistry and Molecular Biology , vol.13 , pp. 158-160
    • Campbell, A.M.1
  • 9
    • 0029027331 scopus 로고
    • A highly conserved nuclear gene for low-level phylogenetics: Elongation factor-1α recovers morphology-based tree for heliothine moths
    • Cho S, Mitchell A, Regier JC, Mitter C, Poole RW, Friedlander TP, Zhao S. 1995. A highly conserved nuclear gene for low-level phylogenetics: elongation factor-1α recovers morphology-based tree for heliothine moths. Mol Biol Evol 12:650-656.
    • (1995) Mol Biol Evol , vol.12 , pp. 650-656
    • Cho, S.1    Mitchell, A.2    Regier, J.C.3    Mitter, C.4    Poole, R.W.5    Friedlander, T.P.6    Zhao, S.7
  • 11
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland DW, Stuart GF, Kirschner MW, Laemmli UK. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem 252:1102-1106.
    • (1977) J Biol Chem , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Stuart, G.F.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 12
    • 0034988595 scopus 로고    scopus 로고
    • Vaccine- and hepatitis B immune globulin-induced escape mutations of hepatitis B virus surface antigen
    • Cooreman MP, Leroux-Roels G, Paulij WP. 2001. Vaccine- and hepatitis B immune globulin-induced escape mutations of hepatitis B virus surface antigen. J Biomed Sci 8:237-247.
    • (2001) J Biomed Sci , vol.8 , pp. 237-247
    • Cooreman, M.P.1    Leroux-Roels, G.2    Paulij, W.P.3
  • 13
    • 0028300782 scopus 로고
    • GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1α
    • Crews CM, Collins JL, Lane WS, Snapper ML, Schreiber SL. 1994. GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1α. J Biol Chem 269:15411-15414.
    • (1994) J Biol Chem , vol.269 , pp. 15411-15414
    • Crews, C.M.1    Collins, J.L.2    Lane, W.S.3    Snapper, M.L.4    Schreiber, S.L.5
  • 14
    • 0031941350 scopus 로고    scopus 로고
    • Elongation factor-1α occurs as two copies in bees: Implications for phylogenetic analysis of EF-1α sequences in insects
    • Danforth BN, Ji S. 1998. Elongation factor-1α occurs as two copies in bees: implications for phylogenetic analysis of EF-1α sequences in insects. Mol Biol Evol 15:225-235.
    • (1998) Mol Biol Evol , vol.15 , pp. 225-235
    • Danforth, B.N.1    Ji, S.2
  • 15
    • 0026012460 scopus 로고
    • Two forms of elongations factor 1α (EF1αO and 42Sp50), present in oocytes, but absent in somatic cells of Xenopus laevis
    • Deschamps S, Morales J, Mazabraud AA, le Maire M, Denis H, Brown DD. 1991. Two forms of elongations factor 1α (EF1αO and 42Sp50), present in oocytes, but absent in somatic cells of Xenopus laevis. J Cell Biol 114:1109-1111.
    • (1991) J Cell Biol , vol.114 , pp. 1109-1111
    • Deschamps, S.1    Morales, J.2    Mazabraud, A.A.3    Le Maire, M.4    Denis, H.5    Brown, D.D.6
  • 16
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphoryl- Ethanolamine
    • Dever TE, Costello CE, Owens CL, Rosenberry TL, Merrick WC. 1989. Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphoryl- ethanolamine. J Biol Chem 264:20518-20525.
    • (1989) J Biol Chem , vol.264 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.E.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 17
    • 0026320055 scopus 로고
    • Compartmentalization and actin binding properties of ABP-50: The elongation factor-1 alpha of Dictyostelium
    • Dharmawardhane S, Demma M, Yang F, Condeelis J. 1991. Compartmentalization and actin binding properties of ABP-50: the elongation factor-1 alpha of Dictyostelium. Cell Motil Cytoskeleton 20:279-288.
    • (1991) Cell Motil Cytoskeleton , vol.20 , pp. 279-288
    • Dharmawardhane, S.1    Demma, M.2    Yang, F.3    Condeelis, J.4
  • 18
    • 0009663357 scopus 로고
    • A multiple comparison procedure for comparing several treatments with a control
    • Dunnett CW. 1955. A multiple comparison procedure for comparing several treatments with a control. J Am Stat Assoc 50:1096-1121.
    • (1955) J Am Stat Assoc , vol.50 , pp. 1096-1121
    • Dunnett, C.W.1
  • 19
    • 0001939930 scopus 로고    scopus 로고
    • Baculovirus pathogenesis
    • Miller LK, editor. New York: Plenum Press
    • Federici BA. 1997. Baculovirus pathogenesis. In: Miller LK, editor. The baculoviruses. New York: Plenum Press. p 34-59.
    • (1997) The Baculoviruses , pp. 34-59
    • Federici, B.A.1
  • 20
    • 0028136693 scopus 로고
    • Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu
    • Gonen H, Smith CE, Siegel NR, Kahana D, Merrick WC, Chakraburtty K, Schwartz, AL, Ciechanover A. 1994. Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu. Proc Natl Acad Sci USA 91:7648-7652.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7648-7652
    • Gonen, H.1    Smith, C.E.2    Siegel, N.R.3    Kahana, D.4    Merrick, W.C.5    Chakraburtty, K.6    Schwartz, A.L.7    Ciechanover, A.8
  • 21
    • 0022481210 scopus 로고
    • Replication of the Trichoplusia ni granulosis and nuclear polyhedrosis viruses in cell cultures
    • Granados RR, Derksen ACG, Dwyer KG. 1986. Replication of the Trichoplusia ni granulosis and nuclear polyhedrosis viruses in cell cultures. Virol 152:472-476.
    • (1986) Virol , vol.152 , pp. 472-476
    • Granados, R.R.1    Derksen, A.C.G.2    Dwyer, K.G.3
  • 22
    • 0000485094 scopus 로고
    • Established insect cell line from the cabbage looper, Trichoplusia ni
    • Hink WF. 1970. Established insect cell line from the cabbage looper, Trichoplusia ni. Nature 226:446-467.
    • (1970) Nature , vol.226 , pp. 446-467
    • Hink, W.F.1
  • 23
    • 0024296635 scopus 로고
    • Two genes encode related cytoplasmic elongation factors 1alpha (EF-1alpha) in Drosophila melanogaster with continuous and stage specific expression
    • Hovemann B, Richter S, Walldorf U, Cziepluch C. 1988. Two genes encode related cytoplasmic elongation factors 1alpha (EF-1alpha) in Drosophila melanogaster with continuous and stage specific expression. Nucleic Acids Res 16:3175-3194.
    • (1988) Nucleic Acids Res , vol.16 , pp. 3175-3194
    • Hovemann, B.1    Richter, S.2    Walldorf, U.3    Cziepluch, C.4
  • 26
    • 0029812091 scopus 로고    scopus 로고
    • Intracellular expression of a single-chain antibody directed to the EGFR leads to growth inhibition of tumor cells
    • Jannot CB, Beerli RR, Mason S, Gullick WJ, Hynes NE. 1996. Intracellular expression of a single-chain antibody directed to the EGFR leads to growth inhibition of tumor cells. Oncogene 13:275-282.
    • (1996) Oncogene , vol.13 , pp. 275-282
    • Jannot, C.B.1    Beerli, R.R.2    Mason, S.3    Gullick, W.J.4    Hynes, N.E.5
  • 27
    • 0028081335 scopus 로고
    • The subunit structure of elongation factor 1 from Artemia: Why two α-chains in this complex?
    • Janssen GMC, van Damme HTF, Kriek J, Amons R, Möller W. 1994. The subunit structure of elongation factor 1 from Artemia: why two α-chains in this complex? J Biol Chem 269:31410-31417.
    • (1994) J Biol Chem , vol.269 , pp. 31410-31417
    • Janssen, G.M.C.1    Van Damme, H.T.F.2    Kriek, J.3    Amons, R.4    Möller, W.5
  • 28
    • 0020508540 scopus 로고
    • Antitumor activity of didemnin B in the human tumor stem cell assay
    • Jiang TL, Liu RH, Salmon SE. 1983. Antitumor activity of didemnin B in the human tumor stem cell assay. Cancer Chemother Pharmacol 11:1-4.
    • (1983) Cancer Chemother Pharmacol , vol.11 , pp. 1-4
    • Jiang, T.L.1    Liu, R.H.2    Salmon, S.E.3
  • 29
    • 0030590642 scopus 로고    scopus 로고
    • Bias in murine IgG isotype immunobilisation. Implications for IgG glycoform analysis ELISA procedures
    • Jones RH, Rademacher TW, Williams PJ. 1996. Bias in murine IgG isotype immunobilisation. Implications for IgG glycoform analysis ELISA procedures. J Immunol Methods 197:109-120.
    • (1996) J Immunol Methods , vol.197 , pp. 109-120
    • Jones, R.H.1    Rademacher, T.W.2    Williams, P.J.3
  • 30
    • 0027933535 scopus 로고
    • Protein translation elongation factor-1 alpha from Trypanosoma brucei binds calmodulin
    • Kaur KJ, Ruben L. 1994. Protein translation elongation factor-1 alpha from Trypanosoma brucei binds calmodulin. J Biol Chem 269:23045-23050.
    • (1994) J Biol Chem , vol.269 , pp. 23045-23050
    • Kaur, K.J.1    Ruben, L.2
  • 31
    • 0027292202 scopus 로고
    • Tissue- Dependent variation in the expression of elongation factor-1 alpha isoforms: Isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha
    • Knudsen SM, Frydenberg J, Clark BF, Leffers H. 1993. Tissue- dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha. Eur J Biochem 215:549-554.
    • (1993) Eur J Biochem , vol.215 , pp. 549-554
    • Knudsen, S.M.1    Frydenberg, J.2    Clark, B.F.3    Leffers, H.4
  • 32
    • 0032576961 scopus 로고    scopus 로고
    • Purification and characterisation of a tissue specific elongation factor 1 alpha (EF-1 alpha 2) from rabbit muscle
    • Kristensen P, Lund A, Clark BF, Cavallius J, Merrick WC. 1998. Purification and characterisation of a tissue specific elongation factor 1 alpha (EF-1 alpha 2) from rabbit muscle. Biochem Biophys Res Commun 245:810-814.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 810-814
    • Kristensen, P.1    Lund, A.2    Clark, B.F.3    Cavallius, J.4    Merrick, W.C.5
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 84990431534 scopus 로고
    • Production of a monoclonal antibody to the arylphorin of Heliothis zea
    • Lenz CL, Greenstone MH. 1988. Production of a monoclonal antibody to the arylphorin of Heliothis zea. Insect Biochem Physiol 9:167-177.
    • (1988) Insect Biochem Physiol , vol.9 , pp. 167-177
    • Lenz, C.L.1    Greenstone, M.H.2
  • 36
    • 0023336956 scopus 로고
    • Expression of three genes for elongation factor 1 alpha during morphogenesis of Mucor racemosus
    • Linz JE, Sypherd PS. 1987. Expression of three genes for elongation factor 1 alpha during morphogenesis of Mucor racemosus. Mol Cell Biol 7:1925-1932.
    • (1987) Mol Cell Biol , vol.7 , pp. 1925-1932
    • Linz, J.E.1    Sypherd, P.S.2
  • 37
    • 1842442241 scopus 로고
    • Measurement of the incorporation of radioactive amino acids into protein by a filter-paper disk method
    • Mans RJ, Novelli GD. 1961. Measurement of the incorporation of radioactive amino acids into protein by a filter-paper disk method. Arch Biochem Biophys 94:48-53.
    • (1961) Arch Biochem Biophys , vol.94 , pp. 48-53
    • Mans, R.J.1    Novelli, G.D.2
  • 38
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262:10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 39
    • 0034958759 scopus 로고    scopus 로고
    • Identification of conformational neutralizing epitopes on the capsid protein of canine calicivirus
    • Matsuura Y, Tohya Y, Mochizuki M, Takase K, Sugimura T. 2001. Identification of conformational neutralizing epitopes on the capsid protein of canine calicivirus. J Gen Virol 82:1695-1702.
    • (2001) J Gen Virol , vol.82 , pp. 1695-1702
    • Matsuura, Y.1    Tohya, Y.2    Mochizuki, M.3    Takase, K.4    Sugimura, T.5
  • 40
    • 0019783997 scopus 로고
    • Establishment of two continuous cell lines of Heliothis virescens (F.) (Lepidoptera: Noctuidae)
    • McIntosh AH, Andrews PA, Ignoffo CM. 1981. Establishment of two continuous cell lines of Heliothis virescens (F.) (Lepidoptera: Noctuidae). In Vitro 17:649-650.
    • (1981) In Vitro , vol.17 , pp. 649-650
    • McIntosh, A.H.1    Andrews, P.A.2    Ignoffo, C.M.3
  • 41
    • 0016083976 scopus 로고
    • Insect cells: Colony formation and cloning in agar medium
    • McIntosh AH, Rechtoris C. 1974. Insect cells: colony formation and cloning in agar medium. In Vitro 10:1-5.
    • (1974) In Vitro , vol.10 , pp. 1-5
    • McIntosh, A.H.1    Rechtoris, C.2
  • 42
    • 0035092528 scopus 로고    scopus 로고
    • Different effects of a single amino acid substitution on three adjacent epitopes in the gp41 C-terminal tail of a neturalizing antibody escape mutant of human immunodeficiency virus type 1
    • McLain L, Brown JL, Cheung L, Reading SA, Parry C, Jones TD, Cleveland SM, Dimmock NJ. 2001. Different effects of a single amino acid substitution on three adjacent epitopes in the gp41 C-terminal tail of a neturalizing antibody escape mutant of human immunodeficiency virus type 1. Arch Virol 146:157-166.
    • (2001) Arch Virol , vol.146 , pp. 157-166
    • McLain, L.1    Brown, J.L.2    Cheung, L.3    Reading, S.A.4    Parry, C.5    Jones, T.D.6    Cleveland, S.M.7    Dimmock, N.J.8
  • 44
    • 0001507213 scopus 로고    scopus 로고
    • The molecular basis of baculovirus host range
    • Miller LK, editor. New York: Plenum Press
    • Miller LK, Lu A. 1997. The molecular basis of baculovirus host range. In: Miller LK, editor. The baculoviruses. New York: Plenum Press. p 217-235.
    • (1997) The Baculoviruses , pp. 217-235
    • Miller, L.K.1    Lu, A.2
  • 45
    • 2342502147 scopus 로고    scopus 로고
    • Innovations in recombinant therapeutics
    • Morrow KJ Jr. 2001. Innovations in recombinant therapeutics. Genet Eng News 21:8.
    • (2001) Genet Eng News , vol.21 , pp. 8
    • Morrow Jr., K.J.1
  • 46
    • 0033582434 scopus 로고    scopus 로고
    • Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1 alpha in the complex with EF-1H
    • Negrutskii BS, Shalak VF, Kerjan P, El'skaya AV, Mirande M. 1999. Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1 alpha in the complex with EF-1H. J Biol Chem 274:4545-4550.
    • (1999) J Biol Chem , vol.274 , pp. 4545-4550
    • Negrutskii, B.S.1    Shalak, V.F.2    Kerjan, P.3    El'skaya, A.V.4    Mirande, M.5
  • 47
    • 0025248661 scopus 로고
    • The mitotic apparatus-associated 51-kDa protein from sea urchin eggs is a GTP-binding protein and is immunologically related to yeast polypeptide elongation factor 1 alpha
    • Ohta K, Toriyama M, Miyazaki M, Murofushi H, Hosoda S, Endo S, Sakai H. 1990. The mitotic apparatus-associated 51-kDa protein from sea urchin eggs is a GTP-binding protein and is immunologically related to yeast polypeptide elongation factor 1 alpha. J Biol Chem 265:3240-3247.
    • (1990) J Biol Chem , vol.265 , pp. 3240-3247
    • Ohta, K.1    Toriyama, M.2    Miyazaki, M.3    Murofushi, H.4    Hosoda, S.5    Endo, S.6    Sakai, H.7
  • 48
    • 0026512711 scopus 로고
    • A specific binding site in Nb2 node lymphoma cells mediates the effects of didemnin B, an immunosuppressive cyclic peptide
    • Shen GK, Zukoski CF, Montgomery DW. 1992. A specific binding site in Nb2 node lymphoma cells mediates the effects of didemnin B, an immunosuppressive cyclic peptide. Int J Immunopharmacol 14:63-73.
    • (1992) Int J Immunopharmacol , vol.14 , pp. 63-73
    • Shen, G.K.1    Zukoski, C.F.2    Montgomery, D.W.3
  • 50
    • 0019062683 scopus 로고
    • The role of eucaryotic factor Tu in protein synthesis. The measurement of the elongation factor Tu content of rabbit reticulocytes and other mammalian cells by a sensitive radioimmunoassay
    • Slobin LI. 1980. The role of eucaryotic factor Tu in protein synthesis. The measurement of the elongation factor Tu content of rabbit reticulocytes and other mammalian cells by a sensitive radioimmunoassay. Eur J Biochem 110:555-563.
    • (1980) Eur J Biochem , vol.110 , pp. 555-563
    • Slobin, L.I.1
  • 51
    • 0000082246 scopus 로고
    • Monoclonal antibodies specific for Laelius pedatus (Bethylidae) and Bracon hebetor (Braconidae), two hymenopterous parasitoids of stored-product insects
    • Stuart MK, Burkholder WE. 1991. Monoclonal antibodies specific for Laelius pedatus (Bethylidae) and Bracon hebetor (Braconidae), two hymenopterous parasitoids of stored-product insects. Biol Control 1:302-308.
    • (1991) Biol Control , vol.1 , pp. 302-308
    • Stuart, M.K.1    Burkholder, W.E.2
  • 52
    • 0031105616 scopus 로고    scopus 로고
    • Immunological detection of hymenopteran parasitism in Helicoverpa zea and Heliothis virescens
    • Stuart MK, Greenstone MH. 1997. Immunological detection of hymenopteran parasitism in Helicoverpa zea and Heliothis virescens. Biol Control 8:197-202.
    • (1997) Biol Control , vol.8 , pp. 197-202
    • Stuart, M.K.1    Greenstone, M.H.2
  • 53
    • 0031626708 scopus 로고    scopus 로고
    • An antibody diagnostic for hymenopteran parasitism is specific for a homologue of elongation factor-1α
    • Stuart MK. 1998. An antibody diagnostic for hymenopteran parasitism is specific for a homologue of elongation factor-1α. Arch Insect Biochem Physiol 39:1-8.
    • (1998) Arch Insect Biochem Physiol , vol.39 , pp. 1-8
    • Stuart, M.K.1
  • 54
    • 0024307032 scopus 로고
    • Cell-free translation in lysates from Spodoptera frugiperda (Lepidoptera: Noctuidae) cells
    • Swerdel MR, Fallon AM. 1989. Cell-free translation in lysates from Spodoptera frugiperda (Lepidoptera: Noctuidae) cells. Comp Biochem Physiol 93B:803-806.
    • (1989) Comp Biochem Physiol , vol.93 B , pp. 803-806
    • Swerdel, M.R.1    Fallon, A.M.2
  • 55
    • 0029670281 scopus 로고    scopus 로고
    • Antiproliferative effect of dehydrodidemnin B (DDB), a depsipeptide isolated from Mediterranean tunicates
    • Urdiales IL, Morata P, De Castro N, Sanchez-Jimenez F. 1996. Antiproliferative effect of dehydrodidemnin B (DDB), a depsipeptide isolated from Mediterranean tunicates. Cancer Lett 102:31-37.
    • (1996) Cancer Lett , vol.102 , pp. 31-37
    • Urdiales, I.L.1    Morata, P.2    De Castro, N.3    Sanchez-Jimenez, F.4
  • 56
    • 0005693451 scopus 로고
    • Making hybridomas
    • Stern NJ, Gamble HR, editors. Beltsville Agricultural Research Center, Agricultural Research Service, U.S. Dept of Agriculture. Totowa, NJ: Rowan & Allanheld, Publishers
    • Van Deusen RA. 1983. Making hybridomas. In: Stern NJ, Gamble HR, editors. Hybridoma technology in agricultural and veterinary research. Beltsville Agricultural Research Center, Agricultural Research Service, U.S. Dept of Agriculture. Totowa, NJ: Rowan & Allanheld, Publishers. p 15-25.
    • (1983) Hybridoma Technology in Agricultural and Veterinary Research , pp. 15-25
    • Van Deusen, R.A.1
  • 57
    • 0017475358 scopus 로고
    • The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera: Noctuidae)
    • Vaughn JL, Goodwin RH, Tompkins GJ, McCawley P. 1977. The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera: Noctuidae). In Vitro 13:213-217.
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Tompkins, G.J.3    McCawley, P.4
  • 58
    • 0028111491 scopus 로고
    • Regulation of phosphatidylinositol 4-kinase by the protein activator PIK-A49. Activation requires phosphorylation of PIK-A49
    • Yang W, Boss WF. 1994. Regulation of phosphatidylinositol 4-kinase by the protein activator PIK-A49. Activation requires phosphorylation of PIK-A49. J Biol Chem 269:3852-3857.
    • (1994) J Biol Chem , vol.269 , pp. 3852-3857
    • Yang, W.1    Boss, W.F.2
  • 59
    • 0029838903 scopus 로고    scopus 로고
    • Intracellular single-chain antibody inhibits integrin VLA-4 maturation and function
    • Yuan Q, Strauch KL, Lobb RR, Hemler ME. 1996. Intracellular single-chain antibody inhibits integrin VLA-4 maturation and function. Biochem J 318:591-596.
    • (1996) Biochem J , vol.318 , pp. 591-596
    • Yuan, Q.1    Strauch, K.L.2    Lobb, R.R.3    Hemler, M.E.4
  • 60
    • 0024550105 scopus 로고
    • Efficacy of didemnin B in suppressing allograft rejection in mice and rats
    • Yuh DD, Zurcher RP, Carmichael PG, Morris RE. 1989. Efficacy of didemnin B in suppressing allograft rejection in mice and rats. Transplant Proc 21:1141-1143.
    • (1989) Transplant Proc , vol.21 , pp. 1141-1143
    • Yuh, D.D.1    Zurcher, R.P.2    Carmichael, P.G.3    Morris, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.