메뉴 건너뛰기




Volumn 39, Issue 1, 1998, Pages 1-8

An antibody diagnostic for hymenopteran parasitism is specific for a homologue of elongation factor-1α

Author keywords

Elongation factor 1 ; Hymenoptera; Noctuidae; Parasitoid

Indexed keywords

ANTIGEN; ELONGATION FACTOR; ELONGATION FACTOR 1; INSECT PROTEIN; MONOCLONAL ANTIBODY;

EID: 0031626708     PISSN: 07394462     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1520-6327(1998)39:1<1::AID-ARCH2>3.0.CO;2-P     Document Type: Article
Times cited : (4)

References (36)
  • 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
  • 3
    • 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
  • 4
    • 0031160057 scopus 로고    scopus 로고
    • A molecular phylogeny of the Aphidiinae (Hymenoptera: Braconidae)
    • Belshaw R, Quicke DLJ (1997): A molecular phylogeny of the Aphidiinae (Hymenoptera: Braconidae). Mol Phylogenet Evol 7:281-293.
    • (1997) Mol Phylogenet Evol , vol.7 , pp. 281-293
    • Belshaw, R.1    Quicke, D.L.J.2
  • 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
    • 0027406211 scopus 로고
    • Characterization of yeast EF-1α: Non-conservation of post-translational modifications
    • Cavallius J, Zoll W, Chakraburtty K, Merrick WC (1993): Characterization of yeast EF-1α: Non-conservation of post-translational modifications. Biochim Biophys Acta 1163:75-80.
    • (1993) Biochim Biophys Acta , vol.1163 , pp. 75-80
    • Cavallius, J.1    Zoll, W.2    Chakraburtty, K.3    Merrick, W.C.4
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine
    • Dever TE, Costello CI, Owens CL, Rosenberry TL, Merrick WC (1989): Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. J Biol Chem 264:20518-20525.
    • (1989) J Biol Chem , vol.264 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.I.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 14
    • 0030007107 scopus 로고    scopus 로고
    • Eukaryotic polypeptide elongation system and its sensitivity to the inhibitory substances of plant origin
    • Gałasiński W (1996): Eukaryotic polypeptide elongation system and its sensitivity to the inhibitory substances of plant origin. Proc Soc Exp Biol Med 212:24-37.
    • (1996) Proc Soc Exp Biol Med , vol.212 , pp. 24-37
    • Gałasiński, W.1
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0026034328 scopus 로고
    • Rapid and sensitive detection of Salmonella (O:6,7) by immunomagnetic monoclonal antibody-based assays
    • Luk JMC, Lindberg AA (1991): Rapid and sensitive detection of Salmonella (O:6,7) by immunomagnetic monoclonal antibody-based assays. J Immunol Methods 137:1-8.
    • (1991) J Immunol Methods , vol.137 , pp. 1-8
    • Luk, J.M.C.1    Lindberg, A.A.2
  • 19
    • 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
  • 20
    • 0030615250 scopus 로고    scopus 로고
    • Phylogenetic utility of elongation factor-1α in Noctuoidea (Insecta: Lepidoptera): The limits of synonymous substitution
    • Mitchell A, Cho S, Regier JC, Mitter C, Poole RW, Matthews M (1997): Phylogenetic utility of elongation factor-1α in Noctuoidea (Insecta: Lepidoptera): The limits of synonymous substitution. Mol Biol Evol 14:381-390.
    • (1997) Mol Biol Evol , vol.14 , pp. 381-390
    • Mitchell, A.1    Cho, S.2    Regier, J.C.3    Mitter, C.4    Poole, R.W.5    Matthews, M.6
  • 21
    • 0023710643 scopus 로고
    • Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor
    • Motorin YA, Wolfson AD, Orlovsky AF, Gladilin KL (1988): Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. FEBS Lett 238:262-264.
    • (1988) FEBS Lett , vol.238 , pp. 262-264
    • Motorin, Y.A.1    Wolfson, A.D.2    Orlovsky, A.F.3    Gladilin, K.L.4
  • 22
    • 0030471363 scopus 로고    scopus 로고
    • Bundling of actin filaments by elongation factor 1α inhibits polymerization at filament ends
    • Murray JW, Edmonds BT, Liu G, Condeelis J (1996): Bundling of actin filaments by elongation factor 1α inhibits polymerization at filament ends. J Cell Biol 135:1309-1321.
    • (1996) J Cell Biol , vol.135 , pp. 1309-1321
    • Murray, J.W.1    Edmonds, B.T.2    Liu, G.3    Condeelis, J.4
  • 23
    • 0025876244 scopus 로고
    • Channeling of aminoacyl-tRNA for protein synthesis in vivo
    • Negrutskii BS, Deutscher MP (1991): Channeling of aminoacyl-tRNA for protein synthesis in vivo. Proc Natl Acad Sci USA 88:4991-4995.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4991-4995
    • Negrutskii, B.S.1    Deutscher, M.P.2
  • 24
    • 0017070903 scopus 로고
    • Elongation factor 1 from Artemia salina: Properties and disaggregation of the enzyme
    • Nombela C, Redfield B, Ochoa S, Weissbach H (1976): Elongation factor 1 from Artemia salina: Properties and disaggregation of the enzyme. Eur J Biochem 65:395-402.
    • (1976) Eur J Biochem , vol.65 , pp. 395-402
    • Nombela, C.1    Redfield, B.2    Ochoa, S.3    Weissbach, H.4
  • 27
    • 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
  • 28
    • 0024516963 scopus 로고
    • Didemnin B prolongs rat heart allograft survival
    • Stevens DW, Jensen RM, Stevens LE (1989): Didemnin B prolongs rat heart allograft survival. Transplant Proc 21:1139-1140.
    • (1989) Transplant Proc , vol.21 , pp. 1139-1140
    • Stevens, D.W.1    Jensen, R.M.2    Stevens, L.E.3
  • 29
    • 0011191329 scopus 로고    scopus 로고
    • Serological diagnosis of parasitism: A monoclonal antibody-based immunodot assay for Microplitis croceipes (Hymenoptera: Braconidae)
    • Symondson WOC, Liddell E (eds): London: Chapman and Hall
    • Stuart MK, Greenstone MH (1996): Serological diagnosis of parasitism: A monoclonal antibody-based immunodot assay for Microplitis croceipes (Hymenoptera: Braconidae). In Symondson WOC, Liddell E (eds): The Ecology of Agricultural Pests: Biochemical Approaches. London: Chapman and Hall, pp 301-321.
    • (1996) The Ecology of Agricultural Pests: Biochemical Approaches , pp. 301-321
    • Stuart, M.K.1    Greenstone, M.H.2
  • 30
    • 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
  • 31
    • 0024600842 scopus 로고
    • Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1α
    • Uetsuki T, Naito A, Nagata S, Kaziro Y (1989): Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1α. J Biol Chem 264:5791-5798.
    • (1989) J Biol Chem , vol.264 , pp. 5791-5798
    • Uetsuki, T.1    Naito, A.2    Nagata, S.3    Kaziro, Y.4
  • 32
    • 0029670281 scopus 로고    scopus 로고
    • Antiproliferative effect of dehydrodidemnin B (DDB), a depsipeptide isolated from Mediterranean tunicates
    • Urdiales JL, 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, J.L.1    Morata, P.2    De Castro, N.3    Sanchez-Jimenez, F.4
  • 33
    • 0026691915 scopus 로고
    • Identification of the sites in the eukaryotic elongation factor 1α involved in the binding of elongation factor 1β and aminoacyl-tRNA
    • van Damme HTF, Amons R, Möller W (1992): Identification of the sites in the eukaryotic elongation factor 1α involved in the binding of elongation factor 1β and aminoacyl-tRNA. Eur J Biochem 207:1025-1034.
    • (1992) Eur J Biochem , vol.207 , pp. 1025-1034
    • Van Damme, H.T.F.1    Amons, R.2    Möller, W.3
  • 34
    • 0024414072 scopus 로고
    • Murine elongation factor 1α (EF-1α) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties
    • Whiteheart SW, Shenbagamurthi P, Chen L, Cotter RJ, Hart GW (1989): Murine elongation factor 1α (EF-1α) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. J Biol Chem 264:14334-14341.
    • (1989) J Biol Chem , vol.264 , pp. 14334-14341
    • Whiteheart, S.W.1    Shenbagamurthi, P.2    Chen, L.3    Cotter, R.J.4    Hart, G.W.5
  • 35
    • 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
  • 36
    • 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.