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Volumn 69, Issue 3, 2008, Pages 107-117

A monoclonal antibody that inhibits translation in Sf21 cell lysates is specific for glyceraldehyde-3-phosphate dehydrogenase

Author keywords

EF 1 ; Glyceraldehyde 3 phosphate dehydrogenase; Monoclonal antibody; Translation

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MONOCLONAL ANTIBODY;

EID: 58049192429     PISSN: 07394462     EISSN: 15206327     Source Type: Journal    
DOI: 10.1002/arch.20271     Document Type: Article
Times cited : (5)

References (39)
  • 1
    • 10644272564 scopus 로고    scopus 로고
    • Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules
    • Andrade J, Pearce ST, Zhao H, Barroso M. 2004. Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules. Biochem J 384(Pt 2):327-336.
    • (2004) Biochem J , vol.384 , Issue.PART 2 , pp. 327-336
    • Andrade, J.1    Pearce, S.T.2    Zhao, H.3    Barroso, M.4
  • 2
    • 34250014485 scopus 로고    scopus 로고
    • Glyceraldehyde-3- phosphate dehydrogenase exerts different biologic activities in apoptotic and proliferating hepatocytes according to its subcellular localization
    • Barbini L, Rodriguez J, Dominguez F, Vega F. 2007. Glyceraldehyde-3- phosphate dehydrogenase exerts different biologic activities in apoptotic and proliferating hepatocytes according to its subcellular localization. Mol Cell Biochem 300:19-28.
    • (2007) Mol Cell Biochem , vol.300 , pp. 19-28
    • Barbini, L.1    Rodriguez, J.2    Dominguez, F.3    Vega, F.4
  • 3
    • 18144423122 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase binds to the AU-Rich 3′ untranslated region of colony-stimulating factor-1 (CSF-1) messenger RNA in human ovarian cancer cells: Possible role in CSF-1 post-transcriptional regulation and tumor phenotype
    • Bonafe N, Gilmore-Hebert M, Folk NL, Azodi M, Zhou Y, Chambers SK. 2005. Glyceraldehyde-3-phosphate dehydrogenase binds to the AU-Rich 3′ untranslated region of colony-stimulating factor-1 (CSF-1) messenger RNA in human ovarian cancer cells: possible role in CSF-1 post-transcriptional regulation and tumor phenotype. Cancer Res 65:3762-3771.
    • (2005) Cancer Res , vol.65 , pp. 3762-3771
    • Bonafe, N.1    Gilmore-Hebert, M.2    Folk, N.L.3    Azodi, M.4    Zhou, Y.5    Chambers, S.K.6
  • 4
    • 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
  • 5
    • 0031907153 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase-S protein distribution during mouse spermatogenesis
    • Bunch DO, Welch JE, Magyar PL, Eddy EM, O'Brien DA. 1998. Glyceraldehyde 3-phosphate dehydrogenase-S protein distribution during mouse spermatogenesis. Biol Reprod 58:834-841.
    • (1998) Biol Reprod , vol.58 , pp. 834-841
    • Bunch, D.O.1    Welch, J.E.2    Magyar, P.L.3    Eddy, E.M.4    O'Brien, D.A.5
  • 7
    • 0029027331 scopus 로고
    • A highly conserved nuclear gene for low-level phylogenetics: Elongation factor-1 alpha 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-1 alpha 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
  • 8
    • 0034078845 scopus 로고    scopus 로고
    • Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro
    • Choudhary S, De BP, Banerjee AK. 2000. Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro. J Virol 74:3634-3641.
    • (2000) J Virol , vol.74 , pp. 3634-3641
    • Choudhary, S.1    De, B.P.2    Banerjee, A.K.3
  • 9
    • 0014690989 scopus 로고
    • Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into dimers or monomers by adenosine triphosphate
    • Constantinides SM, Deal Jr WC. 1969. Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into dimers or monomers by adenosine triphosphate. J Biol Chem 244:5695-5702.
    • (1969) J Biol Chem , vol.244 , pp. 5695-5702
    • Constantinides, S.M.1    Deal Jr, W.C.2
  • 10
    • 0024308384 scopus 로고
    • Immunocytochemical localization of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells
    • Cool BL, Sirover MA. 1989. Immunocytochemical localization of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells. Cancer Res 49:3029-3036.
    • (1989) Cancer Res , vol.49 , pp. 3029-3036
    • Cool, B.L.1    Sirover, M.A.2
  • 11
    • 28744448949 scopus 로고    scopus 로고
    • Amyloid-beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease
    • Cumming RC, Schubert D. 2005. Amyloid-beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease. FASEB J 19:2060-2062.
    • (2005) FASEB J , vol.19 , pp. 2060-2062
    • Cumming, R.C.1    Schubert, D.2
  • 12
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine
    • 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 glycerylphosphorylethanolamine. 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
  • 13
    • 34548101969 scopus 로고    scopus 로고
    • Involvement of glyceraldehyde-3-phosphate dehydrogenase in tumor necrosis factor-related apoptosis-inducing ligand-mediated death of thyroid cancer cells
    • Du ZX, Wang HQ, Zhang HY, Gao DX. 2007. Involvement of glyceraldehyde-3-phosphate dehydrogenase in tumor necrosis factor-related apoptosis-inducing ligand-mediated death of thyroid cancer cells. Endocrinology 148:4352-4361.
    • (2007) Endocrinology , vol.148 , pp. 4352-4361
    • Du, Z.X.1    Wang, H.Q.2    Zhang, H.Y.3    Gao, D.X.4
  • 14
    • 0037195125 scopus 로고    scopus 로고
    • Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion
    • Glaser PE, Han X, Gross RW. 2002. Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion. Proc Natl Acad Sci USA 99:14104-14109.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14104-14109
    • Glaser, P.E.1    Han, X.2    Gross, R.W.3
  • 15
    • 0033568356 scopus 로고    scopus 로고
    • Antibodies to the nonnative forms of d-glyceraldehyde-3-phosphate dehydrogenase: Identification, purification, and influence on the renaturation of the enzyme
    • Grigorieva JA, Dainiak MB, Katrukha AG, Muronetz VI. 1999. Antibodies to the nonnative forms of d-glyceraldehyde-3-phosphate dehydrogenase: identification, purification, and influence on the renaturation of the enzyme. Arch Biochem Biophys 369:252-260.
    • (1999) Arch Biochem Biophys , vol.369 , pp. 252-260
    • Grigorieva, J.A.1    Dainiak, M.B.2    Katrukha, A.G.3    Muronetz, V.I.4
  • 18
    • 23644445641 scopus 로고    scopus 로고
    • Gymnemic acids inhibit rabbit glyceraldehyde-3-phosphate dehydrogenase and induce a smearing of its electrophoretic band and dephosphorylation
    • Izutani Y, Murai T, Imoto T, Ohnishi M, Oda M, Ishijima S. 2005. Gymnemic acids inhibit rabbit glyceraldehyde-3-phosphate dehydrogenase and induce a smearing of its electrophoretic band and dephosphorylation. FEBS Lett 579:4333-4336.
    • (2005) FEBS Lett , vol.579 , pp. 4333-4336
    • Izutani, Y.1    Murai, T.2    Imoto, T.3    Ohnishi, M.4    Oda, M.5    Ishijima, S.6
  • 19
    • 0028081335 scopus 로고
    • The subunit structure of elongation factor 1 from Artemia. Why two alpha-chains in this complex?
    • Janssen GM, van Damme HT, Kriek J, Amons R, Moller W. 1994. The subunit structure of elongation factor 1 from Artemia. Why two alpha-chains in this complex? J Biol Chem 269:31410-31417.
    • (1994) J Biol Chem , vol.269 , pp. 31410-31417
    • Janssen, G.M.1    van Damme, H.T.2    Kriek, J.3    Amons, R.4    Moller, W.5
  • 20
    • 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
  • 21
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto RM, Caswell AH. 1986. Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry 25:657-661.
    • (1986) Biochemistry , vol.25 , pp. 657-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 22
    • 0036175770 scopus 로고    scopus 로고
    • Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: Implications for anchoring mRNA in cell protrusions
    • Liu G, Grant WM, Persky D, Latham Jr VM, Singer RH, Condeelis J. 2002. Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions. Mol Biol Cell 13:579-592.
    • (2002) Mol Biol Cell , vol.13 , pp. 579-592
    • Liu, G.1    Grant, W.M.2    Persky, D.3    Latham Jr, V.M.4    Singer, R.H.5    Condeelis, J.6
  • 23
    • 0030615250 scopus 로고    scopus 로고
    • Phylogenetic utility of elongation factor-1 alpha 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-1 alpha 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
  • 24
    • 0034031362 scopus 로고    scopus 로고
    • Association between elongation factor-1alpha and microtubules in vivo is domain dependent and conditional
    • Moore RC, Cyr RJ. 2000. Association between elongation factor-1alpha and microtubules in vivo is domain dependent and conditional. Cell Motil Cytoskeleton 45:279-292.
    • (2000) Cell Motil Cytoskeleton , vol.45 , pp. 279-292
    • Moore, R.C.1    Cyr, R.J.2
  • 25
    • 0028816615 scopus 로고
    • +-binding region (Rossmann fold)
    • +-binding region (Rossmann fold). J Biol Chem 270:2755-2763.
    • (1995) J Biol Chem , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.2
  • 26
    • 0022406559 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes
    • Ryazanov AG. 1985. Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes. FEBS Lett 192:131-134.
    • (1985) FEBS Lett , vol.192 , pp. 131-134
    • Ryazanov, A.G.1
  • 27
    • 0023921027 scopus 로고
    • Heterogeneity of glyceraldehyde-3- phosphate dehydrogenase from human brain
    • Ryzlak MT, Pietruszko R. 1988. Heterogeneity of glyceraldehyde-3- phosphate dehydrogenase from human brain. Biochim Biophys Acta 954:309-324.
    • (1988) Biochim Biophys Acta , vol.954 , pp. 309-324
    • Ryzlak, M.T.1    Pietruszko, R.2
  • 28
    • 0024805295 scopus 로고
    • Role of lysine methylation in the activities of elongation factor 1 alpha
    • Sherman M, Sypherd PS. 1989. Role of lysine methylation in the activities of elongation factor 1 alpha. Arch Biochem Biophys 275:371-378.
    • (1989) Arch Biochem Biophys , vol.275 , pp. 371-378
    • Sherman, M.1    Sypherd, P.S.2
  • 29
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R, Green MR. 1993. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science 259:365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 30
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover MA. 1999. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1432:159-184.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 31
    • 0037208830 scopus 로고    scopus 로고
    • Monoclonal antibodies to elongation factor-1alpha inhibit in vitro translation in lysates of Sf21 cells
    • Stuart MK, Chamberlain NR. 2003. Monoclonal antibodies to elongation factor-1alpha inhibit in vitro translation in lysates of Sf21 cells. Arch Insect Biochem Physiol 52:17-34.
    • (2003) Arch Insect Biochem Physiol , vol.52 , pp. 17-34
    • Stuart, M.K.1    Chamberlain, N.R.2
  • 32
    • 0029006230 scopus 로고
    • The mode of actions of glyceraldehyde-3-phosphate dehydrogenase identified as an immunoglobulin production stimulating factor
    • Sugahara T, Shirahata S, Sasaki T, Murakami H. 1995. The mode of actions of glyceraldehyde-3-phosphate dehydrogenase identified as an immunoglobulin production stimulating factor. FEBS Lett 368:92-96.
    • (1995) FEBS Lett , vol.368 , pp. 92-96
    • Sugahara, T.1    Shirahata, S.2    Sasaki, T.3    Murakami, H.4
  • 33
    • 0015021387 scopus 로고
    • Reactions of D-glyceraldehyde 3-phosphate dehydrogenase facilitated by oxidized nicotinamide-adenine dinucleotide
    • Trentham DR. 1971. Reactions of D-glyceraldehyde 3-phosphate dehydrogenase facilitated by oxidized nicotinamide-adenine dinucleotide. Biochem J 122:59-69.
    • (1971) Biochem J , vol.122 , pp. 59-69
    • Trentham, D.R.1
  • 34
    • 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
  • 35
    • 0025744934 scopus 로고
    • Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity
    • Venema RC, Peters HI, Traugh JA. 1991. Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity. J Biol Chem 266:12574-12580.
    • (1991) J Biol Chem , vol.266 , pp. 12574-12580
    • Venema, R.C.1    Peters, H.I.2    Traugh, J.A.3
  • 37
    • 0033998548 scopus 로고    scopus 로고
    • Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells
    • Welch JE, Brown PL, O'Brien DA, Magyar PL, Bunch DO, Mori C, Eddy EM. 2000. Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J Androl 21:328-338.
    • (2000) J Androl , vol.21 , pp. 328-338
    • Welch, J.E.1    Brown, P.L.2    O'Brien, D.A.3    Magyar, P.L.4    Bunch, D.O.5    Mori, C.6    Eddy, E.M.7
  • 38
    • 0024414072 scopus 로고
    • Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha
    • Whiteheart SW, Shenbagamurthi P, Chen L, Cotter RJ, Hart GW. 1989. Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. 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
  • 39
    • 0141894222 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein
    • Zhang L, Joshi AK, Smith S. 2003. Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein. J Biol Chem 278:40067-40074.
    • (2003) J Biol Chem , vol.278 , pp. 40067-40074
    • Zhang, L.1    Joshi, A.K.2    Smith, S.3


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