메뉴 건너뛰기




Volumn 37, Issue 1, 2002, Pages 37-52

Regulation of cytosolic malate dehydrogenase by juvenile hormone in Drosophila melanogaster

Author keywords

Drosophila melanogaster; Ecdysone; Enzyme activity; Juvenile hormone; Lipogenesis; Malate dehydrogenase; Metamorphosis

Indexed keywords

DROSOPHILA MELANOGASTER;

EID: 0036363351     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:37:1:37     Document Type: Article
Times cited : (12)

References (96)
  • 1
    • 0027653201 scopus 로고
    • A review on molecular physiology of malate and lactate dehydrogenases in fishes
    • Tripathi, G. (1993) A review on molecular physiology of malate and lactate dehydrogenases in fishes. Biomed. Environ. Sci. 6, 286-318.
    • (1993) Biomed. Environ. Sci. , vol.6 , pp. 286-318
    • Tripathi, G.1
  • 2
    • 0028113441 scopus 로고
    • Malate dehydrogenase: A model for structure, evolution, and catalysis
    • Goward, C. R. and Nicholls, D. J. (1994) Malate dehydrogenase: a model for structure, evolution, and catalysis. Protein Sci. 3, 1883-1888.
    • (1994) Protein Sci. , vol.3 , pp. 1883-1888
    • Goward, C.R.1    Nicholls, D.J.2
  • 5
    • 0030847930 scopus 로고    scopus 로고
    • Lipid mobilization and gluconeogenesis in plants: Do glyoxalate cycle enzyme activities constitute a real cycle? A hypothesis
    • Escher, C. L. and Widmer, F. (1997) Lipid mobilization and gluconeogenesis in plants: do glyoxalate cycle enzyme activities constitute a real cycle? A hypothesis. Biol. Chem. 378, 803-813.
    • (1997) Biol. Chem. , vol.378 , pp. 803-813
    • Escher, C.L.1    Widmer, F.2
  • 7
    • 0016411502 scopus 로고
    • Regulation and physiological functions of malic enzymes
    • B. L. Horecker and E. R. Stadtman eds.; Academic Press, New York & London
    • Frenkel, R. (1975) Regulation and physiological functions of malic enzymes. In: Current Topics in Cell Regulation vol. 9 B. L. Horecker and E. R. Stadtman eds.); Academic Press, New York & London., pp. 157-181.
    • (1975) Current Topics in Cell Regulation , vol.9 , pp. 157-181
    • Frenkel, R.1
  • 8
    • 0029414981 scopus 로고
    • NADP-malic enzyme from maize leaves: A fluorescence study
    • Drincovich, M. F. and Andreo, C. S. (1995) NADP-malic enzyme from maize leaves: A fluorescence study. Biochem. Mol. Biol. Int. 36, 1287-1297.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 1287-1297
    • Drincovich, M.F.1    Andreo, C.S.2
  • 9
    • 0026873602 scopus 로고
    • NADP-malic enzyme from plants
    • Edwards, G. E. and Andreo, C. S. (1992) NADP-malic enzyme from plants. Phytochemistry 31, 1845-1857.
    • (1992) Phytochemistry , vol.31 , pp. 1845-1857
    • Edwards, G.E.1    Andreo, C.S.2
  • 10
    • 0028247085 scopus 로고
    • Hysteresis of cytosolic NADP-malic enzyme II from Tryanosoma cruzi
    • Avilan, L. and Garcia, P. (1994) Hysteresis of cytosolic NADP-malic enzyme II from Tryanosoma cruzi. Mol. Biochem. Parasitol. 65, 225-232.
    • (1994) Mol. Biochem. Parasitol. , vol.65 , pp. 225-232
    • Avilan, L.1    Garcia, P.2
  • 11
    • 0011242982 scopus 로고
    • Changes in lipid synthesis in rat liver during development
    • Ballard, F. J. and Hanson, R. W. (1967) Changes in lipid synthesis in rat liver during development. Biochem. J. 102, 952-958.
    • (1967) Biochem. J. , vol.102 , pp. 952-958
    • Nd, B.F.J.1    Hanson, R.W.2
  • 12
    • 0016881284 scopus 로고
    • Regulation of the oxidative NADP-enzyme tissue levels in Drosophila melanogaster. I. Modulation by dietary carbohydrate and lipid
    • Geer, B. W., Kamiak, S. N., Kidd, K. R., Nishimura, R. A., and Yemm, S. J. (1976) Regulation of the oxidative NADP-enzyme tissue levels in Drosophila melanogaster. I. Modulation by dietary carbohydrate and lipid. J. Exp. Zool. 195, 15-32.
    • (1976) J. Exp. Zool. , vol.195 , pp. 15-32
    • Geer, B.W.1    Kamiak, S.N.2    Kidd, K.R.3    Nishimura, R.A.4    Yemm, S.J.5
  • 13
    • 0018837845 scopus 로고
    • Changes in the hepatic levels of messenger ribonucleic acid for malic enzyme during induction by thyroid hormone or diet
    • Towle, H. C., Mariash, C. N., and Oppenheimer, J. H. (1980) Changes in the hepatic levels of messenger ribonucleic acid for malic enzyme during induction by thyroid hormone or diet. Biochemistry 19, 579-585.
    • (1980) Biochemistry , vol.19 , pp. 579-585
    • Towle, H.C.1    Mariash, C.N.2    Oppenheimer, J.H.3
  • 14
    • 0022403385 scopus 로고
    • Tissue-specific regulation of two functional malic enzyme mRNAs by triiodothyronine
    • Dozin, B., Magnuson, M. A., and Nikodem, V. M. (1985): Tissue-specific regulation of two functional malic enzyme mRNAs by triiodothyronine. Biochemistry 24, 5581-5586.
    • (1985) Biochemistry , vol.24 , pp. 5581-5586
    • Dozin, B.1    Magnuson, M.A.2    Nikodem, V.M.3
  • 15
    • 0022828770 scopus 로고
    • Thyroid hormone regulation of malic enzyme synthesis. Dual tissue-specific control
    • Dozin, B., Magnuson, M. A., and Nikodem, V. M. (1986a): Thyroid hormone regulation of malic enzyme synthesis. Dual tissue-specific control. J. Biol. Chem. 261, 10,290-10,292.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10290-10292
    • Dozin, B.1    Magnuson, M.A.2    Nikodem, V.M.3
  • 16
    • 0022529693 scopus 로고
    • Tissue-specific control of rat malic enzyme activity and messenger RNA levels by a high carbohydrate diet
    • Dozin, B. Rall, I. E., and Nikodem, V. M. (1986b): Tissue-specific control of rat malic enzyme activity and messenger RNA levels by a high carbohydrate diet. Proc. Natl. Acad. Sci. USA 83, 4705-4709.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4705-4709
    • Dozin, B.1    Rall, I.E.2    Nikodem, V.M.3
  • 17
    • 0024542313 scopus 로고
    • Nutritional and hormonal regulation of the gene for avian malic enzyme
    • Goodridge, A. G., Crish, J. F., Hillgartner, F. B., and Wilson, SB. (1989) Nutritional and hormonal regulation of the gene for avian malic enzyme. J. Nutr. 119, 299-308.
    • (1989) J. Nutr. , vol.119 , pp. 299-308
    • Goodridge, A.G.1    Crish, J.F.2    Hillgartner, F.B.3    Wilson, S.B.4
  • 19
    • 0027209396 scopus 로고
    • Regulation of malicenzyme-gene expression by cAMP and retinoic acid in differentiating brown adipocytes
    • Hernandez, A., Garcia-Jimenez, C., Santisteban, P., and Obregon, M. J. (1993) Regulation of malicenzyme-gene expression by cAMP and retinoic acid in differentiating brown adipocytes. Eur. J. Biochem. 215, 285-290.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 285-290
    • Hernandez, A.1    Garcia-Jimenez, C.2    Santisteban, P.3    Obregon, M.J.4
  • 20
    • 7144238800 scopus 로고
    • Dynamics of the activity of isozymes of malate dehydrogenase in ontogenesis of Drosophila virilis
    • In Russian with English Summary
    • Redkin, P. S. (1970) Dynamics of the activity of isozymes of malate dehydrogenase in ontogenesis of Drosophila virilis. Soviet J. Devel. Biol. 1, 89-94 (In Russian with English Summary).
    • (1970) Soviet J. Devel. Biol. , vol.1 , pp. 89-94
    • Redkin, P.S.1
  • 21
    • 0019990647 scopus 로고
    • Age changes of alcohol dehydrogenase, malate dehydrogenase and lactate dehydrogenase in Drosophila melanogaster
    • In Russian with English Summary
    • Chernik, Y. I., Korytko, O. R., and Belokon, E. M. (1982) Age changes of alcohol dehydrogenase, malate dehydrogenase and lactate dehydrogenase in Drosophila melanogaster. Ontogenez 13, 409-516 (In Russian with English Summary).
    • (1982) Ontogenez , vol.13 , pp. 409-516
    • Chernik, Y.I.1    Korytko, O.R.2    Belokon, E.M.3
  • 22
    • 7144236743 scopus 로고
    • A histochemical and microelectrophoretical study of esterases in the organs and tissues of Drosophila melanogaster during embryo-and larvogenesis. 3. Alcohol and malate dehydrogenases
    • In Russian with English Summary
    • Kaplin, V. S. and Korochkin, L. I. (1987) A histochemical and microelectrophoretical study of esterases in the organs and tissues of Drosophila melanogaster during embryo-and larvogenesis. 3. Alcohol and malate dehydrogenases. Ontogenez 18, 215-220. (In Russian with English Summary).
    • (1987) Ontogenez , vol.18 , pp. 215-220
    • Kaplin, V.S.1    Korochkin, L.I.2
  • 24
    • 0000228635 scopus 로고
    • Effect of dietary sucrose and environmental temperature on fatty acid synthesis in Drosophila melanogaster
    • Geer, B. W. and Perille, T. J. (1977) Effect of dietary sucrose and environmental temperature on fatty acid synthesis in Drosophila melanogaster. Insect Biochem. 7, 371-379.
    • (1977) Insect Biochem. , vol.7 , pp. 371-379
    • Geer, B.W.1    Perille, T.J.2
  • 25
    • 84986532552 scopus 로고
    • Regulation of the oxidative NADP-enzyme tissue levels in Drosophila melanogaster. II. The biochemical basis of dietary carbohydrate and D-glycerate modulation
    • Geer, B. W., Woodward, C. G., and Marshall, S. D. (1978a) Regulation of the oxidative NADP-enzyme tissue levels in Drosophila melanogaster. II. The biochemical basis of dietary carbohydrate and D-glycerate modulation. J. Exp. Zool. 203, 391-402.
    • (1978) J. Exp. Zool. , vol.203 , pp. 391-402
    • Geer, B.W.1    Woodward, C.G.2    Marshall, S.D.3
  • 27
    • 0030624815 scopus 로고    scopus 로고
    • Ecdysone-modulated response of Drosophila cytosolic malate dehydrogenase to juvenile hormone
    • Farkas, R. and Knopp, J. (1997) Ecdysone-modulated response of Drosophila cytosolic malate dehydrogenase to juvenile hormone. Arch. Insect Biochem. Physiol. 35, 71-83.
    • (1997) Arch. Insect Biochem. Physiol. , vol.35 , pp. 71-83
    • Farkas, R.1    Knopp, J.2
  • 28
    • 0031777968 scopus 로고    scopus 로고
    • Genetic and hormonal control of cytosolic malate dehydrogenase activity in Drosohphila melanogaster
    • Farkas, R. and Knopp, J. (1998) Genetic and hormonal control of cytosolic malate dehydrogenase activity in Drosohphila melanogaster. Gen. Physiol. Biophys. 17, 37-50.
    • (1998) Gen. Physiol. Biophys. , vol.17 , pp. 37-50
    • Farkas, R.1    Knopp, J.2
  • 30
    • 0017107648 scopus 로고
    • The suppressor of forked mutation in Drosophila melanogaster: Interaction with lozenge gene
    • Snyder, R. D. and Smith, P. D. (1976) The suppressor of forked mutation in Drosophila melanogaster: interaction with lozenge gene. Biochem. Genet. 14, 611-617.
    • (1976) Biochem. Genet. , vol.14 , pp. 611-617
    • Snyder, R.D.1    Smith, P.D.2
  • 31
    • 0001788245 scopus 로고
    • Developmental studies on two ecdysone deficient mutants of Drosophila melanogaster
    • Klose, W., Gateff, E., Emmerich, H., and Beikirch, H. (1980) Developmental studies on two ecdysone deficient mutants of Drosophila melanogaster. Roux's Arch. Devel. Biol. 189, 57-67.
    • (1980) Roux's Arch. Devel. Biol. , vol.189 , pp. 57-67
    • Klose, W.1    Gateff, E.2    Emmerich, H.3    Beikirch, H.4
  • 32
    • 0002924765 scopus 로고
    • The role of su(f) gene function and ecdysterone in transcription of glue polypeptide mRNAs in Drosophila melanogaster
    • Hansson, L. and Lambertsson, A. (1983) The role of su(f) gene function and ecdysterone in transcription of glue polypeptide mRNAs in Drosophila melanogaster. Mol. Gen. Genet. 192, 395-401.
    • (1983) Mol. Gen. Genet. , vol.192 , pp. 395-401
    • Hansson, L.1    Lambertsson, A.2
  • 33
    • 0007750375 scopus 로고
    • Techniques
    • (Ransome, R., ed.), Amsterdam and New York: Elsevier Biomedical Press
    • Ransome, R. (1982) Techniques, in A Handbook of Drosophila Development (Ransome, R., ed.), Amsterdam and New York: Elsevier Biomedical Press, pp. 1-30.
    • (1982) A Handbook of Drosophila Development , pp. 1-30
    • Ransome, R.1
  • 34
    • 0015278018 scopus 로고
    • Ecdysone induction of puffing in polytene chromosomes of Drosophila melanogaster. Effects of inhibitors of RNA synthesis
    • Ashburner, M. (1972) Ecdysone induction of puffing in polytene chromosomes of Drosophila melanogaster. Effects of inhibitors of RNA synthesis. Exp. Cell Res. 71, 433-440.
    • (1972) Exp. Cell Res. , vol.71 , pp. 433-440
    • Ashburner, M.1
  • 35
    • 0016238930 scopus 로고
    • Sequential gene activation by ecdysone in polytene chromosomes of Drosophila melanogaster. II. The effects of inhibitors of protein synthesis
    • Ashburner, M. (1974) Sequential gene activation by ecdysone in polytene chromosomes of Drosophila melanogaster. II. The effects of inhibitors of protein synthesis. Dev. Biol. 39, 141-157.
    • (1974) Dev. Biol. , vol.39 , pp. 141-157
    • Ashburner, M.1
  • 36
    • 0029085807 scopus 로고
    • Ecdysone regulated RNA synthesis in Drosophila larval salivary glands
    • Farkas, R. (1995) Ecdysone regulated RNA synthesis in Drosophila larval salivary glands. Endocr. Regul. 29, 171-185.
    • (1995) Endocr. Regul. , vol.29 , pp. 171-185
    • Farkas, R.1
  • 37
    • 0014251050 scopus 로고
    • Effect of thyroid hormones on metabolism. II. The effect of adrenalectomy or hypophysectomy on response of rat liver enzyme activities to L-thyroxine injection
    • Freedland, R. A., Avery, E. H., and Taylor, A. R. (1968) Effect of thyroid hormones on metabolism. II. The effect of adrenalectomy or hypophysectomy on response of rat liver enzyme activities to L-thyroxine injection. Can. J. Biochem. 46, 141-150.
    • (1968) Can. J. Biochem. , vol.46 , pp. 141-150
    • Freedland, R.A.1    Avery, E.H.2    Taylor, A.R.3
  • 38
    • 0027000797 scopus 로고
    • Nuclear 3,5,3-triiodothyronine receptors and malic enzyme activity in liver of rats fed fish oil and cocoa butter
    • Knopp, J., Klimeš, I., Brtko, J., Šebōková, E., Bohov, P., Hromadová, M., Langer, P., and Baláž, V. (1992) Nuclear 3,5,3-triiodothyronine receptors and malic enzyme activity in liver of rats fed fish oil and cocoa butter. J. Nutr. Biochem. 3, 587-593.
    • (1992) J. Nutr. Biochem. , vol.3 , pp. 587-593
    • Knopp, J.1    Klimeš, I.2    Brtko, J.3    Šeboková, E.4    Bohov, P.5    Hromadová, M.6    Langer, P.7    Baláž, V.8
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford, M. M. (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
  • 41
    • 0001108680 scopus 로고
    • Hormones and Drosophila development
    • (M. Bate and A. Martinez-Arias eds.); Cold Spring Harbor Press, New York
    • Riddiford, L. M. (1993) Hormones and Drosophila development. In: The Development of Drosophila melanogaster, Volume 2. (M. Bate and A. Martinez-Arias eds.); Cold Spring Harbor Press, New York, pp. 899-939.
    • (1993) The Development of Drosophila Melanogaster, Volume 2 , vol.2 , pp. 899-939
    • Riddiford, L.M.1
  • 43
    • 0016590422 scopus 로고
    • Radioimmunoassay of ecdysone: An application to Drosophila larvae and pupae
    • DeReggi, M. L., Hirn, M. H., and Delaage, M. A. (1975) Radioimmunoassay of ecdysone: an application to Drosophila larvae and pupae. Biochem. Biophys. Res. Commun. 66, 1307-1315.
    • (1975) Biochem. Biophys. Res. Commun. , vol.66 , pp. 1307-1315
    • DeReggi, M.L.1    Hirn, M.H.2    Delaage, M.A.3
  • 44
    • 0017715741 scopus 로고
    • Ecdysone titers during postembryonic development of Drosophila melanogaster
    • Hodgetts, R. B., Sage, B., and O'Connor, J. D. (1977) Ecdysone titers during postembryonic development of Drosophila melanogaster. Devel. Biol. 60, 310-317.
    • (1977) Devel. Biol. , vol.60 , pp. 310-317
    • Hodgetts, R.B.1    Sage, B.2    O'Connor, J.D.3
  • 47
    • 0000044092 scopus 로고
    • Relations between ecdysteroid levels and pupal development in the ecd-1 temperature sensitive mutant of Drosophila melanogaster
    • Belinski-Deutsch, S., Busson, D., Lamour-Audit, C., Porcheron, P., Moriniére, M., and Berreur, P. (1983) Relations between ecdysteroid levels and pupal development in the ecd-1 temperature sensitive mutant of Drosophila melanogaster. J. Insect Physiol. 29, 509-514.
    • (1983) J. Insect Physiol. , vol.29 , pp. 509-514
    • Belinski-Deutsch, S.1    Busson, D.2    Lamour-Audit, C.3    Porcheron, P.4    Moriniére, M.5    Berreur, P.6
  • 48
    • 0019505665 scopus 로고
    • The radioimmune assay of ecdysteroid titres in Drosophila melanogaster
    • Richards, G. P. (1981) The radioimmune assay of ecdysteroid titres in Drosophila melanogaster. Mol. Cell. Endocrinol. 21, 181-197.
    • (1981) Mol. Cell. Endocrinol. , vol.21 , pp. 181-197
    • Richards, G.P.1
  • 50
    • 0019502888 scopus 로고
    • Genetic and cytogenetic studies of malic enzyme in Drosophila melanogaster
    • Voelker, R. A., Ohnishi, S., Langley, C. H., Gausz, J., and Gyurkovics, H. (1981) Genetic and cytogenetic studies of malic enzyme in Drosophila melanogaster. Biochem. Genet. 19, 525-534.
    • (1981) Biochem. Genet. , vol.19 , pp. 525-534
    • Voelker, R.A.1    Ohnishi, S.2    Langley, C.H.3    Gausz, J.4    Gyurkovics, H.5
  • 51
    • 0021214478 scopus 로고
    • Characterization of allozyme null and low activity alleles from two natural populations of Drosophila melanogaster
    • Burkhart, B. D., Montgomery, E., Langley, C. H., and Voelker, R. A. (1984) Characterization of allozyme null and low activity alleles from two natural populations of Drosophila melanogaster. Genetics 107, 295-306.
    • (1984) Genetics , vol.107 , pp. 295-306
    • Burkhart, B.D.1    Montgomery, E.2    Langley, C.H.3    Voelker, R.A.4
  • 52
    • 0024078281 scopus 로고
    • Enzymes as biosensors. 2: Hysteretic response of chloroplastic fructose-1,6-biphosphatase to fructose-2,6-biphosphate
    • Soulie, J.-M., Riviere, M., and Ricard, J. (1988) Enzymes as biosensors. 2: Hysteretic response of chloroplastic fructose-1,6-biphosphatase to fructose-2,6-biphosphate. Eur. J. Biochem. 176, 111-117.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 111-117
    • Soulie, J.-M.1    Riviere, M.2    Ricard, J.3
  • 53
    • 0024414261 scopus 로고
    • H-induced bistable dynamic behaviour in the reaction catalysed by glucose-6-phosphate dehydrogenase and conformational hysteresis of the enzyme
    • Aon, M. A., Cortassa, S., Hervagault, J. F., and Thomas, D. (1989) pH-induced bistable dynamic behaviour in the reaction catalysed by glucose-6-phosphate dehydrogenase and conformational hysteresis of the enzyme. Biochem. J. 262, 795-800.
    • (1989) Biochem. J. , vol.262 , pp. 795-800
    • Aon, M.A.1    Cortassa, S.2    Hervagault, J.F.3    Thomas, D.4
  • 54
    • 0025279176 scopus 로고
    • Hysteresis of plant cell-wall β-glucosidase
    • Cheron, G., Noat, G., and Ricard, J. (1990) Hysteresis of plant cell-wall β-glucosidase. Biochem. J. 269, 389-392.
    • (1990) Biochem. J. , vol.269 , pp. 389-392
    • Cheron, G.1    Noat, G.2    Ricard, J.3
  • 55
    • 0022457018 scopus 로고
    • Adaptation of Drosophila enzymes to temperature. V. Heat shock effect on the malate dehydrogenase of Drosophila melanogaster
    • Goulielmos, G., Kilias, G., and Alahiotis, S. N. (1986) Adaptation of Drosophila enzymes to temperature. V. Heat shock effect on the malate dehydrogenase of Drosophila melanogaster. Comp. Biochem. Physiol. B 85, 229-234.
    • (1986) Comp. Biochem. Physiol. B , vol.85 , pp. 229-234
    • Goulielmos, G.1    Kilias, G.2    Alahiotis, S.N.3
  • 56
    • 0033619231 scopus 로고    scopus 로고
    • The origins of insect metamorphosis
    • Truman, J. W. and Riddiford, L. M. (1999) The origins of insect metamorphosis. Nature 401, 447-452.
    • (1999) Nature , vol.401 , pp. 447-452
    • Truman, J.W.1    Riddiford, L.M.2
  • 57
    • 0024291493 scopus 로고
    • Juvenile hormone action mediated in male accessory glands of Drosophila by calcium and kinase C
    • Yamamoto, K., Chadarevian, A., and Pellegrini, M. (1989) Juvenile hormone action mediated in male accessory glands of Drosophila by calcium and kinase C. Science 239, 916-919.
    • (1989) Science , vol.239 , pp. 916-919
    • Yamamoto, K.1    Chadarevian, A.2    Pellegrini, M.3
  • 58
    • 0016906054 scopus 로고
    • Juvenile hormone regulation of cyclic AMP and cAMP phosphodiesterase activity in Oncopeltus fasciatus
    • Everson, R. D. and Feir, D. (1976) Juvenile hormone regulation of cyclic AMP and cAMP phosphodiesterase activity in Oncopeltus fasciatus. J. Insect Physiol. 22, 781-784.
    • (1976) J. Insect Physiol. , vol.22 , pp. 781-784
    • Everson, R.D.1    Feir, D.2
  • 59
    • 0025139156 scopus 로고
    • Allatostatic regulation of juvenile hormone production in vitro by the ring gland of Drosophila melanogaster
    • Richard, D. S., Applebaum, S. W., and Gilbert, L. I. (1990) Allatostatic regulation of juvenile hormone production in vitro by the ring gland of Drosophila melanogaster. Mol. Cell. Endocrinol. 68, 153-161.
    • (1990) Mol. Cell. Endocrinol. , vol.68 , pp. 153-161
    • Richard, D.S.1    Applebaum, S.W.2    Gilbert, L.I.3
  • 60
    • 0021464992 scopus 로고
    • Evidence that levels of malate dehydrogenase and fumarase are increased by cAMP in rat myotubes
    • Lawrence, J. C. Jr. and Salsgiver, W. J. (1984) Evidence that levels of malate dehydrogenase and fumarase are increased by cAMP in rat myotubes. Am. J. Physiol. 247, C33-38.
    • (1984) Am. J. Physiol. , vol.247
    • Lawrence Jr., J.C.1    Salsgiver, W.J.2
  • 61
    • 0032911230 scopus 로고    scopus 로고
    • Glucocorticoids increase retinoid-X receptora expression and enhance thyroid hormone action in primary cultured rat hepatocytes
    • Yamaguchi, S., Murata, Y., Nagaya, T., Hayashi, Y., Ohmori, S., Nimura, Y. and Seo, H. (1999) Glucocorticoids increase retinoid-X receptora expression and enhance thyroid hormone action in primary cultured rat hepatocytes. J. Mol. Endocrinol. 22, 81-90.
    • (1999) J. Mol. Endocrinol. , vol.22 , pp. 81-90
    • Yamaguchi, S.1    Murata, Y.2    Nagaya, T.3    Hayashi, Y.4    Ohmori, S.5    Nimura, Y.6    Seo, H.7
  • 62
    • 0025756824 scopus 로고
    • Triiodothyronine stimulates and cyclic AMP inhibits transcription of the gene for malic enzyme in chick embryo hepatocytes in culture
    • Salati, L. M., Ma, X. J., McCormick, C. C., Stapleton, S. R., and Goodridge, A. G. (1991) Triiodothyronine stimulates and cyclic AMP inhibits transcription of the gene for malic enzyme in chick embryo hepatocytes in culture. J. Biol. Chem. 266, 4010-4016.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4010-4016
    • Salati, L.M.1    Ma, X.J.2    McCormick, C.C.3    Stapleton, S.R.4    Goodridge, A.G.5
  • 63
    • 0030818366 scopus 로고    scopus 로고
    • Cyclic AMP-mediated inhibition of transcription of the malic enzyme gene in chick embryo hepatocytes in culture. Characterization of a cis-acting element far upstream of the promoter
    • Mounier, C., Chen, W., Klautky, S. A., and Goodridge, A. G. (1997) Cyclic AMP-mediated inhibition of transcription of the malic enzyme gene in chick embryo hepatocytes in culture. Characterization of a cis-acting element far upstream of the promoter. J. Biol. Chem. 272, 23,606-23,615.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23606-23615
    • Mounier, C.1    Chen, W.2    Klautky, S.A.3    Goodridge, A.G.4
  • 64
    • 0017148539 scopus 로고
    • Hysteresis at an electrochemical membrane model and its possible role in circulation research
    • Mager, P. P. (1976) Hysteresis at an electrochemical membrane model and its possible role in circulation research. Arzneimittelforschung 26, 1818-1819.
    • (1976) Arzneimittelforschung , vol.26 , pp. 1818-1819
    • Mager, P.P.1
  • 65
    • 0021324378 scopus 로고
    • Studies on the mechanism of inhibition of amphibian oocyte adenylate cyclase by progesterone
    • Jordana, X., Olate, J., Allende, C. C., and Allende, J. E. (1984) Studies on the mechanism of inhibition of amphibian oocyte adenylate cyclase by progesterone. Arch. Biochem. Biophys. 228, 379-387.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 379-387
    • Jordana, X.1    Olate, J.2    Allende, C.C.3    Allende, J.E.4
  • 66
    • 0024519928 scopus 로고
    • Bistability and control for ATP synthase and adenylate cyclase is obtained by the removal of substrate inhibition
    • Schiffmann, Y. (1989) Bistability and control for ATP synthase and adenylate cyclase is obtained by the removal of substrate inhibition. Mol. Cell. Biochem. 86, 19-40.
    • (1989) Mol. Cell. Biochem. , vol.86 , pp. 19-40
    • Schiffmann, Y.1
  • 67
    • 0025320588 scopus 로고
    • The expression of cAMP-dependent protein kinase subunits in primary rat hepatocyte cultures. Cyclic AMP down-regulates its own effector system by decreasing the amount of catalytic subunit and increasing the mRNAs for the inhibitory (R) subunits of cAMP-dependent protein kinase
    • Houge, G., Vintermyr, O. K., and Doskeland, S. O. (1990) The expression of cAMP-dependent protein kinase subunits in primary rat hepatocyte cultures. Cyclic AMP down-regulates its own effector system by decreasing the amount of catalytic subunit and increasing the mRNAs for the inhibitory (R) subunits of cAMP-dependent protein kinase. Mol. Endocrinol. 4, 481-488.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 481-488
    • Houge, G.1    Vintermyr, O.K.2    Doskeland, S.O.3
  • 68
    • 0019449001 scopus 로고
    • Cyclic AMP-mediated control of lipogenic enzyme synthesis during adipose differentiation of 3T3 cells
    • Spiegelman, B. M. and Green, H. (1981) Cyclic AMP-mediated control of lipogenic enzyme synthesis during adipose differentiation of 3T3 cells. Cell 24, 503-510.
    • (1981) Cell , vol.24 , pp. 503-510
    • Spiegelman, B.M.1    Green, H.2
  • 69
    • 0014208265 scopus 로고
    • Purification and properties of tuna supernatant and mitochondrial malate dehydrogenases
    • Kitto, G. B. and Lewis, R. G. (1967) Purification and properties of tuna supernatant and mitochondrial malate dehydrogenases. Biochim. Biophys. Acta 139, 1-15.
    • (1967) Biochim. Biophys. Acta , vol.139 , pp. 1-15
    • Kitto, G.B.1    Lewis, R.G.2
  • 70
    • 0014057424 scopus 로고
    • Malate dehydrogenases. I.A survey of molecular size measured by gel filtration
    • Murphey, W. H., Kitto, G. B., Everse, J. and Kaplan, N. (1967) Malate dehydrogenases. I.A survey of molecular size measured by gel filtration. Biochemistry 6, 603-610.
    • (1967) Biochemistry , vol.6 , pp. 603-610
    • Murphey, W.H.1    Kitto, G.B.2    Everse, J.3    Kaplan, N.4
  • 71
    • 0014940956 scopus 로고
    • Purification and properties of Drosophila malate dehydrogenases
    • McReynolds M. S. and Kitto G. B. (1970) Purification and properties of Drosophila malate dehydrogenases. Biochim. Biophys. Acta 198, (2),165-175.
    • (1970) Biochim. Biophys. Acta , vol.198 , Issue.2 , pp. 165-175
    • McReynolds, M.S.1    Kitto, G.B.2
  • 72
    • 0015911518 scopus 로고
    • Comparative analysis of malate dehydrogenases of Drosophila melanogaster
    • O'Brien, S. J. (1973) Comparative analysis of malate dehydrogenases of Drosophila melanogaster. Biochem. Genet. 10, 191-205.
    • (1973) Biochem. Genet. , vol.10 , pp. 191-205
    • O'Brien, S.J.1
  • 73
    • 0018345762 scopus 로고
    • Biochemical studies of supernatant malate dehydrogenase allozymes in Drosophila melanogaster
    • Alahiotis, S. (1979) Biochemical studies of supernatant malate dehydrogenase allozymes in Drosophila melanogaster. Comp. Biochem. Physiol. 62, 375-380.
    • (1979) Comp. Biochem. Physiol. , vol.62 , pp. 375-380
    • Alahiotis, S.1
  • 74
    • 38249029943 scopus 로고
    • Juvenile hormone increases mitochondrial activities in Drosophila cells
    • Stepien, G., Renaud, M., Savre, I., and Durand, R. (1988) Juvenile hormone increases mitochondrial activities in Drosophila cells. Insect Biochem. 18, 313-321.
    • (1988) Insect Biochem. , vol.18 , pp. 313-321
    • Stepien, G.1    Renaud, M.2    Savre, I.3    Durand, R.4
  • 75
    • 0001571896 scopus 로고
    • Pharmacology of insect juvenile hormones
    • Kerkut, G. A. & Gilbert, L. I., eds. Press, Oxford & New York
    • Sláma, K. (1985) Pharmacology of insect juvenile hormones. In: Kerkut, G. A. & Gilbert, L. I., eds. Comprehensive Insect Physiology, Biochemistry and Pharmacology, vol. 11. Press, Oxford & New York, pp. 357-394.
    • (1985) Comprehensive Insect Physiology, Biochemistry and Pharmacology, Vol. 11 , vol.11 , pp. 357-394
    • Sláma, K.1
  • 76
    • 0014941629 scopus 로고
    • Effects of juvenile hormone on adult differentiation of Drosophila melanogaster
    • Ashburner, M. (1970) Effects of juvenile hormone on adult differentiation of Drosophila melanogaster. Nature 227, 187-189.
    • (1970) Nature , vol.227 , pp. 187-189
    • Ashburner, M.1
  • 77
    • 0028150383 scopus 로고
    • Cellular and molecular actions of juvenile hormone. I. General considerations and premetamorphic actions
    • Riddiford, L. M. (1994) Cellular and molecular actions of juvenile hormone. I. General considerations and premetamorphic actions. Adv. Insect Physiol. 24, 213-274.
    • (1994) Adv. Insect Physiol. , vol.24 , pp. 213-274
    • Riddiford, L.M.1
  • 78
    • 0343050957 scopus 로고
    • A quantitative juvenile hormone assay on Drosophila
    • Postlethwait, J. H. (1973) A quantitative juvenile hormone assay on Drosophila. Dros. Inf. Serv. 50, 135-138.
    • (1973) Dros. Inf. Serv. , vol.50 , pp. 135-138
    • Postlethwait, J.H.1
  • 79
    • 0029715492 scopus 로고    scopus 로고
    • Juvenile hormone: The status of its status quo action
    • Riddiford, L. M. (1996) Juvenile hormone: The status of its status quo action. Arch. Insect Biochem. Physiol. 32, 271-286.
    • (1996) Arch. Insect Biochem. Physiol. , vol.32 , pp. 271-286
    • Riddiford, L.M.1
  • 80
    • 0029138037 scopus 로고
    • Molecular mechanisms of action of juvenile hormone
    • Jones, G. (1995) Molecular mechanisms of action of juvenile hormone. Annu. Rev. Entomol. 40, 147-169.
    • (1995) Annu. Rev. Entomol. , vol.40 , pp. 147-169
    • Jones, G.1
  • 81
    • 0022982337 scopus 로고
    • A Drosophila melanogaster mutant resistant to a chemical analog of juvenile hormone
    • Wilson, T. G. and Fabian, J. (1986) A Drosophila melanogaster mutant resistant to a chemical analog of juvenile hormone. Dev. Biol. 118, 190-201.
    • (1986) Dev. Biol. , vol.118 , pp. 190-201
    • Wilson, T.G.1    Fabian, J.2
  • 82
    • 0023187904 scopus 로고
    • The titre of juvenile hormone during the pupal and adult stages of the life cycle of Drosophila melanogaster
    • Bownes, M. and Rembold, H. (1987) The titre of juvenile hormone during the pupal and adult stages of the life cycle of Drosophila melanogaster. Eur. J. Biochem. 164, 709-712.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 709-712
    • Bownes, M.1    Rembold, H.2
  • 83
    • 0033883124 scopus 로고    scopus 로고
    • The modes of action of juvenile hormones: Some questions we ought to ask
    • Davey, K. G. (2000) The modes of action of juvenile hormones: some questions we ought to ask. Insect Biochem Mol. Biol. 30, 663-669.
    • (2000) Insect Biochem Mol. Biol. , vol.30 , pp. 663-669
    • Davey, K.G.1
  • 84
    • 38249036027 scopus 로고
    • Juvenile hormone in Drosophila. Identification and titer determination during development
    • Sliter, T. J., Sedlak, B. J., Baker, F. C., and Schooley, D. A. (1987) Juvenile hormone in Drosophila. Identification and titer determination during development. Insect Biochem. 17, 161-165.
    • (1987) Insect Biochem. , vol.17 , pp. 161-165
    • Sliter, T.J.1    Sedlak, B.J.2    Baker, F.C.3    Schooley, D.A.4
  • 85
    • 0020353519 scopus 로고
    • Induction of lipogenic enzymes in primary cultures of rat hepatocytes. Relationship between lipogenesis and carbohydrate metabolism
    • Spence, J. T. and Pitot, H. C. (1982) Induction of lipogenic enzymes in primary cultures of rat hepatocytes. Relationship between lipogenesis and carbohydrate metabolism. Eur. J. Biochem. 128, 15-20.
    • (1982) Eur. J. Biochem. , vol.128 , pp. 15-20
    • Spence, J.T.1    Pitot, H.C.2
  • 86
    • 0025086971 scopus 로고
    • Triiodothyronine stimulates transcription of the fatty acid synthase gene in chick embryo hepatocytes in culture. Insulin and insulin-like growth factor amplify that effect
    • Stapleton, S. R., Mitchell, D. A., Salati, L. M., and Goodridge, A. G. (1990) Triiodothyronine stimulates transcription of the fatty acid synthase gene in chick embryo hepatocytes in culture. Insulin and insulin-like growth factor amplify that effect. J. Biol. Chem. 265, 18,442-18,446.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18442-18446
    • Stapleton, S.R.1    Mitchell, D.A.2    Salati, L.M.3    Goodridge, A.G.4
  • 88
    • 0031550514 scopus 로고    scopus 로고
    • Regulation of hepatic stearoyl-CoA desaturase gene 1 by vitamin A
    • Miller, C. W., Waters, K. M., and Ntambi, J. M. (1997) Regulation of hepatic stearoyl-CoA desaturase gene 1 by vitamin A. Biochem. Biophys. Res. Commun. 231, 206-210.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 206-210
    • Miller, C.W.1    Waters, K.M.2    Ntambi, J.M.3
  • 89
    • 0032720636 scopus 로고    scopus 로고
    • Effect of clofibrate on malic enzyme and leptin mRNAs level in rat brown and white adipose tissue
    • Kochan, Z., Karbowska, J., and Swierczynski, J. (1999) Effect of clofibrate on malic enzyme and leptin mRNAs level in rat brown and white adipose tissue. Horm. Metab. Res. 31, 538-542.
    • (1999) Horm. Metab. Res. , vol.31 , pp. 538-542
    • Kochan, Z.1    Karbowska, J.2    Swierczynski, J.3
  • 90
    • 0032871502 scopus 로고    scopus 로고
    • Regulation of stearoyl-CoA desaturase by polyunsaturated fatty acids and cholesterol
    • Ntambi, J. M. (1999) Regulation of stearoyl-CoA desaturase by polyunsaturated fatty acids and cholesterol. J. Lipid Res. 40, 1549-1558.
    • (1999) J. Lipid Res. , vol.40 , pp. 1549-1558
    • Ntambi, J.M.1
  • 91
    • 0029139985 scopus 로고
    • Effects of JH-III and JH-analogs on phase-related growth, egg maturation and lipid metabolism in Schistocerca gregaria females
    • Schneider, M., Wiesel, G., and Dorn, A. (1995) Effects of JH-III and JH-analogs on phase-related growth, egg maturation and lipid metabolism in Schistocerca gregaria females. J. Insect Physiol. 41, 23-31.
    • (1995) J. Insect Physiol. , vol.41 , pp. 23-31
    • Schneider, M.1    Wiesel, G.2    Dorn, A.3
  • 93
    • 0013804754 scopus 로고
    • Effect of saturated fat diets on rat liver NADP-linked enzymes
    • Tepperman, H. M. and Tepperman, J. (1965) Effect of saturated fat diets on rat liver NADP-linked enzymes. Am. J. Physiol. 209, 773-780.
    • (1965) Am. J. Physiol. , vol.209 , pp. 773-780
    • Tepperman, H.M.1    Tepperman, J.2
  • 94
    • 0016394810 scopus 로고
    • Dietary induction of hepatic malic enzyme activity: Differentiation of the induction process
    • Stark, M. J. and Frenkel, R. (1974) Dietary induction of hepatic malic enzyme activity: differentiation of the induction process. Life Sci. 14, 1563-1575.
    • (1974) Life Sci. , vol.14 , pp. 1563-1575
    • Stark, M.J.1    Frenkel, R.2
  • 95
    • 0015596348 scopus 로고
    • Dietary regulation of liver glucose- 6-phosphate dehydrogenase in the rat: Starvation and dietary carbohydrate induction
    • Sassoon, H. F., Dror, Y., Watson, J. J., and Johnson B. C. (1973) Dietary regulation of liver glucose- 6-phosphate dehydrogenase in the rat: starvation and dietary carbohydrate induction. J. Nutr. 103, 321-335.
    • (1973) J. Nutr. , vol.103 , pp. 321-335
    • Sassoon, H.F.1    Dror, Y.2    Watson, J.J.3    Johnson, B.C.4
  • 96
    • 0016425785 scopus 로고
    • Possible alternative functions of rat malic enzyme
    • Stark, M. J., Thompson, B., and Frenkel, R. (1975) Possible alternative functions of rat malic enzyme. Arch. Biochem. Physiol. 166, 174-180.
    • (1975) Arch. Biochem. Physiol. , vol.166 , pp. 174-180
    • Stark, M.J.1    Thompson, B.2    Frenkel, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.