메뉴 건너뛰기




Volumn 287, Issue 37, 2012, Pages 31414-31426

Enhanced energy metabolism contributes to the extended life span of calorie-restricted Caenorhabditis elegans

Author keywords

[No Author keywords available]

Indexed keywords

BENEFICIAL EFFECTS; CAENORHABDITIS ELEGANS; CALORIC RESTRICTION; CYTOSOLIC; ELEGANS; ENERGY METABOLISM; ENERGY SOURCE; FATTY ACID METABOLISM; LIFE SPAN; MULTI-DISCIPLINARY APPROACH; NUMBER OF SPECIES; OVER-EXPRESSION; PHOSPHOENOLPYRUVATE CARBOXYKINASE; PHYSIOLOGICAL RESPONSE; QUANTITATIVE PROTEOMICS; RATE-OF-ENERGY; TCA CYCLE; TRICARBOXYLIC ACID CYCLE; UNDERLYING MECHANISM;

EID: 84866110768     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.377275     Document Type: Article
Times cited : (57)

References (76)
  • 1
    • 0030463128 scopus 로고    scopus 로고
    • Female fitness in Drosophila melanogaster. An interaction between the effect of nutrition and of encounter rate with males
    • Chapman, T., and Partridge, L. (1996) Female fitness in Drosophila melanogaster. An interaction between the effect of nutrition and of encounter rate with males. Proc. Biol. Sci. 263, 755-759
    • (1996) Proc. Biol. Sci. , vol.263 , pp. 755-759
    • Chapman, T.1    Partridge, L.2
  • 2
    • 0037111862 scopus 로고    scopus 로고
    • Caloric restriction and aging in primates. Relevance to humans and possible CR mimetics
    • Lane, M. A., Mattison, J., Ingram, D. K., and Roth, G. S. (2002) Caloric restriction and aging in primates. Relevance to humans and possible CR mimetics. Microsc. Res. Tech. 59, 335-338
    • (2002) Microsc. Res. Tech. , vol.59 , pp. 335-338
    • Lane, M.A.1    Mattison, J.2    Ingram, D.K.3    Roth, G.S.4
  • 3
    • 0034033586 scopus 로고    scopus 로고
    • Caloric restriction and aging. An update
    • Masoro, E. J. (2000) Caloric restriction and aging. An update. Exp. Gerontol. 35, 299-305
    • (2000) Exp. Gerontol. , vol.35 , pp. 299-305
    • Masoro, E.J.1
  • 4
    • 0033738362 scopus 로고    scopus 로고
    • An intervention resembling caloric restriction prolongs life span and retards aging in yeast
    • Jiang, J. C., Jaruga, E., Repnevskaya, M. V., and Jazwinski, S. M. (2000) An intervention resembling caloric restriction prolongs life span and retards aging in yeast. FASEB J. 14, 2135-2137
    • (2000) FASEB J. , vol.14 , pp. 2135-2137
    • Jiang, J.C.1    Jaruga, E.2    Repnevskaya, M.V.3    Jazwinski, S.M.4
  • 5
    • 0029684517 scopus 로고    scopus 로고
    • Caloric restriction and aging
    • Weindruch, R. (1996) Caloric restriction and aging. Sci. Am. 274, 46-52
    • (1996) Sci. Am. , vol.274 , pp. 46-52
    • Weindruch, R.1
  • 6
    • 33751407431 scopus 로고    scopus 로고
    • The longevity effect of dietary restriction in Caenorhabditis elegans
    • Houthoofd, K., and Vanfleteren, J. R. (2006) The longevity effect of dietary restriction in Caenorhabditis elegans. Exp. Gerontol. 41, 1026-1031
    • (2006) Exp. Gerontol. , vol.41 , pp. 1026-1031
    • Houthoofd, K.1    Vanfleteren, J.R.2
  • 7
    • 22744445281 scopus 로고    scopus 로고
    • Overview of caloric restriction and ageing
    • Masoro, E. J. (2005) Overview of caloric restriction and ageing. Mech. Ageing Dev. 126, 913-922
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 913-922
    • Masoro, E.J.1
  • 8
    • 0022517746 scopus 로고
    • The retardation of aging in mice by dietary restriction. Longevity, cancer, immunity and lifetime energy intake
    • Weindruch, R., Walford, R. L., Fligiel, S., and Guthrie, D. (1986) The retardation of aging in mice by dietary restriction. Longevity, cancer, immunity and lifetime energy intake. J. Nutr. 116, 641-654
    • (1986) J. Nutr. , vol.116 , pp. 641-654
    • Weindruch, R.1    Walford, R.L.2    Fligiel, S.3    Guthrie, D.4
  • 10
    • 0141611988 scopus 로고    scopus 로고
    • Subfield history. Caloric restriction, slowing aging, and extending life
    • Masoro, E. J. (2003) Subfield history. Caloric restriction, slowing aging, and extending life. Sci. Aging Knowledge Environ. 2003, RE2
    • (2003) Sci. Aging Knowledge Environ. , vol.2003
    • Masoro, E.J.1
  • 11
    • 10644282295 scopus 로고    scopus 로고
    • The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to life span in C. elegans
    • Apfeld, J., O'Connor, G., McDonagh, T., DiStefano, P. S., and Curtis, R. (2004) The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to life span in C. elegans. Genes Dev. 18, 3004-3009
    • (2004) Genes Dev. , vol.18 , pp. 3004-3009
    • Apfeld, J.1    O'Connor, G.2    McDonagh, T.3    DiStefano, P.S.4    Curtis, R.5
  • 12
    • 4544311861 scopus 로고    scopus 로고
    • The TOR pathway interacts with the insulin signaling pathway to regulate C. elegans larval development, metabolism, and life span
    • Jia, K., Chen, D., and Riddle, D. L. (2004) The TOR pathway interacts with the insulin signaling pathway to regulate C. elegans larval development, metabolism, and life span. Development 131, 3897-3906
    • (2004) Development , vol.131 , pp. 3897-3906
    • Jia, K.1    Chen, D.2    Riddle, D.L.3
  • 13
    • 33746245679 scopus 로고    scopus 로고
    • C. elegans 14-3-3 proteins regulate life span and interact with SIR-2.1 and DAF-16/FOXO
    • Wang, Y., Oh, S. W., Deplancke, B., Luo, J., Walhout, A. J., and Tissenbaum, H. A. (2006) C. elegans 14-3-3 proteins regulate life span and interact with SIR-2.1 and DAF-16/FOXO. Mech. Ageing Dev. 127, 741-747
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 741-747
    • Wang, Y.1    Oh, S.W.2    Deplancke, B.3    Luo, J.4    Walhout, A.J.5    Tissenbaum, H.A.6
  • 14
    • 34249891333 scopus 로고    scopus 로고
    • Two neurons mediate diet restriction-induced longevity in C. elegans
    • Bishop, N. A., and Guarente, L. (2007) Two neurons mediate diet restriction-induced longevity in C. elegans. Nature 447, 545-549
    • (2007) Nature , vol.447 , pp. 545-549
    • Bishop, N.A.1    Guarente, L.2
  • 15
    • 34249888736 scopus 로고    scopus 로고
    • PHA-4/Foxa mediates diet restriction-induced longevity of C. elegans
    • Panowski, S. H., Wolff, S., Aguilaniu, H., Durieux, J., and Dillin, A. (2007) PHA-4/Foxa mediates diet restriction-induced longevity of C. elegans. Nature 447, 550-555
    • (2007) Nature , vol.447 , pp. 550-555
    • Panowski, S.H.1    Wolff, S.2    Aguilaniu, H.3    Durieux, J.4    Dillin, A.5
  • 16
    • 84872219562 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 18
    • 0035942222 scopus 로고    scopus 로고
    • Influences of aging and caloric restriction on the transcriptional profile of skeletal muscle from rhesus monkeys
    • Kayo, T., Allison, D. B., Weindruch, R., and Prolla, T. A. (2001) Influences of aging and caloric restriction on the transcriptional profile of skeletal muscle from rhesus monkeys. Proc. Natl. Acad. Sci. U.S.A. 98, 5093-5098
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5093-5098
    • Kayo, T.1    Allison, D.B.2    Weindruch, R.3    Prolla, T.A.4
  • 19
    • 0033610079 scopus 로고    scopus 로고
    • Gene expression profile of aging and its retardation by caloric restriction
    • Lee, C. K., Klopp, R. G., Weindruch, R., and Prolla, T. A. (1999) Gene expression profile of aging and its retardation by caloric restriction. Science 285, 1390-1393
    • (1999) Science , vol.285 , pp. 1390-1393
    • Lee, C.K.1    Klopp, R.G.2    Weindruch, R.3    Prolla, T.A.4
  • 20
    • 0015319592 scopus 로고
    • The biologic clock. The mitochondria?
    • Harman, D. (1972) The biologic clock. The mitochondria? J. Am. Geriatr. Soc. 20, 145-147
    • (1972) J. Am. Geriatr. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 22
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 23
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fly allows for accurate protein quantification in vivo
    • Sury, M. D., Chen, J. X., and Selbach, M. (2010) The SILAC fly allows for accurate protein quantification in vivo. Mol. Cell. Proteomics 9, 2173-2183
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.X.2    Selbach, M.3
  • 27
    • 0027528788 scopus 로고
    • The genetics of feeding in Caenorhabditis elegans
    • Avery, L. (1993) The genetics of feeding in Caenorhabditis elegans. Genetics 133, 897-917
    • (1993) Genetics , vol.133 , pp. 897-917
    • Avery, L.1
  • 28
    • 0032573178 scopus 로고    scopus 로고
    • The genetics of caloric restriction in Caenorhabditis elegans
    • Lakowski, B., and Hekimi, S. (1998) The genetics of caloric restriction in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 95, 13091-13096
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13091-13096
    • Lakowski, B.1    Hekimi, S.2
  • 29
    • 38449085292 scopus 로고    scopus 로고
    • Maintenance of C. elegans
    • Stiernagle, T. (2006) Maintenance of C. elegans. WormBook, 1-11
    • (2006) WormBook , pp. 1-11
    • Stiernagle, T.1
  • 30
    • 0025942107 scopus 로고
    • Efficient gene transfer in C. elegans. Extrachromosomal maintenance and integration of transforming sequences
    • Mello, C. C., Kramer, J. M., Stinchcomb, D., and Ambros, V. (1991) Efficient gene transfer in C. elegans. Extrachromosomal maintenance and integration of transforming sequences. EMBO J. 10, 3959-3970
    • (1991) EMBO J. , vol.10 , pp. 3959-3970
    • Mello, C.C.1    Kramer, J.M.2    Stinchcomb, D.3    Ambros, V.4
  • 31
    • 78651233674 scopus 로고    scopus 로고
    • Perfluorooctanoic acid for shotgun proteomics
    • Kadiyala, C. S., Tomechko, S. E., and Miyagi, M. (2010) Perfluorooctanoic acid for shotgun proteomics. PLoS One 5, e15332
    • (2010) PLoS One , vol.5
    • Kadiyala, C.S.1    Tomechko, S.E.2    Miyagi, M.3
  • 32
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974) The genetics of Caenorhabditis elegans. Genetics 77, 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 34
    • 0036498771 scopus 로고    scopus 로고
    • Isolation of hepatic mitochondrial contact sites. Previously unrecognized inner membrane components
    • Hoppel, C., Kerner, J., Turkaly, P., Minkler, P., and Tandler, B. (2002) Isolation of hepatic mitochondrial contact sites. Previously unrecognized inner membrane components. Anal. Biochem. 302, 60-69
    • (2002) Anal. Biochem. , vol.302 , pp. 60-69
    • Hoppel, C.1    Kerner, J.2    Turkaly, P.3    Minkler, P.4    Tandler, B.5
  • 35
    • 0014691151 scopus 로고
    • Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase
    • Ballard, F. J., and Hanson, R. W. (1969) Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase. J. Biol. Chem. 244, 5625-5630
    • (1969) J. Biol. Chem. , vol.244 , pp. 5625-5630
    • Ballard, F.J.1    Hanson, R.W.2
  • 36
    • 79960402453 scopus 로고    scopus 로고
    • Mitochondrial carnitine palmitoyltransferase 1a is part of an outer membrane fatty acid transfer complex
    • Lee, K., Kerner, J., and Hoppel, C. L. (2011) Mitochondrial carnitine palmitoyltransferase 1a is part of an outer membrane fatty acid transfer complex. J. Biol. Chem. 286, 25655-25662
    • (2011) J. Biol. Chem. , vol.286 , pp. 25655-25662
    • Lee, K.1    Kerner, J.2    Hoppel, C.L.3
  • 37
    • 65449129608 scopus 로고    scopus 로고
    • Post-translational modifications of mitochondrial outer membrane proteins
    • Distler, A. M., Kerner, J., Lee, K., and Hoppel, C. L. (2009) Post-translational modifications of mitochondrial outer membrane proteins. Methods Enzymol. 457, 97-115
    • (2009) Methods Enzymol. , vol.457 , pp. 97-115
    • Distler, A.M.1    Kerner, J.2    Lee, K.3    Hoppel, C.L.4
  • 38
    • 0014607074 scopus 로고
    • Dietary protein and the control of fatty acid synthesis in rat adipose tissue
    • Jomain, M., and Hanson, R. W. (1969) Dietary protein and the control of fatty acid synthesis in rat adipose tissue. J. Lipid Res. 10, 674-680
    • (1969) J. Lipid Res. , vol.10 , pp. 674-680
    • Jomain, M.1    Hanson, R.W.2
  • 39
    • 0014124329 scopus 로고
    • Phosphoenolpyruvate carboxykinase and pyruvate carboxylase in developing rat liver
    • Ballard, F. J., and Hanson, R. W. (1967) Phosphoenolpyruvate carboxykinase and pyruvate carboxylase in developing rat liver. Biochem. J. 104, 866-871
    • (1967) Biochem. J. , vol.104 , pp. 866-871
    • Ballard, F.J.1    Hanson, R.W.2
  • 40
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • Hsu, A. L., Murphy, C. T., and Kenyon, C. (2003) Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 300, 1142-1145
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 41
    • 0027771804 scopus 로고
    • A C. elegans mutant that lives twice as long as wild type
    • Kenyon, C., Chang, J., Gensch, E., Rudner, A., and Tabtiang, R. (1993) A C. elegans mutant that lives twice as long as wild type. Nature 366, 461-464
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 42
    • 0014184339 scopus 로고
    • Revised linkage map of Escherichia coli
    • Taylor, A. L., and Trotter, C. D. (1967) Revised linkage map of Escherichia coli. Bacteriol. Rev. 31, 332-353
    • (1967) Bacteriol. Rev. , vol.31 , pp. 332-353
    • Taylor, A.L.1    Trotter, C.D.2
  • 43
    • 0021105027 scopus 로고
    • Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis
    • Jekel, P. A., Weijer, W. J., and Beintema, J. J. (1983) Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis. Anal. Biochem. 134, 347-354
    • (1983) Anal. Biochem. , vol.134 , pp. 347-354
    • Jekel, P.A.1    Weijer, W.J.2    Beintema, J.J.3
  • 45
    • 0344392858 scopus 로고    scopus 로고
    • Mutations in a β-tubulin disrupt spindle orientation and microtubule dynamics in the early Caenorhabditis elegans embryo
    • Wright, A. J., and Hunter, C. P. (2003) Mutations in a β-tubulin disrupt spindle orientation and microtubule dynamics in the early Caenorhabditis elegans embryo. Mol. Biol. Cell 14, 4512-4525
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4512-4525
    • Wright, A.J.1    Hunter, C.P.2
  • 48
    • 33751350245 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase mediates anoxia response and survival in Caenorhabditis elegans
    • Mendenhall, A. R., LaRue, B., and Padilla, P. A. (2006) Glyceraldehyde-3-phosphate dehydrogenase mediates anoxia response and survival in Caenorhabditis elegans. Genetics 174, 1173-1187
    • (2006) Genetics , vol.174 , pp. 1173-1187
    • Mendenhall, A.R.1    LaRue, B.2    Padilla, P.A.3
  • 49
    • 26444442036 scopus 로고    scopus 로고
    • A Caenorhabditis elegans nutrient response system partially dependent on nuclear receptor NHR-49
    • Van Gilst, M. R., Hadjivassiliou, H., and Yamamoto, K. R. (2005) A Caenorhabditis elegans nutrient response system partially dependent on nuclear receptor NHR-49. Proc. Natl. Acad. Sci. U.S.A. 102, 13496-13501
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13496-13501
    • Van Gilst, M.R.1    Hadjivassiliou, H.2    Yamamoto, K.R.3
  • 50
    • 0035209841 scopus 로고    scopus 로고
    • Characterization of a cadmium-inducible isoform of pyruvate carboxylase from Caenorhabditis elegans
    • Liao, V. H., and Freedman, J. H. (2001) Characterization of a cadmium-inducible isoform of pyruvate carboxylase from Caenorhabditis elegans. DNA Seq. 12, 137-145
    • (2001) DNA Seq. , vol.12 , pp. 137-145
    • Liao, V.H.1    Freedman, J.H.2
  • 52
    • 68749099747 scopus 로고    scopus 로고
    • Caenorhabditis elegans utilizes dauer pheromone biosynthesis to dispose of toxic peroxisomal fatty acids for cellular homoeostasis
    • Joo, H. J., Yim, Y. H., Jeong, P. Y., Jin, Y. X., Lee, J. E., Kim, H., Jeong, S. K., Chitwood, D. J., and Paik, Y. K. (2009) Caenorhabditis elegans utilizes dauer pheromone biosynthesis to dispose of toxic peroxisomal fatty acids for cellular homoeostasis. Biochem. J. 422, 61-71
    • (2009) Biochem. J. , vol.422 , pp. 61-71
    • Joo, H.J.1    Yim, Y.H.2    Jeong, P.Y.3    Jin, Y.X.4    Lee, J.E.5    Kim, H.6    Jeong, S.K.7    Chitwood, D.J.8    Paik, Y.K.9
  • 53
    • 34250759430 scopus 로고    scopus 로고
    • Fatty acid desaturation and the regulation of adiposity in Caenorhabditis elegans
    • Brock, T. J., Browse, J., and Watts, J. L. (2007) Fatty acid desaturation and the regulation of adiposity in Caenorhabditis elegans. Genetics 176, 865-875
    • (2007) Genetics , vol.176 , pp. 865-875
    • Brock, T.J.1    Browse, J.2    Watts, J.L.3
  • 54
    • 77950818315 scopus 로고    scopus 로고
    • Purification, crystallization, and preliminary crystallographic analysis of very long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans
    • Li, Z., Zhai, Y., Fang, J., Zhou, Q., Geng, Y., and Sun, F. (2010) Purification, crystallization, and preliminary crystallographic analysis of very long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 426-430
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.66 , pp. 426-430
    • Li, Z.1    Zhai, Y.2    Fang, J.3    Zhou, Q.4    Geng, Y.5    Sun, F.6
  • 55
    • 0028099294 scopus 로고
    • Cloning by synteny. Identifying C. briggsae homologs of C. elegans genes
    • Kuwabara, P. E., and Shah, S. (1994) Cloning by synteny. Identifying C. briggsae homologs of C. elegans genes. Nucleic Acids Res. 22, 4414-4418
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4414-4418
    • Kuwabara, P.E.1    Shah, S.2
  • 56
    • 0031830508 scopus 로고    scopus 로고
    • Caenorhabditis elegans SUR-5, a novel but conserved protein, negatively regulates LET-60 Ras activity during vulval induction
    • Gu, T., Orita, S., and Han, M. (1998) Caenorhabditis elegans SUR-5, a novel but conserved protein, negatively regulates LET-60 Ras activity during vulval induction. Mol. Cell. Biol. 18, 4556-4564
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4556-4564
    • Gu, T.1    Orita, S.2    Han, M.3
  • 57
    • 0035872880 scopus 로고    scopus 로고
    • Pod-2, along with pod-1, defines a new class of genes required for polarity in the early Caenorhabditis elegans embryo
    • Tagawa, A., Rappleye, C. A., and Aroian, R. V. (2001) Pod-2, along with pod-1, defines a new class of genes required for polarity in the early Caenorhabditis elegans embryo. Dev. Biol. 233, 412-424
    • (2001) Dev. Biol. , vol.233 , pp. 412-424
    • Tagawa, A.1    Rappleye, C.A.2    Aroian, R.V.3
  • 58
    • 48749115206 scopus 로고    scopus 로고
    • Elongation and desaturation of fatty acids are critical in growth, lipid metabolism and ontogeny of Caenorhabditis elegans
    • Horikawa, M., Nomura, T., Hashimoto, T., and Sakamoto, K. (2008) Elongation and desaturation of fatty acids are critical in growth, lipid metabolism and ontogeny of Caenorhabditis elegans. J. Biochem. 144, 149-158
    • (2008) J. Biochem. , vol.144 , pp. 149-158
    • Horikawa, M.1    Nomura, T.2    Hashimoto, T.3    Sakamoto, K.4
  • 60
    • 0020842715 scopus 로고
    • Chemical and catalytic properties of the peroxisomal acyl-coenzyme A oxidase from Candida tropicalis
    • Coudron, P. E., Frerman, F. E., and Schowalter, D. B. (1983) Chemical and catalytic properties of the peroxisomal acyl-coenzyme A oxidase from Candida tropicalis. Arch Biochem. Biophys. 226, 324-336
    • (1983) Arch Biochem. Biophys. , vol.226 , pp. 324-336
    • Coudron, P.E.1    Frerman, F.E.2    Schowalter, D.B.3
  • 61
    • 48749129833 scopus 로고    scopus 로고
    • Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans
    • Calvo, A. C., Pey, A. L., Ying, M., Loer, C. M., and Martinez, A. (2008) Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans. FASEB J. 22, 3046-3058
    • (2008) FASEB J. , vol.22 , pp. 3046-3058
    • Calvo, A.C.1    Pey, A.L.2    Ying, M.3    Loer, C.M.4    Martinez, A.5
  • 62
    • 1542289928 scopus 로고    scopus 로고
    • Functional characterization of Caenorhabditis elegans heteromeric amino acid transporters
    • Veljkovic, E., Stasiuk, S., Skelly, P. J., Shoemaker, C. B., and Verrey, F. (2004) Functional characterization of Caenorhabditis elegans heteromeric amino acid transporters. J. Biol. Chem. 279, 7655-7662
    • (2004) J. Biol. Chem. , vol.279 , pp. 7655-7662
    • Veljkovic, E.1    Stasiuk, S.2    Skelly, P.J.3    Shoemaker, C.B.4    Verrey, F.5
  • 63
    • 0032103560 scopus 로고    scopus 로고
    • Two oligopeptide transporters from Caenorhabditis elegans. Molecular cloning and functional expression
    • Fei, Y. J., Fujita, T., Lapp, D. F., Ganapathy, V., and Leibach, F. H. (1998) Two oligopeptide transporters from Caenorhabditis elegans. Molecular cloning and functional expression. Biochem. J. 332, 565-572
    • (1998) Biochem. J. , vol.332 , pp. 565-572
    • Fei, Y.J.1    Fujita, T.2    Lapp, D.F.3    Ganapathy, V.4    Leibach, F.H.5
  • 64
    • 0038817360 scopus 로고    scopus 로고
    • Assessing metabolic activity in aging Caenorhabditis elegans. Concepts and controversies
    • Braeckman, B. P., Houthoofd, K., and Vanfleteren, J. R. (2002) Assessing metabolic activity in aging Caenorhabditis elegans. Concepts and controversies. Aging Cell 1, 82-88
    • (2002) Aging Cell , vol.1 , pp. 82-88
    • Braeckman, B.P.1    Houthoofd, K.2    Vanfleteren, J.R.3
  • 65
    • 0014154920 scopus 로고
    • The relative significance of acetate and glucose as precursors for lipid synthesis in liver and adipose tissue from ruminants
    • Hanson, R. W., and Ballard, F. J. (1967) The relative significance of acetate and glucose as precursors for lipid synthesis in liver and adipose tissue from ruminants. Biochem. J. 105, 529-536
    • (1967) Biochem. J. , vol.105 , pp. 529-536
    • Hanson, R.W.1    Ballard, F.J.2
  • 66
    • 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
    • Ballard, F.J.1    Hanson, R.W.2
  • 68
    • 36248964713 scopus 로고    scopus 로고
    • Gene activities that mediate increased life span of C. elegans insulin-like signaling mutants
    • Samuelson, A. V., Carr, C. E., and Ruvkun, G. (2007) Gene activities that mediate increased life span of C. elegans insulin-like signaling mutants. Genes Dev. 21, 2976-2994
    • (2007) Genes Dev. , vol.21 , pp. 2976-2994
    • Samuelson, A.V.1    Carr, C.E.2    Ruvkun, G.3
  • 69
    • 33645472504 scopus 로고    scopus 로고
    • New genes tied to endocrine, metabolic, and dietary regulation of life span from a Caenorhabditis elegans genomic RNAi screen
    • Hansen, M., Hsu, A. L., Dillin, A., and Kenyon, C. (2005) New genes tied to endocrine, metabolic, and dietary regulation of life span from a Caenorhabditis elegans genomic RNAi screen. PLoS Genet. 1, 119-128
    • (2005) PLoS Genet. , vol.1 , pp. 119-128
    • Hansen, M.1    Hsu, A.L.2    Dillin, A.3    Kenyon, C.4
  • 70
    • 77957226879 scopus 로고    scopus 로고
    • drr-2 encodes an eIF4H that acts downstream of TOR in diet restriction-induced longevity of C. elegans
    • Ching, T. T., Paal, A. B., Mehta, A., Zhong, L., and Hsu, A. L. (2010) drr-2 encodes an eIF4H that acts downstream of TOR in diet restriction-induced longevity of C. elegans. Aging Cell 9, 545-557
    • (2010) Aging Cell , vol.9 , pp. 545-557
    • Ching, T.T.1    Paal, A.B.2    Mehta, A.3    Zhong, L.4    Hsu, A.L.5
  • 71
    • 0021284940 scopus 로고
    • Erythrocytic pyruvate kinase deficiency and hemolytic anemia inherited as a dominant trait
    • Etiemble, J., Picat, C., Dhermy, D., Buc, H. A., Morin, M., and Boivin, P. (1984) Erythrocytic pyruvate kinase deficiency and hemolytic anemia inherited as a dominant trait. Am. J. Hematol. 17, 251-260
    • (1984) Am. J. Hematol. , vol.17 , pp. 251-260
    • Etiemble, J.1    Picat, C.2    Dhermy, D.3    Buc, H.A.4    Morin, M.5    Boivin, P.6
  • 72
    • 0015407768 scopus 로고
    • Chronic hemolytic anemia associated with erythrocyte enolase deficiency exacerbated by ingestion of nitrofurantoin
    • Stefanini, M. (1972) Chronic hemolytic anemia associated with erythrocyte enolase deficiency exacerbated by ingestion of nitrofurantoin. Am. J. Clin. Pathol. 58, 408-414
    • (1972) Am. J. Clin. Pathol. , vol.58 , pp. 408-414
    • Stefanini, M.1
  • 74
    • 0017249130 scopus 로고
    • Gluconeogenesis in infancy and childhood. III. Deficiency of the extramitochondrial form of hepatic phosphoenolpyruvate carboxykinase in a case of persistent neonatal hypoglycemia
    • Vidnes, J., and Sovik, O. (1976) Gluconeogenesis in infancy and childhood. III. Deficiency of the extramitochondrial form of hepatic phosphoenolpyruvate carboxykinase in a case of persistent neonatal hypoglycemia. Acta Paediatr. Scand. 65, 307-312
    • (1976) Acta Paediatr. Scand. , vol.65 , pp. 307-312
    • Vidnes, J.1    Sovik, O.2
  • 76
    • 76549174860 scopus 로고
    • The control of biochemical reactions
    • Changeux, J. P. (1965) The control of biochemical reactions. Sci. Am. 212, 36-45
    • (1965) Sci. Am. , vol.212 , pp. 36-45
    • Changeux, J.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.