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Volumn 134, Issue 6 SUPPL., 2004, Pages

Advancing age and other factors influencing the balance between amino acid requirements and toxicity

Author keywords

Aging; Cysteine; Glutathione; Methionine; Methyl groups; Sulfur amino acids

Indexed keywords

AMINO ACID; CYSTEINE; GENOMIC DNA; GLUTATHIONE; HOMOCYSTEINE; METHIONINE; METHYL GROUP; SULFUR AMINO ACID;

EID: 2642544983     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/134.6.1569s     Document Type: Conference Paper
Times cited : (26)

References (59)
  • 2
    • 0030897107 scopus 로고    scopus 로고
    • Splanchnic and whole-body leucine kinetics in young and elderly men
    • Boirie, Y., Gachon, P. & Beaufrère, B. (1997) Splanchnic and whole-body leucine kinetics in young and elderly men. Am. J. Clin. Nutr. 65: 489-495.
    • (1997) Am. J. Clin. Nutr. , vol.65 , pp. 489-495
    • Boirie, Y.1    Gachon, P.2    Beaufrère, B.3
  • 3
    • 0030996515 scopus 로고    scopus 로고
    • Protein requirements and ageing: Metabolic demand and efficiency of utilization
    • Fereday, A., Gibson, N. R., Cox, M. D., Pacy, P. J. & Millward, D.J. (1997) Protein requirements and ageing: metabolic demand and efficiency of utilization. Br. J. Nutr. 77: 685-702.
    • (1997) Br. J. Nutr. , vol.77 , pp. 685-702
    • Fereday, A.1    Gibson, N.R.2    Cox, M.D.3    Pacy, P.J.4    Millward, D.J.5
  • 5
    • 0033924017 scopus 로고    scopus 로고
    • Nitrogen and amino acid requirements: The Massachusetts Institute of Technology amino acid requirement pattern
    • Young, V. R. & Borgonha, S. (2000) Nitrogen and amino acid requirements: the Massachusetts Institute of Technology amino acid requirement pattern. J. Nutr. 130: 1841S-1849S.
    • (2000) J. Nutr. , vol.130
    • Young, V.R.1    Borgonha, S.2
  • 6
    • 0028149323 scopus 로고
    • Increased protein requirements in elderly people: New data and retrospective reassessments
    • Campbell, W. W., Crim, M. C., Dallal, G. E., Young, V. R. & Evans, W. J. (1994) Increased protein requirements in elderly people: new data and retrospective reassessments. Am. J. Clin. Nutr. 60: 501-509.
    • (1994) Am. J. Clin. Nutr. , vol.60 , pp. 501-509
    • Campbell, W.W.1    Crim, M.C.2    Dallal, G.E.3    Young, V.R.4    Evans, W.J.5
  • 7
    • 0014931232 scopus 로고
    • Absence of cystathionase in human fetal liver. Is cystine essential?
    • Sturman, J. A., Gaull, G. E. & Raiha, N.C.R. (1970) Absence of cystathionase in human fetal liver. Is cystine essential? Science 169: 74-76.
    • (1970) Science , vol.169 , pp. 74-76
    • Sturman, J.A.1    Gaull, G.E.2    Raiha, N.C.R.3
  • 8
    • 0031598766 scopus 로고    scopus 로고
    • Amino acids in pediatric and neonatal nutrition
    • Heird, W. C. (1998) Amino acids in pediatric and neonatal nutrition. Curr. Opin. Clin. Nutr. Metab. Care 1: 73-78.
    • (1998) Curr. Opin. Clin. Nutr. Metab. Care , vol.1 , pp. 73-78
    • Heird, W.C.1
  • 9
    • 0035195248 scopus 로고    scopus 로고
    • Methylation demand and homocysteine metabolism: Effects of dietary provision of creatine and guanidinoacetate
    • Stead, L. M., Au, K. P., Jacobs, R. L., Brosnan, M. E. & Brosnan, J. T. (2001) Methylation demand and homocysteine metabolism: effects of dietary provision of creatine and guanidinoacetate. Am. J. Physiol. Endocrinol. Metab. 281: E1096-E1100.
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.281
    • Stead, L.M.1    Au, K.P.2    Jacobs, R.L.3    Brosnan, M.E.4    Brosnan, J.T.5
  • 10
    • 0027753175 scopus 로고
    • Methionine synthase inactivation by nitrous oxide during methionine loading of normal human fibroblasts. Homocysteine remethylation as determinant of enzyme inactivation and homocysteine export
    • Christensen, B. & Ueland, P. M. (1993) Methionine synthase inactivation by nitrous oxide during methionine loading of normal human fibroblasts. Homocysteine remethylation as determinant of enzyme inactivation and homocysteine export. J. Pharmacol. Exp. Ther. 267: 1298-1303.
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 1298-1303
    • Christensen, B.1    Ueland, P.M.2
  • 11
    • 0036328453 scopus 로고    scopus 로고
    • Gene-nutrient interactions and DNA methylation
    • Friso, S. (2002) Gene-nutrient interactions and DNA methylation. J. Nutr. 132: 2382S-2387S.
    • (2002) J. Nutr. , vol.132
    • Friso, S.1
  • 12
    • 0037372003 scopus 로고    scopus 로고
    • Epigenetic regulation of gene expression: How the genome integrates intrinsic and environmental signals
    • Jaenisch, R. & Bird, A. (2003) Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals. Nat. Genet. 33: 245-254.
    • (2003) Nat. Genet. , vol.33 , pp. 245-254
    • Jaenisch, R.1    Bird, A.2
  • 13
    • 0036328026 scopus 로고    scopus 로고
    • Role of DNA methylation in the regulation of cell function: Autoimmunity, aging and cancer
    • Richardson, B. C. (2002) Role of DNA methylation in the regulation of cell function: autoimmunity, aging and cancer. J. Nutr. 132: 2401S-2405S.
    • (2002) J. Nutr. , vol.132
    • Richardson, B.C.1
  • 14
    • 0022000776 scopus 로고
    • A fraction of the mouse genome that is derived from islands of nonmethylated, CpG-rich DNA
    • Bird, A., Taggart, M., Frommer, M., Miller, O. J. & Macleod, D. (1985) A fraction of the mouse genome that is derived from islands of nonmethylated, CpG-rich DNA. Cell 40: 91-99.
    • (1985) Cell , vol.40 , pp. 91-99
    • Bird, A.1    Taggart, M.2    Frommer, M.3    Miller, O.J.4    Macleod, D.5
  • 15
    • 0027141519 scopus 로고
    • Number of CpG islands and genes in human and mouse
    • Antequera, F. & Bird, A. (1993) Number of CpG islands and genes in human and mouse. Proc. Natl. Acad. Sci. USA 90: 11995-11999.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11995-11999
    • Antequera, F.1    Bird, A.2
  • 16
    • 0032770313 scopus 로고    scopus 로고
    • Progressive region-specific de novo methylation of the p16 CpG island in primary human mammary epithelial cell strains during escape from M(O) growth arrest
    • Wong, D. J., Foster, S. A., Galloway, D. A. & Reid, B. J. (1999) Progressive region-specific de novo methylation of the p16 CpG island in primary human mammary epithelial cell strains during escape from M(O) growth arrest. Mol. Cell. Biol. 19: 5642-5651.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5642-5651
    • Wong, D.J.1    Foster, S.A.2    Galloway, D.A.3    Reid, B.J.4
  • 17
    • 0035228079 scopus 로고    scopus 로고
    • X-chromosome inactivation: Counting, choice and initiation
    • Avner, P. & Heard, E. (2001) X-chromosome inactivation: counting, choice and initiation. Nat. Rev. Genet. 2: 59-67.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 59-67
    • Avner, P.1    Heard, E.2
  • 18
    • 0027999284 scopus 로고
    • Regulation of embryonic growth and lysosomal targeting by the imprinted Igf2/Mpr gene
    • Wang, Z. Q., Fung, M. R., Barlow, D. P. & Wagner, E. F. (1994) Regulation of embryonic growth and lysosomal targeting by the imprinted Igf2/ Mpr gene. Nature 372: 464-467.
    • (1994) Nature , vol.372 , pp. 464-467
    • Wang, Z.Q.1    Fung, M.R.2    Barlow, D.P.3    Wagner, E.F.4
  • 20
    • 0036757811 scopus 로고    scopus 로고
    • Infrequent occurrence of age-dependent changes in CpG island methylation as detected by restriction landmark genome scanning
    • Tra, J., Kondo, T., Lu, Q., Kuick, R., Hanash, S. & Richardson, B. (2002) Infrequent occurrence of age-dependent changes in CpG island methylation as detected by restriction landmark genome scanning. Mech. Ageing Dev. 123: 1487-1503.
    • (2002) Mech. Ageing Dev. , vol.123 , pp. 1487-1503
    • Tra, J.1    Kondo, T.2    Lu, Q.3    Kuick, R.4    Hanash, S.5    Richardson, B.6
  • 21
    • 0037357210 scopus 로고    scopus 로고
    • Diet and DNA methylation interactions in cancer prevention
    • Ross, S. A. (2003) Diet and DNA methylation interactions in cancer prevention. Ann. N. Y. Acad. Sci. 983: 197-207.
    • (2003) Ann. N. Y. Acad. Sci. , vol.983 , pp. 197-207
    • Ross, S.A.1
  • 22
    • 0030065081 scopus 로고    scopus 로고
    • Methyl-donor deficiency due to chemically induced glutathione depletion
    • Lertratanangkoon, K., Orkiszewski, R. S. & Scimeca, J. M. (1996) Methyl-donor deficiency due to chemically induced glutathione depletion. Cancer Res. 56: 995-1005.
    • (1996) Cancer Res. , vol.56 , pp. 995-1005
    • Lertratanangkoon, K.1    Orkiszewski, R.S.2    Scimeca, J.M.3
  • 23
    • 0031816123 scopus 로고    scopus 로고
    • Moderate folate depletion increases plasma homocysteine and decreases lymphocyte DNA methylation in postmenopausal women
    • Jacob, R. A., Gretz, D. M., Taylor, P. C., James, S. J., Pogribny, I. P., Miller, B. J., Henning, S. M. & Swendseid, M. E. (1998) Moderate folate depletion increases plasma homocysteine and decreases lymphocyte DNA methylation in postmenopausal women. J. Nutr. 128: 1204-1212.
    • (1998) J. Nutr. , vol.128 , pp. 1204-1212
    • Jacob, R.A.1    Gretz, D.M.2    Taylor, P.C.3    James, S.J.4    Pogribny, I.P.5    Miller, B.J.6    Henning, S.M.7    Swendseid, M.E.8
  • 24
    • 0033580326 scopus 로고    scopus 로고
    • A mammalian protein with specific demethylase activity for mCpG DNA
    • Battacharya, S., Ramchandani, S., Cervoni, N. & Szyf, M. (1999) A mammalian protein with specific demethylase activity for mCpG DNA. Nature 397: 579-583.
    • (1999) Nature , vol.397 , pp. 579-583
    • Battacharya, S.1    Ramchandani, S.2    Cervoni, N.3    Szyf, M.4
  • 26
    • 0037371945 scopus 로고    scopus 로고
    • The expanding network of redox signaling: New observations, complexities, and perspectives
    • Soberman, R. J. (2003) The expanding network of redox signaling: new observations, complexities, and perspectives. J. Clin. Invest. 5: 571-574.
    • (2003) J. Clin. Invest. , vol.5 , pp. 571-574
    • Soberman, R.J.1
  • 27
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel, T. & Holbrook, N. J. (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408: 239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 29
    • 0035865387 scopus 로고    scopus 로고
    • Regulation of cell function by methionine oxidation and reduction
    • Hoshi, T. & Heinemann, S. H. (2001) Regulation of cell function by methionine oxidation and reduction. J. Physiol. 531: 1-11.
    • (2001) J. Physiol. , vol.531 , pp. 1-11
    • Hoshi, T.1    Heinemann, S.H.2
  • 30
    • 0042878460 scopus 로고    scopus 로고
    • Homocysteine mediated expression and secretion of monocyte chemoattractant protein-1 and interleukin-8 in human monocytes
    • Zeng, X., Dai, J., Remick, D. G. & Wang, X. (2003) Homocysteine mediated expression and secretion of monocyte chemoattractant protein-1 and interleukin-8 in human monocytes. Circ. Res. 93: 311-320.
    • (2003) Circ. Res. , vol.93 , pp. 311-320
    • Zeng, X.1    Dai, J.2    Remick, D.G.3    Wang, X.4
  • 31
    • 0035894213 scopus 로고    scopus 로고
    • Modulation of cell injury and survival by high glucose and advancing age
    • Fukagawa, N. K., Li, M., Timblin, C. R. & Mossman, B. T. (2001) Modulation of cell injury and survival by high glucose and advancing age. Free Radic. Biol. Med. 31: 1560-1569.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1560-1569
    • Fukagawa, N.K.1    Li, M.2    Timblin, C.R.3    Mossman, B.T.4
  • 32
    • 0035573652 scopus 로고    scopus 로고
    • Dietary supplementation with methionine and homocysteine promotes early atherosclerosis but not plaque rupture in Apo-E-deficient mice
    • Zhou, J., Møller, J., Danielsen, C. C., Bentzon, J., Ravn, H. B., Austin, R. C. & Falk, E. (2001) Dietary supplementation with methionine and homocysteine promotes early atherosclerosis but not plaque rupture in Apo-E-deficient mice. Arterioscler. Thromb. Vasc. Biol. 21: 1470-1476.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1470-1476
    • Zhou, J.1    Møller, J.2    Danielsen, C.C.3    Bentzon, J.4    Ravn, H.B.5    Austin, R.C.6    Falk, E.7
  • 33
    • 0031921705 scopus 로고    scopus 로고
    • Dietary supplementation with L-methionine impairs the utilization of urea-nitrogen and increases 5-L-oxoprolinuria in normal women consuming a low protein diet
    • Meakins, T. S., Persaud, C. & Jackson, A. A. (1998) Dietary supplementation with L-methionine impairs the utilization of urea-nitrogen and increases 5-L-oxoprolinuria in normal women consuming a low protein diet. J. Nutr. 128: 720-727.
    • (1998) J. Nutr. , vol.128 , pp. 720-727
    • Meakins, T.S.1    Persaud, C.2    Jackson, A.A.3
  • 34
    • 0031815320 scopus 로고    scopus 로고
    • Methionine and cysteine kinetics at different intakes of methionine and cysteine in elderly men and women
    • Fukagawa, N. K., Yu, Y.-M. & Young, V. R. (1998) Methionine and cysteine kinetics at different intakes of methionine and cysteine in elderly men and women. Am. J. Clin. Nutr. 68: 380-388.
    • (1998) Am. J. Clin. Nutr. , vol.68 , pp. 380-388
    • Fukagawa, N.K.1    Yu, Y.-M.2    Young, V.R.3
  • 36
    • 2642559993 scopus 로고    scopus 로고
    • University of Colorado; cystathionine β-synthase (CBS)
    • Allele database statistics [Online]. University of Colorado; cystathionine β-synthase (CBS). http://dec52.1f1.cuni.cz/~mjano/cbs/statistics.php [accessed March 20, 2004].
    • Allele Database Statistics [Online]
  • 37
    • 0019831768 scopus 로고
    • Effect of chronologic age on induction of cystathionine synthase uroporphyrinogen I synthase, and glucose-6-phosphate dehydrogenase activities in lymphocytes
    • Gartler, S. M., Homung, S. K. & Motulsky, A. G. (1981) Effect of chronologic age on induction of cystathionine synthase uroporphyrinogen I synthase, and glucose-6-phosphate dehydrogenase activities in lymphocytes. Proc. Natl. Acad. Sci. USA 78: 1916-1919.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1916-1919
    • Gartler, S.M.1    Homung, S.K.2    Motulsky, A.G.3
  • 38
    • 0015443458 scopus 로고
    • Transsulfuration in fetal and postnatal mammalian liver and brain: Cystathionine synthase, its relation to hormonal influences, and cystathionine
    • Volpe, J. J. & Laster, L. (1972) Transsulfuration in fetal and postnatal mammalian liver and brain: cystathionine synthase, its relation to hormonal influences, and cystathionine. Biol. Neonate 20: 385-403.
    • (1972) Biol. Neonate , vol.20 , pp. 385-403
    • Volpe, J.J.1    Laster, L.2
  • 39
    • 0018568424 scopus 로고
    • Cystathionine synthase in rat brain: Regional and time-of-day differences and their metabolic implications
    • Kohl, R. L. & Quay, W. B. (1979) Cystathionine synthase in rat brain: regional and time-of-day differences and their metabolic implications. J. Neurosci. Res. 4: 189-196.
    • (1979) J. Neurosci. Res. , vol.4 , pp. 189-196
    • Kohl, R.L.1    Quay, W.B.2
  • 40
    • 0021220516 scopus 로고
    • Methionine metabolism in mammals. Distribution of homocysteine between competing pathways
    • Finkelstein, J. D. & Martin, J. J. (1984) Methionine metabolism in mammals. Distribution of homocysteine between competing pathways. J. Biol. Chem. 259: 9508-9513.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9508-9513
    • Finkelstein, J.D.1    Martin, J.J.2
  • 42
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine beta-synthase: A unique pyridoxal 5′-phosphate-dependent heme protein
    • Meier, M., Janosik, M., Kery, V., Kraus, J. P. & Burkhard, P. (2001) Structure of human cystathionine beta-synthase: a unique pyridoxal 5′-phosphate-dependent heme protein. EMBO J. 20: 3910-3916.
    • (2001) EMBO J. , vol.20 , pp. 3910-3916
    • Meier, M.1    Janosik, M.2    Kery, V.3    Kraus, J.P.4    Burkhard, P.5
  • 43
    • 0037046149 scopus 로고    scopus 로고
    • Effects of heme ligand mutations including a pathogenic variant, h65r, on the properties of human cystathionine beta synthase
    • Ojha, S., Wu, J., LoBrutto, R. & Banerjee, R. (2002) Effects of heme ligand mutations including a pathogenic variant, h65r, on the properties of human cystathionine beta synthase. Biochemistry 41: 4649-4654.
    • (2002) Biochemistry , vol.41 , pp. 4649-4654
    • Ojha, S.1    Wu, J.2    LoBrutto, R.3    Banerjee, R.4
  • 44
    • 0035377355 scopus 로고    scopus 로고
    • 31P NMR and pulsed EPR spectroscopy that the heme and PLP cofactors are not proximal in the human enzyme
    • 31P NMR and pulsed EPR spectroscopy that the heme and PLP cofactors are not proximal in the human enzyme. J. Biol. Chem. 276: 19350-19355.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19350-19355
    • Kabil, O.1    Taoka, S.2    LoBrutto, R.3    Shoemaker, R.4    Banerjee, R.5
  • 45
    • 0032566713 scopus 로고    scopus 로고
    • Evidence for heme-mediated redox regulation of human cystathionine β-synthase activity
    • Taoka, S., Ohja, S., Shan, X., Kruger, W. D. & Banerjee, R. (1998) Evidence for heme-mediated redox regulation of human cystathionine β-synthase activity. J. Biol. Chem. 273: 25179-25184.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25179-25184
    • Taoka, S.1    Ohja, S.2    Shan, X.3    Kruger, W.D.4    Banerjee, R.5
  • 46
    • 0034711007 scopus 로고    scopus 로고
    • The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes
    • Mosharov, E., Cranford, M. R. & Banerjee, R. (2000) The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 39: 13005-13011.
    • (2000) Biochemistry , vol.39 , pp. 13005-13011
    • Mosharov, E.1    Cranford, M.R.2    Banerjee, R.3
  • 47
    • 37049125783 scopus 로고
    • Reactions of gases in solution. Part III. Some reactions of nitrous oxide with transition-metal complexes
    • Banks, R.G.S., Henderson, R. J. & Pratt, J. M. (1968) Reactions of gases in solution. Part III. Some reactions of nitrous oxide with transition-metal complexes. J. Chem. Soc. A: 2886-2889.
    • (1968) J. Chem. Soc. A , pp. 2886-2889
    • Banks, R.G.S.1    Henderson, R.J.2    Pratt, J.M.3
  • 48
    • 0001744367 scopus 로고
    • The porphrias
    • (Scriver, C. R., Beaudet, A. L., Sly, W. S., & Valle, D., eds.). McGraw-Hill, New York, NY
    • Kappas, A., Sassa, S., Galbraith, R. A. & Nordman, Y. (1989) The porphrias. In: The Metabolic Basis of Inherited Disease (Scriver, C. R., Beaudet, A. L., Sly, W. S., & Valle, D., eds.), pp. 1305-1365. McGraw-Hill, New York, NY.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 1305-1365
    • Kappas, A.1    Sassa, S.2    Galbraith, R.A.3    Nordman, Y.4
  • 49
  • 50
    • 0022586786 scopus 로고
    • Tryptophan pyrrolase in heme metabolism. Comparative actions of inorganic tin and cobalt and their protoporphyrin chelates on tryptophan pyrrolase in liver
    • Sardana, M.K. & Dummond, G.S. (1986) Tryptophan pyrrolase in heme metabolism. Comparative actions of inorganic tin and cobalt and their protoporphyrin chelates on tryptophan pyrrolase in liver. Biochem. Pharmacol. 35: 473-478.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 473-478
    • Sardana, M.K.1    Dummond, G.S.2
  • 51
    • 0021092439 scopus 로고
    • L-Tryptophan: A common denominator of biochemical and neurological events of acute hepatic porphyria?
    • Litman, D. A. & Correia, M. A. (1983) L-Tryptophan: a common denominator of biochemical and neurological events of acute hepatic porphyria? Science 222: 1031-1033.
    • (1983) Science , vol.222 , pp. 1031-1033
    • Litman, D.A.1    Correia, M.A.2
  • 52
    • 0036175729 scopus 로고    scopus 로고
    • Manipulating the sulfur amino acid content of the early diet and its implications for long-term health
    • Rees, W. D. (2002) Manipulating the sulfur amino acid content of the early diet and its implications for long-term health. Proc. Nutr. Soc. 61: 71-77.
    • (2002) Proc. Nutr. Soc. , vol.61 , pp. 71-77
    • Rees, W.D.1
  • 53
    • 4244027491 scopus 로고    scopus 로고
    • Early changes in maternal sulphur amino acid metabolism caused by maternal protein deficiency
    • abs.
    • Rees, W. D. & Hay, S.M. (2001) Early changes in maternal sulphur amino acid metabolism caused by maternal protein deficiency. Pediatr. Res. 50: 52A (abs.).
    • (2001) Pediatr. Res. , vol.50
    • Rees, W.D.1    Hay, S.M.2
  • 54
    • 0034604524 scopus 로고    scopus 로고
    • Changes in the intracellular homocysteine and glutathione content associated with aging
    • Hernanz, A., Fernández-Vivancos, E., Montiel, C., Vazquez, J. J. & Arnalich, F. (2000) Changes in the intracellular homocysteine and glutathione content associated with aging. Life Sci. 67: 1317-1324.
    • (2000) Life Sci. , vol.67 , pp. 1317-1324
    • Hernanz, A.1    Fernández-Vivancos, E.2    Montiel, C.3    Vazquez, J.J.4    Arnalich, F.5
  • 59
    • 0038315188 scopus 로고    scopus 로고
    • Use of exfoliated cells from target tissues to predict responses to bioactive food components
    • Davis, C. D. (2003) Use of exfoliated cells from target tissues to predict responses to bioactive food components. J. Nutr. 133: 1769-1772.
    • (2003) J. Nutr. , vol.133 , pp. 1769-1772
    • Davis, C.D.1


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