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Volumn 151, Issue 1, 1998, Pages 1-49

Mathematical models of purine metabolism in man

Author keywords

Biochemical systems theory; General mass action system; Mathematical model; Purine metabolism; S system

Indexed keywords

ARTICLE; ENZYME DEFICIENCY; ENZYME MECHANISM; MATHEMATICAL MODEL; MICHAELIS CONSTANT; PURINE METABOLISM;

EID: 0031832789     PISSN: 00255564     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0025-5564(98)10001-9     Document Type: Article
Times cited : (67)

References (119)
  • 1
    • 0021150239 scopus 로고
    • Computer simulation of purine metabolism
    • Franco R., Canela E.I. Computer simulation of purine metabolism. European J. Biochem. 144:1984;305.
    • (1984) European J. Biochem. , vol.144 , pp. 305
    • Franco, R.1    Canela, E.I.2
  • 2
    • 0024393877 scopus 로고
    • Supercomputer analysis of purine and pyrimidine metabolism leading to DNA-Synthesis
    • Heinmets F. Supercomputer analysis of purine and pyrimidine metabolism leading to DNA-Synthesis. Cell Biophys. 14:1989;283.
    • (1989) Cell Biophys. , vol.14 , pp. 283
    • Heinmets, F.1
  • 3
    • 0025080104 scopus 로고
    • Mathematical modelling of the purine metabolism of the rat liver
    • Bartel T., Holzhütter H. Mathematical modelling of the purine metabolism of the rat liver. Biochim. Biophys. Acta. 1035:1990;331.
    • (1990) Biochim. Biophys. Acta , vol.1035 , pp. 331
    • Bartel, T.1    Holzhütter, H.2
  • 4
    • 0017766016 scopus 로고
    • Regulation of nucleotidase activities in animal tisues
    • Fritzson P. Regulation of nucleotidase activities in animal tisues. Adv. Enzyme Regul. 16:1978;43.
    • (1978) Adv. Enzyme Regul. , vol.16 , pp. 43
    • Fritzson, P.1
  • 6
    • 0026323450 scopus 로고
    • Purine nucleoside phosphorilase of bovine liver mithochondria
    • Lewis R.A., Haag R.K. Purine nucleoside phosphorilase of bovine liver mithochondria. Adv. Exp. Med. Biol. B. 309:1991;181.
    • (1991) Adv. Exp. Med. Biol. B , vol.309 , pp. 181
    • Lewis, R.A.1    Haag, R.K.2
  • 7
    • 0014649230 scopus 로고
    • Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions
    • Savageau M.A. Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions. J. Theoret. Biol. 25:1969;365.
    • (1969) J. Theoret. Biol. , vol.25 , pp. 365
    • Savageau, M.A.1
  • 8
    • 0014658880 scopus 로고
    • Biochemical systems analysis II. Steady state solutions for an n-poll system using a power-law approximation
    • Savageau M.A. Biochemical systems analysis II. Steady state solutions for an n-poll system using a power-law approximation. J. Theoret. Biol. 25:1969;370.
    • (1969) J. Theoret. Biol. , vol.25 , pp. 370
    • Savageau, M.A.1
  • 10
    • 0029118323 scopus 로고
    • Comparative characterization of the fermentation pathway of Saccharomyces cerevisiae using biochemical systems theory and metabolic control analysis: Model definition and nomenclature
    • Curto R., Sorribas A., Cascante M. Comparative characterization of the fermentation pathway of Saccharomyces cerevisiae using biochemical systems theory and metabolic control analysis: model definition and nomenclature. Math. Biosci. 130:1995;25.
    • (1995) Math. Biosci. , vol.130 , pp. 25
    • Curto, R.1    Sorribas, A.2    Cascante, M.3
  • 11
    • 0029099156 scopus 로고
    • Comparative characterization of the fermentation pathway of saccharomyces cerevisiae using biochemical systems theory and metabolic control analysis: Steady-state analysys
    • Cascante M., Curto R., Sorribas A. Comparative characterization of the fermentation pathway of saccharomyces cerevisiae using biochemical systems theory and metabolic control analysis: steady-state analysys. Math. Biosci. 130:1995;51.
    • (1995) Math. Biosci. , vol.130 , pp. 51
    • Cascante, M.1    Curto, R.2    Sorribas, A.3
  • 12
    • 0029147559 scopus 로고
    • Comparative characterization of the fermentation pathway of Saccharomyces cerevisiae using biochemical systems theory and metabolic control analysys: Model validation and dynamic behaviour
    • Sorribas A., Curto R., Cascante M. Comparative characterization of the fermentation pathway of Saccharomyces cerevisiae using biochemical systems theory and metabolic control analysys: model validation and dynamic behaviour. Math. Biosci. 130:1995;71.
    • (1995) Math. Biosci. , vol.130 , pp. 71
    • Sorribas, A.1    Curto, R.2    Cascante, M.3
  • 14
    • 0023661067 scopus 로고
    • Accuracy of alternative representations for integrated biochemical systems
    • Voit E.O., Savageau M.A. Accuracy of alternative representations for integrated biochemical systems. Biochemistry. 26:1987;6869.
    • (1987) Biochemistry , vol.26 , pp. 6869
    • Voit, E.O.1    Savageau, M.A.2
  • 15
    • 0000870544 scopus 로고
    • Die kinetik der invertinwirkung
    • Michaelis L., Menten M.L. Die Kinetik der Invertinwirkung. Biochem. Z. 49:1913;333.
    • (1913) Biochem. Z. , vol.49 , pp. 333
    • Michaelis, L.1    Menten, M.L.2
  • 16
    • 45949117248 scopus 로고
    • Biochemical systems theory and metabolic control theory: 1. Fundamental similarities and differences
    • Savageau M.A., Voit E.O., Irvine D.H. Biochemical systems theory and metabolic control theory: 1. Fundamental similarities and differences. Math. Biosc. 86:1987;127.
    • (1987) Math. Biosc. , vol.86 , pp. 127
    • Savageau, M.A.1    Voit, E.O.2    Irvine, D.H.3
  • 17
    • 45949116170 scopus 로고
    • Biochemical systems theory and metabolic control theory: 2. The role of sumation and connectivity relationships
    • Savageau M.A., Voit E.O., Irvine D.H. Biochemical systems theory and metabolic control theory: 2. The role of sumation and connectivity relationships. Math. Biosc. 86:1987;147.
    • (1987) Math. Biosc. , vol.86 , pp. 147
    • Savageau, M.A.1    Voit, E.O.2    Irvine, D.H.3
  • 18
    • 0028131950 scopus 로고
    • Propagation of uncertainty in risk assessments: The need to distinguish between uncertainty due to lack of knowledge and uncertainty due to variability
    • Hoffman F.O., Hammonds J.S. Propagation of uncertainty in risk assessments: the need to distinguish between uncertainty due to lack of knowledge and uncertainty due to variability. Risk Analysis. 14(5):1994;707.
    • (1994) Risk Analysis , vol.14 , Issue.5 , pp. 707
    • Hoffman, F.O.1    Hammonds, J.S.2
  • 20
    • 0000472707 scopus 로고
    • Hyperuricemia and gout
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Ed.), McGraw-Hill, New York
    • T.D. Palella, I.H. Fox, Hyperuricemia and gout in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Ed.), The Metabolic Basis of Inherited Disease, McGraw-Hill, New York, 1989, p. 965.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 965
    • Palella, T.D.1    Fox, I.H.2
  • 22
    • 0018359713 scopus 로고
    • Overproduction of uric acid in hypoxanthine-guanine phosphoribosyltransferase deficiency
    • Edwards N.L., Recker D., Fox I.H. Overproduction of uric acid in hypoxanthine-guanine phosphoribosyltransferase deficiency. J. Clin. Invest. 63:1979;922.
    • (1979) J. Clin. Invest. , vol.63 , pp. 922
    • Edwards, N.L.1    Recker, D.2    Fox, I.H.3
  • 23
    • 0026332347 scopus 로고
    • A syndrome of megaloblastic anemia, inmunodeficiency, and exesive nucleotide degradation
    • Page T., Nyhan W.L., Yu A.L., Yu J. A syndrome of megaloblastic anemia, inmunodeficiency, and exesive nucleotide degradation. Adv. Exp. Med. Biol. 309B:1991;345.
    • (1991) Adv. Exp. Med. Biol. , vol.309 B , pp. 345
    • Page, T.1    Nyhan, W.L.2    Yu, A.L.3    Yu, J.4
  • 24
    • 0344072030 scopus 로고
    • The study of purine utilization and excretion in a xanthinuric man
    • Ayvazian J.H., Skupp S. The study of purine utilization and excretion in a xanthinuric man. J. Clin. Invest. 44:1965;1248.
    • (1965) J. Clin. Invest. , vol.44 , pp. 1248
    • Ayvazian, J.H.1    Skupp, S.2
  • 25
    • 0013984878 scopus 로고
    • Study of the utilization and excretion of dietary purines in a xanthinuric man
    • Ayvazian J.H., Skupp S. Study of the utilization and excretion of dietary purines in a xanthinuric man. J. Clin. Invest. 45:1966;1859.
    • (1966) J. Clin. Invest. , vol.45 , pp. 1859
    • Ayvazian, J.H.1    Skupp, S.2
  • 26
    • 0015852804 scopus 로고
    • Alternative pathways of deoxyadenosine and adenosine metabolism
    • Snyder F.F., Henderson J.F. Alternative pathways of deoxyadenosine and adenosine metabolism. J. Biol. Chem. 248:1973;5899.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5899
    • Snyder, F.F.1    Henderson, J.F.2
  • 27
    • 0017098404 scopus 로고
    • Regulation of de novo purine biosynthesis in human lymphoblasts
    • Hershfield M.S., Seegmiller J.E. Regulation of de novo purine biosynthesis in human lymphoblasts. J. Biol. Chem. 251:1976;7348.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7348
    • Hershfield, M.S.1    Seegmiller, J.E.2
  • 29
    • 0001814559 scopus 로고
    • Adenine phosphoribosyltransferase deficiency and 2,8-dihydroxyadenine lithiasis
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.), McGraw-Hill, New York
    • H.A. Simmonds, A.S. Sahota, K.J. Van Acker, Adenine phosphoribosyltransferase deficiency and 2,8-dihydroxyadenine lithiasis, in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.), The Metabolic Basis of Inherited Disease, McGraw-Hill, New York, 1989, p. 1029.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 1029
    • Simmonds, H.A.1    Sahota, A.S.2    Van Acker, K.J.3
  • 30
    • 0002129738 scopus 로고
    • Adenosine deaminase and [3H] nitrobenzylthioinosine as markers of adenosine metabolism and transport in central purinergic systems
    • M. Williams (Ed.), Humanae Press, Clifton, New Jersey
    • J.D. Geiger, J.I. Nagy, Adenosine deaminase and [3H] nitrobenzylthioinosine as markers of adenosine metabolism and transport in central purinergic systems, in: M. Williams (Ed.), Adenosine and Adenosine Receptors, Humanae Press, Clifton, New Jersey, 1990, p. 225.
    • (1990) Adenosine and Adenosine Receptors , pp. 225
    • Geiger, J.D.1    Nagy, J.I.2
  • 31
    • 0002276159 scopus 로고
    • Immunodeficiency diseases caused by adenosine deaminase deficiency and Purine nucleoside phosphorylase deficiency
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Ed.), McGraw-Hill, New York
    • N.M. Kredich, M.S. Hersfield, Immunodeficiency diseases caused by adenosine deaminase deficiency and Purine nucleoside phosphorylase deficiency, in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Ed.), The Metabolic Basis of Inherited Disease, McGraw-Hill, New York, 1989, p. 1045.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 1045
    • Kredich, N.M.1    Hersfield, M.S.2
  • 32
    • 0020639120 scopus 로고
    • Evidence for a substrate cycle between AMP and adenosine in isolated hepatocytes
    • Bontemps F., Van den Berghe G., Hers H.G. Evidence for a substrate cycle between AMP and adenosine in isolated hepatocytes. Proc. Natl. Acad. Sci. USA. 80:1983;2829.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2829
    • Bontemps, F.1    Van den Berghe, G.2    Hers, H.G.3
  • 33
    • 0002377576 scopus 로고
    • Hereditary xanthinuria
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Ed.), McGraw-Hill, New York
    • E.W. Holmes, J.B. Wyngaarden, Hereditary xanthinuria, in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Ed.), The Metabolic Basis of Inherited Disease, McGraw-Hill, New York, 1989, p. 1085.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 1085
    • Holmes, E.W.1    Wyngaarden, J.B.2
  • 34
    • 0025141378 scopus 로고
    • Pathways of purine metabolism in human adipocytes - Further evidence against a role of adenosine as an endogenous regulator of human fat-cell function
    • Kather H. Pathways of purine metabolism in human adipocytes - Further evidence against a role of adenosine as an endogenous regulator of human fat-cell function. J. Biol. Chem. 265:1990;96.
    • (1990) J. Biol. Chem. , vol.265 , pp. 96
    • Kather, H.1
  • 35
    • 0345365507 scopus 로고
    • Transcription and the Processing of RNA
    • H.R. Horton, L.A. Moran, R.S. Ochs, J.D. Rawn, K.G. Scrimgeour (Ed.), Prentice-Hall, New Jersey, ch. 21
    • H.R. Horton, L.A. Moran, R.S. Ochs, J.D. Rawn, K.G. Scrimgeour, Transcription and the Processing of RNA, in: H.R. Horton, L.A. Moran, R.S. Ochs, J.D. Rawn, K.G. Scrimgeour (Ed.), Principles of Biochemistry, Prentice-Hall, New Jersey, ch. 21, 1993.
    • (1993) Principles of Biochemistry
    • Horton, H.R.1    Moran, L.A.2    Ochs, R.S.3    Rawn, J.D.4    Scrimgeour, K.G.5
  • 36
    • 0022545347 scopus 로고
    • Ribonucleic acid turnover in man: RNA catabolites in urine as measure for the metabolism of each of the three major species of RNA
    • Sander G., Topp H., Heller-Schöch G., Wieland J., Schöch G. Ribonucleic acid turnover in man: RNA catabolites in urine as measure for the metabolism of each of the three major species of RNA. Clin. Sci. 71:1986;367.
    • (1986) Clin. Sci. , vol.71 , pp. 367
    • Sander, G.1    Topp, H.2    Heller-Schöch, G.3    Wieland, J.4    Schöch, G.5
  • 37
    • 0008471013 scopus 로고
    • Sensitivity analysis. A common foundation of theories for the quantitative study of metabolic control
    • E.O. Voit (Ed.), Van Nostrand Reinhold, New York
    • M. Cascante, R. Franco, E.I. Canela, Sensitivity analysis. A common foundation of theories for the quantitative study of metabolic control, in: E.O. Voit (Ed.), Canonical Nonlinear Modeling. S-System Approach to Understanding Complexity, Van Nostrand Reinhold, New York, 1991, pp. 76.
    • (1991) Canonical Nonlinear Modeling. S-System Approach to Understanding Complexity , pp. 76
    • Cascante, M.1    Franco, R.2    Canela, E.I.3
  • 38
    • 0024442732 scopus 로고
    • Constraints among molecular and systemic properties - Implications for physiological genetics
    • Savageau M.A., Sorribas A. Constraints among molecular and systemic properties - Implications for physiological genetics. J. Theoret. Biol. 141:1989;93.
    • (1989) J. Theoret. Biol. , vol.141 , pp. 93
    • Savageau, M.A.1    Sorribas, A.2
  • 40
    • 0002673826 scopus 로고
    • Critique of the enzymologists test tube
    • E. Bittar (Ed.), Jai Press, Greenwich, CT
    • M.A. Savageau, Critique of the enzymologists test tube, in: E. Bittar (Ed.), Foundations of Medical Cell Biology, Jai Press, Greenwich, CT, 1992, pp. 45.
    • (1992) Foundations of Medical Cell Biology , pp. 45
    • Savageau, M.A.1
  • 41
    • 0029134903 scopus 로고
    • Michaelis-Menten mechanism reconsidered: Implications of fractal kinetics
    • Savageau M.A. Michaelis-Menten mechanism reconsidered: implications of fractal kinetics. J. Theoret. Biol. 176:1995;115.
    • (1995) J. Theoret. Biol. , vol.176 , pp. 115
    • Savageau, M.A.1
  • 45
    • 0002862462 scopus 로고
    • Enzyme kinetics in vitro and in vivo: Michaelis-Menten revisited
    • E.E. Bittar (Ed.), Jai Press, Greenwich. Connecticut
    • M.A. Savageau, Enzyme kinetics in vitro and in vivo: Michaelis-Menten revisited, in: E.E. Bittar (Ed.), Principles of Medical Biology, Jai Press, Greenwich. Connecticut, 1995, p. 93.
    • (1995) Principles of Medical Biology , pp. 93
    • Savageau, M.A.1
  • 47
    • 0345365505 scopus 로고
    • Reaction kinetics on clusters and islands
    • Newhouse J.S., Kopleman R. Reaction kinetics on clusters and islands. J. Chem. Phys. 85:1986;6804.
    • (1986) J. Chem. Phys. , vol.85 , pp. 6804
    • Newhouse, J.S.1    Kopleman, R.2
  • 48
    • 2942707058 scopus 로고
    • Quantitative aspects of rapid microfluorometry for the study of enzyme reactions and transport mechanisms in single living cells
    • A.A. Thaer, M. Sernetz (Ed.), Springer, New York
    • E. Kohen, C. Khoen, B. Thorell, G. Wagner, Quantitative aspects of rapid microfluorometry for the study of enzyme reactions and transport mechanisms in single living cells, in: A.A. Thaer, M. Sernetz (Ed.), Fluorescence Techniches in Cell Biology, Springer, New York, 1973, p. 207.
    • (1973) Fluorescence Techniches in Cell Biology , pp. 207
    • Kohen, E.1    Khoen, C.2    Thorell, B.3    Wagner, G.4
  • 49
    • 0016075610 scopus 로고
    • Studies of metabolic events in localized compartments of the living cell by rapid microspectro-fluorometry
    • Kohen E., Thorell B., Khoen C., Solmon J.M. Studies of metabolic events in localized compartments of the living cell by rapid microspectro-fluorometry. Adv. Biol. Med. Phys. 15:1974;271.
    • (1974) Adv. Biol. Med. Phys. , vol.15 , pp. 271
    • Kohen, E.1    Thorell, B.2    Khoen, C.3    Solmon, J.M.4
  • 50
    • 30244438013 scopus 로고
    • Rate processes on fractals: Theory, simulations, and experiments
    • Kopleman R. Rate processes on fractals: theory, simulations, and experiments. J. Statist. Phys. 42:1986;185.
    • (1986) J. Statist. Phys. , vol.42 , pp. 185
    • Kopleman, R.1
  • 51
    • 0024673624 scopus 로고
    • A comparison of variant theories of intact biochemical systems. 2. Flux-oriented and metabolic control theories
    • Sorribas A., Savageau M.A. A comparison of variant theories of intact biochemical systems. 2. Flux-oriented and metabolic control theories. Math. Biosci. 94:1989;195.
    • (1989) Math. Biosci. , vol.94 , pp. 195
    • Sorribas, A.1    Savageau, M.A.2
  • 52
    • 0014222377 scopus 로고
    • Enzyme defect associated with a sex-linked human neurological disorder and excesive purine synthesis
    • Seegmiller J.E., Rosenbloom F.M. Enzyme defect associated with a sex-linked human neurological disorder and excesive purine synthesis. Science. 155:1967;1682.
    • (1967) Science , vol.155 , pp. 1682
    • Seegmiller, J.E.1    Rosenbloom, F.M.2
  • 53
    • 0026911028 scopus 로고
    • Optimization in integrated biochemical systems
    • Voit E.O. Optimization in integrated biochemical systems. Biotechnol. Bioeng. 40:1992;572.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 572
    • Voit, E.O.1
  • 55
    • 0004218236 scopus 로고
    • Gout
    • J.B. Stanbury, J.B. Wyngaarden, D.S. Fredrickson, J.L. Goldstein, M.S. Brown (Ed.), McGraw-Hill, New York
    • J.B. Wyngaarden, W.N. Kelley, Gout, in: J.B. Stanbury, J.B. Wyngaarden, D.S. Fredrickson, J.L. Goldstein, M.S. Brown (Ed.), The Metabolic Basis of Inherited Disease, McGraw-Hill, New York, 1983, p. 1043.
    • (1983) The Metabolic Basis of Inherited Disease , pp. 1043
    • Wyngaarden, J.B.1    Kelley, W.N.2
  • 57
    • 0026318147 scopus 로고
    • Possible metabolic basis for GTP depletion in red cells of patients with PRPP synthetase superactivity
    • Giacomello A., Salerno C. Possible metabolic basis for GTP depletion in red cells of patients with PRPP synthetase superactivity. Adv. Exp. Med. Biol. 309B:1991;253.
    • (1991) Adv. Exp. Med. Biol. , vol.309 B , pp. 253
    • Giacomello, A.1    Salerno, C.2
  • 59
    • 0017750466 scopus 로고
    • The purine nucleotide cycle. Studies of ammonia production by skeletal muscle in situ and in perfused preparations
    • Goodman M.N., Lowenstein J.M. The purine nucleotide cycle. Studies of ammonia production by skeletal muscle in situ and in perfused preparations. J. Biol. Chem. 252:1977;5054.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5054
    • Goodman, M.N.1    Lowenstein, J.M.2
  • 60
    • 0026328599 scopus 로고
    • Purine nucleotides, nucleosides and nucleobases of liver, skeletal muscle, blood and tumor cells during the growth of Erlich Ascites tumor in mice
    • Siems W.G., Grune T., Schmidt R., Uhlig R., Gerber G., Tikhonov Y.V., Pimenov A.M., Toguzov R.T. Purine nucleotides, nucleosides and nucleobases of liver, skeletal muscle, blood and tumor cells during the growth of Erlich Ascites tumor in mice. Adv. Exp. Med. Biol. 309A:1991;113.
    • (1991) Adv. Exp. Med. Biol. , vol.309 A , pp. 113
    • Siems, W.G.1    Grune, T.2    Schmidt, R.3    Uhlig, R.4    Gerber, G.5    Tikhonov, Y.V.6    Pimenov, A.M.7    Toguzov, R.T.8
  • 61
    • 0025768532 scopus 로고
    • Determination of the ultraviolet absorbency and radioactivity of purine compounds separated by high-performance liquid-chromatography - Application to metabolic flux rate analysis
    • Grune T., Siems W.G., Gerber G., Uhlig R. Determination of the ultraviolet absorbency and radioactivity of purine compounds separated by high-performance liquid-chromatography - Application to metabolic flux rate analysis. J. Chromatogr. 553:1991;193.
    • (1991) J. Chromatogr. , vol.553 , pp. 193
    • Grune, T.1    Siems, W.G.2    Gerber, G.3    Uhlig, R.4
  • 63
    • 0020960305 scopus 로고
    • S-adenosyl-L-metionine synthase from human erythrocytes: Role in the regulation of cellular S-adenosylmethionine levels
    • Oden K.L., Clarke S. S-adenosyl-L-metionine synthase from human erythrocytes: role in the regulation of cellular S-adenosylmethionine levels. Biochemistry. 22:1983;2978.
    • (1983) Biochemistry , vol.22 , pp. 2978
    • Oden, K.L.1    Clarke, S.2
  • 64
    • 0026344736 scopus 로고
    • Changes of purine nucleotide metabolism of Erlich ascites cells during transition of tumor growth
    • Grune T., Siems W., Uhlig R., Langen P., Gerber G. Changes of purine nucleotide metabolism of Erlich ascites cells during transition of tumor growth. Adv. Exp. Med. Biol. 309A:1991;109.
    • (1991) Adv. Exp. Med. Biol. , vol.309 A , pp. 109
    • Grune, T.1    Siems, W.2    Uhlig, R.3    Langen, P.4    Gerber, G.5
  • 66
    • 0026326242 scopus 로고
    • Some aspects of purine nucleotide metabolism in human lymphocytes: Nucleotide content in human lymphoblastoid lines transfected with HIV-1
    • Tabucchi A., Carlucci F., Pagani R., Ciccomascolo F., Lopalco L., Siccardi A. Some aspects of purine nucleotide metabolism in human lymphocytes: nucleotide content in human lymphoblastoid lines transfected with HIV-1. Adv. Exp. Med. Biol. 309A:1991;121.
    • (1991) Adv. Exp. Med. Biol. , vol.309 A , pp. 121
    • Tabucchi, A.1    Carlucci, F.2    Pagani, R.3    Ciccomascolo, F.4    Lopalco, L.5    Siccardi, A.6
  • 67
    • 0026318148 scopus 로고
    • Raised IMP-dehydrogenase activity in the erythrocytes of a case of purine nucleoside (PNP) deficiency
    • Morgan G., Strobel S., Montero C., Duley J.A., Davies P.M., Simmonds H.A. Raised IMP-dehydrogenase activity in the erythrocytes of a case of purine nucleoside (PNP) deficiency. Adv. Exp. Med. Biol. 309B:1991;297.
    • (1991) Adv. Exp. Med. Biol. , vol.309 B , pp. 297
    • Morgan, G.1    Strobel, S.2    Montero, C.3    Duley, J.A.4    Davies, P.M.5    Simmonds, H.A.6
  • 68
    • 34547384791 scopus 로고
    • Metabolismo de los nucleótidos purínicos y pirimidínicos
    • T.M. Devlin (Ed.), Reverte S.A., Barcelona
    • J.G. Cory, Metabolismo de los nucleótidos purínicos y pirimidínicos, in: T.M. Devlin (Ed.), Bioquímica, Reverte S.A., Barcelona, 1988, p. 618.
    • (1988) Bioquímica , pp. 618
    • Cory, J.G.1
  • 69
    • 0027215239 scopus 로고
    • Aspects of the regulation of hepatic phosphoribosyl pyrophosphate formation in the obese (ob/ob) mouse - Relationship to the pentose phosphate pathway
    • Kunjara S., Sochor M., Greenbaum A.L., Mclean P. Aspects of the regulation of hepatic phosphoribosyl pyrophosphate formation in the obese (ob/ob) mouse - Relationship to the pentose phosphate pathway. Biochem. Med. Metab. Biol. 49:1993;217.
    • (1993) Biochem. Med. Metab. Biol. , vol.49 , pp. 217
    • Kunjara, S.1    Sochor, M.2    Greenbaum, A.L.3    Mclean, P.4
  • 70
    • 0028168977 scopus 로고
    • Carbohydrate metabolism in dictyostelium discoideum: II. Systems' Analysis
    • Albe K.R., Wright B.E. Carbohydrate metabolism in dictyostelium discoideum: II. Systems' Analysis. J. Theoret. Biol. 169:1994;243.
    • (1994) J. Theoret. Biol. , vol.169 , pp. 243
    • Albe, K.R.1    Wright, B.E.2
  • 71
    • 85036482469 scopus 로고
    • DNA y RNA: Las moléculas de la herencia
    • L. Stryer (Ed.), Reverté S.A., Barcelona
    • L. Stryer. DNA y RNA: Las moléculas de la herencia, in: L. Stryer (Ed.), Bioquímica, Reverté S.A., Barcelona, 1988, p. 71.
    • (1988) Bioquímica , pp. 71
    • Stryer, L.1
  • 72
    • 0024537586 scopus 로고
    • Adenine-nucleotide turnover in hypoxanthine-guanine phosphoribosyl-transferase deficiency - Evidence for an increased contribution of purine biosynthesis de Novo
    • Puig J.G., Fox I.H., Mateos F.A., Jimenez M.L. Adenine-nucleotide turnover in hypoxanthine-guanine phosphoribosyl-transferase deficiency - Evidence for an increased contribution of purine biosynthesis de Novo. Metabolism. 38:1989;410.
    • (1989) Metabolism , vol.38 , pp. 410
    • Puig, J.G.1    Fox, I.H.2    Mateos, F.A.3    Jimenez, M.L.4
  • 73
    • 0021016177 scopus 로고
    • Regulation of de novo purine synthesis in human bone marrow mononuclear cells by hypoxanthine
    • King M.E., Honeysett J.M., Howell S.B. Regulation of de novo purine synthesis in human bone marrow mononuclear cells by hypoxanthine. J. Clin. Invest. 72:1983;965.
    • (1983) J. Clin. Invest. , vol.72 , pp. 965
    • King, M.E.1    Honeysett, J.M.2    Howell, S.B.3
  • 75
    • 0026351519 scopus 로고
    • Purine nucleoside phosphorylase: Allosteric regulation of a dissociating enzyme
    • Traut T.W., Ropp P.A., Poma A. Purine nucleoside phosphorylase: allosteric regulation of a dissociating enzyme. Adv. Exp. Med. Biol. 309B:1991;177.
    • (1991) Adv. Exp. Med. Biol. , vol.309 B , pp. 177
    • Traut, T.W.1    Ropp, P.A.2    Poma, A.3
  • 77
    • 0018746169 scopus 로고
    • Factors affecting the rate of purine ribonucleotide dephosphorylation in human erythrocytes
    • Whelan J.M., Bagnara A.S. Factors affecting the rate of purine ribonucleotide dephosphorylation in human erythrocytes. Biochim. Biophys. Acta. 563:1979;466.
    • (1979) Biochim. Biophys. Acta , vol.563 , pp. 466
    • Whelan, J.M.1    Bagnara, A.S.2
  • 78
    • 0026335867 scopus 로고
    • Long-term evolution of type 1 Adenine phosphoribosyltransferase (APRT) deficiency
    • Van Acker K.J., Simonds H.A. Long-term evolution of type 1 Adenine phosphoribosyltransferase (APRT) deficiency. Adv. Exp. Med. Biol. 309B:1991;91.
    • (1991) Adv. Exp. Med. Biol. , vol.309 B , pp. 91
    • Van Acker, K.J.1    Simonds, H.A.2
  • 79
    • 0024780894 scopus 로고
    • Neurodevelopmental impairment and deranged PRPP and purine nucleotide synthesisin inherited superactivity of PRPPsynthetase
    • Becker M.A., Puig J.G., Mateos F.A., Jimenez M.L., Kim M., Simmonds H.A. Neurodevelopmental impairment and deranged PRPP and purine nucleotide synthesisin inherited superactivity of PRPPsynthetase. Adv. Exp. Med. Biol. 253A:1989;15.
    • (1989) Adv. Exp. Med. Biol. , vol.253 A , pp. 15
    • Becker, M.A.1    Puig, J.G.2    Mateos, F.A.3    Jimenez, M.L.4    Kim, M.5    Simmonds, H.A.6
  • 80
    • 0024780511 scopus 로고
    • Lesch-Nyhan syndrome: Reduced aminoacid concentrations in CSF and brain
    • Harkness R.A. Lesch-Nyhan syndrome: reduced aminoacid concentrations in CSF and brain. Adv. Exp. Med. Biol. 253A:1989;159.
    • (1989) Adv. Exp. Med. Biol. , vol.253 A , pp. 159
    • Harkness, R.A.1
  • 81
    • 0026326063 scopus 로고
    • Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase deficiency in Japanese patients
    • Fujimori S., Tagaya T., Yamaoka N., Kamatani N., Akaoka L. Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase deficiency in Japanese patients. Adv. Exp. Med. Biol. 309B:1991;101.
    • (1991) Adv. Exp. Med. Biol. , vol.309 B , pp. 101
    • Fujimori, S.1    Tagaya, T.2    Yamaoka, N.3    Kamatani, N.4    Akaoka, L.5
  • 82
    • 0015500785 scopus 로고
    • Human phosphoribosylpyrophosphate synthetase kinetic mechanism and end product inhibition
    • Fox I.H., Kelley W.N. Human phosphoribosylpyrophosphate synthetase kinetic mechanism and end product inhibition. J. Biol. Chem. 247:1972;2126.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2126
    • Fox, I.H.1    Kelley, W.N.2
  • 83
    • 0015240245 scopus 로고
    • Human phosphoribosylpyrophosphte synthetase, distribution purification and properties
    • Fox I.H., Kelley W.N. Human phosphoribosylpyrophosphte synthetase, distribution purification and properties. J. Biol. Chem. 246:1971;5739.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5739
    • Fox, I.H.1    Kelley, W.N.2
  • 84
    • 0025210437 scopus 로고
    • Regulation of 5-phosphoribosyl 1-pyrophosphate and of hypoxanthine uptake and release in human erythrocytes by oxypurine cycling
    • Berman P.A.M., Human L. Regulation of 5-phosphoribosyl 1-pyrophosphate and of hypoxanthine uptake and release in human erythrocytes by oxypurine cycling. J. Biol. Chem. 265:1990;6562.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6562
    • Berman, P.A.M.1    Human, L.2
  • 85
    • 0019234227 scopus 로고
    • Kinetic, physical, and regulatory properties of amidophosphoribosyltransferase
    • Holmes E.W. Kinetic, physical, and regulatory properties of amidophosphoribosyltransferase. Adv. Enzyme Regul. 19:1981;215.
    • (1981) Adv. Enzyme Regul. , vol.19 , pp. 215
    • Holmes, E.W.1
  • 86
    • 0015918864 scopus 로고
    • Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties
    • Holmes E.W., McDonald J.A., McCord J.M., Wyngaarden J.B., Kelley W.N. Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties. J. Biol. Chem. 248:1973;144.
    • (1973) J. Biol. Chem. , vol.248 , pp. 144
    • Holmes, E.W.1    McDonald, J.A.2    McCord, J.M.3    Wyngaarden, J.B.4    Kelley, W.N.5
  • 87
    • 0017818621 scopus 로고
    • Regulation of human amidophosphoribosyltransferase: Interaction of ortophosphate, PP-ribose-P, and purine ribonucleotides
    • Kovarsky J., Evans M.C., Holmes E.W. Regulation of human amidophosphoribosyltransferase: interaction of ortophosphate, PP-ribose-P, and purine ribonucleotides. Canad. J. Biochem. 56:1978;334.
    • (1978) Canad. J. Biochem. , vol.56 , pp. 334
    • Kovarsky, J.1    Evans, M.C.2    Holmes, E.W.3
  • 89
    • 0025276048 scopus 로고
    • Cellular concentrations of enzymes and their substrates
    • Albe K.R., Butler M.H., Wright B.E. Cellular concentrations of enzymes and their substrates. J. Theoret. Biol. 143:1990;163.
    • (1990) J. Theoret. Biol. , vol.143 , pp. 163
    • Albe, K.R.1    Butler, M.H.2    Wright, B.E.3
  • 90
    • 0018177022 scopus 로고
    • Human hypoxanthine-guanine phosphoribosyltransferase
    • Giacomello A., Salerno C. Human hypoxanthine-guanine phosphoribosyltransferase. J. Biol. Chem. 253:1978;6038.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6038
    • Giacomello, A.1    Salerno, C.2
  • 91
    • 0014426530 scopus 로고
    • Adenine nucleotidemetabolism of blood platelets. III Adenine phosphoribosyl transferase and nucleotide formation from exogenous adenine
    • Holmsen H., Rozenberg M.C. Adenine nucleotidemetabolism of blood platelets. III Adenine phosphoribosyl transferase and nucleotide formation from exogenous adenine. Biochim. Biophys. Acta. 157:1968;266.
    • (1968) Biochim. Biophys. Acta , vol.157 , pp. 266
    • Holmsen, H.1    Rozenberg, M.C.2
  • 92
    • 0022366637 scopus 로고
    • Common characteristics of mutant adenine phosphoribosyltransferases from four separate Japanese families with 2,8-dihydroxyadenine urolithiasis associated with partial enzyme deficiencies
    • Fujimori S., Akaoka I., Sakamoto K., Yamanaka H., Nishioka K., Kamatani N. Common characteristics of mutant adenine phosphoribosyltransferases from four separate Japanese families with 2,8-dihydroxyadenine urolithiasis associated with partial enzyme deficiencies. Hum. Genet. 71:1985;171.
    • (1985) Hum. Genet. , vol.71 , pp. 171
    • Fujimori, S.1    Akaoka, I.2    Sakamoto, K.3    Yamanaka, H.4    Nishioka, K.5    Kamatani, N.6
  • 93
    • 0014027813 scopus 로고
    • Kinetic studies of adenine phosphoribosyltransferase
    • Hori M., Henderson J.F. Kinetic studies of adenine phosphoribosyltransferase. J. Biol. Chem. 241:1966;3404.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3404
    • Hori, M.1    Henderson, J.F.2
  • 94
    • 0027207458 scopus 로고
    • Inosine monophosphate dehydrogenase from porcine (Sus-scrofa-domestica) thymus - Purification and properties
    • Pugh M.E., Skibo E.B. Inosine monophosphate dehydrogenase from porcine (Sus-scrofa-domestica) thymus - Purification and properties. Comp. Biochem. Physiol. [B]. 105:1993;381.
    • (1993) Comp. Biochem. Physiol. [B] , vol.105 , pp. 381
    • Pugh, M.E.1    Skibo, E.B.2
  • 95
    • 0016281889 scopus 로고
    • Human IMP dehydrogenase kinetics and regulatory properties
    • Holmes E.W., Pehlke D.M., Kelley N. Human IMP dehydrogenase kinetics and regulatory properties. Biochim. Biophys. Acta. 364:1974;209.
    • (1974) Biochim. Biophys. Acta , vol.364 , pp. 209
    • Holmes, E.W.1    Pehlke, D.M.2    Kelley, N.3
  • 98
    • 0016289678 scopus 로고
    • Human adenilosuccinate synthetase. Partial purification, kinetic and regulatory properties of the enzyme from placenta
    • Van der Weyden M.B., Kelley W.N. Human Adenilosuccinate Synthetase. Partial purification, kinetic and regulatory properties of the enzyme from placenta. J. Biol. Chem. 249:1974;7282.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7282
    • Van der Weyden, M.B.1    Kelley, W.N.2
  • 99
    • 0017386692 scopus 로고
    • Purification, crystalization, and properties of adenylosuccinate synthetase from rat skelethal muscle
    • Ogawa H., Shiraki H., Matsuda Y., Kakiuchi K., Nakagawa H. Purification, crystalization, and properties of adenylosuccinate synthetase from rat skelethal muscle. J. Biochem. 81:1977;859.
    • (1977) J. Biochem. , vol.81 , pp. 859
    • Ogawa, H.1    Shiraki, H.2    Matsuda, Y.3    Kakiuchi, K.4    Nakagawa, H.5
  • 100
    • 0027240254 scopus 로고
    • Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase
    • Stone R.L., Zalkin H., Dixon J.E. Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase. J. Biol. Chem. 268:1993;19710.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19710
    • Stone, R.L.1    Zalkin, H.2    Dixon, J.E.3
  • 101
    • 0018374626 scopus 로고
    • Reaction mechanism and specificity of human GMP reductase
    • Spector T., Jones T.E., Miller R.L. Reaction mechanism and specificity of human GMP reductase. J. Biol. Chem. 254:1979;2308.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2308
    • Spector, T.1    Jones, T.E.2    Miller, R.L.3
  • 102
    • 0015982948 scopus 로고
    • Guanosine 5'-phosphate reductase of human erythrocytes
    • Mackenzie J.J., Sorensen L.B. Guanosine 5'-phosphate reductase of human erythrocytes. Biochim. Biophys. Acta. 327:1973;282.
    • (1973) Biochim. Biophys. Acta , vol.327 , pp. 282
    • Mackenzie, J.J.1    Sorensen, L.B.2
  • 103
    • 0025863101 scopus 로고
    • Purification and properties of AMP-deaminase from human uterine smooth-muscle
    • Nagel-Starczynowska G., Nowak G., Kaletha K. Purification and properties of AMP-deaminase from human uterine smooth-muscle. Biochim. Biophys. Acta. 1073:1991;470.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 470
    • Nagel-Starczynowska, G.1    Nowak, G.2    Kaletha, K.3
  • 104
    • 0018276297 scopus 로고
    • Human erythrocyte 5'-AMP aminohydrolase purification and characterization
    • Yun S., Suelter C.H. Human erythrocyte 5'-AMP aminohydrolase purification and characterization. J. Biol. Chem. 253:1978;404.
    • (1978) J. Biol. Chem. , vol.253 , pp. 404
    • Yun, S.1    Suelter, C.H.2
  • 105
    • 0025950664 scopus 로고
    • Molecular-forms of human heart-muscle AMP deaminase
    • Nowak G., Kaletha K. Molecular-forms of human heart-muscle AMP deaminase. Biochem. Med. Metab. Biol. 46:1991;263.
    • (1991) Biochem. Med. Metab. Biol. , vol.46 , pp. 263
    • Nowak, G.1    Kaletha, K.2
  • 106
    • 0026628769 scopus 로고
    • Purification and properties of AMP-deaminase from human kidney
    • Nowak G., Kaletha K. Purification and properties of AMP-deaminase from human kidney. Biochem. Med. Metab. Biol. 47:1992;232.
    • (1992) Biochem. Med. Metab. Biol. , vol.47 , pp. 232
    • Nowak, G.1    Kaletha, K.2
  • 107
    • 0021891879 scopus 로고
    • Protein carboxyl methyltransferases: Two distinct classes of enzymes
    • Clarke S. Protein carboxyl methyltransferases: two distinct classes of enzymes. Ann. Rev. Biochem. 54:1985;479.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 479
    • Clarke, S.1
  • 108
    • 0014690197 scopus 로고
    • On the role of S-adenosyl-L-methionoe in the biosynthesis of spermidine by rat prostate
    • Pegg A.E., Williams-Ashman H.G. On the role of S-adenosyl-L-methionoe in the biosynthesis of spermidine by rat prostate. J. Biol. Chem. 244:1969;682.
    • (1969) J. Biol. Chem. , vol.244 , pp. 682
    • Pegg, A.E.1    Williams-Ashman, H.G.2
  • 109
    • 0026729643 scopus 로고
    • 5'-nucleotidase: Molecular estructure and functional aspects
    • Zimmermann H. 5'-Nucleotidase: molecular estructure and functional aspects. Biochem. J. 285:1992;345.
    • (1992) Biochem. J. , vol.285 , pp. 345
    • Zimmermann, H.1
  • 110
    • 0021906386 scopus 로고
    • Evidence for existence of a cytosol 5'-nucleotidase in chicken heart: Comparision of some properties of heart and liver enzymes
    • Itoh R., Oka J. Evidence for existence of a cytosol 5'-nucleotidase in chicken heart: comparision of some properties of heart and liver enzymes. Comp. Biochem. Physiol. 81B:1985;159.
    • (1985) Comp. Biochem. Physiol. , vol.81 B , pp. 159
    • Itoh, R.1    Oka, J.2
  • 111
    • 0019464958 scopus 로고
    • Purification and some properties of cytosol 5'-nucleotidase from rat liver
    • Itoh R. Purification and some properties of cytosol 5'-nucleotidase from rat liver. Biochim. Biophys. Acta. 657:1981;402.
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 402
    • Itoh, R.1
  • 112
    • 0025238470 scopus 로고
    • Cytoplasmatic 5'(3')-nucleotidase from human placenta
    • Höglund L., Reichard P. Cytoplasmatic 5'(3')-nucleotidase from human placenta. J. Biol. Chem. 265:1990;6589.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6589
    • Höglund, L.1    Reichard, P.2
  • 113
    • 0018786927 scopus 로고
    • Allosteric regulation of calf thymus ribonucleoside diphosphate reductase
    • Eriksson S., Thelander L., Akerman M. Allosteric regulation of calf thymus ribonucleoside diphosphate reductase. Biochemistry. 18:1979;2948.
    • (1979) Biochemistry , vol.18 , pp. 2948
    • Eriksson, S.1    Thelander, L.2    Akerman, M.3
  • 114
    • 25944453231 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer P.D. The binding change mechanism for ATP synthase - Some probabilities and possibilities. Biochim. Biophys. Acta. 276:1993;257.
    • (1993) Biochim. Biophys. Acta , vol.276 , pp. 257
    • Boyer, P.D.1
  • 115
    • 0014010432 scopus 로고
    • Isolation and properties of a testicular ribonucleic acid polymerase
    • Ballard P.L., Williams-Ashman H.G. Isolation and properties of a testicular ribonucleic acid polymerase. J. Biol. Chem. 241:1966;1602.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1602
    • Ballard, P.L.1    Williams-Ashman, H.G.2
  • 116
    • 0018786981 scopus 로고
    • Enzymological Characterization of DNA Polymerase alpha, Basic catalytic properties, processivity, and GAP utilization of the homogeneous enzyme from human KB cells
    • Fisher P.A., Wang T.S., Korn D. Enzymological Characterization of DNA Polymerase alpha, Basic catalytic properties, processivity, and GAP utilization of the homogeneous enzyme from human KB cells. J. Biol. Chem. 254:1979;6128.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6128
    • Fisher, P.A.1    Wang, T.S.2    Korn, D.3
  • 117
    • 78651189275 scopus 로고
    • Studies on avian xanthine dehydrogenases. Properties and patterns of appearance during development
    • Strittmatter C.F. Studies on avian xanthine dehydrogenases. Properties and patterns of appearance during development. J. Biol. Chem. 240:1965;2557.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2557
    • Strittmatter, C.F.1
  • 119
    • 0010472697 scopus 로고
    • Impairment of uric acid excretion in gout
    • Lathem W., Rodnan G.P. Impairment of uric acid excretion in gout. J. Clin. Invest. 41:1962;1955.
    • (1962) J. Clin. Invest. , vol.41 , pp. 1955
    • Lathem, W.1    Rodnan, G.P.2


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