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Volumn 321, Issue 1-2, 2003, Pages 17-23

Beginnings of feedback inhibition, allostery, and multi-protein complexes

Author keywords

Allostery; Aspartate transcarbamylase; Feedback inhibition; Metabolic regulation; Protein complex; Replitase

Indexed keywords

ALLOSTERISM; CELL FUNCTION; MOLECULAR DYNAMICS; NEGATIVE FEEDBACK; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW;

EID: 0242577550     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00839-4     Document Type: Review
Times cited : (29)

References (64)
  • 1
    • 0031800335 scopus 로고    scopus 로고
    • Deciphering the molecular code of hemoglobin allostery
    • Ackers G.K. Deciphering the molecular code of hemoglobin allostery. Adv. Protein Chem. 51:1998;185-253.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 185-253
    • Ackers, G.K.1
  • 2
    • 0242603740 scopus 로고
    • Isoleucine and valine metabolism in Escherichia coli: V. α-ketoisovaleric acid accumulation
    • Adelberg E.A., Umbarger H.E. Isoleucine and valine metabolism in Escherichia coli: V. α-ketoisovaleric acid accumulation. J. Biol. Chem. 205:1953;475-482.
    • (1953) J. Biol. Chem. , vol.205 , pp. 475-482
    • Adelberg, E.A.1    Umbarger, H.E.2
  • 3
    • 0004332571 scopus 로고
    • Regulation of enzyme activity
    • Atkinson D.E. Regulation of enzyme activity. Annu. Rev. Biochem. 35:1966;85-124.
    • (1966) Annu. Rev. Biochem. , vol.35 , pp. 85-124
    • Atkinson, D.E.1
  • 4
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Barnett G., Kennedy E.P. The enzymatic phosphorylation of proteins. J. Biol. Chem. 211:1954;969-988.
    • (1954) J. Biol. Chem. , vol.211 , pp. 969-988
    • Barnett, G.1    Kennedy, E.P.2
  • 5
    • 0033545974 scopus 로고    scopus 로고
    • Assessment of the allosteric mechanisms of aspartate transcarbamylase based on the crystalline structure of the unregulated catalytic subunit
    • Beernick P.T., Endrizzi J.A., et al. Assessment of the allosteric mechanisms of aspartate transcarbamylase based on the crystalline structure of the unregulated catalytic subunit. Proc. Natl. Acad. Sci. U. S. A. 96:1999;5388-5393.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5388-5393
    • Beernick, P.T.1    Endrizzi, J.A.2
  • 6
    • 0025259631 scopus 로고
    • Receptor-effector coupling by G proteins
    • Birnbaumer L., Abramowitz J., et al. Receptor-effector coupling by G proteins. Biochem. Biophys. Acta. 1031:1990;163-224.
    • (1990) Biochem. Biophys. Acta , vol.1031 , pp. 163-224
    • Birnbaumer, L.1    Abramowitz, J.2
  • 7
    • 0242435440 scopus 로고
    • Some factors affecting the secretion of orotic acid by mutants of Aerobacter aerogenes
    • Brooke M.S., Ushiba D., et al. Some factors affecting the secretion of orotic acid by mutants of Aerobacter aerogenes. J. Bacteriol. 68:1954;534-540.
    • (1954) J. Bacteriol. , vol.68 , pp. 534-540
    • Brooke, M.S.1    Ushiba, D.2
  • 8
    • 73049119821 scopus 로고
    • The feedback control mechanism of biosynthetic L-threonone deaminase by L-isoleucine
    • Changeux J.P. The feedback control mechanism of biosynthetic L-threonone deaminase by L-isoleucine. Cold Spring Harbor Symp. Quant. Biol. 26:1961;313-318.
    • (1961) Cold Spring Harbor Symp. Quant. Biol. , vol.26 , pp. 313-318
    • Changeux, J.P.1
  • 9
    • 0020449755 scopus 로고
    • Characteristics of bacteriophage T4-induced complex synthesizing deoxyribonucleotides
    • Chiu C.S., Cook K.S., Greenberg G.R. Characteristics of bacteriophage T4-induced complex synthesizing deoxyribonucleotides. J. Biol. Chem. 257:1982;15087-15097.
    • (1982) J. Biol. Chem. , vol.257 , pp. 15087-15097
    • Chiu, C.S.1    Cook, K.S.2    Greenberg, G.R.3
  • 10
    • 77951302123 scopus 로고
    • La biosynthese induite des enzymes (adaptation enzymatique)
    • Cohn M., Monod J. La biosynthese induite des enzymes (adaptation enzymatique). Adv. Enzymol. 13:1952;67-119.
    • (1952) Adv. Enzymol. , vol.13 , pp. 67-119
    • Cohn, M.1    Monod, J.2
  • 11
    • 84977290695 scopus 로고
    • Cold spring harbor symposia on quantitative biology
    • New York: Cold Spring Harbor Laboratory
    • Cold Spring Harbor Symposia on Quantitative Biology Cellular Regulatory Mechanisms. vol. XXVI:1961;Cold Spring Harbor Laboratory, New York.
    • (1961) Cellular Regulatory Mechanisms , vol.25
  • 12
    • 0242687723 scopus 로고
    • Studies on nutritionally deficient bacterial mutants isolated by means of penicillin
    • Davis B.D. Studies on nutritionally deficient bacterial mutants isolated by means of penicillin. Experientia. 6:1950;41-50.
    • (1950) Experientia , vol.6 , pp. 41-50
    • Davis, B.D.1
  • 13
    • 26344480786 scopus 로고
    • The regulation of pyrimidine synthesis in Neurospora crassa. End-product inhibition and repression of aspartate transcarbamylase
    • Donachie W.D. The regulation of pyrimidine synthesis in Neurospora crassa. End-product inhibition and repression of aspartate transcarbamylase. Biochim. Biophys. Acta. 82:1964;292-294.
    • (1964) Biochim. Biophys. Acta , vol.82 , pp. 292-294
    • Donachie, W.D.1
  • 14
    • 0242435444 scopus 로고
    • Separation of feedback inhibition from activity of aspartate transcarbamylase (ATCase)
    • Gerhart J.C., Pardee A.B. Separation of feedback inhibition from activity of aspartate transcarbamylase (ATCase). Fed. Proc. 20:1961;224.
    • (1961) Fed. Proc. , vol.20 , pp. 224
    • Gerhart, J.C.1    Pardee, A.B.2
  • 15
    • 0001425337 scopus 로고
    • The enzymology of control by feedback inhibition
    • Gerhart J.C., Pardee A.B. The enzymology of control by feedback inhibition. J. Biol. Chem. 237:1962;891-896.
    • (1962) J. Biol. Chem. , vol.237 , pp. 891-896
    • Gerhart, J.C.1    Pardee, A.B.2
  • 16
    • 0000572386 scopus 로고
    • The effect of the feedback inhibitor, CTP, on subunit interactions in aspartate transcarbamylase
    • Gerhart J.C., Pardee A.B. The effect of the feedback inhibitor, CTP, on subunit interactions in aspartate transcarbamylase. Cold Spring Harbor Symp. Quant. Biol. 28:1963;491-496.
    • (1963) Cold Spring Harbor Symp. Quant. Biol. , vol.28 , pp. 491-496
    • Gerhart, J.C.1    Pardee, A.B.2
  • 17
    • 0013784860 scopus 로고
    • Distinct subunits for the regulatory and catalytic activity of aspartate transcarbamylase
    • Gerhart J.C., Schachman H.K. Distinct subunits for the regulatory and catalytic activity of aspartate transcarbamylase. Biochemistry. 4:1965;1054-1062.
    • (1965) Biochemistry , vol.4 , pp. 1054-1062
    • Gerhart, J.C.1    Schachman, H.K.2
  • 18
    • 0015890890 scopus 로고
    • Familial hypercholesterolemia: Identification of a defect in the regulation of 3-hydroxy-3-methyl glutaryl coenzyme A reductase activity associated with the overproduction of cholesterol
    • Goldstein J.L., Brown M. Familial hypercholesterolemia: identification of a defect in the regulation of 3-hydroxy-3-methyl glutaryl coenzyme A reductase activity associated with the overproduction of cholesterol. Proc. Natl. Acad. Sci. U. S. A. 70:1973;2804-2808.
    • (1973) Proc. Natl. Acad. Sci. U. S. A. , vol.70 , pp. 2804-2808
    • Goldstein, J.L.1    Brown, M.2
  • 19
    • 0001033264 scopus 로고
    • The potential for transformation of a biosynthetic enzyme in Escherichia coli
    • Gorini L., Mass W.K. The potential for transformation of a biosynthetic enzyme in Escherichia coli. Biochim. Biophys. Acta. 25:1957;208-209.
    • (1957) Biochim. Biophys. Acta , vol.25 , pp. 208-209
    • Gorini, L.1    Mass, W.K.2
  • 20
    • 0034821747 scopus 로고    scopus 로고
    • Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamylase versus yeast chorismate mutase
    • Helmstaedt K., Krappmann S.J., et al. Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamylase versus yeast chorismate mutase. Microbiol. Mol. Biol. Rev. 65:2001;404-421.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 404-421
    • Helmstaedt, K.1    Krappmann, S.J.2
  • 21
    • 0018823799 scopus 로고
    • Pyrimidine nucleotide biosynthesis in animals: Genes, enzymes, and regulation of UMP biosynthesis
    • Jones M.E. Pyrimidine nucleotide biosynthesis in animals: genes, enzymes, and regulation of UMP biosynthesis. Annu. Rev. Biochem. 49:1980;253-279.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 253-279
    • Jones, M.E.1
  • 23
    • 0001858251 scopus 로고
    • Applications of a theory of enzyme specificity to protein synthesis
    • Koshland D.E. Jr. Applications of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. U. S. A. 44:1958;98-104.
    • (1958) Proc. Natl. Acad. Sci. U. S. A. , vol.44 , pp. 98-104
    • Koshland Jr., D.E.1
  • 24
    • 0037033008 scopus 로고    scopus 로고
    • Proteomics and models for enzyme cooperativity
    • Koshland D.E. Jr., Hamadani K. Proteomics and models for enzyme cooperativity. J. Biol. Chem. 277:2002;46841-46844.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46841-46844
    • Koshland Jr., D.E.1    Hamadani, K.2
  • 25
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D.E. Jr., Nemethy G., et al. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 5:1966;365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2
  • 26
    • 0027399487 scopus 로고
    • Crystal structure of CTP-ligated T state aspartate transcarbamylase at 2.5 A resolution: Implications for ATCase mutants and the mechanism of negative cooperativity
    • Kosman R.P., Gouaux J.E., et al. Crystal structure of CTP-ligated T state aspartate transcarbamylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins. 15:1993;147-176.
    • (1993) Proteins , vol.15 , pp. 147-176
    • Kosman, R.P.1    Gouaux, J.E.2
  • 27
    • 0034047774 scopus 로고    scopus 로고
    • Interactions between protein kinases and proteases in cellular signaling and regulation. Interactions between protein kinases and proteases in cellular signaling and regulation
    • Krebs E.G., Graves J.D. Interactions between protein kinases and proteases in cellular signaling and regulation. Interactions between protein kinases and proteases in cellular signaling and regulation. Adv. Enzyme Regul. 40:2000;441-470.
    • (2000) Adv. Enzyme Regul. , vol.40 , pp. 441-470
    • Krebs, E.G.1    Graves, J.D.2
  • 28
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim W.A. The modular logic of signaling proteins: building allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12:2002;61-68.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 29
    • 0014217178 scopus 로고
    • Cytidine triphosphate synthetase of Escherichia coli B
    • Long C.W., Pardee A.B. Cytidine triphosphate synthetase of Escherichia coli B. J. Biol. Chem. 242:1967;4715-4720.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4715-4720
    • Long, C.W.1    Pardee, A.B.2
  • 30
    • 0000107415 scopus 로고
    • The first enzyme in histidine biosynthesis; the nature of feedback inhibition by histidine
    • Martin R.G. The first enzyme in histidine biosynthesis; the nature of feedback inhibition by histidine. J. Biol. Chem. 238:1963;257-262.
    • (1963) J. Biol. Chem. , vol.238 , pp. 257-262
    • Martin, R.G.1
  • 31
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod J., Changeux J.-P., et al. Allosteric proteins and cellular control systems. J. Mol. Biol. 6:1963;306-329.
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.-P.2
  • 32
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J., Wyman J., et al. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:1965;88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2
  • 33
    • 0034912714 scopus 로고    scopus 로고
    • Transcriptional coactivator complexes
    • Naar A.M., et al. Transcriptional coactivator complexes. Annu. Rev. Biochem. 70:2001;475-501.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 475-501
    • Naar, A.M.1
  • 34
    • 0020714345 scopus 로고
    • Rapid incorporation of label from ribonucleoside diphosphates into DNA by a cell-free high molecular weight fraction from animal cell nuclei
    • Noguchi H., Reddy G.P.V., Pardee A.B. Rapid incorporation of label from ribonucleoside diphosphates into DNA by a cell-free high molecular weight fraction from animal cell nuclei. Cell. 32:1983;443-451.
    • (1983) Cell , vol.32 , pp. 443-451
    • Noguchi, H.1    Reddy, G.P.V.2    Pardee, A.B.3
  • 35
    • 0242603739 scopus 로고
    • Experiments with the chemostat on the rates of amino acid synthesis in bacteria
    • E.J. Boell. Princeton, NJ: Princeton Univ. Press
    • Novick A., Szilard L. Experiments with the chemostat on the rates of amino acid synthesis in bacteria. Boell E.J. Dynamics of Growth Processes. 1954;21-32 Princeton Univ. Press, Princeton, NJ.
    • (1954) Dynamics of Growth Processes , pp. 21-32
    • Novick, A.1    Szilard, L.2
  • 36
    • 0033991699 scopus 로고    scopus 로고
    • Macromolecular compartmentation and channeling
    • Ovadi J., Srere P.A. Macromolecular compartmentation and channeling. Int. Rev. Cytol. 192:2000;255-280.
    • (2000) Int. Rev. Cytol. , vol.192 , pp. 255-280
    • Ovadi, J.1    Srere, P.A.2
  • 37
    • 0001753721 scopus 로고
    • Nucleic acid precursors and protein synthesis
    • Pardee A.B. Nucleic acid precursors and protein synthesis. Proc. Natl. Acad. Sci. U. S. A. 40:1954;263-270.
    • (1954) Proc. Natl. Acad. Sci. U. S. A. , vol.40 , pp. 263-270
    • Pardee, A.B.1
  • 38
    • 0002609734 scopus 로고
    • The control of enzyme activity
    • P.D. Boyer, H. Lardy, & K. Myrback. NY: Academic Press
    • Pardee A.B. The control of enzyme activity. Boyer P.D., Lardy H., Myrback K. The Enzymes. 2nd ed. 1959;681-716 Academic Press, NY.
    • (1959) The Enzymes 2nd ed. , pp. 681-716
    • Pardee, A.B.1
  • 39
    • 84957358412 scopus 로고
    • Inhibition of succinic dehydrogenase by oxalacetate
    • Pardee A.B., Potter V.R. Inhibition of succinic dehydrogenase by oxalacetate. J. Biol. Chem. 176:1948;1085-1094.
    • (1948) J. Biol. Chem. , vol.176 , pp. 1085-1094
    • Pardee, A.B.1    Potter, V.R.2
  • 40
    • 0010139923 scopus 로고
    • The dependence of nucleic acid synthesis on the presence of amino acids in E. coli
    • Pardee A.B., Prestidge L.S. The dependence of nucleic acid synthesis on the presence of amino acids in E. coli. J. Bacteriol. 71:1956;677-683.
    • (1956) J. Bacteriol. , vol.71 , pp. 677-683
    • Pardee, A.B.1    Prestidge, L.S.2
  • 41
    • 0242603733 scopus 로고
    • Chromatophores of Rhodospirillum rubrum
    • Pardee A.B., et al. Chromatophores of Rhodospirillum rubrum. Nature. 169:1952;282-284.
    • (1952) Nature , vol.169 , pp. 282-284
    • Pardee, A.B.1
  • 42
    • 85010253669 scopus 로고
    • The genetic control and cytoplasmic expression of " Inducibility" in the synthesis of β-galactosidase by E. coli
    • Pardee A.B., Jacob F., et al. The genetic control and cytoplasmic expression of "Inducibility" in the synthesis of β-galactosidase by E. coli. J. Mol. Biol. 1:1959;165-178.
    • (1959) J. Mol. Biol. , vol.1 , pp. 165-178
    • Pardee, A.B.1    Jacob, F.2
  • 43
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions
    • Pearson G., Robinson F., et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr. Rev. 22:2001;153-183.
    • (2001) Endocr. Rev. , vol.22 , pp. 153-183
    • Pearson, G.1    Robinson, F.2
  • 44
    • 0025296739 scopus 로고
    • Allosteric interaction of components of the replitase complex is responsible for enzyme cross-inhibition
    • Plucinski T.M., Fager R.S., Reddy G.P. Allosteric interaction of components of the replitase complex is responsible for enzyme cross-inhibition. Mol. Pharmacol. 38:1990;114-120.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 114-120
    • Plucinski, T.M.1    Fager, R.S.2    Reddy, G.P.3
  • 45
    • 0024725673 scopus 로고
    • Compartmentation of deoxypyrimidine nucleotides for nuclear DNA replication in S phase mammalian cells
    • Reddy G.P. Compartmentation of deoxypyrimidine nucleotides for nuclear DNA replication in S phase mammalian cells. J. Mol. Recognit. 2:1989;75-83.
    • (1989) J. Mol. Recognit. , vol.2 , pp. 75-83
    • Reddy, G.P.1
  • 46
    • 0017809276 scopus 로고
    • Functional compartmentation of DNA precursors in T4 phage-infected bacteria
    • Reddy G.P., Mathews C. Functional compartmentation of DNA precursors in T4 phage-infected bacteria. J. Biol. Chem. 253:1978;3461-3467.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3461-3467
    • Reddy, G.P.1    Mathews, C.2
  • 47
    • 0019025846 scopus 로고
    • Multienzyme complex for metabolic channeling in mammalian DNA replication
    • Reddy G.P.V., Pardee A.B. Multienzyme complex for metabolic channeling in mammalian DNA replication. Proc. Natl. Acad. Sci. U. S. A. 77:1980;3312-3316.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3312-3316
    • Reddy, G.P.V.1    Pardee, A.B.2
  • 48
    • 0020479750 scopus 로고
    • Coupled ribonucleoside diphosphate reductions, channeling, and incorporation into DNA of mammalian cells
    • Reddy G.P.V., Pardee A.B. Coupled ribonucleoside diphosphate reductions, channeling, and incorporation into DNA of mammalian cells. J. Biol. Chem. 257:1982;12526-12531.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12526-12531
    • Reddy, G.P.V.1    Pardee, A.B.2
  • 49
    • 0020580432 scopus 로고
    • Inhibitor evidence for allosteric interaction in the replitase multienzyme complex
    • Reddy G.P.V., Pardee A.B. Inhibitor evidence for allosteric interaction in the replitase multienzyme complex. Nature. 303:1983;86-88.
    • (1983) Nature , vol.303 , pp. 86-88
    • Reddy, G.P.V.1    Pardee, A.B.2
  • 50
    • 0003678206 scopus 로고
    • Studies on Biosynthesis in Escherichia coli
    • Washington
    • Roberts R.R., Abelson P.H., et al. Studies on Biosynthesis in Escherichia coli. 1955;607 Carnegie Inst. of Washington Publ. Washington, DC.
    • (1955) , pp. 607
    • Roberts, R.R.1    Abelson, P.H.2
  • 51
    • 0001398450 scopus 로고
    • Studies on the macromolecular organization of microbial cells
    • Schachman H.K., et al. Studies on the macromolecular organization of microbial cells. Arch. Biochem. Biophys. 38:1952;245-260.
    • (1952) Arch. Biochem. Biophys. , vol.38 , pp. 245-260
    • Schachman, H.K.1
  • 52
    • 0010081536 scopus 로고
    • Production and crystallization of aspartate transcarbamylase
    • Shepherdson M., Pardee A.B. Production and crystallization of aspartate transcarbamylase. J. Biol. Chem. 235:1960;3233-3237.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3233-3237
    • Shepherdson, M.1    Pardee, A.B.2
  • 53
    • 0013978134 scopus 로고
    • Allosteric regulation of enzyme activity
    • Stadtman E.R. Allosteric regulation of enzyme activity. Adv. Enzymol. 28:1966;41-154.
    • (1966) Adv. Enzymol. , vol.28 , pp. 41-154
    • Stadtman, E.R.1
  • 55
    • 73049166942 scopus 로고
    • Regulation of the enzyme activity of glutamic dehydrogenase mediated by changes of its structure
    • Tompkins G.M., Yielding K.L. Regulation of the enzyme activity of glutamic dehydrogenase mediated by changes of its structure. Cold Spring Harbor Symp. Quant. Biol. 26:1961;331-341.
    • (1961) Cold Spring Harbor Symp. Quant. Biol. , vol.26 , pp. 331-341
    • Tompkins, G.M.1    Yielding, K.L.2
  • 56
    • 0000832972 scopus 로고
    • Evidence for a negative feedback mechanism in the biosynthesis of isoleucine
    • Umbarger H.E. Evidence for a negative feedback mechanism in the biosynthesis of isoleucine. Science. 123:1956;848.
    • (1956) Science , vol.123 , pp. 848
    • Umbarger, H.E.1
  • 57
    • 0034734275 scopus 로고    scopus 로고
    • Allostery in very large molecular assemblies
    • Van Holde K.E., Miller K.I., et al. Allostery in very large molecular assemblies. Biophys. Chem. 86:2000;165-172.
    • (2000) Biophys. Chem. , vol.86 , pp. 165-172
    • Van Holde, K.E.1    Miller, K.I.2
  • 58
    • 15844412738 scopus 로고    scopus 로고
    • T4 phage gene 32 protein as a candidate organizing factor for the deoxyribonucleoside triphosphate synthetase complex
    • Wheeler L.J., Ray N.B., Ungermann C., et al. T4 phage gene 32 protein as a candidate organizing factor for the deoxyribonucleoside triphosphate synthetase complex. J. Biol. Chem. 271:1996;11156-11162.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11156-11162
    • Wheeler, L.J.1    Ray, N.B.2    Ungermann, C.3
  • 59
    • 0000019673 scopus 로고
    • Regulation of threonine biosynthesis in E. coli
    • Wormser E.H., Pardee A.B. Regulation of threonine biosynthesis in E. coli. Arch. Biochem. Biophys. 78:1958;416-432.
    • (1958) Arch. Biochem. Biophys. , vol.78 , pp. 416-432
    • Wormser, E.H.1    Pardee, A.B.2
  • 60
    • 0016905989 scopus 로고
    • Regulation of purine biosynthesis and turnover
    • Wyngaarden J.B. Regulation of purine biosynthesis and turnover. Adv. Enzyme Regul. 14:1976;25-42.
    • (1976) Adv. Enzyme Regul. , vol.14 , pp. 25-42
    • Wyngaarden, J.B.1
  • 61
    • 0242603734 scopus 로고
    • Studies on pyrimidine synthesis in E. coli
    • Yates R.A., Pardee A.B. Studies on pyrimidine synthesis in E. coli. Science. 120:1954;903.
    • (1954) Science , vol.120 , pp. 903
    • Yates, R.A.1    Pardee, A.B.2
  • 62
    • 0001738509 scopus 로고
    • Control of pyrimidine biosynthesis in E. coli by a feed-back mechanism
    • Yates R.A., Pardee A.B. Control of pyrimidine biosynthesis in E. coli by a feed-back mechanism. J. Biol. Chem. 221:1956;743-756.
    • (1956) J. Biol. Chem. , vol.221 , pp. 743-756
    • Yates, R.A.1    Pardee, A.B.2
  • 63
    • 0001738507 scopus 로고
    • Pyrimidine biosynthesis in E. coli
    • Yates R.A., Pardee A.B. Pyrimidine biosynthesis in E. coli. J. Biol. Chem. 221:1956;757-770.
    • (1956) J. Biol. Chem. , vol.221 , pp. 757-770
    • Yates, R.A.1    Pardee, A.B.2
  • 64
    • 0010081534 scopus 로고
    • Control by uracil of formation of enzymes required for rotate synthesis
    • Yates R.A., Pardee A.B. Control by uracil of formation of enzymes required for rotate synthesis. J. Biol. Chem. 227:1957;677-692.
    • (1957) J. Biol. Chem. , vol.227 , pp. 677-692
    • Yates, R.A.1    Pardee, A.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.