메뉴 건너뛰기




Volumn 179, Issue 15, 1997, Pages 4689-4698

Characterization of a gene cluster for glycogen biosynthesis and a heterotetrameric ADP-glucose pyrophosphorylase from Bacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; GLYCOGEN;

EID: 0030872426     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.15.4689-4698.1997     Document Type: Article
Times cited : (50)

References (54)
  • 1
    • 0028871062 scopus 로고
    • Adenosine diphosphate glucose pyrophosphorylase genes in wheat: Differential expression and gene mapping
    • Ainsworth, C., F. Hosein, M. Tarvis, F. Weir, M. Burrell, K. M. Devos, and M. D. Gale. 1995. Adenosine diphosphate glucose pyrophosphorylase genes in wheat: differential expression and gene mapping. Planta 197:1-10.
    • (1995) Planta , vol.197 , pp. 1-10
    • Ainsworth, C.1    Hosein, F.2    Tarvis, M.3    Weir, F.4    Burrell, M.5    Devos, K.M.6    Gale, M.D.7
  • 2
    • 0024978421 scopus 로고
    • The encoded primary sequence of a rice seed ADP-glucose pyrophosphorylase subunit and its homology to the bacterial enzyme
    • Anderson, J. M., R. Larsen, D. Laudencia, W. T. Kim, D. Morrow, T. W. Okita, and J. Preiss. 1989. The encoded primary sequence of a rice seed ADP-glucose pyrophosphorylase subunit and its homology to the bacterial enzyme. J. Biol. Chem. 264:12238-12242.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12238-12242
    • Anderson, J.M.1    Larsen, R.2    Laudencia, D.3    Kim, W.T.4    Morrow, D.5    Okita, T.W.6    Preiss, J.7
  • 3
    • 0020541951 scopus 로고
    • Biosynthesis of bacterial glycogen: Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glgC gene
    • Baecker, P. A., C. E. Furlong, and J. Preiss. 1983. Biosynthesis of bacterial glycogen: primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glgC gene. J. Biol. Chem. 258:5084-5088.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5084-5088
    • Baecker, P.A.1    Furlong, C.E.2    Preiss, J.3
  • 4
    • 0025101773 scopus 로고
    • The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch-branching enzyme
    • Bhattacharyya, M. K., A. M. Smith, T. H. N. Ellis, C. Hedley, and C. Martin. 1990. The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch-branching enzyme. Cell 60:115-122.
    • (1990) Cell , vol.60 , pp. 115-122
    • Bhattacharyya, M.K.1    Smith, A.M.2    Ellis, T.H.N.3    Hedley, C.4    Martin, C.5
  • 5
    • 0028040192 scopus 로고
    • Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae
    • Cannon, J. F., J. R. Pringle, A. Fiechter, and M. Khalil. 1994. Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae. Genetics 136:485-503.
    • (1994) Genetics , vol.136 , pp. 485-503
    • Cannon, J.F.1    Pringle, J.R.2    Fiechter, A.3    Khalil, M.4
  • 6
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Ferenstein, J. 1987. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783-791.
    • (1987) Evolution , vol.39 , pp. 783-791
    • Ferenstein, J.1
  • 7
    • 0030063579 scopus 로고    scopus 로고
    • Introduction of sense and antisense cDNA for branching enzyme in the amylose-free potato mutant leads to physico-chemical changes in the starch
    • Flipse, E., L. Suurs, C. J. A. M. Keetels, J. Kossmann, E. Jacobsen, and R. G. F. Visser. 1996. Introduction of sense and antisense cDNA for branching enzyme in the amylose-free potato mutant leads to physico-chemical changes in the starch. Planta 198:340-347.
    • (1996) Planta , vol.198 , pp. 340-347
    • Flipse, E.1    Suurs, L.2    Keetels, C.J.A.M.3    Kossmann, J.4    Jacobsen, E.5    Visser, R.G.F.6
  • 8
    • 0025078378 scopus 로고
    • Identification of Lys15 at the active site of Escherichia culi glycogen synthase. Conservation of a Lys-X-Gly-Gly in the bacterial and mammalian enzymes
    • Furukawa, K., M. Tagaya, M. Inouye, J. Preiss, and T. Fukui. 1990. Identification of Lys15 at the active site of Escherichia culi glycogen synthase. Conservation of a Lys-X-Gly-Gly in the bacterial and mammalian enzymes. J. Biol. Chem. 265:2086-2090.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2086-2090
    • Furukawa, K.1    Tagaya, M.2    Inouye, M.3    Preiss, J.4    Fukui, T.5
  • 9
    • 0028174042 scopus 로고
    • Identification of Lys277 at the active site of Escherichia coli glycogen synthase. Application of affinity labeling combined with site-directed mutagenesis
    • Furukawa, K., M. Tagaya, K. Tanizawa, and T. Fukui. 1994. Identification of Lys277 at the active site of Escherichia coli glycogen synthase. Application of affinity labeling combined with site-directed mutagenesis. J. Biol. Chem. 269:868-871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 868-871
    • Furukawa, K.1    Tagaya, M.2    Tanizawa, K.3    Fukui, T.4
  • 10
    • 0014011424 scopus 로고
    • Adenosine diphosphate glucose pyrophosphorylase: A regulatory enzyme in the biosynthesis of starch in spinach chloroplasts
    • Ghosh, H. P., and J. Preiss. 1966. Adenosine diphosphate glucose pyrophosphorylase: a regulatory enzyme in the biosynthesis of starch in spinach chloroplasts. J. Biol. Chem. 241:4491-4504.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4491-4504
    • Ghosh, H.P.1    Preiss, J.2
  • 11
    • 0029866101 scopus 로고    scopus 로고
    • Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation
    • Greene, T. W., S. E. Chantler, M. L. Kahn, G. F. Barry, J. Preiss, and T. W. Okita. 1996. Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation. Proc. Natl. Acad. Sci. USA 93:1509-1513.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1509-1513
    • Greene, T.W.1    Chantler, S.E.2    Kahn, M.L.3    Barry, G.F.4    Preiss, J.5    Okita, T.W.6
  • 12
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C. M., M. Aldea, B. K. Washburn, P. Babitzke, and S. R. Kushner. 1989. New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171:4617-4622.
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 13
    • 0022909286 scopus 로고
    • Promoter used by sigma-29 RNA polymerase from Bacillus subtilis
    • Hay, R. E., K. M. Tatti, B. S. Void, C. J. Green, and C. P. Moran, Jr. 1986. Promoter used by sigma-29 RNA polymerase from Bacillus subtilis. Gene 48:301-306.
    • (1986) Gene , vol.48 , pp. 301-306
    • Hay, R.E.1    Tatti, K.M.2    Void, B.S.3    Green, C.J.4    Moran Jr., C.P.5
  • 14
    • 0026681771 scopus 로고
    • Identification and molecular analysis of glgS, a novel growth-phase-regulated and rpoS-dependent gene involved in glycogen synthesis in Escherichia coli
    • Hengge-Aronis, R., and D. Fischer. 1992. Identification and molecular analysis of glgS, a novel growth-phase-regulated and rpoS-dependent gene involved in glycogen synthesis in Escherichia coli. Mol. Microbiol. 6:1877-1886.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1877-1886
    • Hengge-Aronis, R.1    Fischer, D.2
  • 15
    • 0344198225 scopus 로고
    • Molecular cloning and sequencing of ADP-glucose pyrophosphorylase from Synechocystis PCC6803
    • Kakefuda, G., Y.-Y. Charng, A. A. Iglesias, L. McIntosh, and J. Preiss. 1992. Molecular cloning and sequencing of ADP-glucose pyrophosphorylase from Synechocystis PCC6803. Plant Physiol. 99:359-361.
    • (1992) Plant Physiol. , vol.99 , pp. 359-361
    • Kakefuda, G.1    Charng, Y.-Y.2    Iglesias, A.A.3    McIntosh, L.4    Preiss, J.5
  • 16
    • 0026068257 scopus 로고
    • Molecular cloning and nucleotide sequence of glycogen branching enzyme gene (glgB) from Bacillus stearothermophilus and expression in Escherichia coli and Bacillus subtilis
    • Kiel, J. A. K. W., J. M. Boels, G. Beldman, and G. Venema. 1991. Molecular cloning and nucleotide sequence of glycogen branching enzyme gene (glgB) from Bacillus stearothermophilus and expression in Escherichia coli and Bacillus subtilis. Mol. Gen. Genet. 230:136-144.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 136-144
    • Kiel, J.A.K.W.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 17
    • 0027023616 scopus 로고
    • The glgB gene from the thermophile Bacillus culdolyticus encodes a thermolabile branching enzyme
    • Kiel, J. A. K. W., J. M. Boels, G. Beldman, and G. Venema. 1992. The glgB gene from the thermophile Bacillus culdolyticus encodes a thermolabile branching enzyme. DNA Seq.-J. DNA Seq. Map. 3:221-232.
    • (1992) DNA Seq.-J. DNA Seq. Map. , vol.3 , pp. 221-232
    • Kiel, J.A.K.W.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 18
    • 0028174763 scopus 로고
    • Glycogen in Bacillus subtilis: Molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation
    • Kiel, J. A. K. W., J. M. Boels, G. Beldman, and G. Venema. 1994. Glycogen in Bacillus subtilis: molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation. Mol. Microbiol. 11:203-218.
    • (1994) Mol. Microbiol. , vol.11 , pp. 203-218
    • Kiel, J.A.K.W.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 19
    • 0029903484 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable ADP-glucose pyrophosphorylase from Thermus caldophilus GK-24
    • Ko, J. H., C. H. Kim, D.-S. Lee, and Y. S. Kim. 1996. Purification and characterization of a thermostable ADP-glucose pyrophosphorylase from Thermus caldophilus GK-24. Biochem. J. 319:977-983.
    • (1996) Biochem. J. , vol.319 , pp. 977-983
    • Ko, J.H.1    Kim, C.H.2    Lee, D.-S.3    Kim, Y.S.4
  • 20
    • 0020463405 scopus 로고
    • Glycogen in thermoacidophilic archaebacteria of the genera Sulfolobus, Thermoproteus, Desulfurococcus, and Thermococcus
    • König, H., R. Skorko, W. Zillig, and W.-D. Reiter. 1982. Glycogen in thermoacidophilic archaebacteria of the genera Sulfolobus, Thermoproteus, Desulfurococcus, and Thermococcus. Arch. Microbiol. 132:297-303.
    • (1982) Arch. Microbiol. , vol.132 , pp. 297-303
    • König, H.1    Skorko, R.2    Zillig, W.3    Reiter, W.-D.4
  • 22
    • 0023988701 scopus 로고
    • New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis
    • Kuriki, T., S. Okada, and T. Imanaka. 1988. New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis. J. Bacteriol. 170:1554-1559.
    • (1988) J. Bacteriol. , vol.170 , pp. 1554-1559
    • Kuriki, T.1    Okada, S.2    Imanaka, T.3
  • 23
    • 0004104379 scopus 로고
    • Purification and characterization of thermostable pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis
    • Kuriki, T., J.-H. Park, S. Okada, and T. Imanaka. 1988. Purification and characterization of thermostable pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis. Appl. Environ. Microbiol. 54:2881-2883.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 2881-2883
    • Kuriki, T.1    Park, J.-H.2    Okada, S.3    Imanaka, T.4
  • 24
    • 0028942619 scopus 로고
    • Molecular cloning and characterization of novel isoforms of potato ADP-glucose pyrophosphorylase
    • La Cognata, U., L. Willmitzer, and B. Müller-Röber. 1995. Molecular cloning and characterization of novel isoforms of potato ADP-glucose pyrophosphorylase. Mol. Gen. Genet. 246:538-548.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 538-548
    • La Cognata, U.1    Willmitzer, L.2    Müller-Röber, B.3
  • 25
    • 0030198862 scopus 로고    scopus 로고
    • Identification of the major starch synthase in the soluble fraction of potato tubers
    • Marshall, J., C. Sidebottom, M. Debet, A. M. Smith, and A. Edwards. 1996. Identification of the major starch synthase in the soluble fraction of potato tubers. Plant Cell 8:1121-1135.
    • (1996) Plant Cell , vol.8 , pp. 1121-1135
    • Marshall, J.1    Sidebottom, C.2    Debet, M.3    Smith, A.M.4    Edwards, A.5
  • 26
    • 0020645043 scopus 로고
    • New M13 vectors for cloning
    • Messing, J. 1983. New M13 vectors for cloning. Methods Enzymol. 101:20-78.
    • (1983) Methods Enzymol. , vol.101 , pp. 20-78
    • Messing, J.1
  • 28
  • 30
    • 0021144092 scopus 로고
    • Bacterial glycogen synthesis and its regulation
    • Preiss, J. 1984. Bacterial glycogen synthesis and its regulation. Annu. Rev. Microbiol. 38:419-458.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 419-458
    • Preiss, J.1
  • 31
    • 0002998420 scopus 로고
    • Biology and molecular biology of starch synthesis and its regulation
    • B. J. Miflin (ed.), Oxford University Press, Oxford, United Kingdom
    • Preiss, J. 1991. Biology and molecular biology of starch synthesis and its regulation, p. 59-114. In B. J. Miflin (ed.), Oxford survey of plant molecular and cellular biology. Oxford University Press, Oxford, United Kingdom.
    • (1991) Oxford Survey of Plant Molecular and Cellular Biology , pp. 59-114
    • Preiss, J.1
  • 32
    • 0041111565 scopus 로고
    • Biosynthesis of starch: ADPglucose pyrophosphorylase, the regulatory enzymes of starch synthesis: structure-function relationship
    • Preiss, J. 1993. Biosynthesis of starch: ADPglucose pyrophosphorylase, the regulatory enzymes of starch synthesis: structure-function relationship. Denpun Kagaku 40:117-131.
    • (1993) Denpun Kagaku , vol.40 , pp. 117-131
    • Preiss, J.1
  • 33
    • 0016764585 scopus 로고
    • Biosynthesis of bacterial glycogen: Kinetic studies of a glucose-1-phosphate adenyltransferase (EC 2.7.7.27) from a glycogen-deficient mutant of Escherichia coli B
    • Preiss, J., E. Greenberg, and A. Sbraw. 1975. Biosynthesis of bacterial glycogen: kinetic studies of a glucose-1-phosphate adenyltransferase (EC 2.7.7.27) from a glycogen-deficient mutant of Escherichia coli B. J. Biol. Chem. 250:7631-7638.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7631-7638
    • Preiss, J.1    Greenberg, E.2    Sbraw, A.3
  • 34
    • 0024834054 scopus 로고
    • Physiology, biochemistry and genetics of bacterial glycogen synthesis
    • Preiss, J., and T. Romeo. 1989. Physiology, biochemistry and genetics of bacterial glycogen synthesis. Adv. Microb. Physiol. 30:183-238.
    • (1989) Adv. Microb. Physiol. , vol.30 , pp. 183-238
    • Preiss, J.1    Romeo, T.2
  • 35
    • 0028189275 scopus 로고
    • Molecular biology and regulatory aspects of glycogen biosynthesis in bacteria
    • Preiss, J., and T. Romeo. 1994. Molecular biology and regulatory aspects of glycogen biosynthesis in bacteria. Prog. Nucleic Acid Res. Mol. Biol. 47:299-329.
    • (1994) Prog. Nucleic Acid Res. Mol. Biol. , vol.47 , pp. 299-329
    • Preiss, J.1    Romeo, T.2
  • 36
    • 0028306907 scopus 로고
    • The mechanism of translational coupling in Escherichia coli: Higher order structure in the atpHa mRNA acts as a conformational switch regulating the access of de novo initiating ribosomes
    • Rex, G., B. Surin, G. Besse, B. Schneppe, and J. E. G. McCathy. 1994. The mechanism of translational coupling in Escherichia coli: higher order structure in the atpHA mRNA acts as a conformational switch regulating the access of de novo initiating ribosomes. J. Biol. Chem. 269:18118-18127.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18118-18127
    • Rex, G.1    Surin, B.2    Besse, G.3    Schneppe, B.4    McCathy, J.E.G.5
  • 37
    • 0029796886 scopus 로고    scopus 로고
    • Post-transcriptional regulation of bacterial carbohydrate metabolism: Evidence that the gene product Csra is a global mRNA decay factor
    • Romeo, T. 1996. Post-transcriptional regulation of bacterial carbohydrate metabolism: evidence that the gene product CsrA is a global mRNA decay factor. Res. Microbiol. 147:505-512.
    • (1996) Res. Microbiol. , vol.147 , pp. 505-512
    • Romeo, T.1
  • 38
    • 0023792288 scopus 로고
    • Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes
    • Romeo, T., A. Kumar, and J. Preiss. 1988. Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes. Gene 70:363-376.
    • (1988) Gene , vol.70 , pp. 363-376
    • Romeo, T.1    Kumar, A.2    Preiss, J.3
  • 39
    • 0021828037 scopus 로고
    • Assay of inorganic phosphate in the mild pH range, suitable for measurement of glycogen phosphorylase activity
    • Saheki, S., A. Takeda, and T. Shimazu. 1985. Assay of inorganic phosphate in the mild pH range, suitable for measurement of glycogen phosphorylase activity. Anal. Biochem. 148:277-281.
    • (1985) Anal. Biochem. , vol.148 , pp. 277-281
    • Saheki, S.1    Takeda, A.2    Shimazu, T.3
  • 40
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 42
    • 0016176041 scopus 로고
    • Polysaccharide that may serve as a carbon and energy storage compound for sporulation in Bacillus cereus
    • Slock, J. A., and D. P. Stahly. 1974. Polysaccharide that may serve as a carbon and energy storage compound for sporulation in Bacillus cereus. J. Bacteriol. 120:399-406.
    • (1974) J. Bacteriol. , vol.120 , pp. 399-406
    • Slock, J.A.1    Stahly, D.P.2
  • 43
    • 0001481929 scopus 로고
    • Major differences in isoforms of starch-branching enzyme between developing embryos of round- and wrinkled-seeded peas (Pisum sativum L.)
    • Smith, A. M. 1988. Major differences in isoforms of starch-branching enzyme between developing embryos of round- and wrinkled-seeded peas (Pisum sativum L.). Planta 175:270-279.
    • (1988) Planta , vol.175 , pp. 270-279
    • Smith, A.M.1
  • 44
    • 0001825801 scopus 로고
    • Enzymes of starch synthesis
    • Smith, A. M. 1990. Enzymes of starch synthesis. Methods Plant Biochem. 3:93-102.
    • (1990) Methods Plant Biochem. , vol.3 , pp. 93-102
    • Smith, A.M.1
  • 45
    • 0002625568 scopus 로고
    • Regulatory proteins that control late-growth development
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), American Society for Microbiology, Washington, D.C.
    • Smith, I. 1993. Regulatory proteins that control late-growth development, p. 785-800. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria: Biochemistry, Physiology, and Molecular Genetics , pp. 785-800
    • Smith, I.1
  • 46
    • 0026767213 scopus 로고
    • Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources
    • Smith-White, B. J., and J. Preiss. 1994. Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources. J. Mol. Evol. 34:449-464.
    • (1994) J. Mol. Evol. , vol.34 , pp. 449-464
    • Smith-White, B.J.1    Preiss, J.2
  • 47
    • 0027991845 scopus 로고
    • Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus
    • Takata, H., T. Takaha, T. Kuriki, S. Okada, M. Takagi, and T. Imanaka. 1994. Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus. Appl. Environ. Microbiol. 60:3095-3104.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3095-3104
    • Takata, H.1    Takaha, T.2    Kuriki, T.3    Okada, S.4    Takagi, M.5    Imanaka, T.6
  • 49
    • 0029952935 scopus 로고    scopus 로고
    • Structure of the cyclic glucan produced from amylopectin by Bacillus stearothermophilus branching enzyme
    • Takata, H., T. Takaha, S. Okada, S. Hizukuri, M. Takagi, and T. Imanaka. 1996. Structure of the cyclic glucan produced from amylopectin by Bacillus stearothermophilus branching enzyme. Carbohydr. Res. 295:91-101.
    • (1996) Carbohydr. Res. , vol.295 , pp. 91-101
    • Takata, H.1    Takaha, T.2    Okada, S.3    Hizukuri, S.4    Takagi, M.5    Imanaka, T.6
  • 51
    • 0000985063 scopus 로고
    • ADP-glucose pyrophosphorylase large subunit cDNA from barley endosperm
    • Villand, P., O.-A. Olsen, A. Kilian, and G. N. Kleczknowski. 1992. ADP-glucose pyrophosphorylase large subunit cDNA from barley endosperm. Plant Physiol. 100:1617-1618.
    • (1992) Plant Physiol. , vol.100 , pp. 1617-1618
    • Villand, P.1    Olsen, O.-A.2    Kilian, A.3    Kleczknowski, G.N.4
  • 52
    • 0030571543 scopus 로고    scopus 로고
    • Phylogenetic distribution of the global regulatory gene csrA among eubacteria
    • White, D., M. E. Hart, and T. Romeo. 1996. Phylogenetic distribution of the global regulatory gene csrA among eubacteria. Gene 182:221-223.
    • (1996) Gene , vol.182 , pp. 221-223
    • White, D.1    Hart, M.E.2    Romeo, T.3
  • 53
    • 9044240473 scopus 로고    scopus 로고
    • Coordinate genetic regulation of glycogen catabolism and biosynthesis in Escherichia coli via the CsrA gene product
    • Yang, H., M. Y. Liu, and T. Romeo. 1996. Coordinate genetic regulation of glycogen catabolism and biosynthesis in Escherichia coli via the CsrA gene product. J. Bacteriol. 178:1012-1017.
    • (1996) J. Bacteriol. , vol.178 , pp. 1012-1017
    • Yang, H.1    Liu, M.Y.2    Romeo, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.