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Volumn 35, Issue 3, 2000, Pages 141-196

Understanding and influencing starch biochemistry

Author keywords

Amylopectin; Amylose; And degradtion); Biotechnology; Phosphorylation; Starch (structure; Synthesis

Indexed keywords

AMYLOPECTIN; AMYLOSE; STARCH; SUCROSE;

EID: 0033940474     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (111)

References (417)
  • 2
    • 0030470475 scopus 로고    scopus 로고
    • Cloning and functional analysis of a cDNA encoding a novel starch synthase from potato (Solanum tuberosum L.)
    • Abel, G. J. W., Springer, F., Willmitzer, L., and Kossmann, J., 1996. Cloning and functional analysis of a cDNA encoding a novel starch synthase from potato (Solanum tuberosum L.) Plant J. 10: 981-991.
    • (1996) Plant J. , vol.10 , pp. 981-991
    • Abel, G.J.W.1    Springer, F.2    Willmitzer, L.3    Kossmann, J.4
  • 3
    • 0008600573 scopus 로고
    • Synthesis of α-1:6-glucosidic linkages by a transglucosylase from potato
    • Abdullah, M. and Whelan, W. J., 1960. Synthesis of α-1:6-glucosidic linkages by a transglucosylase from potato. Biochem. J. 75: 12.
    • (1960) Biochem. J. , vol.75 , pp. 12
    • Abdullah, M.1    Whelan, W.J.2
  • 4
    • 0008530698 scopus 로고
    • Starch metabolism in developing and germinating soya bean seeds is independent of β-amylase activity
    • Adams, C. A., Broman, T. H. and Rinne, R. W., 1981. Starch metabolism in developing and germinating soya bean seeds is independent of β-amylase activity. Ann. Bot. 48: 433-439.
    • (1981) Ann. Bot. , vol.48 , pp. 433-439
    • Adams, C.A.1    Broman, T.H.2    Rinne, R.W.3
  • 5
    • 0003356027 scopus 로고
    • Topographic aspects of biosynthesis, extracellular secretion, and intracellular storage of proteins in plant cells
    • Akazawa, T. and Hara-Nishimura, I., 1985. Topographic aspects of biosynthesis, extracellular secretion, and intracellular storage of proteins in plant cells. Ann. Rev. Plant. Physiol. 36: 441-472.
    • (1985) Ann. Rev. Plant. Physiol. , vol.36 , pp. 441-472
    • Akazawa, T.1    Hara-Nishimura, I.2
  • 6
    • 84940971054 scopus 로고
    • Hexose phosphate metabolism by non-photosynthetic tissues of higher plants
    • Preiss, J., Ed., Academic Press, San Diego
    • ap Rees, T., 1988. Hexose phosphate metabolism by non-photosynthetic tissues of higher plants. In: The biochemistry of plants, Vol. 14, pp. 1-34. Preiss, J., Ed., Academic Press, San Diego.
    • (1988) The Biochemistry of Plants , vol.14 , pp. 1-34
    • Rees, T.1
  • 7
    • 0008601325 scopus 로고
    • Potato tuber UDP glucose protein transglucosylase catalyzes its own glycosylation
    • Ardila, F. J. and Tandecarz, J. S., 1992. Potato tuber UDP glucose protein transglucosylase catalyzes its own glycosylation. Plant Physiol. 99: 1342-1347.
    • (1992) Plant Physiol. , vol.99 , pp. 1342-1347
    • Ardila, F.J.1    Tandecarz, J.S.2
  • 8
    • 84987227344 scopus 로고
    • Characterization of endosperm stzarch from high-amylose mutants of rice
    • Asaoka, M., Okuno, K., Sugimoto, Y., Yano, M., Omura, T., and Fuwa H., 1986. Characterization of endosperm stzarch from high-amylose mutants of rice. Starch/ Staerke 38: 114-117.
    • (1986) Starch/Staerke , vol.38 , pp. 114-117
    • Asaoka, M.1    Okuno, K.2    Sugimoto, Y.3    Yano, M.4    Omura, T.5    Fuwa, H.6
  • 9
    • 0003161971 scopus 로고
    • Acceptor molecule of granular-bound starch synthase from sweet-potato roots
    • Baba, T., Yoshii, M., and Kainuma, K., 1987. Acceptor molecule of granular-bound starch synthase from sweet-potato roots. Starch/Staerke 39: 52-56.
    • (1987) Starch/Staerke , vol.39 , pp. 52-56
    • Baba, T.1    Yoshii, M.2    Kainuma, K.3
  • 11
    • 0008601326 scopus 로고
    • Abhandlung zur physikalischen chemie der stärke und der brotbereitung. XXV. Weitere beobachtungen über die blöckchenstruktur der stärkekörner
    • Badenhuizen, N. P., 1936. Abhandlung zur physikalischen Chemie der Stärke und der Brotbereitung. XXV. Weitere Beobachtungen über die Blöckchenstruktur der Stärkekörner. Z. Physik. Chem. (A) 175: 383-395.
    • (1936) Z. Physik. Chem. (A) , vol.175 , pp. 383-395
    • Badenhuizen, N.P.1
  • 12
    • 0008531120 scopus 로고
    • Die struktur des stärkekorns
    • Badenhuizen, N. P., 1937. Die Struktur des Stärkekorns. Protoplasma 28: 293-326.
    • (1937) Protoplasma , vol.28 , pp. 293-326
    • Badenhuizen, N.P.1
  • 13
    • 0008530062 scopus 로고
    • Formation and distribution of amylose and amylopectin in the starch granule
    • Badenhuizen, N. P., 1963. Formation and distribution of amylose and amylopectin in the starch granule. Nature 197: 464-467.
    • (1963) Nature , vol.197 , pp. 464-467
    • Badenhuizen, N.P.1
  • 14
    • 0000915901 scopus 로고
    • Cloning and characterisation of the Brittle-2 gene of maize
    • Bae, J. M., Giroux, M. and Hannah, L., 1990. Cloning and characterisation of the Brittle-2 gene of maize. Maydica 35: 317-322.
    • (1990) Maydica , vol.35 , pp. 317-322
    • Bae, J.M.1    Giroux, M.2    Hannah, L.3
  • 15
    • 0023025007 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-alpha-D-glucan 1,4-alpha-D-glucan 6-alpha-D-1,4-alpha-D-glucanotransferase as deduced from the nucleotide sequence of the glgB gene
    • Baecker, P. A., Greenberg, E., and Preiss, J., 1986. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-alpha-D-glucan 1,4-alpha-D-glucan 6-alpha-D-1,4-alpha-D-glucanotransferase as deduced from the nucleotide sequence of the glgB gene. J. Biol.Chem. 261: 8738-8743.
    • (1986) J. Biol.chem. , vol.261 , pp. 8738-8743
    • Baecker, P.A.1    Greenberg, E.2    Preiss, J.3
  • 18
    • 0000802027 scopus 로고
    • Gibberellic acid regulated expression of α-amylase and six other genes in wheat aleurone layers
    • Baulcombe, D. C. and Buffard, D. 1983. Gibberellic acid regulated expression of α-amylase and six other genes in wheat aleurone layers. Planta 157: 493-501.
    • (1983) Planta , vol.157 , pp. 493-501
    • Baulcombe, D.C.1    Buffard, D.2
  • 21
    • 85132282528 scopus 로고
    • Glucose-1,6-bisphosphate-the regulator of carbohydrate metabolism
    • Beitner, R., Ed., CRC Press
    • Beitner, R., 1985. Glucose-1,6-bisphosphate-the regulator of carbohydrate metabolism. In: The regulation of carbohydrate metabolism, Vol. 1. pp. 1-27. Beitner, R., Ed., CRC Press.
    • (1985) The Regulation of Carbohydrate Metabolism , vol.1 , pp. 1-27
    • Beitner, R.1
  • 23
    • 0000861328 scopus 로고    scopus 로고
    • Starch modification: Challenges and prospects
    • BeMiller, J. N., 1997b. Starch modification: challenges and prospects. Starch/Staerke 49: 127-131.
    • (1997) Starch/Staerke , vol.49 , pp. 127-131
    • BeMiller, J.N.1
  • 24
    • 0029198613 scopus 로고
    • Assessing genotypic softness in single wheat kernels using starch granule associated friabilin as a biochemical marker
    • Bettge, A. D., Morris, C. F., and Greenblatt, G. A. 1995. Assessing genotypic softness in single wheat kernels using starch granule associated friabilin as a biochemical marker. Euphytica 86: 65-72.
    • (1995) Euphytica , vol.86 , pp. 65-72
    • Bettge, A.D.1    Morris, C.F.2    Greenblatt, G.A.3
  • 25
    • 0025101773 scopus 로고
    • The wrinkled seed character described by Mendel is caused by a transposon-like insertion in a gene encoding starch branching enzyme
    • Bhattacharyya, M. K., Smith, A. M., Ellis, T. H. N., Hedley, C., and Martin, C., 1990. The wrinkled seed character 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
  • 26
    • 0025443897 scopus 로고
    • Identification and molecular characterization of shrunken-2 cDNA clones of maize
    • Bhave, M. R., Lawrence, S., Barton, C., and Hannah, L. C., 1990. Identification and molecular characterization of shrunken-2 cDNA clones of maize. Plant Cell 2: 581-588.
    • (1990) Plant Cell , vol.2 , pp. 581-588
    • Bhave, M.R.1    Lawrence, S.2    Barton, C.3    Hannah, L.C.4
  • 27
    • 0001432113 scopus 로고
    • Genetic interactions affecting maize phytoglycogen and the phytoglycogen-forming branching enzyme
    • Black, R. C., Loerch, J. D., McArdle, F. J., and Creech, R. G., 1966. Genetic interactions affecting maize phytoglycogen and the phytoglycogen-forming branching enzyme. Genetics 53: 661-668.
    • (1966) Genetics , vol.53 , pp. 661-668
    • Black, R.C.1    Loerch, J.D.2    McArdle, F.J.3    Creech, R.G.4
  • 28
    • 0032004183 scopus 로고    scopus 로고
    • The degree of starch phosphorylation is related to the chain length distribution of the neutral and the phosphorylated chains of amylopectin
    • Blennow, A., Bay-Smidt, A. M., Wischmann, B., Olsen C. E., and Møller B. L., 1998. The degree of starch phosphorylation is related to the chain length distribution of the neutral and the phosphorylated chains of amylopectin. Carbohydr. Res. 307: 45-54.
    • (1998) Carbohydr. Res. , vol.307 , pp. 45-54
    • Blennow, A.1    Bay-Smidt, A.M.2    Wischmann, B.3    Olsen, C.E.A.4    Møller, B.L.5
  • 29
    • 0025192953 scopus 로고
    • Phosphate 31 NMR studies of spinach leaves and their chloroplasts
    • Bligny, R., Gardestrom, P., Roby, C., and Douce, R., 1990. Phosphate 31 NMR studies of spinach leaves and their chloroplasts. J. Biol. Chem. 265: 1319-1326.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1319-1326
    • Bligny, R.1    Gardestrom, P.2    Roby, C.3    Douce, R.4
  • 30
    • 0027223990 scopus 로고
    • Complete amino acid sequence of puroindoline, a new basic and cystine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning
    • Blochet, J-E., Chevalier, C., Forest, E., Pebay-Peyroula, E., Gautier, M-F., Joudrier, P., Pézolet, M., and Marion, D., 1993. Complete amino acid sequence of puroindoline, a new basic and cystine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning. FEBS Lett. 329: 326-340.
    • (1993) FEBS Lett. , vol.329 , pp. 326-340
    • Blochet, J.-E.1    Chevalier, C.2    Forest, E.3    Pebay-Peyroula, E.4    Gautier, M.-F.5    Joudrier, P.6    Pézolet, M.7    Marion, D.8
  • 32
    • 0030971410 scopus 로고    scopus 로고
    • Initiation of starch biosynthesis: Purification and characterization of UDP-glucose:Protein transglucosylase from potato tubers
    • Bocca, S. N., Rothschild, A., and Tandecarz, J. S., 1997. Initiation of starch biosynthesis: purification and characterization of UDP-glucose:protein transglucosylase from potato tubers. Plant Physiol. Biochem. 35: 205-212.
    • (1997) Plant Physiol. Biochem. , vol.35 , pp. 205-212
    • Bocca, S.N.1    Rothschild, A.2    Tandecarz, J.S.3
  • 33
    • 0029177691 scopus 로고
    • Mutant genes at the r and rb loci affect the structure and physicochenical properties of pea seed starches
    • Bogracheva, T. Y., Davydova, N. I., Genin, Y. V., and Hedley, C. L., 1995. Mutant genes at the r and rb loci affect the structure and physicochenical properties of pea seed starches. J. Exp. Bot. 46: 1905-1913.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1905-1913
    • Bogracheva, T.Y.1    Davydova, N.I.2    Genin, Y.V.3    Hedley, C.L.4
  • 34
    • 0017237006 scopus 로고
    • On the mechanism of amylose branching by potato Q-enzyme
    • Borovosky, D., Smith, E. E., and Whelan, W. J., 1976. On the mechanism of amylose branching by potato Q-enzyme. Eur. J. Biochem. 62: 307-312.
    • (1976) Eur. J. Biochem. , vol.62 , pp. 307-312
    • Borovosky, D.1    Smith, E.E.2    Whelan, W.J.3
  • 35
    • 0018559081 scopus 로고
    • The mechanism of Q-enzyme action and its influence on the structure of amylopectin
    • Borovsky, D., Smith, E. E., Whelan, W.J ., French, D., and Kikumoto, S., 1979. The mechanism of Q-enzyme action and its influence on the structure of amylopectin. Arch. Biochem. Biophys. 198: 627-631.
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 627-631
    • Borovsky, D.1    Smith, E.E.2    Whelan, W.J.3    French, D.4    Kikumoto, S.5
  • 37
    • 0017887611 scopus 로고
    • Multiple forms of starch branching enzyme of maize. Evidence for independent genetic control
    • Boyer, C. D., and Preiss, J., 1978. Multiple forms of starch branching enzyme of maize. Evidence for independent genetic control. Biochem. Biophys. Res. Commun. 80: 169-175.
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 169-175
    • Boyer, C.D.1    Preiss, J.2
  • 38
    • 0008531606 scopus 로고
    • Properties of citrate stimulated starch synthesis catalyzed by starch synthase I of developing maize kernels
    • Boyer, C. D., and Preiss, J., 1979. Properties of citrate stimulated starch synthesis catalyzed by starch synthase I of developing maize kernels. Plant Physiol. 64. 1039-1042
    • (1979) Plant Physiol. , vol.64 , pp. 1039-1042
    • Boyer, C.D.1    Preiss, J.2
  • 39
    • 0000586974 scopus 로고
    • Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases
    • Boyer, C. D. and Preiss, J., 1981. Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases. Plant Physiol. 67: 1141-1145.
    • (1981) Plant Physiol. , vol.67 , pp. 1141-1145
    • Boyer, C.D.1    Preiss, J.2
  • 40
    • 0001876941 scopus 로고
    • Hormones and carbohydrate metabolism in germinating cereal grains
    • Millborrow, B. V., Ed., Academic Press, London
    • Briggs, D. E. 1973. Hormones and carbohydrate metabolism in germinating cereal grains. In: Biosynthesis and its control in plants. pp. 219-277. Millborrow, B. V., Ed., Academic Press, London.
    • (1973) Biosynthesis and Its Control in Plants , pp. 219-277
    • Briggs, D.E.1
  • 41
    • 0024656022 scopus 로고
    • Maturation and subcellular compartmentation of potato starch phosphorylase
    • Brisson, N., Giroux, H., Zollinger, M., Camirand, A., and Simard, C., 1989. Maturation and subcellular compartmentation of potato starch phosphorylase. Plant Cell 1,559-566.
    • (1989) Plant Cell , vol.1 , pp. 559-566
    • Brisson, N.1    Giroux, H.2    Zollinger, M.3    Camirand, A.4    Simard, C.5
  • 42
    • 0031277490 scopus 로고    scopus 로고
    • Starches from A to C: Chlamydomonas reinhardtii as a model microbial system to investigate the biosynthesis of the amylopectin crystal
    • Buléon, A., Gallant, D. J., Bouchet, B., Mouille, G., D'Hulst, C., Kossmann, J., and Ball, S., 1997. Starches from A to C: Chlamydomonas reinhardtii as a model microbial system to investigate the biosynthesis of the amylopectin crystal. Plant Physiol. 115: 949-957.
    • (1997) Plant Physiol. , vol.115 , pp. 949-957
    • Buléon, A.1    Gallant, D.J.2    Bouchet, B.3    Mouille, G.4    D'Hulst, C.5    Kossmann, J.6    Ball, S.7
  • 44
    • 0015690669 scopus 로고
    • The phosphorylases of developing maize seeds
    • Burr, B. and Nelson, O. E., 1973. The phosphorylases of developing maize seeds. Ann. N. Y. Acad. Sci. 210: 129-138.
    • (1973) Ann. N. Y. Acad. Sci. , vol.210 , pp. 129-138
    • Burr, B.1    Nelson, O.E.2
  • 45
  • 46
    • 0001012947 scopus 로고
    • Submicroscopic development and structure of starch granules in cereal endosperms
    • Buttrose, M. S., 1960. Submicroscopic development and structure of starch granules in cereal endosperms. J. Ultrastructure Res. 4: 231-257.
    • (1960) J. Ultrastructure Res. , vol.4 , pp. 231-257
    • Buttrose, M.S.1
  • 47
    • 0001207884 scopus 로고
    • The influence of environment on the shell structure of starch granules
    • Buttrose, M. S., 1962. The influence of environment on the shell structure of starch granules. J. Cell Biol. 14: 159-167
    • (1962) J. Cell Biol. , vol.14 , pp. 159-167
    • Buttrose, M.S.1
  • 48
    • 84979324828 scopus 로고
    • Electron microscopy of acid-degraded starch granules
    • Buttrose, M. S., 1963. Electron microscopy of acid-degraded starch granules. Starch/Staerke 15: 85-92.
    • (1963) Starch/Staerke , vol.15 , pp. 85-92
    • Buttrose, M.S.1
  • 49
    • 0008566614 scopus 로고
    • Carbohydrate relationships in developing and mature endosperm of brittle and related maize genotypes
    • Cameron, J. W. and Teas, H. J., 1954. Carbohydrate relationships in developing and mature endosperm of brittle and related maize genotypes. Am. J. Bot. 41: 50-55.
    • (1954) Am. J. Bot. , vol.41 , pp. 50-55
    • Cameron, J.W.1    Teas, H.J.2
  • 50
    • 0028351246 scopus 로고
    • Detection of specific glucose-3-phosphatase activity in rat liver
    • Canales, J., Buitrago, F., Faraldo, A., and Cameselle, J.C., 1994. Detection of specific glucose-3-phosphatase activity in rat liver. FEBS Lett. 339: 55-58.
    • (1994) FEBS Lett. , vol.339 , pp. 55-58
    • Canales, J.1    Buitrago, F.2    Faraldo, A.3    Cameselle, J.C.4
  • 51
    • 0031195003 scopus 로고    scopus 로고
    • Identification of rat liver glucose-3-phosphate phosphatase as an inositol monophosphatase inhibited by lithium
    • Canales, J., Buitrago, F., Faraldo, A., Avalos, M., and Cameselle, J. C., 1997. Identification of rat liver glucose-3-phosphate phosphatase as an inositol monophosphatase inhibited by lithium. Arch. Biochem. Biophys. 343: 27-34
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 27-34
    • Canales, J.1    Buitrago, F.2    Faraldo, A.3    Avalos, M.4    Cameselle, J.C.5
  • 52
    • 0029186042 scopus 로고
    • BtI, a structural gene for the major 39-44 kDa amyloplast membrane polypeptides
    • Cao, H., Sullivan, T. D., Boyer, C. D., and Shannon, J. C., 1995. BtI, a structural gene for the major 39-44 kDa amyloplast membrane polypeptides. Physiol. Plant. 95: 176-186
    • (1995) Physiol. Plant. , vol.95 , pp. 176-186
    • Cao, H.1    Sullivan, T.D.2    Boyer, C.D.3    Shannon, J.C.4
  • 54
    • 0028807733 scopus 로고
    • Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae
    • Cheng, C., Mu, J., Farkas, I., Huang, D., Goebl, M. G., and Roach, P. J., 1995. Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae. Mol. Cell. Biol. 15: 6632-6640.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6632-6640
    • Cheng, C.1    Mu, J.2    Farkas, I.3    Huang, D.4    Goebl, M.G.5    Roach, P.J.6
  • 55
    • 0017034186 scopus 로고
    • The enzymatic deficiency conditioned by the shrunken-1 mutations in maize
    • Chourey, P. S. and Nelson, O. E., 1976. The enzymatic deficiency conditioned by the shrunken-1 mutations in maize. Biochemical Genetics. 14: 1041-1055.
    • (1976) Biochemical Genetics. , vol.14 , pp. 1041-1055
    • Chourey, P.S.1    Nelson, O.E.2
  • 56
    • 0000941910 scopus 로고
    • Gibberellic acid enhanced synthesis and release of α-amylase and ribonuclease by isolated barley aleurone layers
    • Chrispeels, M. J. and Varner, J. E., 1967. Gibberellic acid enhanced synthesis and release of α-amylase and ribonuclease by isolated barley aleurone layers. Plant Physiol. 42: 398-406.
    • (1967) Plant Physiol. , vol.42 , pp. 398-406
    • Chrispeels, M.J.1    Varner, J.E.2
  • 57
    • 0008594909 scopus 로고
    • A new type of Indian corn from China
    • Collins, G. N., 1909. A new type of Indian corn from China. USDA Bur. Plant Indus. Bull. 161: 1-30
    • (1909) USDA Bur. Plant Indus. Bull. , vol.161 , pp. 1-30
    • Collins, G.N.1
  • 58
    • 0002548171 scopus 로고
    • Pisum sativum and Vicia faba carbohydrates. IV. Granular structure of wrinkled pea starch
    • Colonna, P., Buléon, A., Mercier, C., and Lemaguer, M., 1982. Pisum sativum and Vicia faba carbohydrates. IV. Granular structure of wrinkled pea starch. Carbohydr. Polymers 2: 43-50.
    • (1982) Carbohydr. Polymers , vol.2 , pp. 43-50
    • Colonna, P.1    Buléon, A.2    Mercier, C.3    Lemaguer, M.4
  • 59
    • 0000198207 scopus 로고
    • Macromolecular structure of wrinkled-and smooth-pea starch components
    • Colonna, P. and Mercier, C., 1984. Macromolecular structure of wrinkled-and smooth-pea starch components. Carbohydr. Res. 126: 233-247.
    • (1984) Carbohydr. Res. , vol.126 , pp. 233-247
    • Colonna, P.1    Mercier, C.2
  • 60
    • 0000708149 scopus 로고
    • Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains
    • Cornford, C. A., Black, M., Chapman, J. M., and Baulcombe, D. C., 1986. Expression of α-amylase and other gibberellin-regulated genes in aleurone tissue of developing wheat grains. Planta 169: 420-428.
    • (1986) Planta , vol.169 , pp. 420-428
    • Cornford, C.A.1    Black, M.2    Chapman, J.M.3    Baulcombe, D.C.4
  • 61
    • 0028817160 scopus 로고
    • Properties of potato starch: Effects of genotype and growing conditions
    • Cottrell, J. E., Duffus, C. M., Paterson, L., and Mackay, G.R., 1995. Properties of potato starch: Effects of genotype and growing conditions. Phytochemistry 40: 1057-1064.
    • (1995) Phytochemistry , vol.40 , pp. 1057-1064
    • Cottrell, J.E.1    Duffus, C.M.2    Paterson, L.3    Mackay, G.R.4
  • 63
    • 0000674351 scopus 로고
    • Genetic control of carbohydrate biosynthesis in maize endosperm
    • Creech, R. G., 1965. Genetic control of carbohydrate biosynthesis in maize endosperm. Genetics 52: 1175-1186.
    • (1965) Genetics , vol.52 , pp. 1175-1186
    • Creech, R.G.1
  • 64
    • 0002488054 scopus 로고
    • Genetic analysis and biochemical characterization of mutants impairing glycogen metabolism
    • Piras, R. and Pontis, H.G., Eds., Academic Press, New York
    • Creuzat-Sigal, N., Latil-Damotte, M., Cattaneo, J., and Puig J., 1972. Genetic analysis and biochemical characterization of mutants impairing glycogen metabolism. In: Biochemistry of the glycoside linkage. pp. 647-680. Piras, R. and Pontis, H.G., Eds., Academic Press, New York.
    • (1972) Biochemistry of the Glycoside Linkage , pp. 647-680
    • Creuzat-Sigal, N.1    Latil-Damotte, M.2    Cattaneo, J.3    Puig, J.4
  • 65
    • 11744349958 scopus 로고
    • Die mikroskopie der stärkekörner
    • Ulmann, M. Ed., Verlag Paul Parey, Berlin
    • Czaja, A. T., 1969. Die Mikroskopie der Stärkekörner. In: Handbuch der Stärke in Einzeldarstellungen Vol.6, Ulmann, M. Ed., Verlag Paul Parey, Berlin.
    • (1969) Handbuch der Stärke in Einzeldarstellungen Vol.6 , vol.6
    • Czaja, A.T.1
  • 66
    • 0000144655 scopus 로고
    • Cereal β-amylase: Immunochemical study on two enzyme-deficient inbred lines of rye
    • Daussant, J., Zbaszyniak, B., Sadowski, J., and Wiatroszak, I., 1981. Cereal β-amylase: immunochemical study on two enzyme-deficient inbred lines of rye. Planta, 151: 176-179.
    • (1981) Planta , vol.151 , pp. 176-179
    • Daussant, J.1    Zbaszyniak, B.2    Sadowski, J.3    Wiatroszak, I.4
  • 67
    • 0001358068 scopus 로고
    • Detection and partial characterization of two antigenically distinct ß-amylases in developing kernels of wheat
    • Daussant, J., and Laurière, C., 1990. Detection and partial characterization of two antigenically distinct ß-amylases in developing kernels of wheat. Planta 181: 505-511.
    • (1990) Planta , vol.181 , pp. 505-511
    • Daussant, J.1    Laurière, C.2
  • 68
    • 0002450734 scopus 로고
    • Independent regulatory aspects and posttranslational modifications of two β-amy lases of rye: Use of a mutant inbred line
    • Daussant, J., Sadowski, J., Rorat, C. T., Mayer, C., and Laurière, C., 1991. Independent regulatory aspects and posttranslational modifications of two β-amy lases of rye: use of a mutant inbred line. Plant Physiol. 96: 84-90.
    • (1991) Plant Physiol. , vol.96 , pp. 84-90
    • Daussant, J.1    Sadowski, J.2    Rorat, C.T.3    Mayer, C.4    Laurière, C.5
  • 70
    • 0006128979 scopus 로고
    • Control of α-amylase mRNA accumulation by gibberellic acid and calcium in barley aleurone layers
    • Deikman, J. and Jones, R. L., 1985. Control of α-amylase mRNA accumulation by gibberellic acid and calcium in barley aleurone layers. Plant Physiol. 80: 672-675.
    • (1985) Plant Physiol. , vol.80 , pp. 672-675
    • Deikman, J.1    Jones, R.L.2
  • 71
    • 0026652567 scopus 로고
    • Waxy Chlamydomonas rheinhardtii monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin
    • Delrue, B., Fontaine, T., Routier, F., Decq, A., Wieruszeski, J. M., Van Den Koornhuyse, N., Maddelein, M. L., Fournet, B., and Ball S., 1992. Waxy Chlamydomonas rheinhardtii monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin. J. Bacteriol. 174: 3612-3620.
    • (1992) J. Bacteriol. , vol.174 , pp. 3612-3620
    • Delrue, B.1    Fontaine, T.2    Routier, F.3    Decq, A.4    Wieruszeski, J.M.5    Van Den Koornhuyse, N.6    Maddelein, M.L.7    Fournet, B.8    Ball, S.9
  • 72
    • 0001016713 scopus 로고
    • The purification and characterization of the two forms of soluble starch synthase from developing pea embryos
    • Denyer, K. and Smith, A. M., 1992. The purification and characterization of the two forms of soluble starch synthase from developing pea embryos. Planta 186: 609-617.
    • (1992) Planta , vol.186 , pp. 609-617
    • Denyer, K.1    Smith, A.M.2
  • 73
    • 0027630893 scopus 로고
    • Soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos
    • Denyer, K., Sidebottom, C., Hylton, C. M., and Smith, A. M., 1993. Soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos. Plant J. 4: 191-198.
    • (1993) Plant J. , vol.4 , pp. 191-198
    • Denyer, K.1    Sidebottom, C.2    Hylton, C.M.3    Smith, A.M.4
  • 74
    • 0028874114 scopus 로고
    • The contributions of adenosine 5′-diphosphoglucose pyrophosphorylase and starch-branching enzyme to the control of starch synthesis in developing pea embryos
    • Denyer, K., Foster, J., and Smith A. M., 1995a. The contributions of adenosine 5′-diphosphoglucose pyrophosphorylase and starch-branching enzyme to the control of starch synthesis in developing pea embryos. Planta 197: 57-62.
    • (1995) Planta , vol.197 , pp. 57-62
    • Denyer, K.1    Foster, J.2    Smith, A.M.3
  • 76
    • 0029168494 scopus 로고
    • Identification of multiple isoforms of soluble and granule-bound starch synthase in developing wheat endosperm
    • Denyer, K., Hylton, C. M., Jenner, C. F., and Smith, A. M., 1995c. Identification of multiple isoforms of soluble and granule-bound starch synthase in developing wheat endosperm. Planta 196: 256-265.
    • (1995) Planta , vol.196 , pp. 256-265
    • Denyer, K.1    Hylton, C.M.2    Jenner, C.F.3    Smith, A.M.4
  • 77
    • 0030267532 scopus 로고    scopus 로고
    • The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial
    • Denyer, K., Dunlap, F., Thorbjornsen, T., Keeling, P., and Smith, A. M., 1996a. The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial. Plant Physiol. 112: 779-785.
    • (1996) Plant Physiol. , vol.112 , pp. 779-785
    • Denyer, K.1    Dunlap, F.2    Thorbjornsen, T.3    Keeling, P.4    Smith, A.M.5
  • 78
    • 0030482430 scopus 로고    scopus 로고
    • The elongation of amylose and amylopectin chains in isolated starch granules
    • Denyer, K., Clarke, B., Hylton, C., Tatge, H., and Smith, A. M., 1996b. The elongation of amylose and amylopectin chains in isolated starch granules. Plant J. 10: 1135-1143.
    • (1996) Plant J. , vol.10 , pp. 1135-1143
    • Denyer, K.1    Clarke, B.2    Hylton, C.3    Tatge, H.4    Smith, A.M.5
  • 80
    • 0030737904 scopus 로고    scopus 로고
    • A reversibly glycosylated polypeptide (RGP1) possibly involved in plant cell wall synthesis: Purification, gene cloning, and trans-Golgi localization
    • Dhugga, K. S., Tiwari, S. C., and Ray, P. M., 1997. A reversibly glycosylated polypeptide (RGP1) possibly involved in plant cell wall synthesis: purification, gene cloning, and trans-Golgi localization. PNAS 94: 7679-7684.
    • (1997) PNAS , vol.94 , pp. 7679-7684
    • Dhugga, K.S.1    Tiwari, S.C.2    Ray, P.M.3
  • 82
    • 0001574803 scopus 로고
    • Presence of ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize endosperm
    • Dickinson, D. B. and Preiss, J., 1969. Presence of ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize endosperm. Plant Phys. 44: 1058-1062.
    • (1969) Plant Phys. , vol.44 , pp. 1058-1062
    • Dickinson, D.B.1    Preiss, J.2
  • 83
    • 85013153088 scopus 로고
    • Two classes of starch debranching enzymes from developing maize kernels
    • Doehlert, D. C., and Knutson, C. A. 1991. Two classes of starch debranching enzymes from developing maize kernels. J. Plant Physiol. 13: 566-572.
    • (1991) J. Plant Physiol. , vol.13 , pp. 566-572
    • Doehlert, D.C.1    Knutson, C.A.2
  • 84
    • 0008567145 scopus 로고
    • Ueber Stärkekörner, welche sich mit Jod roth färben
    • Drafert, F. W., 1887. Ueber Stärkekörner, welche sich mit Jod roth färben. Ber. d. deutsch bot. Ges. 5: 108-114
    • (1887) Ber. D. Deutsch Bot. Ges. , vol.5 , pp. 108-114
    • Drafert, F.W.1
  • 85
    • 0026834195 scopus 로고
    • Characterization of cDNAs encoding two isoforms of granule-bound starch synthase which show differential expression in developing storage organs of pea and potato
    • Dry, I., Smith, A., Edwards, A., Bhattacharyya, M., Dunn, P., and Martin, C., 1992. Characterization of cDNAs encoding two isoforms of granule-bound starch synthase which show differential expression in developing storage organs of pea and potato. Plant J. 2: 193-202.
    • (1992) Plant J. , vol.2 , pp. 193-202
    • Dry, I.1    Smith, A.2    Edwards, A.3    Bhattacharyya, M.4    Dunn, P.5    Martin, C.6
  • 86
    • 0029411618 scopus 로고
    • Molecular cloning and characterization of a soluble inorganic pyrophosphotase in potato
    • du Jardin, P., Rojas-Beltran., J., Gephardt, C., and Brasseur, R., 1995. Molecular cloning and characterization of a soluble inorganic pyrophosphotase in potato. Plant Phys. 109: 853-860.
    • (1995) Plant Phys. , vol.109 , pp. 853-860
    • Du Jardin, P.1    Rojas-Beltran, J.2    Gephardt, C.3    Brasseur, R.4
  • 88
    • 0031213930 scopus 로고    scopus 로고
    • Antisense inhibition of cytosolic phosphorylase in potato plants (Solanum tuberosum L.) affects tuber sprouting and flower formation with only little impact on carbohydrate metabolism
    • Duwenig, E., Steup, M., Willmitzer, L., and Kossmann, J., 1997. Antisense inhibition of cytosolic phosphorylase in potato plants (Solanum tuberosum L.) affects tuber sprouting and flower formation with only little impact on carbohydrate metabolism. Plant J. 12: 323-333.
    • (1997) Plant J. , vol.12 , pp. 323-333
    • Duwenig, E.1    Steup, M.2    Willmitzer, L.3    Kossmann, J.4
  • 89
    • 0001624920 scopus 로고
    • Evidence for the inclusion of controlling elements within the structural gene at the waxy locus in maize
    • Echt, C. S. and Schwartz, D., 1981. Evidence for the inclusion of controlling elements within the structural gene at the waxy locus in maize. Genetics 99: 275-284.
    • (1981) Genetics , vol.99 , pp. 275-284
    • Echt, C.S.1    Schwartz, D.2
  • 90
    • 38249042855 scopus 로고
    • Metabolism of UDP glucose by developing embryos of round and wrinkled varieties of Pisum sativum
    • Edwards, J. and ap Rees, T. 1986. Metabolism of UDP glucose by developing embryos of round and wrinkled varieties of Pisum sativum. Phytochemistry 25: 2033-2039.
    • (1986) Phytochemistry , vol.25 , pp. 2033-2039
    • Edwards, J.1    Ap Rees, T.2
  • 91
    • 0029347013 scopus 로고
    • Biochemical and molecular characterization of a novel starch synthase from potato tubers
    • Edwards, A., Marshall, J., Denyer, K., Sidebottom, C., Visser, R. G. F., Martin, C., and Smith, A., 1995. Biochemical and molecular characterization of a novel starch synthase from potato tubers. Plant J. 8: 283-294.
    • (1995) Plant J. , vol.8 , pp. 283-294
    • Edwards, A.1    Marshall, J.2    Denyer, K.3    Sidebottom, C.4    Visser, R.G.F.5    Martin, C.6    Smith, A.7
  • 92
    • 0033028207 scopus 로고    scopus 로고
    • A combined reduction in activity of starch synthase II and III of potato has novel effects on the starch of tubers
    • Edwards, A., Fulton, D. C., Hylton, C. M., Jobling, S. A., Gidley, M., Rössner, U., Martin, C., and Smith, A. M., 1999. A combined reduction in activity of starch synthase II and III of potato has novel effects on the starch of tubers. Plant J. 17: 251-261.
    • (1999) Plant J. , vol.17 , pp. 251-261
    • Edwards, A.1    Fulton, D.C.2    Hylton, C.M.3    Jobling, S.A.4    Gidley, M.5    Rössner, U.6    Martin, C.7    Smith, A.M.8
  • 93
    • 0000121327 scopus 로고
    • Proposed mechanism for the synthesis of starch from glycogen
    • Erlander, S., 1958. Proposed mechanism for the synthesis of starch from glycogen. Enzymologia 19: 273-283.
    • (1958) Enzymologia , vol.19 , pp. 273-283
    • Erlander, S.1
  • 94
    • 0024288969 scopus 로고
    • Enzymic capacities of amyloplasts from wheat (Triticum aestivum) endosperm
    • Entwistle, G. and ap Rees, T., 1988. Enzymic capacities of amyloplasts from wheat (Triticum aestivum) endosperm. Biochem. J. 255: 391-396.
    • (1988) Biochem. J. , vol.255 , pp. 391-396
    • Entwistle, G.1    Ap Rees, T.2
  • 96
    • 0001783262 scopus 로고
    • Use of low-temperature scanning electron microscopy to examine starch structure and behavior
    • Chandrasekaran, Ed., Elsevier Applied Science, New York
    • Fannon, J. E., Hauber, R. J., and BeMiller, J. N., 1992b. Use of low-temperature scanning electron microscopy to examine starch structure and behavior. In: Frontiers in Carbohydrate Research, Vol. 2. pp. 1-23. Chandrasekaran, Ed., Elsevier Applied Science, New York.
    • (1992) Frontiers in Carbohydrate Research , vol.2 , pp. 1-23
    • Fannon, J.E.1    Hauber, R.J.2    BeMiller, J.N.3
  • 97
  • 98
    • 0027949889 scopus 로고
    • Expression of a wild-type GBSS gene introduced into an amylose-free potato mutant by Agrobacterium tumefaciens and the inheritance of the inserts at the microscopic level
    • Flipse, E., Huisman, J. G., de Vries, B. J., Bergervoet, J. E. M., Jacobsen, E., and Visser, R. G. F., 1994. Expression of a wild-type GBSS gene introduced into an amylose-free potato mutant by Agrobacterium tumefaciens and the inheritance of the inserts at the microscopic level. Theor. Appl. Genet. 88: 369-375.
    • (1994) Theor. Appl. Genet. , vol.88 , pp. 369-375
    • Flipse, E.1    Huisman, J.G.2    De Vries, B.J.3    Bergervoet, J.E.M.4    Jacobsen, E.5    Visser, R.G.F.6
  • 99
    • 0029808273 scopus 로고    scopus 로고
    • The dosage effect of the wild-type GBSS allele is linear for GBSS activity but not for amylose content: Absence of amylose has a distinct influence on the physico-chemical properties of starch
    • Flipse, E., Keetels, C. J. A. M., Jacobsen, E., and Visser, R. G. F., 1996a. The dosage effect of the wild-type GBSS allele is linear for GBSS activity but not for amylose content: absence of amylose has a distinct influence on the physico-chemical properties of starch. Theor. Appl. Genet. 92: 121-127.
    • (1996) Theor. Appl. Genet. , vol.92 , pp. 121-127
    • Flipse, E.1    Keetels, C.J.A.M.2    Jacobsen, E.3    Visser, R.G.F.4
  • 100
    • 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., Suurs, L., Keetels, C. J. A. M., Kossmann, J., Jacobsen, E., and Visser, R. G. F., 1996b. 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
  • 101
    • 0000227641 scopus 로고
    • The phosphate-triose phosphate-phosphoglycerate translocator of the chloroplast
    • Flügge, U-I. and Heldt, H. W., 1984. The phosphate-triose phosphate-phosphoglycerate translocator of the chloroplast. Trends Biochem. Sci. 9: 530-533.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 530-533
    • Flügge, U.-I.1    Heldt, H.W.2
  • 103
    • 0000888610 scopus 로고
    • Organization of the starch granules
    • Whistler, R. L., BeMiller, J. N., and Paschall, J. F., Eds., Academic Press, Orlando
    • French, D., 1984 Organization of the starch granules. In: Starch: Chemistry and Technology. pp. 183-247, Whistler, R. L., BeMiller, J. N., and Paschall, J. F., Eds., Academic Press, Orlando.
    • (1984) Starch: Chemistry and Technology , pp. 183-247
    • French, D.1
  • 104
    • 0014216014 scopus 로고
    • Studies on the biosynthesis of starch. II. Some properties of the adenosine diphosphate glucose:Starch glucosyltransferase bound to the starch granule
    • Frydman, R. B. and Cardini, C. E., 1967. Studies on the biosynthesis of starch. II. Some properties of the adenosine diphosphate glucose:starch glucosyltransferase bound to the starch granule. J. Biol. Chem. 242: 312-317.
    • (1967) J. Biol. Chem. , vol.242 , pp. 312-317
    • Frydman, R.B.1    Cardini, C.E.2
  • 105
    • 84987204878 scopus 로고
    • Chain length distribution of amylopectins of double-and triple-mutants containing the waxy gene in the inbred Oh43 maize background
    • Fuwa, H., Glover, D. V., Miyaura, K., Inouchi, N., Konishi, Y., and Sugimoto, Y., 1987. Chain length distribution of amylopectins of double-and triple-mutants containing the waxy gene in the inbred Oh43 maize background. Starch/Staerke 39: 295-298
    • (1987) Starch/Staerke , vol.39 , pp. 295-298
    • Fuwa, H.1    Glover, D.V.2    Miyaura, K.3    Inouchi, N.4    Konishi, Y.5    Sugimoto, Y.6
  • 106
    • 0026466802 scopus 로고
    • Physical characteristics of starch granules and susceptibility to enzymatic degradation
    • Gallant, D. J., Bouchet, B., Buléon, A., and Perez, S., 1992. Physical characteristics of starch granules and susceptibility to enzymatic degradation. Eur. J. Clin. Nutr. 46: S3-S16.
    • (1992) Eur. J. Clin. Nutr. , vol.46
    • Gallant, D.J.1    Bouchet, B.2    Buléon, A.3    Perez, S.4
  • 107
    • 0031100018 scopus 로고    scopus 로고
    • Microscopy of starch: Evidence of a new level of granule organization
    • Gallant, D. J., Bouchet, B., and Baldwin, P. M., 1997. Microscopy of starch: evidence of a new level of granule organization. Carbohydr. Polymers 32: 177-191.
    • (1997) Carbohydr. Polymers , vol.32 , pp. 177-191
    • Gallant, D.J.1    Bouchet, B.2    Baldwin, P.M.3
  • 108
    • 0032029093 scopus 로고    scopus 로고
    • Characterization of dullI, a maize gene coding for a novel starch synthase
    • Gao, M., Wanat, J., Stinard, P. S., James, M. G., and Myers, A. M., 1998. Characterization of dullI, a maize gene coding for a novel starch synthase. Plant Cell 10: 399-412.
    • (1998) Plant Cell , vol.10 , pp. 399-412
    • Gao, M.1    Wanat, J.2    Stinard, P.S.3    James, M.G.4    Myers, A.M.5
  • 110
    • 51249167380 scopus 로고
    • Sucrose synthase catalyses a readily reversible reaction in vivo in developing potato tubers and other plant tissues
    • Geigenberger, P. and Stitt, M. 1993. Sucrose synthase catalyses a readily reversible reaction in vivo in developing potato tubers and other plant tissues. Planta 189: 329-339.
    • (1993) Planta , vol.189 , pp. 329-339
    • Geigenberger, P.1    Stitt, M.2
  • 111
    • 0001237873 scopus 로고
    • Subcellular metabolite levels in spinach leaves. Regulation of sucrose synthesis during diurnal alterations in photosynthetic partitioning
    • Gerhardt, R., Stitt, M., and Heldt, H. W., 1987. Subcellular metabolite levels in spinach leaves. Regulation of sucrose synthesis during diurnal alterations in photosynthetic partitioning. Plant Physiol. 83: 399-407.
    • (1987) Plant Physiol. , vol.83 , pp. 399-407
    • Gerhardt, R.1    Stitt, M.2    Heldt, H.W.3
  • 112
    • 0002733325 scopus 로고
    • Starch degradation and distribution of the starch-degrading enzymes in Vicia faba leaves during diurnal oscillation of amylolytic activity and starch content in chloroplasts
    • Ghiena, C., Schulz, M., and Schnabl, H., 1993. Starch degradation and distribution of the starch-degrading enzymes in Vicia faba leaves during diurnal oscillation of amylolytic activity and starch content in chloroplasts. Plant Physiol. 101: 73-79.
    • (1993) Plant Physiol. , vol.101 , pp. 73-79
    • Ghiena, C.1    Schulz, M.2    Schnabl, H.3
  • 113
    • 0014011424 scopus 로고
    • Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts
    • Ghosh, H. P. and Preiss, J., 1966. Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts. J. Biol. Chem. 241: 4491-4504.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4491-4504
    • Ghosh, H.P.1    Preiss, J.2
  • 114
    • 0001522708 scopus 로고    scopus 로고
    • A procedure to measure amylose in cereal starches and flours with Concanavilin A
    • Gibson, T. S., Solah, V. A., and McCleary, B. V., 1997. A procedure to measure amylose in cereal starches and flours with Concanavilin A. J. Cereal Sci. 25: 111-119.
    • (1997) J. Cereal Sci. , vol.25 , pp. 111-119
    • Gibson, T.S.1    Solah, V.A.2    McCleary, B.V.3
  • 115
    • 45949118079 scopus 로고
    • Factors affecting the crystalline type A-C of native starches and model compounds. A rationalzation of observed effects in terms of polymorphic structures
    • Gidley, M. J., 1987. Factors affecting the crystalline type A-C of native starches and model compounds. A rationalzation of observed effects in terms of polymorphic structures. Carbohydr. Res. 161: 301-304.
    • (1987) Carbohydr. Res. , vol.161 , pp. 301-304
    • Gidley, M.J.1
  • 116
    • 45949117920 scopus 로고
    • Crystallization of malto-oligosaccharides as models of the crystalline forms of starch. Minimum chain-length requirements for the formation of double helices
    • Gidley, M. J. and Bulpin, P. V., 1987. Crystallization of malto-oligosaccharides as models of the crystalline forms of starch. Minimum chain-length requirements for the formation of double helices. Carbohydr. Res. 161: 291-300.
    • (1987) Carbohydr. Res. , vol.161 , pp. 291-300
    • Gidley, M.J.1    Bulpin, P.V.2
  • 117
    • 0001599901 scopus 로고
    • Synthesis of salt soluble proteins in barley. Pulse labeling study of grain filling in liquid cultured detached spikes
    • Giese, H. and Hejgaard, J., 1984. Synthesis of salt soluble proteins in barley. Pulse labeling study of grain filling in liquid cultured detached spikes. Planta 161: 172-177.
    • (1984) Planta , vol.161 , pp. 172-177
    • Giese, H.1    Hejgaard, J.2
  • 118
    • 0028342598 scopus 로고
    • ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize
    • Giroux, M. J. and Hannah, L. C., 1994. ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize. Mol. Gen. Genet. 243: 400-408
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 400-408
    • Giroux, M.J.1    Hannah, L.C.2
  • 119
    • 0029168338 scopus 로고
    • Relationship between endosperm texture and the occurence of friabilin and bound polar lipids on wheat starch
    • Greenblatt, G. A., Bettge, A. D., and Morris, C. F., 1995. Relationship between endosperm texture and the occurence of friabilin and bound polar lipids on wheat starch. Cereal Chem. 72: 172-176.
    • (1995) Cereal Chem. , vol.72 , pp. 172-176
    • Greenblatt, G.A.1    Bettge, A.D.2    Morris, C.F.3
  • 120
    • 0000744294 scopus 로고
    • A starch granule protein associated with endosperm softness in wheat
    • Greenwell, P. and Schofield, J. D., 1986. A starch granule protein associated with endosperm softness in wheat. Cereal Chem. 63: 379-380.
    • (1986) Cereal Chem. , vol.63 , pp. 379-380
    • Greenwell, P.1    Schofield, J.D.2
  • 121
    • 0000600497 scopus 로고
    • Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts
    • Gross, P. and ap Rees, T., 1986. Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts. Planta 167:140-145.
    • (1986) Planta , vol.167 , pp. 140-145
    • Gross, P.1    Ap Rees, T.2
  • 122
    • 0000361233 scopus 로고
    • Differentiation of the properties of the branching isoenzymes from maize (Zea mays)
    • Guan, H-P. and Preiss, J., 1993. Differentiation of the properties of the branching isoenzymes from maize (Zea mays). Plant Physiol. 102: 1269-1273.
    • (1993) Plant Physiol. , vol.102 , pp. 1269-1273
    • Guan, H.-P.1    Preiss, J.2
  • 123
    • 0028409018 scopus 로고
    • Expression of branching enzyme 1 of maize endosperm in Escherischia coli
    • Guan, H-P., Baba, T., and Preiss, J., 1994. Expression of branching enzyme 1 of maize endosperm in Escherischia coli. Plant Physiol. 104: 1449-1453.
    • (1994) Plant Physiol. , vol.104 , pp. 1449-1453
    • Guan, H.-P.1    Baba, T.2    Preiss, J.3
  • 124
    • 0002147496 scopus 로고
    • Changes in envelope permeability during chloroplast development
    • Hampp, R. and Schmidt, H. W., 1976. Changes in envelope permeability during chloroplast development. Planta 129: 69-73.
    • (1976) Planta , vol.129 , pp. 69-73
    • Hampp, R.1    Schmidt, H.W.2
  • 125
    • 0001328421 scopus 로고
    • The reversible formation of starch from glucose-1-phosphate catalysed by potato phosphorylase
    • Hanes, C. S., 1940. The reversible formation of starch from glucose-1-phosphate catalysed by potato phosphorylase. Proc. R. Soc: London. Ser. B. 120: 174-208
    • (1940) Proc. R. Soc: London. Ser. B. , vol.120 , pp. 174-208
    • Hanes, C.S.1
  • 126
    • 84989102482 scopus 로고
    • Sedimentation field flow fractionation combined with multi-angle laser light scattering applied for characterization of starch polymers
    • Hanselmann, R., Ehrat, M., and Widmer, H. M., 1995. Sedimentation field flow fractionation combined with multi-angle laser light scattering applied for characterization of starch polymers. Starch 47: 345-349.
    • (1995) Starch , vol.47 , pp. 345-349
    • Hanselmann, R.1    Ehrat, M.2    Widmer, H.M.3
  • 127
    • 0008600301 scopus 로고
    • Über Versuche die gewachsene Struktur des Stärkekorns mikroskopisch sichtbar zu machen, besonders an lintnerisierter Stärke
    • Hanson, E. A. and Katz, J. R., 1934. Über Versuche die gewachsene Struktur des Stärkekorns mikroskopisch sichtbar zu machen, besonders an lintnerisierter Stärke. Z. Phys. Chem. A168: 339-352
    • (1934) Z. Phys. Chem. , vol.A168 , pp. 339-352
    • Hanson, E.A.1    Katz, J.R.2
  • 129
    • 0000992348 scopus 로고
    • Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during dessication phase of seed development
    • Hara-Nishimura, I., Nishimura, M., and Daussant, J., 1986. Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during dessication phase of seed development. Protoplasma 134: 149-153.
    • (1986) Protoplasma , vol.134 , pp. 149-153
    • Hara-Nishimura, I.1    Nishimura, M.2    Daussant, J.3
  • 130
    • 0032128032 scopus 로고    scopus 로고
    • Isolation and characterization of the zSSIIa and zSSIIb starch synthase cDNA clones from maize endosperm
    • Harn, C., Knight, M., Ramakrishnan, A., Guan, H., Keeling, P. L., and Wasserman, B. P., 1998. Isolation and characterization of the zSSIIa and zSSIIb starch synthase cDNA clones from maize endosperm. Plant Mol. Biol. 37: 639-649.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 639-649
    • Harn, C.1    Knight, M.2    Ramakrishnan, A.3    Guan, H.4    Keeling, P.L.5    Wasserman, B.P.6
  • 131
    • 0031977375 scopus 로고    scopus 로고
    • Evidence that the rug3 locus of pea (Pisum sativum L.) encodes plastidial phosphoglucomutase confirms that the imported substrate for starch synthesis in pea amyloplasts is glucose-6-phosphate
    • Harrison, C. J., Hedley, C. L., and Wang, T. L., 1998. Evidence that the rug3 locus of pea (Pisum sativum L.) encodes plastidial phosphoglucomutase confirms that the imported substrate for starch synthesis in pea amyloplasts is glucose-6-phosphate. Plant J. 13: 753-762.
    • (1998) Plant J. , vol.13 , pp. 753-762
    • Harrison, C.J.1    Hedley, C.L.2    Wang, T.L.3
  • 132
    • 34249957634 scopus 로고
    • A study of the rate of recycling of triose phosphates in heterotrophic Chenopodium rubrum cells, potato tubers, and maize endosperm
    • Hatzfeld, W-D. and Stitt, M., 1990. A study of the rate of recycling of triose phosphates in heterotrophic Chenopodium rubrum cells, potato tubers, and maize endosperm. Planta 180: 198-204.
    • (1990) Planta , vol.180 , pp. 198-204
    • Hatzfeld, W.-D.1    Stitt, M.2
  • 133
    • 0008530064 scopus 로고
    • Starch synthetases from Vitis vinifera and Zea mays
    • Hawker, J. S. and Downton, W. J .S., 1974. Starch synthetases from Vitis vinifera and Zea mays. Phytochemistry 13: 893-900.
    • (1974) Phytochemistry , vol.13 , pp. 893-900
    • Hawker, J.S.1    Downton, W.J.S.2
  • 134
    • 0001148138 scopus 로고
    • Unprimed starch synthesis by soluble ADPglucose-starch glucosyltransferase from potato tubers
    • Hawker, J. S., Ozbun, J. L., and Preiss, J., 1972. Unprimed starch synthesis by soluble ADPglucose-starch glucosyltransferase from potato tubers. Phytochemistry 11, 1287-1293.
    • (1972) Phytochemistry , vol.11 , pp. 1287-1293
    • Hawker, J.S.1    Ozbun, J.L.2    Preiss, J.3
  • 135
    • 0015983293 scopus 로고
    • Interaction of spinach leaf adenosine diphosphate glucose α-1,4-glucan α-4-glycosyl transferase and α-1,4-glucan, α-1,4-glucan-6-glucosyl transferase in synthesis of branched a-glucan
    • Hawker, J. S., Ozbun, J. L., Ozaki, H., Greenberg, E., and Preiss, J., 1974. Interaction of spinach leaf adenosine diphosphate glucose α-1,4-glucan α-4-glycosyl transferase and α-1,4-glucan, α-1,4-glucan-6-glucosyl transferase in synthesis of branched a-glucan. Arch. Biochem. Biophys. 160: 530-551.
    • (1974) Arch. Biochem. Biophys. , vol.160 , pp. 530-551
    • Hawker, J.S.1    Ozbun, J.L.2    Ozaki, H.3    Greenberg, E.4    Preiss, J.5
  • 136
    • 0002467467 scopus 로고
    • Starch synthesis in developing potato tubers
    • Hawker, J. S., Marschner, H., and Krauss, A. (1979) Starch synthesis in developing potato tubers. Physiol. Plant. 46: 25-30.
    • (1979) Physiol. Plant. , vol.46 , pp. 25-30
    • Hawker, J.S.1    Marschner, H.2    Krauss, A.3
  • 137
    • 0028039637 scopus 로고
    • Accumulation of hexoses in leaf vacuoles: Studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or apoplasm
    • Heineke D., Wildenberg K., Sonnewald U., Willmitzer L., and Heldt, H.W., 1994. Accumulation of hexoses in leaf vacuoles: studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or apoplasm. Planta 194: 29-33.
    • (1994) Planta , vol.194 , pp. 29-33
    • Heineke, D.1    Wildenberg, K.2    Sonnewald, U.3    Willmitzer, L.4    Heldt, H.W.5
  • 138
    • 84964191321 scopus 로고
    • Electron microscope observation on helical structure in starch
    • Heyn, A. N. J., 1959. Electron microscope observation on helical structure in starch. Textile Res. J. 29: 366-368.
    • (1959) Textile Res. J. , vol.29 , pp. 366-368
    • Heyn, A.N.J.1
  • 139
    • 84987047461 scopus 로고
    • Role of β-amylase in starch metabolismduring soybean development and germination
    • Hildebrand, D. F. and Hymowitz, T. 1981. Role of β-amylase in starch metabolismduring soybean development and germination. Physiol. Plant. 53: 429-434.
    • (1981) Physiol. Plant. , vol.53 , pp. 429-434
    • Hildebrand, D.F.1    Hymowitz, T.2
  • 140
    • 0002113153 scopus 로고
    • Evidence that glucose 6-phosphate is imported as the substrate for starch synthesis by the plastids of developing pea embryos
    • Hill, L. M. and Smith, A. M., 1991. Evidence that glucose 6-phosphate is imported as the substrate for starch synthesis by the plastids of developing pea embryos. Planta 185: 91-96.
    • (1991) Planta , vol.185 , pp. 91-96
    • Hill, L.M.1    Smith, A.M.2
  • 141
    • 0030483926 scopus 로고    scopus 로고
    • The onset of sucrose accumulation in cold-stored potato tubers is caused by an increased rate of sucrose synthesis and coincides with low levels of hexose-phosphates, an activation of sucrose phosphate synthase and the appearance of a new form of amylase
    • Hill, L. M., Reimholz, R., Schroeder, R., Nielsen, T. H., and Stitt, M., 1996. The onset of sucrose accumulation in cold-stored potato tubers is caused by an increased rate of sucrose synthesis and coincides with low levels of hexose-phosphates, an activation of sucrose phosphate synthase and the appearance of a new form of amylase. Plant Cell Environ. 19: 1223-1237.
    • (1996) Plant Cell Environ. , vol.19 , pp. 1223-1237
    • Hill, L.M.1    Reimholz, R.2    Schroeder, R.3    Nielsen, T.H.4    Stitt, M.5
  • 142
    • 0040687034 scopus 로고
    • Polymodal distribution of the chain lengths of amylopectins, and its significance
    • Hizukuri, S., 1986. Polymodal distribution of the chain lengths of amylopectins, and its significance. Carbohydr. Res. 147: 342-347.
    • (1986) Carbohydr. Res. , vol.147 , pp. 342-347
    • Hizukuri, S.1
  • 143
    • 0002585528 scopus 로고
    • Estimation of the distribution of molecular weight for amylose by the low-angle laser-light-scattering technique combined with high-performance gel chromatography
    • Hizukuri, S. and Takagi, T., 1984. Estimation of the distribution of molecular weight for amylose by the low-angle laser-light-scattering technique combined with high-performance gel chromatography. Carbohydr. Res. 134: 1-10.
    • (1984) Carbohydr. Res. , vol.134 , pp. 1-10
    • Hizukuri, S.1    Takagi, T.2
  • 144
    • 84983947611 scopus 로고
    • Studies on starch phosphate. Part 1. Estimation of glucose-6-phospate residues in starch and the presence of other bound phosphate(s)
    • Hizukuri, S., Tabata, S., and Nikuni, Z., 1970. Studies on starch phosphate. Part 1. Estimation of glucose-6-phospate residues in starch and the presence of other bound phosphate(s). Starch/Staerke 10: 338-343.
    • (1970) Starch/Staerke , vol.10 , pp. 338-343
    • Hizukuri, S.1    Tabata, S.2    Nikuni, Z.3
  • 146
    • 0000471908 scopus 로고
    • Genetic studies on the wx gene of sorghum (Sorghum bicolor (L.) Moench). I. Examination of the protein product of the waxy locus
    • Hseih, J-S., 1988. Genetic studies on the wx gene of sorghum (Sorghum bicolor (L.) Moench). I. Examination of the protein product of the waxy locus. Bot. Bull. Acad. Sinica 29: 293-299.
    • (1988) Bot. Bull. Acad. Sinica , vol.29 , pp. 293-299
    • Hseih, J.-S.1
  • 147
    • 0025429268 scopus 로고
    • Classification and characterization of the rice α-amylase multigene family
    • Huang, N., Sutliff, T. D., Litts, J. C., and Rodriguez, R. A., 1990. Classification and characterization of the rice α-amylase multigene family. Plant Mol. Biol. 14: 655-668.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 655-668
    • Huang, N.1    Sutliff, T.D.2    Litts, J.C.3    Rodriguez, R.A.4
  • 148
    • 0026778658 scopus 로고
    • Classification and evolution of α-amylase genes in plants
    • Huang, N., Stebbins, G. L. and Rodriguez, R. L., 1992. Classification and evolution of α-amylase genes in plants. Proc. Natl. Acad. Sci. USA 89: 7526-7530.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7526-7530
    • Huang, N.1    Stebbins, G.L.2    Rodriguez, R.L.3
  • 149
    • 0030695053 scopus 로고    scopus 로고
    • Visualization of channels and cavities of com and sorghum starch granules
    • Huber, K. C. and BeMiller, J. N., 1997. Visualization of channels and cavities of com and sorghum starch granules. Cereal Chem. 74: 537-541.
    • (1997) Cereal Chem. , vol.74 , pp. 537-541
    • Huber, K.C.1    BeMiller, J.N.2
  • 150
    • 0001172247 scopus 로고
    • The rb mutation of pea causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos
    • Hylton, C. and Smith, A. M., 1992. The rb mutation of pea causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos. Plant Physiol. 99: 1626-1634.
    • (1992) Plant Physiol. , vol.99 , pp. 1626-1634
    • Hylton, C.1    Smith, A.M.2
  • 151
    • 84989102139 scopus 로고
    • Recent advances in knowledge on starch structure
    • Imberty, A., Buleon, A., Vinh, T., and Ferez, S., 1991. Recent advances in knowledge on starch structure. Starch/Staerke 43: 375-384.
    • (1991) Starch/Staerke , vol.43 , pp. 375-384
    • Imberty, A.1    Buleon, A.2    Vinh, T.3    Ferez, S.4
  • 152
    • 84987246013 scopus 로고
    • Chain lenmgth distribution of amylopectins of several single mutants and the normal counterpart, and Sugary-1 phytoglycogen in maize (Zea mays L.)
    • Inouchi, N., Glover, D. V., and Fuwa, H., 1987. Chain lenmgth distribution of amylopectins of several single mutants and the normal counterpart, and Sugary-1 phytoglycogen in maize (Zea mays L.). Starch/Staerke 39: 259-266.
    • (1987) Starch/Staerke , vol.39 , pp. 259-266
    • Inouchi, N.1    Glover, D.V.2    Fuwa, H.3
  • 153
    • 0001384883 scopus 로고
    • Debranching enzyme of potato tubers (Solanum tuberosum L.). I. Purification and some properties of potato isoamylase
    • Ishizaki, Y., Taniguchi, H., Maruyama, Y., and Nakamura, M. 1983. Debranching enzyme of potato tubers (Solanum tuberosum L.). I. Purification and some properties of potato isoamylase. Agric. Biol. Chem. 47: 771-779.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 771-779
    • Ishizaki, Y.1    Taniguchi, H.2    Maruyama, Y.3    Nakamura, M.4
  • 154
    • 0021847270 scopus 로고
    • Control of transcription of α-amylase and rRNA genes in barley aleurone protoplasts by gibberellin and abscisic acid
    • Jacobsen, J. V. and Beach, L. R., 1985. Control of transcription of α-amylase and rRNA genes in barley aleurone protoplasts by gibberellin and abscisic acid. Nature 316: 275-277.
    • (1985) Nature , vol.316 , pp. 275-277
    • Jacobsen, J.V.1    Beach, L.R.2
  • 155
    • 0001612521 scopus 로고
    • Water stress enhances expression of an α-amylase gene in barley leaves
    • Jacobsen, J. V., Hanson, A. D., and Chandler, P. C., 1986. Water stress enhances expression of an α-amylase gene in barley leaves. Plant Physiol. 80: 350-359.
    • (1986) Plant Physiol. , vol.80 , pp. 350-359
    • Jacobsen, J.V.1    Hanson, A.D.2    Chandler, P.C.3
  • 156
    • 0031757072 scopus 로고    scopus 로고
    • The degree of starch phosphorylation as influenced by phosphate deprivation of potato (Solanum tuberosum L.) plants
    • Jacobsen, H.B., Madsen, M. H., Christiansen, J., and Nielsen, T. H., 1998. The degree of starch phosphorylation as influenced by phosphate deprivation of potato (Solanum tuberosum L.) plants. Potato Res. 41: 109-116.
    • (1998) Potato Res. , vol.41 , pp. 109-116
    • Jacobsen, H.B.1    Madsen, M.H.2    Christiansen, J.3    Nielsen, T.H.4
  • 157
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugary1, a determinant of starch granule composition in maize kernels
    • James, M. G., Robertson, D. S. and Myers, A. M., 1995. Characterization of the maize gene sugary1, a determinant of starch granule composition in maize kernels. Plant Cell 7: 417-429
    • (1995) Plant Cell , vol.7 , pp. 417-429
    • James, M.G.1    Robertson, D.S.2    Myers, A.M.3
  • 159
    • 0001196444 scopus 로고
    • Regulation of the synthesis of barley aleurone α-amylase by gibberellic acid and calcium ions
    • Jones, R. L. and Carbonell, J., 1984. Regulation of the synthesis of barley aleurone α-amylase by gibberellic acid and calcium ions. Plant Physiol. 76: 213-218.
    • (1984) Plant Physiol. , vol.76 , pp. 213-218
    • Jones, R.L.1    Carbonell, J.2
  • 160
    • 0001178122 scopus 로고
    • Enzymic capacities of purified cauliflower bud plastids for lipid synthesis and carbohydrate metabolism
    • Journet, E-P. and Douce, R., 1985. Enzymic capacities of purified cauliflower bud plastids for lipid synthesis and carbohydrate metabolism. Plant Physiol. 79: 458-467.
    • (1985) Plant Physiol. , vol.79 , pp. 458-467
    • Journet, E.-P.1    Douce, R.2
  • 161
    • 0014532476 scopus 로고
    • Enzymic degradation of starch granules in the cotyledons of germinating peas
    • Juliano, B. O. and Varner, J. E., 1969. Enzymic degradation of starch granules in the cotyledons of germinating peas. Plant Physiol. 44: 886-892.
    • (1969) Plant Physiol. , vol.44 , pp. 886-892
    • Juliano, B.O.1    Varner, J.E.2
  • 162
    • 0001372333 scopus 로고
    • Characterization of pea chloroplast D-enzyme (4-α-D-glucanotransferase)
    • Kakefuda, G. and Duke, S. H. 1989. Characterization of pea chloroplast D-enzyme (4-α-D-glucanotransferase). Plant Physiol. 91: 136-143.
    • (1989) Plant Physiol. , vol.91 , pp. 136-143
    • Kakefuda, G.1    Duke, S.H.2
  • 163
    • 0000424878 scopus 로고
    • Chloroplast and extrachloroplastidic starch-degrading enzymes in Pisum sativum L
    • Kakefuda, G., Duke, S. H., and Hostak, M. S. 1986. Chloroplast and extrachloroplastidic starch-degrading enzymes in Pisum sativum L. Planta 168: 175-182.
    • (1986) Planta , vol.168 , pp. 175-182
    • Kakefuda, G.1    Duke, S.H.2    Hostak, M.S.3
  • 164
    • 0030432418 scopus 로고    scopus 로고
    • Hepatic production of 1,5-anhydrofructose and 1,5-anhydroglucitol by the third glycogenolytic pathway
    • Kametani, S., Shiga, Y., and Akanuma, H., 1996. Hepatic production of 1,5-anhydrofructose and 1,5-anhydroglucitol by the third glycogenolytic pathway. Eur. J. Biochem. 242: 832-838.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 832-838
    • Kametani, S.1    Shiga, Y.2    Akanuma, H.3
  • 165
    • 0000383172 scopus 로고    scopus 로고
    • Molecular characterisazion of a carbon transporter in plastids from heterotrophic tissues: The glucose 6-phosphate/phosphate antiporter
    • Kammerer, B., Fischer, K., Hilpert, B., Schubert, S., Gutensohn, M., Weber, A., and Flügge, U-I., 1998. Molecular characterisazion of a carbon transporter in plastids from heterotrophic tissues: the glucose 6-phosphate/phosphate antiporter. Plant Cell 7: 417-429.
    • (1998) Plant Cell , vol.7 , pp. 417-429
    • Kammerer, B.1    Fischer, K.2    Hilpert, B.3    Schubert, S.4    Gutensohn, M.5    Weber, A.6    Flügge, U.-I.7
  • 166
    • 0028822675 scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate transporter in higher plants
    • Kampfenkel, K., Möhlmann, T., Batz, O., van Montagu, M., Inzé, D., and Neuhaus, H. E., 1995. Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate transporter in higher plants. FEBS Lett. 374: 351-355.
    • (1995) FEBS Lett. , vol.374 , pp. 351-355
    • Kampfenkel, K.1    Möhlmann, T.2    Batz, O.3    Van Montagu, M.4    Inzé, D.5    Neuhaus, H.E.6
  • 167
    • 0026893753 scopus 로고
    • Metabolic regulation of rice α-amylase and sucrose synthase genes in plants
    • Karrer, E. E. and Rodriguez, R. L. 1992. Metabolic regulation of rice α-amylase and sucrose synthase genes in plants. Plant J. 2: 517-523.
    • (1992) Plant J. , vol.2 , pp. 517-523
    • Karrer, E.E.1    Rodriguez, R.L.2
  • 168
    • 0029767550 scopus 로고    scopus 로고
    • Quantitative method for the survey of starch phosphate derivatives and starch phospholipids by 31P nuclear resonance spectroscopy
    • Kasemsuwan, T. and Jane, J-L., 1996. Quantitative method for the survey of starch phosphate derivatives and starch phospholipids by 31P nuclear resonance spectroscopy. Cereal Chem., 73: 702-707.
    • (1996) Cereal Chem. , vol.73 , pp. 702-707
    • Kasemsuwan, T.1    Jane, J.-L.2
  • 169
    • 0001474375 scopus 로고    scopus 로고
    • Plant biotechnology: Technical barriers to starch improvement
    • Frazier, P. J., Richmond, P., and Donald, A. M., eds. The Royal Society of Chemistry, Cambridge UK
    • Keeling, P. L., 1997. Plant biotechnology: technical barriers to starch improvement. In: Starch structure and functionality. Frazier, P. J., Richmond, P., and Donald, A. M., eds. pp. 180-187. The Royal Society of Chemistry, Cambridge UK.
    • (1997) Starch Structure and Functionality , pp. 180-187
    • Keeling, P.L.1
  • 170
    • 0000954261 scopus 로고
    • Starch synthesis in developing wheat grain. Evidence against the direct involvement of triose phosphates in the metabolic pathway
    • Keeling, P. L., Wood, J. R., Tyson, R. H., and Bridges, I. G., 1988. Starch synthesis in developing wheat grain. Evidence against the direct involvement of triose phosphates in the metabolic pathway. Plant Physiol. 87: 311-319.
    • (1988) Plant Physiol. , vol.87 , pp. 311-319
    • Keeling, P.L.1    Wood, J.R.2    Tyson, R.H.3    Bridges, I.G.4
  • 171
    • 0001575206 scopus 로고
    • Properties of potato α-glucosidase
    • Killilea, S. D. and Clancy, M. J., 1978. Properties of potato α-glucosidase. Photochemistry 17: 1429-1431.
    • (1978) Photochemistry , vol.17 , pp. 1429-1431
    • Killilea, S.D.1    Clancy, M.J.2
  • 173
    • 0001843971 scopus 로고
    • Changes in α-amylase and β-amylase activities during germination of seeds of alfalfa (Medicago sativa L.)
    • Kohno, N. and Nanmori, T., 1991. Changes in α-amylase and β-amylase activities during germination of seeds of alfalfa (Medicago sativa L.). Plant Cell Physiol. 32: 459-456.
    • (1991) Plant Cell Physiol. , vol.32 , pp. 459-1456
    • Kohno, N.1    Nanmori, T.2
  • 175
    • 0030186846 scopus 로고    scopus 로고
    • Expression of Escherichia coli branching enzyme in tubers of amylose-free transgenic potato leads to an increased branching degree of the amylopectin
    • Kortstee, A. J., Vermeesch, A. M. S., de Vries, B., Jacobsen, E., and Visser, R.G.F., 1996. Expression of Escherichia coli branching enzyme in tubers of amylose-free transgenic potato leads to an increased branching degree of the amylopectin. Plant J. 10: 83-90.
    • (1996) Plant J. , vol.10 , pp. 83-90
    • Kortstee, A.J.1    Vermeesch, A.M.S.2    De Vries, B.3    Jacobsen, E.4    Visser, R.G.F.5
  • 176
    • 0032183334 scopus 로고    scopus 로고
    • The influence of an increased degree of branching on the physico-chemical properties of starch from genetically modified potato
    • Kortstee, A. J., Suurs, L. C. J. M., Vermeesch, A. M. S., Keetels, C. J. A. M., Jacobsen, E., and Visser, R. G. F., 1998. The influence of an increased degree of branching on the physico-chemical properties of starch from genetically modified potato. Carbohydr. Polymers 37: 173-184.
    • (1998) Carbohydr. Polymers , vol.37 , pp. 173-184
    • Kortstee, A.J.1    Suurs, L.C.J.M.2    Vermeesch, A.M.S.3    Keetels, C.J.A.M.4    Jacobsen, E.5    Visser, R.G.F.6
  • 177
    • 0028155211 scopus 로고
    • Evidence for a glucose-1-phosphate translocator in storage tissue amyloplasts of potato (Solanum tuberosum) suspension-cultured cells
    • Kosegarten, H. and Mengel, K., 1994. Evidence for a glucose-1-phosphate translocator in storage tissue amyloplasts of potato (Solanum tuberosum) suspension-cultured cells. Physiol. Plant. 91:111-120.
    • (1994) Physiol. Plant. , vol.91 , pp. 111-120
    • Kosegarten, H.1    Mengel, K.2
  • 179
    • 0033150133 scopus 로고    scopus 로고
    • Cloning and functional analysis of a cDNA encoding a starch synthase from potato (Solanum tuberosum L.) that is predominantly expressed in leaf tissue
    • Kossmann, J., Abel, G. J. W., Springer, F., Lloyd, J.and Willmitzer, L., 1999. Cloning and functional analysis of a cDNA encoding a starch synthase from potato (Solanum tuberosum L.) that is predominantly expressed in leaf tissue. Planta 208: 503-511
    • (1999) Planta , vol.208 , pp. 503-511
    • Kossmann, J.1    Abel, G.J.W.2    Springer, F.3    Lloyd, J.4    Willmitzer, L.5
  • 180
    • 0023657286 scopus 로고
    • Primary structure and differential expression of β-amylase in normal and mutant barleys
    • Kreis, M., Williamson, M., Buxton, B., Pywell, J., Hejgaard, J., and Svendsen, I., 1987. Primary structure and differential expression of β-amylase in normal and mutant barleys. Eur. J. Biochem. 169:517-525.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 517-525
    • Kreis, M.1    Williamson, M.2    Buxton, B.3    Pywell, J.4    Hejgaard, J.5    Svendsen, I.6
  • 181
    • 0016632493 scopus 로고
    • A precursor of glycogen biosynthesis α-1,4-glucan protein
    • Krisman, C. R. and Barengo, R., 1975. A precursor of glycogen biosynthesis α-1,4-glucan protein. Eur. J. Biochem. 52: 117-123.
    • (1975) Eur. J. Biochem. , vol.52 , pp. 117-123
    • Krisman, C.R.1    Barengo, R.2
  • 182
    • 0001725393 scopus 로고
    • Maltose metabolism by pea chloroplasts
    • Kruger, N. J. and ap Rees, T., 1983. Maltose metabolism by pea chloroplasts. Planta 158: 179-184.
    • (1983) Planta , vol.158 , pp. 179-184
    • Kruger, N.J.1    Ap Rees, T.2
  • 183
    • 34249921267 scopus 로고
    • Field evaluation of antisense RNA-mediated inhibition of GBSS gene expression in potato
    • Kuipers, A. G. J., Vreem, J. T. M., Meyer, H., Jacobsen, E., Feenstra, W. J., and Visser, R. G. F., 1992. Field evaluation of antisense RNA-mediated inhibition of GBSS gene expression in potato. Euphytica 59: 83-91.
    • (1992) Euphytica , vol.59 , pp. 83-91
    • Kuipers, A.G.J.1    Vreem, J.T.M.2    Meyer, H.3    Jacobsen, E.4    Feenstra, W.J.5    Visser, R.G.F.6
  • 184
    • 0027953123 scopus 로고
    • Formation and deposition of amylose in the potato tuber starch granule are affected by the reduction of granule-bound starch synthase gene expression
    • Kuipers, A. G. J., Jacobsen, E., and Visser, R. G. F., 1994. Formation and deposition of amylose in the potato tuber starch granule are affected by the reduction of granule-bound starch synthase gene expression. Plant Cell 6: 43-52
    • (1994) Plant Cell , vol.6 , pp. 43-52
    • Kuipers, A.G.J.1    Jacobsen, E.2    Visser, R.G.F.3
  • 185
    • 0030599939 scopus 로고    scopus 로고
    • Three isoforms of starch synthase and two isoforms of starch-branching enzyme are present in potato tuber starch
    • Larsson, C-T., Hofvander, P., Khoshnoodi, J., Ek, B., Rask, L., and Larsson, H., 1996. Three isoforms of starch synthase and two isoforms of starch-branching enzyme are present in potato tuber starch. Plant Sci. 117: 9-16.
    • (1996) Plant Sci. , vol.117 , pp. 9-16
    • Larsson, C.-T.1    Hofvander, P.2    Khoshnoodi, J.3    Ek, B.4    Rask, L.5    Larsson, H.6
  • 186
    • 84913845038 scopus 로고
    • Immunohistochemical localisation of β-amylase in resting barley seeds
    • Lauriere, C., Lauriere, M., and Daussant, J., 1986. Immunohistochemical localisation of β-amylase in resting barley seeds. Physiol. Plant. 67:383-388.
    • (1986) Physiol. Plant. , vol.67 , pp. 383-388
    • Lauriere, C.1    Lauriere, M.2    Daussant, J.3
  • 187
    • 0002509838 scopus 로고
    • Particulate UDP-glucose:Protein transglucosylase from potato tuber
    • Lavintman, N. and Cardini, C. E., 1973. Particulate UDP-glucose:protein transglucosylase from potato tuber. FEBS Lett. 29, 43-46.
    • (1973) FEBS Lett. , vol.29 , pp. 43-46
    • Lavintman, N.1    Cardini, C.E.2
  • 188
    • 0016284696 scopus 로고
    • Role of uridine diphosphate glucose in the biosynthesis of starch. Mechanism of enlargement of a glucoproteic acceptor
    • Lavintman, N., Tandecarz, J., Carceller, M., Mendiara, S., and Cardini, C. E., 1974. Role of uridine diphosphate glucose in the biosynthesis of starch. Mechanism of enlargement of a glucoproteic acceptor. Eur. J. Biochem. 50: 145-155.
    • (1974) Eur. J. Biochem. , vol.50 , pp. 145-155
    • Lavintman, N.1    Tandecarz, J.2    Carceller, M.3    Mendiara, S.4    Cardini, C.E.5
  • 189
    • 77956944021 scopus 로고
    • Glycogen and starch debranching enzyme
    • 3 ed. Boyer, P. D., Ed., Academic Press, New York
    • Lee, E. Y. C, and Whelan, W. J., 1971. Glycogen and starch debranching enzyme. In: The enzymes. 3 ed. Vol. 5, pp. 191-234. Boyer, P. D., Ed., Academic Press, New York.
    • (1971) The Enzymes , vol.5 , pp. 191-234
    • Lee, E.Y.C.1    Whelan, W.J.2
  • 192
    • 0000280109 scopus 로고
    • Starch and oligosaccharide synthesis for uridine diphosphate glucose
    • Leloir, L. F., de Fekete, M. A. R. and Cardini, C. E., 1961. Starch and oligosaccharide synthesis for uridine diphosphate glucose. J. Biol. Chem. 236: 636-641.
    • (1961) J. Biol. Chem. , vol.236 , pp. 636-641
    • Leloir, L.F.1    De Fekete, M.A.R.2    Cardini, C.E.3
  • 193
    • 0013817291 scopus 로고
    • The biosynthesis of D-glucose 1,6-diphosphate from D-glucose monophosphates in rat liver
    • Levey, G. S. and Alpert, J. B., 1965. The biosynthesis of D-glucose 1,6-diphosphate from D-glucose monophosphates in rat liver. J. Biol. Chem. 240: 4152-4157
    • (1965) J. Biol. Chem. , vol.240 , pp. 4152-4157
    • Levey, G.S.1    Alpert, J.B.2
  • 194
    • 0008531390 scopus 로고
    • Amylopectin degradation in pea chloroplast extracts
    • Levi, C. and Preiss, J., 1978. Amylopectin degradation in pea chloroplast extracts. Plant Physiol. 61: 218-220.
    • (1978) Plant Physiol. , vol.61 , pp. 218-220
    • Levi, C.1    Preiss, J.2
  • 195
    • 0001489664 scopus 로고
    • Characterization and subcellular localization of debranching enzyme and endoamylase from leaves of sugar beet
    • Li, B., Servaites, J. C., and Geiger, D. R. 1992. Characterization and subcellular localization of debranching enzyme and endoamylase from leaves of sugar beet. Plant Physiol. 98: 1277-1284.
    • (1992) Plant Physiol. , vol.98 , pp. 1277-1284
    • Li, B.1    Servaites, J.C.2    Geiger, D.R.3
  • 196
    • 0000636592 scopus 로고
    • Location of phosphate esters in a wheat starch phosphate by 31 P-nuclear magnetic resonance spectroscopy
    • Lim, S-T. and Seib, P., 1993. Location of phosphate esters in a wheat starch phosphate by 31 P-nuclear magnetic resonance spectroscopy. Cereal Chem. 70: 145-149.
    • (1993) Cereal Chem. , vol.70 , pp. 145-149
    • Lim, S.-T.1    Seib, P.2
  • 197
    • 0008530198 scopus 로고
    • Isolation and characterization of a starchless mutant of Arabidopsis thaliana (L.) Heynh. Lacking ADP glucose pyrophosphorylase activity
    • Lin, T-P., Caspar, T., Somerville, C., and Preiss, J., 1988a. Isolation and characterization of a starchless mutant of Arabidopsis thaliana (L.) Heynh. lacking ADP glucose pyrophosphorylase activity. Plant Phys. 81: 642-645.
    • (1988) Plant Phys. , vol.81 , pp. 642-645
    • Lin, T.-P.1    Caspar, T.2    Somerville, C.3    Preiss, J.4
  • 198
    • 0000984370 scopus 로고
    • A starch-deficient mutant of Arabidopsis thaliana with low ADP glucose pyrophosphorylase activity lacks one of the two subunits of the enzyme
    • Lin, T-P., Caspar, T., Somerville, C., and Preiss, J., 1988b. A starch-deficient mutant of Arabidopsis thaliana with low ADP glucose pyrophosphorylase activity lacks one of the two subunits of the enzyme. Plant. Phys. 88: 1175-1181.
    • (1988) Plant. Phys. , vol.88 , pp. 1175-1181
    • Lin, T.-P.1    Caspar, T.2    Somerville, C.3    Preiss, J.4
  • 199
    • 0001310335 scopus 로고
    • Characterization of D-enzyme (4-α-glucanotransferase) in Arabidopsis leaf
    • Lin, T-P. and Preiss, J., 1988. Characterization of D-enzyme (4-α-glucanotransferase) in Arabidopsis leaf. Plant Physiol., 86: 260-265.
    • (1988) Plant Physiol. , vol.86 , pp. 260-265
    • Lin, T.-P.1    Preiss, J.2
  • 200
    • 0001022490 scopus 로고
    • A nonaqueous procedure for isolating starch granules with associated metabolites from maize (Zea mays L.) endosperm
    • Liu, T-T. Y. and Shannon, J. C., 1981a. A nonaqueous procedure for isolating starch granules with associated metabolites from maize (Zea mays L.) endosperm. Plant Physiol. 67: 518-524.
    • (1981) Plant Physiol. , vol.67 , pp. 518-524
    • Liu, T.-T.Y.1    Shannon, J.C.2
  • 201
    • 0001022489 scopus 로고
    • Measurement of metabolites associated with nonaqueously isolated starch granules from immature Zea mays L. Endosperm
    • Liu, T-T. Y. and Shannon, J. C., 1981b. Measurement of metabolites associated with nonaqueously isolated starch granules from immature Zea mays L. endosperm. Plant Physiol. 67: 525-529.
    • (1981) Plant Physiol. , vol.67 , pp. 525-529
    • Liu, T.-T.Y.1    Shannon, J.C.2
  • 202
    • 0030062571 scopus 로고    scopus 로고
    • An analysis of seed development in Pisum sativum. XIX. Effect of mutant alleles at the R and Rb loci on starch grain size and on the content and composition of starch in developing pea seeds
    • Lloyd, J. R., Wang, T. L., and Hedley, C. L., 1996a. An analysis of seed development in Pisum sativum. XIX. Effect of mutant alleles at the R and Rb loci on starch grain size and on the content and composition of starch in developing pea seeds. J. Exp. Bot. 47: 171-180.
    • (1996) J. Exp. Bot. , vol.47 , pp. 171-180
    • Lloyd, J.R.1    Wang, T.L.2    Hedley, C.L.3
  • 203
    • 0029723286 scopus 로고    scopus 로고
    • Determination of the effect of r and rb mutations on the structure of amylose and amylopectin in pea (Pisum sativum L.)
    • Lloyd, J. R., Hedley, C. L., Bull, V. J., and Ring, S. G., 1996b. Determination of the effect of r and rb mutations on the structure of amylose and amylopectin in pea (Pisum sativum L.). Carbohydr. Polym. 29: 45-49.
    • (1996) Carbohydr. Polym. , vol.29 , pp. 45-49
    • Lloyd, J.R.1    Hedley, C.L.2    Bull, V.J.3    Ring, S.G.4
  • 204
    • 0041154130 scopus 로고    scopus 로고
    • Simultaneous antisense inhibition of two starch synthase isoforms in potato tubers leads to accumulation of grossly modified amylopectin
    • Lloyd, J.R., Landschütze, V., and Kossmann, J., 1999a. Simultaneous antisense inhibition of two starch synthase isoforms in potato tubers leads to accumulation of grossly modified amylopectin. Biochem. J. 338: 515-521.
    • (1999) Biochem. J. , vol.338 , pp. 515-521
    • Lloyd, J.R.1    Landschütze, V.2    Kossmann, J.3
  • 205
    • 0032867095 scopus 로고    scopus 로고
    • The influence of alterations in ADP glucose pyrophosphorylase activities on starch structure and composition in potato tubers
    • Lloyd, J. R., Springer, F., Buléon, A., Müller-Röber, B., Willmitzer, L., and Kossmann, J., 1999b. The influence of alterations in ADP glucose pyrophosphorylase activities on starch structure and composition in potato tubers. Planta 209: 230-238
    • (1999) Planta , vol.209 , pp. 230-238
    • Lloyd, J.R.1    Springer, F.2    Buléon, A.3    Müller-Röber, B.4    Willmitzer, L.5    Kossmann, J.6
  • 206
    • 0027113467 scopus 로고
    • The substrate specificity of isoamylase and the preparation of apo-glycogenin
    • Lomako, J., Lomako, W. M., and Whelan, W. J., 1992. The substrate specificity of isoamylase and the preparation of apo-glycogenin. Carbohydr. Res. 227: 331-338.
    • (1992) Carbohydr. Res. , vol.227 , pp. 331-338
    • Lomako, J.1    Lomako, W.M.2    Whelan, W.J.3
  • 207
    • 0027431287 scopus 로고
    • Glycogen synthesis in the astrocyte: From Glycogenin to proglycogen to glycogen
    • Lomako, J., Lomako, W. M., Whelan, W. J., Dombro, R. S., Neary, J. T., and Norenberg M. D., 1993. Glycogen synthesis in the astrocyte: from Glycogenin to proglycogen to glycogen. FASEB J. 7: 1386-1393.
    • (1993) FASEB J. , vol.7 , pp. 1386-1393
    • Lomako, J.1    Lomako, W.M.2    Whelan, W.J.3    Dombro, R.S.4    Neary, J.T.5    Norenberg, M.D.6
  • 209
    • 0031921128 scopus 로고    scopus 로고
    • Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening
    • Lorberth, R., Ritte, G., Willmitzer, L., and Kossmann, J., 1998. Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening. Nat. Biotechnol. 16: 473-477.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 473-477
    • Lorberth, R.1    Ritte, G.2    Willmitzer, L.3    Kossmann, J.4
  • 210
    • 0001741402 scopus 로고
    • Purification and properties of spinach leaf debranching enzyme
    • Ludwig, I., Ziegler, P., and Beck, E., 1984. Purification and properties of spinach leaf debranching enzyme. Plant Physiol. 74: 856-861.
    • (1984) Plant Physiol. , vol.74 , pp. 856-861
    • Ludwig, I.1    Ziegler, P.2    Beck, E.3
  • 211
    • 49049122639 scopus 로고
    • Enzymic properties of amyloplasts from suspension cultures of soybean
    • Macdonald, F. D. and ap Rees, T., 1983. Enzymic properties of amyloplasts from suspension cultures of soybean. Biochim. Biophys. Acta 755: 81-89.
    • (1983) Biochim. Biophys. Acta , vol.755 , pp. 81-89
    • Macdonald, F.D.1    Ap Rees, T.2
  • 212
    • 0002966811 scopus 로고
    • Cereal α-amylases: Synthesis and action pattern
    • Daussant, J., Mose, J., and Vaughan, J., Eds., Academic Press, London
    • Macgregor, A. M. 1983. Cereal α-amylases: synthesis and action pattern. In: Seed Proteins, pp. 1-34. Daussant, J., Mose, J., and Vaughan, J., Eds., Academic Press, London.
    • (1983) Seed Proteins , pp. 1-34
    • Macgregor, A.M.1
  • 214
    • 0000190052 scopus 로고
    • Purification of a debranching enzyme (R-enzyme) from malted barley, and the role of the enzyme in the digestion of starch granules during the germination of barley seeds
    • Maeda, I., Nikuni, Z., Taniguchi, H., and Nakamura, M., 1978. Purification of a debranching enzyme (R-enzyme) from malted barley, and the role of the enzyme in the digestion of starch granules during the germination of barley seeds. Carbohydr. Res. 61: 309-320.
    • (1978) Carbohydr. Res. , vol.61 , pp. 309-320
    • Maeda, I.1    Nikuni, Z.2    Taniguchi, H.3    Nakamura, M.4
  • 215
    • 0008568867 scopus 로고
    • The inheritance of amylaceous sugary endosperm and its derivatives in maize
    • Mangelsdorf, P. C., 1947. The inheritance of amylaceous sugary endosperm and its derivatives in maize. Genetics 32: 448-458.
    • (1947) Genetics , vol.32 , pp. 448-458
    • Mangelsdorf, P.C.1
  • 217
    • 45149143418 scopus 로고
    • Recent developments in our understanding of amylopectin structure
    • Manners, D. J., 1989. Recent developments in our understanding of amylopectin structure. Carbohydr. Polymers 11: 87-112.
    • (1989) Carbohydr. Polymers , vol.11 , pp. 87-112
    • Manners, D.J.1
  • 218
    • 0014064555 scopus 로고
    • Hydrolysis of the interchain linkages in glycogen-type polysaccharides by a plant enzyme
    • Manners, D. J. and Rowe, K. L., 1967. Hydrolysis of the interchain linkages in glycogen-type polysaccharides by a plant enzyme. Arch. Biochem. Biophys. 119: 585-586.
    • (1967) Arch. Biochem. Biophys. , vol.119 , pp. 585-586
    • Manners, D.J.1    Rowe, K.L.2
  • 219
    • 0008566914 scopus 로고
    • Studies on carbohydrate-metabolizing enzymes, part 21, the α-glucosidase and D-enzyme activity of extracts of carrots and tomatoes
    • Manners, D. J. and Rowe, K. L., 1969. Studies on carbohydrate-metabolizing enzymes, part 21, the α-glucosidase and D-enzyme activity of extracts of carrots and tomatoes. Carbohydr. Res. 153: 357-380.
    • (1969) Carbohydr. Res. , vol.153 , pp. 357-380
    • Manners, D.J.1    Rowe, K.L.2
  • 220
    • 0030198862 scopus 로고    scopus 로고
    • Identification of the major starch synthase in the soluble fraction of potato tubers
    • Marshall, J., Sidebottom, C., Debet, M., Martin, C., Smith, A. M., and Edwards, A., 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    Martin, C.4    Smith, A.M.5    Edwards, A.6
  • 221
    • 0000520019 scopus 로고
    • Estimation and fractionation of the essentially unbranched amylose and branched amylopectin components of starches with Concanavilin A
    • Matheson, N. K. and Welsh, L. A., 1988. Estimation and fractionation of the essentially unbranched amylose and branched amylopectin components of starches with Concanavilin A. Carbohydr. Res. 180: 301-314
    • (1988) Carbohydr. Res. , vol.180 , pp. 301-314
    • Matheson, N.K.1    Welsh, L.A.2
  • 222
    • 0020431374 scopus 로고
    • Soluble starch synthases and starch branching enzymes from cotyledons of smooth-and wrinkled-seeded lines of Pisum sativum L
    • Matters, G. L. and Boyer, C. D., 1982. Soluble starch synthases and starch branching enzymes from cotyledons of smooth-and wrinkled-seeded lines of Pisum sativum L. Biochem. Genet. 20: 833-848.
    • (1982) Biochem. Genet. , vol.20 , pp. 833-848
    • Matters, G.L.1    Boyer, C.D.2
  • 224
    • 0008568717 scopus 로고
    • Ueber stärkekörner, welche sich mit jod roth färben
    • Mayer, A., 1886. Ueber Stärkekörner, welche sich mit Jod roth färben. Ber. d. deutsch bot. Ces. 4: 337-362
    • (1886) Ber. D. Deutsch Bot. Ces. , vol.4 , pp. 337-362
    • Mayer, A.1
  • 226
    • 0001373137 scopus 로고
    • Preferential secretion of R-type α-amylase molecules in rice seed scutellum at high temperatures
    • 880ß-884
    • Mitsui, T. and Akazawa, T., 1986. Preferential secretion of R-type α-amylase molecules in rice seed scutellum at high temperatures. Plant Physiol., 82: 880ß-884.
    • (1986) Plant Physiol. , vol.82
    • Mitsui, T.1    Akazawa, T.2
  • 227
    • 0021871295 scopus 로고
    • Biosynthesis office seed α-amylase: Two pathways of amylase secretion by the scutellum
    • Mitsui, T., Akazawa, T., Christeller, J. T., and Tartakoff, A. M. 1985. Biosynthesis office seed α-amylase: two pathways of amylase secretion by the scutellum. Arch. Biochem. Biophys. 241: 315-328.
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 315-328
    • Mitsui, T.1    Akazawa, T.2    Christeller, J.T.3    Tartakoff, A.M.4
  • 228
    • 0027247801 scopus 로고
    • Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds
    • Mizuno, K., Kawasaki, T., Shimada, H., Satoh, H., Kobayashi, E., Okumura, S., Arai, Y., and Baba, T. 1993. Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds. J. Biol. Chem. 268: 19084-19091.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19084-19091
    • Mizuno, K.1    Kawasaki, T.2    Shimada, H.3    Satoh, H.4    Kobayashi, E.5    Okumura, S.6    Arai, Y.7    Baba, T.8
  • 229
    • 0008531607 scopus 로고
    • Effect of temperature on starch synthesis in potato tuber and in amyloplasts
    • Mohabir, G. and John, P., 1988. Effect of temperature on starch synthesis in potato tuber and in amyloplasts. Plant Physiol. 88: 1222-1228.
    • (1988) Plant Physiol. , vol.88 , pp. 1222-1228
    • Mohabir, G.1    John, P.2
  • 230
    • 0030970353 scopus 로고    scopus 로고
    • ADP-glucose drives starch synthesis in isolated maize endosperm amyloplasts: Characterization of starch synthesis and transport properties across the amyloplast envelope
    • Möhlmann, T., Tjaden, J., Henrichs, G., Quick, W. P., Häusler, R., and Neuhaus, H. E., 1997. ADP-glucose drives starch synthesis in isolated maize endosperm amyloplasts: characterization of starch synthesis and transport properties across the amyloplast envelope. Biochem. J. 324: 503-509.
    • (1997) Biochem. J. , vol.324 , pp. 503-509
    • Möhlmann, T.1    Tjaden, J.2    Henrichs, G.3    Quick, W.P.4    Häusler, R.5    Neuhaus, H.E.6
  • 231
    • 46149136757 scopus 로고
    • Sugar metabolism in developing tubers of Solanum tuberosum
    • Morell, S. and ap Rees, T., 1986. Sugar metabolism in developing tubers of Solanum tuberosum. Phytochemistry 25: 1579-1585
    • (1986) Phytochemistry , vol.25 , pp. 1579-1585
    • Morell, S.1    Ap Rees, T.2
  • 232
    • 0001116629 scopus 로고
    • Isolation and characterization of multiple forms of friabilin
    • Morris, C. F., Greebblatt, G. A., Bettge, A. D., and Malkawi, H. I., 1994. Isolation and characterization of multiple forms of friabilin. J. Cereal Sci. 20: 167-174.
    • (1994) J. Cereal Sci. , vol.20 , pp. 167-174
    • Morris, C.F.1    Greebblatt, G.A.2    Bettge, A.D.3    Malkawi, H.I.4
  • 233
    • 21844488215 scopus 로고
    • Starch lipids and how they relate to starch granule structure and functionality
    • Morrison, W. R., 1995. Starch lipids and how they relate to starch granule structure and functionality. Cer. Foods World 40: 437-446
    • (1995) Cer. Foods World , vol.40 , pp. 437-446
    • Morrison, W.R.1
  • 235
    • 85001670022 scopus 로고
    • Occurrence of friabilin, a low molecular weight protein associated with grain softness, on starch granules isolated from some wheats and related species
    • Morrison, W. R., Greenwell, P., Law, C. N., and Sulaiman, B. D., 1992. Occurrence of friabilin, a low molecular weight protein associated with grain softness, on starch granules isolated from some wheats and related species. J. Cereal Sci. 15: 143-149.
    • (1992) J. Cereal Sci. , vol.15 , pp. 143-149
    • Morrison, W.R.1    Greenwell, P.2    Law, C.N.3    Sulaiman, B.D.4
  • 237
    • 0028083844 scopus 로고
    • Association of a 76-kDa polypeptide with soluble starch synthase I activity in maize (cv B73) endosperm
    • Mu, C., Harn, C., Ko, Y-T., Singletary, G. W., Keeling, P. L., and Wassermann, B. P., 1994. Association of a 76-kDa polypeptide with soluble starch synthase I activity in maize (cv B73) endosperm. Plant J. 6: 151-159.
    • (1994) Plant J. , vol.6 , pp. 151-159
    • Mu, C.1    Harn, C.2    Ko, Y.-T.3    Singletary, G.W.4    Keeling, P.L.5    Wassermann, B.P.6
  • 239
    • 0026533580 scopus 로고
    • Inhibition of the ADP-glucose pyrophosphorylase in transgenic potato tubers leads to sugar storing tubers and influences the tuber formation and expression of tuber storage protein genes
    • Müller-Röber, B., Sonnewald, U., and Willmitzer, L., 1992. Inhibition of the ADP-glucose pyrophosphorylase in transgenic potato tubers leads to sugar storing tubers and influences the tuber formation and expression of tuber storage protein genes. EMBO J. 11: 1229-1238.
    • (1992) EMBO J. , vol.11 , pp. 1229-1238
    • Müller-Röber, B.1    Sonnewald, U.2    Willmitzer, L.3
  • 240
    • 0000289855 scopus 로고
    • Hormonal regulation of α-amylase inhibitor synthesis in germinating barley
    • Mundy, J., 1984. Hormonal regulation of α-amylase inhibitor synthesis in germinating barley. Carlsberg Res. Commun. 49: 439-444.
    • (1984) Carlsberg Res. Commun. , vol.49 , pp. 439-444
    • Mundy, J.1
  • 241
    • 0002294076 scopus 로고
    • Barley α-amylase/subtilisin inhibitor. I. Isolation and characterization
    • Mundy, J., Svendsen, I., and Hejgaard, J., 1983. Barley α-amylase/subtilisin inhibitor. I. Isolation and characterization. Carlsherg Res. Commun. 48: 81-90.
    • (1983) Carlsherg Res. Commun. , vol.48 , pp. 81-90
    • Mundy, J.1    Svendsen, I.2    Hejgaard, J.3
  • 242
    • 0030912925 scopus 로고    scopus 로고
    • Starch synthesis in amyloplasts purified from developing potato tubers
    • Naeem, M., Tetlow, I. J., and Ernes, M. J., 1997. Starch synthesis in amyloplasts purified from developing potato tubers. Plant J. 11: 1095-1103.
    • (1997) Plant J. , vol.11 , pp. 1095-1103
    • Naeem, M.1    Tetlow, I.J.2    Ernes, M.J.3
  • 245
    • 0002056409 scopus 로고    scopus 로고
    • Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis
    • Nakamura, Y., 1996. Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis. Plant Sci. 121: 1-18.
    • (1996) Plant Sci. , vol.121 , pp. 1-18
    • Nakamura, Y.1
  • 246
    • 0030513412 scopus 로고    scopus 로고
    • Changes in the structure of starch and enzyme activities affected by sugary mutations in developing rice endosperm. Possible role of of starch debranching enzyme (R-enzyme) in amylopectin biosynthesis
    • Nakamura, Y., Umemoto, T., Takahata, Y., Komae, K., Amano, E., and Satoh, H., 1996a. Changes in the structure of starch and enzyme activities affected by sugary mutations in developing rice endosperm. Possible role of of starch debranching enzyme (R-enzyme) in amylopectin biosynthesis. Physiol. Plant 97: 491-498.
    • (1996) Physiol. Plant , vol.97 , pp. 491-498
    • Nakamura, Y.1    Umemoto, T.2    Takahata, Y.3    Komae, K.4    Amano, E.5    Satoh, H.6
  • 247
    • 0029681154 scopus 로고    scopus 로고
    • Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: Purification, cDNA and chromosomal location of the gene
    • Nakamura, Y., Umemoto, T., Ogata, N., Kuboki, Y., Yano, M., and Sasaki, T., 1996b. Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: purification, cDNA and chromosomal location of the gene. Planta 199: 209-218.
    • (1996) Planta , vol.199 , pp. 209-218
    • Nakamura, Y.1    Umemoto, T.2    Ogata, N.3    Kuboki, Y.4    Yano, M.5    Sasaki, T.6
  • 248
    • 0030814320 scopus 로고    scopus 로고
    • Correlation between activities of starch debranching enzyme and α-polyglucan structure in the endosperms of sugary-1 mutants of rice
    • Nakamura, Y., Kubo, A., Shimamune, T., Matsuda, T., Harada, K., and Satoh, H., 1997. Correlation between activities of starch debranching enzyme and α-polyglucan structure in the endosperms of sugary-1 mutants of rice. Plant J. 12: 143-153.
    • (1997) Plant J. , vol.12 , pp. 143-153
    • Nakamura, Y.1    Kubo, A.2    Shimamune, T.3    Matsuda, T.4    Harada, K.5    Satoh, H.6
  • 249
    • 0001037454 scopus 로고
    • The enzymatic deficiency in the waxy mutant of maize
    • Nelson, O. E. and Rines, H. W., 1962. The enzymatic deficiency in the waxy mutant of maize. Bitichem. Biophys. Res. Commun. 9: 297-300.
    • (1962) Bitichem. Biophys. Res. Commun. , vol.9 , pp. 297-300
    • Nelson, O.E.1    Rines, H.W.2
  • 250
    • 0001578389 scopus 로고
    • Characterization of glucose-6-phosphate incorporation into starch by isolated intact cauliflower-bud plastids
    • Neuhaus, H. E., Henrichs, G., and Scheibe, R., 1993. Characterization of glucose-6-phosphate incorporation into starch by isolated intact cauliflower-bud plastids. Plant Physiol. 101: 573-578.
    • (1993) Plant Physiol. , vol.101 , pp. 573-578
    • Neuhaus, H.E.1    Henrichs, G.2    Scheibe, R.3
  • 251
    • 0000117374 scopus 로고
    • Control analysis of photosynthate partitioning - Impact of reduced activity of ADP-glucose pyrophosphorylase or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis thaliana (L.) Heynh
    • Neuhaus, H. E., and Stitt, M. E., 1990. Control analysis of photosynthate partitioning - impact of reduced activity of ADP-glucose pyrophosphorylase or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis thaliana (L.) Heynh. Planta 182: 445-454.
    • (1990) Planta , vol.182 , pp. 445-454
    • Neuhaus, H.E.1    Stitt, M.E.2
  • 252
    • 0031036197 scopus 로고    scopus 로고
    • Characterization of a novel ATP/ADP transporter from Arahidopsis thaliana L
    • Neuhaus, H.E., Thom, E., Möhlmann, T., Steup, M., and Kampfenkel, K., 1997. Characterization of a novel ATP/ADP transporter from Arahidopsis thaliana L.. Plant J. 11: 73-83.
    • (1997) Plant J. , vol.11 , pp. 73-83
    • Neuhaus, H.E.1    Thom, E.2    Möhlmann, T.3    Steup, M.4    Kampfenkel, K.5
  • 254
    • 0027977606 scopus 로고
    • Starch phosphorylation in potato tubers proceeds with de novo biosynthesis of starch
    • Nielsen, T.H., Wischman, B., Enevoldsen, K. and Møller, B. L., 1994. Starch phosphorylation in potato tubers proceeds with de novo biosynthesis of starch. Plant Physiol., 105: 111-117.
    • (1994) Plant Physiol. , vol.105 , pp. 111-117
    • Nielsen, T.H.1    Wischman, B.2    Enevoldsen, K.3    Møller, B.L.4
  • 256
    • 0030901647 scopus 로고    scopus 로고
    • A beta-amylase in potato tubers is induced by storage at low temperature
    • Nielsen, T. H., Deiting, U., and Stitt, M., 1997. A beta-amylase in potato tubers is induced by storage at low temperature. Plant Physiol. 113: 503-510.
    • (1997) Plant Physiol. , vol.113 , pp. 503-510
    • Nielsen, T.H.1    Deiting, U.2    Stitt, M.3
  • 258
    • 0002376732 scopus 로고
    • The effect of abscisic acid on the differential expression of α-amylase isozymes in barley aleurone layers
    • Nolan, R. C., Lin, L-S., and Ho, T-H. D., 1987. The effect of abscisic acid on the differential expression of α-amylase isozymes in barley aleurone layers. Plant Mol. Biol. 8: 13-22.
    • (1987) Plant Mol. Biol. , vol.8 , pp. 13-22
    • Nolan, R.C.1    Lin, L.-S.2    Ho, T.-H.D.3
  • 259
    • 0002655738 scopus 로고    scopus 로고
    • Characterization of friabilin polypeptides
    • Oda, S. and Schofield, J. D., 1997. Characterization of friabilin polypeptides. J. Cereal Sci. 26: 29-36
    • (1997) J. Cereal Sci. , vol.26 , pp. 29-36
    • Oda, S.1    Schofield, J.D.2
  • 260
    • 0002433211 scopus 로고
    • Enzymic mechanism of starch breakdown in germinating rice seeds IX. De novo synthesis of β-amylase
    • Okamoto, K.and Akazawa, T. 1980. Enzymic mechanism of starch breakdown in germinating rice seeds IX. De novo synthesis of β-amylase. Plant Physiol. Biochem. 65: 81-84.
    • (1980) Plant Physiol. Biochem. , vol.65 , pp. 81-84
    • Okamoto, K.1    Akazawa, T.2
  • 261
    • 0001004433 scopus 로고
    • Subcellular localization of the starch degredative and biosynthetic enzymes in spinach leaves
    • Okita, T. W., Greenberg, E., Kuhn, D. N., and Preiss, J. 1979. Subcellular localization of the starch degredative and biosynthetic enzymes in spinach leaves. Plant Physiol. 64: 187-192.
    • (1979) Plant Physiol. , vol.64 , pp. 187-192
    • Okita, T.W.1    Greenberg, E.2    Kuhn, D.N.3    Preiss, J.4
  • 262
    • 0008568722 scopus 로고
    • Inheritance of starch characteristics in perisperm of Amaranthus hypocondriacus
    • Okuno, K. and Sakaguchi, S., 1982. Inheritance of starch characteristics in perisperm of Amaranthus hypocondriacus. J. Hered. 73: 467.
    • (1982) J. Hered. , vol.73 , pp. 467
    • Okuno, K.1    Sakaguchi, S.2
  • 263
    • 84989058826 scopus 로고
    • On the origin of a low angle spacing in starch
    • Oostergetel, G. T.and Van Bruggen, E. F. J., 1989. On the origin of a low angle spacing in starch. Starch/Staerke 41: 331-335.
    • (1989) Starch/Staerke , vol.41 , pp. 331-335
    • Oostergetel, G.T.1    Van Bruggen, E.F.J.2
  • 264
    • 0015213784 scopus 로고
    • Multiple forms of α-1,4-glucan synthetase from spinach leaves
    • Ozbun, J. L., Hawker, J. S., and Preiss, J., 1971. Multiple forms of α-1,4-glucan synthetase from spinach leaves. Biochem. Biophys. Res. Commun. 43: 631-636.
    • (1971) Biochem. Biophys. Res. Commun. , vol.43 , pp. 631-636
    • Ozbun, J.L.1    Hawker, J.S.2    Preiss, J.3
  • 265
    • 0015298145 scopus 로고
    • Soluble adenosine diphosphate glucose α-1,4-glucan α-4-glucosyltransferase from spinach leaves
    • Ozbun, J. L., Hawker, J. S., and Preiss, J., 1971. Soluble adenosine diphosphate glucose α-1,4-glucan α-4-glucosyltransferase from spinach leaves. Biochem. J. 126: 953-963.
    • (1971) Biochem. J. , vol.126 , pp. 953-963
    • Ozbun, J.L.1    Hawker, J.S.2    Preiss, J.3
  • 267
    • 84987248074 scopus 로고
    • Über die Phosphorsäure der Kartoffelstärke
    • Palasinski, M., 1980. Über die Phosphorsäure der Kartoffelstärke. Stärke 32: 305-312.
    • (1980) Stärke , vol.32 , pp. 305-312
    • Palasinski, M.1
  • 268
    • 0000523869 scopus 로고
    • Biochemical changes in the rice grain during germination
    • Palmiano, E. P. and Juliano, B. O., 1972. Biochemical changes in the rice grain during germination. Plant Physiol. 49: 751-756.
    • (1972) Plant Physiol. , vol.49 , pp. 751-756
    • Palmiano, E.P.1    Juliano, B.O.2
  • 269
    • 0000420233 scopus 로고
    • A debranching enzyme deficiency in endosperms of the sugary1 mutants of maize
    • Pan, D. and Nelson, O. E., 1984. A debranching enzyme deficiency in endosperms of the sugary1 mutants of maize. Plant Physiol. 74: 324-328
    • (1984) Plant Physiol. , vol.74 , pp. 324-328
    • Pan, D.1    Nelson, O.E.2
  • 270
    • 0014669417 scopus 로고
    • Glucose 1,6-diphosphate formation by phosphoglucomutase in mammalian tissues
    • Passoneau, J. V., Lowry, O. H., Schulz, D. W., and Brown, J. G., 1969. Glucose 1,6-diphosphate formation by phosphoglucomutase in mammalian tissues. J. Biol. Chem. 244: 902-909.
    • (1969) J. Biol. Chem. , vol.244 , pp. 902-909
    • Passoneau, J.V.1    Lowry, O.H.2    Schulz, D.W.3    Brown, J.G.4
  • 271
    • 37049048868 scopus 로고
    • The enzymic synthesis and degradation of starch. XX. The disproportionating enzyme of potato
    • Peat, S., Whelan, W. J., and Rees, W. R., 1956. The enzymic synthesis and degradation of starch. XX. The disproportionating enzyme of potato. J. Chem. Soc. pp. 44-53.
    • (1956) J. Chem. Soc. , pp. 44-53
    • Peat, S.1    Whelan, W.J.2    Rees, W.R.3
  • 272
    • 0019326173 scopus 로고
    • The citrate-stimulated starch synthase of starchy maize kernels: Purification and properties
    • Pollock, C. J. and Preiss, J., 1980. The citrate-stimulated starch synthase of starchy maize kernels: purification and properties. Arch. Biochem. Biophys. 204: 578-588.
    • (1980) Arch. Biochem. Biophys. , vol.204 , pp. 578-588
    • Pollock, C.J.1    Preiss, J.2
  • 273
    • 0000453796 scopus 로고
    • ADP-glucose transport by the chloroplast adenylate translocator is linked to starch biosynthesis
    • Pozueta-Romero, J., Ardita, F., and Akazawa, T., 1991. ADP-glucose transport by the chloroplast adenylate translocator is linked to starch biosynthesis. Plant Physiol. 97: 1565-1572.
    • (1991) Plant Physiol. , vol.97 , pp. 1565-1572
    • Pozueta-Romero, J.1    Ardita, F.2    Akazawa, T.3
  • 274
    • 0025948201 scopus 로고
    • Direct transport of ADPglucose by an adenylate translocator is linked to starch biosynthesis in amyloplasts
    • Pozueta-Romero, J., Frehner, M., Viale, A. M., and Akazawa, T., 1991. Direct transport of ADPglucose by an adenylate translocator is linked to starch biosynthesis in amyloplasts. Proc. Natl. Acad. Sci. USA 88: 5769-5773.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5769-5773
    • Pozueta-Romero, J.1    Frehner, M.2    Viale, A.M.3    Akazawa, T.4
  • 275
    • 0008599643 scopus 로고
    • Synthesis of polysaccharides in higher plants
    • Porter, H. K., 1962. Synthesis of polysaccharides in higher plants. Ann. Rev. Plant Physiol. 13: 303-328
    • (1962) Ann. Rev. Plant Physiol. , vol.13 , pp. 303-328
    • Porter, H.K.1
  • 276
    • 84940969074 scopus 로고
    • Biosynthesis of starch and its degradation
    • Academic Press, San Diego
    • Preiss, J. 1988. Biosynthesis of starch and its degradation. In: The Biochemistry of Plants, Vol. 14, pp. 181-254, Academic Press, San Diego.
    • (1988) The Biochemistry of Plants , vol.14 , pp. 181-254
    • Preiss, J.1
  • 277
    • 0002998420 scopus 로고
    • Biology and molecular biology of starch synthesis and its regulation
    • Preiss, J., 1991. Biology and molecular biology of starch synthesis and its regulation. Oxford Surv. Plant Mol. Cell Biol. 7: 59-114
    • (1991) Oxford Surv. Plant Mol. Cell Biol. , vol.7 , pp. 59-114
    • Preiss, J.1
  • 278
    • 0000813722 scopus 로고
    • Starch biosynthesis and degradation
    • Carbohydrates structure and function, Preiss, J., Ed., Academic Press, San Diego
    • Preiss, J. and Levi, C., 1980. Starch biosynthesis and degradation. In: The biochemistry of plants, Vol. 3, pp. 371-423, Carbohydrates structure and function, Preiss, J., Ed., Academic Press, San Diego.
    • (1980) The Biochemistry of Plants , vol.3 , pp. 371-423
    • Preiss, J.1    Levi, C.2
  • 279
    • 0028891165 scopus 로고
    • Biosynthesis of sulphoquinovosyldiacylglycerol by choloroplast fractions from pea and lettuce
    • Pugh, C. E., Hawkes, T., and Harwood, J. L. 1995. Biosynthesis of sulphoquinovosyldiacylglycerol by choloroplast fractions from pea and lettuce. Phytochemistry 39: 1071-1075.
    • (1995) Phytochemistry , vol.39 , pp. 1071-1075
    • Pugh, C.E.1    Hawkes, T.2    Harwood, J.L.3
  • 280
    • 0000145690 scopus 로고
    • Purification of an autocatalytic protein-glycosylating enzyme from cell suspensions of Daucus carota L
    • Quentmeier, H., Ingold, E., and Seitz, H. U., 1987. Purification of an autocatalytic protein-glycosylating enzyme from cell suspensions of Daucus carota L. Planta 171: 483-488.
    • (1987) Planta , vol.171 , pp. 483-488
    • Quentmeier, H.1    Ingold, E.2    Seitz, H.U.3
  • 281
    • 0008566915 scopus 로고
    • Phosphorus balance in potato tubers
    • Quick, W. A. and Li, P. H., 1976. Phosphorus balance in potato tubers. Potato Res. 19: 305-312
    • (1976) Potato Res. , vol.19 , pp. 305-312
    • Quick, W.A.1    Li, P.H.2
  • 282
    • 0027989849 scopus 로고
    • Cloning of a wheat 15-kDa grain softness protein (GSP). GSP is a mixture of puroindoline-like polypeptides
    • C.
    • Rahman, S., Jolly, C. J., C., Skerritt, J. H., and Wallosheck, A., 1994. Cloning of a wheat 15-kDa grain softness protein (GSP). GSP is a mixture of puroindoline-like polypeptides. Eur. J. Biochem. 223: 917-925
    • (1994) Eur. J. Biochem. , vol.223 , pp. 917-925
    • Rahman, S.1    Jolly, C.J.C.2    Skerritt, J.H.3    Wallosheck, A.4
  • 284
    • 0032081295 scopus 로고    scopus 로고
    • Characterization of SU1 isoamylase, a determinant of storage starch structure in maize
    • Rahman, A., Wong, K-S., Jane, J-L., Myers, A., and James, M. G., 1998. Characterization of SU1 isoamylase, a determinant of storage starch structure in maize. Plant Physiol. 117: 425-435.
    • (1998) Plant Physiol. , vol.117 , pp. 425-435
    • Rahman, A.1    Wong, K.-S.2    Jane, J.-L.3    Myers, A.4    James, M.G.5
  • 285
    • 0001487359 scopus 로고
    • Chromosomal localization and genomic organization of α-amylase genes in rice (Oryza sativa L.)
    • Ranjhan, S., Litts, J. C., Foolad, M. R., and Rodriguez, R. L., 1991. Chromosomal localization and genomic organization of α-amylase genes in rice (Oryza sativa L.). Theor. Appl. Genet., 82: 481-488.
    • (1991) Theor. Appl. Genet. , vol.82 , pp. 481-488
    • Ranjhan, S.1    Litts, J.C.2    Foolad, M.R.3    Rodriguez, R.L.4
  • 286
    • 0029103680 scopus 로고
    • In situ location of a starch granule bound protein in Durum wheat endosperm immunocytochemistry
    • Rayas-Duarte, P., Robinson, S. F., and Freeman, T. P. 1995. In situ location of a starch granule bound protein in Durum wheat endosperm immunocytochemistry. Cereal Chem. 72: 269-274.
    • (1995) Cereal Chem. , vol.72 , pp. 269-274
    • Rayas-Duarte, P.1    Robinson, S.F.2    Freeman, T.P.3
  • 287
    • 0002227061 scopus 로고
    • Adenosine diphosphate glucose and starch synthesis
    • Recondo, E. and Leloir, L. F., 1961. Adenosine diphosphate glucose and starch synthesis. Biochem. Biophys. Res. Commun. 6: 85-88.
    • (1961) Biochem. Biophys. Res. Commun. , vol.6 , pp. 85-88
    • Recondo, E.1    Leloir, L.F.2
  • 289
    • 0027302147 scopus 로고
    • Antisense repression of the chloroplast triose phosphate translocator affects carbon partitioning in transgenic potato plants
    • Riesmeier, J. W., Flügge, U. I., Schulz, B., Heineke, D., Heldt, H. W., Willmitzer, L., and Frommer, W. B., 1993. Antisense repression of the chloroplast triose phosphate translocator affects carbon partitioning in transgenic potato plants. Proc. Natl. Acad. Sci. USA 90: 6160-6164.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6160-6164
    • Riesmeier, J.W.1    Flügge, U.I.2    Schulz, B.3    Heineke, D.4    Heldt, H.W.5    Willmitzer, L.6    Frommer, W.B.7
  • 290
    • 0027958407 scopus 로고
    • Evidence for an essential role of the sucrose transporter in phloem loading and assimilate partitioning
    • Riesmeier, J. W., Willmitzer, L., and Frommer, W. B., 1994. Evidence for an essential role of the sucrose transporter in phloem loading and assimilate partitioning. EMBO J. 13: 1-7.
    • (1994) EMBO J. , vol.13 , pp. 1-7
    • Riesmeier, J.W.1    Willmitzer, L.2    Frommer, W.B.3
  • 291
    • 0345512090 scopus 로고
    • The structure of the starch polysaccharides and their organization in the starch granule
    • Shewry, P. R., Ed., Oxford University Press
    • Ring, S. G., Noel, T. R., and Bull, V. J., 1993. The structure of the starch polysaccharides and their organization in the starch granule. In: Seed storage compounds, Shewry, P. R., Ed., pp. 25-39, Oxford University Press.
    • (1993) Seed Storage Compounds , pp. 25-39
    • Ring, S.G.1    Noel, T.R.2    Bull, V.J.3
  • 292
    • 0001225454 scopus 로고
    • Lintnerized starches. Gel filtration and enzymatic studies of insoluble residues from prolonged acid treatment of potato starch
    • Robin, J. P., Mercier, C., Charbonniére, R., and Guilbot, A., 1974. Lintnerized starches. Gel filtration and enzymatic studies of insoluble residues from prolonged acid treatment of potato starch. Cereal Chem. 51: 389-406.
    • (1974) Cereal Chem. , vol.51 , pp. 389-406
    • Robin, J.P.1    Mercier, C.2    Charbonniére, R.3    Guilbot, A.4
  • 293
    • 0024297043 scopus 로고
    • Structural analysis of the waxy locus from Hordeum vulgare
    • Rohde, W., Becker, D., and Salamini, F., 1988. Structural analysis of the waxy locus from Hordeum vulgare. Nucleic Acids Res. 16: 7185-7186.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7185-7186
    • Rohde, W.1    Becker, D.2    Salamini, F.3
  • 294
    • 0028066315 scopus 로고
    • UDP-glucose:Protein transglucosylase in developing maize endosperm
    • Rothschild, A. and Tandecarz, J. S., 1994. UDP-glucose:protein transglucosylase in developing maize endosperm. Plant Sci. 97: 119-127.
    • (1994) Plant Sci. , vol.97 , pp. 119-127
    • Rothschild, A.1    Tandecarz, J.S.2
  • 295
    • 0008531522 scopus 로고
    • The glucose bisphosphate family of enzymes
    • Rose, Z. B., 1986. The glucose bisphosphate family of enzymes. Trends Biochem. 11: 253-254.
    • (1986) Trends Biochem. , vol.11 , pp. 253-254
    • Rose, Z.B.1
  • 297
    • 0008566118 scopus 로고
    • Effect of maturity and storage on distribution of phosphorus among starch and other components of potato tuber
    • Samotus, B. and Schwimmer, S., 1962. Effect of maturity and storage on distribution of phosphorus among starch and other components of potato tuber. Plant Physiol. 37: 519-522.
    • (1962) Plant Physiol. , vol.37 , pp. 519-522
    • Samotus, B.1    Schwimmer, S.2
  • 298
    • 34250141037 scopus 로고
    • Differential regulation of waxy gene expression in rice endosperm
    • Sano, Y., 1984. Differential regulation of waxy gene expression in rice endosperm. Theor. Appl. Genet. 68: 467-473.
    • (1984) Theor. Appl. Genet. , vol.68 , pp. 467-473
    • Sano, Y.1
  • 299
    • 0000417960 scopus 로고
    • Sugar compartmentation in frost-hardy and partially dehardened cabbage leaf cells
    • Santarius, K. A. and Milde, H., 1977. Sugar compartmentation in frost-hardy and partially dehardened cabbage leaf cells. Planta 136: 163-166
    • (1977) Planta , vol.136 , pp. 163-166
    • Santarius, K.A.1    Milde, H.2
  • 300
    • 0003014519 scopus 로고
    • The α-amylase isoenzymes of developing and germinating wheat grain
    • New York: Academic Press
    • Sargeant, J. G., 1979. The α-amylase isoenzymes of developing and germinating wheat grain. In: The biochemistry of cereals, pp. 339-343, New York: Academic Press.
    • (1979) The Biochemistry of Cereals , pp. 339-343
    • Sargeant, J.G.1
  • 301
    • 0008567439 scopus 로고
    • Multiple isoforms of starch synthetase in maize varieties as revealed by disc-gel electrophoresis and activity staining
    • Schiefer, S., Lee, E. Y. C., and Whelan, W. J., 1973. Multiple isoforms of starch synthetase in maize varieties as revealed by disc-gel electrophoresis and activity staining. FEBS Lett. 30: 129-132.
    • (1973) FEBS Lett. , vol.30 , pp. 129-132
    • Schiefer, S.1    Lee, E.Y.C.2    Whelan, W.J.3
  • 302
    • 0016756189 scopus 로고
    • α-Glucose-1-phosphate, a precursor in the biosynthesis of maltose in higher plants
    • Schilling, N. and Kandler, O., 1975. α-Glucose-1-phosphate, a precursor in the biosynthesis of maltose in higher plants. Trans. Biochem. Soc. 3: 985-987
    • (1975) Trans. Biochem. Soc. , vol.3 , pp. 985-987
    • Schilling, N.1    Kandler, O.2
  • 303
    • 0008601334 scopus 로고
    • Interaction of hydrolytic and phosphorolytic enzymes of starch metabolism in Kalanchoe daigremontiana
    • Schilling, N. and Dittrich, P., 1979. Interaction of hydrolytic and phosphorolytic enzymes of starch metabolism in Kalanchoe daigremontiana. Plants 147: 210-215
    • (1979) Plants , vol.147 , pp. 210-215
    • Schilling, N.1    Dittrich, P.2
  • 304
    • 33947440405 scopus 로고
    • Non-carbohydrate substances in the cereal starches
    • Schoch, T. J., 1942a. Non-carbohydrate substances in the cereal starches. J. Am. Cem. Soc. 64: 2954-2956.
    • (1942) J. Am. Cem. Soc. , vol.64 , pp. 2954-2956
    • Schoch, T.J.1
  • 305
    • 33947447389 scopus 로고
    • Fractionation of starch by selective precipitation with butanol
    • Schoch, T. J., 1942b. Fractionation of starch by selective precipitation with butanol. J. Am. Cem. Soc. 64: 2957-2960.
    • (1942) J. Am. Cem. Soc. , vol.64 , pp. 2957-2960
    • Schoch, T.J.1
  • 306
    • 84989685255 scopus 로고
    • A novel shrunken endosperm mutant of barley
    • Schulman, A. H. and Ahokas, H., 1990. A novel shrunken endosperm mutant of barley. Physiol. Plant. 78: 583-589.
    • (1990) Physiol. Plant. , vol.78 , pp. 583-589
    • Schulman, A.H.1    Ahokas, H.2
  • 307
    • 0027951508 scopus 로고
    • The effect of the shrunken endosperm mutation shx on starch granule development in barley seeds
    • Schulman, A. H., Tester, R. F., Ahokas, H., and Morrison, W. R., 1994. The effect of the shrunken endosperm mutation shx on starch granule development in barley seeds. J. Cereal Sci. 19: 49-55.
    • (1994) J. Cereal Sci. , vol.19 , pp. 49-55
    • Schulman, A.H.1    Tester, R.F.2    Ahokas, H.3    Morrison, W.R.4
  • 308
    • 0028857759 scopus 로고
    • Structural analysis of starch from normal and shx (shrunken endosperm) barley (Hordeum vulgare L.)
    • Schulman, A. H., Tomooka, S., Suzuki, A., Myllarinen, P., and Hizukuri, S., 1995. Structural analysis of starch from normal and shx (shrunken endosperm) barley (Hordeum vulgare L.). Carbohydr. Res. 275: 361-369.
    • (1995) Carbohydr. Res. , vol.275 , pp. 361-369
    • Schulman, A.H.1    Tomooka, S.2    Suzuki, A.3    Myllarinen, P.4    Hizukuri, S.5
  • 309
    • 0002021185 scopus 로고
    • Genetics and physiology of starch development
    • Whistler, R. L., BeMiller, J. N., and Paschall, E. F., Eds., Academic Press, Orlando, FL
    • Shannon, J. and Garwood, D. L., 1984. Genetics and physiology of starch development. In: Starch: chemistry and technology, pp. 25-86, Whistler, R. L., BeMiller, J. N., and Paschall, E. F., Eds., Academic Press, Orlando, FL.
    • (1984) Starch: Chemistry and Technology , pp. 25-86
    • Shannon, J.1    Garwood, D.L.2
  • 310
    • 0030028267 scopus 로고    scopus 로고
    • Nucleotides and nucleotide sugars in developing maize endosperms
    • Shannon, J. C., Pien, F-M., and Liu, K-C., 1996. Nucleotides and nucleotide sugars in developing maize endosperms. Plant Physiol. 110: 835-843.
    • (1996) Plant Physiol. , vol.110 , pp. 835-843
    • Shannon, J.C.1    Pien, F.-M.2    Liu, K.-C.3
  • 311
    • 0032134257 scopus 로고    scopus 로고
    • Brittle-1, an adenylate translocator, facilitates transfer of extraplastidial synthesized ADP-glucose into amyloplasts of maize endosperms
    • Shannon, J. C., Pien, F-M., Cao, H., and Liu, K-C. 1998. Brittle-1, an adenylate translocator, facilitates transfer of extraplastidial synthesized ADP-glucose into amyloplasts of maize endosperms. Plant Physiol. 117: 1235-1252.
    • (1998) Plant Physiol. , vol.117 , pp. 1235-1252
    • Shannon, J.C.1    Pien, F.-M.2    Cao, H.3    Liu, K.-C.4
  • 312
    • 0028406869 scopus 로고
    • Expression of Escherichia coli glycogen synthase in the tubers of transgenic potatoes (Solanum tuberosum) results in a highly branched starch
    • Shewmaker, C. K., Boyer, C. D., Wiesenborn, D. P., Thompson, D. B., Boersig, M. R., Oakes, J. V., and Stalker, D. M., 1994. Expression of Escherichia coli glycogen synthase in the tubers of transgenic potatoes (Solanum tuberosum) results in a highly branched starch. Plant Physiol. 104: 1159-1166.
    • (1994) Plant Physiol. , vol.104 , pp. 1159-1166
    • Shewmaker, C.K.1    Boyer, C.D.2    Wiesenborn, D.P.3    Thompson, D.B.4    Boersig, M.R.5    Oakes, J.V.6    Stalker, D.M.7
  • 313
    • 0001610219 scopus 로고
    • Multiple molecular forms of β-amylase in seeds and vegetative tissues of barley
    • Shewry, P. R., Parmar, S., Buxton, B., Gale, M. D., Liu, C. J., Hejgaard, J., and Kreis, M., 1988. Multiple molecular forms of β-amylase in seeds and vegetative tissues of barley. Planta 176: 127-134.
    • (1988) Planta , vol.176 , pp. 127-134
    • Shewry, P.R.1    Parmar, S.2    Buxton, B.3    Gale, M.D.4    Liu, C.J.5    Hejgaard, J.6    Kreis, M.7
  • 314
    • 14944338748 scopus 로고
    • Fine structure of maize starches from four wx-containing genotypes of the W64A inbred line in relation to gelatinization and retrogradation
    • Shi, Y-C. and Seib, P. A., 1995. Fine structure of maize starches from four wx-containing genotypes of the W64A inbred line in relation to gelatinization and retrogradation. Carbohydr. Polymers 26: 141-147.
    • (1995) Carbohydr. Polymers , vol.26 , pp. 141-147
    • Shi, Y.-C.1    Seib, P.A.2
  • 315
    • 0000152544 scopus 로고
    • Antisense regulation of the rice waxy gene expression using a PCR-amplified fragment of the rice genome reduces the amylose content in grain starch
    • Shimada, H., Tada, Y., Kawasaki, T., and Fujimura, T., 1993. Antisense regulation of the rice waxy gene expression using a PCR-amplified fragment of the rice genome reduces the amylose content in grain starch. Theor. Appl. Genet. 86: 665-672.
    • (1993) Theor. Appl. Genet. , vol.86 , pp. 665-672
    • Shimada, H.1    Tada, Y.2    Kawasaki, T.3    Fujimura, T.4
  • 316
    • 0020858877 scopus 로고
    • Molecular identification and isolation of the waxy locus in maize
    • Shure, M., Wessler, S., and Fedoroff, N., 1983. Molecular identification and isolation of the waxy locus in maize. Cell 35: 225-233.
    • (1983) Cell , vol.35 , pp. 225-233
    • Shure, M.1    Wessler, S.2    Fedoroff, N.3
  • 317
    • 0002058712 scopus 로고
    • Hexose and hexose-phosphate metabolism in barley leaves and roots. Role of glucose 1,6-bisphosphate
    • Sicher, R. C. and Kremer, D. F., 1990. Hexose and hexose-phosphate metabolism in barley leaves and roots. Role of glucose 1,6-bisphosphate. Plant Sci. 67: 47-56.
    • (1990) Plant Sci. , vol.67 , pp. 47-56
    • Sicher, R.C.1    Kremer, D.F.2
  • 318
    • 84989665775 scopus 로고
    • Control of carbohydrate metabolism in a starchless mutant of Arabidopsis thaliana
    • Sicher, R. C. and Kremer, D. F., 1992. Control of carbohydrate metabolism in a starchless mutant of Arabidopsis thaliana. Physiol. Plant. 85: 446-452.
    • (1992) Physiol. Plant. , vol.85 , pp. 446-452
    • Sicher, R.C.1    Kremer, D.F.2
  • 320
    • 0028973872 scopus 로고
    • Beta-Glucosylarginine: A new glucose-protein in a self-glucosylating protein from sweet corn
    • Singh, D. G., Lomako, J., Lomako, W. M., Whelan, W. J., Meyer, H. E., Serwe, M., and Metzger, J. W., 1995. Beta-Glucosylarginine: a new glucose-protein in a self-glucosylating protein from sweet corn. FEBS Lett. 376: 61-64.
    • (1995) FEBS Lett. , vol.376 , pp. 61-64
    • Singh, D.G.1    Lomako, J.2    Lomako, W.M.3    Whelan, W.J.4    Meyer, H.E.5    Serwe, M.6    Metzger, J.W.7
  • 321
    • 0027113458 scopus 로고
    • α-1,4-glucan synthesis by a chloroplastic phosphorylase isolated from spinach leaves is independent of added primer
    • Sivak, M. N., 1992. α-1,4-glucan synthesis by a chloroplastic phosphorylase isolated from spinach leaves is independent of added primer. Carbohydr. Res. 227: 241-255.
    • (1992) Carbohydr. Res. , vol.227 , pp. 241-255
    • Sivak, M.N.1
  • 322
    • 85051574469 scopus 로고
    • Starch synthesis in seeds
    • Kigel, J. and Galili, G., Eds., Marcel Dekker, New York
    • Sivak, M. N. and Preiss, J., 1994. Starch synthesis in seeds. In: Seed Development and Germination. pp. 139-168, Kigel, J. and Galili, G., Eds., Marcel Dekker, New York.
    • (1994) Seed Development and Germination , pp. 139-168
    • Sivak, M.N.1    Preiss, J.2
  • 324
  • 325
    • 0019741739 scopus 로고
    • Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme
    • Sivak, M. N., Tandecarz, J. S., and Cardini, C. E., 1981a. Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme. Arch. Biochem. Biophys. 212: 525-536.
    • (1981) Arch. Biochem. Biophys. , vol.212 , pp. 525-536
    • Sivak, M.N.1    Tandecarz, J.S.2    Cardini, C.E.3
  • 326
    • 0019760924 scopus 로고
    • Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product
    • Sivak, M. N., Tandecarz, J. S., and Cardini, C. E., 1981b. Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product. Arch. Biochem. Biophys. 212: 537-545.
    • (1981) Arch. Biochem. Biophys. , vol.212 , pp. 537-545
    • Sivak, M.N.1    Tandecarz, J.S.2    Cardini, C.E.3
  • 327
    • 0030765885 scopus 로고    scopus 로고
    • Engineering plant metabolism
    • Smeekens, S., 1997. Engineering plant metabolism. Trends Plant Sci. 2: 286-288.
    • (1997) Trends Plant Sci. , vol.2 , pp. 286-288
    • Smeekens, S.1
  • 328
    • 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
  • 329
    • 0000060178 scopus 로고
    • Evidence that the "waxy" protein of pea (Pisum sativum L.) is not the major starch-granule-bound starch synthase
    • Smith, A. M., 1990. Evidence that the "waxy" protein of pea (Pisum sativum L.) is not the major starch-granule-bound starch synthase. Planta 181: 310-315.
    • (1990) Planta , vol.181 , pp. 310-315
    • Smith, A.M.1
  • 330
    • 84987013540 scopus 로고
    • Tansley review No. 39: Starch synthesis in developing pea embryos
    • Smith, A. M. and Denyer, K., 1992. Tansley review No. 39: Starch synthesis in developing pea embryos. New Phytol. 122: 21-33.
    • (1992) New Phytol. , vol.122 , pp. 21-33
    • Smith, A.M.1    Denyer, K.2
  • 331
    • 0001366025 scopus 로고
    • Evidence that the rb locus alters the starch content of developing pea embryos through an effect on ADP glucose pyrophosphorylase
    • Smith, A. M., Bettey, M., and Bedford, I. D., 1989. Evidence that the rb locus alters the starch content of developing pea embryos through an effect on ADP glucose pyrophosphorylase. Plant Phys. 89: 1279-1284.
    • (1989) Plant Phys. , vol.89 , pp. 1279-1284
    • Smith, A.M.1    Bettey, M.2    Bedford, I.D.3
  • 333
    • 0025808151 scopus 로고
    • The discovery of glycogenin and the priming mechanism for glycogen biosynthesis
    • Smythe, C. and Cohen, P., 1991. The discovery of glycogenin and the priming mechanism for glycogen biosynthesis. Eur. J. Biochem. 200: 625-632.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 625-632
    • Smythe, C.1    Cohen, P.2
  • 334
    • 0029240175 scopus 로고
    • A second L-type isozyme of potato glucan phosphorylase: Cloning, antisense inhibition and expression analysis
    • Sonnewald, U., Basner, A., Greve, B., and Steup, M., 1995. A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis. Plant Mol. Biol. 27: 567-576.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 567-576
    • Sonnewald, U.1    Basner, A.2    Greve, B.3    Steup, M.4
  • 336
    • 0008599743 scopus 로고
    • Some effects of the waxy gene in corn on properties of the endosperm starch
    • Sprague, G. F., Brimhall, B., and Hixon, R. M., 1943. Some effects of the waxy gene in corn on properties of the endosperm starch. J. Am. Soc. Agron. 35: 817-822
    • (1943) J. Am. Soc. Agron. , vol.35 , pp. 817-822
    • Sprague, G.F.1    Brimhall, B.2    Hixon, R.M.3
  • 337
    • 0028190934 scopus 로고
    • Cloning, antisense RNA inhibition, and the coordinated expression of UDP-glucose pyrophosphorylase with starch biosynthetic genes in potato tubers
    • Spychalla, J. P., Scheffler, B. E., Sowokinos, J. R., and Bevan, M. W., 1994. Cloning, antisense RNA inhibition, and the coordinated expression of UDP-glucose pyrophosphorylase with starch biosynthetic genes in potato tubers. J. Plant. Physiol. 144: 444-453.
    • (1994) J. Plant. Physiol. , vol.144 , pp. 444-453
    • Spychalla, J.P.1    Scheffler, B.E.2    Sowokinos, J.R.3    Bevan, M.W.4
  • 338
    • 0026458333 scopus 로고
    • Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase
    • Stark, D. M., Timmerman, K. P., Barry, G. F., Preiss, J., and Kishore, G. M., 1992. Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase. Science 258: 287-292.
    • (1992) Science , vol.258 , pp. 287-292
    • Stark, D.M.1    Timmerman, K.P.2    Barry, G.F.3    Preiss, J.4    Kishore, G.M.5
  • 339
    • 84940995250 scopus 로고
    • Starch degradation
    • Academic Press, San Diego
    • Steup, M., 1988. Starch degradation. In: The biochemistry of plants Vol 14, pp. 255-295, Academic Press, San Diego.
    • (1988) The Biochemistry of Plants Vol 14 , vol.14 , pp. 255-295
    • Steup, M.1
  • 340
    • 0027144390 scopus 로고
    • Genetic isolation, cloning, and analysis of a mutator-induced, dominant antimorph of the maize amylose extender1 locus
    • Stinard, P. S., Robertson, D. S., and Schnable, P. S., 1993. Genetic isolation, cloning, and analysis of a mutator-induced, dominant antimorph of the maize amylose extender1 locus. Plant Cell 5: 1555-1566.
    • (1993) Plant Cell , vol.5 , pp. 1555-1566
    • Stinard, P.S.1    Robertson, D.S.2    Schnable, P.S.3
  • 341
    • 0001520667 scopus 로고
    • β-amylase from mustard Sinapsis alba L. Cotyledons. Immunochemical evidence for synthesis de novo during photoregulated seedling development
    • Subbaramaiah, K. and Sharma R., 1989. β-amylase from mustard Sinapsis alba L. cotyledons. Immunochemical evidence for synthesis de novo during photoregulated seedling development. Plant Phys. 89: 860-866.
    • (1989) Plant Phys. , vol.89 , pp. 860-866
    • Subbaramaiah, K.1    Sharma, R.2
  • 342
    • 0002638681 scopus 로고
    • Proteins associated with the surface of wheat starch granules purified by centrifuging through caesium chloride
    • Sulaiman, B. D., and Morrison, W. R. 1990. Proteins associated with the surface of wheat starch granules purified by centrifuging through caesium chloride. J. Cereal Sci. 12: 53-62.
    • (1990) J. Cereal Sci. , vol.12 , pp. 53-62
    • Sulaiman, B.D.1    Morrison, W.R.2
  • 343
    • 0026291471 scopus 로고
    • Analysis of maize Brittle-1 alleles and a defective suppressor-mutator-induced mutatable allele
    • Sullivan, T. D., Strelow, L.I., Illingworth, C. A., Phillips, R. L., and Nelson, O. E., 1991. Analysis of maize Brittle-1 alleles and a defective suppressor-mutator-induced mutatable allele. Plant Cell 3: 1337-1348.
    • (1991) Plant Cell , vol.3 , pp. 1337-1348
    • Sullivan, T.D.1    Strelow, L.I.2    Illingworth, C.A.3    Phillips, R.L.4    Nelson, O.E.5
  • 344
    • 0028980954 scopus 로고
    • The maize brittle-1 gene encodes amyloplast membrane polypeptides
    • Sullivan, T. and Kaneko, Y., 1995. The maize brittle-1 gene encodes amyloplast membrane polypeptides. Planta 196: 477-484.
    • (1995) Planta , vol.196 , pp. 477-484
    • Sullivan, T.1    Kaneko, Y.2
  • 345
    • 0008599744 scopus 로고
    • The water-soluble polysaccharides of sweet corn
    • Sumner, J. B. and Somers, G. F., 1944. The water-soluble polysaccharides of sweet corn. Arch. Biochem. 4: 7-9.
    • (1944) Arch. Biochem. , vol.4 , pp. 7-9
    • Sumner, J.B.1    Somers, G.F.2
  • 346
    • 0026145963 scopus 로고
    • Characterization of an α-amylase multigene cluster in rice
    • Sutliff, T. D., Huang, N., Litts, J. C., and Rodriguez, R. L. 1991. Characterization of an α-amylase multigene cluster in rice. Plant Mol. Biol. 16: 579-592.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 579-592
    • Sutliff, T.D.1    Huang, N.2    Litts, J.C.3    Rodriguez, R.L.4
  • 347
    • 0029853690 scopus 로고    scopus 로고
    • Characterization of transgenic potato (Solanum tuberosum L.) tubers with increased ADPglucose pyrophosphorylase
    • Sweetlove, L. J., Burrell, M. M., and Ap Rees, T., 1996a Characterization of transgenic potato (Solanum tuberosum L.) tubers with increased ADPglucose pyrophosphorylase. Biochem. J., 320: 487-492.
    • (1996) Biochem. J. , vol.320 , pp. 487-492
    • Sweetlove, L.J.1    Burrell, M.M.2    Ap Rees, T.3
  • 348
    • 0029902429 scopus 로고    scopus 로고
    • Starch metabolism in tubers of transgenic potato (Solanum tuberosum) with increased ADPglucose pyrophosphorylase
    • Sweetlove, L. J., Burrell, M. M., and ap Rees, T., 1996b. Starch metabolism in tubers of transgenic potato (Solanum tuberosum) with increased ADPglucose pyrophosphorylase. Biochem. J. 320: 493-498.
    • (1996) Biochem. J. , vol.320 , pp. 493-498
    • Sweetlove, L.J.1    Burrell, M.M.2    Ap Rees, T.3
  • 349
    • 84987226629 scopus 로고
    • Composition and properties of commercial and native starches
    • Swinkels, J. J. M., 1985. Composition and properties of commercial and native starches. Starch/Staerke 37: 1-5
    • (1985) Starch/Staerke , vol.37 , pp. 1-5
    • Swinkels, J.J.M.1
  • 350
    • 84984005700 scopus 로고
    • Studies on starch phosphate. II. Isolation of glucose 3-phosphate and maltose phosphate by acid hydrolysis of potato starch
    • Tabata, S. and Hizukuri, S., 1971. Studies on starch phosphate. II. Isolation of glucose 3-phosphate and maltose phosphate by acid hydrolysis of potato starch. Starch/Staerke 23: 267-271.
    • (1971) Starch/Staerke , vol.23 , pp. 267-271
    • Tabata, S.1    Hizukuri, S.2
  • 351
    • 0027458378 scopus 로고
    • Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism
    • Takaha, T., Yanase, M., Okada, S., and Smith, S.M., 1993. Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. J. Biol. Chem. 268: 1391-1396.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1391-1396
    • Takaha, T.1    Yanase, M.2    Okada, S.3    Smith, S.M.4
  • 352
    • 0031833364 scopus 로고    scopus 로고
    • Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase)
    • Takaha, T., Critchley, J., Okada, S., and Smith, S. M., 1998. Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase). Planta 205: 445-451.
    • (1998) Planta , vol.205 , pp. 445-451
    • Takaha, T.1    Critchley, J.2    Okada, S.3    Smith, S.M.4
  • 353
    • 0000781796 scopus 로고    scopus 로고
    • Structural characterisation of high molecular weight starch granule bound proteins in wheat (Triticum aestivum L.)
    • Takaoka, M., Watanabe, S., Sassa, H., Yamamori, M, Nakamura, T., Sasakuma, T., and Hirano, H., 1997. Structural characterisation of high molecular weight starch granule bound proteins in wheat (Triticum aestivum L.). J. Agric. Food Chem. 45: 2929-2934.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2929-2934
    • Takaoka, M.1    Watanabe, S.2    Sassa, H.3    Yamamori, M.4    Nakamura, T.5    Sasakuma, T.6    Hirano, H.7
  • 354
    • 0027551651 scopus 로고
    • Structures of B90 (sugary) and W64A (normal) maize starches
    • Takeda, Y. and Preiss, J., 1993. Structures of B90 (sugary) and W64A (normal) maize starches. Carbohydr. Res. 240: 265-275.
    • (1993) Carbohydr. Res. , vol.240 , pp. 265-275
    • Takeda, Y.1    Preiss, J.2
  • 355
    • 0002166575 scopus 로고
    • Examination of the purity and structure of amylose by gel-permeation chromatography
    • Takeda, Y., Shirasaka, K., and Hizukuri, S., 1984. Examination of the purity and structure of amylose by gel-permeation chromatography. Carbohydr. Res. 132: 83-92.
    • (1984) Carbohydr. Res. , vol.132 , pp. 83-92
    • Takeda, Y.1    Shirasaka, K.2    Hizukuri, S.3
  • 356
    • 0001114581 scopus 로고
    • Purification and structure of amylose from rice starch
    • Takeda, Y., Hizukuri, S., and Juliano, B. O. 1986. Purification and structure of amylose from rice starch. Carbohydr. Res. 148: 299-308.
    • (1986) Carbohydr. Res. , vol.148 , pp. 299-308
    • Takeda, Y.1    Hizukuri, S.2    Juliano, B.O.3
  • 357
    • 45949116140 scopus 로고
    • Structures of rice amylopectins with low and high affinities for iodine
    • Takeda, Y., Hizukuri, S., and Juliano, B. O. 1987. Structures of rice amylopectins with low and high affinities for iodine. Carbohydr. Res. 168: 79-88.
    • (1987) Carbohydr. Res. , vol.168 , pp. 79-88
    • Takeda, Y.1    Hizukuri, S.2    Juliano, B.O.3
  • 358
    • 0027551838 scopus 로고
    • Branching of amylose by the branching isoenzymes of maize endosperm
    • Takeda, Y., Guan, H-P., and Preiss, J. 1993. Branching of amylose by the branching isoenzymes of maize endosperm. Carbohydr. Res. 246: 253-263.
    • (1993) Carbohydr. Res. , vol.246 , pp. 253-263
    • Takeda, Y.1    Guan, H.-P.2    Preiss, J.3
  • 359
    • 0028093886 scopus 로고
    • Starch synthesis and carbohydrate oxidation in amyloplasts from developing wheat endosperm
    • Tetlow, I. J., Blissett, K. J. and Ernes, M. J., 1994. Starch synthesis and carbohydrate oxidation in amyloplasts from developing wheat endosperm. Planta 194: 454-460.
    • (1994) Planta , vol.194 , pp. 454-460
    • Tetlow, I.J.1    Blissett, K.J.2    Ernes, M.J.3
  • 360
    • 0030483916 scopus 로고    scopus 로고
    • Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm
    • Thorbjørnsen, T., Villand, P., Denyer, K., Olsen, O. A. and Smith A. M., 1996. Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm. Plant J. 10: 243-250.
    • (1996) Plant J. , vol.10 , pp. 243-250
    • Thorbjørnsen, T.1    Villand, P.2    Denyer, K.3    Olsen, O.A.4    Smith, A.M.5
  • 361
    • 0032439289 scopus 로고    scopus 로고
    • Altered plastidic ATP/ ADP-transporter activitiy influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch
    • Tjaden, J., Möhlmann, T., Kampfenkel, K., Henrichs, G., and Neuhaus, H. E., 1998. Altered plastidic ATP/ ADP-transporter activitiy influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch. Plant J. 16: 531-540.
    • (1998) Plant J. , vol.16 , pp. 531-540
    • Tjaden, J.1    Möhlmann, T.2    Kampfenkel, K.3    Henrichs, G.4    Neuhaus, H.E.5
  • 362
    • 85009537938 scopus 로고
    • Changes of a rice debranching enzyme during seed formation and germination
    • Toguri, T. 1991. Changes of a rice debranching enzyme during seed formation and germination. J. Plant Physiol. 137: 541-546.
    • (1991) J. Plant Physiol. , vol.137 , pp. 541-546
    • Toguri, T.1
  • 363
    • 0031027256 scopus 로고    scopus 로고
    • Importance of isoforms of starch-branching enzyme in determining the structure of starch in pea leaves
    • Tomlinson, K., Lloyd, J. R., and Smith, A. M., 1997. Importance of isoforms of starch-branching enzyme in determining the structure of starch in pea leaves. Plant J. 11: 31-43.
    • (1997) Plant J. , vol.11 , pp. 31-43
    • Tomlinson, K.1    Lloyd, J.R.2    Smith, A.M.3
  • 364
    • 0027978717 scopus 로고
    • A mutant of Arabidopsis thaliana lacking the ability to transport glucose across the chloroplast envelope
    • Trethewey, R. N. and ap Rees, T., 1994a. A mutant of Arabidopsis thaliana lacking the ability to transport glucose across the chloroplast envelope. Biochem. J., 301: 449-454.
    • (1994) Biochem. J. , vol.301 , pp. 449-454
    • Trethewey, R.N.1    Ap Rees, T.2
  • 365
    • 0028191115 scopus 로고
    • The role of the hexose transporter in the chloroplasts of Arabodopsis thaliana L
    • Trethewey, R. N. and ap Rees, T., 1994b. The role of the hexose transporter in the chloroplasts of Arabodopsis thaliana L. Planta, 195: 168-174.
    • (1994) Planta , vol.195 , pp. 168-174
    • Trethewey, R.N.1    Ap Rees, T.2
  • 366
    • 0031873436 scopus 로고    scopus 로고
    • Combined expression of glucokinase and invertase in potato tubers leads to a dramatic reduction in starch accumulation and a stimulation of glycolysis
    • Trethewey, R. N., Geigenberger, P., Riedel, K., Hajirezaei, M-R., Sonnewald, U., Stitt, M., Riesmeier, J. W., and Willmitzer, L., 1998. Combined expression of glucokinase and invertase in potato tubers leads to a dramatic reduction in starch accumulation and a stimulation of glycolysis. Plant J. 15: 109-118.
    • (1998) Plant J. , vol.15 , pp. 109-118
    • Trethewey, R.N.1    Geigenberger, P.2    Riedel, K.3    Hajirezaei, M.-R.4    Sonnewald, U.5    Stitt, M.6    Riesmeier, J.W.7    Willmitzer, L.8
  • 367
    • 0015988432 scopus 로고
    • The function of the Waxy locus in starch synthesis in maize endosperm
    • Tsai, C. Y., 1974. The function of the Waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11: 83-96.
    • (1974) Biochem. Genet. , vol.11 , pp. 83-96
    • Tsai, C.Y.1
  • 368
    • 0014023725 scopus 로고
    • Starch-deficient mutant lacking adenosine diphosphate glucose pyrophosphorylase activity
    • Tsai, C. Y. and Nelson, O. E., 1966. Starch-deficient mutant lacking adenosine diphosphate glucose pyrophosphorylase activity. Science 151: 341-343.
    • (1966) Science , vol.151 , pp. 341-343
    • Tsai, C.Y.1    Nelson, O.E.2
  • 369
    • 0001549597 scopus 로고
    • Phosphorylases I and II of maize endosperm
    • Tsai, C. Y. and Nelson, O. E., 1968. Phosphorylases I and II of maize endosperm. Plant Physiol. 43: 103-112.
    • (1968) Plant Physiol. , vol.43 , pp. 103-112
    • Tsai, C.Y.1    Nelson, O.E.2
  • 370
    • 0001566111 scopus 로고
    • Mutations at the shrunken-4 locus in maize that produce three altered phosphorylases
    • Tsai, C. Y. and Nelson, O. E., 1969a. Mutations at the shrunken-4 locus in maize that produce three altered phosphorylases. Genetics 61: 813-821.
    • (1969) Genetics , vol.61 , pp. 813-821
    • Tsai, C.Y.1    Nelson, O.E.2
  • 371
    • 0014468724 scopus 로고
    • Two additional phosphorylases in developing maize seed
    • Tsai, C. Y. and Nelson, O. E., 1969b. Two additional phosphorylases in developing maize seed. Plant Physiol. 44: 159-167.
    • (1969) Plant Physiol. , vol.44 , pp. 159-167
    • Tsai, C.Y.1    Nelson, O.E.2
  • 372
    • 0027134680 scopus 로고
    • An analysis of soluble starch synthase isozymes from the developing grains of normal and shx cv. Bomi barley (Hordeum vulgare L.)
    • Tyynelä, J. and Schulman, A. H., 1993. An analysis of soluble starch synthase isozymes from the developing grains of normal and shx cv. Bomi barley (Hordeum vulgare L.). Physiol. Plant. 89: 835-841.
    • (1993) Physiol. Plant. , vol.89 , pp. 835-841
    • Tyynelä, J.1    Schulman, A.H.2
  • 373
    • 0029140410 scopus 로고
    • Metabolism of starch synthesis in developing grains of the shx shrunken mutant of barley (Hordeum vulgare)
    • Tyynelä, J., Stitt, M., Lönneborg, A., Smeekens, S., and Schulman, A. H., 1995. Metabolism of starch synthesis in developing grains of the shx shrunken mutant of barley (Hordeum vulgare). Physiol. Plant. 93: 77-84.
    • (1995) Physiol. Plant. , vol.93 , pp. 77-84
    • Tyynelä, J.1    Stitt, M.2    Lönneborg, A.3    Smeekens, S.4    Schulman, A.H.5
  • 374
    • 0001802996 scopus 로고
    • Starch synthesis by isolated amyloplasts from wheat endosperm
    • Tyson, R. H. and ap Rees, T., 1988. Starch synthesis by isolated amyloplasts from wheat endosperm. Planta 175: 33-38.
    • (1988) Planta , vol.175 , pp. 33-38
    • Tyson, R.H.1    Ap Rees, T.2
  • 375
    • 0000554896 scopus 로고
    • Glucan phosphorylase forms in cotyledons of Pisum sativum L.: Localization, developmental change, in vitro translation, and processing
    • van Berkel, J., Conrads-Strauch, J., and Steup, M, 1991. Glucan phosphorylase forms in cotyledons of Pisum sativum L.: localization, developmental change, in vitro translation, and processing. Planta 185: 432-439.
    • (1991) Planta , vol.185 , pp. 432-439
    • Van Berkel, J.1    Conrads-Strauch, J.2    Steup, M.3
  • 376
    • 0032575558 scopus 로고    scopus 로고
    • Amylose is synthesized in vitro by extension of and cleavage from amylopectin
    • Van De Wal, M., D'Hulst, C., Vincken, J. P., Buleon, A., Visser, R., and Ball, S., 1998. Amylose is synthesized in vitro by extension of and cleavage from amylopectin. J. Biol. Chem. 273: 22232-22240.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22232-22240
    • De Van Wal, M.1    D'Hulst, C.2    Vincken, J.P.3    Buleon, A.4    Visser, R.5    Ball, S.6
  • 378
    • 0000200707 scopus 로고    scopus 로고
    • Phosphorylated α (1,4) glucans for potato starch branching enzyme I
    • Viksø-Nielsen, A., Blennow, A., Nielsen, T. H., and Møller, B. L. 1998. Phosphorylated α (1,4) glucans for potato starch branching enzyme I. Plant Physiol. 117: 869-875.
    • (1998) Plant Physiol. , vol.117 , pp. 869-875
    • Viksø-Nielsen, A.1    Blennow, A.2    Nielsen, T.H.3    Møller, B.L.4
  • 379
    • 0026875704 scopus 로고
    • PCR amplification and sequences of cDNA clones for the small and large subunits of ADP-glucose pyrophosphorylase from barley tissue
    • Villand, P., Aalen, R., Olsen., O-A., Lüthi, E., Lönneborg, A., and Kleczowski, L., 1992. PCR amplification and sequences of cDNA clones for the small and large subunits of ADP-glucose pyrophosphorylase from barley tissue. Plant Mol. Biol. 19: 381-389.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 381-389
    • Villand, P.1    Aalen, R.2    Lüthi, E.3    Lönneborg, A.4    Kleczowski, L.5
  • 380
    • 0028092299 scopus 로고
    • Is there an alternative pathway for starch biosynthesis in cereal seeds?
    • Villand, P. and Kleczowski, L., 1994. Is there an alternative pathway for starch biosynthesis in cereal seeds? Z. Natuirforsch. Teil C, 49: 215-219.
    • (1994) Z. Natuirforsch. Teil C , vol.49 , pp. 215-219
    • Villand, P.1    Kleczowski, L.2
  • 381
    • 84987189221 scopus 로고
    • Waxy gene factor and residual protein of rice starch granules
    • Villareal, C. P. and Juliano, B. O., 1986. Waxy gene factor and residual protein of rice starch granules. Starch/ Staerke 38: 118-119.
    • (1986) Starch/ Staerke , vol.38 , pp. 118-119
    • Villareal, C.P.1    Juliano, B.O.2
  • 383
    • 0001125381 scopus 로고
    • Fluoride-induced inhibition of starch biosynthesis in developing potato (Solanum tuberosum L.) tubers is associated with pyrophosphate accumulation
    • Viola, R. and Davies, H. V., 1991. Fluoride-induced inhibition of starch biosynthesis in developing potato (Solanum tuberosum L.) tubers is associated with pyrophosphate accumulation. Plant Physiol. 97: 638-643.
    • (1991) Plant Physiol. , vol.97 , pp. 638-643
    • Viola, R.1    Davies, H.V.2
  • 384
    • 0027052913 scopus 로고
    • Rabbit skeletal muscle glycogenin: Molecular cloning and production of fully functional protein in Escherichia coli
    • Viskupic, E., Cao, Y., Zhang, W., Cheng, C., Depaoli Roach, A. A., and Roach, P. J. 1992. Rabbit skeletal muscle glycogenin: molecular cloning and production of fully functional protein in Escherichia coli. J. Biol. Chem. 267: 25759-25763.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25759-25763
    • Viskupic, E.1    Cao, Y.2    Zhang, W.3    Cheng, C.4    Depaoli Roach, A.A.5    Roach, P.J.6
  • 385
    • 0026027970 scopus 로고
    • Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs
    • Visser, R. G. F., Somhorst, I., Kuipers, G. J., Ruys, N. J., Feenstra, W. J., and Jacobsen, E., 1991. Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs. Mol. Gen. Genet. 225: 289-296.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 289-296
    • Visser, R.G.F.1    Somhorst, I.2    Kuipers, G.J.3    Ruys, N.J.4    Feenstra, W.J.5    Jacobsen, E.6
  • 386
    • 0031167299 scopus 로고    scopus 로고
    • Analysis of the native structure of starch granule with X-ray microfocus diffraction
    • Waigh, T. A., Hopkinson, I., Donald, A. M., Butler, M. F., Heidelbach, F., and Riekel, C., 1997. Analysis of the native structure of starch granule with X-ray microfocus diffraction. Macromolecules 30: 3813-3820.
    • (1997) Macromolecules , vol.30 , pp. 3813-3820
    • Waigh, T.A.1    Hopkinson, I.2    Donald, A.M.3    Butler, M.F.4    Heidelbach, F.5    Riekel, C.6
  • 387
    • 0008565421 scopus 로고
    • Synthesis of amylose by potato D-enzyme
    • Walker, G. J. and Whelan, W. J. 1959. Synthesis of amylose by potato D-enzyme. Nature 183: 46
    • (1959) Nature , vol.183 , pp. 46
    • Walker, G.J.1    Whelan, W.J.2
  • 388
    • 0000360369 scopus 로고
    • The action of some α-amylases on starch granules
    • Walker, G. J. and Hope, P. M., 1963. The action of some α-amylases on starch granules. Biochem. J. 86: 452-462.
    • (1963) Biochem. J. , vol.86 , pp. 452-462
    • Walker, G.J.1    Hope, P.M.2
  • 390
    • 0001677498 scopus 로고
    • Characterization of starch structures of 17 maize endosperm mutant genotypes with Oh43 inbred line background
    • Wang, Y-J., White, P., Pollak, L., and Jane, J-L., 1993a. Characterization of starch structures of 17 maize endosperm mutant genotypes with Oh43 inbred line background. Cereal Chem. 70: 171-179.
    • (1993) Cereal Chem. , vol.70 , pp. 171-179
    • Wang, Y.-J.1    White, P.2    Pollak, L.3    Jane, J.-L.4
  • 391
    • 0000464470 scopus 로고
    • Amylopectin and intermediate materials in starches from mutant genotypes of the Oh43 inbred line
    • Wang, Y-J., White, P., Pollak, L., and Jane, J-L., 1993b. Amylopectin and intermediate materials in starches from mutant genotypes of the Oh43 inbred line. Cereal Chem. 70: 521-525.
    • (1993) Cereal Chem. , vol.70 , pp. 521-525
    • Wang, Y.-J.1    White, P.2    Pollak, L.3    Jane, J.-L.4
  • 392
    • 0030901434 scopus 로고    scopus 로고
    • Characterization of a maize β-amylase cDNA clone and its expression during seed germination
    • Wang, S-M., Lue, W-L., Shu-Yuann, W., Huang, H-W., and Chen, J., 1997. Characterization of a maize β-amylase cDNA clone and its expression during seed germination. Plant Physiol. 113: 403-409.
    • (1997) Plant Physiol. , vol.113 , pp. 403-409
    • Wang, S.-M.1    Lue, W.-L.2    Shu-Yuann, W.3    Huang, H.-W.4    Chen, J.5
  • 393
    • 0032191986 scopus 로고    scopus 로고
    • Expression of a yeast-derived invertase in developing cotyledons of Vicia narbonensis alters the carbohydrate state and affects storage functions
    • Weber, H., Heim, U., Golombek, S., Borisjuk, L., Manteuffel, R., and Wobus, U., 1998. Expression of a yeast-derived invertase in developing cotyledons of Vicia narbonensis alters the carbohydrate state and affects storage functions. Plant J. 16: 163-172.
    • (1998) Plant J. , vol.16 , pp. 163-172
    • Weber, H.1    Heim, U.2    Golombek, S.3    Borisjuk, L.4    Manteuffel, R.5    Wobus, U.6
  • 394
    • 0001432052 scopus 로고
    • An endogenous α-amylase inhibitor in barley kernels
    • Weselake, R. J., MacGregor, A. W., and Hill, R. D., 1983. An endogenous α-amylase inhibitor in barley kernels. Plant Physiol. 72: 809-812.
    • (1983) Plant Physiol. , vol.72 , pp. 809-812
    • Weselake, R.J.1    MacGregor, A.W.2    Hill, R.D.3
  • 395
    • 0028112556 scopus 로고
    • Enzymes of starch metabolism in poplar wood during fall and winter
    • Witt, W. and Sauter, J. J., 1994. Enzymes of starch metabolism in poplar wood during fall and winter. J. Plant Physiol., 143: 625-631.
    • (1994) J. Plant Physiol. , vol.143 , pp. 625-631
    • Witt, W.1    Sauter, J.J.2
  • 396
    • 0030445615 scopus 로고    scopus 로고
    • Purification and properties of a starch granule-degrading a-amylase from potato tubers
    • Witt, W. and Sauter, J. J., 1996. Purification and properties of a starch granule-degrading a-amylase from potato tubers. J. Exp. Bot. 47: 1789-1795.
    • (1996) J. Exp. Bot. , vol.47 , pp. 1789-1795
    • Witt, W.1    Sauter, J.J.2
  • 397
    • 0029197703 scopus 로고
    • Binding of endoamylase to native starch grains from poplar wood
    • Witt, W., Buchholz, A., and Sauter, J. J., 1995. Binding of endoamylase to native starch grains from poplar wood. J. Exp. Bot. 46: 1761-1769.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1761-1769
    • Witt, W.1    Buchholz, A.2    Sauter, J.J.3
  • 398
    • 0032161159 scopus 로고    scopus 로고
    • Pride and prejudice: The discovery of the primer for glycogen synthesis
    • Whelan W. J., 1998. Pride and prejudice: the discovery of the primer for glycogen synthesis. Protein Sci. 7: 2038-2041.
    • (1998) Protein Sci. , vol.7 , pp. 2038-2041
    • Whelan, W.J.1
  • 399
    • 0008566250 scopus 로고
    • Action of salivary α-amylase on amylopectin and glycogen
    • Whelan, W. J. and Roberts, P. J. P., 1952. Action of salivary α-amylase on amylopectin and glycogen. Nature 170: 748-749.
    • (1952) Nature , vol.170 , pp. 748-749
    • Whelan, W.J.1    Roberts, P.J.P.2
  • 400
    • 0001166725 scopus 로고
    • Fine structure of starch granule sections
    • Whistler, R. L. and Turner, E. S., 1955. Fine structure of starch granule sections. J. Polymer Sci. 18: 153-156.
    • (1955) J. Polymer Sci. , vol.18 , pp. 153-156
    • Whistler, R.L.1    Turner, E.S.2
  • 401
    • 33751386118 scopus 로고
    • Influence of competitive adsorbtion of a lysopalmitoylphosphatidylcholine on the functional properites of puroindoline, a lipidbinding protein isolated from wheat flour
    • Wilde, P. J., Clark, D. C., and Didier, M. 1993. Influence of competitive adsorbtion of a lysopalmitoylphosphatidylcholine on the functional properites of puroindoline, a lipidbinding protein isolated from wheat flour. J. Agric. Food Chem. 41: 1570-1576.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1570-1576
    • Wilde, P.J.1    Clark, D.C.2    Didier, M.3
  • 402
    • 0008530430 scopus 로고
    • Conversion of active and inactive debranching enzymes in rice seeds
    • Yamamada, J., 1981a. Conversion of active and inactive debranching enzymes in rice seeds. Agric. Biol. Chem. 45: 747-750.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 747-750
    • Yamamada, J.1
  • 403
    • 0008567441 scopus 로고
    • Inactive debranching enzyme in rice seeds and its activation
    • Yamamada, J. 1981b. Inactive debranching enzyme in rice seeds and its activation. Carbohydr. Res. 90: 153-157.
    • (1981) Carbohydr. Res. , vol.90 , pp. 153-157
    • Yamamada, J.1
  • 404
    • 0031239046 scopus 로고    scopus 로고
    • Large-scale EST sequencing in rice
    • Yamamoto, K. and Sasaki, T., 1997. Large-scale EST sequencing in rice. Plant Mol. Biol. 35: 135-144.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 135-144
    • Yamamoto, K.1    Sasaki, T.2
  • 405
    • 0019050301 scopus 로고
    • Purification and characterization of limit dextrinase from Pisum sativum L
    • Yellowlees, D. 1980. Purification and characterization of limit dextrinase from Pisum sativum L. Carbohydr. Res. 83: 109-118.
    • (1980) Carbohydr. Res. , vol.83 , pp. 109-118
    • Yellowlees, D.1
  • 406
    • 0027499832 scopus 로고
    • Alpha-1-4-glucan lyase, a new class of starch-glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds
    • Yu, S., Kenne, L., and Pedersen, M., 1993. Alpha-1-4-glucan lyase, a new class of starch-glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds. Biochim. Biophys. Acta 1156: 313-320.
    • (1993) Biochim. Biophys. Acta , vol.1156 , pp. 313-320
    • Yu, S.1    Kenne, L.2    Pedersen, M.3
  • 407
    • 0027492818 scopus 로고
    • Alpha-1-4-glucan lyase, a new class of starch-glycogen-degrading enzyme. II. Subcellular localization and partial amino acid sequence
    • Yu, S. and Pedersen, M., 1993. Alpha-1-4-glucan lyase, a new class of starch-glycogen-degrading enzyme. II. Subcellular localization and partial amino acid sequence. Planta 191: 137-142.
    • (1993) Planta , vol.191 , pp. 137-142
    • Yu, S.1    Pedersen, M.2
  • 408
    • 0028989882 scopus 로고
    • Alpha-1-4-glucan lyase, a new class of starch-glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism
    • Yu, S., Ahmad, T., Kenne, L., and Pedersen, M., 1995. Alpha-1-4-glucan lyase, a new class of starch-glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism. Biochim. Biophys. Acta 1244: 1-9.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 1-9
    • Yu, S.1    Ahmad, T.2    Kenne, L.3    Pedersen, M.4
  • 409
    • 0030965769 scopus 로고    scopus 로고
    • Efficient purification and partial amino acid sequencing of two α-1,4-glucan lyases from fungi
    • Yu, S., Christensen, T. M. I. E., Kragh, K., Bojsen, K., and Marcussen, J., 1997. Efficient purification and partial amino acid sequencing of two α-1,4-glucan lyases from fungi. Biochim. Biophys. Acta 1339: 311-320.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 311-320
    • Yu, S.1    Christensen, T.M.I.E.2    Kragh, K.3    Bojsen, K.4    Marcussen, J.5
  • 410
    • 0001826232 scopus 로고
    • Fine structure of amylopectin in relation to gelatinization and retrogradation behaviour of maize starches from three wx-containing genotypes in two inbred lines
    • Yuan, R. C., Thompson, D. B., and Boyer, C. D., 1993. Fine structure of amylopectin in relation to gelatinization and retrogradation behaviour of maize starches from three wx-containing genotypes in two inbred lines. Cereal Chem. 70: 81-89.
    • (1993) Cereal Chem. , vol.70 , pp. 81-89
    • Yuan, R.C.1    Thompson, D.B.2    Boyer, C.D.3
  • 411
    • 0032192047 scopus 로고    scopus 로고
    • A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen
    • Zeeman, S. C., Umemoto, T., Lue, W-L., Au-Yeung, P., Martin, C., Smith, A. M., and Chen, J., 1998a. A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen. Plant Cell 10: 1699-1711.
    • (1998) Plant Cell , vol.10 , pp. 1699-1711
    • Zeeman, S.C.1    Umemoto, T.2    Lue, W.-L.3    Au-Yeung, P.4    Martin, C.5    Smith, A.M.6    Chen, J.7
  • 412
    • 0032143523 scopus 로고    scopus 로고
    • A starch-accumulating mutant of Arabidopsis thaliana deficient in a starch-hydrolyzing enzyme
    • Zeeman, S. C. Northrop, F., Smith, A. M., and ap Rees, T., 1998b. A starch-accumulating mutant of Arabidopsis thaliana deficient in a starch-hydrolyzing enzyme. Plant J. 15: 357-365.
    • (1998) Plant J. , vol.15 , pp. 357-365
    • Zeeman, S.C.1    Northrop, F.2    Smith, A.M.3    Ap Rees, T.4
  • 413
    • 0028002663 scopus 로고
    • Development of β-amylase activity and polymorphism in wheat seedling shoot
    • Ziegler, P., Daussant, J., and Loos, K., 1994. Development of β-amylase activity and polymorphism in wheat seedling shoot. J. Exp. Bot. 45: 1147-1155.
    • (1994) J. Exp. Bot. , vol.45 , pp. 1147-1155
    • Ziegler, P.1    Daussant, J.2    Loos, K.3
  • 414
    • 0001823674 scopus 로고
    • Molecules to granules: A comprehensive review
    • Zobel, H. F., 1988. Molecules to granules: a comprehensive review. Starch/Stärke 40: 1-7.
    • (1988) Starch/Stärke , vol.40 , pp. 1-7
    • Zobel, H.F.1
  • 415
    • 0027346055 scopus 로고
    • Analysis of the expression of potato uridinediphosphate-glucose pyrophosphorylase and its inhibition by antisense RNA
    • Zrenner, R., Willmitzer, L., and Sonnewald U., 1993. Analysis of the expression of potato uridinediphosphate-glucose pyrophosphorylase and its inhibition by antisense RNA. Planta 190: 247-252.
    • (1993) Planta , vol.190 , pp. 247-252
    • Zrenner, R.1    Willmitzer, L.2    Sonnewald, U.3
  • 416
    • 0029107792 scopus 로고
    • Evidence of the crucial role of sucrose synthase for sink strength using transgenic potato plants (Solanum tuberosum L.)
    • Zrenner, R., Salanoubat, M., Willmitzer, L., and Sonnewald, U., 1995. Evidence of the crucial role of sucrose synthase for sink strength using transgenic potato plants (Solanum tuberosum L.). Plant J. 7: 97-107.
    • (1995) Plant J. , vol.7 , pp. 97-107
    • Zrenner, R.1    Salanoubat, M.2    Willmitzer, L.3    Sonnewald, U.4
  • 417
    • 0000287416 scopus 로고
    • Hormonal regulation of α-amylase gene transcription in wild oat (Avena fatua L.) aleurone protoplasts
    • Zwar, J. A. and Hooley, R., 1986. Hormonal regulation of α-amylase gene transcription in wild oat (Avena fatua L.) aleurone protoplasts. Plant Physiol. 80: 459-463.
    • (1986) Plant Physiol. , vol.80 , pp. 459-463
    • Zwar, J.A.1    Hooley, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.