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Volumn 18, Issue 4, 1999, Pages 489-525

Sucrose-starch conversion in heterotrophic tissues of plants

Author keywords

Adenylate translocator; ADPGlc; ADPGlc pyrophosphorylase; Amyloplast; Cyclic turnover of starch; Phosphate translocator; Source sink; Starch biosynthesis; Sucrose synthase; Sucrose starch transition; Transgenic plants; UDPGlc pyrophosphorylase

Indexed keywords

BIOSYNTHESIS; CARBOHYDRATE METABOLISM; COMPLEMENTARY DNA; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; HEXOKINASE; PLANT METABOLISM; PYROPHOSPHATE; STARCH SYNTHASE; STARCH; SUCROSE SYNTHASE; SUCROSE; URIDINE 5' DIPHOSPHATE; URIDINE TRIPHOSPHATE GLUCOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; URIDINE TRIPHOSPHATE;

EID: 0032772985     PISSN: 07352689     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0735-2689(99)00381-0     Document Type: Review
Times cited : (32)

References (216)
  • 1
    • 0007860425 scopus 로고
    • Reminiscences, collaborations and reflections
    • Akazawa, T. 1994. Reminiscences, collaborations and reflections. Photosynth. Res. 39: 93-113.
    • (1994) Photosynth. Res. , vol.39 , pp. 93-113
    • Akazawa, T.1
  • 2
    • 0344294331 scopus 로고
    • Sucrose-starch transition in plant cells
    • Pontis, H. G., Salerno, G. L., Echeverria, E. J., Eds., American Society of Plant Physiologists
    • Akazawa, T., Lin, C.-H., Lin, J.-H., and Smith, N. 1995. Sucrose-starch transition in plant cells. In: International Symposium on Sucrose Metabolism, Pontis, H. G., Salerno, G. L., Echeverria, E. J., Eds., American Society of Plant Physiologists, pp. 115-127.
    • (1995) International Symposium on Sucrose Metabolism , pp. 115-127
    • Akazawa, T.1    Lin, C.-H.2    Lin, J.-H.3    Smith, N.4
  • 3
    • 0346163660 scopus 로고
    • Adenylate-translocator and starch biosynthesis in plastids
    • Huang, A. H. C. and Taiz, L., Eds., The American Society of Plant Physiologists
    • Akazawa, T., Pozueta-Romero, J., and Ardila, F. 1991. Adenylate-translocator and starch biosynthesis in plastids. In: Molecular Approaches to Compartmentation and Metabolic Regulation, Huang, A. H. C. and Taiz, L., Eds., The American Society of Plant Physiologists, pp. 74-85
    • (1991) Molecular Approaches to Compartmentation and Metabolic Regulation , pp. 74-85
    • Akazawa, T.1    Pozueta-Romero, J.2    Ardila, F.3
  • 4
    • 0013118036 scopus 로고
    • Preparation and characterization of envelope membranes from nongreen plastids
    • Alban, C., Joyard, J., and Douce, R. 1988. Preparation and characterization of envelope membranes from nongreen plastids. Plant Physiol. 88: 709-717.
    • (1988) Plant Physiol. , vol.88 , pp. 709-717
    • Alban, C.1    Joyard, J.2    Douce, R.3
  • 6
    • 0024978421 scopus 로고
    • The encoded primary sequence of a rice seed ADP-glucose pyrophosphorylase subunit and its homology to the bacterial enzyme
    • Anderson, J. M., Hnilo, J., Larsen, R., Okita, T. W., Morrell, M., and Preiss, J. 1989. The encoded primary sequence of a rice seed ADP-glucose pyrophosphorylase subunit and its homology to the bacterial enzyme. J. Biol. Chem. 264: 12238-12242.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12238-12242
    • Anderson, J.M.1    Hnilo, J.2    Larsen, R.3    Okita, T.W.4    Morrell, M.5    Preiss, J.6
  • 7
    • 0030988807 scopus 로고    scopus 로고
    • Developmental changes of enzymes involved in conversion of sucrose to hexose-phosphate during early tuberisation of potato
    • Appeldoorn, N. J. K., de Bruijin, S. M., Kout-Gronsveld, E. A. M., Visser, R. G. F., Urengdenhil, D., and van der Plas, L. H. W. 1997. Developmental changes of enzymes involved in conversion of sucrose to hexose-phosphate during early tuberisation of potato. Planta 202: 220-226.
    • (1997) Planta , vol.202 , pp. 220-226
    • Appeldoorn, N.J.K.1    De Bruijin, S.M.2    Kout-Gronsveld, E.A.M.3    Visser, R.G.F.4    Urengdenhil, D.5    Van Der Plas, L.H.W.6
  • 8
    • 84940971054 scopus 로고
    • Hexose phosphate metabolism by nonphotosynthetic tissues of higher plants
    • Preiss, J., Ed., Academic Press, New York
    • ap Rees, T. 1988. Hexose phosphate metabolism by nonphotosynthetic tissues of higher plants. In: The Biochemistry of Plants, Preiss, J., Ed., Vol. 14, Academic Press, New York. pp. 1-33.
    • (1988) The Biochemistry of Plants , vol.14 , pp. 1-33
    • Ap Rees, T.1
  • 9
    • 0002128892 scopus 로고
    • Synthesis of storage starch
    • Pollack, C. J., Farrar, J. F., and Gordon, A. J., Eds., Bios Scientific Publishers, Oxford, UK
    • ap Rees, T. 1992. Synthesis of storage starch. In: Carbon Partitioning within and between Organisms, Pollack, C. J., Farrar, J. F., and Gordon, A. J., Eds., Bios Scientific Publishers, Oxford, UK. pp. 115-131.
    • (1992) Carbon Partitioning Within and between Organisms , pp. 115-131
    • Ap Rees, T.1
  • 10
    • 0002615458 scopus 로고
    • Where do plants make ADP-glc?
    • Pontis, H. G., Salerno, G. L., and Echeverria, E. J., Eds. American Society of Plant Physiologists
    • ap Rees, T. 1995. Where do plants make ADP-glc? In: International Symposium On Sucrose Metabolism. Pontis, H. G., Salerno, G. L., and Echeverria, E. J., Eds. American Society of Plant Physiologists, pp. 143-155.
    • (1995) International Symposium on Sucrose Metabolism , pp. 143-155
    • Ap Rees, T.1
  • 11
    • 0000108355 scopus 로고
    • Carbohydrate metabolism in developing potatoes
    • ap Rees, T. and Morrell, S. 1990. Carbohydrate metabolism in developing potatoes. Am. Potato J. 67: 835-847.
    • (1990) Am. Potato J. , vol.67 , pp. 835-847
    • Ap Rees, T.1    Morrell, S.2
  • 12
    • 0345588701 scopus 로고
    • Adenylate uptake by proplastids from cultured cells of tobacco (Nicotiana tabacum L. cv. BA2) indicates that an adenylate translocator is present in all types of plastids
    • Ardila, F., Pozueta-Romero, J., and Akazawa, T. 1993. Adenylate uptake by proplastids from cultured cells of tobacco (Nicotiana tabacum L. cv. BA2) indicates that an adenylate translocator is present in all types of plastids. Plant Cell Physiol. 34: 237-242.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 237-242
    • Ardila, F.1    Pozueta-Romero, J.2    Akazawa, T.3
  • 13
    • 0001357053 scopus 로고
    • Photosynthesis by isolated chloroplasts
    • Arnon, D. I., Allen, M. B., and Whatley, F. R. 1954. Photosynthesis by isolated chloroplasts. Nature 174: 394-396.
    • (1954) Nature , vol.174 , pp. 394-396
    • Arnon, D.I.1    Allen, M.B.2    Whatley, F.R.3
  • 14
    • 0002050897 scopus 로고    scopus 로고
    • Carbohydrate metabolism: Storage carbohydrates
    • Dennis, D. and Dey, P. M., Eds. Academic Press
    • Avigad, G. and Dey, P. M. 1997. Carbohydrate metabolism: storage carbohydrates. In: Plant Biochemistry, Dennis, D. and Dey, P. M., Eds. Academic Press, pp. 143-204.
    • (1997) Plant Biochemistry , pp. 143-204
    • Avigad, G.1    Dey, P.M.2
  • 15
    • 0000915901 scopus 로고
    • Cloning and characterization of the brittle-2 gene of maize
    • Bae, J. M., Giroux, M., and Hannah, J. C., 1990. Cloning and characterization 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, J.C.3
  • 17
    • 0028356127 scopus 로고
    • Glucose- and ADPGlc-dependent starch synthesis in isolated cauliflower-bud amyloplasts. Analysis of the interaction of various potential precursors
    • Batz, O., Maass, U., Henrichs, G., Scheibe, R., and Neuhaus, H. E. 1994. Glucose- and ADPGlc-dependent starch synthesis in isolated cauliflower-bud amyloplasts. Analysis of the interaction of various potential precursors. Biochim. Biophys. Acta 1200: 148-154.
    • (1994) Biochim. Biophys. Acta , vol.1200 , pp. 148-154
    • Batz, O.1    Maass, U.2    Henrichs, G.3    Scheibe, R.4    Neuhaus, H.E.5
  • 18
    • 0029170307 scopus 로고
    • Purification of chloroplasts from fruits of green pepper (Capsicum annuum L.) and characterization of starch synthesis. Evidence for a functional chloroplastic hexose-phosphate translocator
    • Batz, O., Scheibe, R., and Neuhaus, H. E. 1995. Purification of chloroplasts from fruits of green pepper (Capsicum annuum L.) and characterization of starch synthesis. Evidence for a functional chloroplastic hexose-phosphate translocator. Planta 196: 50-57.
    • (1995) Planta , vol.196 , pp. 50-57
    • Batz, O.1    Scheibe, R.2    Neuhaus, H.E.3
  • 19
    • 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
  • 20
    • 0021036494 scopus 로고
    • Preparation and characterization of membranes fractions enriched in outer and inner membranes from spinach chloroplasts I. Electrophoretic and immunochemical analyses
    • Block, M. A., Dorne, A-J., Joyard, J., and Douce, R. 1983a. Preparation and characterization of membranes fractions enriched in outer and inner membranes from spinach chloroplasts I. Electrophoretic and immunochemical analyses. J. Biol. Chem. 258: 13273-13280.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13273-13280
    • Block, M.A.1    Dorne, A.-J.2    Joyard, J.3    Douce, R.4
  • 21
    • 0021100246 scopus 로고
    • Preparation and characterization of membranes fractions enriched in outer and inner membranes from spinach chloroplasts II. Biochemical characterization
    • Block, M. A., Dorne, A-J., Joyard, J., and Douce, R. 1983b. Preparation and characterization of membranes fractions enriched in outer and inner membranes from spinach chloroplasts II. Biochemical characterization. J. Biol. Chem. 258: 13281-13286.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13281-13286
    • Block, M.A.1    Dorne, A.-J.2    Joyard, J.3    Douce, R.4
  • 22
    • 0001325327 scopus 로고
    • Specific transport of inorganic phosphate, glucose-6-phosphate, dihydroxy-acetone phosphate and 3-phosphoglycerate into amyloplasts from pea roots
    • Borchert, S., Grosse, H., and Heldt, H. W. 1989. Specific transport of inorganic phosphate, glucose-6-phosphate, dihydroxy-acetone phosphate and 3-phosphoglycerate into amyloplasts from pea roots. FEBS Lett. 253: 183-186.
    • (1989) FEBS Lett. , vol.253 , pp. 183-186
    • Borchert, S.1    Grosse, H.2    Heldt, H.W.3
  • 23
    • 0001063776 scopus 로고
    • Studies of the enzymic capacities and transport properties of pea root plastids
    • Borchert, S., Harborth, J., Schünemann, D., Hoferichter, P., and Heldt, H. W. 1993. Studies of the enzymic capacities and transport properties of pea root plastids. Plant Physiol. 101: 303-312.
    • (1993) Plant Physiol. , vol.101 , pp. 303-312
    • Borchert, S.1    Harborth, J.2    Schünemann, D.3    Hoferichter, P.4    Heldt, H.W.5
  • 24
    • 0000083779 scopus 로고    scopus 로고
    • Effect of expression of UDP-glucose pyrophosphorylase ribozyme and antisense RNAs on the enzyme activity and carbohydrate composition of field-grown transgenic potato plants
    • Borovkov, A., McClean, P. E., Sowokinos, J. R., Ruud, S. H., and Secor, G. A. 1996. Effect of expression of UDP-glucose pyrophosphorylase ribozyme and antisense RNAs on the enzyme activity and carbohydrate composition of field-grown transgenic potato plants. J. Plant Physiol. 147: 644-652.
    • (1996) J. Plant Physiol. , vol.147 , pp. 644-652
    • Borovkov, A.1    McClean, P.E.2    Sowokinos, J.R.3    Ruud, S.H.4    Secor, G.A.5
  • 25
    • 0001552084 scopus 로고
    • Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L.
    • Bowsher, C. G., Hucklesby, D. P., and Emes, M. J. 1989. Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L. Planta 177: 359-366
    • (1989) Planta , vol.177 , pp. 359-366
    • Bowsher, C.G.1    Hucklesby, D.P.2    Emes, M.J.3
  • 27
    • 0030485242 scopus 로고    scopus 로고
    • BT1, a protein critical for in vivo starch accumulation in maize endosperm, is not detected in maize endosperm suspension cultures
    • Cao, H. and Shannon, J. C. 1996. BT1, a protein critical for in vivo starch accumulation in maize endosperm, is not detected in maize endosperm suspension cultures. Physiol. Plant. 97: 665-673.
    • (1996) Physiol. Plant. , vol.97 , pp. 665-673
    • Cao, H.1    Shannon, J.C.2
  • 28
    • 0030993286 scopus 로고    scopus 로고
    • BT1, a possible adenylate translocator, is developmentally expressed in maize endosperm but not detected in starchy tissues from several other species
    • Cao, H. and Shannon J. C. 1997. BT1, a possible adenylate translocator, is developmentally expressed in maize endosperm but not detected in starchy tissues from several other species. Physiol. Plant. 100: 400-406.
    • (1997) Physiol. Plant. , vol.100 , pp. 400-406
    • Cao, H.1    Shannon, J.C.2
  • 29
    • 0029186042 scopus 로고
    • Bt1, 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. Bt1, 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
  • 30
    • 0002135275 scopus 로고
    • Alterations in growth, photosynthesis, and respiration in a starchless mutant of Arabidopsis thaliana (L.) deficient in chloroplast phosphoglucomutase activity
    • Caspar, T., Huber, S. C., and Somerville, C. 1985. Alterations in growth, photosynthesis, and respiration in a starchless mutant of Arabidopsis thaliana (L.) deficient in chloroplast phosphoglucomutase activity. Plant Physiol. 79: 11-17.
    • (1985) Plant Physiol. , vol.79 , pp. 11-17
    • Caspar, T.1    Huber, S.C.2    Somerville, C.3
  • 31
    • 0024958949 scopus 로고
    • Gravitropism in a starchless mutant of Arabidopsis
    • Caspar, T. and Pickard, B. G. 1989. Gravitropism in a starchless mutant of Arabidopsis. Planta 177: 185-197.
    • (1989) Planta , vol.177 , pp. 185-197
    • Caspar, T.1    Pickard, B.G.2
  • 32
    • 0344294326 scopus 로고
    • Role of sucrose synthase in sucrose-starch conversion in rice grains
    • Chen, H.-H., Sung, H.-Y., and Su, J. C. 1981. Role of sucrose synthase in sucrose-starch conversion in rice grains. Proc. Natl. Sci. Counc. Part B. 5: 165-170.
    • (1981) Proc. Natl. Sci. Counc. Part B. , vol.5 , pp. 165-170
    • Chen, H.-H.1    Sung, H.-Y.2    Su, J.C.3
  • 33
    • 0031759987 scopus 로고    scopus 로고
    • ADP-Glucose pyrophosphorylase is localized to both the cytoplasm and plastids in developing pericarp of tomato fruit
    • Chen, B.-Y., Wang, Y., and Janes. H.-W. 1998. ADP-Glucose pyrophosphorylase is localized to both the cytoplasm and plastids in developing pericarp of tomato fruit. Plant Physiol. 116: 101-106.
    • (1998) Plant Physiol. , vol.116 , pp. 101-106
    • Chen, B.-Y.1    Wang, Y.2    Janes, H.-W.3
  • 34
    • 0017034186 scopus 로고
    • The enzymatic deficiency conditionated by the shrunken-1 mutation in maize
    • Chourey, P. S. and Nelson, O. E. 1976. The enzymatic deficiency conditionated by the shrunken-1 mutation in maize. Biochem. Genet. 14: 1041-1055.
    • (1976) Biochem. Genet. , vol.14 , pp. 1041-1055
    • Chourey, P.S.1    Nelson, O.E.2
  • 35
    • 0028070484 scopus 로고
    • Epistatic interaction and functional compensation between the two tissue- and cell-specific sucrose synthase genes in maize
    • Chourey, P. S. and Taliercio, E. W. 1994. Epistatic interaction and functional compensation between the two tissue- and cell-specific sucrose synthase genes in maize. Proc. Natl. Acad. Sci. 91: 7917-7921.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 7917-7921
    • Chourey, P.S.1    Taliercio, E.W.2
  • 36
    • 0019412749 scopus 로고
    • Separation and characterization of inner and outer envelope membranes of pea chloroplasts
    • Cline, K., Andrews, J. Mersey, B., Newcomb, E. N., and Keegstra, K. 1982. Separation and characterization of inner and outer envelope membranes of pea chloroplasts. Proc. Natl. Acad. Sci. 78: 3595-3599.
    • (1982) Proc. Natl. Acad. Sci. , vol.78 , pp. 3595-3599
    • Cline, K.1    Andrews, J.2    Mersey, B.3    Newcomb, E.N.4    Keegstra, K.5
  • 37
    • 0014196738 scopus 로고
    • Oxygen evolution by isolated chloroplasts with carbon dioxide as the hydrogen acceptor. A requirement for orthophosphate or pyrophosphate
    • Cockburn, W., Baldry, C. W., and Walker, D. A. 1967. Oxygen evolution by isolated chloroplasts with carbon dioxide as the hydrogen acceptor. A requirement for orthophosphate or pyrophosphate . Biochim. Biophys. Acta 131: 594-596.
    • (1967) Biochim. Biophys. Acta , vol.131 , pp. 594-596
    • Cockburn, W.1    Baldry, C.W.2    Walker, D.A.3
  • 38
    • 0028035606 scopus 로고
    • Metabolism of glucose monophosphates by leucoplasts and amyloplasts from soybean cultures
    • Coates, S. A. and ap Rees, T. 1994. Metabolism of glucose monophosphates by leucoplasts and amyloplasts from soybean cultures. Phytochemistry 244: 881-883.
    • (1994) Phytochemistry , vol.244 , pp. 881-883
    • Coates, S.A.1    Ap Rees, T.2
  • 39
    • 84994932061 scopus 로고
    • Relationship between pyrophosphate: Fructose-6-phosphate, 1-phosphotransferase, sucrose breakdown, and respiration
    • Dancer, J. E. and ap Rees, T. 1989. Relationship between pyrophosphate: fructose-6-phosphate, 1-phosphotransferase, sucrose breakdown, and respiration. J. Plant Physiol. 135: 197-206.
    • (1989) J. Plant Physiol. , vol.135 , pp. 197-206
    • Dancer, J.E.1    Ap Rees, T.2
  • 40
    • 0001154667 scopus 로고
    • Cytosolic cycles regulate the accumulation of sucrose in heterotrophic cell-suspension cultures of Chenopodium rubrum
    • Dancer, J. W., Hatzfeld, W. D., and Stitt, M. 1990. Cytosolic cycles regulate the accumulation of sucrose in heterotrophic cell-suspension cultures of Chenopodium rubrum. Planta 182: 223-231.
    • (1990) Planta , vol.182 , pp. 223-231
    • Dancer, J.W.1    Hatzfeld, W.D.2    Stitt, M.3
  • 41
    • 0038382401 scopus 로고
    • Mechanism of glucose transfer from sucrose into the starch granule of sweet corn
    • de Fekete, M. A. R. and Cardini, C. E. 1964. Mechanism of glucose transfer from sucrose into the starch granule of sweet corn. Arch. Biochem. Biophys. 104: 173-184.
    • (1964) Arch. Biochem. Biophys. , vol.104 , pp. 173-184
    • De Fekete, M.A.R.1    Cardini, C.E.2
  • 42
    • 0030267532 scopus 로고    scopus 로고
    • The major form of ADP-glucose pyrophosphorylase in maize (Zea mays L.) endosperm is extra-plastidial
    • Denyer, K., Dunlap, F., Thuørbjornsen, T., Keeling, P., and Smith, A. M. 1996. The major form of ADP-glucose pyrophosphorylase in maize (Zea mays L.) endosperm is extra-plastidial. Plant Physiol. 112: 779-785.
    • (1996) Plant Physiol. , vol.112 , pp. 779-785
    • Denyer, K.1    Dunlap, F.2    Thuørbjornsen, T.3    Keeling, P.4    Smith, A.M.5
  • 43
    • 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. 1995. 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
  • 44
    • 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 Physiol. 44: 1058-1062.
    • (1969) Plant Physiol. , vol.44 , pp. 1058-1062
    • Dickinson, D.B.1    Preiss, J.2
  • 45
    • 0017225005 scopus 로고
    • Isolation and characterization of mutations affecting UDPG pyrophosphorylase activity in Dictyostelium discoideum
    • Dimond, R. L., Farnsworth, P. A., and Loomis, W. F. 1976. Isolation and characterization of mutations affecting UDPG pyrophosphorylase activity in Dictyostelium discoideum. Dev. Biol. 50: 169-181.
    • (1976) Dev. Biol. , vol.50 , pp. 169-181
    • Dimond, R.L.1    Farnsworth, P.A.2    Loomis, W.F.3
  • 46
    • 0001360382 scopus 로고
    • Sugar metabolism in developing kernels of starch-deficient endosperm mutants of maize
    • Doehlert, D. C. and Kuo, T. M. 1990. Sugar metabolism in developing kernels of starch-deficient endosperm mutants of maize. Plant Physiol. 92: 990-994.
    • (1990) Plant Physiol. , vol.92 , pp. 990-994
    • Doehlert, D.C.1    Kuo, T.M.2
  • 47
    • 0015821014 scopus 로고
    • Isolation and properties of the envelope of spinach chloroplasts
    • Douce, R., Holz, R. B., and Benson, A. A. 1973. Isolation and properties of the envelope of spinach chloroplasts. J. Biol. Chem. 248: 7215-7222.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7215-7222
    • Douce, R.1    Holz, R.B.2    Benson, A.A.3
  • 48
    • 0025224152 scopus 로고
    • Biochemistry and function of the plastid envelope
    • Douce, R. and Joyard, J. 1990. Biochemistry and function of the plastid envelope. Annu. Rev. Cell Biol. 6: 173-216.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 173-216
    • Douce, R.1    Joyard, J.2
  • 49
    • 0001036645 scopus 로고
    • A comparison of two sucrose synthase isozymes from normal and shrunken 1 maize
    • Echt, C. S. and Chourey, P. S. 1985. A comparison of two sucrose synthase isozymes from normal and shrunken 1 maize. Plant Physiol. 79: 530-536.
    • (1985) Plant Physiol. , vol.79 , pp. 530-536
    • Echt, C.S.1    Chourey, P.S.2
  • 50
    • 0028825708 scopus 로고
    • Characterization of sucrose synthase from rice grains for the enzymic synthesis of UDP and TDP glucose
    • Elling, L. and Kula, M.-R. 1995. Characterization of sucrose synthase from rice grains for the enzymic synthesis of UDP and TDP glucose. Enz. Microb. Tech. 17: 929-934.
    • (1995) Enz. Microb. Tech. , vol.17 , pp. 929-934
    • Elling, L.1    Kula, M.-R.2
  • 51
    • 0031464334 scopus 로고    scopus 로고
    • Metabolite transport in non-photosynthetic plastids
    • Emes, M. and Neuhaus, H. E. 1997. Metabolite transport in non-photosynthetic plastids. J. Exp. Bot. 48: 1995-2005.
    • (1997) J. Exp. Bot. , vol.48 , pp. 1995-2005
    • Emes, M.1    Neuhaus, H.E.2
  • 52
    • 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
  • 53
    • 0001261938 scopus 로고
    • Enzymic synthesis of adenosine diphosphate glucose from glucose 1-phosphate and adenosine triphosphate
    • Espada, J. 1962. Enzymic synthesis of adenosine diphosphate glucose from glucose 1-phosphate and adenosine triphosphate. J. Biol. Chem. 237: 3577-3581.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3577-3581
    • Espada, J.1
  • 54
    • 0002722074 scopus 로고
    • Monomeric and oligomeric sugars and sugar derivatives - Occurrence, metabolism, function
    • Loewus, F. A. and Tanner, W., Eds., Springer, Berlin
    • Feingold, D. S. 1982. Monomeric and oligomeric sugars and sugar derivatives - occurrence, metabolism, function. In: Encyclopedia of Plant Physiology, New Series. Vol. 13A, Loewus, F. A. and Tanner, W., Eds., Springer, Berlin, pp. 3-76.
    • (1982) Encyclopedia of Plant Physiology, New Series , vol.13 A , pp. 3-76
    • Feingold, D.S.1
  • 55
    • 0000509336 scopus 로고
    • Sugar transformations in plants
    • Stumpf, P. K. and Conn, E. E. Eds., Academic Press, New York
    • Feingold, D. S. and Avigad, G. 1980. Sugar transformations in plants. In: The Biochemistry of Plants. Vol. 3, Stumpf, P. K. and Conn, E. E. Eds., Academic Press, New York, pp. 101-170.
    • (1980) The Biochemistry of Plants , vol.3 , pp. 101-170
    • Feingold, D.S.1    Avigad, G.2
  • 56
    • 0031105611 scopus 로고    scopus 로고
    • A new class of plastidic phosphate translocators: A putative link between primary and secondary metabolism by the phosphoenol-pyruvate/phosphate antiporter
    • Fischer, K, Kammerer, B, Gutensohn, M., Arbinger, B., Weber, A., Häusler, R. E., and Flügge, U.-I. 1997. A new class of plastidic phosphate translocators: a putative link between primary and secondary metabolism by the phosphoenol-pyruvate/phosphate antiporter. Plant Cell 9: 453-462.
    • (1997) Plant Cell , vol.9 , pp. 453-462
    • Fischer, K.1    Kammerer, B.2    Gutensohn, M.3    Arbinger, B.4    Weber, A.5    Häusler, R.E.6    Flügge, U.-I.7
  • 57
    • 0024574552 scopus 로고
    • The triosephosphate-3-phosphoglycerate-phosphate trans-locator from spinach chloroplasts: Nucleotide sequence of a full length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts
    • Flügge, U. I., Fischer, K., Gross, A., Sebald, W., Lottspeich, F., and Eckerskorn, C. 1989. The triosephosphate-3-phosphoglycerate-phosphate trans-locator from spinach chloroplasts: nucleotide sequence of a full length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts. EMBO J. 8: 39-46.
    • (1989) EMBO J. , vol.8 , pp. 39-46
    • Flügge, U.I.1    Fischer, K.2    Gross, A.3    Sebald, W.4    Lottspeich, F.5    Eckerskorn, C.6
  • 58
    • 0028155460 scopus 로고
    • A rapid method for measuring organelle-specific substrate transport in homogenates from plant tissues
    • Flügge, U. I. and Weber, A. 1994. A rapid method for measuring organelle-specific substrate transport in homogenates from plant tissues. Planta 194: 181-185.
    • (1994) Planta , vol.194 , pp. 181-185
    • Flügge, U.I.1    Weber, A.2
  • 59
    • 0025914006 scopus 로고
    • The major chloroplast envelope polypeptide is the phosphate translocator and not the protein import receptor
    • Flügge, U. I., Weber, A., Fischer, K., Lottspeich, F., Eckerskorn, Waegemann, K., and Soil, J. 1991. The major chloroplast envelope polypeptide is the phosphate translocator and not the protein import receptor. Nature 353.
    • (1991) Nature , pp. 353
    • Flügge, U.I.1    Weber, A.2    Fischer, K.3    Lottspeich, F.4    Eckerskorn5    Waegemann, K.6    Soil, J.7
  • 60
    • 0002606124 scopus 로고
    • Metabolism of glucose 6-phosphate by plastids from developing pea embryos
    • Foster J. M. and Smith, A. M. 1993. Metabolism of glucose 6-phosphate by plastids from developing pea embryos. Planta 190: 17-24.
    • (1993) Planta , vol.190 , pp. 17-24
    • Foster, J.M.1    Smith, A.M.2
  • 61
    • 0001598607 scopus 로고
    • Enzyme sets of glycolysis, gluconeogenesis, and oxidative pentose phosphate pathway are not complete in nongreen highly purified amyloplasts of sycamore (Acer pseudoplatanus L.) cell suspension cultures
    • Frehner, M., Pozueta-Romero, J., and Akazawa, T. 1990. Enzyme sets of glycolysis, gluconeogenesis, and oxidative pentose phosphate pathway are not complete in nongreen highly purified amyloplasts of sycamore (Acer pseudoplatanus L.) cell suspension cultures. Plant Physiol. 94: 538-544.
    • (1990) Plant Physiol. , vol.94 , pp. 538-544
    • Frehner, M.1    Pozueta-Romero, J.2    Akazawa, T.3
  • 62
    • 0027954143 scopus 로고
    • When growing potato tubers are detached from their mother plant there is a rapid inhibition of starch synthesis, involving inhibition of ADP-glucose pyrophosphorylase
    • Geigenberger P., Merlo, L., Reimholz, R., and Stitt, M. 1994. When growing potato tubers are detached from their mother plant there is a rapid inhibition of starch synthesis, involving inhibition of ADP-glucose pyrophosphorylase. Planta 193: 486-493.
    • (1994) Planta , vol.193 , pp. 486-493
    • Geigenberger, P.1    Merlo, L.2    Reimholz, R.3    Stitt, M.4
  • 63
    • 34249922554 scopus 로고
    • A futile cycle of sucrose synthesis and degradation is involved in regulating partitioning between sucrose, starch and respiration in cotyledons of germinating Ricinus communis L. seedlings when phloem transport is inhibited
    • Geigenberger, P. and Stitt, M. 1991. A futile cycle of sucrose synthesis and degradation is involved in regulating partitioning between sucrose, starch and respiration in cotyledons of germinating Ricinus communis L. seedlings when phloem transport is inhibited. Planta 185: 81-90.
    • (1991) Planta , vol.185 , pp. 81-90
    • Geigenberger, P.1    Stitt, M.2
  • 64
    • 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
  • 65
    • 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
  • 66
    • 0031772789 scopus 로고    scopus 로고
    • Maize endosperm ADP-glucose pyrophopsorylase shrunken 2 and brittle 2 subunit interactions
    • Greene, T. W. and Hannah, L. C. 1998. Maize endosperm ADP-glucose pyrophopsorylase shrunken 2 and brittle 2 subunit interactions. Plant Cell 40: 1295-1306
    • (1998) Plant Cell , vol.40 , pp. 1295-1306
    • Greene, T.W.1    Hannah, L.C.2
  • 67
    • 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
  • 68
    • 0000023327 scopus 로고
    • Comparison of the kinetic properties, inhibition, and labelling of the phosphate translocators from maize and spinach mesophyll chloroplasts
    • Gross, A., Brückner, G., Heldt, H. W., and Flügge, U.-I. 1990. Comparison of the kinetic properties, inhibition, and labelling of the phosphate translocators from maize and spinach mesophyll chloroplasts. Planta 180: 262-271.
    • (1990) Planta , vol.180 , pp. 262-271
    • Gross, A.1    Brückner, G.2    Heldt, H.W.3    Flügge, U.-I.4
  • 69
    • 0031416259 scopus 로고    scopus 로고
    • The spatial distribution of sucrose synthase isozymes in barley
    • Guerin, J. and Carbonero, P. 1997. The spatial distribution of sucrose synthase isozymes in barley. Plant Physiol. 114: 55-62.
    • (1997) Plant Physiol. , vol.114 , pp. 55-62
    • Guerin, J.1    Carbonero, P.2
  • 70
    • 0028110601 scopus 로고
    • Transgenic potato plants with strongly decreased expression of pyrophosphate: Fructose-6-phosphate phosphotransferase show no visible phenotype and only minor changes in metabolic fluxes in their tubers
    • Hajirezaei, M., Sonnewald, U., Viola, R., Carlisle, S. Dennis, D., and Stitt, M. 1994. Transgenic potato plants with strongly decreased expression of pyrophosphate: fructose-6-phosphate phosphotransferase show no visible phenotype and only minor changes in metabolic fluxes in their tubers. Planta 192: 16-30.
    • (1994) Planta , vol.192 , pp. 16-30
    • Hajirezaei, M.1    Sonnewald, U.2    Viola, R.3    Carlisle, S.4    Dennis, D.5    Stitt, M.6
  • 71
    • 43949169197 scopus 로고
    • Biotechnological modification of carbohydrates for sweet corn and maize improvement
    • Hannah, L. C., Giroux, M. J., and Boyer, C. 1993. Biotechnological modification of carbohydrates for sweet corn and maize improvement. Sci. Hort. 55: 177-197.
    • (1993) Sci. Hort. , vol.55 , pp. 177-197
    • Hannah, L.C.1    Giroux, M.J.2    Boyer, C.3
  • 72
    • 0017151912 scopus 로고
    • Characterization of ADPG pyrophosphorylase from shrunken 2 and brittle 2 mutants of maize
    • Hannah, L. C. and Nelson, O. E. 1976. Characterization of ADPG pyrophosphorylase from shrunken 2 and brittle 2 mutants of maize. Biochem. Gen. 14: 547-560.
    • (1976) Biochem. Gen. , vol.14 , pp. 547-560
    • Hannah, L.C.1    Nelson, O.E.2
  • 73
    • 0345156624 scopus 로고
    • Polypeptide composition of stroma, internal membranes, and inner membranes of amyloplasts from cultured cells of sycamore (Acer pseudoplatanus)
    • Harinasut, P., Akazawa, T., Zhou, F. G., and Takabe, T. 1988. Polypeptide composition of stroma, internal membranes, and inner membranes of amyloplasts from cultured cells of sycamore (Acer pseudoplatanus). Plant Cell Physiol. 29: 1315-1321.
    • (1988) Plant Cell Physiol. , vol.29 , pp. 1315-1321
    • Harinasut, P.1    Akazawa, T.2    Zhou, F.G.3    Takabe, T.4
  • 74
    • 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
  • 75
    • 0000401603 scopus 로고
    • The chloroplast envelope: Structure, function and role in leaf metabolism
    • Heber U. and Heldt, H. W. 1981. The chloroplast envelope: structure, function and role in leaf metabolism. Annu. Rev. Plant Physiol. 32: 139-168.
    • (1981) Annu. Rev. Plant Physiol. , vol.32 , pp. 139-168
    • Heber, U.1    Heldt, H.W.2
  • 76
    • 0002552053 scopus 로고
    • Adenine nucleotide translocation in spinach chloroplasts
    • Heldt, H. W. 1969. Adenine nucleotide translocation in spinach chloroplasts. FEBS Lett. 178: 15-19.
    • (1969) FEBS Lett. , vol.178 , pp. 15-19
    • Heldt, H.W.1
  • 77
    • 0345156622 scopus 로고
    • Metabolite transport in intact spinach chloroplasts
    • Barber, J., Ed., Elsevier/New Holland Biomedical Press
    • Heldt, H. W. 1976. Metabolite transport in intact spinach chloroplasts. In: The Intact Chloroplasts. Barber, J., Ed., Elsevier/New Holland Biomedical Press, pp. 215-234.
    • (1976) The Intact Chloroplasts , pp. 215-234
    • Heldt, H.W.1
  • 78
    • 0004760296 scopus 로고
    • Diversity of specificity and function of phosphate translocators in various plastids
    • Heldt, H, W., Flügge, U.-I., and Borchert, S. 1991. Diversity of specificity and function of phosphate translocators in various plastids. Plant Physiol. 95: 341-343.
    • (1991) Plant Physiol. , vol.95 , pp. 341-343
    • Heldt, H.W.1    Flügge, U.-I.2    Borchert, S.3
  • 79
    • 49849118107 scopus 로고
    • Metabolite transport across spinach chloroplasts
    • Heldt, H. W. and Rapley, L. 1970a. Metabolite transport across spinach chloroplasts. FEBS Lett. 7: 139.
    • (1970) FEBS Lett. , vol.7 , pp. 139
    • Heldt, H.W.1    Rapley, L.2
  • 80
    • 0001226340 scopus 로고
    • Specific transport of inorganic phosphate, 3-phosphoglycerate and of dicarboxylates across the inner membrane of spinach chloroplasts
    • Heldt, H. W. and Rapley, L. 1970b. Specific transport of inorganic phosphate, 3-phosphoglycerate and of dicarboxylates across the inner membrane of spinach chloroplasts. FEBS Lett. 10: 143-148.
    • (1970) FEBS Lett. , vol.10 , pp. 143-148
    • Heldt, H.W.1    Rapley, L.2
  • 81
    • 0002113153 scopus 로고
    • Evidence that glucose 6-phosphate is imported as the substrate for starch synthesis by 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 plastids of developing pea embryos. Planta 185: 91-96.
    • (1991) Planta , vol.185 , pp. 91-96
    • Hill, L.M.1    Smith, A.M.2
  • 82
    • 0028815182 scopus 로고
    • Coupled movements of glucose 6-phosphate and triose phosphate through the envelopes of plastids from developing embryos of pea (Pisum sativum L.)
    • Hill, L. M. and Smith, A. M. 1995. Coupled movements of glucose 6-phosphate and triose phosphate through the envelopes of plastids from developing embryos of pea (Pisum sativum L.). J. Plant Physiol. 146: 411-417.
    • (1995) J. Plant Physiol. , vol.146 , pp. 411-417
    • Hill, L.M.1    Smith, A.M.2
  • 83
    • 0028086967 scopus 로고
    • Complete nucleotide sequence of the maize (Zea mays L.) sucrose synthase 2 cDNA
    • Huang, X. F., Quoc, B. N., Chourey, P. S., and Yelle, S. 1994. Complete nucleotide sequence of the maize (Zea mays L.) sucrose synthase 2 cDNA. Plant Physiol. 104: 293-294.
    • (1994) Plant Physiol. , vol.104 , pp. 293-294
    • Huang, X.F.1    Quoc, B.N.2    Chourey, P.S.3    Yelle, S.4
  • 84
    • 0001890756 scopus 로고
    • Role of sucrose phosphate synthase in sucrose biosynthesis in ripening bananas and its relationship to the respiratory climacteric
    • Hubbard, H. L., Pharr, D. M., and Huber, S. C. 1990. Role of sucrose phosphate synthase in sucrose biosynthesis in ripening bananas and its relationship to the respiratory climacteric. Plant Physiol. 94: 201-208.
    • (1990) Plant Physiol. , vol.94 , pp. 201-208
    • Hubbard, H.L.1    Pharr, D.M.2    Huber, S.C.3
  • 85
    • 0000786283 scopus 로고
    • A novel sucrose synthase pathway for sucrose degradation in cultured sycamore cells
    • Huber, S. C. and Akazawa, T. 1986. A novel sucrose synthase pathway for sucrose degradation in cultured sycamore cells. Plant Physiol. 81: 1008-1013.
    • (1986) Plant Physiol. , vol.81 , pp. 1008-1013
    • Huber, S.C.1    Akazawa, T.2
  • 86
    • 0030267085 scopus 로고    scopus 로고
    • Phosphorylation of serine-15 of maize leaf sucrose synthase: Occurrence in vivo and possible regulatory significance
    • Huber, S. C., Huber, J. L., Liao, P.-C., Gape, D. A., McMichael, R. W., Chourey, P. S., Hannah, L. C., and Kock, K. 1996. Phosphorylation of serine-15 of maize leaf sucrose synthase: occurrence in vivo and possible regulatory significance. Plant Physiol. 112: 793-820.
    • (1996) Plant Physiol. , vol.112 , pp. 793-820
    • Huber, S.C.1    Huber, J.L.2    Liao, P.-C.3    Gape, D.A.4    McMichael, R.W.5    Chourey, P.S.6    Hannah, L.C.7    Kock, K.8
  • 87
    • 0019502378 scopus 로고
    • The role of futile cycles in the regulation of carbohydrate metabolism
    • Hue, L. 1980. The role of futile cycles in the regulation of carbohydrate metabolism. Adv. Enzymol. 52: 247-291.
    • (1980) Adv. Enzymol. , vol.52 , pp. 247-291
    • Hue, L.1
  • 88
    • 0001172247 scopus 로고
    • The rb-mutation of peas causes structural and regulatory changes in ADPG pyrophosphorylase from developing embryos
    • Hylton, C. and Smith, A. 1992. The rb-mutation of peas causes structural and regulatory changes in ADPG pyrophosphorylase from developing embryos. Plant Physiol. 99: 1626-1634.
    • (1992) Plant Physiol. , vol.99 , pp. 1626-1634
    • Hylton, C.1    Smith, A.2
  • 89
    • 34249839467 scopus 로고
    • Inorganic pyrophosphate content and metabolites in potato and tobacco plants expressing E. coli pyrophosphatase in their cytosol
    • Jelitto, T., Sonnewald, U., Willmitzer, L., Hajirezeai, M., and Stitt, M. 1992. Inorganic pyrophosphate content and metabolites in potato and tobacco plants expressing E. coli pyrophosphatase in their cytosol. Planta 188: 238-244.
    • (1992) Planta , vol.188 , pp. 238-244
    • Jelitto, T.1    Sonnewald, U.2    Willmitzer, L.3    Hajirezeai, M.4    Stitt, M.5
  • 90
    • 0001178122 scopus 로고
    • Enzymic capacities of purified cauliflower bud plastids for lipid biosynthesis and carbohydrate metabolism
    • Journet, E. P. and Douce, R. 1985. Enzymic capacities of purified cauliflower bud plastids for lipid biosynthesis and carbohydrate metabolism. Plant Physiol. 79: 458-467.
    • (1985) Plant Physiol. , vol.79 , pp. 458-467
    • Journet, E.P.1    Douce, R.2
  • 91
    • 0020490258 scopus 로고
    • Characterization of envelope membrane polypeptides from spinach chloroplasts
    • Joyard, J., Grossman, A. R., Bartlett, S. G., Douce, R., and Chua, N-H. 1982. Characterization of envelope membrane polypeptides from spinach chloroplasts. J. Biol. Chem. 257: 1095-1101.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1095-1101
    • Joyard, J.1    Grossman, A.R.2    Bartlett, S.G.3    Douce, R.4    Chua, N.-H.5
  • 92
    • 0031834277 scopus 로고    scopus 로고
    • Molecular characterization 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 characterization of a carbon transporter in plastids from heterotrophic tissues: the glucose 6-phosphate/phosphate antiporter. Plant Cell 10: 105-117
    • (1998) Plant Cell , vol.10 , pp. 105-117
    • Kammerer, B.1    Fischer, K.2    Hilpert, B.3    Schubert, S.4    Gutensohn, M.5    Weber, A.6    Flügge, U.-I.7
  • 93
    • 0028822675 scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants
    • Kampfenkel, K., Möhlmann, T., Batz, O., Montagu, M. V., Inze, D., and Neuhaus, H. E. 1995. Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants. FEBS Lett. 374: 351-355.
    • (1995) FEBS Lett. , vol.374 , pp. 351-355
    • Kampfenkel, K.1    Möhlmann, T.2    Batz, O.3    Montagu, M.V.4    Inze, D.5    Neuhaus, H.E.6
  • 94
    • 0028190781 scopus 로고
    • Starch and fatty acid synthesis in plastids from developing embryos of oilseed rape (Brassica napus L.)
    • Kang, F. and Rawsthorne, S. 1994. Starch and fatty acid synthesis in plastids from developing embryos of oilseed rape (Brassica napus L.). Plant J. 6: 795-805.
    • (1994) Plant J. , vol.6 , pp. 795-805
    • Kang, F.1    Rawsthorne, S.2
  • 95
    • 0344726326 scopus 로고
    • Evidence against triose phosphate transport into amyloplasts of developing wheat and maize grain
    • Boyer, C. D., Shannon, J. C., and Hardison, R. C., Eds., American Society of Plant Physiologists
    • Keeling P. L. 1989. Evidence against triose phosphate transport into amyloplasts of developing wheat and maize grain. In: Physiology, Biochemistry, and Genetics of Nongreen Plastids, Boyer, C. D., Shannon, J. C., and Hardison, R. C., Eds., American Society of Plant Physiologists, pp. 63-78.
    • (1989) Physiology, Biochemistry, and Genetics of Nongreen Plastids , pp. 63-78
    • Keeling, P.L.1
  • 96
    • 34250076038 scopus 로고
    • Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase
    • Keeling, P. L., Bacon, P. J., and Holt, D. C. 1993. Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase. Planta 191: 342-348.
    • (1993) Planta , vol.191 , pp. 342-348
    • Keeling, P.L.1    Bacon, P.J.2    Holt, D.C.3
  • 97
    • 0000954261 scopus 로고
    • Starch biosynthesis 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 biosynthesis 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
  • 99
    • 0001387246 scopus 로고
    • Immunocytochemical localization of ADPglucose pyrophosphorylase in developing potato tuber cells
    • Kim, T. K., Franceschi, V. R., Okita, T. W., Robinson, N. L., Morell, M., and Preiss, J. 1989. Immunocytochemical localization of ADPglucose pyrophosphorylase in developing potato tuber cells. Plant Physiol. 91: 217-220.
    • (1989) Plant Physiol. , vol.91 , pp. 217-220
    • Kim, T.K.1    Franceschi, V.R.2    Okita, T.W.3    Robinson, N.L.4    Morell, M.5    Preiss, J.6
  • 100
    • 0001451455 scopus 로고
    • Purification, characterization, and localization of rice UDP-glucose pyrophosphorylase
    • Kimura, S., Mitsui, T., Matsuoka, T., and Igaue, I. 1992. Purification, characterization, and localization of rice UDP-glucose pyrophosphorylase. Plant Physiol. Biochem. 30: 683.
    • (1992) Plant Physiol. Biochem. , vol.30 , pp. 683
    • Kimura, S.1    Mitsui, T.2    Matsuoka, T.3    Igaue, I.4
  • 101
  • 102
    • 0024958927 scopus 로고
    • Amyloplasts are necessary for full gravitropic sensitivity in roots of Arabidopsis thaliana
    • Kiss, J. Z., Hertel, R., and Sack, F. D. 1989. Amyloplasts are necessary for full gravitropic sensitivity in roots of Arabidopsis thaliana. Planta 177: 198-206.
    • (1989) Planta , vol.177 , pp. 198-206
    • Kiss, J.Z.1    Hertel, R.2    Sack, F.D.3
  • 103
    • 0028253742 scopus 로고
    • Glucose activation and metabolism through UDP-glucose pyrophosphorylase in plants
    • Kleczkowski, L. A. 1994. Glucose activation and metabolism through UDP-glucose pyrophosphorylase in plants. Phytochemistry 37: 1507-1515.
    • (1994) Phytochemistry , vol.37 , pp. 1507-1515
    • Kleczkowski, L.A.1
  • 104
    • 0000850942 scopus 로고    scopus 로고
    • Back to the drawing board: Redefining starch synthesis in cereals
    • Kleczkowski, L. A. 1996. Back to the drawing board: redefining starch synthesis in cereals. Trends Plant Sci. 1: 363-364.
    • (1996) Trends Plant Sci. , vol.1 , pp. 363-364
    • Kleczkowski, L.A.1
  • 105
    • 0027139421 scopus 로고
    • Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation
    • Kleczkowski, L. A., Villand, P., Lüthi, E., Olsen, O. A., and Preiss, Y. 1993. Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation. Plant Physiol. 101: 179-186.
    • (1993) Plant Physiol. , vol.101 , pp. 179-186
    • Kleczkowski, L.A.1    Villand, P.2    Lüthi, E.3    Olsen, O.A.4    Preiss, Y.5
  • 106
    • 0000862389 scopus 로고
    • Energy requirements for fatty acid and glycerolipid biosynthesis from acetate by isolated pea root plastids
    • Kleppinger-Sparace, K., Stahl, R. J., and Sparace, S. A. 1992. Energy requirements for fatty acid and glycerolipid biosynthesis from acetate by isolated pea root plastids. Plant Physiol. 98: 723-727.
    • (1992) Plant Physiol. , vol.98 , pp. 723-727
    • Kleppinger-Sparace, K.1    Stahl, R.J.2    Sparace, S.A.3
  • 107
    • 0024600466 scopus 로고
    • Molecular aspects of the adenine nucleotide carrier from mitochondria
    • Klingenberg, M. 1989. Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 270: 1-14.
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 108
    • 0024659096 scopus 로고
    • The amyloplast targetting transit peptide of waxy protein of maize also mediates protein transport in vitro into chloroplasts
    • Klösgen, R. B., Saedler, H., and Weil, J. H. 1989. The amyloplast targetting transit peptide of waxy protein of maize also mediates protein transport in vitro into chloroplasts. Mol. Gen. Genet. 217: 155-161.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 155-161
    • Klösgen, R.B.1    Saedler, H.2    Weil, J.H.3
  • 109
    • 0028895458 scopus 로고
    • Long-term 13C labeling of starch and sucrose during the course of amyloplast development in intact suspension-cultured storage cells of potato (Solanum tuberosum)
    • Kösegarten, H., Kalinowski, H.-O., and Mengel, K. 1995. Long-term 13C labeling of starch and sucrose during the course of amyloplast development in intact suspension-cultured storage cells of potato (Solanum tuberosum). J. Plant Physiol. 146: 405-410.
    • (1995) J. Plant Physiol. , vol.146 , pp. 405-410
    • Kösegarten, H.1    Kalinowski, H.-O.2    Mengel, K.3
  • 110
    • 0028155211 scopus 로고
    • Evidence for a glucose 1-phosphate translocator in storage tissue amyloplast of potato (Solanum tuberosum) suspension-cultured cells
    • Kösegarten, H. and Mengel, K. 1994. Evidence for a glucose 1-phosphate translocator in storage tissue amyloplast of potato (Solanum tuberosum) suspension-cultured cells. Physiol. Plant. 91: 111-120.
    • (1994) Physiol. Plant. , vol.91 , pp. 111-120
    • Kösegarten, H.1    Mengel, K.2
  • 111
    • 0001898187 scopus 로고
    • Cloning and expression analysis of the plastidic fructose-1,6-bisphosphatase coding sequence from potato: Circumstantial evidence for the import of hexose into choroplasts
    • Kossmann, J., Müller-Röber, B., Dyer, T. A., Raines, C. A., Sonnewald, U., and Willmitzer, L. 1992. Cloning and expression analysis of the plastidic fructose-1,6-bisphosphatase coding sequence from potato: circumstantial evidence for the import of hexose into choroplasts. Planta 188: 7-12.
    • (1992) Planta , vol.188 , pp. 7-12
    • Kossmann, J.1    Müller-Röber, B.2    Dyer, T.A.3    Raines, C.A.4    Sonnewald, U.5    Willmitzer, L.6
  • 112
    • 0344294273 scopus 로고
    • Ph.D. Dissertation, University of Groningen, The Netherlands
    • Kram, A. M. 1995. Structure and Biosynthesis of Starch. Ph.D. Dissertation, University of Groningen, The Netherlands.
    • (1995) Structure and Biosynthesis of Starch
    • Kram, A.M.1
  • 113
    • 0000510503 scopus 로고
    • Localization of branching enzyme in potato tuber cells with the use of immunoelectron microscopy
    • Kram, A. M., Oostergetel, G. T., and van Bruggen, E. F. J. 1993. Localization of branching enzyme in potato tuber cells with the use of immunoelectron microscopy. Plant Physiol. 101: 237-243.
    • (1993) Plant Physiol. , vol.101 , pp. 237-243
    • Kram, A.M.1    Oostergetel, G.T.2    Van Bruggen, E.F.J.3
  • 114
    • 0028942619 scopus 로고
    • Molecular cloning and characterization of a novel isoform of potato ADP-glucose pyrophosphorylase
    • La Cognata, U., Willmitzer, L., and Müller-Röber, B. 1995. Molecular cloning and characterization of a novel isoform of potato ADP-glucose pyrophosphorylase. Mol. Gen. Genet. 246: 538-548.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 538-548
    • La Cognata, U.1    Willmitzer, L.2    Müller-Röber, B.3
  • 115
    • 0001723914 scopus 로고
    • Sucrose-starch transforming system in rice grains-A tracer feeding study
    • Lee, P. D. and Su, J. C. 1982. Sucrose-starch transforming system in rice grains-A tracer feeding study. Proc. Natl. Sci. Counc. Part B. 6: 189-196.
    • (1982) Proc. Natl. Sci. Counc. Part B. , vol.6 , pp. 189-196
    • Lee, P.D.1    Su, J.C.2
  • 116
    • 0018958496 scopus 로고
    • Biosynthesis of bacterial glycogen: Purification and properties of Salmonella typhimurium LT-2 adenosine diphosphate glucose pyrophosphorylase
    • Lehmann, M. and Preiss, J. 1980. Biosynthesis of bacterial glycogen: purification and properties of Salmonella typhimurium LT-2 adenosine diphosphate glucose pyrophosphorylase. J. Bacteriol. 143: 120-127.
    • (1980) J. Bacteriol. , vol.143 , pp. 120-127
    • Lehmann, M.1    Preiss, J.2
  • 117
    • 0004053615 scopus 로고
    • Worth Publ. Inc. New York, U.S.A.
    • Lehninger, A. L. 1975. In: Biochemistry. Worth Publ. Inc. New York, U.S.A.
    • (1975) Biochemistry
    • Lehninger, A.L.1
  • 118
    • 0001058123 scopus 로고
    • ATPase and acid phosphatase activities associated with vacuoles isolated from storage roots of red beet (Beta vulgaris L.)
    • Leigh, R. A. and Walker, R. R. 1980. ATPase and acid phosphatase activities associated with vacuoles isolated from storage roots of red beet (Beta vulgaris L.). Planta 150: 222-229.
    • (1980) Planta , vol.150 , pp. 222-229
    • Leigh, R.A.1    Walker, R.R.2
  • 119
    • 0026668598 scopus 로고
    • Information for targetting to the chloroplastic inner envelope membrane is contained in the mature region of the maize Btl-encoded protein
    • Li, H. M., Sullivan, T. D., and Keegstra, K. 1992. Information for targetting to the chloroplastic inner envelope membrane is contained in the mature region of the maize Btl-encoded protein. J. Biol. Chem. 267: 18999-19004.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18999-19004
    • Li, H.M.1    Sullivan, T.D.2    Keegstra, K.3
  • 120
    • 0001117527 scopus 로고
    • Isolation and characterization of a starch less mutant of Arabidopsis thaliana (L.) Heynh lacking ADPglucose pyrophosphorylase activity
    • Lin, T-P., Caspar, T., Somerville, C. R., and Preiss, J. 1988a. Isolation and characterization of a starch less mutant of Arabidopsis thaliana (L.) Heynh lacking ADPglucose pyrophosphorylase activity. Plant Physiol. 86: 1131-1135.
    • (1988) Plant Physiol. , vol.86 , pp. 1131-1135
    • Lin, T.-P.1    Caspar, T.2    Somerville, C.R.3    Preiss, J.4
  • 121
    • 0000984370 scopus 로고
    • A starch deficient mutant of Arabidopsis thaliana with low ADPglucose pyrophosphorylase activity lacks one of the two subunits of the enzyme
    • Lin, T.-P., Caspar, T., Somerville, C. R., and Preiss, J. 1988b. A starch deficient mutant of Arabidopsis thaliana with low ADPglucose pyrophosphorylase activity lacks one of the two subunits of the enzyme. Plant Physiol. 88: 1175-1181.
    • (1988) Plant Physiol. , vol.88 , pp. 1175-1181
    • Lin, T.-P.1    Caspar, T.2    Somerville, C.R.3    Preiss, J.4
  • 122
    • 0345156592 scopus 로고
    • Carbohydrate transfer into isolated maize (Zea mays L.) amyloplasts
    • Liu K.-C., Boyer, C. D., and Shannon, J. C. 1992. Carbohydrate transfer into isolated maize (Zea mays L.) amyloplasts. Plant Physiol. 99: S39.
    • (1992) Plant Physiol. , vol.99
    • Liu, K.-C.1    Boyer, C.D.2    Shannon, J.C.3
  • 123
    • 0024300744 scopus 로고
    • Linked sucrose synthase genes in group-7 chromosomes in hexaploid wheat (Triticum aestivum L.)
    • Marana, C., Garcia-Olmedo, F., and Carbonero, P. 1988. Linked sucrose synthase genes in group-7 chromosomes in hexaploid wheat (Triticum aestivum L.). Gene 63: 253-260.
    • (1988) Gene , vol.63 , pp. 253-260
    • Marana, C.1    Garcia-Olmedo, F.2    Carbonero, P.3
  • 124
    • 0029328417 scopus 로고
    • Starch biosynthesis
    • Martin, C. and Smith, A. M. 1995. Starch biosynthesis. Plant Cell 7: 971-985.
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 125
    • 0028817209 scopus 로고
    • Intracellular immunolocalization of adenosine 5′-diphosphoglucose pyrophosphorylase in developing endosperm cells of maize (Zea mays L.)
    • Miller, M. E. and Chourey, P. S. 1995. Intracellular immunolocalization of adenosine 5′-diphosphoglucose pyrophosphorylase in developing endosperm cells of maize (Zea mays L.). Planta 197: 522-527.
    • (1995) Planta , vol.197 , pp. 522-527
    • Miller, M.E.1    Chourey, P.S.2
  • 126
    • 0028940690 scopus 로고
    • Analysis of carbohydrate transport across the envelope of isolated cauliflower bud amyloplasts
    • Möhlmann, T., Batz, O., Maass, U., and Neuhaus, H.E. 1995. Analysis of carbohydrate transport across the envelope of isolated cauliflower bud amyloplasts. Biochem. J. 307: 521-526.
    • (1995) Biochem. J. , vol.307 , pp. 521-526
    • Möhlmann, T.1    Batz, O.2    Maass, U.3    Neuhaus, H.E.4
  • 127
    • 0030970353 scopus 로고    scopus 로고
    • ADPglucose 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. ADPglucose 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
  • 128
    • 0000769546 scopus 로고
    • Sucrose synthase of soybean nodules
    • Morell, M. K. and Copeland, L. 1985. Sucrose synthase of soybean nodules. Plant Physiol. 78: 149-154.
    • (1985) Plant Physiol. , vol.78 , pp. 149-154
    • Morell, M.K.1    Copeland, L.2
  • 129
    • 0000083366 scopus 로고
    • The biochemistry and molecular biology of starch synthesis in cereals
    • Morell, M. K., Rahman, S., Abrahams, S. L., and Appels, R. 1995. The biochemistry and molecular biology of starch synthesis in cereals. Aust. J. Plant Physiol. 22: 647-660.
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 647-660
    • Morell, M.K.1    Rahman, S.2    Abrahams, S.L.3    Appels, R.4
  • 130
    • 84994964585 scopus 로고
    • Approaches to influence starch quantity and starch quality in transgenic plants
    • Müller-Röber B. T. and Kossmann, J. 1994. Approaches to influence starch quantity and starch quality in transgenic plants. Plant Cell Environ. 17: 601-613.
    • (1994) Plant Cell Environ. , vol.17 , pp. 601-613
    • Müller-Röber, B.T.1    Kossmann, J.2
  • 131
    • 0025080561 scopus 로고
    • One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose
    • Müller-Röber, B. T., Kossmann, J., Hannah, L. C., Willmitzer, L., and Sonnewald, U. 1990. One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose. Mol Gen Genet. 224: 136-146.
    • (1990) Mol Gen Genet. , vol.224 , pp. 136-146
    • Müller-Röber, B.T.1    Kossmann, J.2    Hannah, L.C.3    Willmitzer, L.4    Sonnewald, U.5
  • 132
    • 0026533580 scopus 로고
    • Inhibition of the ADPglucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes
    • Müller-Röber, B. T., Sonnewald, U., and Willmitzer, L. 1992. Inhibition of the ADPglucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences 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.T.1    Sonnewald, U.2    Willmitzer, L.3
  • 133
    • 0344726304 scopus 로고
    • Enzymic mechanism of starch synthesis in ripening rice grains
    • Murata, T., Sugiyama, T., and Akazawa, T. 1964. Enzymic mechanism of starch synthesis in ripening rice grains. Arch. Biochem. Biophys. 107: 92-101.
    • (1964) Arch. Biochem. Biophys. , vol.107 , pp. 92-101
    • Murata, T.1    Sugiyama, T.2    Akazawa, T.3
  • 134
    • 0001129245 scopus 로고
    • Invertases
    • Boyer, P. D., Lardy, H., and Myrbäck, K., Eds., Academic Press, New York
    • Myrbäck, K. 1960. Invertases. In: The Enzymes 2nd ed. Boyer, P. D., Lardy, H., and Myrbäck, K., Eds., Academic Press, New York, pp. 379-396.
    • (1960) The Enzymes 2nd Ed. , pp. 379-396
    • Myrbäck, K.1
  • 135
    • 0030912925 scopus 로고    scopus 로고
    • Starch synthesis in amyloplasts purified from developing potato tubers
    • Naeem, M., Tetlow, I. J., and Emes, 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    Emes, M.J.3
  • 137
    • 0027438890 scopus 로고
    • Purification of highly intact plastids from various heterotrophic plant tissues: Analysis of enzymic equipment and precursor dependency for starch biosynthesis
    • Neuhaus, H. E., Batz, O., Thom, E., and Scheibe, R. 1993a. Purification of highly intact plastids from various heterotrophic plant tissues: analysis of enzymic equipment and precursor dependency for starch biosynthesis. Biochem. J. 196: 395-401.
    • (1993) Biochem. J. , vol.196 , pp. 395-401
    • Neuhaus, H.E.1    Batz, O.2    Thom, E.3    Scheibe, R.4
  • 138
    • 0001578389 scopus 로고
    • Characterization of glucose-6-P incorporation into starch by isolated intact cauliflower-bud plastids
    • Neuhaus, H. E., Henrichs, G., and Scheibe, R. 1993b. Characterization of glucose-6-P 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
  • 139
    • 0029168324 scopus 로고
    • Starch degradation in intact amyloplasts isolated from cauliflower floral buds (Brassica oleracea L.)
    • Neuhaus, H. E., Henrichs, G., and Scheibe, R. 1995. Starch degradation in intact amyloplasts isolated from cauliflower floral buds (Brassica oleracea L.) Planta 195: 496-504.
    • (1995) Planta , vol.195 , pp. 496-504
    • Neuhaus, H.E.1    Henrichs, G.2    Scheibe, R.3
  • 140
    • 0004891678 scopus 로고
    • Comparison of pyrophosphate turnover and the maximum catalytic activity of pyrophosphate: Fructose-6-phosphate phosphotransferase in leaves
    • Neuhaus, H. E., Krause, K., and Stitt, M. 1990. Comparison of pyrophosphate turnover and the maximum catalytic activity of pyrophosphate: fructose-6-phosphate phosphotransferase in leaves. Phytochemistry 29: 3411.
    • (1990) Phytochemistry , vol.29 , pp. 3411
    • Neuhaus, H.E.1    Krause, K.2    Stitt, M.3
  • 141
    • 0030039392 scopus 로고    scopus 로고
    • Unidirectional transport of orthophosphate across the envelope of isolated cauliflower-bud amyloplasts
    • Neuhaus, H. E. and Maass, U. 1996. Unidirectional transport of orthophosphate across the envelope of isolated cauliflower-bud amyloplasts. Planta 198: 542-548.
    • (1996) Planta , vol.198 , pp. 542-548
    • Neuhaus, H.E.1    Maass, U.2
  • 142
    • 0000117374 scopus 로고
    • Control 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. 1990. Control 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.2
  • 143
    • 0031036197 scopus 로고    scopus 로고
    • Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L.
    • Neuhaus, H. E., Thorn, E., Möhlmann, T., Steup, M., and Kampfenkel, K. 1997. Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L. Plant J. 11: 73-82.
    • (1997) Plant J. , vol.11 , pp. 73-82
    • Neuhaus, H.E.1    Thorn, E.2    Möhlmann, T.3    Steup, M.4    Kampfenkel, K.5
  • 144
    • 0344726297 scopus 로고
    • Isolation and characterization of the amyloplast envelope-membrane from cultured white-wild cells of sycamore (Acer pseudoplatanus L.)
    • Ngernprasirtsiri, J., Harinasut, P., Macherel, D., Strzalka, K., Takabe, T., Akazawa, T., and Kojima, K. 1988. Isolation and characterization of the amyloplast envelope-membrane from cultured white-wild cells of sycamore (Acer pseudoplatanus L.). Plant Physiol. 87: 371-378.
    • (1988) Plant Physiol. , vol.87 , pp. 371-378
    • Ngernprasirtsiri, J.1    Harinasut, P.2    Macherel, D.3    Strzalka, K.4    Takabe, T.5    Akazawa, T.6    Kojima, K.7
  • 145
    • 0007674076 scopus 로고
    • Immunochemical analysis shows that an ATP/ADP-translocator is associated with the inner envelope membranes of amyloplasts from Acer pseudoplatanus L.
    • Ngernprasirtsiri J., Takabe, T., and Akazawa, T. 1989. Immunochemical analysis shows that an ATP/ADP-translocator is associated with the inner envelope membranes of amyloplasts from Acer pseudoplatanus L. Plant Physiol. 89: 1024-1027.
    • (1989) Plant Physiol. , vol.89 , pp. 1024-1027
    • Ngernprasirtsiri, J.1    Takabe, T.2    Akazawa, T.3
  • 147
    • 0001260817 scopus 로고
    • Is there an alternative pathway for starch synthesis?
    • Okita, T. W. 1992. Is there an alternative pathway for starch synthesis? Plant Physiol. 100: 560-564.
    • (1992) Plant Physiol. , vol.100 , pp. 560-564
    • Okita, T.W.1
  • 148
    • 0012467850 scopus 로고
    • Many maize inbreds lack an endosperm cytosolic phosphoglucomutase
    • Pan, D., Strelow, L. I., and Nelson, O. E. 1995. Many maize inbreds lack an endosperm cytosolic phosphoglucomutase. Plant Physiol. 93: 1650-1653.
    • (1995) Plant Physiol. , vol.93 , pp. 1650-1653
    • Pan, D.1    Strelow, L.I.2    Nelson, O.E.3
  • 150
    • 0000211041 scopus 로고
    • Biochemical mechanism of starch biosynthesis in amyloplasts from cultured cells of sycamore (Acer pseudoplatanus)
    • Pozueta-Romero, J. and Akazawa, T. 1993. Biochemical mechanism of starch biosynthesis in amyloplasts from cultured cells of sycamore (Acer pseudoplatanus). J. Exp. Bot. 44(Suppl.): 297-306.
    • (1993) J. Exp. Bot. , vol.44 , Issue.SUPPL. , pp. 297-306
    • Pozueta-Romero, J.1    Akazawa, T.2
  • 151
    • 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., and Akazawa, T. 1991a. 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.3    Akazawa, T.4
  • 152
    • 0026003280 scopus 로고
    • Filtering centrifugation through two layers of silicone oil: A method for kinetic analysis of rapid metabolite transport in organelles
    • Pozueta-Romero, J., Frehner, M., and Akazawa, T. 1991b. Filtering centrifugation through two layers of silicone oil: a method for kinetic analysis of rapid metabolite transport in organelles. Cell Struct. Funct. 16: 357-363.
    • (1991) Cell Struct. Funct. , vol.16 , pp. 357-363
    • Pozueta-Romero, J.1    Frehner, M.2    Akazawa, T.3
  • 153
    • 0000453796 scopus 로고
    • ADP-glucose transport by the chloroplast adenylate translocator is linked to starch biosynthesis
    • Pozueta-Romero, J., Ardila, F., and Akazawa, T. 1991c. 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    Ardila, F.2    Akazawa, T.3
  • 154
    • 0026550805 scopus 로고
    • A method for accurate analysis of intermembrane space in organelles enclosed by double envelope membranes
    • Pozueta-Romero, J., Ardila, F., Akazawa, T., and Kojima, K. 1992. A method for accurate analysis of intermembrane space in organelles enclosed by double envelope membranes. Cell Struct. Funct. 17: 47-53.
    • (1992) Cell Struct. Funct. , vol.17 , pp. 47-53
    • Pozueta-Romero, J.1    Ardila, F.2    Akazawa, T.3    Kojima, K.4
  • 155
    • 0025883138 scopus 로고
    • Comparative analysis of mitochondrial and amyloplast ATP/ADP translocators
    • Pozueta-Romero, J., Viale, A. M., and Akazawa, T. 1991d. Comparative analysis of mitochondrial and amyloplast ATP/ADP translocators. FEBS Lett. 287: 62-66.
    • (1991) FEBS Lett. , vol.287 , pp. 62-66
    • Pozueta-Romero, J.1    Viale, A.M.2    Akazawa, T.3
  • 156
    • 0000194569 scopus 로고
    • Biosynthesis of starch and its regulation
    • Biochem. of Plants Preiss, J., Ed. Academic Press, New York
    • Preiss, J. 1988. Biosynthesis of starch and its regulation. Biochem. of Plants. In: The Biochemistry of Plants. Preiss, J., Ed. Vol. 14. Academic Press, New York. pp. 182-249.
    • (1988) The Biochemistry of Plants , vol.14 , pp. 182-249
    • Preiss, J.1
  • 157
    • 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
  • 159
    • 0028056951 scopus 로고
    • Expression of ADP-glucose pyrophosphorylase in maize (Zea mays L.) grain and source leaf during grain filling
    • Prioul, J. L., Jeannette, E., Reyss, A., Gregory, N., Giroux, M., Hannah, L. C., and Causse, M. 1994. Expression of ADP-glucose pyrophosphorylase in maize (Zea mays L.) grain and source leaf during grain filling. Plant Physiol. 104: 179-187.
    • (1994) Plant Physiol. , vol.104 , pp. 179-187
    • Prioul, J.L.1    Jeannette, E.2    Reyss, A.3    Gregory, N.4    Giroux, M.5    Hannah, L.C.6    Causse, M.7
  • 160
    • 0029838255 scopus 로고    scopus 로고
    • Evidence for two types of phosphate translocators in sweet-pepper (Capsicum annuum L.) fruit chromoplasts
    • Quick, W. P. and Neuhaus, H. E. 1996. Evidence for two types of phosphate translocators in sweet-pepper (Capsicum annuum L.) fruit chromoplasts. Biochem. J. 320: 7-10.
    • (1996) Biochem. J. , vol.320 , pp. 7-10
    • Quick, W.P.1    Neuhaus, H.E.2
  • 161
    • 0022425706 scopus 로고
    • Effect of sucrose starvation on sycamore (Acer pseudoplatanus) cell carbohydrate and Pi status
    • Rebeille, F, Bligny, R., Martin, J-B., and Douce, R. 1985. Effect of sucrose starvation on sycamore (Acer pseudoplatanus) cell carbohydrate and Pi status. Biochem. J. 226: 679-684.
    • (1985) Biochem. J. , vol.226 , pp. 679-684
    • Rebeille, F.1    Bligny, R.2    Martin, J.-B.3    Douce, R.4
  • 162
    • 0027302147 scopus 로고
    • Antisense repression of the chloroplast triose phosphate translocator affects carbon partitioning in transgenic potato plants
    • Riesmeier, J. W., Flügge, U. I. Schultz, 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    Schultz, B.3    Heineke, D.4    Heldt, H.W.5    Willmitzer, L.6    Frommer, W.B.7
  • 163
    • 0001146856 scopus 로고
    • Sink metabolism in tomato fruit. Developmental changes in carbohydrate metabolizing enzymes
    • Robinson, N. L., Hewitt, J. D., and Bennett, A. B. 1988. Sink metabolism in tomato fruit. Developmental changes in carbohydrate metabolizing enzymes. Plant Physiol. 87: 727-730.
    • (1988) Plant Physiol. , vol.87 , pp. 727-730
    • Robinson, N.L.1    Hewitt, J.D.2    Bennett, A.B.3
  • 164
    • 0000191626 scopus 로고
    • Localization of carbohydrate metabolizing enzymes in guard cells of Commelina communis
    • Robinson, N. L. and Preiss, J. 1987. Localization of carbohydrate metabolizing enzymes in guard cells of Commelina communis. Plant Physiol. 85: 360-364.
    • (1987) Plant Physiol. , vol.85 , pp. 360-364
    • Robinson, N.L.1    Preiss, J.2
  • 165
    • 0001052544 scopus 로고
    • Purification and characterization of sucrose synthase from the cotyledons of Vicia faba L.
    • Ross, H. A. and Davies, H. 1992. Purification and characterization of sucrose synthase from the cotyledons of Vicia faba L. Plant Physiol. 100: 1008-1013.
    • (1992) Plant Physiol. , vol.100 , pp. 1008-1013
    • Ross, H.A.1    Davies, H.2
  • 166
    • 0026199675 scopus 로고
    • Gravitropism and starch statoliths in an Arabidopsis mutant
    • Saether, N. and Iversen, T. H. 1991. Gravitropism and starch statoliths in an Arabidopsis mutant. Planta 184: 491-497.
    • (1991) Planta , vol.184 , pp. 491-497
    • Saether, N.1    Iversen, T.H.2
  • 167
    • 0023574446 scopus 로고
    • Molecular cloning and sequencing of sucrose synthase cDNA from potato (Solanum tuberosum L.): Preliminary characterization of sucrose synthase mRNA distribution
    • Salanoubat, M. and Beillard, G. 1987. Molecular cloning and sequencing of sucrose synthase cDNA from potato (Solanum tuberosum L.): preliminary characterization of sucrose synthase mRNA distribution. Gene 60: 47-56.
    • (1987) Gene , vol.60 , pp. 47-56
    • Salanoubat, M.1    Beillard, G.2
  • 168
    • 0026640065 scopus 로고
    • Homologous sucrose synthase genes in barley (Hordeum vulgare) are located in chromosomes 7H (syn.1) and 2H
    • Sanchez de la Hoz, P., Vicente-Carbajosa, J., Mena, M., and Carbonero, P. 1992. Homologous sucrose synthase genes in barley (Hordeum vulgare) are located in chromosomes 7H (syn.1) and 2H. FEBS Lett. 310: 46-50.
    • (1992) FEBS Lett. , vol.310 , pp. 46-50
    • Sanchez De La Hoz, P.1    Vicente-Carbajosa, J.2    Mena, M.3    Carbonero, P.4
  • 169
    • 0030888543 scopus 로고    scopus 로고
    • Sucrose-to-starch metabolism in tomato fruit undergoing transient starch accumulation
    • Schaffer, A. A. and Petreikov, M. 1997. Sucrose-to-starch metabolism in tomato fruit undergoing transient starch accumulation. Plant Physiol. 113: 739-746.
    • (1997) Plant Physiol. , vol.113 , pp. 739-746
    • Schaffer, A.A.1    Petreikov, M.2
  • 170
    • 0029855746 scopus 로고    scopus 로고
    • The impact of reduced vacuolar invertase activity on the photosynthetic and carbohydrate metabolism of tomato
    • Scholes, J., Bundock, N., Wilde, R., and Rolfe, S. 1996. The impact of reduced vacuolar invertase activity on the photosynthetic and carbohydrate metabolism of tomato. Planta 200: 265-272.
    • (1996) Planta , vol.200 , pp. 265-272
    • Scholes, J.1    Bundock, N.2    Wilde, R.3    Rolfe, S.4
  • 172
    • 0028851252 scopus 로고
    • Transport of inorganic phosphate and C3- and C6-sugar phosphates across the envelope membranes of potato tuber amyloplasts
    • Schott, K., Borchert, S., Müller-Röber, B., and Heldt, H. 1995. Transport of inorganic phosphate and C3- and C6-sugar phosphates across the envelope membranes of potato tuber amyloplasts. Planta 196: 647-652.
    • (1995) Planta , vol.196 , pp. 647-652
    • Schott, K.1    Borchert, S.2    Müller-Röber, B.3    Heldt, H.4
  • 173
    • 0028254291 scopus 로고
    • Specific transport of inorganic phosphate and C3- and C6-sugar-phosphates across the envelope membranes of tomato (Lycopersicon esculentum) leaf chloroplasts, tomato fruit-chloroplasts, and fruit-chromoplasts
    • Schünemann, D. and Borchert, S. 1994. Specific transport of inorganic phosphate and C3- and C6-sugar-phosphates across the envelope membranes of tomato (Lycopersicon esculentum) leaf chloroplasts, tomato fruit-chloroplasts, and fruit-chromoplasts. Bot. Acta 107: 461-467.
    • (1994) Bot. Acta , vol.107 , pp. 461-467
    • Schünemann, D.1    Borchert, S.2
  • 174
    • 0001313742 scopus 로고
    • ATP/ADP translocator from pea root plastids. Comparison with translocators from spinach chloroplast, and pea leaf mitochondria
    • Schünemann, D., Borchert, S., Flügge, U. I., and Heldt, H. W. 1993. ATP/ADP translocator from pea root plastids. Comparison with translocators from spinach chloroplast, and pea leaf mitochondria. Plant Physiol. 103: 131-137.
    • (1993) Plant Physiol. , vol.103 , pp. 131-137
    • Schünemann, D.1    Borchert, S.2    Flügge, U.I.3    Heldt, H.W.4
  • 175
    • 0032134257 scopus 로고    scopus 로고
    • Brittle-1, an adenylate translocator, facilitates transfer of extraplastidal synthesized ADP-glucose into amyloplasts of maize endosperms
    • Shannon, J. C., Pien, F.-M., Cao, P., and Liu, K.-C. 1998. Brittle-1, an adenylate translocator, facilitates transfer of extraplastidal synthesized
    • (1998) Plant Physiol , vol.117 , pp. 1235-1252
    • Shannon, J.C.1    Pien, F.-M.2    Cao, P.3    Liu, K.-C.4
  • 176
    • 0030028267 scopus 로고    scopus 로고
    • Nucleotides and nucleotide sugars in developing maize endosperms. Synthesis of ADP-glucose in brittle 1
    • Shannon, J. C., Pien, F.-M., and Liu, K.-C. 1996. Nucleotides and nucleotide sugars in developing maize endosperms. Synthesis of ADP-glucose in brittle 1. 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
  • 177
    • 0000797202 scopus 로고
    • Modifying starch biosynthesis in potatoes
    • Shewmaker, C. K. and Stalker, D. M. 1992. Modifying starch biosynthesis in potatoes. Plant Physiol. 100: 1083-1086.
    • (1992) Plant Physiol. , vol.100 , pp. 1083-1086
    • Shewmaker, C.K.1    Stalker, D.M.2
  • 178
    • 0001081096 scopus 로고
    • Comparative enzymic studies of sucrose metabolism in the taproots and fibrous roots of Beta vulgaris L.
    • Silvius, J. E. and Snyder, F. W. 1979. Comparative enzymic studies of sucrose metabolism in the taproots and fibrous roots of Beta vulgaris L. Plant Physiol. 64: 1070-1073.
    • (1979) Plant Physiol. , vol.64 , pp. 1070-1073
    • Silvius, J.E.1    Snyder, F.W.2
  • 179
    • 0031046802 scopus 로고    scopus 로고
    • Influence of gene dosage on carbohydrate synthesis and enzymatic activities in endosperm of starch-deficient mutants of maize
    • Singletary, G. W., Banisadr, R., and Keeling, P. 1997. Influence of gene dosage on carbohydrate synthesis and enzymatic activities in endosperm of starch-deficient mutants of maize. Plant Physiol. 113: 293-304.
    • (1997) Plant Physiol. , vol.113 , pp. 293-304
    • Singletary, G.W.1    Banisadr, R.2    Keeling, P.3
  • 180
    • 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 Physiol. 89: 1279-1284.
    • (1989) Plant Physiol. , vol.89 , pp. 1279-1284
    • Smith, A.M.1    Bettey, M.2    Bedford, I.D.3
  • 181
    • 0029138717 scopus 로고
    • What controls the amount and structure of starch in storage organs?
    • Smith, A. M., Denyer, K., and Martin, C. R. 1995. What controls the amount and structure of starch in storage organs? Plant Physiol. 107: 673-677.
    • (1995) Plant Physiol. , vol.107 , pp. 673-677
    • Smith, A.M.1    Denyer, K.2    Martin, C.R.3
  • 182
    • 0026767213 scopus 로고
    • Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources
    • Smith-White, B. J. and Preiss, J. 1992. Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources. J. Mol. Evol. 34: 449-464.
    • (1992) J. Mol. Evol. , vol.34 , pp. 449-464
    • Smith-White, B.J.1    Preiss, J.2
  • 183
    • 0001749216 scopus 로고
    • Measurement of the pyrophosphate content of plant tissues
    • Smyth, D. A. and Black, C. C. 1984. Measurement of the pyrophosphate content of plant tissues. Plant Physiol. 75: 862-864.
    • (1984) Plant Physiol. , vol.75 , pp. 862-864
    • Smyth, D.A.1    Black, C.C.2
  • 184
    • 0026893738 scopus 로고
    • Expression of E. coli inorganic pyrophosphatase in transgenic plants alters photoassimilate partitioning
    • Sonnewald, U. 1992. Expression of E. coli inorganic pyrophosphatase in transgenic plants alters photoassimilate partitioning. Plant J. 2: 571-581.
    • (1992) Plant J. , vol.2 , pp. 571-581
    • Sonnewald, U.1
  • 185
    • 0026192098 scopus 로고
    • Transgenic tobacco plants expressing yeast-derived invertase in either the cytosol, vacuole or apoplast: A powerful tool for studying sucrose metabolism and sink/source interactions
    • Sonnewald, U., Brauer, M., von Schaewen, A., Stitt, M., and Willmitzer, L. 1991. Transgenic tobacco plants expressing yeast-derived invertase in either the cytosol, vacuole or apoplast: a powerful tool for studying sucrose metabolism and sink/source interactions. Plant J. 1: 95-106.
    • (1991) Plant J. , vol.1 , pp. 95-106
    • Sonnewald, U.1    Brauer, M.2    Von Schaewen, A.3    Stitt, M.4    Willmitzer, L.5
  • 187
    • 0001433930 scopus 로고
    • Pyrophosphorylases in Solanum tuberosum. IV. Purification, tissue distribution, and physicochemical properties of UDP-glucose pyrophosphorylase
    • Sowokinos, J. R., Spychalla, J. P., and Desborough, S. L. 1993. Pyrophosphorylases in Solanum tuberosum. IV. Purification, tissue distribution, and physicochemical properties of UDP-glucose pyrophosphorylase. Plant Physiol. 101: 1073-1080.
    • (1993) Plant Physiol. , vol.101 , pp. 1073-1080
    • Sowokinos, J.R.1    Spychalla, J.P.2    Desborough, S.L.3
  • 188
    • 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 Bewan, M. W. 1904. 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.
    • (1904) J. Plant Physiol. , vol.144 , pp. 444-453
    • Spychalla, J.P.1    Scheffler, B.E.2    Sowokinos, J.R.3    Bewan, M.W.4
  • 189
    • 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
  • 190
    • 0029106136 scopus 로고
    • Development- and organ-specific expression of genes for sucrose synthase and three isoenzymes of acid β-fructofuranosidase in carrot
    • Sturm, A., Sebkova, V., Lorenz, L., Hardegger, M., Lienhard, S., and Under, C. 1995. Development- and organ-specific expression of genes for sucrose synthase and three isoenzymes of acid β-fructofuranosidase in carrot. Planta 195: 601-610.
    • (1995) Planta , vol.195 , pp. 601-610
    • Sturm, A.1    Sebkova, V.2    Lorenz, L.3    Hardegger, M.4    Lienhard, S.5    Under, C.6
  • 191
    • 0006302390 scopus 로고
    • Some aspects of sucrose metabolism in plants
    • Su, J.-C. 1982. Some aspects of sucrose metabolism in plants. Proc. Natl. Sci. Council. Part B. 6: 172-180.
    • (1982) Proc. Natl. Sci. Council. Part B. , vol.6 , pp. 172-180
    • Su, J.-C.1
  • 192
    • 0008762706 scopus 로고
    • Metabolic roles of sucrose synthase: Example of rice isozymes encoded by three isogenes
    • Pontis, H. G., Salerno, G. L., and Echeverria, E. J., Eds., American Society of Plant Physiologists
    • Su, J.-C. 1995. Metabolic roles of sucrose synthase: example of rice isozymes encoded by three isogenes. In: International Symposium on Sucrose Metabolism. Pontis, H. G., Salerno, G. L., and Echeverria, E. J., Eds., American Society of Plant Physiologists, pp. 40-48.
    • (1995) International Symposium on Sucrose Metabolism , pp. 40-48
    • Su, J.-C.1
  • 193
    • 0028980954 scopus 로고
    • The maize brittle 1 gene encodes amyloplast membrane polypeptides
    • Sullivan, T. D. 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.D.1    Kaneko, Y.2
  • 194
    • 0026291471 scopus 로고
    • Analysis of maize Brittle 1 alleles and a defective suppressor mutator-induced mutable allele
    • Sullivan, T. D., Strelow, L. I., Illingworth, C. A., Phillips, R. L., and Nelson Jr., O. E. 1991. Analysis of maize Brittle 1 alleles and a defective suppressor mutator-induced mutable 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., Jr.5
  • 195
    • 0345255484 scopus 로고
    • Sucrose synthase in wild tomato, Lycopersicon chmielewskii, and tomato fruit sink strength
    • Sun, J., Loboda, T., Sung, S-J. S., Black, C. C. 1992. Sucrose synthase in wild tomato, Lycopersicon chmielewskii, and tomato fruit sink strength. Plant Physiol. 98: 1163-1169.
    • (1992) Plant Physiol. , vol.98 , pp. 1163-1169
    • Sun, J.1    Loboda, T.2    Sung, S.-J.S.3    Black, C.C.4
  • 196
    • 0029853690 scopus 로고    scopus 로고
    • Characterization of transgenic potato (Solanum tuberosum) tubers with increased ADPglucose pyrophosphorylase
    • Sweetlove, L. J., Burrell, M., and ap Rees, T. 1996a. Characterization of transgenic potato (Solanum tuberosum) tubers with increased ADPglucose pyrophosphorylase. Biochem. J. 320: 481-492.
    • (1996) Biochem. J. , vol.320 , pp. 481-492
    • Sweetlove, L.J.1    Burrell, M.2    Ap Rees, T.3
  • 197
    • 0029902429 scopus 로고    scopus 로고
    • Starch metabolism in tubers of transgenic potato (Solanum tuberosum) with increased ADPglucose pyrophosphorylase
    • Sweetlove, L. J., Burrell, 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.2    Ap Rees, T.3
  • 198
    • 0042600227 scopus 로고
    • On the initiation of starch synthesis
    • Pontis, H. G., Salerno, G. L., and Echeverria, E. J., Eds., American Society of Plant Physiologists
    • Tandecarz, J. S., Ardila, F. J., Bocca, S. N., Moreno, S., and Rothchild, A. 1995. On the initiation of starch synthesis. In: International Symposium on Sucrose Metabolism. Pontis, H. G., Salerno, G. L., and Echeverria, E. J., Eds., American Society of Plant Physiologists, pp. 107-114.
    • (1995) International Symposium on Sucrose Metabolism , pp. 107-114
    • Tandecarz, J.S.1    Ardila, F.J.2    Bocca, S.N.3    Moreno, S.4    Rothchild, A.5
  • 199
    • 0000633840 scopus 로고
    • A rapid method for the isolation of purified amyloplasts from wheat endosperm
    • Tetlow, I. J., Blissett, K. J., and Emes, M. J. 1993. A rapid method for the isolation of purified amyloplasts from wheat endosperm. Planta 189: 597-600.
    • (1993) Planta , vol.189 , pp. 597-600
    • Tetlow, I.J.1    Blissett, K.J.2    Emes, M.J.3
  • 200
    • 0028093886 scopus 로고
    • Starch synthesis and carbohydrate oxidation in amyloplasts from developing wheat endosperm
    • Tetlow, I. J., Blissett, K. J., and Emes, 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    Emes, M.J.3
  • 201
    • 0030483916 scopus 로고    scopus 로고
    • Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplast in barley endosperm
    • Thorbjørnsen, T., Villand, P., Denyer, K., Olsen, O.-A., and Smith, A. M. 1996a. Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplast 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
  • 202
    • 0030062188 scopus 로고    scopus 로고
    • A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare)
    • Thorbjørnsen, T., Villand, P., Kleczkowski, L. A., and Olsen, O.-A. 1996b. A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare). Biochem. J. 313: 149-154.
    • (1996) Biochem. J. , vol.313 , pp. 149-154
    • Thorbjørnsen, T.1    Villand, P.2    Kleczkowski, L.A.3    Olsen, O.-A.4
  • 203
    • 0014023725 scopus 로고
    • Starch-deficient maize mutant lacking adenosine diphosphate glucose pyrophosphorylase activity
    • Tsai, C. Y. and Nelson, O. E. 1966. Starch-deficient maize 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
  • 204
    • 0001802996 scopus 로고
    • Starch synthesis by isolated amyloplasts from wheat endosperm
    • Tyson, R. H. and apRees, 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    ApRees, T.2
  • 205
    • 0013801221 scopus 로고
    • Verteilung und wanderung von phosphoglycerat zwischen den chloroplasten und den cytoplasma während der photosynthese
    • Urbach, W., Hudson, M. A., Ullrich, W., Santarius, K. A., and Heber, U. 1965. Verteilung und Wanderung von Phosphoglycerat zwischen den Chloroplasten und den Cytoplasma während der Photosynthese. Z. Naturforsch. 20b: 890.
    • (1965) Z. Naturforsch. , vol.20 B , pp. 890
    • Urbach, W.1    Hudson, M.A.2    Ullrich, W.3    Santarius, K.A.4    Heber, U.5
  • 206
    • 85032068397 scopus 로고
    • UDP-glucose pyrophosphorylase from the plant fractions of nitrogen-fixing soybean modules
    • Vella, J. and Copeland, L. 1990. UDP-glucose pyrophosphorylase from the plant fractions of nitrogen-fixing soybean modules. Physiol. Plant. 78: 140.
    • (1990) Physiol. Plant. , vol.78 , pp. 140
    • Vella, J.1    Copeland, L.2
  • 207
    • 0026875704 scopus 로고
    • PCR-amplification and sequences of cDNA clones for the small and large subunits of AGPase from barley tissues
    • Villand, P., Aalen, R., Olsen, O. A., Lonneborg, A., Luthi, E., and Kleczkowski, L. A. 1992. PCR-amplification and sequences of cDNA clones for the small and large subunits of AGPase from barley tissues. Plant Mol. Biol. 19: 381-389.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 381-389
    • Villand, P.1    Aalen, R.2    Olsen, O.A.3    Lonneborg, A.4    Luthi, E.5    Kleczkowski, L.A.6
  • 208
    • 0028092299 scopus 로고
    • Is there an alternative pathway for starch biosynthesis in cereal seeds?
    • Villand R. and Kleczkowski, L. A. 1993. Is there an alternative pathway for starch biosynthesis in cereal seeds? Z. Naturforsch. 49: 215-219.
    • (1993) Z. Naturforsch. , vol.49 , pp. 215-219
    • Villand, R.1    Kleczkowski, L.A.2
  • 209
    • 34249924858 scopus 로고
    • Pathways of starch and sucrose biosynthesis in developing tubers of potato (Solanum tuberosum L.) and seeds of faba bean (Vicia faba L.)
    • Viola, R., Davies, H. W., and Chudek, A. R. 1991. Pathways of starch and sucrose biosynthesis in developing tubers of potato (Solanum tuberosum L.) and seeds of faba bean (Vicia faba L.). Planta 183: 202-208.
    • (1991) Planta , vol.183 , pp. 202-208
    • Viola, R.1    Davies, H.W.2    Chudek, A.R.3
  • 210
    • 0026027970 scopus 로고
    • Inhibition of the expression of the gene for granule-bound starch synthase in potato by antisense constructs
    • Visser, R. G., Somhorst, F. 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.1    Somhorst, F.I.2    Kuipers, G.J.3    Ruys, N.J.4    Feenstra, W.J.5    Jacobsen, E.6
  • 211
    • 0004487542 scopus 로고    scopus 로고
    • Tell me where all past years are
    • Walker, D. A. 1997. Tell me where all past years are. Photosynth. Res. 51: 1-26.
    • (1997) Photosynth. Res. , vol.51 , pp. 1-26
    • Walker, D.A.1
  • 213
    • 0000785628 scopus 로고
    • Sucrose synthase, starch accumulation, and tomato fruit sink strength
    • Wang, F., Sanz, A., Brenner, M. L., and Smith. A. 1993. Sucrose synthase, starch accumulation, and tomato fruit sink strength. Plant Physiol. 101: 321-327.
    • (1993) Plant Physiol. , vol.101 , pp. 321-327
    • Wang, F.1    Sanz, A.2    Brenner, M.L.3    Smith, A.4
  • 214
    • 0001197431 scopus 로고
    • Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves
    • Weiner, H., Stitt, M., and Heldt, H. W. 1987. Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves. Biochim. Biophys. Acta 893: 18-21.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 18-21
    • Weiner, H.1    Stitt, M.2    Heldt, H.W.3
  • 215
    • 0029107792 scopus 로고
    • Evidence of the crucial role of sucrose synthase for sink strength using transgenic pototo 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 pototo 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
  • 216
    • 0027346055 scopus 로고
    • Analysis of the expression of potato uridine-diphosphate-glucose pyrophosphorylase and its inhibition by antisense RNA
    • Zrenner, R., Willmitzer, L., and Sonnewald, U. 1993. Analysis of the expression of potato uridine-diphosphate-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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.