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Volumn 5, Issue 7, 2000, Pages 291-298

Engineering starch for increased quantity and quality

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL PATHWAY; CARBOHYDRATE SYNTHESIS; GENETIC MANIPULATION; METABOLIC ENGINEERING; STARCH; TRANSGENE;

EID: 0034235937     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(00)01657-5     Document Type: Review
Times cited : (151)

References (57)
  • 1
    • 0027551706 scopus 로고
    • Towards modifying plants for altered starch content and composition
    • Visser R.G.F., Jacobsen E. Towards modifying plants for altered starch content and composition. Trends Biotechnol. 11:1993;63-68.
    • (1993) Trends Biotechnol. , vol.11 , pp. 63-68
    • Visser, R.G.F.1    Jacobsen, E.2
  • 2
    • 84994964585 scopus 로고
    • Approaches to influence starch quantity and starch quality in transgenic plants
    • Müller-Röber B., Koßmann J. Approaches to influence starch quantity and starch quality in transgenic plants. Plant Cell Environ. 17:1994;601-613.
    • (1994) Plant Cell Environ. , vol.17 , pp. 601-613
    • Müller-Röber, B.1    Koßmann, J.2
  • 3
    • 0002969050 scopus 로고
    • High amylose and waxy corns
    • A.R. Hallauer. CRC Press
    • Fergason V. High amylose and waxy corns. Hallauer A.R. Specialty Corns. 1994;55-77 CRC Press.
    • (1994) Specialty Corns , pp. 55-77
    • Fergason, V.1
  • 6
    • 0001260817 scopus 로고
    • Is there an alternative pathway for starch synthesis?
    • Okita T.W. Is there an alternative pathway for starch synthesis? Plant Physiol. 100:1992;560-564.
    • (1992) Plant Physiol. , vol.100 , pp. 560-564
    • Okita, T.W.1
  • 7
    • 0025784801 scopus 로고
    • Starch biosynthesis and its regulation
    • Preiss J.et al. Starch biosynthesis and its regulation. Biochem. Soc. Trans. 19:1991;539-547.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 539-547
    • Preiss, J.1
  • 8
    • 0017151912 scopus 로고
    • Characterization of ADP-glucose pyrophosphorylase from Shrunken-2 and Brittle-2 mutants of maize
    • Hannah L.C., Nelson O.E. Characterization of ADP-glucose pyrophosphorylase from Shrunken-2 and Brittle-2 mutants of maize. Biochem. Genet. 14:1976;547-560.
    • (1976) Biochem. Genet. , vol.14 , pp. 547-560
    • Hannah, L.C.1    Nelson, O.E.2
  • 9
    • 0027398378 scopus 로고
    • Expression of the potato tuber ADP-glucose pyrophosphorylase in Escherichia coli
    • Iglesias A.A.et al. Expression of the potato tuber ADP-glucose pyrophosphorylase in Escherichia coli. J. Biol. Chem. 268:1993;1081-1086.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1081-1086
    • Iglesias, A.A.1
  • 10
    • 0000388198 scopus 로고
    • Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm
    • Plaxton W.C., Preiss J. Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm. Plant Physiol. 83:1987;105-112.
    • (1987) Plant Physiol. , vol.83 , pp. 105-112
    • Plaxton, W.C.1    Preiss, J.2
  • 11
    • 0002684202 scopus 로고
    • 3-Phosphoglyceric acid activation of maize endosperm ADP-glucose pyrophosphorylase following proteolytic cleavage of the SH2 or BT2 subunits
    • H.D. et al. Pontis. American Society of Plant Physiologists
    • Hannah L.C.et al. 3-Phosphoglyceric acid activation of maize endosperm ADP-glucose pyrophosphorylase following proteolytic cleavage of the SH2 or BT2 subunits. Pontis H.D.et al. Sucrose Metabolism, Biochemistry and Molecular Biology (Vol.14). 1995;72-79 American Society of Plant Physiologists.
    • (1995) Sucrose Metabolism, Biochemistry and Molecular Biology (Vol.14) , pp. 72-79
    • Hannah, L.C.1
  • 12
    • 0027139421 scopus 로고
    • Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation
    • Kleczkowski L.A.et al. Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation. Plant Physiol. 101:1993;179-186.
    • (1993) Plant Physiol. , vol.101 , pp. 179-186
    • Kleczkowski, L.A.1
  • 13
    • 0001608011 scopus 로고
    • Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm
    • Olive M.et al. Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm. Plant Mol. Biol. 12:1989;525-538.
    • (1989) Plant Mol. Biol. , vol.12 , pp. 525-538
    • Olive, M.1
  • 14
    • 0001387246 scopus 로고
    • Immunocytochemical localization of ADPglucose pyrophosphorylase in developing potato tuber cells
    • -220
    • Kim W.T.et al. Immunocytochemical localization of ADPglucose pyrophosphorylase in developing potato tuber cells. Plant Physiol. 91:1989;217. -220.
    • (1989) Plant Physiol. , vol.91 , pp. 217
    • Kim, W.T.1
  • 15
    • 0001481929 scopus 로고
    • Major differences in isoforms of starch branching enzyme between developing embryos of round- and wrinkled-seeded peas (Pisum sativum. L)
    • Smith A.M. Major differences in isoforms of starch branching enzyme between developing embryos of round- and wrinkled-seeded peas (Pisum sativum. L). Planta. 175:1988;270-279.
    • (1988) Planta , vol.175 , pp. 270-279
    • Smith, A.M.1
  • 16
    • 0030267532 scopus 로고    scopus 로고
    • The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial
    • Denyer K.et al. The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial. Plant Physiol. 112:1996;779-785.
    • (1996) Plant Physiol. , vol.112 , pp. 779-785
    • Denyer, K.1
  • 17
    • 0030483916 scopus 로고    scopus 로고
    • Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm
    • Thorbjornsen T.et al. Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm. Plant J. 10:1996;243-250.
    • (1996) Plant J. , vol.10 , pp. 243-250
    • Thorbjornsen, T.1
  • 18
    • 0015988432 scopus 로고
    • The function of the waxy locus in starch synthesis in maize endosperm
    • Tsai C.Y. The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11:1974;83-96.
    • (1974) Biochem. Genet. , vol.11 , pp. 83-96
    • Tsai, C.Y.1
  • 19
    • 0032029094 scopus 로고    scopus 로고
    • Mutations in the gene encoding starch synthase II profoundly alter amylopectin structure in pea embryos
    • Craig J.et al. Mutations in the gene encoding starch synthase II profoundly alter amylopectin structure in pea embryos. Plant Cell. 10:1998;413-426.
    • (1998) Plant Cell , vol.10 , pp. 413-426
    • Craig, J.1
  • 20
    • 0032029093 scopus 로고    scopus 로고
    • Characterization of dull1, a maize mutant gene coding for a novel starch synthase
    • Gao M.et al. Characterization of dull1, a maize mutant gene coding for a novel starch synthase. Plant Cell. 10:1998;399-412.
    • (1998) Plant Cell , vol.10 , pp. 399-412
    • Gao, M.1
  • 21
    • 0027203773 scopus 로고
    • Toward an understanding of the biogenesis of the starch granule. Evidence that Chlamydomonas soluble starch synthase II controls the synthesis of intermediate size glucans of amylopectin
    • Fontaine T.et al. Toward an understanding of the biogenesis of the starch granule. Evidence that Chlamydomonas soluble starch synthase II controls the synthesis of intermediate size glucans of amylopectin. J. Biol. Chem. 268:1993;16223-16230.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16223-16230
    • Fontaine, T.1
  • 22
    • 0041154130 scopus 로고    scopus 로고
    • Simultaneous antisense inhibition of two starch synthase isoforms in potato tuber leads to accumulation of grossly modified amylopectin
    • Lloyd J.R.et al. Simultaneous antisense inhibition of two starch synthase isoforms in potato tuber leads to accumulation of grossly modified amylopectin. Biochem. J. 338:1999;515-521.
    • (1999) Biochem. J. , vol.338 , pp. 515-521
    • Lloyd, J.R.1
  • 23
    • 0033028207 scopus 로고    scopus 로고
    • A combined reduction in activity of starch synthases II and III of potato has novel effects on the starch of tubers
    • Edwards A.et al. A combined reduction in activity of starch synthases II and III of potato has novel effects on the starch of tubers. Plant J. 17:1999;251-261.
    • (1999) Plant J. , vol.17 , pp. 251-261
    • Edwards, A.1
  • 24
    • 0025101773 scopus 로고
    • The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch branching enzyme
    • Bhattacharyya M.K.et al. The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch branching enzyme. Cell. 60:1990;115-122.
    • (1990) Cell , vol.60 , pp. 115-122
    • Bhattacharyya, M.K.1
  • 25
    • 0027247801 scopus 로고
    • Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds
    • Mizuno K.et al. Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds. J. Biol. Chem. 268:1993;19084-19091.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19084-19091
    • Mizuno, K.1
  • 26
    • 0029140539 scopus 로고
    • Starch branching enzymes belonging to distinct enzyme families are differentially expressed during pea embryo development
    • Burton R.A.et al. Starch branching enzymes belonging to distinct enzyme families are differentially expressed during pea embryo development. Plant J. 7:1995;3-15.
    • (1995) Plant J. , vol.7 , pp. 3-15
    • Burton, R.A.1
  • 27
    • 0029328417 scopus 로고
    • Starch biosynthesis
    • Martin C., Smith A.M. Starch biosynthesis. Plant Cell. 7:1995;971-985.
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 28
    • 0000361233 scopus 로고
    • Differentiation of the properties of the branching isozymes from maize (Zea mays)
    • Guan H.P., Preiss J. Differentiation of the properties of the branching isozymes from maize (Zea mays). Plant Physiol. 102:1993;1269-1273.
    • (1993) Plant Physiol , vol.102 , pp. 1269-1273
    • Guan, H.P.1    Preiss, J.2
  • 29
    • 0000586974 scopus 로고
    • Evidence for independent genetic control of the multiple forms of maize endosperm starch branching enzymes and starch synthases
    • Boyer C., Preiss J. Evidence for independent genetic control of the multiple forms of maize endosperm starch branching enzymes and starch synthases. Plant Physiol. 67:1981;1141-1145.
    • (1981) Plant Physiol. , vol.67 , pp. 1141-1145
    • Boyer, C.1    Preiss, J.2
  • 30
    • 0032748917 scopus 로고    scopus 로고
    • The starch debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm
    • Kubo A.et al. The starch debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm. Plant Physiol. 121:1999;399-409.
    • (1999) Plant Physiol , vol.121 , pp. 399-409
    • Kubo, A.1
  • 31
    • 0029823269 scopus 로고    scopus 로고
    • Preamylopectin processing: A mandatory step for starch biosynthesis in plants
    • Mouille G.et al. Preamylopectin processing. a mandatory step for starch biosynthesis in plants Plant Cell. 8:1996;1353-1366.
    • (1996) Plant Cell , vol.8 , pp. 1353-1366
    • Mouille, G.1
  • 32
    • 0030576530 scopus 로고    scopus 로고
    • From glycogen to amylopectin: A model for the biogenesis of the plant starch granule
    • Ball S.et al. From glycogen to amylopectin. a model for the biogenesis of the plant starch granule Cell. 86:1996;349-352.
    • (1996) Cell , vol.86 , pp. 349-352
    • Ball, S.1
  • 33
    • 0032192047 scopus 로고    scopus 로고
    • A mutant Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen
    • Zeeman S.C.et al. A mutant Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen. Plant Cell. 10:1998;1699-1711.
    • (1998) Plant Cell , vol.10 , pp. 1699-1711
    • Zeeman, S.C.1
  • 34
    • 0026533580 scopus 로고
    • Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes
    • Müller-Röber B.et al. Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes. EMBO J. 11:1992;1229-1238.
    • (1992) EMBO J. , vol.11 , pp. 1229-1238
    • Müller-Röber, B.1
  • 35
    • 0026458333 scopus 로고
    • Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase
    • Stark D.M.et al. Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase. Science. 258:1992;287-292.
    • (1992) Science , vol.258 , pp. 287-292
    • Stark, D.M.1
  • 36
    • 0029902429 scopus 로고    scopus 로고
    • Starch metabolism in tubers of transgenic potato (Solanum tuberosum) with increased ADPglucose pyrophosphorylase
    • Sweetlove L.J.et al. Starch metabolism in tubers of transgenic potato (Solanum tuberosum) with increased ADPglucose pyrophosphorylase. Biochem. J. 320:1996;493-498.
    • (1996) Biochem. J. , vol.320 , pp. 493-498
    • Sweetlove, L.J.1
  • 37
    • 0030579802 scopus 로고    scopus 로고
    • A single gene mutation that increases maize seed weight
    • Giroux M.J.et al. A single gene mutation that increases maize seed weight. Proc. Natl. Acad. Sci. U.S.A. 93:1996;5824-5829.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5824-5829
    • Giroux, M.J.1
  • 38
    • 0040559800 scopus 로고    scopus 로고
    • The contribution of adenosine 5′-diphosphoglucose pyrophosphorylase to the control of starch synthesis in potato tubers
    • Sweetlove L.J.et al. The contribution of adenosine 5′-diphosphoglucose pyrophosphorylase to the control of starch synthesis in potato tubers. Planta. 209:1999;330-337.
    • (1999) Planta , vol.209 , pp. 330-337
    • Sweetlove, L.J.1
  • 39
    • 0032544014 scopus 로고    scopus 로고
    • Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics
    • Greene T.W.et al. Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics. Proc. Natl. Acad. Sci. U.S.A. 95:1998;10322-10327.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10322-10327
    • Greene, T.W.1
  • 40
    • 0032573220 scopus 로고    scopus 로고
    • Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
    • Greene T.W., Hannah L.C. Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions. Proc. Natl. Acad. Sci. U.S.A. 95:1998;13342-13347.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13342-13347
    • Greene, T.W.1    Hannah, L.C.2
  • 41
    • 0032007679 scopus 로고    scopus 로고
    • Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase
    • Laughlin M.J.et al. Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase. Phytochemistry. 47:1998;621-629.
    • (1998) Phytochemistry , vol.47 , pp. 621-629
    • Laughlin, M.J.1
  • 42
    • 0029360584 scopus 로고
    • Adenosine 5′-diphosphate-glucose pyrophosphorylase from potato tuber: Significance of the N-terminus of the small subunit for catalytic properties and heat stability
    • Ballicora M.A.et al. Adenosine 5′-diphosphate-glucose pyrophosphorylase from potato tuber. significance of the N-terminus of the small subunit for catalytic properties and heat stability Plant Physiol. 109:1995;245-251.
    • (1995) Plant Physiol. , vol.109 , pp. 245-251
    • Ballicora, M.A.1
  • 43
    • 0032867095 scopus 로고    scopus 로고
    • The influence of alterations in ADP-glucose pyrophosphorylase activities on starch structure and composition in potato tubers
    • Lloyd J.R.et al. The influence of alterations in ADP-glucose pyrophosphorylase activities on starch structure and composition in potato tubers. Planta. 209:1999;230-238.
    • (1999) Planta , vol.209 , pp. 230-238
    • Lloyd, J.R.1
  • 44
    • 0032825955 scopus 로고    scopus 로고
    • The relationship between the rate of starch synthesis, the adenosine 5′-diphosphoglucose concentration and the amylose content of starch in developing pea embryos
    • Clarke B.R.et al. The relationship between the rate of starch synthesis, the adenosine 5′-diphosphoglucose concentration and the amylose content of starch in developing pea embryos. Planta. 209:1999;324-329.
    • (1999) Planta , vol.209 , pp. 324-329
    • Clarke, B.R.1
  • 45
    • 0033572794 scopus 로고    scopus 로고
    • Specificity of starch synthase isoforms from potato
    • Edwards A.et al. Specificity of starch synthase isoforms from potato. Eur. J. Biochem. 266:1999;724-736.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 724-736
    • Edwards, A.1
  • 46
    • 0033119569 scopus 로고    scopus 로고
    • A minor form of starch branching enzyme in potato (Solanum tuberosum L.) tubers has a major effect on starch structure: Cloning and characterisation of multiple forms of SBE A.
    • Jobling S.A. A minor form of starch branching enzyme in potato (Solanum tuberosum L.) tubers has a major effect on starch structure: cloning and characterisation of multiple forms of SBE A. Plant J. 18:1999;163-171.
    • (1999) Plant J. , vol.18 , pp. 163-171
    • Jobling, S.A.1
  • 47
    • 0030613631 scopus 로고    scopus 로고
    • Construction of chimeric enzymes out of maize endosperm branching enzymes I and II: Activity and properties
    • Kuriki T.et al. Construction of chimeric enzymes out of maize endosperm branching enzymes I and II. activity and properties J. Biol. Chem. 272:1997;28999-29004.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28999-29004
    • Kuriki, T.1
  • 48
    • 0032439289 scopus 로고    scopus 로고
    • Altered plastidic ATP/ADP transporter activity influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch
    • Tjaden J.et al. Altered plastidic ATP/ADP transporter activity influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch. Plant J. 16:1998;531-540.
    • (1998) Plant J. , vol.16 , pp. 531-540
    • Tjaden, J.1
  • 49
    • 0032134257 scopus 로고    scopus 로고
    • Brittle-1, an adenylate translocator, facilitates transfer of extraplastidial synthesized ADP-glucose into amyloplasts of maize endosperms
    • Shannon J.C.et al. Brittle-1, an adenylate translocator, facilitates transfer of extraplastidial synthesized ADP-glucose into amyloplasts of maize endosperms. Plant Physiol. 117:1998;1235-1252.
    • (1998) Plant Physiol. , vol.117 , pp. 1235-1252
    • Shannon, J.C.1
  • 50
    • 0032127317 scopus 로고    scopus 로고
    • Overexpression of pyrophosphatase leads to increased sucrose degradaion and starch synthesis, increased activities of enzymes for sucrose-starch interconversions, and increase levels of nucleotides in growing potato tubers
    • Geigenberger P.et al. Overexpression of pyrophosphatase leads to increased sucrose degradaion and starch synthesis, increased activities of enzymes for sucrose-starch interconversions, and increase levels of nucleotides in growing potato tubers. Planta. 205:1998;428-437.
    • (1998) Planta , vol.205 , pp. 428-437
    • Geigenberger, P.1
  • 51
    • 0032825479 scopus 로고    scopus 로고
    • Orotate leads to a specific increase in uridine nucleotide levels and a stimulation of sucrose degradation and starch synthesis in discs from growing potato tubers
    • Loef I.et al. Orotate leads to a specific increase in uridine nucleotide levels and a stimulation of sucrose degradation and starch synthesis in discs from growing potato tubers. Planta. 209:1999;314-323.
    • (1999) Planta , vol.209 , pp. 314-323
    • Loef, I.1
  • 52
    • 13044272911 scopus 로고    scopus 로고
    • Genetic and biochemical evidence for the involvement of the α-1,4 glucanotransferases in amylopectin synthesis
    • Colleoni C.et al. Genetic and biochemical evidence for the involvement of the α-1,4 glucanotransferases in amylopectin synthesis. Plant Physiol. 120:1999;993-1003.
    • (1999) Plant Physiol. , vol.120 , pp. 993-1003
    • Colleoni, C.1
  • 53
    • 0031833364 scopus 로고    scopus 로고
    • Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase)
    • Takaha T.et al. Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase). Planta. 205:1998;445-451.
    • (1998) Planta , vol.205 , pp. 445-451
    • Takaha, T.1
  • 54
    • 0032543440 scopus 로고    scopus 로고
    • Cyclic glucans produced by the intramolecular transglycosylation activity of potato D-enzyme on amylopectin
    • Takaha T.et al. Cyclic glucans produced by the intramolecular transglycosylation activity of potato D-enzyme on amylopectin. Biochem. Biophys. Res. Commun. 247:1998;493-497.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 493-497
    • Takaha, T.1
  • 55
    • 0034123997 scopus 로고    scopus 로고
    • Reversible binding of the starch-related R1 protein to the surface of transitory starch granules
    • Ritte G.et al. Reversible binding of the starch-related R1 protein to the surface of transitory starch granules. Plant J. 21:2000;387-391.
    • (2000) Plant J. , vol.21 , pp. 387-391
    • Ritte, G.1
  • 56
    • 0031921128 scopus 로고    scopus 로고
    • Inhibition of a starch granule-bound protein leads to modified starch and repression of cold sweetening
    • Lorberth R.et al. Inhibition of a starch granule-bound protein leads to modified starch and repression of cold sweetening. Nat. Biotechnol. 16:1998;473-477.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 473-477
    • Lorberth, R.1
  • 57
    • 0028038926 scopus 로고
    • Fructan as a new carbohydrate in transgenic potato plants
    • van der Meer I.M.et al. Fructan as a new carbohydrate in transgenic potato plants. Plant Cell. 6:1994;561-570.
    • (1994) Plant Cell , vol.6 , pp. 561-570
    • Van Der Meer, I.M.1


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