메뉴 건너뛰기




Volumn 55, Issue 3-4, 2003, Pages 107-120

Synthesis of novel starches in planta: Opportunities and challenges

Author keywords

Starch granule; Starch modification; Starch synthesis; Starch transformation

Indexed keywords

BIOSYNTHESIS; CARBOHYDRATES; COMPOSITION; CROPS; FATTY ACIDS; GENETIC ENGINEERING; NUTRITION; PLANTS (BOTANY); POLYMERIZATION;

EID: 0346196464     PISSN: 00389056     EISSN: None     Source Type: Journal    
DOI: 10.1002/star.200390036     Document Type: Review
Times cited : (76)

References (141)
  • 2
    • 0033246747 scopus 로고    scopus 로고
    • Processing biodegradable packaging material from starches using extrusion technology
    • M. N. Riaz: Processing biodegradable packaging material from starches using extrusion technology. Cereal Foods World 1999, 44, 705-709.
    • (1999) Cereal Foods World , vol.44 , pp. 705-709
    • Riaz, M.N.1
  • 3
    • 0001114581 scopus 로고
    • Purification and structure of amylose from rice starch
    • Y. Takeda, S. Hizukuri, B. O. Juliano: Purification and structure of amylose from rice starch. Carbohydr. Res. 1986, 148, 299-308.
    • (1986) Carbohydr. Res. , vol.148 , pp. 299-308
    • Takeda, Y.1    Hizukuri, S.2    Juliano, B.O.3
  • 4
    • 0000195804 scopus 로고
    • Structures of branched molecules of amylose of various origins and molar fractions of branched and unbranched fractions
    • Y. Takeda, S. Hizukuri: Structures of branched molecules of amylose of various origins and molar fractions of branched and unbranched fractions. Carbohydr. Res. 1987, 165, 139-145.
    • (1987) Carbohydr. Res. , vol.165 , pp. 139-145
    • Takeda, Y.1    Hizukuri, S.2
  • 6
    • 21844514376 scopus 로고
    • Potato starch: New prospects for an old product
    • R. J. Alexander: Potato starch: new prospects for an old product. Cereal Foods World 1995, 40, 763-764.
    • (1995) Cereal Foods World , vol.40 , pp. 763-764
    • Alexander, R.J.1
  • 7
    • 0034003526 scopus 로고    scopus 로고
    • Recent progress toward understanding biosynthesis of the amylopectin crystal
    • A. M. Myers, M. K. Morell, M. G. James, S. G. Ball: Recent progress toward understanding biosynthesis of the amylopectin crystal. Plant Physiol. 2000, 122, 989-997.
    • (2000) Plant Physiol. , vol.122 , pp. 989-997
    • Myers, A.M.1    Morell, M.K.2    James, M.G.3    Ball, S.G.4
  • 8
    • 0001698419 scopus 로고
    • Relationship between the distribution of the chain length of amylopectin and the crystalline structure of starch granules
    • S. Hizukuri: Relationship between the distribution of the chain length of amylopectin and the crystalline structure of starch granules. Carbohydr. Res. 1985, 141, 295-306.
    • (1985) Carbohydr. Res. , vol.141 , pp. 295-306
    • Hizukuri, S.1
  • 10
    • 0000472373 scopus 로고
    • A rare carbohydrate in maize
    • P. Weatherwax: A rare carbohydrate in maize. Genetics 1922, 7, 568-572.
    • (1922) Genetics , vol.7 , pp. 568-572
    • Weatherwax, P.1
  • 11
    • 0001538696 scopus 로고
    • Enzymic mechanism of starch synthesis in glutinous rice grains
    • T. Murata, T. Sugiyama, T. Akazawa: Enzymic mechanism of starch synthesis in glutinous rice grains. Biochem. Biophys. Res. Commun. 1965, 18, 371-376.
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 371-376
    • Murata, T.1    Sugiyama, T.2    Akazawa, T.3
  • 12
    • 0001960478 scopus 로고
    • Endosperm characters in hybrids between barley varieties with starchy and waxy endosperms
    • T. Ono, H. Suzuki: Endosperm characters in hybrids between barley varieties with starchy and waxy endosperms. Seihen Ziho1957, 8, 11-19.
    • (1957) Seihen Ziho , vol.8 , pp. 11-19
    • Ono, T.1    Suzuki, H.2
  • 15
    • 0001323715 scopus 로고
    • Characterization of starch granules from waxy, non-waxy and hybrid seeds of Amaranthus hypochondriacus
    • Y. Konishi, H. Nojima, K. Okuno, M. Asaoka, H. Fuwa: Characterization of starch granules from waxy, non-waxy and hybrid seeds of Amaranthus hypochondriacus L. Agric. Biol. Chem. 1985, 49, 1965-1971.
    • (1985) L. Agric. Biol. Chem. , vol.49 , pp. 1965-1971
    • Konishi, Y.1    Nojima, H.2    Okuno, K.3    Asaoka, M.4    Fuwa, H.5
  • 16
    • 0002021185 scopus 로고
    • Starch: Chemistry and technology
    • (Eds. R. L. Whistler, J. N. BeMiller, E. F. Paschall), Academic Press, Orlando, Fl
    • J. C. Shannon, D. L. Garwood: Starch: Chemistry and technology, in Genetics and Physiology of Starch Development (Eds. R. L. Whistler, J. N. BeMiller, E. F. Paschall), Academic Press, Orlando, Fl., 1984.
    • (1984) Genetics and Physiology of Starch Development
    • Shannon, J.C.1    Garwood, D.L.2
  • 18
    • 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
    • M. K. Bhattacharyya, A. M. Smith, T. H. N. Ellis, C. Hedley, C. Martin: The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch branching enzyme. Cell 1990, 60, 115-121.
    • (1990) Cell , vol.60 , pp. 115-121
    • Bhattacharyya, M.K.1    Smith, A.M.2    Ellis, T.H.N.3    Hedley, C.4    Martin, C.5
  • 19
    • 0031826891 scopus 로고    scopus 로고
    • Effect of wheat starch structure on swelling power
    • T. Sasaki, J. Matsuki: Effect of wheat starch structure on swelling power. Cereal Chem. 1998, 75, 525-529.
    • (1998) Cereal Chem. , vol.75 , pp. 525-529
    • Sasaki, T.1    Matsuki, J.2
  • 21
    • 21844488215 scopus 로고
    • Starch lipids and how they relate to starch granule structure and functionality
    • W. R. Morrison, Starch lipids and how they relate to starch granule structure and functionality. Cereal Foods World 1995, 40, 437-446.
    • (1995) Cereal Foods World , vol.40 , pp. 437-446
    • Morrison, W.R.1
  • 23
    • 0001228002 scopus 로고
    • Location of phosphate groups in potato amylopectin
    • Y. Takeda, S. Hizukuri: Location of phosphate groups in potato amylopectin. Carbohydr. Res. 1982, 102, 321-327.
    • (1982) Carbohydr. Res. , vol.102 , pp. 321-327
    • Takeda, Y.1    Hizukuri, S.2
  • 24
    • 0000837914 scopus 로고    scopus 로고
    • Characterization of the difference of starch branching enzyme activities in normal and low amylopectin maize during kernel development
    • C. Sidebottom, M. Kirkland, B. Strongitharm, R. Jeffcoat: Characterization of the difference of starch branching enzyme activities in normal and low amylopectin maize during kernel development. J. Cereal Sci. 1998, 27, 279-287.
    • (1998) J. Cereal Sci. , vol.27 , pp. 279-287
    • Sidebottom, C.1    Kirkland, M.2    Strongitharm, B.3    Jeffcoat, R.4
  • 27
    • 0026585394 scopus 로고
    • Starch granules large and small
    • J. P. Stark, A. Lynn: Starch granules large and small. Biochem. Soc. Trans. 1992, 20, 7-12.
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 7-12
    • Stark, J.P.1    Lynn, A.2
  • 28
    • 84983947887 scopus 로고
    • The size distribution among starch granules in wheat endosperm
    • A. D. Evers: The size distribution among starch granules in wheat endosperm. Stärke 1973, 25, 303-304.
    • (1973) Stärke , vol.25 , pp. 303-304
    • Evers, A.D.1
  • 30
    • 0344542064 scopus 로고    scopus 로고
    • Granule size distribution and chemical composition of starches from 12 soft wheat cultivars
    • M. O. Raeker, C. S. Gaines, P. L. Finney, T. Donelson: Granule size distribution and chemical composition of starches from 12 soft wheat cultivars. Cereal Chem. 1998, 75, 721-728.
    • (1998) Cereal Chem. , vol.75 , pp. 721-728
    • Raeker, M.O.1    Gaines, C.S.2    Finney, P.L.3    Donelson, T.4
  • 31
    • 0000734757 scopus 로고    scopus 로고
    • Influence of starch granule size distribution on bread characteristics
    • S. Sahlstrom, E. Brathen, P. Lea, K. Autio: Influence of starch granule size distribution on bread characteristics. J. Cereal Sci. 1998, 28, 157-164.
    • (1998) J. Cereal Sci. , vol.28 , pp. 157-164
    • Sahlstrom, S.1    Brathen, E.2    Lea, P.3    Autio, K.4
  • 32
    • 0033025439 scopus 로고    scopus 로고
    • Separation and characterization of A- And B-type starch granules in wheat endosperm
    • M. Peng, M. Gao, E.- S. M. Abdel-Aal, P. Hucl, R. N. Chibbar: Separation and characterization of A- and B-type starch granules in wheat endosperm. Cereal Chem. 1999, 76, 375-379.
    • (1999) Cereal Chem. , vol.76 , pp. 375-379
    • Peng, M.1    Gao, M.2    Abdel-Aal, E.S.M.3    Hucl, P.4    Chibbar, R.N.5
  • 33
    • 0030803741 scopus 로고    scopus 로고
    • Sources of variation for starch gelatinization, pasting and gelation properties in wheat
    • M. Zeng, C. F. Morris, I. L. Batty, C. W. Wrigley: Sources of variation for starch gelatinization, pasting and gelation properties in wheat. Cereal Chem. 1997, 74, 63-71.
    • (1997) Cereal Chem. , vol.74 , pp. 63-71
    • Zeng, M.1    Morris, C.F.2    Batty, I.L.3    Wrigley, C.W.4
  • 34
    • 0037102816 scopus 로고    scopus 로고
    • Structural and physical characteristics of waxy and other wheat starches
    • S.-H. Yoo, J.-L. Jane: Structural and physical characteristics of waxy and other wheat starches. Carbohydr. Polym. 2002, 49, 297-305.
    • (2002) Carbohydr. Polym. , vol.49 , pp. 297-305
    • Yoo, S.-H.1    Jane, J.-L.2
  • 35
    • 0002591153 scopus 로고
    • Effect of amylose molecular size and amylopectin branch length on paste properties of starch
    • J.-L. Jane, J.-F. Chen: Effect of amylose molecular size and amylopectin branch length on paste properties of starch. Cereal Chem. 1992, 69, 60-65.
    • (1992) Cereal Chem. , vol.69 , pp. 60-65
    • Jane, J.-L.1    Chen, J.-F.2
  • 36
    • 0031921128 scopus 로고    scopus 로고
    • Inhibition of a starch granule-bound protein leads to modified starch and repression of cold sweetening
    • R. Lorberth, G. Ritte, L. Willmitzer, J. Kossman: Inhibition of a starch granule-bound protein leads to modified starch and repression of cold sweetening. Nat. Biotechnol. 1998, 16, 473-477.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 473-477
    • Lorberth, R.1    Ritte, G.2    Willmitzer, L.3    Kossman, J.4
  • 37
    • 0345318773 scopus 로고
    • Compositional and morphological characterization of cow cockle (Saponaria vacaria) seed, a potential alternative crop
    • G. Mazza, C. G. Biliaderis, R. Przybylski, B. D. Oomah: Compositional and morphological characterization of cow cockle (Saponaria vacaria) seed, a potential alternative crop. J. Agric. Food Chem. 1992, 40, 1520-1523.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1520-1523
    • Mazza, G.1    Biliaderis, C.G.2    Przybylski, R.3    Oomah, B.D.4
  • 38
    • 84989103443 scopus 로고
    • Starch as a stilt material in carbonless copy paper - New developments
    • W. Nachtergaele, J. Van Nuffel: Starch as a stilt material in carbonless copy paper - new developments. Starch/Stärke 1989, 41, 386-392.
    • (1989) Starch/Stärke , vol.41 , pp. 386-392
    • Nachtergaele, W.1    Van Nuffel, J.2
  • 40
    • 0026692328 scopus 로고
    • Effect of starch granule size on physical properties of starch-filled polyethylene film
    • S. T. Lim, J.-L: Jane, S. Rajagopalan, P. A. Seib: Effect of starch granule size on physical properties of starch-filled polyethylene film. Biotechnol. Progr. 1992, 8, 51-57.
    • (1992) Biotechnol. Progr. , vol.8 , pp. 51-57
    • Lim, S.T.1    Jane, J.-L.2    Rajagopalan, S.3    Seib, P.A.4
  • 41
    • 84985633296 scopus 로고
    • Degradable polymers of the future
    • A.-C. Albertsson, S. Karlsson: Degradable polymers of the future. Acta Polym. 1995, 46, 114-123.
    • (1995) Acta Polym. , vol.46 , pp. 114-123
    • Albertsson, A.-C.1    Karlsson, S.2
  • 42
    • 0030295336 scopus 로고    scopus 로고
    • Developments in the understanding of starch functionality
    • A.-M. Hermansson, K. Svegmark: Developments in the understanding of starch functionality. Trends Food Sci. 1996, 7, 345-353.
    • (1996) Trends Food Sci. , vol.7 , pp. 345-353
    • Hermansson, A.-M.1    Svegmark, K.2
  • 43
    • 0030431032 scopus 로고    scopus 로고
    • Complex carbohydrates and resistant starch
    • I. Brown: Complex carbohydrates and resistant starch. Nutrition Rev. 1996, 54, S115-S119.
    • (1996) Nutrition Rev. , vol.54
    • Brown, I.1
  • 44
    • 0034235937 scopus 로고    scopus 로고
    • Engineering starch for increased quantity and quality
    • C. J. Slattery, H. Kavakli, T. W. Okita: Engineering starch for increased quantity and quality. Trends Plant Sci. 2000, 5, 291-298.
    • (2000) Trends Plant Sci. , vol.5 , pp. 291-298
    • Slattery, C.J.1    Kavakli, H.2    Okita, T.W.3
  • 45
    • 0007272445 scopus 로고
    • Cereal starches within the European Community - Agricultural production, dry and wet milling and potential use in industry
    • L. Munck, F. Rexen, L. Haastrup: Cereal starches within the European Community - agricultural production, dry and wet milling and potential use in industry. Starch/Stärke 1988, 40, 81-87.
    • (1988) Starch/Stärke , vol.40 , pp. 81-87
    • Munck, L.1    Rexen, F.2    Haastrup, L.3
  • 46
    • 0030288603 scopus 로고    scopus 로고
    • Filling of poly(lactic acid) with native starch
    • S. Jacobsen, H. G. Fritz: Filling of poly(lactic acid) with native starch. Polym. Eng. Sci. 1996, 36, 2799-2804.
    • (1996) Polym. Eng. Sci. , vol.36 , pp. 2799-2804
    • Jacobsen, S.1    Fritz, H.G.2
  • 48
  • 49
    • 0033940474 scopus 로고    scopus 로고
    • Understanding and influencing starch biochemistry
    • J. Kossman, J. Lloyd: Understanding and influencing starch biochemistry. Crit. Rev. Biochem. Mol. Biol. 2000, 35, 141-196.
    • (2000) Crit. Rev. Biochem. Mol. Biol. , vol.35 , pp. 141-196
    • Kossman, J.1    Lloyd, J.2
  • 50
    • 0026652567 scopus 로고
    • Waxy Chlamydomonas reinhardtii: Monocellular algal mutants defective in amylose biosynthesis and granule bound starch synthase activity accumulate a structurally modified amylopectin
    • B. Delrue, T. Fontaine, F. Routier, A. Decq, J. M. Wieruszeski, N. Van den Koornhuyse, M.-L. Maddelein, B. Fournet, S. G. Ball: Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose biosynthesis and granule bound starch synthase activity accumulate a structurally modified amylopectin. J. Bacteriol. 1992, 174, 3612-3620.
    • (1992) J. Bacteriol. , vol.174 , pp. 3612-3620
    • Delrue, B.1    Fontaine, T.2    Routier, F.3    Decq, A.4    Wieruszeski, J.M.5    Van Den Koornhuyse, N.6    Maddelein, M.-L.7    Fournet, B.8    Ball, S.G.9
  • 51
    • 0003006270 scopus 로고
    • A Chlamydomonas reinhardtii low starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADP-glucose pyrophosphorylase
    • S. Ball, I. Marianne, L. Dirick, M. Fresnoy, B. Delrue, A. Decq: A Chlamydomonas reinhardtii low starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADP-glucose pyrophosphorylase. Planta 1991, 185, 17-26.
    • (1991) Planta , vol.185 , pp. 17-26
    • Ball, S.1    Marianne, I.2    Dirick, L.3    Fresnoy, M.4    Delrue, B.5    Decq, A.6
  • 53
    • 0026458333 scopus 로고
    • Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase
    • D. M. Stark, K. Timmerman, G. F. Barry, J. Preiss, G. M. Kishore: Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase. Science 1992, 258, 287-292.
    • (1992) Science , vol.258 , pp. 287-292
    • Stark, D.M.1    Timmerman, K.2    Barry, G.F.3    Preiss, J.4    Kishore, G.M.5
  • 54
    • 0027139421 scopus 로고
    • Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation
    • L. A. Kleczkowski, P. Villand, E. Lüthi, O-A. Olsen, J. Preiss: Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation. Plant Physiol. 1993, 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, J.5
  • 55
    • 0026767213 scopus 로고
    • Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources
    • B. J. Smith-White, J. Preiss: Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources. J. Mol. Evol. 1992, 34, 449-464.
    • (1992) J. Mol. Evol. , vol.34 , pp. 449-464
    • Smith-White, B.J.1    Preiss, J.2
  • 56
    • 0028138290 scopus 로고
    • Allosteric sites of the large subunit of the spinach leaf ADP-glucose pyrophosphorylase
    • K. Ball, J. Preiss: Allosteric sites of the large subunit of the spinach leaf ADP-glucose pyrophosphorylase. J. Biol. Chem. 1994, 269, 24706-24711.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24706-24711
    • Ball, K.1    Preiss, J.2
  • 57
    • 0014011424 scopus 로고
    • 3-phosphoglycerate and orthophosphate modulation of adenosine diphosphoglucose pyrophosphorylase activity
    • H. P. Ghosh, J. Preiss: 3-phosphoglycerate and orthophosphate modulation of adenosine diphosphoglucose pyrophosphorylase activity. J. Biol. Chem. 1966, 241, 4491-4504.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4491-4504
    • Ghosh, H.P.1    Preiss, J.2
  • 58
    • 0001608011 scopus 로고
    • Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm
    • M. R. Olive, R. J. Ellis, W. W. Schuch: Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm. Plant Mol. Biol. 1989, 12, 525-538.
    • (1989) Plant Mol. Biol. , vol.12 , pp. 525-538
    • Olive, M.R.1    Ellis, R.J.2    Schuch, W.W.3
  • 59
    • 0030267532 scopus 로고    scopus 로고
    • The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial
    • K. Denyer, F. Dunlap, T. Thorbjørnsen, P. Keeling, A. M. Smith: The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial. Plant Physiol. 1996, 112, 779-785.
    • (1996) Plant Physiol. , vol.112 , pp. 779-785
    • Denyer, K.1    Dunlap, F.2    Thorbjørnsen, T.3    Keeling, P.4    Smith, A.M.5
  • 60
    • 0030483916 scopus 로고    scopus 로고
    • Distinct isoforms of ADP-glucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm
    • T. Thorbjørnsen, P. Villand, K. Denyer, O. Olsen, A. M. Smith: Distinct isoforms of ADP-glucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm. Plant J. 1996, 10, 243-250.
    • (1996) Plant J. , vol.10 , pp. 243-250
    • Thorbjørnsen, T.1    Villand, P.2    Denyer, K.3    Olsen, O.4    Smith, A.M.5
  • 61
    • 0001037454 scopus 로고
    • The enzymatic deficiency in the waxy mutant of maize
    • O. E. Nelson, H. W. Rines: The enzymatic deficiency in the waxy mutant of maize. Biochem. Biophys. Res. Commun. 1962, 9, 297-300.
    • (1962) Biochem. Biophys. Res. Commun. , vol.9 , pp. 297-300
    • Nelson, O.E.1    Rines, H.W.2
  • 64
    • 0032419443 scopus 로고    scopus 로고
    • A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.)
    • N. Fujita, T. Taira: A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.). Planta 1998, 207, 125-132.
    • (1998) Planta , vol.207 , pp. 125-132
    • Fujita, N.1    Taira, T.2
  • 65
    • 0032186436 scopus 로고    scopus 로고
    • Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat
    • T. Nakamura, P. Vrinten, K. Hayakawa, J. Ikeda: Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat. Plant Physiol. 1998, 118, 451-459.
    • (1998) Plant Physiol. , vol.118 , pp. 451-459
    • Nakamura, T.1    Vrinten, P.2    Hayakawa, K.3    Ikeda, J.4
  • 66
    • 0029347013 scopus 로고
    • Biochemical and molecular characterization of a novel starch synthase from potato tubers
    • A. Edwards, J. Marshall, C. Sidebottom, R. G. F. Visser, A. M. Smith, C. Martin: Biochemical and molecular characterization of a novel starch synthase from potato tubers. Plant J. 1995, 8, 283-294.
    • (1995) Plant J. , vol.8 , pp. 283-294
    • Edwards, A.1    Marshall, J.2    Sidebottom, C.3    Visser, R.G.F.4    Smith, A.M.5    Martin, C.6
  • 68
    • 0033652252 scopus 로고    scopus 로고
    • Isolation, characterization and expression analysis of starch synthase IIa cDNA from wheat (Triticum aestivum L.)
    • M. Gao, R.N. Chibbar: Isolation, characterization and expression analysis of starch synthase IIa cDNA from wheat (Triticum aestivum L.). Genome 2000, 43, 768-775.
    • (2000) Genome , vol.43 , pp. 768-775
    • Gao, M.1    Chibbar, R.N.2
  • 72
    • 0035664649 scopus 로고    scopus 로고
    • Isolation, characterization and expression analysis of starch synthase I from wheat (Triticum aestivum L)
    • M. Peng, P. Hucl, R. N. Chibbar: Isolation, characterization and expression analysis of starch synthase I from wheat (Triticum aestivum L). Plant Sci. 2001, 161, 1055-1062.
    • (2001) Plant Sci. , vol.161 , pp. 1055-1062
    • Peng, M.1    Hucl, P.2    Chibbar, R.N.3
  • 73
    • 0032029093 scopus 로고    scopus 로고
    • Characterization of dull1, a maize gene coding for a novel starch synthase
    • M. Gao, J. Wanat, P. S. Stinard, M. G. James, A. M. Myers: Characterization of dull1, a maize gene coding for a novel starch synthase. Plant Cell 1998, 10, 399-412.
    • (1998) Plant Cell , vol.10 , pp. 399-412
    • Gao, M.1    Wanat, J.2    Stinard, P.S.3    James, M.G.4    Myers, A.M.5
  • 74
    • 0034089676 scopus 로고    scopus 로고
    • The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family
    • Z. Li, G. Mouille, K.-H. Behjat, S. Rahman, B. Clarke, K. R. Gale, R. Appels, M. K. Morell: The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family. Plant Physiol. 2000, 123, 613-624.
    • (2000) Plant Physiol. , vol.123 , pp. 613-624
    • Li, Z.1    Mouille, G.2    Behjat, K.-H.3    Rahman, S.4    Clarke, B.5    Gale, K.R.6    Appels, R.7    Morell, M.K.8
  • 75
    • 0030198862 scopus 로고    scopus 로고
    • Identification of the major starch synthase in the soluble fraction of potato tubers
    • J. Marshall, C. Sidebottom, M. Debet, C. Martin, A. M. Smith, A. Edwards: Identification of the major starch synthase in the soluble fraction of potato tubers. Plant Cell 1996, 8, 1121-1135.
    • (1996) Plant Cell , vol.8 , pp. 1121-1135
    • Marshall, J.1    Sidebottom, C.2    Debet, M.3    Martin, C.4    Smith, A.M.5    Edwards, A.6
  • 76
    • 0033914389 scopus 로고    scopus 로고
    • Genetic elimination of a starch granule protein, SGP-1, of wheat generates an altered starch with apparent high amylose
    • M. Yamamori, S. Fujita, K. Hayakawa, J. Matsuki, T. Yasui: Genetic elimination of a starch granule protein, SGP-1, of wheat generates an altered starch with apparent high amylose. Theor. Appl. Genet. 2000, 101, 21-29.
    • (2000) Theor. Appl. Genet. , vol.101 , pp. 21-29
    • Yamamori, M.1    Fujita, S.2    Hayakawa, K.3    Matsuki, J.4    Yasui, T.5
  • 77
    • 0033028207 scopus 로고    scopus 로고
    • A combined reduction in the activity of starch synthases II and III in potato has novel effects on the starch of tubers
    • A. Edwards, D. C. Fulton, C. M. Hylton, S. A. Jobling, M. Gidley, U. Rössner, C. Martin, A. M. Smith: A combined reduction in the activity of starch synthases II and III in potato has novel effects on the starch of tubers. Plant J. 1999, 17, 251-261.
    • (1999) Plant J. , vol.17 , pp. 251-261
    • Edwards, A.1    Fulton, D.C.2    Hylton, C.M.3    Jobling, S.A.4    Gidley, M.5    Rössner, U.6    Martin, C.7    Smith, A.M.8
  • 78
    • 0001677498 scopus 로고
    • Characterisation of starch structures of 17 maize endosperm mutant genotypes with Oh43 inbred line background
    • Y.-J. Wang, P. White, L. Pollak, J.-L. Jane: Characterisation of starch structures of 17 maize endosperm mutant genotypes with Oh43 inbred line background. Cereal Chem. 1993, 70, 171-179.
    • (1993) Cereal Chem. , vol.70 , pp. 171-179
    • Wang, Y.-J.1    White, P.2    Pollak, L.3    Jane, J.-L.4
  • 79
    • 0000674351 scopus 로고
    • Genetic control of carbohydrate synthesis in maize
    • R. G. Creech: Genetic control of carbohydrate synthesis in maize. Genetics 1965, 52, 1175-1186.
    • (1965) Genetics , vol.52 , pp. 1175-1186
    • Creech, R.G.1
  • 80
    • 0033080353 scopus 로고    scopus 로고
    • Analysis of purified maize starch syntheses IIa and IIb: SS isoforms can be distinguished based on their kinetic properties
    • J. M. Imparl-Radosevich, D. J. Nichols, P. Li, A. L. McKean, P. L. Keeling, H. Guan: Analysis of purified maize starch syntheses IIa and IIb: SS isoforms can be distinguished based on their kinetic properties. Arch. Biochem. Biophys. 1999, 382, 131-138.
    • (1999) Arch. Biochem. Biophys. , vol.382 , pp. 131-138
    • Imparl-Radosevich, J.M.1    Nichols, D.J.2    Li, P.3    McKean, A.L.4    Keeling, P.L.5    Guan, H.6
  • 81
    • 0017887611 scopus 로고
    • Multiple forms of starch branching enzyme of maize: Evidence for independent genetic control
    • C. D. Boyer, J. Preiss: Multiple forms of starch branching enzyme of maize: evidence for independent genetic control. Biochem. Biophys. Res. Commun. 1978, 80, 169-175.
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 169-175
    • Boyer, C.D.1    Preiss, J.2
  • 83
    • 0000634105 scopus 로고    scopus 로고
    • Isolation of a starch branching enzyme 1 cDNA from a wheat endosperm library. (Accession No. Y12320). Plant Gene Register (#PGR97-094)
    • A. Repellin, R.B. Nair, M. Båga, R.N. Chibbar: Isolation of a starch branching enzyme 1 cDNA from a wheat endosperm library. (Accession No. Y12320). Plant Gene Register (#PGR97-094). Plant Physiol. 1997, 114, 1145.
    • (1997) Plant Physiol. , vol.114 , pp. 1145
    • Repellin, A.1    Nair, R.B.2    Båga, M.3    Chibbar, R.N.4
  • 84
    • 0035128288 scopus 로고    scopus 로고
    • Characterization of a cDNA ecoding a type I starch branching enzyme produced in developing wheat (Triticum aestivum L.) kernels
    • A. Repellin, M. Båga, R. N. Chibbar: Characterization of a cDNA ecoding a type I starch branching enzyme produced in developing wheat (Triticum aestivum L.) kernels. J. Plant Physiol. 2001, 158, 91-100.
    • (2001) J. Plant Physiol. , vol.158 , pp. 91-100
    • Repellin, A.1    Båga, M.2    Chibbar, R.N.3
  • 85
    • 0031040103 scopus 로고    scopus 로고
    • Differential expression and properties of starch branching enzyme isoforms in developing wheat endosperm
    • M. K. Morell, A. Blennow, B. Kosar-Hashemi, M. S. Samuel: Differential expression and properties of starch branching enzyme isoforms in developing wheat endosperm. Plant Physiol. 1997, 113, 201-208.
    • (1997) Plant Physiol. , vol.113 , pp. 201-208
    • Morell, M.K.1    Blennow, A.2    Kosar-Hashemi, B.3    Samuel, M.S.4
  • 86
    • 0026038971 scopus 로고
    • Cloning and expression analysis of a potato cDNA that encodes branching enzyme: Evidence for co-expression of starch biosynthesis genes
    • J. Kossmann, R. G. F. Visser, B. Muller-Rober, L. Willmitzer, U. Sonnedwald: Cloning and expression analysis of a potato cDNA that encodes branching enzyme: evidence for co-expression of starch biosynthesis genes. Mol. Gen. Genet. 1991, 230, 39-44.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 39-44
    • Kossmann, J.1    Visser, R.G.F.2    Muller-Rober, B.3    Willmitzer, L.4    Sonnedwald, U.5
  • 87
    • 0027450139 scopus 로고
    • Molecular analysis of the gene encoding a rice starch branching enzyme
    • I. Kawasaki, K. Mizuno, T. Baba, H. Shimada: Molecular analysis of the gene encoding a rice starch branching enzyme. Mol. Gen. Genet. 1993, 237, 10-16.
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 10-16
    • Kawasaki, I.1    Mizuno, K.2    Baba, T.3    Shimada, H.4
  • 89
    • 0027031479 scopus 로고
    • Cloning, partial sequencing and expression of a cDNA coding for branching enzyme in cassava
    • S. N. I. M. Salehuzzaman, E. Jacobsen, R. G. F. Visser: Cloning, partial sequencing and expression of a cDNA coding for branching enzyme in cassava. Plant Mol. Biol. 1992, 20, 809-819.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 809-819
    • Salehuzzaman, S.N.I.M.1    Jacobsen, E.2    Visser, R.G.F.3
  • 90
    • 0000361233 scopus 로고
    • Differentiation of the properties of the branching isozymes of maize (Zea mays)
    • H. P. Guan, J. Preiss: Differentiation of the properties of the branching isozymes of maize (Zea mays). Plant Physiol. 1993, 102, 1269-1273.
    • (1993) Plant Physiol. , vol.102 , pp. 1269-1273
    • Guan, H.P.1    Preiss, J.2
  • 91
    • 0027551838 scopus 로고
    • Branching of amylose by the branching isozymes of maize endosperm
    • Y. Takeda, H. P. Guan, J. Preiss: Branching of amylose by the branching isozymes of maize endosperm. Carbohydr. Res. 1993, 240, 253-263.
    • (1993) Carbohydr. Res. , vol.240 , pp. 253-263
    • Takeda, Y.1    Guan, H.P.2    Preiss, J.3
  • 92
    • 0031131624 scopus 로고    scopus 로고
    • Independent genetic control of maize starch branching enzymes IIa and IIb
    • M. Gao, D. K. Fisher, K.-Y. Kim, J. C. Shannon, M. J. Guiltinan: Independent genetic control of maize starch branching enzymes IIa and IIb. Plant Physiol. 1997, 114, 69-78.
    • (1997) Plant Physiol. , vol.114 , pp. 69-78
    • Gao, M.1    Fisher, D.K.2    Kim, K.-Y.3    Shannon, J.C.4    Guiltinan, M.J.5
  • 93
    • 0031588790 scopus 로고    scopus 로고
    • Isolation, characterization and expression analysis of a starch branching enzyme II cDNA from wheat
    • R. B. Nair, M. Båga, G. J. Scoles, K. K. Kartha, R. N. Chibbar: Isolation, characterization and expression analysis of a starch branching enzyme II cDNA from wheat. Plant Sci. 1997, 122, 153-163.
    • (1997) Plant Sci. , vol.122 , pp. 153-163
    • Nair, R.B.1    Båga, M.2    Scoles, G.J.3    Kartha, K.K.4    Chibbar, R.N.5
  • 94
    • 0032159287 scopus 로고    scopus 로고
    • The two genes encoding starch branching enzyme IIa and IIb are differentially expressed in barley
    • C. Sun, S. Puthigae, S. Ahlandsberg, C. Jansson: The two genes encoding starch branching enzyme IIa and IIb are differentially expressed In barley. Plant Physiol. 1998, 118, 37-49.
    • (1998) Plant Physiol. , vol.118 , pp. 37-49
    • Sun, C.1    Puthigae, S.2    Ahlandsberg, S.3    Jansson, C.4
  • 95
    • 0032104812 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of starch branching enzyme II from potato
    • C.-T. Larsson, J. Khoshnoodi, B. Ek, L. Rask, H. Larsson: Molecular cloning and characterisation of starch branching enzyme II from potato. Plant Mol. Biol. 1998, 37, 505-511.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 505-511
    • Larsson, C.-T.1    Khoshnoodi, J.2    Ek, B.3    Rask, L.4    Larsson, H.5
  • 96
    • 0027247801 scopus 로고
    • Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds
    • K. Mizuno, T. Kawasaki, H. Shimada, H. Satoh, E. Kobayashi, S. Okumura, Y. Arai, T. J. Baba: Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds. Biol. Chem. 1993, 268, 19084-19091.
    • (1993) Biol. Chem. , vol.268 , pp. 19084-19091
    • Mizuno, K.1    Kawasaki, T.2    Shimada, H.3    Satoh, H.4    Kobayashi, E.5    Okumura, S.6    Arai, Y.7    Baba, T.J.8
  • 97
    • 0030106256 scopus 로고    scopus 로고
    • Evolutionary conservation and expression patterns of maize starch branching enzyme I and IIb suggests isoform specialization
    • M. Gao, D. K. Fisher, K.-N. Kim, J. C. Shannon, M. J. Guiltinan: Evolutionary conservation and expression patterns of maize starch branching enzyme I and IIb suggests isoform specialization. Plant Mol. Biol. 1996, 30, 1223-1232.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 1223-1232
    • Gao, M.1    Fisher, D.K.2    Kim, K.-N.3    Shannon, J.C.4    Guiltinan, M.J.5
  • 100
    • 0030063579 scopus 로고    scopus 로고
    • Introduction of sense and antisense cDNA for branching enzyme in the amylose-free potato mutant leads to physico-chemical changes in the starch
    • E. Flipse, L. Suurs, C. J. A. M. Keetels, J. Kossman, E. Jacobsen, R. G. F. Visser: Introduction of sense and antisense cDNA for branching enzyme in the amylose-free potato mutant leads to physico-chemical changes in the starch. Planta 1996, 198, 340-347.
    • (1996) Planta , vol.198 , pp. 340-347
    • Flipse, E.1    Suurs, L.2    Keetels, C.J.A.M.3    Kossman, J.4    Jacobsen, E.5    Visser, R.G.F.6
  • 101
    • 0033834354 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a granule-bound 152 kilodalton starch-branching enzyme in wheat
    • M. Båga, R. B. Nair, A. Repellin, G. J. Scoles, R. N. Chibbar: Isolation of a cDNA encoding a granule-bound 152 kilodalton starch-branching enzyme in wheat. Plant Physiol. 2000, 124, 253-263.
    • (2000) Plant Physiol. , vol.124 , pp. 253-263
    • Båga, M.1    Nair, R.B.2    Repellin, A.3    Scoles, G.J.4    Chibbar, R.N.5
  • 102
    • 0033825658 scopus 로고    scopus 로고
    • Starch branching enzymes preferentially associated with A-type starch granules in wheat endosperm
    • M. Peng, M. Gao, M. Båga, P. Hucl, R.N. Chibbar: Starch branching enzymes preferentially associated with A-type starch granules in wheat endosperm. Plant Physiol. 2000, 124, 265-272.
    • (2000) Plant Physiol. , vol.124 , pp. 265-272
    • Peng, M.1    Gao, M.2    Båga, M.3    Hucl, P.4    Chibbar, R.N.5
  • 103
    • 0002056409 scopus 로고    scopus 로고
    • Some properties of starch debranching enzymes and their possible roles in amylopectin synthesis
    • Y. Nakamura: Some properties of starch debranching enzymes and their possible roles in amylopectin synthesis. Plant Sci. 1996, 121, 1-18.
    • (1996) Plant Sci. , vol.121 , pp. 1-18
    • Nakamura, Y.1
  • 104
    • 0032866910 scopus 로고    scopus 로고
    • Purification and molecular genetic characterization of ZPU1, a pullulanase-type starch-debranching enzyme from maize
    • M. K. Beatty, A. Rahman, H. Cao, W. Woodman, M. Lee, A. M. Myers, M. G. James: Purification and molecular genetic characterization of ZPU1, a pullulanase-type starch-debranching enzyme from maize. Plant Physiol. 1999, 119, 255-266.
    • (1999) Plant Physiol. , vol.119 , pp. 255-266
    • Beatty, M.K.1    Rahman, A.2    Cao, H.3    Woodman, W.4    Lee, M.5    Myers, A.M.6    James, M.G.7
  • 105
    • 0001384883 scopus 로고
    • Debranching enzymes of potato tubers (Solanum tubersosum L.) I. Purification and some properties of potato isoamylase
    • Y. Ishizaki, H. Taniguchi, Y. Maruyama, M. Nakamura: Debranching enzymes of potato tubers (Solanum tubersosum L.) I. Purification and some properties of potato isoamylase. Agric. Biol. Chem. 1983, 47, 771-779.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 771-779
    • Ishizaki, Y.1    Taniguchi, H.2    Maruyama, Y.3    Nakamura, M.4
  • 106
    • 0033118441 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice
    • N. Fujita, A. Kubo, P. B. Francisco, M. Nakakita, K. Harada, N. Minaka, Y. Nakamura: Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice. Planta 1999, 208, 283-293.
    • (1999) Planta , vol.208 , pp. 283-293
    • Fujita, N.1    Kubo, A.2    Francisco, P.B.3    Nakakita, M.4    Harada, K.5    Minaka, N.6    Nakamura, Y.7
  • 107
    • 0035040208 scopus 로고    scopus 로고
    • Biochemical characterization of wild-type and mutant isoamylases from Chlamydomonas reinhardtii supports function of the multimeric enzyme organization in amylopectin maturation
    • D. Dauvillee, C. Colleoni, G. Mouille, M.K. Morell, C. d'Hulst, F. Wattebled, L. Lienard, D. Delvalle, J.-P. Ral, A. M. Myers, S. G. Ball: Biochemical characterization of wild-type and mutant isoamylases from Chlamydomonas reinhardtii supports function of the multimeric enzyme organization in amylopectin maturation. Plant Physiol. 2001, 125, 1723-1731.
    • (2001) Plant Physiol. , vol.125 , pp. 1723-1731
    • Dauvillee, D.1    Colleoni, C.2    Mouille, G.3    Morell, M.K.4    D'Hulst, C.5    Wattebled, F.6    Lienard, L.7    Delvalle, D.8    Ral, J.-P.9    Myers, A.M.10    Ball, S.G.11
  • 108
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinating grains of barley
    • R. A. Burton, X.-Q. Zhang, M. Hrmova, G. B. Fincher: A single limit dextrinase gene is expressed both in the developing endosperm and in germinating grains of barley. Plant Physiol. 1999, 119, 859-871.
    • (1999) Plant Physiol. , vol.119 , pp. 859-871
    • Burton, R.A.1    Zhang, X.-Q.2    Hrmova, M.3    Fincher, G.B.4
  • 109
    • 0000420233 scopus 로고
    • A debranching enzyme deficiency in endosperms of sugary-1 mutants of maize
    • D. Pan, O. E. Nelson: A debranching enzyme deficiency in endosperms of sugary-1 mutants of maize. Plant Physiol. 1984, 74, 324.
    • (1984) Plant Physiol. , vol.74 , pp. 324
    • Pan, D.1    Nelson, O.E.2
  • 110
    • 0030814320 scopus 로고    scopus 로고
    • Correlation between activities of starch debranching enzyme and α-polyglucan structure in endosperms of sugary-1 mutants of rice
    • Y. Nakamura, A. Kubo, T. Shimamune, T. Matsuda, K. Harada, H. Satoh: Correlation between activities of starch debranching enzyme and α-polyglucan structure in endosperms of sugary-1 mutants of rice. Plant J. 1997, 12, 143-153.
    • (1997) Plant J. , vol.12 , pp. 143-153
    • Nakamura, Y.1    Kubo, A.2    Shimamune, T.3    Matsuda, T.4    Harada, K.5    Satoh, H.6
  • 111
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugary-1, a determinant of starch composition in kernels
    • M. Q. James, D. S. Robertson, A. M. Myers: Characterization of the maize gene sugary-1, a determinant of starch composition in kernels. Plant Cell 1995, 7, 417-429.
    • (1995) Plant Cell , vol.7 , pp. 417-429
    • James, M.Q.1    Robertson, D.S.2    Myers, A.M.3
  • 113
    • 0032192047 scopus 로고    scopus 로고
    • A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen
    • S. C. Zeeman, T. Umemoto, W.-L. Lue, P. Au-Yeung, C. Martin, A. M. Smith, J. Chen: A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen. Plant Cell 1998, 10, 1699-1711.
    • (1998) Plant Cell , vol.10 , pp. 1699-1711
    • Zeeman, S.C.1    Umemoto, T.2    Lue, W.-L.3    Au-Yeung, P.4    Martin, C.5    Smith, A.M.6    Chen, J.7
  • 116
    • 0034123997 scopus 로고    scopus 로고
    • Reversible binding of the starch-related R1 protein to the surface of transitory starch granules
    • G. Ritte, R. Lorberth, M. Steup: Reversible binding of the starch-related R1 protein to the surface of transitory starch granules. Plant J. 2000, 21, 387-391.
    • (2000) Plant J. , vol.21 , pp. 387-391
    • Ritte, G.1    Lorberth, R.2    Steup, M.3
  • 117
    • 0001310335 scopus 로고
    • Characterization of D-enzyme (4-alpha-glucanotransferase) in Arabadopsis leaf
    • T.-P. Lin, J. Prelss: Characterization of D-enzyme (4-alpha- glucanotransferase) in Arabadopsis leaf. Plant Physiol. 1988, 86, 260-265.
    • (1988) Plant Physiol. , vol.86 , pp. 260-265
    • Lin, T.-P.1    Prelss, J.2
  • 118
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coll: Transport, metabolism and regulation
    • W. Boos, H. Shuman: Maltose/maltodextrin system of Escherichia coll: transport, metabolism and regulation. Microbiol. Mol. Biol. Rev. 1998, 62, 204-229.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, H.2
  • 121
    • 0031833364 scopus 로고    scopus 로고
    • Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase)
    • T. Takaha, J. Critchley, S. Okada, S. M. Smith: Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase). Planta 1998, 205, 445-451.
    • (1998) Planta , vol.205 , pp. 445-451
    • Takaha, T.1    Critchley, J.2    Okada, S.3    Smith, S.M.4
  • 122
    • 0031464334 scopus 로고    scopus 로고
    • Metabolism and transport in non-photosynthetic plastids
    • M. J. Emes, H. E. Neuhaus: Metabolism and transport in non-photosynthetic plastids. J. Exp. Bot. 1997, 48, 1995-2005.
    • (1997) J. Exp. Bot. , vol.48 , pp. 1995-2005
    • Emes, M.J.1    Neuhaus, H.E.2
  • 123
    • 0032439289 scopus 로고    scopus 로고
    • Altered plastidic ATP/ADP transporter activity influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch
    • J. Tjaden, T. Mohlmann, K. Kampfenkel, G. Henrichs, H.E. Neuhaus: Altered plastidic ATP/ADP transporter activity influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch. Plant J. 1998, 16, 531-540.
    • (1998) Plant J. , vol.16 , pp. 531-540
    • Tjaden, J.1    Mohlmann, T.2    Kampfenkel, K.3    Henrichs, G.4    Neuhaus, H.E.5
  • 124
    • 0032134257 scopus 로고    scopus 로고
    • Brittle-1, an adenylate translocator, facilitates transfer of extraplastidial synthesized ADP-glucose into amyloplasts
    • J. C. Shannon, F.-M. Pien, H. Cao, K.-C. Liu: Brittle-1, an adenylate translocator, facilitates transfer of extraplastidial synthesized ADP-glucose into amyloplasts. Plant Physiol. 1998, 117, 1235-1252.
    • (1998) Plant Physiol. , vol.117 , pp. 1235-1252
    • Shannon, J.C.1    Pien, F.-M.2    Cao, H.3    Liu, K.-C.4
  • 125
    • 0000586974 scopus 로고
    • Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases
    • C. D. Boyer, J. Preiss: Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases. Plant Physiol. 1981, 67, 1141-1145.
    • (1981) Plant Physiol. , vol.67 , pp. 1141-1145
    • Boyer, C.D.1    Preiss, J.2
  • 126
    • 0034775955 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of the effects of amylose extender mutation in rice endosperm
    • A. Nishi, Y. Nakamura, N. Tanaka, H. Satoh: Biochemical and genetic analysis of the effects of amylose extender mutation in rice endosperm. Plant Physiol. 2001, 127, 459-472.
    • (2001) Plant Physiol. , vol.127 , pp. 459-472
    • Nishi, A.1    Nakamura, Y.2    Tanaka, N.3    Satoh, H.4
  • 128
    • 0032127317 scopus 로고    scopus 로고
    • Overexpression of pyrophosphorylase leads to increased sucrose degradation and starch synthesis, increased activities of enzymes for sucrose-starch interconversion, and increased levels of nucleotides in growing potato tubers
    • P. Geigenberger, M. Hajirezaei, M. Geiger, U. Deiting, U. Sonnewald, M. Stitt: Overexpression of pyrophosphorylase leads to increased sucrose degradation and starch synthesis, increased activities of enzymes for sucrose-starch interconversion, and increased levels of nucleotides in growing potato tubers. Planta 1998, 205, 428-437.
    • (1998) Planta , vol.205 , pp. 428-437
    • Geigenberger, P.1    Hajirezaei, M.2    Geiger, M.3    Deiting, U.4    Sonnewald, U.5    Stitt, M.6
  • 129
    • 0035633355 scopus 로고    scopus 로고
    • Identifying valuable corn quality traits for starch production
    • L. A. Johnson, C. L. Hardy, C. P. Baumel, P. J. White: Identifying valuable corn quality traits for starch production. Cereal Foods World 2001, 46, 417-423.
    • (2001) Cereal Foods World , vol.46 , pp. 417-423
    • Johnson, L.A.1    Hardy, C.L.2    Baumel, C.P.3    White, P.J.4
  • 130
    • 0035213394 scopus 로고    scopus 로고
    • Seeds for a better future: "low phytate" grains help to overcome malnutrition and reduce pollution
    • V. Raboy: Seeds for a better future: "low phytate" grains help to overcome malnutrition and reduce pollution. Trends Plant Sci. 2001, 6, 458-465.
    • (2001) Trends Plant Sci. , vol.6 , pp. 458-465
    • Raboy, V.1
  • 133
    • 0037666477 scopus 로고    scopus 로고
    • Structural, physicochemical, and pasting properties of starches from potato plants with repressed r1-gene
    • A. Vikso-Nielsen, A. Blennow, K. Jorgensen, K. H. Kristensen, A. Jensen, B. Lindberg Moller: Structural, physicochemical, and pasting properties of starches from potato plants with repressed r1-gene. Biomacromolecules 2001, 2, 836-843.
    • (2001) Biomacromolecules , vol.2 , pp. 836-843
    • Vikso-Nielsen, A.1    Blennow, A.2    Jorgensen, K.3    Kristensen, K.H.4    Jensen, A.5    Moller, B.L.6
  • 134
    • 0008555237 scopus 로고    scopus 로고
    • Frequent absence of GBSSI B isoprotein in endosperm starch of Canadian wheat cultivars
    • T. Demeke, P. Hucl, R. N. Chibbar: Frequent absence of GBSSI B isoprotein in endosperm starch of Canadian wheat cultivars. Starch/Stärke 2000, 52, 349-352.
    • (2000) Starch/Stärke , vol.52 , pp. 349-352
    • Demeke, T.1    Hucl, P.2    Chibbar, R.N.3
  • 135
    • 0032880533 scopus 로고    scopus 로고
    • Biochemical characterization of the waxy a protein and Its effect on starch properties
    • T. Demeke, P. Hucl, E. S. M. Abdel-Aal, M. Båga, R. N. Chibbar: Biochemical characterization of the waxy A protein and Its effect on starch properties. Cereal Chem. 1999, 76, 694-698.
    • (1999) Cereal Chem. , vol.76 , pp. 694-698
    • Demeke, T.1    Hucl, P.2    Abdel-Aal, E.S.M.3    Båga, M.4    Chibbar, R.N.5
  • 138
    • 21844488215 scopus 로고
    • Starch lipids and how they relate to starch granule structure and functionality
    • W. R. Morrison: Starch lipids and how they relate to starch granule structure and functionality. Cereal Foods World 1995, 40, 437-446.
    • (1995) Cereal Foods World , vol.40 , pp. 437-446
    • Morrison, W.R.1
  • 139
    • 0031668613 scopus 로고    scopus 로고
    • Role of phosphorous in viscosity, gelatinization and retrogradation of starch
    • P.-Y. Lin, Z. Czuchajowska: Role of phosphorous in viscosity, gelatinization and retrogradation of starch. Cereal Chem. 1998, 75, 705-709.
    • (1998) Cereal Chem. , vol.75 , pp. 705-709
    • Lin, P.-Y.1    Czuchajowska, Z.2
  • 140
    • 0029970864 scopus 로고    scopus 로고
    • Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase
    • J. R. Pear, V. Kawagoe, W. E. Schreckengost, D. P. Delmer, D. M. Stalker: Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase. Proc. Natl. Acad. Sci. USA 1996, 93, 12637-12642.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12637-12642
    • Pear, J.R.1    Kawagoe, V.2    Schreckengost, W.E.3    Delmer, D.P.4    Stalker, D.M.5
  • 141
    • 0034077121 scopus 로고    scopus 로고
    • Cellulose biosynthesis: A model for understanding the assembly of biopolymers
    • R. M. Brown, I. M. Saxena: Cellulose biosynthesis: a model for understanding the assembly of biopolymers. Plant Physiol. Biochem. 2000, 38, 57-67.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 57-67
    • Brown, R.M.1    Saxena, I.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.