메뉴 건너뛰기




Volumn 12, Issue 4, 2013, Pages 413-426

Wheat (Triticum aestivum L. and T. turgidum L. ssp. durum) Kernel Hardness: I. Current View on the Role of Puroindolines and Polar Lipids

Author keywords

[No Author keywords available]

Indexed keywords

DURUM WHEAT CULTIVARS; PROTEIN MATRIX; PUROINDOLINE A; PUROINDOLINES; RESEARCH NEEDS; STARCH GRANULES; STRUCTURE , PROPERTIES; TRITICUM AESTIVUM;

EID: 84879167558     PISSN: None     EISSN: 15414337     Source Type: Journal    
DOI: 10.1111/1541-4337.12019     Document Type: Article
Times cited : (51)

References (130)
  • 1
    • 12444334661 scopus 로고    scopus 로고
    • Real time RT-PCR and flow cytometry to investigate wheat kernel hardness: role of puroindoline genes and proteins
    • Amoroso MG, Longobardo L, Capparelli R. 2004. Real time RT-PCR and flow cytometry to investigate wheat kernel hardness: role of puroindoline genes and proteins. Biotechnol Lett 26:1731-7.
    • (2004) Biotechnol Lett , vol.26 , pp. 1731-1737
    • Amoroso, M.G.1    Longobardo, L.2    Capparelli, R.3
  • 2
    • 33745770062 scopus 로고    scopus 로고
    • Early nonsense: mRNA decay solves a translational problem
    • Amrani N, Sachs MS, Jacobson A. 2006. Early nonsense: mRNA decay solves a translational problem. Nat Rev Mol Cell Biol 7:415-25.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 415-425
    • Amrani, N.1    Sachs, M.S.2    Jacobson, A.3
  • 3
    • 0036746523 scopus 로고    scopus 로고
    • Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry
    • Andon NL, Hollingworth S, Koller A, Greenland AJ, Yates JR, Haynes PA. 2002. Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics 2:1156-68.
    • (2002) Proteomics , vol.2 , pp. 1156-1168
    • Andon, N.L.1    Hollingworth, S.2    Koller, A.3    Greenland, A.J.4    Yates, J.R.5    Haynes, P.A.6
  • 4
    • 47549101696 scopus 로고    scopus 로고
    • In vitro starch-binding experiments: study of the proteins related to grain hardness of wheat
    • In: Buck HT, Nisi JE, Salomon N, editors. Dordrecht, the Netherlands: Springer.
    • Bako A, Gardonyi M, Tamas L. 2007. In vitro starch-binding experiments: study of the proteins related to grain hardness of wheat. In: Buck HT, Nisi JE, Salomon N, editors. Wheat production in stressed environments. Dordrecht, the Netherlands: Springer. p 685-91.
    • (2007) Wheat production in stressed environments , pp. 685-691
    • Bako, A.1    Gardonyi, M.2    Tamas, L.3
  • 5
    • 33646261644 scopus 로고    scopus 로고
    • Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability
    • Balmer Y, Vensel WH, DuPont FM, Buchanan BB, Hurkman WJ. 2006. Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability. J Exp Bot 57:1591-602.
    • (2006) J Exp Bot , vol.57 , pp. 1591-1602
    • Balmer, Y.1    Vensel, W.H.2    DuPont, F.M.3    Buchanan, B.B.4    Hurkman, W.J.5
  • 7
    • 0001764563 scopus 로고
    • Protein secretion in wheat endosperm - formation of the matrix protein
    • Bechtel DB, Gaines RL, Pomeranz Y. 1982. Protein secretion in wheat endosperm - formation of the matrix protein. Cereal Chem 59:336-43.
    • (1982) Cereal Chem , vol.59 , pp. 336-343
    • Bechtel, D.B.1    Gaines, R.L.2    Pomeranz, Y.3
  • 8
    • 0029840895 scopus 로고    scopus 로고
    • Determining endosperm texture of developing hard and soft red winter wheats dried by different methods using the single-kernel wheat characterization system
    • Bechtel DB, Wilson JD, Martin CR. 1996. Determining endosperm texture of developing hard and soft red winter wheats dried by different methods using the single-kernel wheat characterization system. Cereal Chem 73:567-70.
    • (1996) Cereal Chem , vol.73 , pp. 567-570
    • Bechtel, D.B.1    Wilson, J.D.2    Martin, C.R.3
  • 10
    • 0346035018 scopus 로고    scopus 로고
    • Expression of wild-type pinB sequence in transgenic wheat complements a hard phenotype
    • Beecher B, Bettge A, Smidansky E, Giroux MJ. 2002a. Expression of wild-type pinB sequence in transgenic wheat complements a hard phenotype. Theor Appl Genet 105:870-7.
    • (2002) Theor Appl Genet , vol.105 , pp. 870-877
    • Beecher, B.1    Bettge, A.2    Smidansky, E.3    Giroux, M.J.4
  • 13
    • 0027223990 scopus 로고
    • Complete amino-acid-sequence of puroindoline, a new basic and cystine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning
    • Blochet JE, Chevalier C, Forest E, Pebaypeyroula E, Gautier MF, Joudrier P, Pezolet M, Marion D. 1993. Complete amino-acid-sequence of puroindoline, a new basic and cystine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning. FEBS Lett 329:336-40.
    • (1993) FEBS Lett , vol.329 , pp. 336-340
    • Blochet, J.E.1    Chevalier, C.2    Forest, E.3    Pebaypeyroula, E.4    Gautier, M.F.5    Joudrier, P.6    Pezolet, M.7    Marion, D.8
  • 14
    • 54549098138 scopus 로고    scopus 로고
    • Structure and orientation of puroindolines into wheat galactolipid monolayers
    • Bottier C, Gean J, Desbat B, Renault A, Marion D, Vie V. 2008. Structure and orientation of puroindolines into wheat galactolipid monolayers. Langmuir 24:10901-9.
    • (2008) Langmuir , vol.24 , pp. 10901-10909
    • Bottier, C.1    Gean, J.2    Desbat, B.3    Renault, A.4    Marion, D.5    Vie, V.6
  • 16
    • 0344668741 scopus 로고    scopus 로고
    • Puroindoline A-gene expression is involved in association of puroindolines to starch
    • Capparelli R, Borriello G, Giroux MJ, Amoroso MG. 2003. Puroindoline A-gene expression is involved in association of puroindolines to starch. Theor Appl Genet 107:1463-8.
    • (2003) Theor Appl Genet , vol.107 , pp. 1463-1468
    • Capparelli, R.1    Borriello, G.2    Giroux, M.J.3    Amoroso, M.G.4
  • 17
    • 26944446211 scopus 로고    scopus 로고
    • Two plant puroindolines colocalize in wheat seed and in vitro synergistically fight against pathogens
    • Capparelli R, Amoroso MG, Palumbo D, Iannaccone M, Faleri C, Cresti M. 2005. Two plant puroindolines colocalize in wheat seed and in vitro synergistically fight against pathogens. Plant Mol Biol 58:857-67.
    • (2005) Plant Mol Biol , vol.58 , pp. 857-867
    • Capparelli, R.1    Amoroso, M.G.2    Palumbo, D.3    Iannaccone, M.4    Faleri, C.5    Cresti, M.6
  • 19
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action
    • Chan DI, Prenner EJ, Vogel HJ. 2006. Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim Biophys Acta Biomem 1758:1184-202.
    • (2006) Biochim Biophys Acta Biomem , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 22
    • 0033199578 scopus 로고    scopus 로고
    • The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1-Angstrom resolution
    • Charvolin D, Douliez JP, Marion D, Cohen-Addad C, Pebay-Peyroula E. 1999. The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1-Angstrom resolution. Eur J Biochem 264:562-8.
    • (1999) Eur J Biochem , vol.264 , pp. 562-568
    • Charvolin, D.1    Douliez, J.P.2    Marion, D.3    Cohen-Addad, C.4    Pebay-Peyroula, E.5
  • 23
    • 30544432967 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of puroindoline a and b alleles in Chinese landraces and historical cultivars
    • Chen F, He ZH, Xia XC, Xia LQ, Zhang XY, Lillemo M, Morris CF. 2006. Molecular and biochemical characterization of puroindoline a and b alleles in Chinese landraces and historical cultivars. Theor Appl Genet 112:400-9.
    • (2006) Theor Appl Genet , vol.112 , pp. 400-409
    • Chen, F.1    He, Z.H.2    Xia, X.C.3    Xia, L.Q.4    Zhang, X.Y.5    Lillemo, M.6    Morris, C.F.7
  • 25
    • 33847650458 scopus 로고    scopus 로고
    • Single amino acid substitutions in puroindoline-b mutants influence lipid binding properties
    • Clifton LA, Lad MD, Green RJ, Frazier RA. 2007. Single amino acid substitutions in puroindoline-b mutants influence lipid binding properties. Biochemistry 46:2260-6.
    • (2007) Biochemistry , vol.46 , pp. 2260-2266
    • Clifton, L.A.1    Lad, M.D.2    Green, R.J.3    Frazier, R.A.4
  • 27
    • 0002096547 scopus 로고    scopus 로고
    • Continuous manufacturing process
    • In: Kruger JE, Matsuo RB, Dick JW, editors. St. Paul, MN: AACC International.
    • Dalbon G, Grivon D, Pagani MA. 1996. Continuous manufacturing process. In: Kruger JE, Matsuo RB, Dick JW, editors. Pasta and noodle technology. St. Paul, MN: AACC International. p 13-58.
    • (1996) Pasta and noodle technology , pp. 13-58
    • Dalbon, G.1    Grivon, D.2    Pagani, M.A.3
  • 31
    • 0026772271 scopus 로고
    • Amino acid sequence of a nonspecific wheat phospholipid transfer protein and its conformation as revealed by infrared and Raman spectroscopy. Role of disulfide bridges and phospholipids in the stabilization of the α-helix structure
    • Désormeaux A, Blochet JE, Pézolet M, Marion D. 1992. Amino acid sequence of a nonspecific wheat phospholipid transfer protein and its conformation as revealed by infrared and Raman spectroscopy. Role of disulfide bridges and phospholipids in the stabilization of the α-helix structure. Biochim Biophys Acta 1121:137-52.
    • (1992) Biochim Biophys Acta , vol.1121 , pp. 137-152
    • Désormeaux, A.1    Blochet, J.E.2    Pézolet, M.3    Marion, D.4
  • 32
    • 0008820727 scopus 로고
    • Kernel hardness and baking quality of wheat: a genetic analysis using chromosome substitution lines
    • Doekes GJ, Belderok B. 1976. Kernel hardness and baking quality of wheat: a genetic analysis using chromosome substitution lines. Euphytica 25:565-76.
    • (1976) Euphytica , vol.25 , pp. 565-576
    • Doekes, G.J.1    Belderok, B.2
  • 33
    • 0036512409 scopus 로고    scopus 로고
    • Galactolipids rule in seed plants
    • Dörmann P, Benning C. 2002. Galactolipids rule in seed plants. Trends Plant Sci 7:112-8.
    • (2002) Trends Plant Sci , vol.7 , pp. 112-118
    • Dörmann, P.1    Benning, C.2
  • 34
    • 0033853295 scopus 로고    scopus 로고
    • Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid-binding proteins from cereal kernels
    • Douliez JP, Michon T, Elmorjani K, Marion D. 2000. Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid-binding proteins from cereal kernels. J Cereal Sci 32:1-20.
    • (2000) J Cereal Sci , vol.32 , pp. 1-20
    • Douliez, J.P.1    Michon, T.2    Elmorjani, K.3    Marion, D.4
  • 35
    • 0001003310 scopus 로고    scopus 로고
    • Interaction of puroindolines with wheat flour polar lipids determines their foaming properties
    • Dubreil L, Compoint JP, Marion D. 1997. Interaction of puroindolines with wheat flour polar lipids determines their foaming properties. J Agric Food Chem 45:108-16.
    • (1997) J Agric Food Chem , vol.45 , pp. 108-116
    • Dubreil, L.1    Compoint, J.P.2    Marion, D.3
  • 37
    • 49649103165 scopus 로고    scopus 로고
    • Puroindoline-a and puroindoline-b interact with the Saccharomyces cerevisiae plasma membrane through different amino acids present in their tryptophan-rich domain
    • Evrard A, Lagarde V, Joudrier P, Gautier MF. 2008. Puroindoline-a and puroindoline-b interact with the Saccharomyces cerevisiae plasma membrane through different amino acids present in their tryptophan-rich domain. J Cereal Sci 48:379-86.
    • (2008) J Cereal Sci , vol.48 , pp. 379-386
    • Evrard, A.1    Lagarde, V.2    Joudrier, P.3    Gautier, M.F.4
  • 38
    • 2642572758 scopus 로고    scopus 로고
    • Expression of wheat puroindoline-b reduces scab susceptibility in transgenic apple (Malus x domestica Borkh.)
    • Faize M, Sourice S, Dupuis F, Parisi L, Gautier MF, Chevreau E. 2004. Expression of wheat puroindoline-b reduces scab susceptibility in transgenic apple (Malus x domestica Borkh.). Plant Sci 167:347-54.
    • (2004) Plant Sci , vol.167 , pp. 347-354
    • Faize, M.1    Sourice, S.2    Dupuis, F.3    Parisi, L.4    Gautier, M.F.5    Chevreau, E.6
  • 40
    • 72449143105 scopus 로고    scopus 로고
    • In planta mutagenesis determines the functional regions of the wheat puroindoline proteins
    • Feiz L, Beecher B, Martin JM, Giroux MJ. 2009a. In planta mutagenesis determines the functional regions of the wheat puroindoline proteins. Genetics 183:853-60.
    • (2009) Genetics , vol.183 , pp. 853-860
    • Feiz, L.1    Beecher, B.2    Martin, J.M.3    Giroux, M.J.4
  • 41
    • 67649213927 scopus 로고    scopus 로고
    • Puroindolines co-localize to the starch granule surface and increase seed-bound polar lipid content
    • Feiz L, Wanjugi HW, Melnyk CW, Altosaar I, Martin JM, Giroux MJ. 2009b. Puroindolines co-localize to the starch granule surface and increase seed-bound polar lipid content. J Cereal Sci 50:91-8.
    • (2009) J Cereal Sci , vol.50 , pp. 91-98
    • Feiz, L.1    Wanjugi, H.W.2    Melnyk, C.W.3    Altosaar, I.4    Martin, J.M.5    Giroux, M.J.6
  • 42
    • 73449121128 scopus 로고    scopus 로고
    • Quantitative characterization of polar lipids from wheat whole meal, flour, and starch
    • Finnie SM, Jeannotte R, Faubion JM. 2009. Quantitative characterization of polar lipids from wheat whole meal, flour, and starch. Cereal Chem 86:637-45.
    • (2009) Cereal Chem , vol.86 , pp. 637-645
    • Finnie, S.M.1    Jeannotte, R.2    Faubion, J.M.3
  • 43
    • 0002305398 scopus 로고
    • Isolation and characterization of amyloplast envelope membranes from Solanum tuberosum
    • Fishwick MJ, Wright AJ. 1980. Isolation and characterization of amyloplast envelope membranes from Solanum tuberosum. Phytochemistry 19:55-9.
    • (1980) Phytochemistry , vol.19 , pp. 55-59
    • Fishwick, M.J.1    Wright, A.J.2
  • 44
    • 0028406286 scopus 로고
    • Triticum aestivum puroindolines, two basic cystine-rich seed proteins: cDNA sequence-analysis and developmental gene-expression
    • Gautier MF, Aleman ME, Guirao A, Marion D, Joudrier P. 1994. Triticum aestivum puroindolines, two basic cystine-rich seed proteins: cDNA sequence-analysis and developmental gene-expression. Plant Mol Biol 25:43-57.
    • (1994) Plant Mol Biol , vol.25 , pp. 43-57
    • Gautier, M.F.1    Aleman, M.E.2    Guirao, A.3    Marion, D.4    Joudrier, P.5
  • 45
    • 0034646623 scopus 로고    scopus 로고
    • Puroindoline genes are highly conserved in diploid ancestor wheats and related species but absent in tetraploid Triticum species
    • Gautier MF, Cosson P, Guirao A, Alary R, Joudrier P. 2000. Puroindoline genes are highly conserved in diploid ancestor wheats and related species but absent in tetraploid Triticum species. Plant Sci 153:81-91.
    • (2000) Plant Sci , vol.153 , pp. 81-91
    • Gautier, M.F.1    Cosson, P.2    Guirao, A.3    Alary, R.4    Joudrier, P.5
  • 46
    • 16244420731 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of common wheat cultivars lacking puroindoline a
    • Gazza L, Nocente F, Ng PKW, Pogna NE. 2005. Genetic and biochemical analysis of common wheat cultivars lacking puroindoline a. Theor Appl Genet 110:470-8.
    • (2005) Theor Appl Genet , vol.110 , pp. 470-478
    • Gazza, L.1    Nocente, F.2    Ng, P.K.W.3    Pogna, N.E.4
  • 47
    • 78650467611 scopus 로고    scopus 로고
    • Development of durum wheat (Triticum turgidum ssp. durum) lines with soft kernel texture by chromosome engineering
    • In: Appels R, Eastwood RF, Lagudah E, Langridge P, Mackay M, McIntyre L, Sharp P, editors. Sydney, Australia: Sydney University Press.
    • Gazza L, Zanella L, Pogna NE. 2008. Development of durum wheat (Triticum turgidum ssp. durum) lines with soft kernel texture by chromosome engineering. In: Appels R, Eastwood RF, Lagudah E, Langridge P, Mackay M, McIntyre L, Sharp P, editors. Proceedings of the 11th International Wheat Genetics Symposium. Sydney, Australia: Sydney University Press. p 339-41.
    • (2008) Proceedings of the 11th International Wheat Genetics Symposium , pp. 339-341
    • Gazza, L.1    Zanella, L.2    Pogna, N.E.3
  • 48
    • 0030783659 scopus 로고    scopus 로고
    • A glycine to serine change in puroindoline b is associated with wheat grain hardness and low levels of starch-surface friabilin
    • Giroux MJ, Morris CF. 1997. A glycine to serine change in puroindoline b is associated with wheat grain hardness and low levels of starch-surface friabilin. Theor Appl Genet 95:857-64.
    • (1997) Theor Appl Genet , vol.95 , pp. 857-864
    • Giroux, M.J.1    Morris, C.F.2
  • 49
    • 0032568572 scopus 로고    scopus 로고
    • Wheat grain hardness results from highly conserved mutations in the friabilin components puroindoline a and b
    • Giroux MJ, Morris CF. 1998. Wheat grain hardness results from highly conserved mutations in the friabilin components puroindoline a and b. Proc Natl Acad Sci USA 95:6262-6.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6262-6266
    • Giroux, M.J.1    Morris, C.F.2
  • 50
    • 0029168338 scopus 로고
    • Relationship between endosperm texture and the occurrence of friabilin and bound polar lipids on wheat starch
    • Greenblatt GA, Bettge AD, Morris CF. 1995. Relationship between endosperm texture and the occurrence of friabilin and bound polar lipids on wheat starch. Cereal Chem 72:172-6.
    • (1995) Cereal Chem , vol.72 , pp. 172-176
    • Greenblatt, G.A.1    Bettge, A.D.2    Morris, C.F.3
  • 51
    • 0000744294 scopus 로고
    • A starch granule protein associated with endosperm softness in wheat
    • Greenwell P, Schofield JD. 1986. A starch granule protein associated with endosperm softness in wheat. Cereal Chem 63:379-80.
    • (1986) Cereal Chem , vol.63 , pp. 379-380
    • Greenwell, P.1    Schofield, J.D.2
  • 52
    • 84985384479 scopus 로고
    • The distribution of acyl lipids in the germ, aleurone, starch and non-starch endosperm of four wheat varieties
    • Hargin KD, Morrison WR. 1980. The distribution of acyl lipids in the germ, aleurone, starch and non-starch endosperm of four wheat varieties. J Sci Food Agric 31:877-88.
    • (1980) J Sci Food Agric , vol.31 , pp. 877-888
    • Hargin, K.D.1    Morrison, W.R.2
  • 53
    • 84879143848 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of puroindoline A and B alleles in Chinese improved cultivars and landraces
    • In: Buck HT, Nisi JE, Salomon N, editors. Dordrecht, the Netherlands: Springer.
    • He ZH, Chen F, Xia XC, Xia LQ, Zhang XY, Lillemo M, Morris CF. 2007. Molecular and biochemical characterization of puroindoline A and B alleles in Chinese improved cultivars and landraces. In: Buck HT, Nisi JE, Salomon N, editors. Wheat production in stressed environments. Dordrecht, the Netherlands: Springer. p 441-8.
    • (2007) Wheat production in stressed environments , pp. 441-448
    • He, Z.H.1    Chen, F.2    Xia, X.C.3    Xia, L.Q.4    Zhang, X.Y.5    Lillemo, M.6    Morris, C.F.7
  • 54
    • 0000207681 scopus 로고
    • TMbase - a database of membrane spanning proteins segments
    • Hofmann K, Stoffel W. 1993. TMbase - a database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 374:166.
    • (1993) Biol Chem Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 55
    • 2142731181 scopus 로고    scopus 로고
    • Wheat puroindolines interact to form friabilin and control wheat grain hardness
    • Hogg AC, Sripo T, Beecher B, Martin JM, Giroux MJ. 2004. Wheat puroindolines interact to form friabilin and control wheat grain hardness. Theor Appl Genet 108:1089-97.
    • (2004) Theor Appl Genet , vol.108 , pp. 1089-1097
    • Hogg, A.C.1    Sripo, T.2    Beecher, B.3    Martin, J.M.4    Giroux, M.J.5
  • 56
    • 0002383187 scopus 로고
    • Structural differences in hard and soft wheat
    • 56.
    • Hoseney RC, Seib PA. 1973. Structural differences in hard and soft wheat. Bakers Dig 47:26-8/56.
    • (1973) Bakers Dig , vol.47 , pp. 26-28
    • Hoseney, R.C.1    Seib, P.A.2
  • 57
    • 0002601682 scopus 로고
    • Comparison of the foaming and interfacial properties of two related lipid-binding proteins from wheat in the presence of a competing surfactant
    • In: Dickinson E, Lorient D, editors. London, UK: Royal Society of Chemistry.
    • Husband F, Wilde PJ, Marion D, Clark DC. 1994. Comparison of the foaming and interfacial properties of two related lipid-binding proteins from wheat in the presence of a competing surfactant. In: Dickinson E, Lorient D, editors. Food macromolecules and colloids. London, UK: Royal Society of Chemistry. p 285-97.
    • (1994) Food macromolecules and colloids , pp. 285-297
    • Husband, F.1    Wilde, P.J.2    Marion, D.3    Clark, D.C.4
  • 58
    • 0042060932 scopus 로고    scopus 로고
    • Conformation of a bactericidal domain of puroindoline a: structure and mechanism of action of a 13-residue antimicrobial peptide
    • Jing WG, Demcoe AR, Vogel HJ. 2003. Conformation of a bactericidal domain of puroindoline a: structure and mechanism of action of a 13-residue antimicrobial peptide. J Bacteriol 185:4938-47.
    • (2003) J Bacteriol , vol.185 , pp. 4938-4947
    • Jing, W.G.1    Demcoe, A.R.2    Vogel, H.J.3
  • 59
    • 34250079623 scopus 로고
    • Characterisation of the wheat Mr 15000 "grain-softness protein" and analysis of the relationship between its accumulation in the whole seed and grain softness
    • Jolly CJ, Rahman S, Kortt AA, Higgings TJV. 1993. Characterisation of the wheat Mr 15000 "grain-softness protein" and analysis of the relationship between its accumulation in the whole seed and grain softness. Theor Appl Genet 86:589-97.
    • (1993) Theor Appl Genet , vol.86 , pp. 589-597
    • Jolly, C.J.1    Rahman, S.2    Kortt, A.A.3    Higgings, T.J.V.4
  • 61
    • 84862790131 scopus 로고    scopus 로고
    • Increased resistance to penicillium seed rot in transgenic wheat over-expressing puroindolines
    • Kim KH, Feiz L, Dyer AT, Grey W, Hogg AC, Martin JM, Giroux MJ. 2012. Increased resistance to penicillium seed rot in transgenic wheat over-expressing puroindolines. J Phytopathol 160:243-7.
    • (2012) J Phytopathol , vol.160 , pp. 243-247
    • Kim, K.H.1    Feiz, L.2    Dyer, A.T.3    Grey, W.4    Hogg, A.C.5    Martin, J.M.6    Giroux, M.J.7
  • 62
    • 84865973850 scopus 로고    scopus 로고
    • Puroindolines are associated with decreased polar lipid breakdown during wheat seed development
    • Kim KH, Feiz L, Martin JM, Giroux MJ. 2012b. Puroindolines are associated with decreased polar lipid breakdown during wheat seed development. J Cereal Sci 52:142-6.
    • (2012) J Cereal Sci , vol.52 , pp. 142-146
    • Kim, K.H.1    Feiz, L.2    Martin, J.M.3    Giroux, M.J.4
  • 63
    • 0001599514 scopus 로고    scopus 로고
    • Spectroscopic characterisation of the lipid-binding properties of wheat puroindolines
    • Kooijman M, Orsel R, Hessing M, Hamer RJ, Bekkers ACAPA. 1997. Spectroscopic characterisation of the lipid-binding properties of wheat puroindolines. J Cereal Sci 26:145-59.
    • (1997) J Cereal Sci , vol.26 , pp. 145-159
    • Kooijman, M.1    Orsel, R.2    Hessing, M.3    Hamer, R.J.4    Bekkers, A.C.A.P.A.5
  • 64
    • 0035129002 scopus 로고    scopus 로고
    • Expression of wheat puroindoline genes in transgenic rice enhances grain softness
    • Krishnamurthy K, Giroux MJ. 2001. Expression of wheat puroindoline genes in transgenic rice enhances grain softness. Nat Biotechnol 19:162-6.
    • (2001) Nat Biotechnol , vol.19 , pp. 162-166
    • Krishnamurthy, K.1    Giroux, M.J.2
  • 66
    • 0029818223 scopus 로고    scopus 로고
    • Determination of the secondary structure and conformation of puroindolines by infrared and Raman spectroscopy
    • Le
    • Le Bihan TL, Blochet JE, Desormeaux A, Marion D, Pezolet M. 1996. Determination of the secondary structure and conformation of puroindolines by infrared and Raman spectroscopy. Biochemistry 35:12712-22.
    • (1996) Biochemistry , vol.35 , pp. 12712-12722
    • Bihan, T.L.1    Blochet, J.E.2    Desormeaux, A.3    Marion, D.4    Pezolet, M.5
  • 67
    • 0032534793 scopus 로고    scopus 로고
    • Interaction of the wheat endosperm lipid-binding protein puroindoline-a with phospholipids
    • Le
    • Le Guernevé C, Seigneuret M, Marion D. 1998. Interaction of the wheat endosperm lipid-binding protein puroindoline-a with phospholipids. Arch Biochem Biophys 360:179-86.
    • (1998) Arch Biochem Biophys , vol.360 , pp. 179-186
    • Guernevé, C.1    Seigneuret, M.2    Marion, D.3
  • 68
    • 33646249121 scopus 로고    scopus 로고
    • Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions
    • Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, Vieths S, Rosch P. 2006. Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem J 395:463-72.
    • (2006) Biochem J , vol.395 , pp. 463-472
    • Lehmann, K.1    Schweimer, K.2    Reese, G.3    Randow, S.4    Suhr, M.5    Becker, W.M.6    Vieths, S.7    Rosch, P.8
  • 69
    • 79953281960 scopus 로고    scopus 로고
    • New insight into puroindoline function inferred from their subcellar localization in developing hard and soft near-isogenic endosperm and their relationship with polymer size of storage proteins
    • Lesage VS, Bouchet B, Rhazi L, Elmorjani K, Branlard G, Marion D. 2011. New insight into puroindoline function inferred from their subcellar localization in developing hard and soft near-isogenic endosperm and their relationship with polymer size of storage proteins. J Cereal Sci 53:231-8.
    • (2011) J Cereal Sci , vol.53 , pp. 231-238
    • Lesage, V.S.1    Bouchet, B.2    Rhazi, L.3    Elmorjani, K.4    Branlard, G.5    Marion, D.6
  • 70
    • 84855878008 scopus 로고    scopus 로고
    • Proteomes of hard and soft near-isogenic wheat lines reveal that kernel hardness is related to the amplification of a stress response during endosperm development
    • Lesage VS, Merlino M, Chambon C, Bouchet B, Marion D, Branlard G. 2012. Proteomes of hard and soft near-isogenic wheat lines reveal that kernel hardness is related to the amplification of a stress response during endosperm development. J Exp Bot 63:1001-11.
    • (2012) J Exp Bot , vol.63 , pp. 1001-1011
    • Lesage, V.S.1    Merlino, M.2    Chambon, C.3    Bouchet, B.4    Marion, D.5    Branlard, G.6
  • 71
    • 0034077696 scopus 로고    scopus 로고
    • A leucine to proline mutation in puroindoline b is frequently present in hard wheats from northern Europe
    • Lillemo M, Morris CF. 2000. A leucine to proline mutation in puroindoline b is frequently present in hard wheats from northern Europe. Theor Appl Genet 100:1100-7.
    • (2000) Theor Appl Genet , vol.100 , pp. 1100-1107
    • Lillemo, M.1    Morris, C.F.2
  • 72
    • 44049095288 scopus 로고    scopus 로고
    • Expression of puroindoline a enhances leaf rust resistance in transgenic tetraploid wheat
    • Luo L, Zhang JR, Yang GX, Li Y, Li KX, He GY. 2008. Expression of puroindoline a enhances leaf rust resistance in transgenic tetraploid wheat. Mol Biol Rep 35:195-200.
    • (2008) Mol Biol Rep , vol.35 , pp. 195-200
    • Luo, L.1    Zhang, J.R.2    Yang, G.X.3    Li, Y.4    Li, K.X.5    He, G.Y.6
  • 73
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur MW, Thornton JM. 1991. Influence of proline residues on protein conformation. J Mol Biol 218:397-412.
    • (1991) J Mol Biol , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 75
    • 79956129888 scopus 로고    scopus 로고
    • Evolution of polyploid Triticum wheats under cultivation: the role of domestication, natural hybridization and allopolyploid speciation in their diversification
    • Matsuoka Y. 2011. Evolution of polyploid Triticum wheats under cultivation: the role of domestication, natural hybridization and allopolyploid speciation in their diversification. Plant Cell Physiol 52:750-64.
    • (2011) Plant Cell Physiol , vol.52 , pp. 750-764
    • Matsuoka, Y.1
  • 77
    • 84867579440 scopus 로고    scopus 로고
    • Expression, purification and antimicrobial activity of puroindoline A protein and its mutants
    • Miao Y, Chen L, Wang C, Wang Y, Zheng Q, Goa C, Yang G, He G. 2012. Expression, purification and antimicrobial activity of puroindoline A protein and its mutants. Amino Acids 43:1689-96.
    • (2012) Amino Acids , vol.43 , pp. 1689-1696
    • Miao, Y.1    Chen, L.2    Wang, C.3    Wang, Y.4    Zheng, Q.5    Goa, C.6    Yang, G.7    He, G.8
  • 78
    • 0036010779 scopus 로고    scopus 로고
    • Puroindolines: the molecular genetic basis of wheat grain hardness
    • Morris CF. 2002. Puroindolines: the molecular genetic basis of wheat grain hardness. Plant Mol Biol 48:633-47.
    • (2002) Plant Mol Biol , vol.48 , pp. 633-647
    • Morris, C.F.1
  • 79
    • 84863555873 scopus 로고    scopus 로고
    • The distal portion of the short arm of wheat (Triticum aestivum L.) chromosome 5D controls endosperm vitreosity and grain hardness
    • Morris CF, Beecher BS. 2012. The distal portion of the short arm of wheat (Triticum aestivum L.) chromosome 5D controls endosperm vitreosity and grain hardness. Theor Appl Genet 125:247-54.
    • (2012) Theor Appl Genet , vol.125 , pp. 247-254
    • Morris, C.F.1    Beecher, B.S.2
  • 80
    • 47549104536 scopus 로고    scopus 로고
    • Reconciliation of D-genome puroindoline allele designations with current DNA sequence data
    • Morris CF, Bhave M. 2008. Reconciliation of D-genome puroindoline allele designations with current DNA sequence data. J Cereal Sci 48:277-87.
    • (2008) J Cereal Sci , vol.48 , pp. 277-287
    • Morris, C.F.1    Bhave, M.2
  • 82
    • 0035121609 scopus 로고    scopus 로고
    • Prevalence of puroindoline grain hardness genotypes among historically significant North American spring and winter wheats
    • Morris CF, Lillemo M, Simeone MC, Giroux MJ, Babb SL, Kidwell KK. 2001. Prevalence of puroindoline grain hardness genotypes among historically significant North American spring and winter wheats. Crop Sci 41:218-28.
    • (2001) Crop Sci , vol.41 , pp. 218-228
    • Morris, C.F.1    Lillemo, M.2    Simeone, M.C.3    Giroux, M.J.4    Babb, S.L.5    Kidwell, K.K.6
  • 83
    • 78650474945 scopus 로고    scopus 로고
    • Transfer of soft kernel texture from Triticum aestivum to durum wheat, Triticum turgidum ssp. durum
    • Morris CF, Simeone MC, King GE, Lafiandra D. 2011. Transfer of soft kernel texture from Triticum aestivum to durum wheat, Triticum turgidum ssp. durum. Crop Sci 51:114-22.
    • (2011) Crop Sci , vol.51 , pp. 114-122
    • Morris, C.F.1    Simeone, M.C.2    King, G.E.3    Lafiandra, D.4
  • 84
    • 0002844905 scopus 로고
    • Wheat lipid composition
    • Morrison WR. 1978. Wheat lipid composition. Cereal Chem 55:548-58.
    • (1978) Cereal Chem , vol.55 , pp. 548-558
    • Morrison, W.R.1
  • 85
    • 84985417793 scopus 로고
    • Distribution of soft wheat kernel lipids into flour milling fractions
    • Morrison WR, Hargin KD. 1981. Distribution of soft wheat kernel lipids into flour milling fractions. J Sci Food Agric 32:579-87.
    • (1981) J Sci Food Agric , vol.32 , pp. 579-587
    • Morrison, W.R.1    Hargin, K.D.2
  • 86
    • 0002658881 scopus 로고
    • The effect of group 5 chromosomes on the free polar lipids and breadmaking quality of wheat
    • Morrison WR, Law CN, Wylie LJ, Coventry AM, Seekings J. 1989. The effect of group 5 chromosomes on the free polar lipids and breadmaking quality of wheat. J Cereal Sci 9:41-51.
    • (1989) J Cereal Sci , vol.9 , pp. 41-51
    • Morrison, W.R.1    Law, C.N.2    Wylie, L.J.3    Coventry, A.M.4    Seekings, J.5
  • 87
    • 0002655738 scopus 로고    scopus 로고
    • Characterisation of friabilin polypeptides
    • Oda S, Schofield JD. 1997. Characterisation of friabilin polypeptides. J Cereal Sci 26:29-36.
    • (1997) J Cereal Sci , vol.26 , pp. 29-36
    • Oda, S.1    Schofield, J.D.2
  • 90
    • 0344011459 scopus 로고    scopus 로고
    • Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis
    • Pantoja-Uceda D, Bruix M, Gimenez-Gallego G, Rico M, Santoro J. 2003. Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. Biochemistry 42:13839-47.
    • (2003) Biochemistry , vol.42 , pp. 13839-13847
    • Pantoja-Uceda, D.1    Bruix, M.2    Gimenez-Gallego, G.3    Rico, M.4    Santoro, J.5
  • 91
    • 2642549932 scopus 로고    scopus 로고
    • Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties
    • Pantoja-Uceda D, Shewry PR, Bruix M, Tatham AS, Santoro J, Rico M. 2004. Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties. Biochemistry 43:6976-86.
    • (2004) Biochemistry , vol.43 , pp. 6976-6986
    • Pantoja-Uceda, D.1    Shewry, P.R.2    Bruix, M.3    Tatham, A.S.4    Santoro, J.5    Rico, M.6
  • 92
    • 81455131539 scopus 로고    scopus 로고
    • Lipids in bread making: sources, interactions, and impact on bread quality
    • Pareyt B, Finnie SM, Putseys JA, Delcour JA. 2011. Lipids in bread making: sources, interactions, and impact on bread quality. J Cereal Sci 54:266-79.
    • (2011) J Cereal Sci , vol.54 , pp. 266-279
    • Pareyt, B.1    Finnie, S.M.2    Putseys, J.A.3    Delcour, J.A.4
  • 93
    • 84879137376 scopus 로고    scopus 로고
    • Wheat (Triticum aestivum L. and T. turgidum L. ssp. durum) kernel hardness: II. Implication for and role of puroindolines in end-product quality
    • Pauly A, Pareyt B, Fierens E, Delcour JA. 2013. Wheat (Triticum aestivum L. and T. turgidum L. ssp. durum) kernel hardness: II. Implication for and role of puroindolines in end-product quality. Compr Rev Food Sci F.
    • (2013) Compr Rev Food Sci F.
    • Pauly, A.1    Pareyt, B.2    Fierens, E.3    Delcour, J.A.4
  • 94
    • 79551622460 scopus 로고    scopus 로고
    • Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides
    • Philips RL, Palombo EA, Panozzo JF, Bhave M. 2011. Puroindolines, Pin alleles, hordoindolines and grain softness proteins are sources of bactericidal and fungicidal peptides. J Cereal Sci 53:112-7.
    • (2011) J Cereal Sci , vol.53 , pp. 112-117
    • Philips, R.L.1    Palombo, E.A.2    Panozzo, J.F.3    Bhave, M.4
  • 95
    • 33645587536 scopus 로고    scopus 로고
    • Wheat
    • In: Kulp K, Ponte JGJ, editors. New York, NY: Marcel Dekker.
    • Posner ES. 2000. Wheat. In: Kulp K, Ponte JGJ, editors. Handbook of cereal science and technology. New York, NY: Marcel Dekker. p 1-29.
    • (2000) Handbook of cereal science and technology , pp. 1-29
    • Posner, E.S.1
  • 96
    • 85018263916 scopus 로고    scopus 로고
    • Wheat flour milling
    • In: Khan K, Shewry PR, editors. St. Paul, MN: AACC International.
    • Posner ES. 2009. Wheat flour milling. In: Khan K, Shewry PR, editors. Wheat: chemistry and technology. St. Paul, MN: AACC International. p 119-52.
    • (2009) Wheat: chemistry and technology , pp. 119-152
    • Posner, E.S.1
  • 98
    • 56349098077 scopus 로고    scopus 로고
    • Genome organisation and retrotransposon driven molecular evolution of the endosperm Hardness (Ha) locus in Triticum aestivum cv. Glenlea
    • Ragupathy R, Cloutier S. 2008. Genome organisation and retrotransposon driven molecular evolution of the endosperm Hardness (Ha) locus in Triticum aestivum cv. Glenlea. Mol Genet Genom 280:467-81.
    • (2008) Mol Genet Genom , vol.280 , pp. 467-481
    • Ragupathy, R.1    Cloutier, S.2
  • 99
    • 0027989849 scopus 로고
    • Cloning of a wheat 15-kDa grain softness protein (GSP) - GSP is a mixture of puroindoline-like polypeptides
    • Rahman S, Jolly CJ, Skerritt JH, Wallosheck A. 1994. Cloning of a wheat 15-kDa grain softness protein (GSP) - GSP is a mixture of puroindoline-like polypeptides. Eur J Biochem 223:917-25.
    • (1994) Eur J Biochem , vol.223 , pp. 917-925
    • Rahman, S.1    Jolly, C.J.2    Skerritt, J.H.3    Wallosheck, A.4
  • 100
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions
    • Schibli DJ, Epand RF, Vogel HJ, Epand RM. 2002. Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochem Cell Biol 80:667-77.
    • (2002) Biochem Cell Biol , vol.80 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, H.J.3    Epand, R.M.4
  • 101
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane proteins
    • Schiffer M, Chang C-H, Stevens FJ. 1992. The functions of tryptophan residues in membrane proteins. Protein Eng 5:213-4.
    • (1992) Protein Eng , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.-H.2    Stevens, F.J.3
  • 102
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig J. 2004. Thermodynamics of lipid-peptide interactions. Biochim Biophys Acta Biomem 1666:40-50.
    • (2004) Biochim Biophys Acta Biomem , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 103
    • 0036010140 scopus 로고    scopus 로고
    • Cereal seed storage proteins: structures, properties and role in grain utilization
    • Shewry PR, Halford NG. 2002. Cereal seed storage proteins: structures, properties and role in grain utilization. J Exp Bot 53:947-58.
    • (2002) J Exp Bot , vol.53 , pp. 947-958
    • Shewry, P.R.1    Halford, N.G.2
  • 105
    • 11144334766 scopus 로고    scopus 로고
    • Isolation and characterisation of friabilin genes in rye
    • Simeone MC, Lafiandra D. 2005. Isolation and characterisation of friabilin genes in rye. J Cereal Sci 41:115-22.
    • (2005) J Cereal Sci , vol.41 , pp. 115-122
    • Simeone, M.C.1    Lafiandra, D.2
  • 108
    • 0033578401 scopus 로고    scopus 로고
    • Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor
    • Sreerama N, Manning MC, Powers ME, Zhang JX, Goldenberg DP, Woody RW. 1999. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor. Biochemistry 38:10814-22.
    • (1999) Biochemistry , vol.38 , pp. 10814-10822
    • Sreerama, N.1    Manning, M.C.2    Powers, M.E.3    Zhang, J.X.4    Goldenberg, D.P.5    Woody, R.W.6
  • 109
    • 33746066004 scopus 로고    scopus 로고
    • Puroindoline b limits binding of puroindoline a to starch and grain softness
    • Swan CG, Meyer FD, Hogg AC, Martin JM, Giroux MJ. 2006. Puroindoline b limits binding of puroindoline a to starch and grain softness. Crop Sci 46:1656-65.
    • (2006) Crop Sci , vol.46 , pp. 1656-1665
    • Swan, C.G.1    Meyer, F.D.2    Hogg, A.C.3    Martin, J.M.4    Giroux, M.J.5
  • 110
    • 84970610806 scopus 로고
    • Inheritance of grain hardness in wheat as measured by particle size index
    • Symes KJ. 1965. Inheritance of grain hardness in wheat as measured by particle size index. Aust J Agric Res 16:113-23.
    • (1965) Aust J Agric Res , vol.16 , pp. 113-123
    • Symes, K.J.1
  • 111
    • 75849157960 scopus 로고    scopus 로고
    • A barley Hordoindoline mutation resulted in an increase in grain hardness
    • Takahashi A, Ikeda TM, Takayama T, Yanagisawa T. 2010. A barley Hordoindoline mutation resulted in an increase in grain hardness. Theor Appl Genet 120:519-26.
    • (2010) Theor Appl Genet , vol.120 , pp. 519-526
    • Takahashi, A.1    Ikeda, T.M.2    Takayama, T.3    Yanagisawa, T.4
  • 112
    • 51249179648 scopus 로고
    • Distribution of lipids in the germ, endosperm, pericarp and tip cap of amylomaize, Lg-11 hybrid maize and waxy maize
    • Tan SL, Morrison WR. 1979. Distribution of lipids in the germ, endosperm, pericarp and tip cap of amylomaize, Lg-11 hybrid maize and waxy maize. J Am Oil Chem Soc 56:531-5.
    • (1979) J Am Oil Chem Soc , vol.56 , pp. 531-535
    • Tan, S.L.1    Morrison, W.R.2
  • 113
    • 0032500703 scopus 로고    scopus 로고
    • Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins
    • Tanchak MA, Schernthaner JP, Giband M, Altosaar I. 1998. Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins. Plant Sci 137:173-84.
    • (1998) Plant Sci , vol.137 , pp. 173-184
    • Tanchak, M.A.1    Schernthaner, J.P.2    Giband, M.3    Altosaar, I.4
  • 114
    • 84862759456 scopus 로고    scopus 로고
    • Trafficking and deposition of prolamins in wheat
    • Tosi P. 2012. Trafficking and deposition of prolamins in wheat. J Cereal Sci 56:81-90.
    • (2012) J Cereal Sci , vol.56 , pp. 81-90
    • Tosi, P.1
  • 115
    • 0036888472 scopus 로고    scopus 로고
    • Substitutions and deletions of genes related to grain hardness in wheat and their effect on grain texture
    • Tranquilli G, Heaton J, Chicaiza O, Dubcovsky J. 2002. Substitutions and deletions of genes related to grain hardness in wheat and their effect on grain texture. Crop Sci 42:1812-7.
    • (2002) Crop Sci , vol.42 , pp. 1812-1817
    • Tranquilli, G.1    Heaton, J.2    Chicaiza, O.3    Dubcovsky, J.4
  • 116
    • 0036841834 scopus 로고    scopus 로고
    • Endosperm texture in wheat
    • Turnbull KM, Rahman S. 2002. Endosperm texture in wheat. J Cereal Sci 36:327-37.
    • (2002) J Cereal Sci , vol.36 , pp. 327-337
    • Turnbull, K.M.1    Rahman, S.2
  • 117
    • 0037639845 scopus 로고    scopus 로고
    • Early expression of grain hardness in the developing wheat endosperm
    • Turnbull KM, Marion D, Gaborit T, Appels R, Rahman S. 2003a. Early expression of grain hardness in the developing wheat endosperm. Planta 216:699-706.
    • (2003) Planta , vol.216 , pp. 699-706
    • Turnbull, K.M.1    Marion, D.2    Gaborit, T.3    Appels, R.4    Rahman, S.5
  • 118
    • 0037572275 scopus 로고    scopus 로고
    • The organization of genes tightly linked to the Ha locus in Aegilops tauschii, the D-genome donor to wheat
    • Turnbull KM, Turner M, Mukai Y, Yamamoto M, Morell MK, Appels R, Rahman S. 2003b. The organization of genes tightly linked to the Ha locus in Aegilops tauschii, the D-genome donor to wheat. Genome 46:330-8.
    • (2003) Genome , vol.46 , pp. 330-338
    • Turnbull, K.M.1    Turner, M.2    Mukai, Y.3    Yamamoto, M.4    Morell, M.K.5    Appels, R.6    Rahman, S.7
  • 120
    • 84879139804 scopus 로고    scopus 로고
    • Wheat data
    • USDA-ERS. Available from: Accessed 2013 February 21.
    • USDA-ERS. 2012. Wheat data. Available from: http://www.ers.usda.gov./ Accessed 2013 February 21.
    • (2012)
  • 122
    • 77956448705 scopus 로고    scopus 로고
    • The tryptophan-rich domain of puroindoline is directly associated with the starch granule surface as judged by tryptic shaving and mass spectrometry
    • Wall ML, Wheeler HL, Smith JC, Figeys D, Altosaar I. 2010. The tryptophan-rich domain of puroindoline is directly associated with the starch granule surface as judged by tryptic shaving and mass spectrometry. J Cereal Sci 52:115-20.
    • (2010) J Cereal Sci , vol.52 , pp. 115-120
    • Wall, M.L.1    Wheeler, H.L.2    Smith, J.C.3    Figeys, D.4    Altosaar, I.5
  • 123
    • 33847305553 scopus 로고    scopus 로고
    • The role of puroindoline A and B individually and in combination on grain hardness and starch association
    • Wanjugi HW, Hogg AC, Martin JM, Giroux MJ. 2007. The role of puroindoline A and B individually and in combination on grain hardness and starch association. Crop Sci 47:67-76.
    • (2007) Crop Sci , vol.47 , pp. 67-76
    • Wanjugi, H.W.1    Hogg, A.C.2    Martin, J.M.3    Giroux, M.J.4
  • 124
    • 34247232760 scopus 로고    scopus 로고
    • Promoter analysis and immunolocalisation show that puroindoline genes are exclusively expressed in starchy endosperm cells of wheat grain
    • Wiley PR, Tosi P, Evrard A, Lovegrove A, Jones HD, Shewry PR. 2007. Promoter analysis and immunolocalisation show that puroindoline genes are exclusively expressed in starchy endosperm cells of wheat grain. Plant Mol Biol 64:125-36.
    • (2007) Plant Mol Biol , vol.64 , pp. 125-136
    • Wiley, P.R.1    Tosi, P.2    Evrard, A.3    Lovegrove, A.4    Jones, H.D.5    Shewry, P.R.6
  • 125
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody RW. 1994. Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur Biophys J Biophy 23:253-62.
    • (1994) Eur Biophys J Biophy , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 126
    • 85027282524 scopus 로고    scopus 로고
    • Wheat: a unique grain for the world
    • In: Khan K, Shewry PR, editors. St. Paul, MN: AACC International.
    • Wrigley CW. 2009. Wheat: a unique grain for the world. In: Khan K, Shewry PR, editors. Wheat: chemistry and technology. St. Paul, MN: AACC International. p 1-17.
    • (2009) Wheat: chemistry and technology , pp. 1-17
    • Wrigley, C.W.1
  • 127
    • 12444258769 scopus 로고    scopus 로고
    • Occurence of puroindoline alleles in Chinese winter wheats
    • Xia LQ, Chen F, He ZH, Chen XM, Morris CF. 2005. Occurence of puroindoline alleles in Chinese winter wheats. Cereal Chem 82:38-43.
    • (2005) Cereal Chem , vol.82 , pp. 38-43
    • Xia, L.Q.1    Chen, F.2    He, Z.H.3    Chen, X.M.4    Morris, C.F.5
  • 128
    • 39649093888 scopus 로고    scopus 로고
    • Silencing of puroindoline a alters the kernel texture in transgenic bread wheat
    • Xia LQ, Geng HW, Chen XM, He ZH, Lillemo M, Morris CF. 2008. Silencing of puroindoline a alters the kernel texture in transgenic bread wheat. J Cereal Sci 47:331-8.
    • (2008) J Cereal Sci , vol.47 , pp. 331-338
    • Xia, L.Q.1    Geng, H.W.2    Chen, X.M.3    He, Z.H.4    Lillemo, M.5    Morris, C.F.6
  • 130
    • 47549086500 scopus 로고    scopus 로고
    • Evidence of physical interactions of puroindoline proteins using the yeast two-hybrid system
    • Ziemann M, Ramalingam A, Bhave M. 2008. Evidence of physical interactions of puroindoline proteins using the yeast two-hybrid system. Plant Sci 175:307-11.
    • (2008) Plant Sci , vol.175 , pp. 307-311
    • Ziemann, M.1    Ramalingam, A.2    Bhave, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.