메뉴 건너뛰기




Volumn 44, Issue 8, 1999, Pages 572-578

The formation of Glutenin Polymer in practice

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0033409258     PISSN: 01466283     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (32)

References (80)
  • 1
    • 0003094095 scopus 로고    scopus 로고
    • Structure-function relationships of wheat proteins
    • S. Damodaran and A. Paraf, Eds. M. Dekker Inc.
    • MacRitchie, F., and Lafiandra, D. Structure-function relationships of wheat proteins. In: Food Proteins and Their Applications. S. Damodaran and A. Paraf, Eds. M. Dekker Inc., 1997.
    • (1997) Food Proteins and their Applications
    • MacRitchie, F.1    Lafiandra, D.2
  • 2
    • 0000118081 scopus 로고
    • A comparative study of the proteins of wheat of diverse baking quality
    • Orth, R.A., and Bushuk, W. A comparative study of the proteins of wheat of diverse baking quality. Cereal Chem. 49:268, 1972.
    • (1972) Cereal Chem. , vol.49 , pp. 268
    • Orth, R.A.1    Bushuk, W.2
  • 3
    • 0001331275 scopus 로고
    • Fractionation and quantitative differences of glutenin from wheat varieties varying in baking quality
    • Huebner, F. R., and Wall, J.S. Fractionation and quantitative differences of glutenin from wheat varieties varying in baking quality. Cereal Chem. 53: 258, 1972.
    • (1972) Cereal Chem. , vol.53 , pp. 258
    • Huebner, F.R.1    Wall, J.S.2
  • 4
    • 0020743169 scopus 로고
    • Solubilization and characterization of wheat gluten proteins; correlations between the amount of aggregated proteins and baking quality
    • Field, J. M., Shewry, P. R., and Miflin, B. J. Solubilization and characterization of wheat gluten proteins; correlations between the amount of aggregated proteins and baking quality. J. Sci. Food Agric. 34:370, 1983.
    • (1983) J. Sci. Food Agric. , vol.34 , pp. 370
    • Field, J.M.1    Shewry, P.R.2    Miflin, B.J.3
  • 5
    • 0002420364 scopus 로고
    • Biochemical basis of flour properties in bread wheats. II. Effects of the variation in the quantity and size distribution of polymeric proteins
    • Gupta, R. B., Khan, K., and MacRitchie, F. Biochemical basis of flour properties in bread wheats. II. Effects of the variation in the quantity and size distribution of polymeric proteins. J. Cereal Sci. 18:23, 1993.
    • (1993) J. Cereal Sci. , vol.18 , pp. 23
    • Gupta, R.B.1    Khan, K.2    MacRitchie, F.3
  • 7
    • 0029999609 scopus 로고    scopus 로고
    • Giant proteins with flour power
    • Wrigley, C. W. Giant proteins with flour power. Nature 381:738, 1996.
    • (1996) Nature , vol.381 , pp. 738
    • Wrigley, C.W.1
  • 9
    • 0002643154 scopus 로고
    • Glutenin structure in relation to wheat quality
    • Y. Pomeranz, Ed. American Association of Cereal Chemists, St. Paul, MN
    • Kasarda, D. D. Glutenin structure in relation to wheat quality. In: Wheat Is Unique. Y. Pomeranz, Ed. American Association of Cereal Chemists, St. Paul, MN, 1989.
    • (1989) Wheat is Unique
    • Kasarda, D.D.1
  • 11
    • 21044440695 scopus 로고
    • The high molecular weight subunits of wheat glutenin
    • Shewry, P. R., Halford, N. G., and Tatham, A. S. The high molecular weight subunits of wheat glutenin. J. Cereal Sci. 15:105, 1992.
    • (1992) J. Cereal Sci. , vol.15 , pp. 105
    • Shewry, P.R.1    Halford, N.G.2    Tatham, A.S.3
  • 12
    • 0001045321 scopus 로고
    • Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sulfatepolyacrylamide gel electrophoresis, and N-terminal amino acid sequencing
    • Lew, E. J. L., Kuzmicky, D. D., and Kasarda, D. D. Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sulfatepolyacrylamide gel electrophoresis, and N-terminal amino acid sequencing. Cereal Chem. 69:508, 1992.
    • (1992) Cereal Chem. , vol.69 , pp. 508
    • Lew, E.J.L.1    Kuzmicky, D.D.2    Kasarda, D.D.3
  • 13
    • 0030665877 scopus 로고    scopus 로고
    • Molecular characterization of a LMW-GS gene located on chromosome 1B and the development of primers specific for the Glu-B3 complex locus in durum wheat
    • D'Ovidio, R., Simeone, M., Masci, S., and Porceddu, E. Molecular characterization of a LMW-GS gene located on chromosome 1B and the development of primers specific for the Glu-B3 complex locus in durum wheat. Theor. Appl. Genet. 95:1119, 1997.
    • (1997) Theor. Appl. Genet. , vol.95 , pp. 1119
    • D'Ovidio, R.1    Simeone, M.2    Masci, S.3    Porceddu, E.4
  • 14
    • 0032244631 scopus 로고    scopus 로고
    • Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer
    • Masci, S., D'Ovidio, R., Lafiandra, D., and Kasarda D. D. Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer. Plant Physiol. 118:1147, 1998.
    • (1998) Plant Physiol. , vol.118 , pp. 1147
    • Masci, S.1    D'Ovidio, R.2    Lafiandra, D.3    Kasarda D, D.4
  • 16
    • 43949161467 scopus 로고
    • Influence of high Mr glutenin subunits on glutenin polymers and rheological properties of gluten and gluten sufractions of near-isogenic lines of wheat Sicco
    • Popineau, Y., Cornec, M., Lefebvre, J., and B. Marchylo. Influence of high Mr glutenin subunits on glutenin polymers and rheological properties of gluten and gluten sufractions of near-isogenic lines of wheat Sicco. J. Cereal Sci. 19:231, 1994.
    • (1994) J. Cereal Sci. , vol.19 , pp. 231
    • Popineau, Y.1    Cornec, M.2    Lefebvre, J.3    Marchylo, B.4
  • 17
    • 85025511673 scopus 로고
    • Dough and baking quality of wheat lines deficient in glutenin subunits controlled by the Glu-A1, Glu-B1 and Glu-D1 loci
    • Lawrence, G. J., MacRitchie, F., and Wrigley, C. W. Dough and baking quality of wheat lines deficient in glutenin subunits controlled by the Glu-A1, Glu-B1 and Glu-D1 loci. J. Cereal Sci. 7:109, 1988.
    • (1988) J. Cereal Sci. , vol.7 , pp. 109
    • Lawrence, G.J.1    MacRitchie, F.2    Wrigley, C.W.3
  • 19
    • 0031890683 scopus 로고    scopus 로고
    • High molecular weight glutenin subunit variation in wild and cultivated einkorn wheats (Triticum ssp. Poaceae)
    • Ciaffi, M., Dominici, L., and Lafiandra D. High molecular weight glutenin subunit variation in wild and cultivated einkorn wheats (Triticum ssp. Poaceae). Pl. Syst. Evol. 209:123, 1998.
    • (1998) Pl. Syst. Evol. , vol.209 , pp. 123
    • Ciaffi, M.1    Dominici, L.2    Lafiandra, D.3
  • 20
    • 72549105482 scopus 로고
    • Polymorphism and genetic control of high-molecular-weight glutenin subunit in wild tetraploid wheat Triticum turgidum var. dicoccoides
    • Levy, A. A., Galili, G., and Feldman, M. Polymorphism and genetic control of high-molecular-weight glutenin subunit in wild tetraploid wheat Triticum turgidum var. dicoccoides. Heredity 61:63, 1988.
    • (1988) Heredity , vol.61 , pp. 63
    • Levy, A.A.1    Galili, G.2    Feldman, M.3
  • 23
    • 0031048143 scopus 로고    scopus 로고
    • Introduction to bread wheat (Triticum aestivum L.) and assessment for bread-making quality of alleles from T. Boeoticum Boiss. Ssp. Thaoudar at Glu-A1 encoding two high-molecular-weight subunits of glutenin
    • Rogers, W. J., Miller, T. E., Payne, P. I., Seekings, J. A., Holt, L. M., and Law, C. N. Introduction to bread wheat (Triticum aestivum L.) and assessment for bread-making quality of alleles from T. boeoticum Boiss. ssp. thaoudar at Glu-A1 encoding two high-molecular-weight subunits of glutenin. Euphytica 93:19, 1997.
    • (1997) Euphytica , vol.93 , pp. 19
    • Rogers, W.J.1    Miller, T.E.2    Payne, P.I.3    Seekings, J.A.4    Holt, L.M.5    Law, C.N.6
  • 25
    • 84989071088 scopus 로고
    • Grain quality and yield characteristics of D-genome disomic substitution lines in Langdon (Triticum turgidum var. durum)
    • Liu, C. Y., Rathjen, A. J., Shepherd, K. W., Gras, P. W., and Giles, L. C. Grain quality and yield characteristics of D-genome disomic substitution lines in Langdon (Triticum turgidum var. durum). Plant Breeding 114:34, 1995.
    • (1995) Plant Breeding , vol.114 , pp. 34
    • Liu, C.Y.1    Rathjen, A.J.2    Shepherd, K.W.3    Gras, P.W.4    Giles, L.C.5
  • 26
    • 84989085051 scopus 로고
    • Transfer of the Glu-D1 gene from chromosome 1D of bread wheat to chromosome 1R in hexaploid triticale
    • Lukaszewki, A. J., and Curtis, C. A. Transfer of the Glu-D1 gene from chromosome 1D of bread wheat to chromosome 1R in hexaploid triticale. Plant Breeding 109:203, 1992.
    • (1992) Plant Breeding , vol.109 , pp. 203
    • Lukaszewki, A.J.1    Curtis, C.A.2
  • 27
    • 0028112645 scopus 로고
    • Transfer of the Glu-D1 gene from chromosome 1D to chromosome 1A in triticale
    • Lukaszewki, A. J. and Curtis, C. A. Transfer of the Glu-D1 gene from chromosome 1D to chromosome 1A in triticale. Plant Breeding 112:177, 1994.
    • (1994) Plant Breeding , vol.112 , pp. 177
    • Lukaszewki, A.J.1    Curtis, C.A.2
  • 29
    • 0031406869 scopus 로고    scopus 로고
    • Isolation of a chromosomally engineered durum wheat line carrying the common wheat Glu-D1d allele
    • Vitellozzi, F., Ciaffi, M., Dominici, L., and Ceoloni, C. Isolation of a chromosomally engineered durum wheat line carrying the common wheat Glu-D1d allele. Agronomie 17:413, 1997.
    • (1997) Agronomie , vol.17 , pp. 413
    • Vitellozzi, F.1    Ciaffi, M.2    Dominici, L.3    Ceoloni, C.4
  • 34
    • 43949171664 scopus 로고
    • New data supporting high Mr glutenin subunits 5 as the determinant of qualitative differences in the pairs 5+10 vs 2+12
    • Lafiandra, D., D'Ovidio, R., Porceddu, E., Margiotta, B., Colaprico, G. New data supporting high Mr glutenin subunits 5 as the determinant of qualitative differences in the pairs 5+10 vs 2+12. J. Cereal Sci. 18:197, 1993.
    • (1993) J. Cereal Sci. , vol.18 , pp. 197
    • Lafiandra, D.1    D'Ovidio, R.2    Porceddu, E.3    Margiotta, B.4    Colaprico, G.5
  • 35
    • 0002658370 scopus 로고
    • Allelic variation at glutenin subunit and gliadin loci, Glu-1, Glu-3 Gli-1 of common wheats. II. Biochemical basis of the allelic effects on dough properties
    • Gupta, R. B., and MacRitchie, F. Allelic variation at glutenin subunit and gliadin loci, Glu-1, Glu-3 and Gli-1 of common wheats. II. Biochemical basis of the allelic effects on dough properties. J. Cereal Sci. 19:19, 1994.
    • (1994) J. Cereal Sci. , vol.19 , pp. 19
    • Gupta, R.B.1    MacRitchie, F.2
  • 36
    • 84990809434 scopus 로고
    • Purification and characterization of HMW glutenin subunits encoded by chromosome 1B of durum wheat (Triticum durum)
    • Tatham, A. S., Field, J. M., Keen, J. N., Jackson, P. J., and Shewry, P. R. Purification and characterization of HMW glutenin subunits encoded by chromosome 1B of durum wheat (Triticum durum). J. Cereal Sci. 14:11, 1991.
    • (1991) J. Cereal Sci. , vol.14 , pp. 11
    • Tatham, A.S.1    Field, J.M.2    Keen, J.N.3    Jackson, P.J.4    Shewry, P.R.5
  • 37
    • 0003011013 scopus 로고
    • Purification and characterization of high Mr glutenin subunit 20 and its linked y-type subunit from durum wheat
    • Buonocore, F., Caporale, C., Lafiandra, D. Purification and characterization of high Mr glutenin subunit 20 and its linked y-type subunit from durum wheat. J. Cereal Sci. 23:195, 1995.
    • (1995) J. Cereal Sci. , vol.23 , pp. 195
    • Buonocore, F.1    Caporale, C.2    Lafiandra, D.3
  • 38
    • 0001920021 scopus 로고    scopus 로고
    • On the elasticity of wheat gluten
    • Belton, P. S. On the elasticity of wheat gluten. J. Cereal Sci. 29:103, 1999.
    • (1999) J. Cereal Sci. , vol.29 , pp. 103
    • Belton, P.S.1
  • 39
    • 85010878056 scopus 로고
    • 1D-coded D subunits of low-molecular-weight glutenins from Chinese spring have 1D-coded omega-type N-terminal sequences and contain cysteine
    • Masci, S. M., Lafiandra, D., Porceddu, E., Lew, E. J.-L., Tao, H. P., Kasarda, D. D. 1D-coded D subunits of low-molecular-weight glutenins from Chinese Spring have 1D-coded omega-type N-terminal sequences and contain cysteine. Cereal Chem. 70:581, 1993.
    • (1993) Cereal Chem. , vol.70 , pp. 581
    • Masci, S.M.1    Lafiandra, D.2    Porceddu, E.3    Lew, E.J.-L.4    Tao, H.P.5    Kasarda, D.D.6
  • 40
    • 0003348435 scopus 로고    scopus 로고
    • Purification and characterization of a novel polymeric endosperm protein from wheat (Triticum aestivum L.)
    • C. W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne
    • Gianibelli, M. C., Larroque, O., and MacRitchie, F. Purification and characterization of a novel polymeric endosperm protein from wheat (Triticum aestivum L.). In: Gluten '96. C. W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne, 1996.
    • (1996) Gluten '96
    • Gianibelli, M.C.1    Larroque, O.2    MacRitchie, F.3
  • 41
    • 0031873120 scopus 로고    scopus 로고
    • Biochemical characterisation of a D glutenin subunit encoded at the Glu-B3 locus
    • Nieto-Taladriz, M. T., Rodriguez-Quijano, M., and Carrillo, M. J. Biochemical characterisation of a D glutenin subunit encoded at the Glu-B3 locus. Genome 41:215, 1998.
    • (1998) Genome , vol.41 , pp. 215
    • Nieto-Taladriz, M.T.1    Rodriguez-Quijano, M.2    Carrillo, M.J.3
  • 42
    • 0031062310 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of novel low molecular weight glutenin subunits in wheat (Triticum aestivum L.)
    • Sreeramulu, G., and Singh, N. K. Genetic and biochemical characterization of novel low molecular weight glutenin subunits in wheat (Triticum aestivum L.). Genome 40:41, 1997.
    • (1997) Genome , vol.40 , pp. 41
    • Sreeramulu, G.1    Singh, N.K.2
  • 43
    • 0030799308 scopus 로고    scopus 로고
    • The a-gliadin gene family. I. Characterization of ten new wheat a-gliadin genomic clones, evidence for limited sequence conservation of flanking DNA, and Southern analysis of the gene family
    • Anderson, J. C. Litts, F. C. Greene. The a-gliadin gene family. I. Characterization of ten new wheat a-gliadin genomic clones, evidence for limited sequence conservation of flanking DNA, and Southern analysis of the gene family. Theor. Appl. Genet. 95:50, 1997.
    • (1997) Theor. Appl. Genet. , vol.95 , pp. 50
    • Anderson, J.C.1    Litts, F.C.2    Greene3
  • 44
    • 0028888451 scopus 로고    scopus 로고
    • Nucleotide sequence of a g-gliadin type gene from a durum wheat: Correlation with a g-type glutenin subunit from the same biotype
    • D'Ovidio, R., Simeone, M., Masci, S., Porceddu, E. and Kasarda, D. D. Nucleotide sequence of a g-gliadin type gene from a durum wheat: Correlation with a g-type glutenin subunit from the same biotype. Cereal Chem. 72: 443, 1996.
    • (1996) Cereal Chem. , vol.72 , pp. 443
    • D'Ovidio, R.1    Simeone, M.2    Masci, S.3    Porceddu, E.4    Kasarda, D.D.5
  • 45
    • 0029318631 scopus 로고
    • Disulfide bonds in wheat gluten: Cystine peptides derived from gluten proteins following peptic and thermolytic digestion
    • Keck, B., Kohler, P., and Wieser, H. Disulfide bonds in wheat gluten: cystine peptides derived from gluten proteins following peptic and thermolytic digestion. Z. Lebensm. Unters. Forsch. 200:432, 1995.
    • (1995) Z. Lebensm. Unters. Forsch. , vol.200 , pp. 432
    • Keck, B.1    Kohler, P.2    Wieser, H.3
  • 46
    • 0002459318 scopus 로고    scopus 로고
    • Evidence for the presence of only one cysteine residue in the D-type low molecular weight subunits of wheat glutenin
    • Masci, S., Egorov, T. A., Ronchi, C., Kuzmicky, D. D., Lafiandra, D., and Kasarda, D. D. Evidence for the presence of only one cysteine residue in the D-type low molecular weight subunits of wheat glutenin. J. Cereal Sci. 29:17, 1999.
    • (1999) J. Cereal Sci. , vol.29 , pp. 17
    • Masci, S.1    Egorov, T.A.2    Ronchi, C.3    Kuzmicky, D.D.4    Lafiandra, D.5    Kasarda, D.D.6
  • 48
    • 0028248829 scopus 로고
    • A null Gli-D1 allele with a positive effect on bread wheat quality
    • Branlard, G., and Dardevet, M. A. A null Gli-D1 allele with a positive effect on bread wheat quality. J. Cereal Sci. 20:235, 1994.
    • (1994) J. Cereal Sci. , vol.20 , pp. 235
    • Branlard, G.1    Dardevet, M.A.2
  • 49
    • 0041147545 scopus 로고    scopus 로고
    • Effects of allelic variation at the Glu-D1 and Gli-D1/Glu-D3 loci on dough and polymer properties
    • C.W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne
    • Ciaffi, M., Lafiandra, D., Dominici, L., Ravaglia, S., Gupta, R., and MacRitchie, F. Effects of allelic variation at the Glu-D1 and Gli-D1/Glu-D3 loci on dough and polymer properties. In: Gluten '96, C.W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne, 1996.
    • (1996) Gluten '96
    • Ciaffi, M.1    Lafiandra, D.2    Dominici, L.3    Ravaglia, S.4    Gupta, R.5    MacRitchie, F.6
  • 50
    • 0032923390 scopus 로고    scopus 로고
    • Sequence variation at the Sec-1 locus of rye, Secale ce reale (Poaceae)
    • Clarke, B. C., and Appels, R. Sequence variation at the Sec-1 locus of rye, Secale ce reale (Poaceae). Pl. Syst. Evol. 214:1, 1999.
    • (1999) Pl. Syst. Evol. , vol.214 , pp. 1
    • Clarke, B.C.1    Appels, R.2
  • 51
    • 0009533029 scopus 로고    scopus 로고
    • Evidences for the presence of disulfide bonds between beta-amylase and low molecular weight glutenin subunits
    • C. W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne
    • Peruffo, A. D. B., Pogna, N. E., and Curioni, A. Evidences for the presence of disulfide bonds between beta-amylase and low molecular weight glutenin subunits. In: Gluten '96, C. W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne, 1996.
    • (1996) Gluten '96
    • Peruffo, A.D.B.1    Pogna, N.E.2    Curioni, A.3
  • 52
    • 0005183802 scopus 로고    scopus 로고
    • The quantity of bound beta-amylases is related to the size of gluten polymers
    • C. W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne
    • Curioni, A., Pogna, N. E., and Peruffo, A. D. B. The quantity of bound beta-amylases is related to the size of gluten polymers. In: Gluten '96, C. W. Wrigley, Ed. Royal Australian Chemical Institute, Melbourne, 1996.
    • (1996) Gluten '96
    • Curioni, A.1    Pogna, N.E.2    Peruffo, A.D.B.3
  • 53
    • 0002316286 scopus 로고
    • Genotype and environment effects on quality characteristics of hard red winter wheat
    • Peterson, C. J., Graybosch, R. A., Baezinger, P. S., and Grombacher, A. W. Genotype and environment effects on quality characteristics of hard red winter wheat. Crop Sci. 32:98, 1992.
    • (1992) Crop Sci. , vol.32 , pp. 98
    • Peterson, C.J.1    Graybosch, R.A.2    Baezinger, P.S.3    Grombacher, A.W.4
  • 54
    • 0001178017 scopus 로고
    • Quantitative variation among gliadins of wheats grown in different environments
    • Huebner, F. R., and Bietz, J. A. Quantitative variation among gliadins of wheats grown in different environments. Cereal Chem. 65:362, 1988.
    • (1988) Cereal Chem. , vol.65 , pp. 362
    • Huebner, F.R.1    Bietz, J.A.2
  • 55
    • 0000766050 scopus 로고
    • Effect of environment on wheat storage proteins as determined by quantitative reversed-phase high-performance liquid chromatography
    • Marchylo, B. A., Kruger, J. E., and Hatcher, D. W. Effect of environment on wheat storage proteins as determined by quantitative reversed-phase high-performance liquid chromatography. Cereal Chem. 67:370, 1990.
    • (1990) Cereal Chem. , vol.67 , pp. 370
    • Marchylo, B.A.1    Kruger, J.E.2    Hatcher, D.W.3
  • 56
    • 0002251311 scopus 로고
    • Combined reversed phase high performance liquid chromatography (RP-HPLC) and electrophoretical techniques in genetics and breeding of wheat storage proteins
    • J. E. Kruger and J. A. Bietz, Eds. American Association of Cereal Chemists, St. Paul, MN
    • Lafiandra D., Porceddu, E., Colaprico, G., Margiotta, B. Combined reversed phase high performance liquid chromatography (RP-HPLC) and electrophoretical techniques in genetics and breeding of wheat storage proteins. In: HPLC of Cereal and Legume Proteins. J. E. Kruger and J. A. Bietz, Eds. American Association of Cereal Chemists, St. Paul, MN, 1994.
    • (1994) HPLC of Cereal and Legume Proteins
    • Lafiandra, D.1    Porceddu, E.2    Colaprico, G.3    Margiotta, B.4
  • 57
    • 0001959557 scopus 로고
    • Quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis of total proteins extracted from different wheat varieties: Effect of protein content
    • Fullington, J. G., Cole, E. W., and Kasarda, D. D. Quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis of total proteins extracted from different wheat varieties: effect of protein content. Cereal Chem. 60:65, 1983.
    • (1983) Cereal Chem. , vol.60 , pp. 65
    • Fullington, J.G.1    Cole, E.W.2    Kasarda, D.D.3
  • 58
    • 34250120069 scopus 로고
    • The effect of additions of Aegilops longissima chromosomes on grain protein in common wheat
    • Levy, A. A., Galili, G., and Feldman, M. The effect of additions of Aegilops longissima chromosomes on grain protein in common wheat. Theor. Appl. Genet. 69:429, 1985.
    • (1985) Theor. Appl. Genet. , vol.69 , pp. 429
    • Levy, A.A.1    Galili, G.2    Feldman, M.3
  • 59
    • 0000933271 scopus 로고
    • Relationships between protein composition and functional properties of wheat hours
    • Gupta, R. B., Batey, I. L., and MacRitchie, F. Relationships between protein composition and functional properties of wheat Hours. Cereal Chem. 69:125, 1992.
    • (1992) Cereal Chem. , vol.69 , pp. 125
    • Gupta, R.B.1    Batey, I.L.2    MacRitchie, F.3
  • 60
    • 0000486919 scopus 로고
    • Influence of nitrogen on the potential bread-baking quality of two wheat cultivars differing in their responses to increasing nitrogen supplies
    • Scheromm, P., Martin, G., Bergoin, A., and Autran, J. C. Influence of nitrogen on the potential bread-baking quality of two wheat cultivars differing in their responses to increasing nitrogen supplies. Cereal Chem. 69:664, 1992.
    • (1992) Cereal Chem. , vol.69 , pp. 664
    • Scheromm, P.1    Martin, G.2    Bergoin, A.3    Autran, J.C.4
  • 61
    • 0030859718 scopus 로고    scopus 로고
    • Effect of nitrogen fertilization on quantity of flour protein components, dough properties, and breadmaking quality of wheat
    • Pechanek, U., Karger, A., Groger, S., Charvat, B., Schoggl, G., and Lelley, T. Effect of nitrogen fertilization on quantity of flour protein components, dough properties, and breadmaking quality of wheat. Cereal Chem. 74:800, 1997.
    • (1997) Cereal Chem. , vol.74 , pp. 800
    • Pechanek, U.1    Karger, A.2    Groger, S.3    Charvat, B.4    Schoggl, G.5    Lelley, T.6
  • 62
    • 0001517289 scopus 로고
    • Quality-related endosperm proteins in sulfur-deficient and normal wheat grain
    • Fullington, J. G., Miskelly, D. M., Wrigley, C. W., and Kasarda, D. D. Quality-related endosperm proteins in sulfur-deficient and normal wheat grain. J. Cereal Sci. 5:233, 1987.
    • (1987) J. Cereal Sci. , vol.5 , pp. 233
    • Fullington, J.G.1    Miskelly, D.M.2    Wrigley, C.W.3    Kasarda, D.D.4
  • 63
    • 0000178535 scopus 로고
    • Functionality-composition relationships of wheat flour as a result of variation in sulfur availability
    • MacRitchie, F., and Gupta, R. Functionality-composition relationships of wheat flour as a result of variation in sulfur availability. Aust. J. Agric. Res. 44:1767, 1993.
    • (1993) Aust. J. Agric. Res. , vol.44 , pp. 1767
    • MacRitchie, F.1    Gupta, R.2
  • 64
    • 84971056579 scopus 로고
    • Some effects of temperature regime during grain filling in wheat quality
    • Randall, P. J., and Moss, H. J. Some effects of temperature regime during grain filling in wheat quality. Aust. J. Agric. Res. 41:603, 1990.
    • (1990) Aust. J. Agric. Res. , vol.41 , pp. 603
    • Randall, P.J.1    Moss, H.J.2
  • 65
    • 84970583578 scopus 로고
    • Seasonal changes in wheat grain quality associated with high temperatures during grain filling
    • Blumenthal, C. S., Batey, I. L., Bekes, F., Wrigley. C. W., and Barlow, E. W. R. Seasonal changes in wheat grain quality associated with high temperatures during grain filling. Aust. J. Agric. Res. 42:21, 1991.
    • (1991) Aust. J. Agric. Res. , vol.42 , pp. 21
    • Blumenthal, C.S.1    Batey, I.L.2    Bekes, F.3    Wrigley C, W.4    Barlow, E.W.R.5
  • 66
    • 0000028843 scopus 로고
    • Wheat cultivars vary widely in their responses of grain yield and quality to short periods of post-anthesis heat stress
    • Stone, P. J., and Nicholas, M. E. Wheat cultivars vary widely in their responses of grain yield and quality to short periods of post-anthesis heat stress. Aust. J. Plant Physiol. 21:887, 1994.
    • (1994) Aust. J. Plant Physiol. , vol.21 , pp. 887
    • Stone, P.J.1    Nicholas, M.E.2
  • 68
    • 0002452667 scopus 로고
    • Environmental modification of hard red winter whet flour protein composition
    • Graybosch, R. A., Peterson, C. J., Baezinger, P. S., and Shelton, D. R. Environmental modification of hard red winter whet flour protein composition. J. Cereal Sci. 22:45, 1995.
    • (1995) J. Cereal Sci. , vol.22 , pp. 45
    • Graybosch, R.A.1    Peterson, C.J.2    Baezinger, P.S.3    Shelton, D.R.4
  • 69
    • 0031826890 scopus 로고    scopus 로고
    • Quality of hard red winter wheat grown under high temperature conditions during maturation and ripening
    • Gibson, L. R., McCluskey, P. J., Tilley, K. A., and Paulsen, G. M. Quality of hard red winter wheat grown under high temperature conditions during maturation and ripening. Cereal Chem. 75:421, 1998.
    • (1998) Cereal Chem. , vol.75 , pp. 421
    • Gibson, L.R.1    McCluskey, P.J.2    Tilley, K.A.3    Paulsen, G.M.4
  • 71
    • 0001054078 scopus 로고
    • Temperature variation during grain filling and changes in wheat-grain quality
    • Wrigley, C. W., Blumenthal, C., Gras, P. W., and Barlow, E. W. R. Temperature variation during grain filling and changes in wheat-grain quality. Aust. J. Plant Physiol. 21:875, 1994.
    • (1994) Aust. J. Plant Physiol. , vol.21 , pp. 875
    • Wrigley, C.W.1    Blumenthal, C.2    Gras, P.W.3    Barlow, E.W.R.4
  • 72
    • 0031850220 scopus 로고    scopus 로고
    • Effects of cultivar and temperature during grain filling on wheat protein content, composition, and dough mixing properties
    • Uhlen, A. K., Hafskjold, R., Kalhovd, A. H., Sahlstrom, S., Longva, A., and Magnus, E. M. Effects of cultivar and temperature during grain filling on wheat protein content, composition, and dough mixing properties. Cereal Chem. 75:460, 1998.
    • (1998) Cereal Chem. , vol.75 , pp. 460
    • Uhlen, A.K.1    Hafskjold, R.2    Kalhovd, A.H.3    Sahlstrom, S.4    Longva, A.5    Magnus, E.M.6
  • 73
    • 0002298387 scopus 로고
    • Growth environment and wheat quality: The effect of heat stress on dough properties and gluten proteins
    • Blumenthal, C. S., Barlow, E. W. R., and Wrigley, C. W. Growth environment and wheat quality: the effect of heat stress on dough properties and gluten proteins. J. Cereal Sci. 18:3, 1993.
    • (1993) J. Cereal Sci. , vol.18 , pp. 3
    • Blumenthal, C.S.1    Barlow, E.W.R.2    Wrigley, C.W.3
  • 74
    • 0039368071 scopus 로고
    • Effect of heat stress on the pattern of protein synthesis in wheat endosperm
    • J. F. Panozzo and P. G. Downie, Eds. Royal Australian Chemical Institute, Melbourne
    • th Australian Cereal Chemistry Conference. J. F. Panozzo and P. G. Downie, Eds. Royal Australian Chemical Institute, Melbourne, 1994.
    • (1994) th Australian Cereal Chemistry Conference
    • Bernardin, J.E.1    Witt, S.C.2    Milenic, J.3
  • 75
    • 0002977126 scopus 로고    scopus 로고
    • Effect of heat shock during grain filling on the gluten protein composition of bread wheat
    • Ciaffi, M., Tozzi, L., Borghi, B., Corbellini, M., and Lafiandra, D. Effect of heat shock during grain filling on the gluten protein composition of bread wheat. J. Cereal Sci. 24:91, 1996.
    • (1996) J. Cereal Sci. , vol.24 , pp. 91
    • Ciaffi, M.1    Tozzi, L.2    Borghi, B.3    Corbellini, M.4    Lafiandra, D.5
  • 76
    • 0030449994 scopus 로고    scopus 로고
    • Effect of timing of heat stress during grain filling on two wheat varieties differing in heat tolerance. II. Fractional protein accumulation
    • Stone, P. J., and Nicholas, M. E. Effect of timing of heat stress during grain filling on two wheat varieties differing in heat tolerance. II. Fractional protein accumulation. Aust. J. Plant Physiol. 23:739, 1996.
    • (1996) Aust. J. Plant Physiol. , vol.23 , pp. 739
    • Stone, P.J.1    Nicholas, M.E.2
  • 77
    • 0029199626 scopus 로고
    • Identification of wheat genotypes tolerant to the effects of heat stress on grain quality
    • Blumenthal, C. S., Bekes, F., Gras, P. W., Barlow, E. W. R., and Wrigley, C. W. Identification of wheat genotypes tolerant to the effects of heat stress on grain quality. Cereal Chem. 72:539, 1995.
    • (1995) Cereal Chem. , vol.72 , pp. 539
    • Blumenthal, C.S.1    Bekes, F.2    Gras, P.W.3    Barlow, E.W.R.4    Wrigley, C.W.5
  • 78
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston, R. S., Viitanen, P. V., and Vierling, E. Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32:191, 1996.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 79
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can mantain a substrate in a folding-competent state
    • Lee, G. J., Roseman, A. M., Saibil, H. R., and Vierling, E. A small heat shock protein stably binds heat-denatured model substrates and can mantain a substrate in a folding-competent state. EMBO J. 16:659, 1997.
    • (1997) EMBO J. , vol.16 , pp. 659
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 80
    • 0030722384 scopus 로고    scopus 로고
    • Heat shock temperature acclimation of normal secretory protein synthesis in barley aleurone cells
    • Campbell, J. D., Fielding, L. A., and Brodl, M. R. Heat shock temperature acclimation of normal secretory protein synthesis in barley aleurone cells. Plant, Cell & Env. 20:1349, 1997.
    • (1997) Plant, Cell & Env. , vol.20 , pp. 1349
    • Campbell, J.D.1    Fielding, L.A.2    Brodl, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.