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Volumn , Issue , 2011, Pages 449-477

Biochemistry, Physiology, and Genetics of Endosperm Mobilization in Germinated Barley Grain

Author keywords

Barley grain structure and composition; Biochemistry, physiology and genetics of endosperm mobilization in germinated barley grain; Composition of mature barley grain; Deposition of key cell wall polysaccharides in developing endosperm of barley; Enzymes, hydrolyzing maltose and small maltodextrins to glucose, complete hydrolysis of starch; Hormonal regulation of germination in barley grain; Hydrolytic enzyme importance in malting and brewing industries, barley breeders selecting for rapid and uniform modification of barley grain; Newly introduced breeding technologies as quantitative trait locus (QTL) analyses, emerging in the 1990s; Phytohormone role antagonistic phytohormones GA and abscisic acid (ABA), involved in a complex interplay of activities; Thioredoxins, playing important roles in germinated barley grain

Indexed keywords


EID: 84886459352     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470958636.ch14     Document Type: Chapter
Times cited : (17)

References (191)
  • 1
    • 0016611070 scopus 로고
    • New substrate for investigating specificity of beta-glucan hydolases
    • Anderson, M.A. and B.A. Stone. 1975. New substrate for investigating specificity of beta-glucan hydolases. FEBS Lett. 52:202-207.
    • (1975) FEBS Lett , vol.52 , pp. 202-207
    • Anderson, M.A.1    Stone, B.A.2
  • 2
    • 0002536774 scopus 로고
    • Solution properties of wheat-flour arabinoxylans and enzymatically modified arabinoxylans
    • Andrewartha, K.A., D.R. Phillips, and B.A. Stone. 1979. Solution properties of wheat-flour arabinoxylans and enzymatically modified arabinoxylans. Carbohydr. Res. 77:191.
    • (1979) Carbohydr. Res , vol.77 , pp. 191
    • Andrewartha, K.A.1    Phillips, D.R.2    Stone, B.A.3
  • 3
    • 4243848387 scopus 로고
    • Mobilization of polysaccharide reserves from endosperm
    • In D.R. Murray (ed.)., 2:Germination and Reserve Mobilization. Academic Press, Sydney.
    • Ashford, A.E. and F. Gubler. 1984. Mobilization of polysaccharide reserves from endosperm,, pp. 117-162. In D.R. Murray (ed.). Seed Physiology. 2:Germination and Reserve Mobilization. Academic Press, Sydney.
    • (1984) Seed Physiology , pp. 117-162
    • Ashford, A.E.1    Gubler, F.2
  • 4
    • 0001731592 scopus 로고
    • Chemistry and organization of aleurone cell wall components from wheat and barley
    • Bacic, A. and B.A. Stone. 1981. Chemistry and organization of aleurone cell wall components from wheat and barley. Aust. J. Plant Physiol. 8:475-495.
    • (1981) Aust. J. Plant Physiol , vol.8 , pp. 475-495
    • Bacic, A.1    Stone, B.A.2
  • 5
    • 34247601653 scopus 로고    scopus 로고
    • Spatio-temporal profiling and degradation of alpha-amylase isozymes during barley seed germination
    • Bak-Jensen, K.S., S. Laugesen, O. Ostergaard, C. Finnie, P. Roepstorff, and B. Svensson. 2007. Spatio-temporal profiling and degradation of alpha-amylase isozymes during barley seed germination. FEBS J. 274:2552-2565.
    • (2007) FEBS J , vol.274 , pp. 2552-2565
    • Bak-Jensen, K.S.1    Laugesen, S.2    Ostergaard, O.3    Finnie, C.4    Roepstorff, P.5    Svensson, B.6
  • 8
    • 0030238170 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs encoding (1→4)-ß-xylan endohydro-lases from the aleurone layer of germinated barley (Hordeum vulgare)
    • Banik, M., T.P.J. Garrett, and G.B. Fincher. 1996. Molecular cloning of cDNAs encoding (1→4)-ß-xylan endohydro-lases from the aleurone layer of germinated barley (Hordeum vulgare). Plant Mol. Biol. 31:1163-1172.
    • (1996) Plant Mol. Biol , vol.31 , pp. 1163-1172
    • Banik, M.1    Garrett, T.P.J.2    Fincher, G.B.3
  • 9
    • 0031025401 scopus 로고    scopus 로고
    • Structure, hormonal regulation and chromosomal location of genes encoding barley (1→4)-ß-xylan endohydrolases
    • Banik, M., C.-D. Li, P. Langridge, and G.B. Fincher. 1997. Structure, hormonal regulation and chromosomal location of genes encoding barley (1→4)-ß-xylan endohydrolases. Mol. Gen. Genet. 253:599-608.
    • (1997) Mol. Gen. Genet , vol.253 , pp. 599-608
    • Banik, M.1    Li, C.-D.2    Langridge, P.3    Fincher, G.B.4
  • 10
    • 0003914094 scopus 로고    scopus 로고
    • Seeds:Ecology, Biogeography, and Evolution of Dormancy and Germination
    • Academic Press, San Diego, CA.
    • Baskin, C.C. and J.M. Baskin. 1998. Seeds:Ecology, Biogeography, and Evolution of Dormancy and Germination. Academic Press, San Diego, CA.
    • (1998)
    • Baskin, C.C.1    Baskin, J.M.2
  • 11
    • 0036302168 scopus 로고    scopus 로고
    • Plant thioredoxins:the multiplicity conundrum
    • Baumann, U. and J. Juttner. 2002. Plant thioredoxins:the multiplicity conundrum. Cell. Mol. Life Sci. 59:1042-1057.
    • (2002) Cell. Mol. Life Sci , vol.59 , pp. 1042-1057
    • Baumann, U.1    Juttner, J.2
  • 12
    • 34948847005 scopus 로고    scopus 로고
    • Indirect enzyme-antibody sandwich enzyme-linked immunosorbent assay for quantification of TAXI and XIP type xylanase inhibitors in wheat and other cereals
    • Beaugrand, J., K. Gebruers, C. Ververken, E. Fierens, E. Dornez, B.M. Goddeeris, J.A. Delcour, and C.M. Courtin. 2007. Indirect enzyme-antibody sandwich enzyme-linked immunosorbent assay for quantification of TAXI and XIP type xylanase inhibitors in wheat and other cereals. J. Agric. Food Chem. 55:7682-7688.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 7682-7688
    • Beaugrand, J.1    Gebruers, K.2    Ververken, C.3    Fierens, E.4    Dornez, E.5    Goddeeris, B.M.6    Delcour, J.A.7    Courtin, C.M.8
  • 13
    • 0000892934 scopus 로고
    • Purification and characterization of barley aleurone xylanase
    • Benjavongkulchai, E. and M.S. Spencer. 1986. Purification and characterization of barley aleurone xylanase. Planta 169:415-419.
    • (1986) Planta , vol.169 , pp. 415-419
    • Benjavongkulchai, E.1    Spencer, M.S.2
  • 14
    • 0033082464 scopus 로고    scopus 로고
    • Endosperm development
    • Berger, F. 1999. Endosperm development. Curr. Opin. Plant Biol. 2:28-32.
    • (1999) Curr. Opin. Plant Biol , vol.2 , pp. 28-32
    • Berger, F.1
  • 15
    • 0029928068 scopus 로고    scopus 로고
    • Thiocalsin:a thioredoxin-linked, substrate-specific protease dependent on calcium
    • Besse, I., J.H. Wong, K. Kobrehel, and B.B. Buchanan. 1996. Thiocalsin:a thioredoxin-linked, substrate-specific protease dependent on calcium. Proc. Natl. Acad. Sci. U. S. A. 93:3169-3175.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 3169-3175
    • Besse, I.1    Wong, J.H.2    Kobrehel, K.3    Buchanan, B.B.4
  • 16
    • 0035127810 scopus 로고    scopus 로고
    • Cell death of barley aleu-rone protoplasts is mediated by reactive oxygen species
    • Bethke, P.C. and R.L. Jones. 2001. Cell death of barley aleu-rone protoplasts is mediated by reactive oxygen species. Plant J. 25:19-29.
    • (2001) Plant J , vol.25 , pp. 19-29
    • Bethke, P.C.1    Jones, R.L.2
  • 17
    • 0032740905 scopus 로고    scopus 로고
    • Hormonally regulated programmed cell death in barley aleurone cells
    • Bethke, P.C., J.E. Lonsdale, A. Fath, and R.L. Jones. 1999. Hormonally regulated programmed cell death in barley aleurone cells. Plant Cell 11:1033-1046.
    • (1999) Plant Cell , vol.11 , pp. 1033-1046
    • Bethke, P.C.1    Lonsdale, J.E.2    Fath, A.3    Jones, R.L.4
  • 18
    • 0003961667 scopus 로고
    • Physiology and Biochemistry of Seeds in Relation to Germination
    • Springer, Berlin.
    • Bewley,J.D. and M. Black. 1983. Physiology and Biochemistry of Seeds in Relation to Germination, Vol. I. Springer, Berlin.
    • (1983) , vol.I
    • Bewley, J.D.1    Black, M.2
  • 19
    • 41649104153 scopus 로고    scopus 로고
    • Quantifying the sensitivity of barley seed germination to oxygen, abscisic acid, and gibberellin using a population-based threshold model
    • Bradford, K.J., R.L. Benech-Arnold, D. Côme, and F. Corbineau. 2008. Quantifying the sensitivity of barley seed germination to oxygen, abscisic acid, and gibberellin using a population-based threshold model. J. Exp. Bot. 59:335-347.
    • (2008) J. Exp. Bot , vol.59 , pp. 335-347
    • Bradford, K.J.1    Benech-Arnold, R.L.2    Côme, D.3    Corbineau, F.4
  • 20
    • 19344378949 scopus 로고    scopus 로고
    • The potential use of (1→3,1→4)-ß-D-glucans as functional food ingredients
    • Brennan, C.S. and L.J. Cleary. 2005. The potential use of (1→3,1→4)-ß-D-glucans as functional food ingredients. J. Cereal Sci. 42:1-13.
    • (2005) J. Cereal Sci , vol.42 , pp. 1-13
    • Brennan, C.S.1    Cleary, L.J.2
  • 21
    • 0004121290 scopus 로고
    • Barley
    • Chapman and Hall, London.
    • Briggs, D.E. 1978. Barley. Chapman and Hall, London.
    • (1978)
    • Briggs, D.E.1
  • 22
    • 0004259551 scopus 로고    scopus 로고
    • Malts and Malting
    • 1st ed. Aspen Publishers, London, UK.
    • Briggs, D.E. 2002. Malts and Malting, 1st ed. Aspen Publishers, London, UK.
    • (2002)
    • Briggs, D.E.1
  • 23
    • 0028105507 scopus 로고
    • Endosperm development in barley-microtubule involvement in the morphogenetic pathway
    • Brown, R.C., B.E. Lemmon, and O.A. Olsen. 1994. Endosperm development in barley-microtubule involvement in the morphogenetic pathway. Plant Cell 6:1241-1252.
    • (1994) Plant Cell , vol.6 , pp. 1241-1252
    • Brown, R.C.1    Lemmon, B.E.2    Olsen, O.A.3
  • 24
    • 0035787039 scopus 로고    scopus 로고
    • The diffusive transport of gibberellins and abscisic acid through the aleurone layer of germinating barley grain:a mathematical model
    • Bruggeman, F.J., K.R. Libbenga, and B. Van Duijn. 2001. The diffusive transport of gibberellins and abscisic acid through the aleurone layer of germinating barley grain:a mathematical model. Planta 214:89-96.
    • (2001) Planta , vol.214 , pp. 89-96
    • Bruggeman, F.J.1    Libbenga, K.R.2    Van Duijn, B.3
  • 25
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley
    • Burton, R.A., X.Q. Zhang, M. Hrmova, and G.B. Fincher. 1999. A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol. 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
  • 26
    • 0036852074 scopus 로고    scopus 로고
    • Characterization of the genes encoding the cytosolic and plastidial forms of ADP-glucose pyrophosphorylase in wheat endosperm
    • Burton, R.A., P.E. Johnson, D.M. Beckles, G.B. Fincher, H.L. Jenner, M.J. Naldrett, and K. Denyer. 2002. Characterization of the genes encoding the cytosolic and plastidial forms of ADP-glucose pyrophosphorylase in wheat endosperm. Plant Physiol. 130:1464-1475.
    • (2002) Plant Physiol , vol.130 , pp. 1464-1475
    • Burton, R.A.1    Johnson, P.E.2    Beckles, D.M.3    Fincher, G.B.4    Jenner, H.L.5    Naldrett, M.J.6    Denyer, K.7
  • 28
    • 48549094244 scopus 로고    scopus 로고
    • The genetics and transcriptional profiles of the cellulose synthase-l ike HvCslF gene family in barley
    • Burton, R.A., S.A. Jobling, A.J. Harvey, N.J. Shirley, D.E. Mather, A. Bacic, and G.B. Fincher. 2008. The genetics and transcriptional profiles of the cellulose synthase-l ike HvCslF gene family in barley. Plant Physiol. 146:1821-1833.
    • (2008) Plant Physiol , vol.146 , pp. 1821-1833
    • Burton, R.A.1    Jobling, S.A.2    Harvey, A.J.3    Shirley, N.J.4    Mather, D.E.5    Bacic, A.6    Fincher, G.B.7
  • 29
    • 0034967035 scopus 로고    scopus 로고
    • Synthesis, processing and export of cytoplasmic endo-beta-1,4-xylanase from barley aleurone during germination
    • Caspers, M.P., F. Lok, K.M. Sinjorgo, M.J. van Zeijl, K.A. Nielsen, and V. Cameron-Mills. 2001. Synthesis, processing and export of cytoplasmic endo-beta-1,4-xylanase from barley aleurone during germination. Plant J. 26:191-204.
    • (2001) Plant J , vol.26 , pp. 191-204
    • Caspers, M.P.1    Lok, F.2    Sinjorgo, K.M.3    Van Zeijl, M.J.4    Nielsen, K.A.5    Cameron-Mills, V.6
  • 30
    • 0033428817 scopus 로고    scopus 로고
    • Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
    • Cho, M.J., J.H. Wong, C. Marx, W. Jiang, P.G. Lemaux, and B.B. Buchanan. 1999. Overexpression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain. Proc. Natl. Acad. Sci. U. S. A. 96:14641-14646.
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 14641-14646
    • Cho, M.J.1    Wong, J.H.2    Marx, C.3    Jiang, W.4    Lemaux, P.G.5    Buchanan, B.B.6
  • 31
    • 0000941910 scopus 로고
    • Gibberellic acid-enhanced synthesis and release of alpha-amylase and ribo-nuclease by isolated barley and aleurone layers
    • Chrispeels, M.J. and J.E. Varner. 1967. Gibberellic acid-enhanced synthesis and release of alpha-amylase and ribo-nuclease by isolated barley and aleurone layers. Plant Physiol. 42:398-406.
    • (1967) Plant Physiol , vol.42 , pp. 398-406
    • Chrispeels, M.J.1    Varner, J.E.2
  • 32
    • 2942674460 scopus 로고    scopus 로고
    • Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley alpha-glucosidase
    • Clark, S.E., E.H. Muslin, and C.A. Henson. 2004. Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley alpha-glucosidase. Protein Eng. Des. Sel. 17:245-249.
    • (2004) Protein Eng. Des. Sel , vol.17 , pp. 245-249
    • Clark, S.E.1    Muslin, E.H.2    Henson, C.A.3
  • 33
    • 0000705704 scopus 로고
    • Endosperm cell number in barley
    • Cochrane, M.P. and C.M. Duffus. 1981. Endosperm cell number in barley. Nature 289:399-401.
    • (1981) Nature , vol.289 , pp. 399-401
    • Cochrane, M.P.1    Duffus, C.M.2
  • 34
    • 0041093826 scopus 로고
    • Relationship of mixed link beta-glucan accumulation to accumulation of free sugars and other glucans in the developing barley endosperm
    • Coles, G. 1979. Relationship of mixed link beta-glucan accumulation to accumulation of free sugars and other glucans in the developing barley endosperm. Carlsberg Res. Commun. 44:439-453.
    • (1979) Carlsberg Res. Commun , vol.44 , pp. 439-453
    • Coles, G.1
  • 35
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes:an integrated database approach
    • In H.J. Gilbert, G. Davies, B. Henrissat and B. Svensson (eds)., The Royal Society of Chemistry, Cambridge.
    • Coutinho, P.M. and Henrissat, B. 1999. Carbohydrate-active enzymes:an integrated database approach, pp. 3-12. In H.J. Gilbert, G. Davies, B. Henrissat and B. Svensson (eds). Recent Advances in Carbohydrate Bioengineering. The Royal Society of Chemistry, Cambridge.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 36
    • 0028064951 scopus 로고
    • The expression of serine carboxypepti-dases during maturation and germination of the barley grain
    • Dal Degan, F., A. Rocher, V. Cameron-Mills, and D. von Wettstein. 1994. The expression of serine carboxypepti-dases during maturation and germination of the barley grain. Proc. Natl. Acad. Sci. U. S. A. 91:8209-8213.
    • (1994) Proc. Natl. Acad. Sci. U. S. A , vol.91 , pp. 8209-8213
    • Dal Degan, F.1    Rocher, A.2    Cameron-Mills, V.3    Von Wettstein, D.4
  • 37
    • 0000014240 scopus 로고
    • Gibberellic-acid-induced and release of cell-wall-degrading endoxylanase by isolated aleurone layers of barley
    • Dashek, W.V. and M.J. Chrispeels. 1977. Gibberellic-acid-induced and release of cell-wall-degrading endoxylanase by isolated aleurone layers of barley. Planta 134:251-256.
    • (1977) Planta , vol.134 , pp. 251-256
    • Dashek, W.V.1    Chrispeels, M.J.2
  • 38
    • 0024288439 scopus 로고
    • The A-and B-chains of carboxypeptidase I from germinated barley originate from a single precursor polypeptide
    • Doan, N.P. and G.B. Fincher. 1988. The A-and B-chains of carboxypeptidase I from germinated barley originate from a single precursor polypeptide. J. Biol. Chem. 263:11106-11110.
    • (1988) J. Biol. Chem , vol.263 , pp. 11106-11110
    • Doan, N.P.1    Fincher, G.B.2
  • 39
    • 0141986391 scopus 로고
    • Formation of the barley grain-morphology, physiology, and biochemistry
    • In A.W. MacGregor and R.S. Bhatty (eds.)., American Association of Cereal Chemists, St. Paul, MN.
    • Duffus, C.M. and M.P. Cochrane. 1993. Formation of the barley grain-morphology, physiology, and biochemistry,, pp. 31-72. In A.W. MacGregor and R.S. Bhatty (eds.). Barley:Chemistry and Technology. American Association of Cereal Chemists, St. Paul, MN.
    • (1993) Barley:Chemistry and Technology , pp. 31-72
    • Duffus, C.M.1    Cochrane, M.P.2
  • 40
    • 0000704990 scopus 로고    scopus 로고
    • Thermostability variation in alleles of barley beta-amylase
    • Eglinton, J.K., P. Langridge, and D.E. Evans. 1998. Thermostability variation in alleles of barley beta-amylase. J. Cereal Sci. 28:301-309.
    • (1998) J. Cereal Sci , vol.28 , pp. 301-309
    • Eglinton, J.K.1    Langridge, P.2    Evans, D.E.3
  • 41
    • 0017679490 scopus 로고
    • Peptidases in germinating barley grain:properties, localization and possible functions
    • Enari, T.M. and J. Mikola. 1977. Peptidases in germinating barley grain:properties, localization and possible functions. Ciba Found. Symp. 50:335-352.
    • (1977) Ciba Found. Symp , vol.50 , pp. 335-352
    • Enari, T.M.1    Mikola, J.2
  • 42
    • 33645145479 scopus 로고    scopus 로고
    • Plant cell wall biosynthesis:genetic, biochemical and functional genomics approaches to the identification of key genes
    • Farrokhi, N., R.A. Burton, L. Brownfield, M. Hrmova, S.M. Wilson, A. Bacic, and G.B. Fincher. 2006. Plant cell wall biosynthesis:genetic, biochemical and functional genomics approaches to the identification of key genes. Plant Biotechnol. J. 4:145-167.
    • (2006) Plant Biotechnol. J , vol.4 , pp. 145-167
    • Farrokhi, N.1    Burton, R.A.2    Brownfield, L.3    Hrmova, M.4    Wilson, S.M.5    Bacic, A.6    Fincher, G.B.7
  • 44
    • 0033773875 scopus 로고    scopus 로고
    • A novel type of arabinoxylan arabinofuranohydrolase isolated from germinated barley-analysis of substrate preference and specificity by nano-probe NMR
    • Ferre, H., A. Broberg, J.O. Duus, and K.K. Thomsen. 2000. A novel type of arabinoxylan arabinofuranohydrolase isolated from germinated barley-analysis of substrate preference and specificity by nano-probe NMR. Eur. J. Biochem. 267:6633-6641.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6633-6641
    • Ferre, H.1    Broberg, A.2    Duus, J.O.3    Thomsen, K.K.4
  • 45
    • 84948073034 scopus 로고    scopus 로고
    • A merging of paths:abscisic acid and hormonal cross-talk in the control of seed dormancy maintenance and alleviation
    • In K. Bradford and H. Nonogaki (eds.)., Blackwell Publishing, Oxford.
    • Feurtado, J.A. and A.R. Kermode. 2007. A merging of paths:abscisic acid and hormonal cross-talk in the control of seed dormancy maintenance and alleviation,, pp. 176-223. In K. Bradford and H. Nonogaki (eds.). Seed Development, Dormancy and Germination. Annual Plant Reviews, Vol. 27. Blackwell Publishing, Oxford.
    • (2007) Seed Development, Dormancy and Germination. Annual Plant Reviews , vol.27 , pp. 176-223
    • Feurtado, J.A.1    Kermode, A.R.2
  • 48
    • 84978566967 scopus 로고
    • Morphology and chemical composition of barley endosperm cell walls
    • Fincher, G.B. 1975. Morphology and chemical composition of barley endosperm cell walls. J. Inst. Brew. 81:116-122.
    • (1975) J. Inst. Brew , vol.81 , pp. 116-122
    • Fincher, G.B.1
  • 49
    • 84978600612 scopus 로고
    • Ferulic acid in barley cell walls:a fluorescence study
    • Fincher, G.B. 1976. Ferulic acid in barley cell walls:a fluorescence study. J. Inst. Brew. 82:347-349.
    • (1976) J. Inst. Brew , vol.82 , pp. 347-349
    • Fincher, G.B.1
  • 50
    • 0000860075 scopus 로고
    • Molecular and cellular biology associated with endosperm mobilization in germinating cereal-grains
    • Fincher, G.B. 1989. Molecular and cellular biology associated with endosperm mobilization in germinating cereal-grains. Annu. Rev. Plant Physiol. Plant Mol. Biol. 40:305-346.
    • (1989) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.40 , pp. 305-346
    • Fincher, G.B.1
  • 51
    • 84886550580 scopus 로고    scopus 로고
    • Genomics
    • In C. Wrigley, H. Corke, and C.E. Walker (eds.)., Elsevier Academic Press, Oxford, UK.
    • Fincher, G.B. and P. Langridge. 2004. Genomics,, pp. 16-24. In C. Wrigley, H. Corke, and C.E. Walker (eds.). Encyclopedia of Grain Science, Vol. 2. Elsevier Academic Press, Oxford, UK.
    • (2004) Encyclopedia of Grain Science , vol.2 , pp. 16-24
    • Fincher, G.B.1    Langridge, P.2
  • 52
    • 0022954033 scopus 로고
    • Cell walls and their components in cereal grain technology
    • In Y. Pomeranz (ed.)., American Association of Cereal Chemists, St. Paul, MN.
    • Fincher, G.B. and B.A. Stone. 1986. Cell walls and their components in cereal grain technology, p. 364. In Y. Pomeranz (ed.). Advances in Cereal Science and Technology, Vol. VIII. American Association of Cereal Chemists, St. Paul, MN.
    • (1986) Advances in Cereal Science and Technology , vol.VIII , pp. 364
    • Fincher, G.B.1    Stone, B.A.2
  • 53
    • 33645468717 scopus 로고    scopus 로고
    • Chemistry of nonstarch polysaccharides
    • In C. Wrigley, H. Corke, and C.E. Walker (eds.)., Elsevier, Oxford.
    • Fincher, G.B. and B.A. Stone. 2004. Chemistry of nonstarch polysaccharides,, pp. 206-223. In C. Wrigley, H. Corke, and C.E. Walker (eds.). Encyclopedia of Grain Science. Elsevier, Oxford.
    • (2004) Encyclopedia of Grain Science , pp. 206-223
    • Fincher, G.B.1    Stone, B.A.2
  • 56
    • 32644485468 scopus 로고    scopus 로고
    • Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome
    • Finnie, C., K.S. Bak-Jensen, S. Laugesen, P. Roepstorff, and B. Svensson. 2006. Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome. Plant Sci. 170. 808-821.
    • (2006) Plant Sci , vol.170 , pp. 808-821
    • Finnie, C.1    Bak-Jensen, K.S.2    Laugesen, S.3    Roepstorff, P.4    Svensson, B.5
  • 57
    • 0036939344 scopus 로고    scopus 로고
    • SEP-1-a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgare L
    • Fontanini, D. and B.L. Jones. 2002. SEP-1-a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgare L. cv. Morex. Planta 215:885-893.
    • (2002) cv. Morex. Planta , vol.215 , pp. 885-893
    • Fontanini, D.1    Jones, B.L.2
  • 58
    • 0034126439 scopus 로고    scopus 로고
    • Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point alpha-glucosidase from barley malt
    • Frandsen, T.P., F. Lok, E. Mirgorodskaya, P. Roepstorff, and B. Svensson. 2000. Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point alpha-glucosidase from barley malt. Plant Physiol. 123:275-286.
    • (2000) Plant Physiol , vol.123 , pp. 275-286
    • Frandsen, T.P.1    Lok, F.2    Mirgorodskaya, E.3    Roepstorff, P.4    Svensson, B.5
  • 59
    • 84970561092 scopus 로고
    • Localization of arginine-rich protein in mature seeds of some members of Gramineae
    • Fulcher, R., T. O'Brien, and D. Simmonds. 1972. Localization of arginine-rich protein in mature seeds of some members of Gramineae. Aust. J. Biol. Sci. 25:487.
    • (1972) Aust. J. Biol. Sci , vol.25 , pp. 487
    • Fulcher, R.1    O'Brien, T.2    Simmonds, D.3
  • 60
    • 0041473769 scopus 로고    scopus 로고
    • Molecular dissection of a dormancy QTL region near the chromosome 7 (5H) L telomere in barley
    • Gao, W., J.A. Clancy, F. Han, D. Prada, A. Kleinhofs, and S.E. Ullrich. 2003. Molecular dissection of a dormancy QTL region near the chromosome 7 (5H) L telomere in barley. Theor. Appl. Genet. 107:552-529.
    • (2003) Theor. Appl. Genet , vol.107 , pp. 552-529
    • Gao, W.1    Clancy, J.A.2    Han, F.3    Prada, D.4    Kleinhofs, A.5    Ullrich, S.E.6
  • 61
    • 4544285801 scopus 로고    scopus 로고
    • Fine mapping of a malting-quality QTL complex near the chromosome 4H S telomere in barley
    • North American Barley Genome Project
    • Gao, W., J.A. Clancy, F. Han, B.L. Jones, A. Budde, D.M. Wesenberg, A. Kleinhofs, S.E. Ullrich, and North American Barley Genome Project. 2004. Fine mapping of a malting-quality QTL complex near the chromosome 4H S telomere in barley. Theor. Appl. Genet. 109:750-760.
    • (2004) Theor. Appl. Genet , vol.109 , pp. 750-760
    • Gao, W.1    Clancy, J.A.2    Han, F.3    Jones, B.L.4    Budde, A.5    Wesenberg, D.M.6    Kleinhofs, A.7    Ullrich, S.E.8
  • 62
    • 0012586535 scopus 로고
    • On the relative role of the scutellum and aleurone in the production of hydrolases during germination of barley
    • Gibbons, G.C. 1981. On the relative role of the scutellum and aleurone in the production of hydrolases during germination of barley. Carlsberg Res. Commun. 46:215-225.
    • (1981) Carlsberg Res. Commun , vol.46 , pp. 215-225
    • Gibbons, G.C.1
  • 63
    • 22444436615 scopus 로고    scopus 로고
    • Changes in cell wall polysaccharides in developing barley (Hordeum vulgare) coleoptiles
    • Gibeaut, D.M., M. Pauly, A. Bacic, and G.B. Fincher. 2005. Changes in cell wall polysaccharides in developing barley (Hordeum vulgare) coleoptiles. Planta 221:729-738.
    • (2005) Planta , vol.221 , pp. 729-738
    • Gibeaut, D.M.1    Pauly, M.2    Bacic, A.3    Fincher, G.B.4
  • 65
    • 0035062614 scopus 로고    scopus 로고
    • Gibberellin/abscisic acid antagonism in barley aleurone cells:site of action of the protein kinase PKABA1 in relation to gibberellin signaling molecules
    • Gómez-Cadenas, A., R. Zentella, M.K. Walker-Simmons, and T.H. Ho. 2001. Gibberellin/abscisic acid antagonism in barley aleurone cells:site of action of the protein kinase PKABA1 in relation to gibberellin signaling molecules. Plant Cell 13:667-679.
    • (2001) Plant Cell , vol.13 , pp. 667-679
    • Gómez-Cadenas, A.1    Zentella, R.2    Walker-Simmons, M.K.3    Ho, T.H.4
  • 66
    • 0029410792 scopus 로고
    • Gibberellin-regulated expression of an myb gene in barley aleurone cells:evidence for Myb transactivation of a high-pI alpha-amylase gene promoter
    • Gubler, F., R. Kalla, J.K. Roberts, and J.V. Jacobsen. 1995. Gibberellin-regulated expression of an myb gene in barley aleurone cells:evidence for Myb transactivation of a high-pI alpha-amylase gene promoter. Plant Cell 7:1879-1891.
    • (1995) Plant Cell , vol.7 , pp. 1879-1891
    • Gubler, F.1    Kalla, R.2    Roberts, J.K.3    Jacobsen, J.V.4
  • 67
    • 0033041146 scopus 로고    scopus 로고
    • Target genes and regulatory domains of the GAMYB transcriptional activator in cereal aleurone
    • Gubler, F., D. Raventos, M. Keys, R. Watts, J. Mundy, and J.V. Jacobsen. 1999. Target genes and regulatory domains of the GAMYB transcriptional activator in cereal aleurone. Plant J. 17:1-9.
    • (1999) Plant J , vol.17 , pp. 1-9
    • Gubler, F.1    Raventos, D.2    Keys, M.3    Watts, R.4    Mundy, J.5    Jacobsen, J.V.6
  • 69
    • 48549086776 scopus 로고    scopus 로고
    • Regulation of dormancy in barley by blue light and after-ripening:effects on abscisic acid and gibberellin metabolism
    • Gubler, F., T. Hughes, P. Waterhouse, and J. Jacobsen. 2008. Regulation of dormancy in barley by blue light and after-ripening:effects on abscisic acid and gibberellin metabolism. Plant Physiol. 147:886-896.
    • (2008) Plant Physiol , vol.147 , pp. 886-896
    • Gubler, F.1    Hughes, T.2    Waterhouse, P.3    Jacobsen, J.4
  • 70
    • 0001876687 scopus 로고
    • Release and activation of barley ß-amylase by malt endopeptidases
    • Guerin, J.R., R.C.M. Lance, and W. Wallace. 1992. Release and activation of barley ß-amylase by malt endopeptidases. J. Cereal Sci. 15:5-14.
    • (1992) J. Cereal Sci , vol.15 , pp. 5-14
    • Guerin, J.R.1    Lance, R.C.M.2    Wallace, W.3
  • 71
    • 53749096015 scopus 로고    scopus 로고
    • An abscisic acid-induced protein, HVA22, inhibits gibberellin-mediated programmed cell death in cereal aleurone cells
    • Guo, W.J. and T.H. David Ho. 2008. An abscisic acid-induced protein, HVA22, inhibits gibberellin-mediated programmed cell death in cereal aleurone cells. Plant Physiol. 147:1710-1722.
    • (2008) Plant Physiol , vol.147 , pp. 1710-1722
    • Guo, W.J.1    David Ho, T.H.2
  • 72
    • 0001992521 scopus 로고
    • Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers
    • Hammerton, R.W. and T.H. Ho. 1986. Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers. Plant Physiol. 80:692-697.
    • (1986) Plant Physiol , vol.80 , pp. 692-697
    • Hammerton, R.W.1    Ho, T.H.2
  • 74
    • 0008153317 scopus 로고
    • Amino acid and peptide transport in higher plants
    • Hardy, D.J. and J.W. Payne. 1992. Amino acid and peptide transport in higher plants. Plant Physiol. 11:59-73.
    • (1992) Plant Physiol , vol.11 , pp. 59-73
    • Hardy, D.J.1    Payne, J.W.2
  • 76
    • 84978558616 scopus 로고
    • "Free" and "bound"-amylases during malting of barley:characterization by two-dimensional immunoelectrophoresis
    • Hejgaard, J. 1978. "Free" and "bound"-amylases during malting of barley:characterization by two-dimensional immunoelectrophoresis. J. Inst. Brew. 84:43-46.
    • (1978) J. Inst. Brew , vol.84 , pp. 43-46
    • Hejgaard, J.1
  • 77
    • 0032059448 scopus 로고    scopus 로고
    • Glycosidase families
    • Henrissat, B. 1998. Glycosidase families. Biochem. Soc. Trans. 26:153-156.
    • (1998) Biochem. Soc. Trans , vol.26 , pp. 153-156
    • Henrissat, B.1
  • 78
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and A. Bairoch. 1996. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316:695-696.
    • (1996) Biochem. J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 79
    • 34648835377 scopus 로고    scopus 로고
    • Detection of seed dormancy QTL in multiple mapping populations derived from crosses involving novel barley germplasm
    • Hori, K., K. Sato, and K. Takeda. 2007. Detection of seed dormancy QTL in multiple mapping populations derived from crosses involving novel barley germplasm. Theor. Appl. Genet. 115:869-876.
    • (2007) Theor. Appl. Genet , vol.115 , pp. 869-876
    • Hori, K.1    Sato, K.2    Takeda, K.3
  • 81
    • 84877970837 scopus 로고    scopus 로고
    • Enzymic hydrolysis of cereal (1→3,1→4)-ß-glucans
    • In J.R. Whitaker, A.G.J. Voragen, and D.W.S. Wong (eds.)., CRC Press, Boca Raton, FL.
    • Hrmova, M. and G.B. Fincher. 2002. Enzymic hydrolysis of cereal (1→3,1→4)-ß-glucans, pp. 943-960. In J.R. Whitaker, A.G.J. Voragen, and D.W.S. Wong (eds.). Handbook of Food Enzymology. CRC Press, Boca Raton, FL.
    • (2002) Handbook of Food Enzymology , pp. 943-960
    • Hrmova, M.1    Fincher, G.B.2
  • 82
    • 0029670041 scopus 로고    scopus 로고
    • Barley beta-D-glucan exohydrolases with beta-D-glucosidase activity-purification, characterization, and determination of primary structure from a cDNA clone
    • Hrmova, M., A.J. Harvey, J. Wang, N.J. Shirley, G.P. Jones, B.A. Stone, P.B. Hoj, and G.B. Fincher. 1996. Barley beta-D-glucan exohydrolases with beta-D-glucosidase activity-purification, characterization, and determination of primary structure from a cDNA clone. J. Biol. Chem. 271:5277-5286.
    • (1996) J. Biol. Chem , vol.271 , pp. 5277-5286
    • Hrmova, M.1    Harvey, A.J.2    Wang, J.3    Shirley, N.J.4    Jones, G.P.5    Stone, B.A.6    Hoj, P.B.7    Fincher, G.B.8
  • 83
    • 0032079561 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism of a barley ß-D-glucosidase/(1→4)-ß-D-glucan exohydrolase
    • Hrmova, M., E.A. MacGregor, P. Biely, R.J. Stewart, and G.B. Fincher. 1998. Substrate binding and catalytic mechanism of a barley ß-D-glucosidase/(1→4)-ß-D-glucan exohydrolase. J. Biol. Chem. 273:11134-11143.
    • (1998) J. Biol. Chem , vol.273 , pp. 11134-11143
    • Hrmova, M.1    MacGregor, E.A.2    Biely, P.3    Stewart, R.J.4    Fincher, G.B.5
  • 86
    • 0036218979 scopus 로고    scopus 로고
    • Genetic control of quantitative grain and malt quality traits in barley
    • Igartua, E., P.M. Hayes, W.T.B. Thomas, R. Meyer, and D.E. Mather. 2002. Genetic control of quantitative grain and malt quality traits in barley. J. Crop Prod. 5:131-164.
    • (2002) J. Crop Prod , vol.5 , pp. 131-164
    • Igartua, E.1    Hayes, P.M.2    Thomas, W.T.B.3    Meyer, R.4    Mather, D.E.5
  • 87
    • 0037263489 scopus 로고    scopus 로고
    • SAD:a new DOF protein from barley that activates transcription of a cathepsin B-like thiol protease gene in the aleurone of germinating seeds
    • Isabel-LaMoneda, I., I. Diaz, M. Martinez, M. Mena, and P. Carbonero. 2003. SAD:a new DOF protein from barley that activates transcription of a cathepsin B-like thiol protease gene in the aleurone of germinating seeds. Plant J. 33:329-340.
    • (2003) Plant J , vol.33 , pp. 329-340
    • Isabel-LaMoneda, I.1    Diaz, I.2    Martinez, M.3    Mena, M.4    Carbonero, P.5
  • 88
    • 0000818395 scopus 로고
    • Characterization of the alpha-amylases synthesized by aleurone layers of Himalaya barley in response to gibberellic acid
    • Jacobsen, J.V. and T.J. Higgins. 1982. Characterization of the alpha-amylases synthesized by aleurone layers of Himalaya barley in response to gibberellic acid. Plant Physiol. 70:1647-1653.
    • (1982) Plant Physiol , vol.70 , pp. 1647-1653
    • Jacobsen, J.V.1    Higgins, T.J.2
  • 89
    • 0036067325 scopus 로고    scopus 로고
    • Abscisic acid, phaseic acid and gibberellin contents associated with dormancy and germination in barley
    • Jacobsen, J.V., D.W. Pearce, A.T. Poole, R.P. Pharis, and L.N. Mander. 2002. Abscisic acid, phaseic acid and gibberellin contents associated with dormancy and germination in barley. Physiol. Plant. 115:428-441.
    • (2002) Physiol. Plant , vol.115 , pp. 428-441
    • Jacobsen, J.V.1    Pearce, D.W.2    Poole, A.T.3    Pharis, R.P.4    Mander, L.N.5
  • 90
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins:structure and function in plant cells
    • Jacquot, J.P., J.M. Lancelin, and Y. Meyer. 1997. Thioredoxins:structure and function in plant cells. New Phytol. 136:543-570.
    • (1997) New Phytol , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 91
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugary1, a determinant of starch composition in kernels
    • James, M.G., D.S. Robertson, and A.M. Myers. 1995. Characterization of the maize gene sugary1, a determinant of starch composition in kernels. Plant Cell 7:417-429.
    • (1995) Plant Cell , vol.7 , pp. 417-429
    • James, M.G.1    Robertson, D.S.2    Myers, A.M.3
  • 92
    • 0025784036 scopus 로고
    • Regulation of synthesis and transport of secreted proteins in cereal aleurone
    • Jones, R.L. and J.V. Jacobsen. 1991. Regulation of synthesis and transport of secreted proteins in cereal aleurone. Int. Rev. Cytol. 126:49-88.
    • (1991) Int. Rev. Cytol , vol.126 , pp. 49-88
    • Jones, R.L.1    Jacobsen, J.V.2
  • 93
    • 1042289392 scopus 로고    scopus 로고
    • XIP-I, a xyla-nase inhibitor protein from wheat:a novel protein function
    • Juge, N., F. Payan, and G. Williamson. 2004. XIP-I, a xyla-nase inhibitor protein from wheat:a novel protein function. Biochim. Biophys. Acta 1696:203-211.
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 203-211
    • Juge, N.1    Payan, F.2    Williamson, G.3
  • 94
    • 0034124523 scopus 로고    scopus 로고
    • Cell wall and membrane-associated exo-ß-D-glucanases from developing maize seedlings
    • Kim, J.B., A.T. Olek, and N.C. Carpita. 2000. Cell wall and membrane-associated exo-ß-D-glucanases from developing maize seedlings. Plant Physiol. 123:471-485.
    • (2000) Plant Physiol , vol.123 , pp. 471-485
    • Kim, J.B.1    Olek, A.T.2    Carpita, N.C.3
  • 95
    • 57749111178 scopus 로고    scopus 로고
    • Inheritance of (1→3) (1→4)-beta-D-glucan content in barley (Hordeum vulgare L.)
    • Proc. 9th Int. Barley Genet. Symp., Brno, Czech Republic, June 20-26, 2004
    • Kim, H.S., K.G. Park, S.B. Baek, Y.G. Son, C.W. Lee, J.C. Kim, J.G. Kim, and J.H. Nam. 2004. Inheritance of (1→3) (1→4)-beta-D-glucan content in barley (Hordeum vulgare L.), pp. 543-548. Proc. 9th Int. Barley Genet. Symp., Brno, Czech Republic, June 20-26, 2004
    • (2004) , pp. 543-548
    • Kim, H.S.1    Park, K.G.2    Baek, S.B.3    Son, Y.G.4    Lee, C.W.5    Kim, J.C.6    Kim, J.G.7    Nam, J.H.8
  • 96
    • 0025944354 scopus 로고
    • Role of the NADP/thioredoxin system in the reduction of alphaamylase and trypsin inhibitor proteins
    • Kobrehel, K., B.C. Yee, and B.B. Buchanan. 1991. Role of the NADP/thioredoxin system in the reduction of alphaamylase and trypsin inhibitor proteins. J. Biol. Chem. 266:16135-16140.
    • (1991) J. Biol. Chem , vol.266 , pp. 16135-16140
    • Kobrehel, K.1    Yee, B.C.2    Buchanan, B.B.3
  • 98
    • 0002898965 scopus 로고
    • Purification and characterization of gibberellic acid-induced cysteine endo-proteases in barley aleurone layers
    • Koehler, S.M. and T.H.D. Ho. 1988. Purification and characterization of gibberellic acid-induced cysteine endo-proteases in barley aleurone layers. Plant Physiol. 87:95-103.
    • (1988) Plant Physiol , vol.87 , pp. 95-103
    • Koehler, S.M.1    Ho, T.H.D.2
  • 99
    • 0025465440 scopus 로고
    • Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers
    • a
    • Koehler, S.M. and T.H.D. Ho. 1990a. Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers. Plant Cell 2:769-783.
    • (1990) Plant Cell , vol.2 , pp. 769-783
    • Koehler, S.M.1    Ho, T.H.D.2
  • 100
    • 0000023298 scopus 로고
    • A major gibberellic acid-induced barley cysteine proteinase which digests hordein
    • b
    • Koehler, S.M. and T.H.D. Ho. 1990b. A major gibberellic acid-induced barley cysteine proteinase which digests hordein. Plant Physiol. 94:251-258.
    • (1990) Plant Physiol , vol.94 , pp. 251-258
    • Koehler, S.M.1    Ho, T.H.D.2
  • 101
    • 0031080526 scopus 로고    scopus 로고
    • Purification and characterization of wall-bound exo-1,3-β-D-glucanase from barley (Hordeum vulgare L.) seedlings
    • Kotake, T., N. Nakagawa, K. Takeda, and N. Sakurai. 1997. Purification and characterization of wall-bound exo-1,3-β-D-glucanase from barley (Hordeum vulgare L.) seedlings. Plant Cell Physiol. 38:194-200.
    • (1997) Plant Cell Physiol , vol.38 , pp. 194-200
    • Kotake, T.1    Nakagawa, N.2    Takeda, K.3    Sakurai, N.4
  • 102
    • 0023657286 scopus 로고
    • Primary structure and differential expression of α-amylase in normal and mutant barleys
    • Kreis, M., M. Williamson, B. Buxton, J. Pywell, J. Hejgaard, and I. Svendsen. 1987. Primary structure and differential expression of α-amylase in normal and mutant barleys. Eur. J. Biochem. 169:517-525.
    • (1987) Eur. J. Biochem , vol.169 , pp. 517-525
    • Kreis, M.1    Williamson, M.2    Buxton, B.3    Pywell, J.4    Hejgaard, J.5    Svendsen, I.6
  • 103
    • 0031873219 scopus 로고    scopus 로고
    • Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family
    • Kristensen, M., V. Planchot, J.-I. Abe, and B. Svensson. 1998. Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family. Cereal Chem. 75:473-479.
    • (1998) Cereal Chem , vol.75 , pp. 473-479
    • Kristensen, M.1    Planchot, V.2    Abe, J.-I.3    Svensson, B.4
  • 104
    • 50049112388 scopus 로고    scopus 로고
    • Time course for the development of enzymes in barley
    • Kuntz, R.J. and C.W. Bamforth. 2007. Time course for the development of enzymes in barley. J. Inst. Brew. 113:196-205.
    • (2007) J. Inst. Brew , vol.113 , pp. 196-205
    • Kuntz, R.J.1    Bamforth, C.W.2
  • 105
    • 0030087964 scopus 로고    scopus 로고
    • Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells
    • Kuo, A.L., S. Cappelluti, M. CervantesCervantes, M. Rodriguez, and D.S. Bush. 1996. Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells. Plant Cell 8:259-269.
    • (1996) Plant Cell , vol.8 , pp. 259-269
    • Kuo, A.L.1    Cappelluti, S.2    CervantesCervantes, M.3    Rodriguez, M.4    Bush, D.S.5
  • 106
    • 0015051534 scopus 로고
    • The substrate specificity of amylopectin-debranching enzymes from sweet corn
    • Lee, E.Y., J.J. Marshall, and W.J. Whelan. 1971. The substrate specificity of amylopectin-debranching enzymes from sweet corn. Arch. Biochem. Biophys. 143:365-374.
    • (1971) Arch. Biochem. Biophys , vol.143 , pp. 365-374
    • Lee, E.Y.1    Marshall, J.J.2    Whelan, W.J.3
  • 107
    • 0035874475 scopus 로고    scopus 로고
    • Barley arabinoxylan arabinofuranohydrolases:purification, characterization and determination of primary structures from cDNA clones
    • Lee, R.C., R.A. Burton, M. Hrmova, and G.B. Fincher. 2001. Barley arabinoxylan arabinofuranohydrolases:purification, characterization and determination of primary structures from cDNA clones. Biochem. J. 356:181-189.
    • (2001) Biochem. J , vol.356 , pp. 181-189
    • Lee, R.C.1    Burton, R.A.2    Hrmova, M.3    Fincher, G.B.4
  • 110
    • 0025670511 scopus 로고
    • The isolation and characterization of a barley 1,3-1,4-beta-glucanase gene
    • Litts, J.C., C.R. Simmons, E.E. Karrer, N. Huang, and R.L. Rodriguez. 1990. The isolation and characterization of a barley 1,3-1,4-beta-glucanase gene. Eur. J. Biochem. 194:831-838.
    • (1990) Eur. J. Biochem , vol.194 , pp. 831-838
    • Litts, J.C.1    Simmons, C.R.2    Karrer, E.E.3    Huang, N.4    Rodriguez, R.L.5
  • 111
    • 0034162708 scopus 로고    scopus 로고
    • Gibberellin and abscisic acid signalling in aleurone
    • Lovegrove, A. and R. Hooley. 2000. Gibberellin and abscisic acid signalling in aleurone. Trends Plant Sci. 5:102-110.
    • (2000) Trends Plant Sci , vol.5 , pp. 102-110
    • Lovegrove, A.1    Hooley, R.2
  • 112
    • 0001391690 scopus 로고
    • The four major forms of barley α-amylase:purification, characterization and structural relationship
    • Lundgard, R. and B. Svensson. 1987. The four major forms of barley α-amylase:purification, characterization and structural relationship. Carlsberg Res. Commun. 52:313-326.
    • (1987) Carlsberg Res. Commun , vol.52 , pp. 313-326
    • Lundgard, R.1    Svensson, B.2
  • 113
    • 0034619496 scopus 로고    scopus 로고
    • Removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity of barley beta-amylase
    • Ma, Y.F., J.K. Eglinton, D.E. Evans, S.J. Logue, and P. Langridge. 2000. Removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity of barley beta-amylase. Biochemistry 39:13350-13355.
    • (2000) Biochemistry , vol.39 , pp. 13350-13355
    • Ma, Y.F.1    Eglinton, J.K.2    Evans, D.E.3    Logue, S.J.4    Langridge, P.5
  • 114
    • 1042266306 scopus 로고    scopus 로고
    • The proteinaceous inhibitor of limit dextrinase in barley and malt
    • MacGregor, E.A. 2004. The proteinaceous inhibitor of limit dextrinase in barley and malt. Biochim. Biophys. Acta 1696:165-170.
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 165-170
    • MacGregor, E.A.1
  • 115
    • 0002895097 scopus 로고
    • Carbohydrates of the barley grain
    • In A.W. MacGregor and R.S. Bhatty (eds.)., American Association of Cereal Chemists, St. Paul, MN.
    • MacGregor, A.W. and G.B. Fincher. 1993. Carbohydrates of the barley grain,, pp. 73-130. In A.W. MacGregor and R.S. Bhatty (eds.). Barley:Chemistry and Technology. American Association of Cereal Chemists, St. Paul, MN.
    • (1993) Barley:Chemistry and Technology , pp. 73-130
    • MacGregor, A.W.1    Fincher, G.B.2
  • 116
    • 0010232927 scopus 로고
    • Changes in levels of alpha-amylase components in barley tissues during germination and early seedling growth
    • MacGregor, A.W., F.H. MacDougall, C. Mayer, and J. Daussant. 1984. Changes in levels of alpha-amylase components in barley tissues during germination and early seedling growth. Plant Physiol. 75:203-206.
    • (1984) Plant Physiol , vol.75 , pp. 203-206
    • MacGregor, A.W.1    MacDougall, F.H.2    Mayer, C.3    Daussant, J.4
  • 117
    • 27744528809 scopus 로고    scopus 로고
    • A QTL located on chromosome 4A associated with dormancy in white-and red-grained wheats of diverse origin
    • Mares, D., K. Mrva, J. Cheong, K. Williams, B. Watson, E. Storlie, M. Sutherland, and Y. Zou. 2005. A QTL located on chromosome 4A associated with dormancy in white-and red-grained wheats of diverse origin. Theor. Appl. Genet. 111:1357-1364.
    • (2005) Theor. Appl. Genet , vol.111 , pp. 1357-1364
    • Mares, D.1    Mrva, K.2    Cheong, J.3    Williams, K.4    Watson, B.5    Storlie, E.6    Sutherland, M.7    Zou, Y.8
  • 118
    • 0033928015 scopus 로고    scopus 로고
    • QTL analysis of malting quality in barley based on the doubled haploid progeny of two elite North American varieties representing different germplasm groups
    • the NABGP.
    • Marquez-Cedillo, L.A., P.M. Hayes, B.L. Jones, A. Kleinhofs, W.G. Legge, B.G. Rossnagel, K. Sato, S.E. Ullrich, D.M. Wesenberg, and the NABGP. 2000. QTL analysis of malting quality in barley based on the doubled haploid progeny of two elite North American varieties representing different germplasm groups. Theor. Appl. Genet. 101:173-184.
    • (2000) Theor. Appl. Genet , vol.101 , pp. 173-184
    • Marquez-Cedillo, L.A.1    Hayes, P.M.2    Jones, B.L.3    Kleinhofs, A.4    Legge, W.G.5    Rossnagel, B.G.6    Sato, K.7    Ullrich, S.E.8    Wesenberg, D.M.9
  • 119
    • 0029328417 scopus 로고
    • Starch synthesis
    • Martin, C. and A.M. Smith. 1995. Starch synthesis. Plant Cell 7:971-985.
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 120
    • 0037338198 scopus 로고    scopus 로고
    • A cathepsin B-like cysteine pro tease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves
    • Martínez, M., I. Rubio-Somoza, P. Carbonero, and I. Díaz. 2003. A cathepsin B-like cysteine pro tease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves. J. Exp. Bot. 54:951-959.
    • (2003) J. Exp. Bot , vol.54 , pp. 951-959
    • Martínez, M.1    Rubio-Somoza, I.2    Carbonero, P.3    Díaz, I.4
  • 122
    • 0001475691 scopus 로고
    • Expression sites and developmental regulation of genes encoding (1-3,1-4)-beta-glucanases in germinated barley
    • McFadden, G.I., B. Ahluwalia, A.E. Clarke, and G.B. Fincher. 1988. Expression sites and developmental regulation of genes encoding (1-3,1-4)-beta-glucanases in germinated barley. Planta 173:500-508.
    • (1988) Planta , vol.173 , pp. 500-508
    • McFadden, G.I.1    Ahluwalia, B.2    Clarke, A.E.3    Fincher, G.B.4
  • 123
    • 45649084937 scopus 로고    scopus 로고
    • Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savi-nase reveal a novel mode of inhibition
    • Micheelsen, P.O., J. Vévodová, L. De Maria, P.R. Ostergaard, E.P. Friis, K. Wilson, and M. Skjøt. 2008. Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savi-nase reveal a novel mode of inhibition. J. Mol. Biol. 380:681-690.
    • (2008) J. Mol. Biol , vol.380 , pp. 681-690
    • Micheelsen, P.O.1    Vévodová, J.2    De Maria, L.3    Ostergaard, P.R.4    Friis, E.P.5    Wilson, K.6    Skjøt, M.7
  • 124
    • 0033593468 scopus 로고    scopus 로고
    • The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 Å resolution
    • Mikami, B., H.J. Yoon, and N. Yoshigi. 1999. The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 Å resolution. J. Mol. Biol. 285:1235-1243.
    • (1999) J. Mol. Biol , vol.285 , pp. 1235-1243
    • Mikami, B.1    Yoon, H.J.2    Yoshigi, N.3
  • 125
    • 0030152393 scopus 로고    scopus 로고
    • A major cysteine proteinase, EPB, in germinating barley seeds:structure of two intronless genes and regulation of expression
    • Mikkonen, A., I. Porali, M. Cercós, and T.H.D. Ho. 1996. A major cysteine proteinase, EPB, in germinating barley seeds:structure of two intronless genes and regulation of expression. Plant Mol. Biol. 31:239-254.
    • (1996) Plant Mol. Biol , vol.31 , pp. 239-254
    • Mikkonen, A.1    Porali, I.2    Cercós, M.3    Ho, T.H.D.4
  • 127
    • 33847242987 scopus 로고    scopus 로고
    • QTL analysis of a cross between European and North American malting barleys reveals a putative candidate gene for beta-glucan content on chromosome 1H
    • Molina-Cano, J.L., M. Moralejo, M. Elia, P. Munoz, J.R. Russell, A.M. Perez-Vendrell, F. Ciudad, and J.S. Swanston. 2007. QTL analysis of a cross between European and North American malting barleys reveals a putative candidate gene for beta-glucan content on chromosome 1H. Mol. Breed. 19:275-284.
    • (2007) Mol. Breed , vol.19 , pp. 275-284
    • Molina-Cano, J.L.1    Moralejo, M.2    Elia, M.3    Munoz, P.4    Russell, J.R.5    Perez-Vendrell, A.M.6    Ciudad, F.7    Swanston, J.S.8
  • 128
    • 34547109079 scopus 로고    scopus 로고
    • The HvDOF19 transcription factor mediates the abscisic acid-dependent repression of hydrolase genes in germinating barley aleurone
    • Moreno-Risueno, M.A., I. Díaz, L. Carrillo, R. Fuentes, and P. Carbonero. 2007. The HvDOF19 transcription factor mediates the abscisic acid-dependent repression of hydrolase genes in germinating barley aleurone. Plant J. 51:352-365.
    • (2007) Plant J , vol.51 , pp. 352-365
    • Moreno-Risueno, M.A.1    Díaz, I.2    Carrillo, L.3    Fuentes, R.4    Carbonero, P.5
  • 129
    • 0000818906 scopus 로고
    • Changes in cell-wall polysaccharides of germinating grains
    • Morrall, P. and D.E. Briggs. 1978. Changes in cell-wall polysaccharides of germinating grains. Phytochemistry 17:1495-1502.
    • (1978) Phytochemistry , vol.17 , pp. 1495-1502
    • Morrall, P.1    Briggs, D.E.2
  • 130
    • 0002294076 scopus 로고
    • Barley α-amylase/subtilisin inhibitor. I. Isolation and characterization
    • Mundy, J., I. Svendsen, and J. Hejgaard. 1983. Barley α-amylase/subtilisin inhibitor. I. Isolation and characterization. Carlsberg Res. Commun. 48:81-91.
    • (1983) Carlsberg Res. Commun , vol.48 , pp. 81-91
    • Mundy, J.1    Svendsen, I.2    Hejgaard, J.3
  • 131
    • 0010525757 scopus 로고
    • Messenger RNAs from the scutellum and aleurone of germinating barley encode (1→3,1→4)-ß-D-glucanase, α-amylase and carboxypeptidase
    • Mundy, J., A. Brandt, and G.B. Fincher. 1985. Messenger RNAs from the scutellum and aleurone of germinating barley encode (1→3,1→4)-ß-D-glucanase, α-amylase and carboxypeptidase. Plant Physiol. 79:867-871.
    • (1985) Plant Physiol , vol.79 , pp. 867-871
    • Mundy, J.1    Brandt, A.2    Fincher, G.B.3
  • 132
    • 0036184149 scopus 로고    scopus 로고
    • The effect of proline insertions on the thermostability of a barley alpha-glucosidase
    • Muslin, E.H., S.E. Clark, and C.A. Henson. 2002. The effect of proline insertions on the thermostability of a barley alpha-glucosidase. Protein Eng. 15:29-33.
    • (2002) Protein Eng , vol.15 , pp. 29-33
    • Muslin, E.H.1    Clark, S.E.2    Henson, C.A.3
  • 133
    • 32644463519 scopus 로고    scopus 로고
    • Production of enzymatically active recombinant full-length barley high pI alpha-glucosidase of glycoside family 31 by high cell-density fermentation of Pichia pastoris and affinity purification
    • Naested, H., B. Kramhøft, F. Lok, K. Bojsen, S. Yu, and B. Svensson. 2006. Production of enzymatically active recombinant full-length barley high pI alpha-glucosidase of glycoside family 31 by high cell-density fermentation of Pichia pastoris and affinity purification. Protein Expr. Purif. 46:56-63.
    • (2006) Protein Expr. Purif , vol.46 , pp. 56-63
    • Naested, H.1    Kramhøft, B.2    Lok, F.3    Bojsen, K.4    Yu, S.5    Svensson, B.6
  • 134
    • 0029681154 scopus 로고    scopus 로고
    • Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm:purification, cDNA and chromosomal localization of the gene
    • Nakamura, Y., T. Umemoto, N. Ogata, Y. Kuboki, M. Yano, and T. Sasaki. 1996. Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm:purification, cDNA and chromosomal localization of the gene. Planta 199:209-218.
    • (1996) Planta , vol.199 , pp. 209-218
    • Nakamura, Y.1    Umemoto, T.2    Ogata, N.3    Kuboki, Y.4    Yano, M.5    Sasaki, T.6
  • 135
    • 1042289398 scopus 로고    scopus 로고
    • Barley alpha-amylase/subtilisin inhibitor:structure, biophysics and protein engineering
    • Nielsen, P.K., B.C. Bønsager, K. Fukuda, and B. Svensson. 2004. Barley alpha-amylase/subtilisin inhibitor:structure, biophysics and protein engineering. Biochim. Biophys. Acta 1696:157-164.
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 157-164
    • Nielsen, P.K.1    Bønsager, B.C.2    Fukuda, K.3    Svensson, B.4
  • 136
    • 0242321032 scopus 로고    scopus 로고
    • Metabolism of hydrogen peroxide during reserve mobilization and programmed cell death of barley (Hordeum vulgare L.) aleurone layer cells
    • Palma, K. and A.R. Kermode. 2003. Metabolism of hydrogen peroxide during reserve mobilization and programmed cell death of barley (Hordeum vulgare L.) aleurone layer cells. Free Radic. Biol. Med. 35:1261-1270.
    • (2003) Free Radic. Biol. Med , vol.35 , pp. 1261-1270
    • Palma, K.1    Kermode, A.R.2
  • 138
    • 4444351968 scopus 로고    scopus 로고
    • Functional association between malting quality trait components and cDNA array based expression patterns in barley (Hordeum vulgare L.)
    • Potokina, E., M. Caspers, M. Prasad, R. Kota, H. Zhang, N. Sreenivasulu, M. Wang, and A. Graner. 2004. Functional association between malting quality trait components and cDNA array based expression patterns in barley (Hordeum vulgare L.). Mol. Breed. 14:153-170.
    • (2004) Mol. Breed , vol.14 , pp. 153-170
    • Potokina, E.1    Caspers, M.2    Prasad, M.3    Kota, R.4    Zhang, H.5    Sreenivasulu, N.6    Wang, M.7    Graner, A.8
  • 139
    • 29544448480 scopus 로고    scopus 로고
    • Expression genetics and haplotype analysis reveal cis regulation of serine carboxypeptidase I (Cxp1), a candidate gene for malting quality in barley (Hordeum vulgare L.)
    • Potokina, E., M. Prasad, L. Malysheva, M.S. Röder, and A. Graner. 2006. Expression genetics and haplotype analysis reveal cis regulation of serine carboxypeptidase I (Cxp1), a candidate gene for malting quality in barley (Hordeum vulgare L.). Funct. Integr. Genomics 6:25-35.
    • (2006) Funct. Integr. Genomics , vol.6 , pp. 25-35
    • Potokina, E.1    Prasad, M.2    Malysheva, L.3    Röder, M.S.4    Graner, A.5
  • 140
    • 37249073867 scopus 로고    scopus 로고
    • Gene expression quantitative trait locus analysis of 16 000 barley genes reveals a complex pattern of genome-wide transcriptional regulation
    • Potokina, E., A. Druka, Z. Luo, R. Wise, R. Waugh, and M. Kearsey. 2008. Gene expression quantitative trait locus analysis of 16 000 barley genes reveals a complex pattern of genome-wide transcriptional regulation. Plant J. 53:90-101.
    • (2008) Plant J , vol.53 , pp. 90-101
    • Potokina, E.1    Druka, A.2    Luo, Z.3    Wise, R.4    Waugh, R.5    Kearsey, M.6
  • 142
    • 11444251891 scopus 로고    scopus 로고
    • A centromeric region on chromosome 6(6H) affects dormancy in an induced mutant in barley
    • Prada, D., I. Romagosa, S.E. Ullrich, and J.L. Molina-Cano. 2005. A centromeric region on chromosome 6(6H) affects dormancy in an induced mutant in barley. J. Exp. Bot. 56:47-54.
    • (2005) J. Exp. Bot , vol.56 , pp. 47-54
    • Prada, D.1    Romagosa, I.2    Ullrich, S.E.3    Molina-Cano, J.L.4
  • 143
    • 0032081295 scopus 로고    scopus 로고
    • Characterization of SU1 isoamylase, a determinant of storage starch structure in maize
    • Rahman, A., K. Wong, J. Jane, A.M. Myers, and M.G. James. 1998. Characterization of SU1 isoamylase, a determinant of storage starch structure in maize. Plant Physiol. 117:425-435.
    • (1998) Plant Physiol , vol.117 , pp. 425-435
    • Rahman, A.1    Wong, K.2    Jane, J.3    Myers, A.M.4    James, M.G.5
  • 144
    • 33747887154 scopus 로고    scopus 로고
    • Turning on gibberellin and abscisic acid signaling
    • Razem, F.A., K. Baron, and R.D. Hill. 2006. Turning on gibberellin and abscisic acid signaling. Curr. Opin. Plant Biol. 9:454-459.
    • (2006) Curr. Opin. Plant Biol , vol.9 , pp. 454-459
    • Razem, F.A.1    Baron, K.2    Hill, R.D.3
  • 145
    • 0033969448 scopus 로고    scopus 로고
    • Specific inhibition of barley alpha-amylase 2 by barley alpha-amylase/subtilisin inhibitor depends on charge interactions and can be conferred to isozyme 1 by mutation
    • Rodenburg, K.W., F. Vall é e, N. Juge, N. Aghajari, X. Guo, R. Haser, and B. Svensson. 2000. Specific inhibition of barley alpha-amylase 2 by barley alpha-amylase/subtilisin inhibitor depends on charge interactions and can be conferred to isozyme 1 by mutation. Eur. J. Biochem. 267:1019-1029.
    • (2000) Eur. J. Biochem , vol.267 , pp. 1019-1029
    • Rodenburg, K.W.1    Vallée, F.2    Juge, N.3    Aghajari, N.4    Guo, X.5    Haser, R.6    Svensson, B.7
  • 147
    • 0011742571 scopus 로고
    • Aleurain:a barley thiol protease closely related to mammalian cathep-sin H
    • Rogers, J.C., D. Dean, and G.R. Heck. 1985. Aleurain:a barley thiol protease closely related to mammalian cathep-sin H. Proc. Natl. Acad. Sci. U. S. A. 82:6512-6516.
    • (1985) Proc. Natl. Acad. Sci. U. S. A , vol.82 , pp. 6512-6516
    • Rogers, J.C.1    Dean, D.2    Heck, G.R.3
  • 149
    • 38649107053 scopus 로고    scopus 로고
    • Understanding gibberellic acid signaling-are we there yet?
    • Schwechheimer, C. 2008. Understanding gibberellic acid signaling-are we there yet? Curr. Opin. Plant Biol. 11. 9-15.
    • (2008) Curr. Opin. Plant Biol , vol.11 , pp. 9-15
    • Schwechheimer, C.1
  • 151
    • 38949203862 scopus 로고    scopus 로고
    • The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds:gene expression, protein profiles, and interactions between isoforms of thio-redoxin h and thioredoxin reductase
    • Shahpiri, A., B. Svensson, and C. Finnie. 2008. The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds:gene expression, protein profiles, and interactions between isoforms of thio-redoxin h and thioredoxin reductase. Plant Physiol. 146:789-799.
    • (2008) Plant Physiol , vol.146 , pp. 789-799
    • Shahpiri, A.1    Svensson, B.2    Finnie, C.3
  • 154
    • 0004259001 scopus 로고
    • Seed Dormancy in Grasses
    • Cambridge University Press, Cambridge, UK.
    • Simpson, G.M. 1990. Seed Dormancy in Grasses. Cambridge University Press, Cambridge, UK.
    • (1990)
    • Simpson, G.M.1
  • 155
    • 0037360442 scopus 로고    scopus 로고
    • Structure and function of cereal and related higher plant (1→4)-ß-xylan endohydrolases
    • Simpson, D.J., G.B. Fincher, A.H.C. Huang, and V. Cameron-Mills. 2003. Structure and function of cereal and related higher plant (1→4)-ß-xylan endohydrolases. J. Cereal Sci. 37:111-127.
    • (2003) J. Cereal Sci , vol.37 , pp. 111-127
    • Simpson, D.J.1    Fincher, G.B.2    Huang, A.H.C.3    Cameron-Mills, V.4
  • 156
    • 0024310205 scopus 로고
    • Purification and characterization of three (1→4)-ß-D-xylan endohydrolases from germinating barley
    • Slade, A., P.B. Hoj, N. Morrice, and G.G. Fincher. 1989. Purification and characterization of three (1→4)-ß-D-xylan endohydrolases from germinating barley. Eur. J. Biochem. 185:533-539.
    • (1989) Eur. J. Biochem , vol.185 , pp. 533-539
    • Slade, A.1    Hoj, P.B.2    Morrice, N.3    Fincher, G.G.4
  • 157
    • 0000211193 scopus 로고
    • Developmental regulation of (1,3;1,4)-ß-glucanase gene expression in barley
    • Tissue-specific expression of individual isoenzymes.
    • Slakeski, N. and G.B. Fincher. 1992. Developmental regulation of (1,3;1,4)-ß-glucanase gene expression in barley. Tissue-specific expression of individual isoenzymes. Plant Physiol. 99:1226-1231.
    • (1992) Plant Physiol , vol.99 , pp. 1226-1231
    • Slakeski, N.1    Fincher, G.B.2
  • 158
    • 0025649961 scopus 로고
    • Structure and tissue-specifc regulation of genes encoding barley (1→3,1→4)-beta-glucan endohydrolases
    • Slakeski, N., D.C. Baulcombe, K.M. Devos, B. Ahluwalia, D.N.P. Doan, and G.B. Fincher. 1990. Structure and tissue-specifc regulation of genes encoding barley (1→3,1→4)-beta-glucan endohydrolases. Mol. Gen. Genet. 224:437-449.
    • (1990) Mol. Gen. Genet , vol.224 , pp. 437-449
    • Slakeski, N.1    Baulcombe, D.C.2    Devos, K.M.3    Ahluwalia, B.4    Doan, D.N.P.5    Fincher, G.B.6
  • 159
    • 0025787427 scopus 로고
    • C-terminal processing of barley α-amylase 1 in malt, aleurone protoplasts, and yeast
    • Søgaard, M., F.L. Olsen, and B. Svensson. 1991. C-terminal processing of barley α-amylase 1 in malt, aleurone protoplasts, and yeast. Proc. Natl. Acad. Sci. U. S. A. 88. 8140-8144.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8140-8144
    • Søgaard, M.1    Olsen, F.L.2    Svensson, B.3
  • 160
    • 0017412928 scopus 로고
    • Uptake of small peptides by the scutellum of germinating barley
    • Sopanen, T., D. Burston, and D.M. Matthews. 1977. Uptake of small peptides by the scutellum of germinating barley. FEBS Lett. 79:4-7.
    • (1977) FEBS Lett , vol.79 , pp. 4-7
    • Sopanen, T.1    Burston, D.2    Matthews, D.M.3
  • 161
    • 4143071393 scopus 로고    scopus 로고
    • Antisense downregulation of the barley limit dextrinase inhibitor modulates starch granule size distribution, starch composition and amylopectin structure
    • Stahl, Y., S. Coates, J.H. Bryce, and P.C. Morris. 2004. Antisense downregulation of the barley limit dextrinase inhibitor modulates starch granule size distribution, starch composition and amylopectin structure. Plant J. 39:599-611.
    • (2004) Plant J , vol.39 , pp. 599-611
    • Stahl, Y.1    Coates, S.2    Bryce, J.H.3    Morris, P.C.4
  • 162
    • 0034949020 scopus 로고    scopus 로고
    • Mutant barley (1→3;1→4)-beta-glucan endohydrolases with enhanced thermostability
    • Stewart, R.J., J.N. Varghese, T.P.J. Garrett, P.B. Hoj, and G.B. Fincher. 2001. Mutant barley (1→3;1→4)-beta-glucan endohydrolases with enhanced thermostability. Protein Eng. 14:245-253.
    • (2001) Protein Eng , vol.14 , pp. 245-253
    • Stewart, R.J.1    Varghese, J.N.2    Garrett, T.P.J.3    Hoj, P.B.4    Fincher, G.B.5
  • 163
    • 0033150446 scopus 로고    scopus 로고
    • Analyses of isoamylase gene activity in wild-type barley indicate its involvement in starch synthesis
    • Sun, C., P. Sathish, S. Ahlandsberg, and C. Jansson. 1999. Analyses of isoamylase gene activity in wild-type barley indicate its involvement in starch synthesis. Plant Mol. Biol. 40:431-443.
    • (1999) Plant Mol. Biol , vol.40 , pp. 431-443
    • Sun, C.1    Sathish, P.2    Ahlandsberg, S.3    Jansson, C.4
  • 164
    • 0002770411 scopus 로고
    • Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley
    • Svendsen, I., J. Hejgaard, and J. Mundy. 1986. Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley. Carlsberg Res. Commun. 51:141-157.
    • (1986) Carlsberg Res. Commun , vol.51 , pp. 141-157
    • Svendsen, I.1    Hejgaard, J.2    Mundy, J.3
  • 165
    • 0001033505 scopus 로고
    • Production of cell wall hydrolysing enzymes by barley aleurone layers in response to gibberellic acid
    • Taiz, L. and W.A. Honigman. 1976. Production of cell wall hydrolysing enzymes by barley aleurone layers in response to gibberellic acid. Plant Physiol. 58:380-386.
    • (1976) Plant Physiol , vol.58 , pp. 380-386
    • Taiz, L.1    Honigman, W.A.2
  • 166
    • 0002899634 scopus 로고
    • Gibberellic acid, beta-1,3-glucanase and cell wals of barley aleurone layers
    • Taiz, L. and R.L. Jones. 1970. Gibberellic acid, beta-1,3-glucanase and cell wals of barley aleurone layers. Planta 92:73.
    • (1970) Planta , vol.92 , pp. 73
    • Taiz, L.1    Jones, R.L.2
  • 167
    • 0003056218 scopus 로고
    • Plasmodesmata and an associated cell wall component in barley aleurone tissue
    • Taiz, L. and R.L. Jones. 1973. Plasmodesmata and an associated cell wall component in barley aleurone tissue. Am. J. Bot. 60:67-75.
    • (1973) Am. J. Bot , vol.60 , pp. 67-75
    • Taiz, L.1    Jones, R.L.2
  • 168
    • 0034101067 scopus 로고    scopus 로고
    • Purification and characterization of hor-dolisin, a subtilisin-l ike serine endoprotease from barley
    • Terp, N., K.K. Thomsen, I. Svendsen, A. Davy, and D.J. Simpson. 2000. Purification and characterization of hor-dolisin, a subtilisin-l ike serine endoprotease from barley. J. Plant Physiol. 156:468-476.
    • (2000) J. Plant Physiol , vol.156 , pp. 468-476
    • Terp, N.1    Thomsen, K.K.2    Svendsen, I.3    Davy, A.4    Simpson, D.J.5
  • 169
    • 0032190488 scopus 로고    scopus 로고
    • Expression of enzymatically active, recombinant barley alpha-glucosidase in yeast and immunological detection of alpha-glucosidase from seed tissue
    • Tibbot, B.K., C.A. Henson, and R.W. Skadsen. 1998. Expression of enzymatically active, recombinant barley alpha-glucosidase in yeast and immunological detection of alpha-glucosidase from seed tissue. Plant Mol. Biol. 38. 379-391.
    • (1998) Plant Mol. Biol , vol.38 , pp. 379-391
    • Tibbot, B.K.1    Henson, C.A.2    Skadsen, R.W.3
  • 170
    • 26444434267 scopus 로고    scopus 로고
    • (1→3),(1→4)-ß-D-Glucans in the cell walls of the Poales (sensu lato):an immunogold labeling study using a monoclonal antibody
    • Trethewey, J.A.K., L.M. Campbell, and P.J. Harris. 2005. (1→3),(1→4)-ß-D-Glucans in the cell walls of the Poales (sensu lato):an immunogold labeling study using a monoclonal antibody. Am. J. Bot. 92:1669-1683.
    • (2005) Am. J. Bot , vol.92 , pp. 1669-1683
    • Trethewey, J.A.K.1    Campbell, L.M.2    Harris, P.J.3
  • 171
    • 34248193815 scopus 로고    scopus 로고
    • Nitrate transporters and peptide transporters
    • Tsay, Y.F., C.C. Chiu, C.B. Tsai, C.H. Ho, and P.K. Hsu. 2007. Nitrate transporters and peptide transporters. FEBS Lett. 581:2290-2300.
    • (2007) FEBS Lett , vol.581 , pp. 2290-2300
    • Tsay, Y.F.1    Chiu, C.C.2    Tsai, C.B.3    Ho, C.H.4    Hsu, P.K.5
  • 174
    • 0028270319 scopus 로고
    • Characterization, crystallization and preliminary X-r ay crystallographic analysis of the complex between barley alpha-amylase and the bifunctional alphaamylase/subtilisin inhibitor from barley seeds
    • Vallée, F., A. Kadziola, Y. Bourne, J. Abe, B. Svensson, and R. Haser. 1994. Characterization, crystallization and preliminary X-r ay crystallographic analysis of the complex between barley alpha-amylase and the bifunctional alphaamylase/subtilisin inhibitor from barley seeds. J. Mol. Biol. 236:368-371.
    • (1994) J. Mol. Biol , vol.236 , pp. 368-371
    • Vallée, F.1    Kadziola, A.2    Bourne, Y.3    Abe, J.4    Svensson, B.5    Haser, R.6
  • 177
    • 0033081517 scopus 로고    scopus 로고
    • Threedimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese, J.N., M. Hrmova, and G.B. Fincher. 1999. Threedimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 7:179-190.
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 179
    • 0020989466 scopus 로고
    • Characterization of a dithiol-dependent peptide-transport protein in the scutellum of germinating barley
    • Walker-Smith, D.J. and J.W. Payne. 1983. Characterization of a dithiol-dependent peptide-transport protein in the scutellum of germinating barley. Biochem. Soc. Trans. 11:800-803.
    • (1983) Biochem. Soc. Trans , vol.11 , pp. 800-803
    • Walker-Smith, D.J.1    Payne, J.W.2
  • 180
    • 1442360976 scopus 로고    scopus 로고
    • The changes of beta-glucan content and beta-glucanase activity in barley before and after malting and their relationships to malt qualities
    • Wang, J.M., G.P. Zhang, J.X. Chen, and F.B. Wu. 2004. The changes of beta-glucan content and beta-glucanase activity in barley before and after malting and their relationships to malt qualities. Food Chem. 86:223-228.
    • (2004) Food Chem , vol.86 , pp. 223-228
    • Wang, J.M.1    Zhang, G.P.2    Chen, J.X.3    Wu, F.B.4
  • 181
    • 0033931153 scopus 로고    scopus 로고
    • The barley scutellar peptide transporter:biochemical characterization and localization to the plasma membrane
    • Waterworth, W.M., C.E. West, and C.M. Bray. 2000. The barley scutellar peptide transporter:biochemical characterization and localization to the plasma membrane. J. Exp. Bot. 51:1201-1209.
    • (2000) J. Exp. Bot , vol.51 , pp. 1201-1209
    • Waterworth, W.M.1    West, C.E.2    Bray, C.M.3
  • 182
    • 0032127987 scopus 로고    scopus 로고
    • Cloning and functional characterisation of a peptide transporter expressed in the scutellum of barley grain during the early stages of germination
    • West, C.E., W.M. Waterworth, S.M. Stephens, C.P. Smith, and C.M. Bray. 1998. Cloning and functional characterisation of a peptide transporter expressed in the scutellum of barley grain during the early stages of germination. Plant J. 15:221-229.
    • (1998) Plant J , vol.15 , pp. 221-229
    • West, C.E.1    Waterworth, W.M.2    Stephens, S.M.3    Smith, C.P.4    Bray, C.M.5
  • 183
    • 33746895133 scopus 로고    scopus 로고
    • Temporal and spatial appearance of wall polysaccharides during cellularization of barley (Hordeum vulgare) endosperm
    • Wilson, S.M., R.A. Burton, M.S. Doblin, B.A. Stone, E. Newbigin, G.B. Fincher, and A. Bacic. 2006. Temporal and spatial appearance of wall polysaccharides during cellularization of barley (Hordeum vulgare) endosperm. Planta 224:655-667.
    • (2006) Planta , vol.224 , pp. 655-667
    • Wilson, S.M.1    Burton, R.A.2    Doblin, M.S.3    Stone, B.A.4    Newbigin, E.5    Fincher, G.B.6    Bacic, A.7
  • 184
    • 0037058928 scopus 로고    scopus 로고
    • Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone
    • Wong, J.H., Y.B. Kim, P.H. Ren, N. Cai, M.J. Cho, P. Hedden, P.G. Lemaux, and B.B. Buchanan. 2002. Transgenic barley grain overexpressing thioredoxin shows evidence that the starchy endosperm communicates with the embryo and the aleurone. Proc. Natl. Acad. Sci. USA. 99:16325-16330.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16325-16330
    • Wong, J.H.1    Kim, Y.B.2    Ren, P.H.3    Cai, N.4    Cho, M.J.5    Hedden, P.6    Lemaux, P.G.7    Buchanan, B.B.8
  • 185
    • 0037298311 scopus 로고    scopus 로고
    • A Mak-like kinase is a repressor of GAMYB in barley aleurone
    • Woodger, F.J., F. Gubler, B.J. Pogson, and J.V. Jacobsen. 2003. A Mak-like kinase is a repressor of GAMYB in barley aleurone. Plant J. 33:707-717.
    • (2003) Plant J , vol.33 , pp. 707-717
    • Woodger, F.J.1    Gubler, F.2    Pogson, B.J.3    Jacobsen, J.V.4
  • 186
    • 0020023025 scopus 로고
    • Purification and chemical properties of two 1,3:1,4-ß-glucan endohydro-lases from germinating barley
    • Woodward, J.R. and G.B. Fincher. 1982. Purification and chemical properties of two 1,3:1,4-ß-glucan endohydro-lases from germinating barley. Eur. J. Biochem. 121:663-669.
    • (1982) Eur. J. Biochem , vol.121 , pp. 663-669
    • Woodward, J.R.1    Fincher, G.B.2
  • 187
    • 49049126040 scopus 로고
    • Water-soluble (1→3),(1→4)-ß-D-glucans from barley (Hordeum vulgare) endosperm. I. Physicochemical properties
    • a
    • Woodward, J.R., D.R. Phillips, and G.B. Fincher. 1983a. Water-soluble (1→3),(1→4)-ß-D-glucans from barley (Hordeum vulgare) endosperm. I. Physicochemical properties. Carbohydr. Polym. 3:143-156.
    • (1983) Carbohydr. Polym , vol.3 , pp. 143-156
    • Woodward, J.R.1    Phillips, D.R.2    Fincher, G.B.3
  • 188
    • 0001449372 scopus 로고
    • Water-soluble (1→3),(1→4)-ß-D-glucans from barley (Hordeum vulgare) endosperm. II. Fine structure
    • b
    • Woodward, J.R., G.B. Fincher, and B.A. Stone. 1983b. Water-soluble (1→3),(1→4)-ß-D-glucans from barley (Hordeum vulgare) endosperm. II. Fine structure. Carbohydr. Polym. 3:207-225.
    • (1983) Carbohydr. Polym , vol.3 , pp. 207-225
    • Woodward, J.R.1    Fincher, G.B.2    Stone, B.A.3
  • 189
    • 0001395550 scopus 로고
    • Development of proteolytic activities during barley malting and their localization in the green malt kernel
    • Zhang, N. and B.L. Jones. 1995. Development of proteolytic activities during barley malting and their localization in the green malt kernel. J. Cereal Sci. 22:147-155.
    • (1995) J. Cereal Sci , vol.22 , pp. 147-155
    • Zhang, N.1    Jones, B.L.2
  • 190
    • 0035207894 scopus 로고    scopus 로고
    • Cultivar and environmental effects on (1,3;1,4)-beta-D-glucan and protein content in malting barley
    • Zhang, G., J. Chen, J. Wang, and S. Ding. 2001. Cultivar and environmental effects on (1,3;1,4)-beta-D-glucan and protein content in malting barley. J. Cereal Sci. 34:295-301.
    • (2001) J. Cereal Sci , vol.34 , pp. 295-301
    • Zhang, G.1    Chen, J.2    Wang, J.3    Ding, S.4
  • 191
    • 55549145143 scopus 로고    scopus 로고
    • Interactions of two transcriptional repressors and two transcriptional activators in modulating gibberellin signaling in aleurone cells
    • Zou, X., D. Neuman, and QJ. Shen. 2008. Interactions of two transcriptional repressors and two transcriptional activators in modulating gibberellin signaling in aleurone cells. Plant Physiol. 148:176-186.
    • (2008) Plant Physiol , vol.148 , pp. 176-186
    • Zou, X.1    Neuman, D.2    Shen, Q.J.3


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