메뉴 건너뛰기




Volumn 72, Issue 6, 2012, Pages 1015-1026

Redox regulation of glutenin subunit assembly in the plant endoplasmic reticulum

Author keywords

Disulfide bond; Endoplasmic reticulum; Glutathione; Glutenin; Redox; Triticum spp

Indexed keywords

DISULFIDE BONDS; ENDOPLASMIC RETICULUM; GLUTATHIONES; GLUTENIN; REDOX; TRITICUM SPP;

EID: 84871943391     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12020     Document Type: Article
Times cited : (10)

References (61)
  • 3
    • 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. (1991) Seasonal changes in wheat grain quality associated with high temperatures during grain filling. Aust. J. Agric. Res. 42, 21-30.
    • (1991) Aust. J. Agric. Res. , vol.42 , pp. 21-30
    • Blumenthal, C.S.1    Batey, I.L.2    Bekes, F.3    Wrigley, C.W.4    Barlow, E.W.R.5
  • 4
    • 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. (1993) Growth environment and wheat quality: the effect of heat-stress on dough properties and gluten proteins. J. Cereal Sci. 18, 3-21.
    • (1993) J. Cereal Sci. , vol.18 , pp. 3-21
    • Blumenthal, C.S.1    Barlow, E.W.R.2    Wrigley, C.W.3
  • 5
  • 6
    • 0020993866 scopus 로고
    • Ricin and Ricinus communis agglutinin subunits are all derived from a single-size polypeptide precursor
    • Butterworth, A.G. and Lord, J.M. (1983) Ricin and Ricinus communis agglutinin subunits are all derived from a single-size polypeptide precursor. Eur. J. Biochem. 137, 57-65.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 57-65
    • Butterworth, A.G.1    Lord, J.M.2
  • 8
    • 33645784167 scopus 로고    scopus 로고
    • The role of glutathione in disulfide bond formation and endoplasmic reticulum-generated oxidative stress
    • Chakravarthi, S., Jessop, C.E. and Bulleid, N.J. (2006) The role of glutathione in disulfide bond formation and endoplasmic reticulum-generated oxidative stress. EMBO Rep. 7, 271-275.
    • (2006) EMBO Rep. , vol.7 , pp. 271-275
    • Chakravarthi, S.1    Jessop, C.E.2    Bulleid, N.J.3
  • 9
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulfide bond formation
    • Cuozzo, J.W. and Kaiser, C.A. (1999) Competition between glutathione and protein thiols for disulfide bond formation. Nat. Cell Biol. 1, 130-135.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 10
    • 79955556641 scopus 로고    scopus 로고
    • Heat induces the splicing by IRE1 of an mRNA encoding a transcription factor involved in the unfolded protein response in Arabidopsis
    • Deng, Y., Humbert, S., Liu, J.X., Srivastava, R., Rothstein, S.J. and Howell, S.H. (2011) Heat induces the splicing by IRE1 of an mRNA encoding a transcription factor involved in the unfolded protein response in Arabidopsis. Proc. Natl Acad. Sci. USA, 108, 7247-7252.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7247-7252
    • Deng, Y.1    Humbert, S.2    Liu, J.X.3    Srivastava, R.4    Rothstein, S.J.5    Howell, S.H.6
  • 11
    • 0042262430 scopus 로고    scopus 로고
    • Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins
    • Dixon, D.P., Van Lith, M., Edwards, R. and Benham, A.M. (2003) Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins. Antioxid. Redox Signal. 5, 389-396.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 389-396
    • Dixon, D.P.1    Van Lith, M.2    Edwards, R.3    Benham, A.M.4
  • 12
    • 80052914146 scopus 로고    scopus 로고
    • Dynamic trafficking of wheat c-gliadin and its structural domains in tobacco cells, studied with fluorescent protein fusions
    • Francin-Allami, M., Saumonneau, A., Lavenant, L., Bouder, A., Sparkes, I.A., Hawes, C. and Popineau, Y. (2011) Dynamic trafficking of wheat c-gliadin and its structural domains in tobacco cells, studied with fluorescent protein fusions. J. Exp. Bot. 62, 4507-4520.
    • (2011) J. Exp. Bot. , vol.62 , pp. 4507-4520
    • Francin-Allami, M.1    Saumonneau, A.2    Lavenant, L.3    Bouder, A.4    Sparkes, I.A.5    Hawes, C.6    Popineau, Y.7
  • 13
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand, A.R. and Kaiser, C.A. (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell, 1, 161-170.
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 14
    • 0032486270 scopus 로고    scopus 로고
    • Free ricin A chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts
    • Frigerio, L., Vitale, A., Lord, J.M., Ceriotti, A. and Roberts, L.M. (1998) Free ricin A chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts. J. Biol. Chem. 273, 14194-14199.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14194-14199
    • Frigerio, L.1    Vitale, A.2    Lord, J.M.3    Ceriotti, A.4    Roberts, L.M.5
  • 15
    • 55849100775 scopus 로고    scopus 로고
    • A membrane-tethered transcription factor defines a branch of the heat stress response in Arabidopsis thaliana
    • Gao, H., Brandizzi, F., Benning, C. and Larkin, R.M. (2008) A membrane-tethered transcription factor defines a branch of the heat stress response in Arabidopsis thaliana. Proc. Natl Acad. Sci. USA, 105, 16398-16403.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 16398-16403
    • Gao, H.1    Brandizzi, F.2    Benning, C.3    Larkin, R.M.4
  • 16
    • 0035164832 scopus 로고    scopus 로고
    • Biochemical, genetic, and molecular characterization of wheat glutenin and its component subunits
    • Gianibelli, M.C., Larroque, O.R., MacRitchie, F. and Wrigley, C.W. (2001) Biochemical, genetic, and molecular characterization of wheat glutenin and its component subunits. Cereal Chem. 78, 635-646.
    • (2001) Cereal Chem. , vol.78 , pp. 635-646
    • Gianibelli, M.C.1    Larroque, O.R.2    MacRitchie, F.3    Wrigley, C.W.4
  • 17
    • 69949093360 scopus 로고    scopus 로고
    • An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations
    • Hansen, R.E. and Winther, J.R. (2009) An introduction to methods for analyzing thiols and disulfides: reactions, reagents, and practical considerations. Anal. Biochem. 394, 147-158.
    • (2009) Anal. Biochem. , vol.394 , pp. 147-158
    • Hansen, R.E.1    Winther, J.R.2
  • 18
    • 0030993676 scopus 로고    scopus 로고
    • An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein storage vacuoles of plants
    • Hiraiwa, N., Kondo, M., Nishimura, M. and Hara-Nishimura, I. (1997) An aspartic endopeptidase is involved in the breakdown of propeptides of storage proteins in protein storage vacuoles of plants. Eur. J. Biochem. 246, 133-141.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 133-141
    • Hiraiwa, N.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 19
    • 19044379862 scopus 로고    scopus 로고
    • Phylogenetic analyses identify 10 classes of the protein disul-fide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins
    • Houston, N.L., Fan, C.Z., Xiang, Q.Y., Schulze, J.M., Jung, R. and Boston, R. S. (2005) Phylogenetic analyses identify 10 classes of the protein disul-fide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol. 137, 762-778.
    • (2005) Plant Physiol. , vol.137 , pp. 762-778
    • Houston, N.L.1    Fan, C.Z.2    Xiang, Q.Y.3    Schulze, J.M.4    Jung, R.5    Boston, R.S.6
  • 20
    • 0038051905 scopus 로고    scopus 로고
    • Studies on the distribution and binding of endogenous glutathione in wheat dough and gluten: Binding sites of endogenous glutathione in glutenins
    • Hüttner, S. and Wieser, H. (2001) Studies on the distribution and binding of endogenous glutathione in wheat dough and gluten: binding sites of endogenous glutathione in glutenins. Eur. Food Res. Technol. 213,460-464.
    • (2001) Eur. Food Res. Technol. , vol.213 , pp. 460-464
    • Hüttner, S.1    Wieser, H.2
  • 21
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A.J. and Lodish, H.F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science, 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 22
    • 11244319355 scopus 로고    scopus 로고
    • Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells
    • Jessop, C.E. and Bulleid, N.J. (2004) Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. J. Biol. Chem. 279, 55341-55347.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55341-55347
    • Jessop, C.E.1    Bulleid, N.J.2
  • 23
    • 67649205136 scopus 로고    scopus 로고
    • Endogenous redox agents and enzymes that affect protein network formation during breadmaking
    • Joye, I.J., Lagrain, B. and Delcour, J.A. (2009) Endogenous redox agents and enzymes that affect protein network formation during breadmaking. J. Cereal Sci. 50, 1-10.
    • (2009) J. Cereal Sci. , vol.50 , pp. 1-10
    • Joye, I.J.1    Lagrain, B.2    Delcour, J.A.3
  • 24
    • 33751392287 scopus 로고
    • Kinetics and equilibria of thiol disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione
    • Keire, D.A., Strauss, E., Guo, W., Noszal, B. and Rabenstein, D.L. (1992) Kinetics and equilibria of thiol disulfide interchange reactions of selected biological thiols and related molecules with oxidized glutathione. J. Org. Chem. 57, 123-127.
    • (1992) J. Org. Chem. , vol.57 , pp. 123-127
    • Keire, D.A.1    Strauss, E.2    Guo, W.3    Noszal, B.4    Rabenstein, D.L.5
  • 25
    • 78650400337 scopus 로고    scopus 로고
    • Relationship between endogenous protein disulfide isomerase family proteins and glutenin macropolymer
    • Koh, A., Nishimura, K. and Urade, R. (2010) Relationship between endogenous protein disulfide isomerase family proteins and glutenin macropolymer. J. Agric. Food Chem. 58, 12970-12975.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 12970-12975
    • Koh, A.1    Nishimura, K.2    Urade, R.3
  • 26
    • 0022425912 scopus 로고
    • Nucleotide sequence of cloned cDNA coding for preproricin
    • Lamb, F.I., Roberts, L.M. and Lord, J.M. (1985) Nucleotide sequence of cloned cDNA coding for preproricin. Eur. J. Biochem. 148, 265-270.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 265-270
    • Lamb, F.I.1    Roberts, L.M.2    Lord, J.M.3
  • 27
    • 79955878526 scopus 로고    scopus 로고
    • Re-examination of the role of interplay between glutathione and protein disulfide isomerase
    • Lappi, A.K. and Ruddock, L.W. (2011) Re-examination of the role of interplay between glutathione and protein disulfide isomerase. J. Mol. Biol. 409, 238-249.
    • (2011) J. Mol. Biol. , vol.409 , pp. 238-249
    • Lappi, A.K.1    Ruddock, L.W.2
  • 28
    • 0742305352 scopus 로고    scopus 로고
    • The endoplasmic reticulum membrane is permeable to small molecules
    • Le Gall, S., Neuhof, A. and Rapoport, T.A. (2004) The endoplasmic reticulum membrane is permeable to small molecules. Mol. Biol. Cell, 15, 447-455.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 447-455
    • Le Gall, S.1    Neuhof, A.2    Rapoport, T.A.3
  • 29
    • 0000756406 scopus 로고
    • Equilibrium constants for thiol disul-fide interchange reactions: A coherent, corrected set
    • Lees, W.J. and Whitesides, G.M. (1993) Equilibrium constants for thiol disul-fide interchange reactions: a coherent, corrected set. J. Org. Chem. 58, 642-647.
    • (1993) J. Org. Chem. , vol.58 , pp. 642-647
    • Lees, W.J.1    Whitesides, G.M.2
  • 30
    • 0026478698 scopus 로고
    • Evidence for a novel route for transport of wheat storage proteins to vacuoles
    • Levanony, H., Rubin, R., Altschuler, Y. and Galili, G. (1992) Evidence for a novel route for transport of wheat storage proteins to vacuoles. J. Cell Biol. 119, 1117-1128.
    • (1992) J. Cell Biol. , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altschuler, Y.3    Galili, G.4
  • 31
    • 1642331655 scopus 로고    scopus 로고
    • Glutathione and related thiol compounds: The importance of protein-bound glutathione and related protein-bound compounds in gluten proteins
    • Li, W., Tsiami, A.A., Bollecker, S.S. and Schofield, J.D. (2004) Glutathione and related thiol compounds: the importance of protein-bound glutathione and related protein-bound compounds in gluten proteins. J. Cereal Sci. 39, 213-224.
    • (2004) J. Cereal Sci. , vol.39 , pp. 213-224
    • Li, W.1    Tsiami, A.A.2    Bollecker, S.S.3    Schofield, J.D.4
  • 32
    • 58449096493 scopus 로고    scopus 로고
    • A relaxed specificity in interchain disulfide bond formation characterizes the assembly of a lowmolecular-weight glutenin subunit in the endoplasmic reticulum
    • Lombardi, A., Barbante, A., Della Cristina, P., Rosiello, D., Castellazzi, C.L., Sbano, L., Masci, S. and Ceriotti, A. (2009) A relaxed specificity in interchain disulfide bond formation characterizes the assembly of a lowmolecular-weight glutenin subunit in the endoplasmic reticulum. Plant Physiol. 149, 412-423.
    • (2009) Plant Physiol. , vol.149 , pp. 412-423
    • Lombardi, A.1    Barbante, A.2    Della Cristina, P.3    Rosiello, D.4    Castellazzi, C.L.5    Sbano, L.6    Masci, S.7    Ceriotti, A.8
  • 33
    • 0015914077 scopus 로고
    • Streptomycin-resistant plants from callus culture of haploid tobacco
    • Maliga, P., Sz-Breznovits, A. and Marton, L. (1973) Streptomycin- resistant plants from callus culture of haploid tobacco. Nat. New Biol. 244,29-30.
    • (1973) Nat. New Biol. , vol.244 , pp. 29-30
    • Maliga, P.1    Sz-Breznovits, A.2    Marton, L.3
  • 34
    • 77954173918 scopus 로고    scopus 로고
    • Oxidative folding in the endoplasmic reticulum: Towards a multiple oxidant hypothesis
    • Margittai, E. and Bánhegyi, G. (2010) Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis. FEBS Lett. 584,2995-2998.
    • (2010) FEBS Lett. , vol.584 , pp. 2995-2998
    • Margittai, E.1    Bánhegyi, G.2
  • 35
    • 77951224364 scopus 로고    scopus 로고
    • Disulfide formation in plant storage vacuoles permits assembly of a multimeric lectin
    • Marshall, R.S., Frigerio, L. and Roberts, L.M. (2010) Disulfide formation in plant storage vacuoles permits assembly of a multimeric lectin. Biochem. J. 427, 513-521.
    • (2010) Biochem. J. , vol.427 , pp. 513-521
    • Marshall, R.S.1    Frigerio, L.2    Roberts, L.M.3
  • 36
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • Merksamer, P.I., Trusina, A. and Papa, F.R. (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell, 135, 933-947.
    • (2008) Cell , vol.135 , pp. 933-947
    • Merksamer, P.I.1    Trusina, A.2    Papa, F.R.3
  • 37
    • 0034906367 scopus 로고    scopus 로고
    • Quantitative in vivo measurement of glutathione in Arabidopsis cells
    • Meyer, A.J., May, M.J. and Fricker, M. (2001) Quantitative in vivo measurement of glutathione in Arabidopsis cells. Plant J. 27, 67-78.
    • (2001) Plant J. , vol.27 , pp. 67-78
    • Meyer, A.J.1    May, M.J.2    Fricker, M.3
  • 39
    • 0021933493 scopus 로고
    • Evolution and heterogeneity of the a/b-type and c-type gliadin DNA sequences
    • Okita, T.W., Cheesbrough, V. and Reeves, C.D. (1985) Evolution and heterogeneity of the a/b-type and c-type gliadin DNA sequences. J. Biol. Chem. 260, 8203-8213.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8203-8213
    • Okita, T.W.1    Cheesbrough, V.2    Reeves, C.D.3
  • 40
    • 69549111486 scopus 로고    scopus 로고
    • ER membrane-localized oxidoreductase Ero1 is required for disulfide bond formation in the rice endosperm
    • Onda, Y., Kumamaru, T. and Kawagoe, Y. (2009) ER membrane-localized oxidoreductase Ero1 is required for disulfide bond formation in the rice endosperm. Proc. Natl Acad. Sci. USA, 106, 14156-14161.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14156-14161
    • Onda, Y.1    Kumamaru, T.2    Kawagoe, Y.3
  • 41
    • 79952310220 scopus 로고    scopus 로고
    • Distinct roles of protein disulfide isomerase and P5 sulfhydryl oxidoreductases in multiple pathways for oxidation of structurally diverse storage proteins in rice
    • Onda, Y., Nagamine, A., Sakurai, M., Kumamaru, T., Ogawa, M. and Kawagoe, Y. (2011) Distinct roles of protein disulfide isomerase and P5 sulfhydryl oxidoreductases in multiple pathways for oxidation of structurally diverse storage proteins in rice. Plant Cell, 23, 210-223.
    • (2011) Plant Cell , vol.23 , pp. 210-223
    • Onda, Y.1    Nagamine, A.2    Sakurai, M.3    Kumamaru, T.4    Ogawa, M.5    Kawagoe, Y.6
  • 42
    • 0035943660 scopus 로고    scopus 로고
    • Role of individual disulfide bonds in the structural maturation of a low-molecular-weight glutenin subunit
    • Orsi, A., Sparvoli, F. and Ceriotti, A. (2001) Role of individual disulfide bonds in the structural maturation of a low-molecular-weight glutenin subunit. J. Biol. Chem. 276, 32322-32329.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32322-32329
    • Orsi, A.1    Sparvoli, F.2    Ceriotti, A.3
  • 43
    • 0001906328 scopus 로고
    • Subunit composition of wheat glutenin proteins isolated by gel-filtration in a dissociating medium
    • Payne, P.I. and Corfield, K.G. (1979) Subunit composition of wheat glutenin proteins isolated by gel-filtration in a dissociating medium. Planta, 145, 83-88.
    • (1979) Planta , vol.145 , pp. 83-88
    • Payne, P.I.1    Corfield, K.G.2
  • 45
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard, M.G., Travers, K.J. and Weissman, J.S. (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell, 1, 171-182.
    • (1998) Mol. Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 46
    • 0142031157 scopus 로고    scopus 로고
    • Changes in the glutathione thiol-disulfide status during wheat grain development
    • Rhazi, L., Cazalis, R., Lemelin, E. and Aussenac, T. (2003) Changes in the glutathione thiol-disulfide status during wheat grain development. Plant Physiol. Biochem. 41, 895-902.
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 895-902
    • Rhazi, L.1    Cazalis, R.2    Lemelin, E.3    Aussenac, T.4
  • 47
    • 0024673608 scopus 로고
    • Tissue-specific expression of a wheat high-molecular-weight glutenin gene in transgenic tobacco
    • Robert, L.S., Thompson, R.D. and Flavell, R.B. (1989) Tissue-specific expression of a wheat high-molecular-weight glutenin gene in transgenic tobacco. Plant Cell, 1, 569-578.
    • (1989) Plant Cell , vol.1 , pp. 569-578
    • Robert, L.S.1    Thompson, R.D.2    Flavell, R.B.3
  • 48
    • 11944255947 scopus 로고
    • Evidence for the presence of two different types of protein bodies in wheat endosperm
    • Rubin, R., Levanony, H. and Galili, G. (1992) Evidence for the presence of two different types of protein bodies in wheat endosperm. Plant Physiol. 99, 718-724.
    • (1992) Plant Physiol. , vol.99 , pp. 718-724
    • Rubin, R.1    Levanony, H.2    Galili, G.3
  • 49
    • 84871975403 scopus 로고    scopus 로고
    • Redox potentials of cysteine residues in peptides and proteins: Methods for their determination
    • (Buchner, J. and Moroder, L., eds). Cambridge, UK: Royal Society of Chemistry Publishing
    • Rabenstein, D.L. (2009) Redox potentials of cysteine residues in peptides and proteins: methods for their determination. In Oxidative Folding of Peptides and Proteins (Buchner, J. and Moroder, L., eds). Cambridge, UK: Royal Society of Chemistry Publishing, pp. 220-235.
    • (2009) Oxidative Folding of Peptides and Proteins , pp. 220-235
    • Rabenstein, D.L.1
  • 51
    • 0028243830 scopus 로고
    • Mechanisms of assembly of wheat high-molecular-weight glutenins inferred from expression of wild-type and mutant subunits in transgenic tobacco
    • Shani, N., Rosenberg, N., Kasarda, D.D. and Galili, G. (1994) Mechanisms of assembly of wheat high-molecular-weight glutenins inferred from expression of wild-type and mutant subunits in transgenic tobacco. J. Biol. Chem. 269, 8924-8930.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8924-8930
    • Shani, N.1    Rosenberg, N.2    Kasarda, D.D.3    Galili, G.4
  • 52
    • 79952987484 scopus 로고    scopus 로고
    • Gene networks in the synthesis and deposition of protein polymers during grain development of wheat
    • She, M., Ye, X., Yan, Y., Howit, C., Belgard, M. and Ma, W. (2011) Gene networks in the synthesis and deposition of protein polymers during grain development of wheat. Funct. Integr. Genomics, 11, 23-35.
    • (2011) Funct. Integr. Genomics , vol.11 , pp. 23-35
    • She, M.1    Ye, X.2    Yan, Y.3    Howit, C.4    Belgard, M.5    Ma, W.6
  • 55
    • 0012342479 scopus 로고    scopus 로고
    • Disulphide bonds in wheat gluten proteins
    • Tatham, A.S. and Shewry, P.R. (1997) Disulphide bonds in wheat gluten proteins. J. Cereal Sci. 25, 207-227.
    • (1997) J. Cereal Sci. , vol.25 , pp. 207-227
    • Tatham, A.S.1    Shewry, P.R.2
  • 57
    • 79959746399 scopus 로고    scopus 로고
    • Distribution of gluten proteins in bread wheat (Triticum aestivum) grain
    • Tosi, P., Gritsch, C.S., He, J. and Shewry, P.R. (2011) Distribution of gluten proteins in bread wheat (Triticum aestivum) grain. Ann. Bot. 108, 23-35.
    • (2011) Ann. Bot. , vol.108 , pp. 23-35
    • Tosi, P.1    Gritsch, C.S.2    He, J.3    Shewry, P.R.4
  • 58
    • 0028588562 scopus 로고
    • The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi
    • Valetti, C. and Sitia, R. (1994) The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi. Mol. Biol. Cell, 5, 1311-1324.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1311-1324
    • Valetti, C.1    Sitia, R.2
  • 59
    • 16544394131 scopus 로고    scopus 로고
    • Protein quality control mechanisms and protein storage in the endoplasmic reticulum: A conflict of interests
    • Vitale, A. and Ceriotti, A. (2004) Protein quality control mechanisms and protein storage in the endoplasmic reticulum: a conflict of interests. Plant Physiol. 136, 3420-3426.
    • (2004) Plant Physiol. , vol.136 , pp. 3420-3426
    • Vitale, A.1    Ceriotti, A.2
  • 60
    • 0036331480 scopus 로고    scopus 로고
    • Contrasting effects of chronic heat stress and heat shock on kernel weight and flour quality in wheat
    • Wardlaw, I.F., Blumenthal, C.S., Larroque, O.R. and Wrigley, C.W. (2002) Contrasting effects of chronic heat stress and heat shock on kernel weight and flour quality in wheat. Funct. Plant Biol. 29, 25-34.
    • (2002) Funct. Plant Biol. , vol.29 , pp. 25-34
    • Wardlaw, I.F.1    Blumenthal, C.S.2    Larroque, O.R.3    Wrigley, C.W.4
  • 61
    • 0029999609 scopus 로고    scopus 로고
    • Giant proteins with flour power
    • Wrigley, C.W. (1996) Giant proteins with flour power. Nature, 381, 738-739.
    • (1996) Nature , vol.381 , pp. 738-739
    • Wrigley, C.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.