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Volumn 10, Issue 9, 2015, Pages

The role of cysteine residues in redox regulation and protein stability of Arabidopsis thaliana starch synthase 1

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; CYSTEINE; DISULFIDE; GLUCOSE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEPENDENT THIOREDOXIN REDUCTASE C; SERINE; STARCH SYNTHASE; STARCH SYNTHASE 1; THIOL DISULFIDE; THIOREDOXIN; THIOREDOXIN F1; THIOREDOXIN M4; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; GLUCOSYLTRANSFERASE; SS1 PROTEIN, ARABIDOPSIS;

EID: 84947418428     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0136997     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 84881446336 scopus 로고    scopus 로고
    • Future Cereal Starch Bioengineering: Cereal Ancestors Encounter Gene Technology and Designer Enzymes
    • Blennow A, Jensen SL, Shaik SS, Skryhan K, Carciofi M, Holm PB, et al. Future Cereal Starch Bioengineering: Cereal Ancestors Encounter Gene Technology and Designer Enzymes. Cereal Chem. 2013; 90: 274-287. doi: 10.1094/CCHEM-01-13-0010-FI
    • (2013) Cereal Chem , vol.90 , pp. 274-287
    • Blennow, A.1    Jensen, S.L.2    Shaik, S.S.3    Skryhan, K.4    Carciofi, M.5    Holm, P.B.6
  • 2
    • 84861862587 scopus 로고    scopus 로고
    • Starch in the Arabidopsis plant
    • Smith AM. Starch in the Arabidopsis plant. Starch-Stärke. 2012; 00: 1-14. doi: 10.1002/star. 201100163
    • (2012) Starch-Stärke , pp. 1-14
    • Smith, A.M.1
  • 3
    • 84861696465 scopus 로고    scopus 로고
    • Starch turnover: Pathways regulation and role in growth
    • Elsevier Ltd;
    • Stitt M, Zeeman SC. Starch turnover: pathways, regulation and role in growth. Curr Opin Plant Biol. Elsevier Ltd; 2012; 15: 282-92. doi: 10.1016/j.pbi.2012.03.016
    • (2012) Curr Opin Plant Biol , vol.15 , pp. 282-292
    • Stitt, M.1    Zeeman, S.C.2
  • 4
    • 84880570732 scopus 로고    scopus 로고
    • Starch metabolism in Arabidopsis
    • PMID: 23393426
    • Streb S, Zeeman SC. Starch metabolism in Arabidopsis. Arabidopsis Book. 2012; 10: e0160. doi: 10. 1199/tab.0160 PMID: 23393426
    • (2012) Arabidopsis Book , vol.10 , pp. e0160
    • Streb, S.1    Zeeman, S.C.2
  • 5
    • 77950519125 scopus 로고    scopus 로고
    • Helix-breaking news: Fighting crystalline starch energy deposits in the cell
    • PMID: 20149714
    • Blennow A, Engelsen SB. Helix-breaking news: fighting crystalline starch energy deposits in the cell. Trends Plant Sci. 2010; 15: 236-40. doi: 10.1016/j.tplants.2010.01.009 PMID: 20149714
    • (2010) Trends Plant Sci , vol.15 , pp. 236-240
    • Blennow, A.1    Engelsen, S.B.2
  • 6
    • 79953701211 scopus 로고    scopus 로고
    • Regulation of starch metabolism: The age of enlightenment?
    • Elsevier Ltd;
    • Kötting O, Kossmann J, Zeeman SC, Lloyd JR. Regulation of starch metabolism: the age of enlightenment? Curr Opin Plant Biol. Elsevier Ltd; 2010; 13: 321-9. doi: 10.1016/j.pbi.2010.01.003
    • (2010) Curr Opin Plant Biol , vol.13 , pp. 321-329
    • Kötting, O.1    Kossmann, J.2    Zeeman, S.C.3    Lloyd, J.R.4
  • 7
    • 20044385057 scopus 로고    scopus 로고
    • Redox regulation of carbon storage and partitioning in response to light and sugars
    • PMID: 15863446
    • Geigenberger P, Kolbe A, Tiessen A. Redox regulation of carbon storage and partitioning in response to light and sugars. J Exp Bot. 2005; 56: 1469-79. doi: 10.1093/jxb/eri178 PMID: 15863446
    • (2005) J Exp Bot , vol.56 , pp. 1469-1479
    • Geigenberger, P.1    Kolbe, A.2    Tiessen, A.3
  • 8
    • 84876787676 scopus 로고    scopus 로고
    • Plant type ferredoxins and ferredoxin-dependent metabolism
    • PMID: 23190083
    • Hanke G, Mulo P. Plant type ferredoxins and ferredoxin-dependent metabolism. Plant Cell Environ. 2013; 36: 1071-84. doi: 10.1111/pce.12046 PMID: 23190083
    • (2013) Plant Cell Environ , vol.36 , pp. 1071-1084
    • Hanke, G.1    Mulo, P.2
  • 9
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • PMID: 18377232
    • Schürmann P, Buchanan BB. The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid Redox Signal. 2008; 10: 1235-74. doi: 10.1089/ars.2007.1931 PMID: 18377232
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 10
    • 84964314650 scopus 로고    scopus 로고
    • Metabolic Control of Redox and Redox Control of Metabolism in Plants
    • Geigenberger P, Fernie AR. Metabolic Control of Redox and Redox Control of Metabolism in Plants. Antioxid Redox Signal. 2014; 00: 1-33. doi: 10.1089/ars.2014.6018
    • (2014) Antioxid Redox Signal , pp. 1-33
    • Geigenberger, P.1    Fernie, A.R.2
  • 11
    • 79953709713 scopus 로고    scopus 로고
    • Novel regulators in photosynthetic redox control of plant metabolism and gene expression
    • PMID: 21205617
    • Dietz K-J, Pfannschmidt T. Novel regulators in photosynthetic redox control of plant metabolism and gene expression. Plant Physiol. 2011; 155: 1477-85. doi: 10.1104/pp.110.170043 PMID: 21205617
    • (2011) Plant Physiol , vol.155 , pp. 1477-1485
    • Dietz, K.-J.1    Pfannschmidt, T.2
  • 13
    • 29944441650 scopus 로고    scopus 로고
    • Thioredoxins in Arabidopsis and other plants
    • PMID: 16307307
    • Meyer Y, Reichheld JP, Vignols F. Thioredoxins in Arabidopsis and other plants. Photosynth Res. 2005; 86: 419-33. doi: 10.1007/s11120-005-5220-y PMID: 16307307
    • (2005) Photosynth Res , vol.86 , pp. 419-433
    • Meyer, Y.1    Reichheld, J.P.2    Vignols, F.3
  • 15
    • 84878018743 scopus 로고    scopus 로고
    • Overexpression of plastidial thioredoxin f leads to enhanced starch accumulation in tobacco leaves
    • PMID: 23398733
    • Sanz-Barrio R, Corral-Martinez P, Ancin M, Segui-Simarro JM, Farran I. Overexpression of plastidial thioredoxin f leads to enhanced starch accumulation in tobacco leaves. Plant Biotechnol J. 2013; 11: 618-27. doi: 10.1111/pbi.12052 PMID: 23398733
    • (2013) Plant Biotechnol J. , vol.11 , pp. 618-627
    • Sanz-Barrio, R.1    Corral-Martinez, P.2    Ancin, M.3    Segui-Simarro, J.M.4    Farran, I.5
  • 16
    • 84870491144 scopus 로고    scopus 로고
    • Inactivation of thioredoxin f1 leads to decreased light activation of ADP-glucose pyrophosphorylase and altered diurnal starch turnover in leaves of Arabidopsis plants
    • PMID: 22646759
    • Thormählen I, Ruber J, von Roepenack-Lahaye E, Ehrlich S-M, Massot V, Hümmer C, et al. Inactivation of thioredoxin f1 leads to decreased light activation of ADP-glucose pyrophosphorylase and altered diurnal starch turnover in leaves of Arabidopsis plants. Plant Cell Environ. 2013; 36: 16-29. doi: 10. 1111/j.1365-3040.2012.02549.x PMID: 22646759
    • (2013) Plant Cell Environ , vol.36 , pp. 16-29
    • Thormählen, I.1    Ruber, J.2    Von Roepenack-Lahaye, E.3    Ehrlich, S.-M.4    Massot, V.5    Hümmer, C.6
  • 17
    • 33749233825 scopus 로고    scopus 로고
    • Rice NTRC is a highefficiency redox system for chloroplast protection against oxidative damage
    • PMID: 16891402
    • Pérez-Ruiz JM, Spínola MC, Kirchsteiger K, Moreno J, Sahrawy M, Cejudo FJ. Rice NTRC is a highefficiency redox system for chloroplast protection against oxidative damage. Plant Cell. 2006; 18: 2356-68. doi: 10.1105/tpc.106.041541 PMID: 16891402
    • (2006) Plant Cell , vol.18 , pp. 2356-2368
    • Pérez-Ruiz, J.M.1    Spínola, M.C.2    Kirchsteiger, K.3    Moreno, J.4    Sahrawy, M.5    Cejudo, F.J.6
  • 18
    • 67649880593 scopus 로고    scopus 로고
    • NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts
    • PMID: 19470473
    • Michalska J, Zauber H, Buchanan BB, Cejudo FJ, Geigenberger P. NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts. Proc Natl Acad Sci U S A. 2009; 106: 9908-13. doi: 10.1073/pnas.0903559106 PMID: 19470473
    • (2009) Proc Natl Acad Sci U S A. , vol.106 , pp. 9908-9913
    • Michalska, J.1    Zauber, H.2    Buchanan, B.B.3    Cejudo, F.J.4    Geigenberger, P.5
  • 19
    • 84861709976 scopus 로고    scopus 로고
    • NADPH thioredoxin reductase C is localized in plastids of photosynthetic and nonphotosynthetic tissues and is involved in lateral root formation in Arabidopsis
    • PMID: 22505729
    • Kirchsteiger K, Ferrández J, Pascual MB, González M, Cejudo FJ. NADPH thioredoxin reductase C is localized in plastids of photosynthetic and nonphotosynthetic tissues and is involved in lateral root formation in Arabidopsis. Plant Cell. 2012; 24: 1534-48. doi: 10.1105/tpc.111.092304 PMID: 22505729
    • (2012) Plant Cell , vol.24 , pp. 1534-1548
    • Kirchsteiger, K.1    Ferrández, J.2    Pascual, M.B.3    González, M.4    Cejudo, F.J.5
  • 20
    • 33644541407 scopus 로고    scopus 로고
    • A complete ferredoxin/ thioredoxin system regulates fundamental processes in amyloplasts
    • PMID: 16481623
    • Balmer Y, Vensel WH, Cai N, Manieri W, Schürmann P, Hurkman WJ, et al. A complete ferredoxin/ thioredoxin system regulates fundamental processes in amyloplasts. Proc Natl Acad Sci U S A. 2006; 103: 2988-93. doi: 10.1073/pnas.0511040103 PMID: 16481623
    • (2006) Proc Natl Acad Sci U S A. , vol.103 , pp. 2988-2993
    • Balmer, Y.1    Vensel, W.H.2    Cai, N.3    Manieri, W.4    Schürmann, P.5    Hurkman, W.J.6
  • 21
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • PMID: 15862094
    • Buchanan BB, Balmer Y. Redox regulation: a broadening horizon. Annu Rev Plant Biol. 2005; 56: 187-220. doi: 10.1146/annurev.arplant.56.032604.144246 PMID: 15862094
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 22
    • 0142214642 scopus 로고    scopus 로고
    • ADP-Glucose Pyrophosphorylase Is Activated by Posttranslational Redox-Modification in Response to Light and to Sugars in Leaves of Arabidopsis and Other Plant Species
    • PMID: 12972664
    • Hendriks JHM, Kolbe A, Gibon Y, Stitt M, Geigenberger P. ADP-Glucose Pyrophosphorylase Is Activated by Posttranslational Redox-Modification in Response to Light and to Sugars in Leaves of Arabidopsis and Other Plant Species. Plant Physiol. 2003; 133: 838-849. PMID: 12972664
    • (2003) Plant Physiol , vol.133 , pp. 838-849
    • Hendriks, J.H.M.1    Kolbe, A.2    Gibon, Y.3    Stitt, M.4    Geigenberger, P.5
  • 23
    • 84859510233 scopus 로고    scopus 로고
    • Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves
    • PMID: 22098298
    • Hädrich N, Hendriks JHM, Kötting O, Arrivault S, Feil R, Zeeman SC, et al. Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves. Plant J. 2012; 70: 231-42. doi: 10.1111/j.1365-313X.2011. 04860.x PMID: 22098298
    • (2012) Plant J. , vol.70 , pp. 231-242
    • Hädrich, N.1    Hendriks, J.H.M.2    Kötting, O.3    Arrivault, S.4    Feil, R.5    Zeeman, S.C.6
  • 24
    • 13444311548 scopus 로고    scopus 로고
    • Alpha-glucan, water dikinase (GWD): A plastidic enzyme with redox-regulated and coordinated catalytic activity and binding affinity
    • PMID: 15665090
    • Mikkelsen R, Mutenda KE, Mant A, Schürmann P, Blennow A. Alpha-glucan, water dikinase (GWD): a plastidic enzyme with redox-regulated and coordinated catalytic activity and binding affinity. Proc Natl Acad Sci U S A. 2005; 102: 1785-90. PMID: 15665090
    • (2005) Proc Natl Acad Sci U S A. , vol.102 , pp. 1785-1790
    • Mikkelsen, R.1    Mutenda, K.E.2    Mant, A.3    Schürmann, P.4    Blennow, A.5
  • 25
    • 84863671631 scopus 로고    scopus 로고
    • Comprehensive survey of redox sensitive starch metabolising enzymes in Arabidopsis thaliana
    • PMID: 22789914
    • Glaring MA, Skryhan K, Kötting O, Zeeman SC, Blennow A. Comprehensive survey of redox sensitive starch metabolising enzymes in Arabidopsis thaliana. Plant Physiol Biochem. 2012; 58: 89-97. doi: 10. 1016/j.plaphy.2012.06.017 PMID: 22789914
    • (2012) Plant Physiol Biochem , vol.58 , pp. 89-97
    • Glaring, M.A.1    Skryhan, K.2    Kötting, O.3    Zeeman, S.C.4    Blennow, A.5
  • 27
    • 0032143523 scopus 로고    scopus 로고
    • A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme
    • PMID: 9750347
    • Zeeman SC, Northrop F, Smith AM, Rees T. A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme. Plant J. 1998; 15: 357-65. PMID: 9750347
    • (1998) Plant J. , vol.15 , pp. 357-365
    • Zeeman, S.C.1    Northrop, F.2    Smith, A.M.3    Rees, T.4
  • 28
    • 27644567790 scopus 로고    scopus 로고
    • Soluble starch synthase I: A major determinant for the synthesis of amylopectin in Arabidopsis thaliana leaves
    • PMID: 16045475
    • Delvallé D, Dumez S, Wattebled F, Roldán I, Planchot V, Berbezy P, et al. Soluble starch synthase I: a major determinant for the synthesis of amylopectin in Arabidopsis thaliana leaves. Plant J. 2005; 43: 398-412. doi: 10.1111/j.1365-313X.2005.02462.x PMID: 16045475
    • (2005) Plant J. , vol.43 , pp. 398-412
    • Delvallé, D.1    Dumez, S.2    Wattebled, F.3    Roldán, I.4    Planchot, V.5    Berbezy, P.6
  • 29
    • 70350214641 scopus 로고    scopus 로고
    • Oligosaccharide binding in Escherichia coli glycogen synthase
    • PMID: 19761218
    • Sheng F, Yep A, Feng L, Preiss J, Geiger JH. Oligosaccharide binding in Escherichia coli glycogen synthase. Biochemistry. 2009; 48: 10089-97. doi: 10.1021/bi900916t PMID: 19761218
    • (2009) Biochemistry , vol.48 , pp. 10089-10097
    • Sheng, F.1    Yep, A.2    Feng, L.3    Preiss, J.4    Geiger, J.H.5
  • 31
    • 58149193233 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository and associated resources
    • PMID: 18931379
    • Kiefer F, Arnold K, Künzli M, Bordoli L, Schwede T. The SWISS-MODEL Repository and associated resources. Nucleic Acids Res. 2009; 37: D387-92. doi: 10.1093/nar/gkn750 PMID: 18931379
    • (2009) Nucleic Acids Res , vol.37 , pp. D387-D392
    • Kiefer, F.1    Arnold, K.2    Künzli, M.3    Bordoli, L.4    Schwede, T.5
  • 32
    • 67650516761 scopus 로고    scopus 로고
    • The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase
    • PMID: 19244233
    • Sheng F, Jia X, Yep A, Preiss J, Geiger JH. The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase. J Biol Chem. 2009; 284: 17796-807. doi: 10.1074/jbc.M809804200 PMID: 19244233
    • (2009) J Biol Chem , vol.284 , pp. 17796-17807
    • Sheng, F.1    Jia, X.2    Yep, A.3    Preiss, J.4    Geiger, J.H.5
  • 33
    • 84865495972 scopus 로고    scopus 로고
    • Interdomain Disulfide Bridge in the Rice Granule Bound Starch Synthase i Catalytic Domain as Elucidated by X-Ray Structure Analysis
    • PMID: 22878205
    • Momma M, Fujimoto Z. Interdomain Disulfide Bridge in the Rice Granule Bound Starch Synthase I Catalytic Domain as Elucidated by X-Ray Structure Analysis. Biosci Biotechnol Biochem. 2012; 76: 1591-1595. doi: 10.1271/bbb.120305 PMID: 22878205
    • (2012) Biosci Biotechnol Biochem , vol.76 , pp. 1591-1595
    • Momma, M.1    Fujimoto, Z.2
  • 34
    • 1542319703 scopus 로고    scopus 로고
    • Identification and characterization of a critical region in the glycogen synthase from Escherichia coli
    • PMID: 14665620
    • Yep A, Ballicora M a, Sivak MN, Preiss J. Identification and characterization of a critical region in the glycogen synthase from Escherichia coli. J Biol Chem. 2004; 279: 8359-67. doi: 10.1074/jbc. M312686200 PMID: 14665620
    • (2004) J Biol Chem , vol.279 , pp. 8359-8367
    • Yep, A.1    Ballicora, M.A.2    Sivak, M.N.3    Preiss, J.4
  • 35
    • 84886038090 scopus 로고    scopus 로고
    • Photosynthesis-related quantities for education and modeling
    • PMID: 24162971
    • Antal TK, Kovalenko IB, Rubin AB, Tyystjärvi E. Photosynthesis-related quantities for education and modeling. Photosynth Res. 2013; 117: 1-30. doi: 10.1007/s11120-013-9945-8 PMID: 24162971
    • (2013) Photosynth Res , vol.117 , pp. 1-30
    • Antal, T.K.1    Kovalenko, I.B.2    Rubin, A.B.3    Tyystjärvi, E.4
  • 36
    • 84901711172 scopus 로고    scopus 로고
    • Klebsormidium flaccidum genome reveals primary factors for plant terrestrial adaptation
    • Nature Publishing Group;
    • Hori K, Maruyama F, Fujisawa T, Togashi T, Yamamoto N, Seo M, et al. Klebsormidium flaccidum genome reveals primary factors for plant terrestrial adaptation. Nat Commun. Nature Publishing Group; 2014; 5: 3978. doi: 10.1038/ncomms4978
    • (2014) Nat Commun , vol.5 , pp. 3978
    • Hori, K.1    Maruyama, F.2    Fujisawa, T.3    Togashi, T.4    Yamamoto, N.5    Seo, M.6
  • 37
    • 0033966939 scopus 로고    scopus 로고
    • Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin
    • PMID: 10625679
    • Ballicora MA, Frueauf JB, Fu Y, Schürmann P, Preiss J. Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin. J Biol Chem. 2000; 275: 1315-20. PMID: 10625679
    • (2000) J Biol Chem , vol.275 , pp. 1315-1320
    • Ballicora, M.A.1    Frueauf, J.B.2    Fu, Y.3    Schürmann, P.4    Preiss, J.5
  • 38
    • 84872805864 scopus 로고    scopus 로고
    • Insight into the redox regulation of the phosphoglucan phosphatase SEX4 involved in starch degradation
    • PMID: 22372537
    • Silver DM, Silva LP, Issakidis-Bourguet E, Glaring M a, Schriemer DC, Moorhead GBG. Insight into the redox regulation of the phosphoglucan phosphatase SEX4 involved in starch degradation. FEBS J. 2013; 280: 538-48. doi: 10.1111/j.1742-4658.2012.08546.x PMID: 22372537
    • (2013) FEBS J. , vol.280 , pp. 538-548
    • Silver, D.M.1    Silva, L.P.2    Issakidis-Bourguet, E.3    Glaring, M.A.4    Schriemer, D.C.5    Moorhead, G.B.G.6
  • 39
    • 33745961686 scopus 로고    scopus 로고
    • Redox Regulation of a Novel Plastid-Targeted b- Amylase
    • PMID: 16698902
    • Sparla F, Costa A, Lo Schiavo F, Pupillo P, Trost P. Redox Regulation of a Novel Plastid-Targeted b- Amylase. Plant Physiol. 2006; 141: 840-850. PMID: 16698902
    • (2006) Plant Physiol , vol.141 , pp. 840-850
    • Sparla, F.1    Costa, A.2    Lo Schiavo, F.3    Pupillo, P.4    Trost, P.5
  • 40
    • 78650636350 scopus 로고    scopus 로고
    • Thioredoxin-regulated betaamylase (BAM1) triggers diurnal starch degradation in guard cells, and in mesophyll cells under osmotic stress
    • PMID: 20876336
    • Valerio C, Costa A, Marri L, Issakidis-Bourguet E, Pupillo P, Trost P, et al. Thioredoxin-regulated betaamylase (BAM1) triggers diurnal starch degradation in guard cells, and in mesophyll cells under osmotic stress. J Exp Bot. 2011; 62: 545-55. doi: 10.1093/jxb/erq288 PMID: 20876336
    • (2011) J Exp Bot , vol.62 , pp. 545-555
    • Valerio, C.1    Costa, A.2    Marri, L.3    Issakidis-Bourguet, E.4    Pupillo, P.5    Trost, P.6
  • 41
    • 84888386468 scopus 로고    scopus 로고
    • Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic α-amylase
    • PMID: 24089528
    • Seung D, Thalmann M, Sparla F, Abou Hachem M, Lee SK, Issakidis-Bourguet E, et al. Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic α-amylase. J Biol Chem. 2013; 288: 33620-33. doi: 10.1074/jbc.M113.514794 PMID: 24089528
    • (2013) J Biol Chem , vol.288 , pp. 33620-33633
    • Seung, D.1    Thalmann, M.2    Sparla, F.3    Abou Hachem, M.4    Lee, S.K.5    Issakidis-Bourguet, E.6
  • 42
  • 43
    • 65249135989 scopus 로고    scopus 로고
    • Prompt and easy activation by specific thioredoxins of calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex
    • PMID: 19825612
    • Marri L, Zaffagnini M, Collin V, Issakidis-Bourguet E, Lemaire SD, Pupillo P, et al. Prompt and easy activation by specific thioredoxins of calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex. Mol Plant. 2009; 2: 259-69. doi: 10.1093/mp/ssn061 PMID: 19825612
    • (2009) Mol Plant , vol.2 , pp. 259-269
    • Marri, L.1    Zaffagnini, M.2    Collin, V.3    Issakidis-Bourguet, E.4    Lemaire, S.D.5    Pupillo, P.6
  • 44
    • 20044391613 scopus 로고    scopus 로고
    • Chloroplasts as source and target of cellular redox regulation: A discussion on chloroplast redox signals in the context of plant physiology
    • PMID: 15863449
    • Baier M, Dietz K-J. Chloroplasts as source and target of cellular redox regulation: a discussion on chloroplast redox signals in the context of plant physiology. J Exp Bot. 2005; 56: 1449-62. doi: 10.1093/jxb/ eri161 PMID: 15863449
    • (2005) J Exp Bot , vol.56 , pp. 1449-1462
    • Baier, M.1    Dietz, K.-J.2
  • 45
    • 48949104251 scopus 로고    scopus 로고
    • The integration of glutathione homeostasis and redox signaling
    • PMID: 18171593
    • Meyer AJ. The integration of glutathione homeostasis and redox signaling. J Plant Physiol. 2008; 165: 1390-403. doi: 10.1016/j.jplph.2007.10.015 PMID: 18171593
    • (2008) J Plant Physiol , vol.165 , pp. 1390-1403
    • Meyer, A.J.1
  • 46
    • 84879161353 scopus 로고    scopus 로고
    • The roles of conditional disorder in redox proteins
    • Elsevier Ltd;
    • Reichmann D, Jakob U. The roles of conditional disorder in redox proteins. Curr Opin Struct Biol. Elsevier Ltd; 2013; 23: 436-42. doi: 10.1016/j.sbi.2013.02.006
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 436-442
    • Reichmann, D.1    Jakob, U.2
  • 47
    • 84885438749 scopus 로고    scopus 로고
    • Oxidative Protein-Folding Systems in Plant Cells
    • Onda Y. Oxidative Protein-Folding Systems in Plant Cells. Int J Cell Biol. 2013; 2013. doi: 10.1155/ 2013/585431
    • (2013) Int J Cell Biol , vol.2013
    • Onda, Y.1
  • 48
    • 0033861403 scopus 로고    scopus 로고
    • Relationship between the occurrence of cysteine in proteins and the complexity of organisms
    • PMID: 10908643
    • Miseta A, Csutora P. Relationship between the occurrence of cysteine in proteins and the complexity of organisms. Mol Biol Evol. 2000; 17: 1232-9. PMID: 10908643
    • (2000) Mol Biol Evol , vol.17 , pp. 1232-1239
    • Miseta, A.1    Csutora, P.2
  • 50
    • 84927950117 scopus 로고    scopus 로고
    • New insights into redox control of starch degradation
    • Elsevier Ltd;
    • Santelia D, Trost P, Sparla F. New insights into redox control of starch degradation. Curr Opin Plant Biol. Elsevier Ltd; 2015; 25: 1-9. doi: 10.1016/j.pbi.2015.04.003
    • (2015) Curr Opin Plant Biol , vol.25 , pp. 1-9
    • Santelia, D.1    Trost, P.2    Sparla, F.3
  • 51
    • 84896859048 scopus 로고    scopus 로고
    • Overexpression of chloroplast NADPH-dependent thioredoxin reductase in Arabidopsis enhances leaf growth and elucidates in vivo function of reductase and thioredoxin domains
    • PMID: 24115951
    • Toivola J, Nikkanen L, Dahlström KM, Salminen T a, Lepistö A, Vignols HF, et al. Overexpression of chloroplast NADPH-dependent thioredoxin reductase in Arabidopsis enhances leaf growth and elucidates in vivo function of reductase and thioredoxin domains. Front Plant Sci. 2013; 4: 389. doi: 10. 3389/fpls.2013.00389 PMID: 24115951
    • (2013) Front Plant Sci , vol.4 , pp. 389
    • Toivola, J.1    Nikkanen, L.2    Dahlström, K.M.3    Salminen, T.A.4    Lepistö, A.5    Vignols, H.F.6
  • 52
    • 33745530598 scopus 로고    scopus 로고
    • Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana
    • PMID: 16551270
    • Lunn JE, Feil R, Hendriks JHM, Gibon Y, Morcuende R, Osuna D, et al. Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana. Biochem J. 2006; 397: 139-48. doi: 10.1042/ BJ20060083 PMID: 16551270
    • (2006) Biochem J. , vol.397 , pp. 139-148
    • Lunn, J.E.1    Feil, R.2    Hendriks, J.H.M.3    Gibon, Y.4    Morcuende, R.5    Osuna, D.6
  • 53
    • 74549127543 scopus 로고    scopus 로고
    • Dynamics of starch granule biogenesis-the role of redox-regulated enzymes and low-affinity carbohydrate-binding modules
    • Blennow A, Svensson B. Dynamics of starch granule biogenesis-the role of redox-regulated enzymes and low-affinity carbohydrate-binding modules. Biocatal Biotransformation. 2010; 28: 3-9. doi: 10. 3109/10242420903408211
    • (2010) Biocatal Biotransformation , vol.28 , pp. 3-9
    • Blennow, A.1    Svensson, B.2
  • 55
    • 0032935861 scopus 로고    scopus 로고
    • Chloro P a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • PMID: 10338008
    • Emanuelsson O, Nielsen H, von Heijne G. Chloro P, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 1999; 8: 978-84. doi: 10.1110/ps.8.5.978 PMID: 10338008
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 56
    • 0029175398 scopus 로고
    • Measurement of equilibrium midpoint potentials of thiol/disulfide regulatory groups on thioredoxin-activated chloroplast enzymes
    • PMID: 7476356
    • Hutchison RS, Ort DR. Measurement of equilibrium midpoint potentials of thiol/disulfide regulatory groups on thioredoxin-activated chloroplast enzymes. Methods Enzymol. 1995; 252: 220-8. PMID: 7476356
    • (1995) Methods Enzymol , vol.252 , pp. 220-228
    • Hutchison, R.S.1    Ort, D.R.2
  • 57
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • PMID: 2204424
    • Brandts JF, Lin LN. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry. 1990; 29: 6927-40. PMID: 2204424
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2


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