메뉴 건너뛰기




Volumn 72, Issue 3, 2012, Pages 378-389

An intermolecular disulfide-based light switch for chloroplast psbD gene expression in Chlamydomonas reinhardtii

Author keywords

Chlamydomonas; chloroplast gene expression; Nac2; redox control; ribonucleoprotein particle

Indexed keywords

ALGAL CELLS; CARBON METABOLISM; CHLAMYDOMONAS; CHLAMYDOMONAS REINHARDTII; COVALENT LINK; GREEN ALGA; HIGH MOLECULAR WEIGHT; INTERMOLECULAR DISULFIDE BRIDGES; LIGHT CONTROL; LIGHT SWITCHES; MOLECULAR BASIS; NAC2; ON DYNAMICS; PHOTOSYSTEM II; REACTION CENTER; RIBONUCLEOPROTEINS; SDS-PAGE; STABILIZATION FACTORS; THIOREDOXIN REDUCTASE;

EID: 84868214112     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2012.05083.x     Document Type: Article
Times cited : (26)

References (55)
  • 1
    • 33646231034 scopus 로고    scopus 로고
    • The chloroplast protein disulfide isomerase RB60 reacts with a regulatory disulfide of the RNA-binding protein RB47
    • Alergand, T., Peled-Zehavi, H., Katz, Y., and, Danon, A., (2006) The chloroplast protein disulfide isomerase RB60 reacts with a regulatory disulfide of the RNA-binding protein RB47. Plant Cell Physiol. 47, 540-548.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 540-548
    • Alergand, T.1    Peled-Zehavi, H.2    Katz, Y.3    Danon, A.4
  • 3
    • 79953711431 scopus 로고    scopus 로고
    • Expression of plastid genes: Organelle-specific elaborations on a prokaryotic scaffold
    • Barkan, A., (2011) Expression of plastid genes: organelle-specific elaborations on a prokaryotic scaffold. Plant Physiol. 155, 1520-1532.
    • (2011) Plant Physiol. , vol.155 , pp. 1520-1532
    • Barkan, A.1
  • 4
    • 33845687519 scopus 로고    scopus 로고
    • ATAB 2 is a novel factor in the signalling pathway of light-controlled synthesis of photosystem proteins
    • Barneche, F., Winter, V., Crevecoeur, M., and, Rochaix, J.D., (2006) ATAB 2 is a novel factor in the signalling pathway of light-controlled synthesis of photosystem proteins. EMBO J. 25, 5907-5918.
    • (2006) EMBO J. , vol.25 , pp. 5907-5918
    • Barneche, F.1    Winter, V.2    Crevecoeur, M.3    Rochaix, J.D.4
  • 5
    • 0037298277 scopus 로고    scopus 로고
    • Redox control of posttranscriptional processes in the chloroplast
    • Barnes, D., and, Mayfield, S.P., (2003) Redox control of posttranscriptional processes in the chloroplast. Antioxid. Redox Signal. 5, 89-94.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 89-94
    • Barnes, D.1    Mayfield, S.P.2
  • 6
    • 3142655271 scopus 로고    scopus 로고
    • Identification and characterization of a novel RNA binding protein that associates with the 5'-untranslated region of the chloroplast psbA mRNA
    • Barnes, D., Cohen, A., Bruick, R.K., Kantardjieff, K., Fowler, S., Efuet, E., and, Mayfield, S.P., (2004) Identification and characterization of a novel RNA binding protein that associates with the 5'-untranslated region of the chloroplast psbA mRNA. Biochemistry, 43, 8541-8550.
    • (2004) Biochemistry , vol.43 , pp. 8541-8550
    • Barnes, D.1    Cohen, A.2    Bruick, R.K.3    Kantardjieff, K.4    Fowler, S.5    Efuet, E.6    Mayfield, S.P.7
  • 9
    • 0034601028 scopus 로고    scopus 로고
    • The Nac2 gene of Chlamydomonas encodes a chloroplast TPR-like protein involved in psbD mRNA stability
    • Boudreau, E., Nickelsen, J., Lemaire, S.D., Ossenbühl, F., and, Rochaix, J.-D., (2000) The Nac2 gene of Chlamydomonas encodes a chloroplast TPR-like protein involved in psbD mRNA stability. EMBO J. 19, 3366-3376.
    • (2000) EMBO J. , vol.19 , pp. 3366-3376
    • Boudreau, E.1    Nickelsen, J.2    Lemaire, S.D.3    Ossenbühl, F.4    Rochaix, J.-D.5
  • 10
    • 31344461715 scopus 로고    scopus 로고
    • Structure, circadian regulation and bioinformatic analysis of the unique sigma factor gene in Chlamydomonas reinhardtii
    • Carter, M.L., Smith, A.C., Kobayashi, H., Purton, S., and, Herrin, D.L., (2004) Structure, circadian regulation and bioinformatic analysis of the unique sigma factor gene in Chlamydomonas reinhardtii. Photosynth. Res. 82, 339-349.
    • (2004) Photosynth. Res. , vol.82 , pp. 339-349
    • Carter, M.L.1    Smith, A.C.2    Kobayashi, H.3    Purton, S.4    Herrin, D.L.5
  • 11
    • 19044379043 scopus 로고    scopus 로고
    • A proposed mechanism for the inhibitory effects of oxidative stress on Rubisco assembly and its subunit expression
    • Cohen, I., Knopf, J.A., Irihimovitch, V., and, Shapira, M., (2005) A proposed mechanism for the inhibitory effects of oxidative stress on Rubisco assembly and its subunit expression. Plant Physiol. 137, 738-746.
    • (2005) Plant Physiol. , vol.137 , pp. 738-746
    • Cohen, I.1    Knopf, J.A.2    Irihimovitch, V.3    Shapira, M.4
  • 12
    • 79953709713 scopus 로고    scopus 로고
    • Novel regulators in photosynthetic redox control of plant metabolism and gene expression
    • Dietz, K.-J., and, Pfannschmidt, T., (2011) Novel regulators in photosynthetic redox control of plant metabolism and gene expression. Plant Physiol. 155, 1477-1485.
    • (2011) Plant Physiol. , vol.155 , pp. 1477-1485
    • Dietz, K.-J.1    Pfannschmidt, T.2
  • 13
    • 0036324267 scopus 로고    scopus 로고
    • Searching limiting steps in the expression of chloroplast-encoded proteins: Relations between gene copy number, transcription, transcript abundance and translation rate in the chloroplast of Chlamydomonas reinhardtii
    • Eberhard, S., Drapier, D., and, Wollman, F.-A., (2002) Searching limiting steps in the expression of chloroplast-encoded proteins: relations between gene copy number, transcription, transcript abundance and translation rate in the chloroplast of Chlamydomonas reinhardtii. Plant J. 31, 149-160.
    • (2002) Plant J. , vol.31 , pp. 149-160
    • Eberhard, S.1    Drapier, D.2    Wollman, F.-A.3
  • 14
    • 0024745101 scopus 로고
    • Blue light regulates the accumulation of two psbD-psbC transcripts in barley chloroplasts
    • Gamble, P.E., and, Mullet, J.E., (1989) Blue light regulates the accumulation of two psbD-psbC transcripts in barley chloroplasts. EMBO J. 8, 2785-2794.
    • (1989) EMBO J. , vol.8 , pp. 2785-2794
    • Gamble, P.E.1    Mullet, J.E.2
  • 15
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii
    • Gorman, D.S., and, Levine, R.P., (1965) Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc. Natl Acad. Sci. USA, 54, 1665-1669.
    • (1965) Proc. Natl Acad. Sci. USA , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 16
    • 29644434820 scopus 로고    scopus 로고
    • Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate
    • Hu, T., Prabhakaran, M., Acharya, S.A., and, Manjula, B.N., (2005) Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate. Biochem. J. 392, 555-564.
    • (2005) Biochem. J. , vol.392 , pp. 555-564
    • Hu, T.1    Prabhakaran, M.2    Acharya, S.A.3    Manjula, B.N.4
  • 17
    • 0034717170 scopus 로고    scopus 로고
    • Glutathione redox potential modulated by reactive oxygen species regulates translation of rubisco large subunit in the chloroplast
    • Irihimovitch, V., and, Shapira, M., (2000) Glutathione redox potential modulated by reactive oxygen species regulates translation of rubisco large subunit in the chloroplast. J. Biol. Chem. 275, 16289-16295.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16289-16295
    • Irihimovitch, V.1    Shapira, M.2
  • 19
    • 84856487868 scopus 로고    scopus 로고
    • Lumen thiol oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis
    • Karamoko, M., Cline, S., Redding, K., Ruiz, N., and, Hamel, P.P., (2011) Lumen thiol oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis. Plant Cell, 23, 4462-4475.
    • (2011) Plant Cell , vol.23 , pp. 4462-4475
    • Karamoko, M.1    Cline, S.2    Redding, K.3    Ruiz, N.4    Hamel, P.P.5
  • 20
    • 0036809427 scopus 로고    scopus 로고
    • The active site of the thioredoxin-like domain of chloroplast protein disulfide isomerase, RB60, catalyzes the redox-regulated binding of chloroplast poly(A)-binding protein, RB47, to the 5' untranslated region of psbA mRNA
    • Kim, J., and, Mayfield, S.P., (2002) The active site of the thioredoxin-like domain of chloroplast protein disulfide isomerase, RB60, catalyzes the redox-regulated binding of chloroplast poly(A)-binding protein, RB47, to the 5' untranslated region of psbA mRNA. Plant Cell Physiol. 43, 1238-1243.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1238-1243
    • Kim, J.1    Mayfield, S.P.2
  • 21
    • 65249089101 scopus 로고    scopus 로고
    • NADPH thioredoxin reductase C controls the redox status of chloroplast 2-Cys peroxiredoxins in Arabidopsis thaliana
    • Kirchsteiger, K., Pulido, P., González, M., and, Cejudo, F.J., (2009) NADPH thioredoxin reductase C controls the redox status of chloroplast 2-Cys peroxiredoxins in Arabidopsis thaliana. Mol. Plant, 2, 298-307.
    • (2009) Mol. Plant , vol.2 , pp. 298-307
    • Kirchsteiger, K.1    Pulido, P.2    González, M.3    Cejudo, F.J.4
  • 22
    • 31544482201 scopus 로고    scopus 로고
    • Translation of chloroplast psbD mRNA in Chlamydomonas is controlled by a secondary RNA structure blocking the AUG start codon
    • Klinkert, B., Elles, I., and, Nickelsen, J., (2006) Translation of chloroplast psbD mRNA in Chlamydomonas is controlled by a secondary RNA structure blocking the AUG start codon. Nucleic Acids Res. 34, 386-394.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 386-394
    • Klinkert, B.1    Elles, I.2    Nickelsen, J.3
  • 24
    • 79957868780 scopus 로고    scopus 로고
    • Function of plastid sigma factors in higher plants: Regulation of gene expression or just preservation of constitutive transcription?
    • Lerbs-Mache, S., (2011) Function of plastid sigma factors in higher plants: regulation of gene expression or just preservation of constitutive transcription? Plant Mol. Biol. 76, 235-249.
    • (2011) Plant Mol. Biol. , vol.76 , pp. 235-249
    • Lerbs-Mache, S.1
  • 25
    • 0023840317 scopus 로고
    • Comparative analysis of the biogenesis of photosystem II in the wild-type and Y-1 mutant of Chlamydomonas reinhardtii
    • Malnoe, P., Mayfield, S.P., and, Rochaix, J.D., (1988) Comparative analysis of the biogenesis of photosystem II in the wild-type and Y-1 mutant of Chlamydomonas reinhardtii. J. Cell Biol. 106, 609-616.
    • (1988) J. Cell Biol. , vol.106 , pp. 609-616
    • Malnoe, P.1    Mayfield, S.P.2    Rochaix, J.D.3
  • 27
    • 80053331274 scopus 로고    scopus 로고
    • Covalent conjugation of poly(ethylene glycol) to proteins and peptides: Strategies and methods
    • (Mark, S.S. ed.). Totowa: Humana Press
    • Mero, A., Clementi, C., Veronese, F.M., and, Pasut, G., (2011) Covalent conjugation of poly(ethylene glycol) to proteins and peptides: strategies and methods. In Bioconjugation Protocols (, Mark, S.S., ed.). Totowa: Humana Press, pp. 95-129.
    • (2011) Bioconjugation Protocols , pp. 95-129
    • Mero, A.1    Clementi, C.2    Veronese, F.M.3    Pasut, G.4
  • 28
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., and, Herrmann, J.M., (2005) A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell, 121, 1059-1069.
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 29
    • 67649880593 scopus 로고    scopus 로고
    • NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts
    • Michalska, J., Zauber, H., Buchanan, B.B., Cejudo, F.J., and, Geigenberger, P., (2009) NTRC links built-in thioredoxin to light and sucrose in regulating starch synthesis in chloroplasts and amyloplasts. Proc. Natl Acad. Sci. USA, 106, 9908-9913.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 9908-9913
    • Michalska, J.1    Zauber, H.2    Buchanan, B.B.3    Cejudo, F.J.4    Geigenberger, P.5
  • 31
    • 33645728659 scopus 로고    scopus 로고
    • Chloroplast biogenesis of photosystem II cores involves a series of assembly-controlled steps that regulate translation
    • Minai, L., Wostrikoff, K., Wollman, F.-A., and, Choquet, Y., (2006) Chloroplast biogenesis of photosystem II cores involves a series of assembly-controlled steps that regulate translation. Plant Cell, 18, 159-175.
    • (2006) Plant Cell , vol.18 , pp. 159-175
    • Minai, L.1    Wostrikoff, K.2    Wollman, F.-A.3    Choquet, Y.4
  • 32
    • 33644828133 scopus 로고    scopus 로고
    • NAB1 is an RNA binding protein involved in the light-regulated differential expression of the light-harvesting antenna of Chlamydomonas reinhardtii
    • Mussgnug, J.H., Wobbe, L., Elles, I., et al. (2005) NAB1 is an RNA binding protein involved in the light-regulated differential expression of the light-harvesting antenna of Chlamydomonas reinhardtii. Plant Cell, 17, 3409-3421.
    • (2005) Plant Cell , vol.17 , pp. 3409-3421
    • Mussgnug, J.H.1    Wobbe, L.2    Elles, I.3
  • 34
    • 0033133576 scopus 로고    scopus 로고
    • Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas
    • Nickelsen, J., Fleischmann, M., Boudreau, E., Rahire, M., and, Rochaix, J.D., (1999) Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas. Plant Cell, 11, 957-970.
    • (1999) Plant Cell , vol.11 , pp. 957-970
    • Nickelsen, J.1    Fleischmann, M.2    Boudreau, E.3    Rahire, M.4    Rochaix, J.D.5
  • 35
    • 79955422174 scopus 로고    scopus 로고
    • S-Adenosyl-l-methionine induces compaction of nascent peptide chain inside the ribosomal exit tunnel upon translation arrest in the Arabidopsis CGS1 gene
    • Onoue, N., Yamashita, Y., Nagao, N., Goto, D.B., Onouchi, H., and, Naito, S., (2011) S-Adenosyl-l-methionine induces compaction of nascent peptide chain inside the ribosomal exit tunnel upon translation arrest in the Arabidopsis CGS1 gene. J. Biol. Chem. 286, 14903-14912.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14903-14912
    • Onoue, N.1    Yamashita, Y.2    Nagao, N.3    Goto, D.B.4    Onouchi, H.5    Naito, S.6
  • 36
    • 0033776506 scopus 로고    scopus 로고
    • Cis- and trans-acting determinants for translation of psbD mRNA in Chlamydomonas reinhardtii
    • Ossenbühl, F., and, Nickelsen, J., (2000) Cis- and trans-acting determinants for translation of psbD mRNA in Chlamydomonas reinhardtii. Mol. Cell. Biol. 20, 8134-8142.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8134-8142
    • Ossenbühl, F.1    Nickelsen, J.2
  • 37
    • 79953684285 scopus 로고    scopus 로고
    • A comparative analysis of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system from plants and cyanobacteria
    • Pascual, M.B., Mata-Cabana, A., Florencio, F.J., Lindahl, M., and, Cejudo, F.J., (2011) A comparative analysis of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system from plants and cyanobacteria. Plant Physiol. 155, 1806-1816.
    • (2011) Plant Physiol. , vol.155 , pp. 1806-1816
    • Pascual, M.B.1    Mata-Cabana, A.2    Florencio, F.J.3    Lindahl, M.4    Cejudo, F.J.5
  • 38
    • 33749233825 scopus 로고    scopus 로고
    • Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage
    • Pérez-Ruiz, J.M., Spínola, M.C., Kirchsteiger, K., Moreno, J., Sahrawy, M., and, Cejudo, F.J., (2006) Rice NTRC is a high-efficiency redox system for chloroplast protection against oxidative damage. Plant Cell, 18, 2356-2368.
    • (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
  • 39
    • 84868193881 scopus 로고    scopus 로고
    • Enrichment of native, high molecular weight ribonucleoprotein complexes from chloroplasts by consecutive gel filtration steps
    • Schwarz, C., and, Nickelsen, J., (2010) Enrichment of native, high molecular weight ribonucleoprotein complexes from chloroplasts by consecutive gel filtration steps. Endocytobiosis Cell Res. 20, 89-94.
    • (2010) Endocytobiosis Cell Res. , vol.20 , pp. 89-94
    • Schwarz, C.1    Nickelsen, J.2
  • 40
    • 37849006499 scopus 로고    scopus 로고
    • Synthesis of the D2 protein of photosystem II in Chlamydomonas is controlled by a high molecular mass complex containing the RNA stabilization factor Nac2 and the translational activator RBP40
    • Schwarz, C., Elles, I., Kortmann, J., Piotrowski, M., and, Nickelsen, J., (2007) Synthesis of the D2 protein of photosystem II in Chlamydomonas is controlled by a high molecular mass complex containing the RNA stabilization factor Nac2 and the translational activator RBP40. Plant Cell, 19, 3627-3639.
    • (2007) Plant Cell , vol.19 , pp. 3627-3639
    • Schwarz, C.1    Elles, I.2    Kortmann, J.3    Piotrowski, M.4    Nickelsen, J.5
  • 41
    • 79851508389 scopus 로고    scopus 로고
    • Protein import into chloroplasts - How chaperones feature into the game
    • Schwenkert, S., Soll, J., and, Bölter, B., (2011) Protein import into chloroplasts-how chaperones feature into the game. Biochim. Biophys. Acta, 1808, 901-911.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 901-911
    • Schwenkert, S.1    Soll, J.2    Bölter, B.3
  • 42
    • 6344235622 scopus 로고    scopus 로고
    • A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana
    • Serrato, A.J., Pérez-Ruiz, J.M., Spínola, M.C., and, Cejudo, F.J., (2004) A novel NADPH thioredoxin reductase, localized in the chloroplast, which deficiency causes hypersensitivity to abiotic stress in Arabidopsis thaliana. J. Biol. Chem. 279, 43821-43827.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43821-43827
    • Serrato, A.J.1    Pérez-Ruiz, J.M.2    Spínola, M.C.3    Cejudo, F.J.4
  • 43
    • 33745861722 scopus 로고    scopus 로고
    • Conservation and diversity of the cellular disulfide bond formation pathways
    • Sevier, C.S., and, Kaiser, C.A., (2006) Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid. Redox Signal. 8, 797-811.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 797-811
    • Sevier, C.S.1    Kaiser, C.A.2
  • 44
    • 71249151181 scopus 로고    scopus 로고
    • Preprotein import into chloroplasts via the Toc and Tic complexes is regulated by redox signals in Pisum sativum
    • Stengel, A., Benz, J.P., Buchanan, B.B., Soll, J., and, Bölter, B., (2009) Preprotein import into chloroplasts via the Toc and Tic complexes is regulated by redox signals in Pisum sativum. Mol. Plant, 2, 1181-1197.
    • (2009) Mol. Plant , vol.2 , pp. 1181-1197
    • Stengel, A.1    Benz, J.P.2    Buchanan, B.B.3    Soll, J.4    Bölter, B.5
  • 45
    • 45249097787 scopus 로고    scopus 로고
    • The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility
    • Ströher, E., and, Dietz, K.-J., (2008) The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. Physiol. Plant. 133, 566-583.
    • (2008) Physiol. Plant. , vol.133 , pp. 566-583
    • Ströher, E.1    Dietz, K.-J.2
  • 46
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebitsh, T., Levitan, A., Sofer, A., and, Danon, A., (2000) Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities. Mol. Cell. Biol. 20, 1116-1123.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1116-1123
    • Trebitsh, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 47
    • 65649127785 scopus 로고    scopus 로고
    • Pegylated derivatives of recombinant human arginase (rhArg1) for sustained in vivo activity in cancer therapy: Preparation, characterization and analysis of their pharmacodynamics in vivo and in vitro and action upon hepatocellular carcinoma cell (HCC)
    • Tsui, S.-M., Lam, W.-M., Lam, T.-L., et al. (2009) Pegylated derivatives of recombinant human arginase (rhArg1) for sustained in vivo activity in cancer therapy: preparation, characterization and analysis of their pharmacodynamics in vivo and in vitro and action upon hepatocellular carcinoma cell (HCC). Cancer Cell Int. 9, 9.
    • (2009) Cancer Cell Int. , vol.9 , pp. 9
    • Tsui, S.-M.1    Lam, W.-M.2    Lam, T.-L.3
  • 48
    • 0034029659 scopus 로고    scopus 로고
    • Stability determinants in the chloroplast psbB/T/H mRNAs of Chlamydomonas reinhardtii
    • Vaistij, F.E., Goldschmidt-Clermont, M., Wostrikoff, K., and, Rochaix, J.D., (2000) Stability determinants in the chloroplast psbB/T/H mRNAs of Chlamydomonas reinhardtii. Plant J. 21, 469-482.
    • (2000) Plant J. , vol.21 , pp. 469-482
    • Vaistij, F.E.1    Goldschmidt-Clermont, M.2    Wostrikoff, K.3    Rochaix, J.D.4
  • 49
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • Veronese, F.M., (2001) Peptide and protein PEGylation: a review of problems and solutions. Biomaterials, 22, 405-417.
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 50
    • 49349107642 scopus 로고    scopus 로고
    • Disulfide bond formation in chloroplasts: Formation of disulfide bonds in signaling chloroplast proteins
    • Wittenberg, G., and, Danon, A., (2008) Disulfide bond formation in chloroplasts: formation of disulfide bonds in signaling chloroplast proteins. Plant Sci. 175, 459-466.
    • (2008) Plant Sci. , vol.175 , pp. 459-466
    • Wittenberg, G.1    Danon, A.2
  • 51
    • 69449090357 scopus 로고    scopus 로고
    • Cysteine modification of a specific repressor protein controls the translational status of nucleus-encoded LHCII mRNAs in Chlamydomonas
    • Wobbe, L., Blifernez, O., Schwarz, C., Mussgnug, J.H., Nickelsen, J., and, Kruse, O., (2009) Cysteine modification of a specific repressor protein controls the translational status of nucleus-encoded LHCII mRNAs in Chlamydomonas. Proc. Natl Acad. Sci. USA, 106, 13290-13295.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13290-13295
    • Wobbe, L.1    Blifernez, O.2    Schwarz, C.3    Mussgnug, J.H.4    Nickelsen, J.5    Kruse, O.6
  • 52
    • 33745877260 scopus 로고    scopus 로고
    • Development of tumor targeting anti-MUC-1 multimer: Effects of di-scFv unpaired cysteine location on PEGylation and tumor binding
    • Xiong, C.-Y., Natarajan, A., Shi, X.-B., Denardo, G.L., and, Denardo, S.J., (2006) Development of tumor targeting anti-MUC-1 multimer: effects of di-scFv unpaired cysteine location on PEGylation and tumor binding. Protein Eng. Des. Sel. 19, 359-367.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 359-367
    • Xiong, C.-Y.1    Natarajan, A.2    Shi, X.-B.3    Denardo, G.L.4    Denardo, S.J.5
  • 53
    • 1642313885 scopus 로고    scopus 로고
    • RNA binding activity of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit from Chlamydomonas reinhardtii
    • Yosef, I., Irihimovitch, V., Knopf, J.A., Cohen, I., Orr-Dahan, I., Nahum, E., Keasar, C., and, Shapira, M., (2004) RNA binding activity of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit from Chlamydomonas reinhardtii. J. Biol. Chem. 279, 10148-10156.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10148-10156
    • Yosef, I.1    Irihimovitch, V.2    Knopf, J.A.3    Cohen, I.4    Orr-Dahan, I.5    Nahum, E.6    Keasar, C.7    Shapira, M.8
  • 55
    • 0031953257 scopus 로고    scopus 로고
    • Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii
    • Zerges, W., and, Rochaix, J.D., (1998) Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii. J. Cell Biol. 140, 101-110.
    • (1998) J. Cell Biol. , vol.140 , pp. 101-110
    • Zerges, W.1    Rochaix, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.