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Volumn 65, Issue , 2013, Pages 157-188

Genomics of the Pleïotropic Glutathione System in Cyanobacteria

Author keywords

Formaldehyde; Glutaredoxins; Glutathione; Glyoxalases; Iron sulphur cluster; Methylglyoxal; Oxidative stress

Indexed keywords


EID: 84871675776     PISSN: 00652296     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394313-2.00005-6     Document Type: Chapter
Times cited : (27)

References (102)
  • 3
    • 58349101981 scopus 로고    scopus 로고
    • The puzzle of plastid evolution
    • Archibald J.M. The puzzle of plastid evolution. Current Biology: CB 2009, 19:R81-R88.
    • (2009) Current Biology: CB , vol.19
    • Archibald, J.M.1
  • 4
    • 18444416836 scopus 로고    scopus 로고
    • Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120
    • Ashida H., Sawa Y., Shibata H. Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant & Cell Physiology 2005, 46:557-562.
    • (2005) Plant & Cell Physiology , vol.46 , pp. 557-562
    • Ashida, H.1    Sawa, Y.2    Shibata, H.3
  • 5
    • 78149364258 scopus 로고    scopus 로고
    • Dynamic changes in the proteome of Synechocystis 6803 in response to CO(2) limitation revealed by quantitative proteomics
    • Battchikova N., Vainonen J.P., Vorontsova N., Keranen M., Carmel D., Aro E.M. Dynamic changes in the proteome of Synechocystis 6803 in response to CO(2) limitation revealed by quantitative proteomics. Journal of Proteome Research 2010, 9:5896-5912.
    • (2010) Journal of Proteome Research , vol.9 , pp. 5896-5912
    • Battchikova, N.1    Vainonen, J.P.2    Vorontsova, N.3    Keranen, M.4    Carmel, D.5    Aro, E.M.6
  • 6
    • 80052528579 scopus 로고    scopus 로고
    • The danger of annotation by analogy: most "thiI" genes play no role in thiamine biosynthesis
    • Bender R.A. The danger of annotation by analogy: most "thiI" genes play no role in thiamine biosynthesis. Journal of Bacteriology 2011, 193:4574-4575.
    • (2011) Journal of Bacteriology , vol.193 , pp. 4574-4575
    • Bender, R.A.1
  • 7
    • 84871676951 scopus 로고    scopus 로고
    • Up-regulation of plasmid-encoded genes during stationary phase in Synechocystis sp. PCC 6803, a cyanobacterium
    • Beria B.M., Pakrasi H.B. Up-regulation of plasmid-encoded genes during stationary phase in Synechocystis sp. PCC 6803, a cyanobacterium. Applied and Environmental Microbiology 2012.
    • (2012) Applied and Environmental Microbiology
    • Beria, B.M.1    Pakrasi, H.B.2
  • 8
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt C., Lillig C.H., Holmgren A. Thioredoxins and glutaredoxins as facilitators of protein folding. Biochimica et Biophysica Acta 2008, 1783:641-650.
    • (2008) Biochimica et Biophysica Acta , vol.1783 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 9
    • 27344432194 scopus 로고    scopus 로고
    • Phytochelatin plays a role in UV-B tolerance in N2-fixing cyanobacterium Anabaena doliolum
    • Bhargava P., Srivastava A.K., Urmil S., Rai L.C. Phytochelatin plays a role in UV-B tolerance in N2-fixing cyanobacterium Anabaena doliolum. Journal of Plant Physiology 2005, 162:1220-1225.
    • (2005) Journal of Plant Physiology , vol.162 , pp. 1220-1225
    • Bhargava, P.1    Srivastava, A.K.2    Urmil, S.3    Rai, L.C.4
  • 10
    • 78649762173 scopus 로고    scopus 로고
    • Essential role of glutathione in acclimation to environmental and redox perturbations in the cyanobacterium Synechocystis sp. PCC 6803
    • Cameron J.C., Pakrasi H.B. Essential role of glutathione in acclimation to environmental and redox perturbations in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiology 2010, 154:1672-1685.
    • (2010) Plant Physiology , vol.154 , pp. 1672-1685
    • Cameron, J.C.1    Pakrasi, H.B.2
  • 11
    • 79958231364 scopus 로고    scopus 로고
    • Glutathione facilitates antibiotic resistance and photosystem I stability during exposure to gentamicin in cyanobacteria
    • Cameron J.C., Pakrasi H.B. Glutathione facilitates antibiotic resistance and photosystem I stability during exposure to gentamicin in cyanobacteria. Applied and Environmental Microbiology 2011, 77:3547-3550.
    • (2011) Applied and Environmental Microbiology , vol.77 , pp. 3547-3550
    • Cameron, J.C.1    Pakrasi, H.B.2
  • 12
    • 0030878556 scopus 로고    scopus 로고
    • Three insertion sequences from the cyanobacterium Synechocystis PCC6803 support the occurrence of horizontal DNA transfer among bacteria
    • Cassier-Chauvat C., Poncelet M., Chauvat F. Three insertion sequences from the cyanobacterium Synechocystis PCC6803 support the occurrence of horizontal DNA transfer among bacteria. Gene 1997, 195:257-266.
    • (1997) Gene , vol.195 , pp. 257-266
    • Cassier-Chauvat, C.1    Poncelet, M.2    Chauvat, F.3
  • 14
    • 0020655825 scopus 로고
    • Transformation in the cyanobacterium Synechococcus R2: improvement of efficiency; role of the pUH24 plasmid
    • Chauvat F., Astier C., Vedel F., Joset-Espardellier F. Transformation in the cyanobacterium Synechococcus R2: improvement of efficiency; role of the pUH24 plasmid. Molecular and General Genetics 1983, 191:39-45.
    • (1983) Molecular and General Genetics , vol.191 , pp. 39-45
    • Chauvat, F.1    Astier, C.2    Vedel, F.3    Joset-Espardellier, F.4
  • 16
    • 18344418957 scopus 로고    scopus 로고
    • Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes
    • research0025
    • Copley S.D., Dhillon J.K. Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes. Genome Biology 2002, 3. research0025.
    • (2002) Genome Biology , vol.3
    • Copley, S.D.1    Dhillon, J.K.2
  • 19
    • 0033587499 scopus 로고    scopus 로고
    • Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site
    • Danielson U.H., Jiang F., Hansson L.O., Mannervik B. Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site. Biochemistry 1999, 38:9254-9263.
    • (1999) Biochemistry , vol.38 , pp. 9254-9263
    • Danielson, U.H.1    Jiang, F.2    Hansson, L.O.3    Mannervik, B.4
  • 20
    • 82355190258 scopus 로고    scopus 로고
    • Exopolysaccharide-producing cyanobacteria in heavy metal removal from water: molecular basis and practical applicability of the biosorption process
    • De Philippis R., Colica G., Micheletti E. Exopolysaccharide-producing cyanobacteria in heavy metal removal from water: molecular basis and practical applicability of the biosorption process. Applied Microbiology and Biotechnology 2011, 92:697-708.
    • (2011) Applied Microbiology and Biotechnology , vol.92 , pp. 697-708
    • De Philippis, R.1    Colica, G.2    Micheletti, E.3
  • 21
    • 3142559798 scopus 로고    scopus 로고
    • Function and regulation of the cyanobacterial genes lexA, recA and ruvB: LexA is critical to the survival of cells facing inorganic carbon starvation
    • Domain F., Houot L., Chauvat F., Cassier-Chauvat C. Function and regulation of the cyanobacterial genes lexA, recA and ruvB: LexA is critical to the survival of cells facing inorganic carbon starvation. Molecular Microbiology 2004, 53:65-80.
    • (2004) Molecular Microbiology , vol.53 , pp. 65-80
    • Domain, F.1    Houot, L.2    Chauvat, F.3    Cassier-Chauvat, C.4
  • 22
    • 78751638661 scopus 로고    scopus 로고
    • Engineering cyanobacteria to generate high-value products
    • Ducat D.C., Way J.C., Silver P.A. Engineering cyanobacteria to generate high-value products. Trends in Biotechnology 2011, 29:95-103.
    • (2011) Trends in Biotechnology , vol.29 , pp. 95-103
    • Ducat, D.C.1    Way, J.C.2    Silver, P.A.3
  • 23
    • 0035153837 scopus 로고    scopus 로고
    • Characterization and analysis of an NAD(P)H dehydrogenase transcriptional regulator critical for the survival of cyanobacteria facing inorganic carbon starvation and osmotic stress
    • Figge R.M., Cassier-Chauvat C., Chauvat F., Cerff R. Characterization and analysis of an NAD(P)H dehydrogenase transcriptional regulator critical for the survival of cyanobacteria facing inorganic carbon starvation and osmotic stress. Molecular Microbiology 2001, 39:455-468.
    • (2001) Molecular Microbiology , vol.39 , pp. 455-468
    • Figge, R.M.1    Cassier-Chauvat, C.2    Chauvat, F.3    Cerff, R.4
  • 26
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • Forman H.J., Maiorino M., Ursini F. Signaling functions of reactive oxygen species. Biochemistry 2010, 49:835-842.
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 28
    • 33744938480 scopus 로고    scopus 로고
    • Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG
    • Gonzalez C.F., Proudfoot M., Brown G., Korniyenko Y., Mori H., Savchenko A.V., et al. Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG. The Journal of Biological Chemistry 2006, 281:14514-14522.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 14514-14522
    • Gonzalez, C.F.1    Proudfoot, M.2    Brown, G.3    Korniyenko, Y.4    Mori, H.5    Savchenko, A.V.6
  • 30
    • 0020049959 scopus 로고
    • Transformation in the cyanobacterium Synechocystis sp 6803
    • Grigorieva G., Shestakov S. Transformation in the cyanobacterium Synechocystis sp 6803. FEMS Microbiology Letters 1982, 13:367-370.
    • (1982) FEMS Microbiology Letters , vol.13 , pp. 367-370
    • Grigorieva, G.1    Shestakov, S.2
  • 31
    • 78650006123 scopus 로고    scopus 로고
    • Molecular biology of cyanobacterial salt acclimation
    • Hagemann M. Molecular biology of cyanobacterial salt acclimation. FEMS Microbiology Reviews 2011, 35:87-123.
    • (2011) FEMS Microbiology Reviews , vol.35 , pp. 87-123
    • Hagemann, M.1
  • 32
    • 79951741634 scopus 로고    scopus 로고
    • Structural and functional diversity of glutaredoxins in yeast
    • Herrero E., Belli G., Casa C. Structural and functional diversity of glutaredoxins in yeast. Current Protein & Peptide Science 2010, 11:659-668.
    • (2010) Current Protein & Peptide Science , vol.11 , pp. 659-668
    • Herrero, E.1    Belli, G.2    Casa, C.3
  • 33
    • 81155161902 scopus 로고    scopus 로고
    • Cyanobacterial genomics for ecology and biotechnology
    • Hess W.R. Cyanobacterial genomics for ecology and biotechnology. Current Opinion in Microbiology 2011, 14:608-614.
    • (2011) Current Opinion in Microbiology , vol.14 , pp. 608-614
    • Hess, W.R.1
  • 35
    • 38049184229 scopus 로고    scopus 로고
    • Cadmium triggers an integrated reprogramming of the metabolism of Synechocystis PCC6803, under the control of the Slr1738 regulator
    • Houot L., Floutier M., Marteyn B., Michaut M., Picciocchi A., Legrain P., et al. Cadmium triggers an integrated reprogramming of the metabolism of Synechocystis PCC6803, under the control of the Slr1738 regulator. BMC Genomics 2007, 8:350.
    • (2007) BMC Genomics , vol.8 , pp. 350
    • Houot, L.1    Floutier, M.2    Marteyn, B.3    Michaut, M.4    Picciocchi, A.5    Legrain, P.6
  • 36
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay J.A. Cellular defenses against superoxide and hydrogen peroxide. Annual Review of Biochemistry 2008, 77:755-776.
    • (2008) Annual Review of Biochemistry , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 39
    • 77953357030 scopus 로고    scopus 로고
    • Calcifying cyanobacteria-the potential of biomineralization for carbon capture and storage
    • Jansson C., Northen T. Calcifying cyanobacteria-the potential of biomineralization for carbon capture and storage. Current Opinion in Biotechnology 2010, 21:365-371.
    • (2010) Current Opinion in Biotechnology , vol.21 , pp. 365-371
    • Jansson, C.1    Northen, T.2
  • 40
    • 0029092651 scopus 로고
    • Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120
    • Jiang F., Hellman U., Sroga G.E., Bergman B., Mannervik B. Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120. The Journal of Biological Chemistry 1995, 270:22882-22889.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 22882-22889
    • Jiang, F.1    Hellman, U.2    Sroga, G.E.3    Bergman, B.4    Mannervik, B.5
  • 41
    • 0030606608 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions (supplement)
    • Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions (supplement). DNA Research: An International Journal for Rapid Publication of Reports on Genes and Genomes 1996, 3:185-209.
    • (1996) DNA Research: An International Journal for Rapid Publication of Reports on Genes and Genomes , vol.3 , pp. 185-209
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6
  • 42
    • 84455193453 scopus 로고    scopus 로고
    • Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803
    • Kim S.G., Chung J.S., Sutton R.B., Lee J.S., Lopez-Maury L., Lee S.Y., et al. Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803. Biochimica et Biophysica Acta 2012, 1824:392-403.
    • (2012) Biochimica et Biophysica Acta , vol.1824 , pp. 392-403
    • Kim, S.G.1    Chung, J.S.2    Sutton, R.B.3    Lee, J.S.4    Lopez-Maury, L.5    Lee, S.Y.6
  • 43
    • 77955483673 scopus 로고    scopus 로고
    • The photoactive orange carotenoid protein and photoprotection in cyanobacteria
    • Kirilovsky D. The photoactive orange carotenoid protein and photoprotection in cyanobacteria. Advances in Experimental Medicine and Biology 2010, 675:139-159.
    • (2010) Advances in Experimental Medicine and Biology , vol.675 , pp. 139-159
    • Kirilovsky, D.1
  • 44
    • 23644445048 scopus 로고    scopus 로고
    • Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases
    • Ko J., Kim I., Yoo S., Min B., Kim K., Park C. Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases. Journal of Bacteriology 2005, 187:5782-5789.
    • (2005) Journal of Bacteriology , vol.187 , pp. 5782-5789
    • Ko, J.1    Kim, I.2    Yoo, S.3    Min, B.4    Kim, K.5    Park, C.6
  • 45
    • 0024399346 scopus 로고
    • Insertional mutagenesis by random cloning of antibiotic resistance genes into the genome of the cyanobacterium Synechocystis strain PCC 6803
    • Labarre J., Chauvat F., Thuriaux P. Insertional mutagenesis by random cloning of antibiotic resistance genes into the genome of the cyanobacterium Synechocystis strain PCC 6803. Journal of Bacteriology 1989, 171:3449-3457.
    • (1989) Journal of Bacteriology , vol.171 , pp. 3449-3457
    • Labarre, J.1    Chauvat, F.2    Thuriaux, P.3
  • 48
    • 20444389441 scopus 로고    scopus 로고
    • Expression and oxidative stress tolerance studies of glutaredoxin from cyanobacterium Synechocystis sp. PCC 6803 in Escherichia coli
    • Li M., Huang W., Yang Q., Liu X., Wu Q. Expression and oxidative stress tolerance studies of glutaredoxin from cyanobacterium Synechocystis sp. PCC 6803 in Escherichia coli. Protein Expression and Purification 2005, 42:85-91.
    • (2005) Protein Expression and Purification , vol.42 , pp. 85-91
    • Li, M.1    Huang, W.2    Yang, Q.3    Liu, X.4    Wu, Q.5
  • 50
    • 84863229142 scopus 로고    scopus 로고
    • Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2
    • Li H., Mapolelo D.T., Randeniya S., Johnson M.K., Outten C.E. Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2. Biochemistry 2012, 51:1687-1696.
    • (2012) Biochemistry , vol.51 , pp. 1687-1696
    • Li, H.1    Mapolelo, D.T.2    Randeniya, S.3    Johnson, M.K.4    Outten, C.E.5
  • 51
    • 71349087596 scopus 로고    scopus 로고
    • Enhancement of glutathione production with a tripeptidase-deficient recombinant Escherichia coli
    • Lin J., Liao X., Zhang J., Du G., Chen J. Enhancement of glutathione production with a tripeptidase-deficient recombinant Escherichia coli. Journal of Industrial Microbiology & Biotechnology 2009, 36:1447-1452.
    • (2009) Journal of Industrial Microbiology & Biotechnology , vol.36 , pp. 1447-1452
    • Lin, J.1    Liao, X.2    Zhang, J.3    Du, G.4    Chen, J.5
  • 53
    • 0016258975 scopus 로고
    • Control of macromolecular composition and cell division in the blue-green alga Anacystis nidulans
    • Mann N., Carr N.G. Control of macromolecular composition and cell division in the blue-green alga Anacystis nidulans. Journal of General Microbiology 1974, 83:399-405.
    • (1974) Journal of General Microbiology , vol.83 , pp. 399-405
    • Mann, N.1    Carr, N.G.2
  • 54
    • 84856566415 scopus 로고    scopus 로고
    • Analysis of two marine metagenomes reveals the diversity of plasmids in oceanic environments
    • Ma Y., Paulsen I.T., Palenik B. Analysis of two marine metagenomes reveals the diversity of plasmids in oceanic environments. Environmental Microbiology 2012, 14:453-466.
    • (2012) Environmental Microbiology , vol.14 , pp. 453-466
    • Ma, Y.1    Paulsen, I.T.2    Palenik, B.3
  • 55
    • 67749122097 scopus 로고    scopus 로고
    • Characterization of the Synechocystis strain PCC 6803 penicillin-binding proteins and cytokinetic proteins FtsQ and FtsW and their network of interactions with ZipN
    • Marbouty M., Mazouni K., Saguez C., Cassier-Chauvat C., Chauvat F. Characterization of the Synechocystis strain PCC 6803 penicillin-binding proteins and cytokinetic proteins FtsQ and FtsW and their network of interactions with ZipN. Journal of Bacteriology 2009, 191:5123-5133.
    • (2009) Journal of Bacteriology , vol.191 , pp. 5123-5133
    • Marbouty, M.1    Mazouni, K.2    Saguez, C.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 56
    • 70349909319 scopus 로고    scopus 로고
    • ZipN, an FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803
    • Marbouty M., Saguez C., Cassier-Chauvat C., Chauvat F. ZipN, an FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803. Molecular Microbiology 2009, 74:409-420.
    • (2009) Molecular Microbiology , vol.74 , pp. 409-420
    • Marbouty, M.1    Saguez, C.2    Cassier-Chauvat, C.3    Chauvat, F.4
  • 57
    • 77955482969 scopus 로고    scopus 로고
    • Multicellularity in a heterocyst-forming cyanobacterium: pathways for intercellular communication
    • Mariscal V., Flores E. Multicellularity in a heterocyst-forming cyanobacterium: pathways for intercellular communication. Advances in Experimental Medicine and Biology 2010, 675:123-135.
    • (2010) Advances in Experimental Medicine and Biology , vol.675 , pp. 123-135
    • Mariscal, V.1    Flores, E.2
  • 58
    • 58149308104 scopus 로고    scopus 로고
    • The thioredoxin reductase-glutaredoxins-ferredoxin crossroad pathway for selenate tolerance in Synechocystis PCC6803
    • Marteyn B., Domain F., Legrain P., Chauvat F., Cassier-Chauvat C. The thioredoxin reductase-glutaredoxins-ferredoxin crossroad pathway for selenate tolerance in Synechocystis PCC6803. Molecular Microbiology 2009, 71:520-532.
    • (2009) Molecular Microbiology , vol.71 , pp. 520-532
    • Marteyn, B.1    Domain, F.2    Legrain, P.3    Chauvat, F.4    Cassier-Chauvat, C.5
  • 60
    • 0027370605 scopus 로고
    • Transfer and replication of RSF1010-derived plasmids in several cyanobacteria of the genera Synechocystis and Synechococcus
    • Mermet-Bouvier P., Cassier-Chauvat C., Marraccini P., Chauvat F. Transfer and replication of RSF1010-derived plasmids in several cyanobacteria of the genera Synechocystis and Synechococcus. Current Microbiology 1993, 27:323-327.
    • (1993) Current Microbiology , vol.27 , pp. 323-327
    • Mermet-Bouvier, P.1    Cassier-Chauvat, C.2    Marraccini, P.3    Chauvat, F.4
  • 62
    • 70350787143 scopus 로고    scopus 로고
    • Aldo-keto reductase (AKR) superfamily: genomics and annotation
    • Mindnich R.D., Penning T.M. Aldo-keto reductase (AKR) superfamily: genomics and annotation. Human Genomics 2009, 3:362-370.
    • (2009) Human Genomics , vol.3 , pp. 362-370
    • Mindnich, R.D.1    Penning, T.M.2
  • 63
    • 16244387910 scopus 로고    scopus 로고
    • Identification of cyanobacterial cell division genes by comparative and mutational analyses
    • Miyagishima S.Y., Wolk C.P., Osteryoung K.W. Identification of cyanobacterial cell division genes by comparative and mutational analyses. Molecular Microbiology 2005, 56:126-143.
    • (2005) Molecular Microbiology , vol.56 , pp. 126-143
    • Miyagishima, S.Y.1    Wolk, C.P.2    Osteryoung, K.W.3
  • 64
    • 84858445695 scopus 로고    scopus 로고
    • 2+-activated glyoxalase I from Escherichia coli: substrate specificity, kinetic isotope effects and evolution within the betaalphabetabetabeta superfamily
    • 2+-activated glyoxalase I from Escherichia coli: substrate specificity, kinetic isotope effects and evolution within the betaalphabetabetabeta superfamily. Journal of Inorganic Biochemistry 2012, 108:133-140.
    • (2012) Journal of Inorganic Biochemistry , vol.108 , pp. 133-140
    • Mullings, K.Y.1    Sukdeo, N.2    Suttisansanee, U.3    Ran, Y.4    Honek, J.F.5
  • 65
    • 84872652184 scopus 로고    scopus 로고
    • High performance analysis of the cyanobacterial metabolism via liquid chromatography coupled to a LTQ-Orbitrap mass spectrometer: evidence that glucose reprograms the whole carbon metabolism and triggers oxidative stress
    • Narainsamy K., Cassier-Chauvat C., Junot C., Chauvat F. High performance analysis of the cyanobacterial metabolism via liquid chromatography coupled to a LTQ-Orbitrap mass spectrometer: evidence that glucose reprograms the whole carbon metabolism and triggers oxidative stress. Metabolomics 2011.
    • (2011) Metabolomics
    • Narainsamy, K.1    Cassier-Chauvat, C.2    Junot, C.3    Chauvat, F.4
  • 66
    • 0030875378 scopus 로고    scopus 로고
    • The gshB gene in the cyanobacterium Synechococcus sp. PCC 7942 encodes a functional glutathione synthetase
    • Okumura N., Masamoto K., Wada H. The gshB gene in the cyanobacterium Synechococcus sp. PCC 7942 encodes a functional glutathione synthetase. Microbiology 1997, 143(Pt 9):2883-2890.
    • (1997) Microbiology , vol.143 , Issue.PART 9 , pp. 2883-2890
    • Okumura, N.1    Masamoto, K.2    Wada, H.3
  • 67
    • 84355166449 scopus 로고    scopus 로고
    • Proteomics combines morphological, physiological and biochemical attributes to unravel the survival strategy of Anabaena sp. PCC7120 under arsenic stress
    • Pandey S., Rai R., Rai L.C. Proteomics combines morphological, physiological and biochemical attributes to unravel the survival strategy of Anabaena sp. PCC7120 under arsenic stress. Journal of Proteomics 2012, 75:921-937.
    • (2012) Journal of Proteomics , vol.75 , pp. 921-937
    • Pandey, S.1    Rai, R.2    Rai, L.C.3
  • 69
    • 77952961827 scopus 로고    scopus 로고
    • On the chemistry, toxicology and genetics of the cyanobacterial toxins, microcystin, nodularin, saxitoxin and cylindrospermopsin
    • Pearson L., Mihali T., Moffitt M., Kellmann R., Neilan B. On the chemistry, toxicology and genetics of the cyanobacterial toxins, microcystin, nodularin, saxitoxin and cylindrospermopsin. Marine Drugs 2010, 8:1650-1680.
    • (2010) Marine Drugs , vol.8 , pp. 1650-1680
    • Pearson, L.1    Mihali, T.2    Moffitt, M.3    Kellmann, R.4    Neilan, B.5
  • 70
    • 65249101414 scopus 로고    scopus 로고
    • Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins
    • Perez-Perez M.E., Martin-Figueroa E., Florencio F.J. Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins. Molecular Plant 2009, 2:270-283.
    • (2009) Molecular Plant , vol.2 , pp. 270-283
    • Perez-Perez, M.E.1    Martin-Figueroa, E.2    Florencio, F.J.3
  • 71
    • 37349036175 scopus 로고    scopus 로고
    • CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster
    • Picciocchi A., Saguez C., Boussac A., Cassier-Chauvat C., Chauvat F. CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster. Biochemistry 2007, 46:15018-15026.
    • (2007) Biochemistry , vol.46 , pp. 15018-15026
    • Picciocchi, A.1    Saguez, C.2    Boussac, A.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 72
    • 84857242898 scopus 로고    scopus 로고
    • Cyanophora paradoxa genome elucidates origin of photosynthesis in algae and plants
    • Price D.C., Chan C.X., Yoon H.S., Yang E.C., Qiu H., Weber A.P., et al. Cyanophora paradoxa genome elucidates origin of photosynthesis in algae and plants. Science 2012, 335:843-847.
    • (2012) Science , vol.335 , pp. 843-847
    • Price, D.C.1    Chan, C.X.2    Yoon, H.S.3    Yang, E.C.4    Qiu, H.5    Weber, A.P.6
  • 74
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation
    • Rouhier N., Lemaire S.D., Jacquot J.P. The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annual Review of Plant Biology 2008, 59:143-166.
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.P.3
  • 76
    • 79551515101 scopus 로고    scopus 로고
    • The paleobiological record of photosynthesis
    • Schopf W.J. The paleobiological record of photosynthesis. Photosynthesis Research 2011, 107:87-101.
    • (2011) Photosynthesis Research , vol.107 , pp. 87-101
    • Schopf, W.J.1
  • 77
    • 68249143313 scopus 로고    scopus 로고
    • The mechanism of iron homeostasis in the unicellular cyanobacterium Synechocystis sp. PCC 6803 and its relationship to oxidative stress
    • Shcolnick S., Summerfield T.C., Reytman L., Sherman L.A., Keren N. The mechanism of iron homeostasis in the unicellular cyanobacterium Synechocystis sp. PCC 6803 and its relationship to oxidative stress. Plant Physiology 2009, 150:2045-2056.
    • (2009) Plant Physiology , vol.150 , pp. 2045-2056
    • Shcolnick, S.1    Summerfield, T.C.2    Reytman, L.3    Sherman, L.A.4    Keren, N.5
  • 80
    • 0035831449 scopus 로고    scopus 로고
    • A genetic investigation of the essential role of glutathione: mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast
    • Spector D., Labarre J., Toledano M.B. A genetic investigation of the essential role of glutathione: mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast. The Journal of Biological Chemistry 2001, 276:7011-7016.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 7011-7016
    • Spector, D.1    Labarre, J.2    Toledano, M.B.3
  • 83
    • 80055069623 scopus 로고    scopus 로고
    • Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum
    • Suttisansanee U., Lau K., Lagishetty S., Rao K.N., Swaminathan S., Sauder J.M., et al. Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum. The Journal of Biological Chemistry 2011, 286:38367-38374.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 38367-38374
    • Suttisansanee, U.1    Lau, K.2    Lagishetty, S.3    Rao, K.N.4    Swaminathan, S.5    Sauder, J.M.6
  • 85
    • 84865185475 scopus 로고    scopus 로고
    • Glutathione serves an extracellular defence function to decrease arsenite accumulation and toxicity in yeast
    • Thorsen M., Jacobson T., Vooijs R., Navarrete C., Bliek T., Schat H., et al. Glutathione serves an extracellular defence function to decrease arsenite accumulation and toxicity in yeast. Molecular Microbiology 2012, 84:1177-1188.
    • (2012) Molecular Microbiology , vol.84 , pp. 1177-1188
    • Thorsen, M.1    Jacobson, T.2    Vooijs, R.3    Navarrete, C.4    Bliek, T.5    Schat, H.6
  • 87
    • 79952038830 scopus 로고    scopus 로고
    • Overproduction of a rice aldo-keto reductase increases oxidative and heat stress tolerance by malondialdehyde and methylglyoxal detoxification
    • Turoczy Z., Kis P., Torok K., Cserhati M., Lendvai A., Dudits D., et al. Overproduction of a rice aldo-keto reductase increases oxidative and heat stress tolerance by malondialdehyde and methylglyoxal detoxification. Plant Molecular Biology 2011, 75:399-412.
    • (2011) Plant Molecular Biology , vol.75 , pp. 399-412
    • Turoczy, Z.1    Kis, P.2    Torok, K.3    Cserhati, M.4    Lendvai, A.5    Dudits, D.6
  • 90
    • 79960584007 scopus 로고    scopus 로고
    • Genome mining demonstrates the widespread occurrence of gene clusters encoding bacteriocins in cyanobacteria
    • Wang H., Fewer D.P., Sivonen K. Genome mining demonstrates the widespread occurrence of gene clusters encoding bacteriocins in cyanobacteria. PloS One 2011, 6:e22384.
    • (2011) PloS One , vol.6
    • Wang, H.1    Fewer, D.P.2    Sivonen, K.3
  • 92
    • 34547842543 scopus 로고    scopus 로고
    • Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates
    • Wiktelius E., Stenberg G. Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates. The Biochemical Journal 2007, 406:115-123.
    • (2007) The Biochemical Journal , vol.406 , pp. 115-123
    • Wiktelius, E.1    Stenberg, G.2
  • 93
    • 57749202256 scopus 로고    scopus 로고
    • Panning for chemical gold: marine bacteria as a source of new therapeutics
    • Williams P.G. Panning for chemical gold: marine bacteria as a source of new therapeutics. Trends in Biotechnology 2009, 27:45-52.
    • (2009) Trends in Biotechnology , vol.27 , pp. 45-52
    • Williams, P.G.1
  • 96
    • 33746207862 scopus 로고    scopus 로고
    • Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002
    • Xu D., Liu X., Guo C., Zhao J. Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002. Microbiology 2006, 152:2013-2021.
    • (2006) Microbiology , vol.152 , pp. 2013-2021
    • Xu, D.1    Liu, X.2    Guo, C.3    Zhao, J.4
  • 102
    • 79953139204 scopus 로고    scopus 로고
    • Engineering cyanobacteria for fuels and chemicals production
    • Zhou J., Li Y. Engineering cyanobacteria for fuels and chemicals production. Protein Cell 2010, 1:207-210.
    • (2010) Protein Cell , vol.1 , pp. 207-210
    • Zhou, J.1    Li, Y.2


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