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Volumn , Issue , 2013, Pages

Thiol redox sensitivity of two key enzymes of heme biosynthesis and pentose phosphate pathways: Uroporphyrinogen decarboxylase and transketolase

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ASSAY; CONSERVED RESIDUES; HEME BIOSYNTHESIS; NATURAL SUBSTRATES; PENTOSE PHOSPHATE PATHWAY; PROTEOMIC TECHNIQUES; REDOX SENSITIVES; TUMOUR PROGRESSION;

EID: 84881524193     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2013/932472     Document Type: Article
Times cited : (14)

References (53)
  • 1
    • 77949967131 scopus 로고    scopus 로고
    • Targeting metabolic transformation for cancer therapy
    • 2-s2.0-77949967131 10.1038/nrc2817
    • Tennant D. A., Durán R. V., Gottlieb E., Targeting metabolic transformation for cancer therapy. Nature Reviews Cancer 2010 10 4 267 277 2-s2.0-77949967131 10.1038/nrc2817
    • (2010) Nature Reviews Cancer , vol.10 , Issue.4 , pp. 267-277
    • Tennant, D.A.1    Durán, R.V.2    Gottlieb, E.3
  • 2
    • 24044489207 scopus 로고    scopus 로고
    • Yeast and cancer
    • 2-s2.0-32944458452
    • Hartwell L. H., Yeast and cancer. Bioscience Reports 2004 24 4-5 523 544 2-s2.0-32944458452
    • (2004) Bioscience Reports , vol.24 , Issue.4-5 , pp. 523-544
    • Hartwell, L.H.1
  • 3
    • 70349240206 scopus 로고    scopus 로고
    • Tumor cell energy metabolism and its common features with yeast metabolism
    • 2-s2.0-70349240206 10.1016/j.bbcan.2009.07.003
    • Diaz-Ruiz R., Uribe-Carvajal S., Devin A., Rigoulet M., Tumor cell energy metabolism and its common features with yeast metabolism. Biochimica et Biophysica Acta 2009 1796 2 252 265 2-s2.0-70349240206 10.1016/j.bbcan.2009.07. 003
    • (2009) Biochimica et Biophysica Acta , vol.1796 , Issue.2 , pp. 252-265
    • Diaz-Ruiz, R.1    Uribe-Carvajal, S.2    Devin, A.3    Rigoulet, M.4
  • 4
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • 2-s2.0-12444279265
    • Warburg O., On the origin of cancer cells. Science 1956 123 3191 309 314 2-s2.0-12444279265
    • (1956) Science , vol.123 , Issue.3191 , pp. 309-314
    • Warburg, O.1
  • 5
    • 0000089325 scopus 로고
    • Observations on the carbohydrate metabolism of tumours
    • Crabtree H. G., Observations on the carbohydrate metabolism of tumours. The Biochemical Journal 1929 23 3 536 545
    • (1929) The Biochemical Journal , vol.23 , Issue.3 , pp. 536-545
    • Crabtree, H.G.1
  • 6
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • 2-s2.0-79952284127 10.1016/j.cell.2011.02.013
    • Hanahan D., Weinberg R. A., Hallmarks of cancer: the next generation. Cell 2011 144 5 646 674 2-s2.0-79952284127 10.1016/j.cell.2011.02.013
    • (2011) Cell , vol.144 , Issue.5 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 7
    • 84875345177 scopus 로고    scopus 로고
    • Iron and copper in mitochondrial diseases
    • Xu W., Barrientos T., Andrews N. C., Iron and copper in mitochondrial diseases. Cell Metabolism 2013 17 3 319 328
    • (2013) Cell Metabolism , vol.17 , Issue.3 , pp. 319-328
    • Xu, W.1    Barrientos, T.2    Andrews, N.C.3
  • 8
    • 0035474950 scopus 로고    scopus 로고
    • Recent advances in disorders of iron metabolism: Mutations, mechanisms and modifiers
    • Roy C. N., Andrews N. C., Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers. Human Molecular Genetics 2001 10 20 2181 2186 2-s2.0-0035474950 (Pubitemid 32998830)
    • (2001) Human Molecular Genetics , vol.10 , Issue.20 , pp. 2181-2186
    • Roy, C.N.1    Andrews, N.C.2
  • 9
    • 79951876764 scopus 로고    scopus 로고
    • Cysteine-based redox switches in enzymes
    • 2-s2.0-79951876764 10.1089/ars.2010.3376
    • Klomsiri C., Karplus P. A., Poole L. B., Cysteine-based redox switches in enzymes. Antioxidants and Redox Signaling 2011 14 6 1065 1077 2-s2.0-79951876764 10.1089/ars.2010.3376
    • (2011) Antioxidants and Redox Signaling , vol.14 , Issue.6 , pp. 1065-1077
    • Klomsiri, C.1    Karplus, P.A.2    Poole, L.B.3
  • 10
    • 79954504166 scopus 로고    scopus 로고
    • Basic principles and emerging concepts in the redox control of transcription factors
    • 2-s2.0-79954504166 10.1089/ars.2010.3534
    • Brigelius-Flohé R., Flohé L., Basic principles and emerging concepts in the redox control of transcription factors. Antioxidants and Redox Signaling 2011 15 8 2335 2381 2-s2.0-79954504166 10.1089/ars.2010.3534
    • (2011) Antioxidants and Redox Signaling , vol.15 , Issue.8 , pp. 2335-2381
    • Brigelius-Flohé, R.1    Flohé, L.2
  • 11
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • 2-s2.0-51349088530 10.1089/ars.2008.2089
    • Mieyal J. J., Gallogly M. M., Qanungo S., Sabens E. A., Shelton M. D., Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxidants and Redox Signaling 2008 10 11 1941 1988 2-s2.0-51349088530 10.1089/ars.2008.2089
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.11 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 12
    • 84867730651 scopus 로고    scopus 로고
    • Protein-thiol oxidation and cell death: Regulatory role of glutaredoxins
    • Allen E. M. G., Mieyal J. J., Protein-thiol oxidation and cell death: regulatory role of glutaredoxins. Antioxidants & Redox Signaling 2012 17 12 1748 1763
    • (2012) Antioxidants & Redox Signaling , vol.17 , Issue.12 , pp. 1748-1763
    • Allen, E.M.G.1    Mieyal, J.J.2
  • 14
    • 63649159793 scopus 로고    scopus 로고
    • Shotgun redox proteomics identifies specifically modified cysteines in key metabolic enzymes under oxidative stress in Saccharomyces cerevisiae
    • 2-s2.0-63649159793 10.1016/j.jprot.2009.01.023
    • McDonagh B., Ogueta S., Lasarte G., Padilla C. A., Bárcena J. A., Shotgun redox proteomics identifies specifically modified cysteines in key metabolic enzymes under oxidative stress in Saccharomyces cerevisiae. Journal of Proteomics 2009 72 4 677 689 2-s2.0-63649159793 10.1016/j.jprot.2009.01.023
    • (2009) Journal of Proteomics , vol.72 , Issue.4 , pp. 677-689
    • McDonagh, B.1    Ogueta, S.2    Lasarte, G.3    Padilla, C.A.4    Bárcena, J.A.5
  • 15
    • 0032956855 scopus 로고    scopus 로고
    • Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress
    • Grant C. M., Quinn K. A., Dawes I. W., Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress. Molecular and Cellular Biology 1999 19 4 2650 2656 2-s2.0-0032956855 (Pubitemid 29144509)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.4 , pp. 2650-2656
    • Grant, C.M.1    Quinn, K.A.2    Dawes, I.W.3
  • 16
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • 2-s2.0-0028170673
    • Ravichandran V., Seres T., Moriguchi T., Thomas J. A., Johnston R. B. Jr., S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. Journal of Biological Chemistry 1994 269 40 25010 25015 2-s2.0-0028170673
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston Jr., R.B.5
  • 17
    • 0028204459 scopus 로고
    • S-Thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment
    • Schuppe-Koistinen I., Moldeus P., Bergman T., Cotgreave I. A., S-Thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment. European Journal of Biochemistry 1994 221 3 1033 1037 2-s2.0-0028204459 (Pubitemid 24146205)
    • (1994) European Journal of Biochemistry , vol.221 , Issue.3 , pp. 1033-1037
    • Schuppe-Koistinen, I.1    Moldeus, P.2    Bergman, T.3    Cotgreave, I.A.4
  • 18
    • 79955389754 scopus 로고    scopus 로고
    • Biosynthetic and iron metabolism is regulated by thiol proteome changes dependent on glutaredoxin-2 and mitochondrial peroxiredoxin-1 in Saccharomyces cerevisiae
    • 2-s2.0-79955389754 10.1074/jbc.M110.193102
    • McDonagh B., Padilla C. A., Pedrajas J. R., Barcena J. A., Biosynthetic and iron metabolism is regulated by thiol proteome changes dependent on glutaredoxin-2 and mitochondrial peroxiredoxin-1 in Saccharomyces cerevisiae. Journal of Biological Chemistry 2011 286 17 15565 15576 2-s2.0-79955389754 10.1074/jbc.M110.193102
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.17 , pp. 15565-15576
    • McDonagh, B.1    Padilla, C.A.2    Pedrajas, J.R.3    Barcena, J.A.4
  • 20
    • 84875181661 scopus 로고    scopus 로고
    • Oxidants, antioxidants and the current incurability of metastatic cancers
    • 120144
    • Watson J., Oxidants, antioxidants and the current incurability of metastatic cancers. Open Biology 2013 3 1 120144
    • (2013) Open Biology , vol.3 , Issue.1
    • Watson, J.1
  • 21
    • 82155171284 scopus 로고    scopus 로고
    • Regulation of reactive oxygen species in stem cells and cancer stem cells
    • 2-s2.0-82155171284 10.1002/jcp.22764
    • Kobayashi C. I., Suda T., Regulation of reactive oxygen species in stem cells and cancer stem cells. Journal of Cellular Physiology 2012 227 2 421 430 2-s2.0-82155171284 10.1002/jcp.22764
    • (2012) Journal of Cellular Physiology , vol.227 , Issue.2 , pp. 421-430
    • Kobayashi, C.I.1    Suda, T.2
  • 22
    • 44549088704 scopus 로고    scopus 로고
    • The biochemistry of heme biosynthesis
    • 2-s2.0-44549088704 10.1016/j.abb.2008.02.015
    • Heinemann I. U., Jahn M., Jahn D., The biochemistry of heme biosynthesis. Archives of Biochemistry and Biophysics 2008 474 2 238 251 2-s2.0-44549088704 10.1016/j.abb.2008.02.015
    • (2008) Archives of Biochemistry and Biophysics , vol.474 , Issue.2 , pp. 238-251
    • Heinemann, I.U.1    Jahn, M.2    Jahn, D.3
  • 23
    • 0032729833 scopus 로고    scopus 로고
    • Molecular mechanism of heme signaling in yeast: The transcriptional activator Hap1 serves as the key mediator
    • DOI 10.1007/s000180050442
    • Zhang L., Hach A., Molecular mechanism of heme signaling in yeast: the transcriptional activator Hap1 serves as the key mediator. Cellular and Molecular Life Sciences 1999 56 5-6 415 426 2-s2.0-0032729833 10.1007/s000180050442 (Pubitemid 29520832)
    • (1999) Cellular and Molecular Life Sciences , vol.56 , Issue.5-6 , pp. 415-426
    • Zhang, L.1    Hach, A.2
  • 25
    • 79251504609 scopus 로고    scopus 로고
    • Uroporphyrinogen decarboxylase is a radiosensitizing target for head and neck cancer
    • Ito E., Yue S., Moriyama E. H., Uroporphyrinogen decarboxylase is a radiosensitizing target for head and neck cancer. Science Translational Medicine 2011 3 67 67ra7
    • (2011) Science Translational Medicine , vol.3 , Issue.67
    • Ito, E.1    Yue, S.2    Moriyama, E.H.3
  • 26
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex N., Peitsch M. C., SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997 18 15 2714 2723 2-s2.0-0031473847 10.1002/elps.1150181505 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 27
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • DOI 10.1091/mbc.01-10-0517
    • Rodríguez-Manzaneque M. T., Tamarit J., Bellí G., Ros J., Herrero E., Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Molecular Biology of the Cell 2002 13 4 1109 1121 2-s2.0-0036226063 10.1091/mbc.01-10-0517 (Pubitemid 34309609)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.4 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 29
  • 30
    • 80054856160 scopus 로고    scopus 로고
    • Thiol redox proteomics identifies differential targets of cytosolic and mitochondrial glutaredoxin-2 isoforms in Saccharomyces cerevisiae. Reversible S-glutathionylation of DHBP synthase (RIB3)
    • 2-s2.0-80054856160 10.1016/j.jprot.2011.04.018
    • McDonagh B., Requejo R., Fuentes-Almagro C. A., Ogueta S., Bárcena J. A., Padilla C. A., Thiol redox proteomics identifies differential targets of cytosolic and mitochondrial glutaredoxin-2 isoforms in Saccharomyces cerevisiae. Reversible S-glutathionylation of DHBP synthase (RIB3). Journal of Proteomics 2011 74 11 2487 2497 2-s2.0-80054856160 10.1016/j.jprot.2011.04.018
    • (2011) Journal of Proteomics , vol.74 , Issue.11 , pp. 2487-2497
    • McDonagh, B.1    Requejo, R.2    Fuentes-Almagro, C.A.3    Ogueta, S.4    Bárcena, J.A.5    Padilla, C.A.6
  • 31
    • 0037096975 scopus 로고    scopus 로고
    • Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments
    • DOI 10.1042/BJ20020570
    • Pedrajas J. R., Porras P., Martínez-Galisteo E., Padilla C. A., Miranda-Vizuete A., Bárcena J. A., Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments. Biochemical Journal 2002 364 3 617 623 2-s2.0-0037096975 10.1042/BJ20020570 (Pubitemid 34680835)
    • (2002) Biochemical Journal , vol.364 , Issue.3 , pp. 617-623
    • Pedrajas, J.R.1    Porras, P.2    Martinez-Galisteo, E.3    Padilla, C.A.4    Miranda-Vizuete, A.5    Barcena, J.A.6
  • 33
    • 4544269846 scopus 로고    scopus 로고
    • Transketolase from Leishmania mexicana has a dual subcellular localization
    • DOI 10.1042/BJ20040459
    • Veitch N. J., Maugeri D. A., Cazzulo J. J., Lindqvist Y., Barrett M. P., Transketolase from Leishmania mexicana has a dual subcellular localization. Biochemical Journal 2004 382 2 759 767 2-s2.0-4544269846 10.1042/BJ20040459 (Pubitemid 39243943)
    • (2004) Biochemical Journal , vol.382 , Issue.2 , pp. 759-767
    • Veitch, N.J.1    Maugeri, D.A.2    Cazzulo, J.J.3    Lindqvist, Y.4    Barrett, M.P.5
  • 34
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • 2-s2.0-69949115433 10.1074/jbc.M109.021394
    • Park J. W., Mieyal J. J., Rhee S. G., Chock P. B., Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. Journal of Biological Chemistry 2009 284 35 23364 23374 2-s2.0-69949115433 10.1074/jbc.M109.021394
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.35 , pp. 23364-23374
    • Park, J.W.1    Mieyal, J.J.2    Rhee, S.G.3    Chock, P.B.4
  • 35
    • 33845611917 scopus 로고    scopus 로고
    • The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3- phosphate dehydrogenase is selectively regulated by glutathionylation
    • DOI 10.1111/j.1742-4658.2006.05577.x
    • Zaffagnini M., Michelet L., Marchand C., Sparla F., Decottignies P., Le Maréchal P., Miginiac-Maslow M., Noctor G., Trost P., Lemaire S. D., The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3- phosphate dehydrogenase is selectively regulated by glutathionylation. FEBS Journal 2007 274 1 212 226 2-s2.0-33845611917 10.1111/j.1742-4658.2006.05577.x (Pubitemid 44952910)
    • (2007) FEBS Journal , vol.274 , Issue.1 , pp. 212-226
    • Zaffagnini, M.1    Michelet, L.2    Marchand, C.3    Sparla, F.4    Decottignies, P.5    Le Marechal, P.6    Miginiac-Maslow, M.7    Noctor, G.8    Trost, P.9    Lemaire, S.D.10
  • 36
    • 34249903638 scopus 로고    scopus 로고
    • Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay
    • DOI 10.1016/j.freeradbiomed.2007.03.025, PII S0891584907002201
    • Raturi A., Mutus B., Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay. Free Radical Biology and Medicine 2007 43 1 62 70 2-s2.0-34249903638 10.1016/j.freeradbiomed.2007.03.025 (Pubitemid 46874840)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.1 , pp. 62-70
    • Raturi, A.1    Mutus, B.2
  • 37
    • 0025264250 scopus 로고
    • Purification and properties of uroporphyrinogen decarboxylase from Saccharomyces cerevisiae. Yeast uroporphyrinogen decarboxylase
    • Felix F., Brouillet N., Purification and properties of uroporphyrinogen decarboxylase from Saccharomyces cerevisiae. Yeast uroporphyrinogen decarboxylase. European Journal of Biochemistry 1990 188 2 393 403 2-s2.0-0025264250 (Pubitemid 20106254)
    • (1990) European Journal of Biochemistry , vol.188 , Issue.2 , pp. 393-403
    • Felix, F.1    Brouillet, N.2
  • 38
    • 2342498602 scopus 로고    scopus 로고
    • The role of cysteine 160 in thiamine diphosphate binding of the Calvin-Benson-Bassham cycle transketolase of Rhodobacter sphaeroides
    • DOI 10.1016/j.abb.2004.03.027, PII S0003986104001675
    • Bobst C. E., Tabita F. R., The role of cysteine 160 in thiamine diphosphate binding of the Calvin-Benson-Bassham cycle transketolase of Rhodobacter sphaeroides. Archives of Biochemistry and Biophysics 2004 426 1 43 54 2-s2.0-2342498602 10.1016/j.abb.2004.03.027 (Pubitemid 38595129)
    • (2004) Archives of Biochemistry and Biophysics , vol.426 , Issue.1 , pp. 43-54
    • Bobst, C.E.1    Tabita, F.R.2
  • 40
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5Å resolution
    • 2-s2.0-0026762799
    • Lindqvist Y., Schneider G., Ermler U., Sundstrom M., Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5Å resolution. EMBO Journal 1992 11 7 2373 2379 2-s2.0-0026762799
    • (1992) EMBO Journal , vol.11 , Issue.7 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundstrom, M.4
  • 41
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution
    • DOI 10.1006/jmbi.1994.1299
    • Nikkola M., Lindqvist Y., Schneider G., Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution. Journal of Molecular Biology 1994 238 3 387 404 2-s2.0-0028305456 10.1006/jmbi.1994.1299 (Pubitemid 24154719)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.3 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 42
    • 79958233011 scopus 로고    scopus 로고
    • Redox biology: Computational approaches to the investigation of functional cysteine residues
    • 2-s2.0-79958233011 10.1089/ars.2010.3561
    • Marino S. M., Gladyshev V. N., Redox biology: computational approaches to the investigation of functional cysteine residues. Antioxidants and Redox Signaling 2011 15 1 135 146 2-s2.0-79958233011 10.1089/ars.2010.3561
    • (2011) Antioxidants and Redox Signaling , vol.15 , Issue.1 , pp. 135-146
    • Marino, S.M.1    Gladyshev, V.N.2
  • 44
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • 2-s2.0-55149107716 10.1152/ajpcell.00283.2008
    • Jones D. P., Radical-free biology of oxidative stress. American Journal of Physiology 2008 295 4 C849 C868 2-s2.0-55149107716 10.1152/ajpcell.00283.2008
    • (2008) American Journal of Physiology , vol.295 , Issue.4
    • Jones, D.P.1
  • 45
    • 79957441981 scopus 로고    scopus 로고
    • The disulfide proteome and other reactive cysteine proteomes: Analysis and functional significance
    • 2-s2.0-79957441981 10.1089/ars.2010.3551
    • Lindahl M., Mata-Cabana A., Kieselbach T., The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance. Antioxidants and Redox Signaling 2011 14 12 2581 2642 2-s2.0-79957441981 10.1089/ars.2010.3551
    • (2011) Antioxidants and Redox Signaling , vol.14 , Issue.12 , pp. 2581-2642
    • Lindahl, M.1    Mata-Cabana, A.2    Kieselbach, T.3
  • 46
    • 0032079342 scopus 로고    scopus 로고
    • Crystal structure of human uroporphyrinogen decarboxylase
    • DOI 10.1093/emboj/17.9.2463
    • Whitby F. G., Phillips J. D., Kushner J. P., Hill C. P., Crystal structure of human uroporphyrinogen decarboxylase. EMBO Journal 1998 17 9 2463 2471 2-s2.0-0032079342 10.1093/emboj/17.9.2463 (Pubitemid 28221182)
    • (1998) EMBO Journal , vol.17 , Issue.9 , pp. 2463-2471
    • Whitby, F.G.1    Phillips, J.D.2    Kushner, J.P.3    Hill, C.P.4
  • 47
    • 3142722152 scopus 로고    scopus 로고
    • The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase
    • DOI 10.1074/jbc.M403721200
    • Lange H., Mühlenhoff U., Denzel M., Kispal G., Lill R., The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase. Journal of Biological Chemistry 2004 279 28 29101 29108 2-s2.0-3142722152 10.1074/jbc.M403721200 (Pubitemid 38915781)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29101-29108
    • Lange, H.1    Muhlenhoff, U.2    Denzel, M.3    Kispal, G.4    Lill, R.5
  • 48
    • 33751529756 scopus 로고    scopus 로고
    • Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae
    • DOI 10.1242/cjs.03229
    • Pujol-Carrion N., Belli G., Herrero E., Nogues A., de la Torre-Ruiz M. A., Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae. Journal of Cell Science 2006 119 21 4554 4564 2-s2.0-33751529756 10.1242/cjs.03229 (Pubitemid 44830654)
    • (2006) Journal of Cell Science , vol.119 , Issue.21 , pp. 4554-4564
    • Pujol-Carrion, N.1    Belli, G.2    Herrero, E.3    Nogues, A.4    De La Torre-Ruiz, M.A.5
  • 49
    • 1842478044 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Glutaredoxin 5-deficient Cells Subjected to Continuous Oxidizing Conditions Are Affected in the Expression of Specific Sets of Genes
    • DOI 10.1074/jbc.M311879200
    • Bellí G., Molina M. M., García-Martínez J., Pérez-Ortsín J. E., Herrero E., Saccharomyces cerevisiae Glutaredoxin 5-deficient Cells Subjected to Continuous Oxidizing Conditions Are Affected in the Expression of Specific Sets of Genes. Journal of Biological Chemistry 2004 279 13 12386 12395 2-s2.0-1842478044 10.1074/jbc.M311879200 (Pubitemid 38445806)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12386-12395
    • Belli, G.1    Molina, M.M.2    Garcia-Martinez, J.3    Perez-Ortsin, J.E.4    Herrero, E.5
  • 51
    • 0017336797 scopus 로고
    • Thioredoxin and glutathione regulate photosynthesis in chloroplasts
    • Wolosiuk R. A., Buchanan B. B., Thioredoxin and glutathione regulate photosynthesis in chloroplasts. Nature 1977 266 5602 565 567 2-s2.0-0017336797 (Pubitemid 8079253)
    • (1977) Nature , vol.266 , Issue.5602 , pp. 565-567
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 53
    • 77954217477 scopus 로고    scopus 로고
    • Redox regulation of chlorophyll biosynthesis
    • 2-s2.0-77954217477 10.1016/j.phytochem.2010.03.022
    • Stenbaek A., Jensen P. E., Redox regulation of chlorophyll biosynthesis. Phytochemistry 2010 71 8-9 853 859 2-s2.0-77954217477 10.1016/j.phytochem.2010. 03.022
    • (2010) Phytochemistry , vol.71 , Issue.8-9 , pp. 853-859
    • Stenbaek, A.1    Jensen, P.E.2


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