Redox control and oxidative stress in yeast cells
Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains...
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Published in | Biochimica et biophysica acta Vol. 1780; no. 11; pp. 1217 - 1235 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.11.2008
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Subjects | |
Online Access | Get full text |
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Abstract | Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in
Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in
S. cerevisiae (Pap1 in
Schizosaccharomyces pombe and Cap1 in
Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules. |
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AbstractList | Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules.Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules. Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules. Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules. |
Author | Ros, Joaquim Bellí, Gemma Herrero, Enrique Cabiscol, Elisa |
Author_xml | – sequence: 1 givenname: Enrique surname: Herrero fullname: Herrero, Enrique email: enric.herrero@cmb.udl.cat – sequence: 2 givenname: Joaquim surname: Ros fullname: Ros, Joaquim – sequence: 3 givenname: Gemma surname: Bellí fullname: Bellí, Gemma – sequence: 4 givenname: Elisa surname: Cabiscol fullname: Cabiscol, Elisa |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18178164$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1073/pnas.0602048103 10.1002/j.1460-2075.1986.tb04256.x 10.1091/mbc.E02-08-0546 10.1016/j.bbamcr.2006.05.003 10.1007/s00726-006-0448-1 10.1099/mic.0.27945-0 10.1042/bj20030638 10.1007/BF02426954 10.1074/jbc.M410219200 10.1074/jbc.M312421200 10.1074/jbc.271.46.28831 10.1074/jbc.M408340200 10.1093/jxb/erl001 10.1074/jbc.M406576200 10.1046/j.1365-2958.2001.02283.x 10.1128/MCB.21.24.8483-8489.2001 10.1074/jbc.M508622200 10.1016/j.neuro.2006.05.012 10.1091/mbc.01-06-0288 10.1074/jbc.M600138200 10.1074/jbc.M008377200 10.1006/exnr.2002.8072 10.1023/A:1005427919188 10.1002/j.1460-2075.1994.tb06304.x 10.1242/jcs.03229 10.1074/jbc.M500678200 10.1186/gb-2004-5-7-229 10.1016/S0969-2126(01)00154-X 10.1074/jbc.M304296200 10.1016/j.freeradbiomed.2005.12.017 10.1016/S1383-5718(01)00213-3 10.1074/jbc.M306312200 10.1101/gad.12.10.1453 10.1111/j.1365-2958.2005.04822.x 10.1074/jbc.M402795200 10.1093/emboj/17.24.7416 10.1074/jbc.M601968200 10.1101/gad.13.13.1653 10.1016/S0006-2952(99)00289-0 10.1046/j.1365-2958.2000.01890.x 10.1016/j.febslet.2007.07.002 10.1074/jbc.M105524200 10.1016/j.cmet.2006.02.011 10.1074/jbc.M508400200 10.1016/S0021-9258(18)52350-4 10.1042/0264-6021:3530411 10.1128/MCB.24.19.8753-8764.2004 10.1002/yea.1392 10.1016/j.bbapap.2004.09.003 10.1002/j.1460-2075.1996.tb00576.x 10.1089/152308604771978354 10.1111/j.1742-4658.2006.05116.x 10.1074/jbc.M511649200 10.1093/emboj/16.5.1035 10.1038/nature05804 10.1016/j.tibs.2004.05.005 10.1111/j.1582-4934.2004.tb00275.x 10.1016/j.cellbi.2004.11.010 10.1074/jbc.274.38.27002 10.1093/emboj/19.19.5157 10.1073/pnas.0700481104 10.1073/pnas.94.18.9585 10.1073/pnas.93.12.5777 10.1016/S0092-8674(01)00300-2 10.1074/jbc.M606639200 10.1046/j.0022-3042.2002.00744.x 10.1016/S0304-4173(87)80003-4 10.1046/j.1365-2958.1999.01360.x 10.1091/mbc.9.5.1081 10.1111/j.1574-6976.2001.tb00570.x 10.1074/jbc.M001706200 10.1101/gad.12.10.1464 10.1023/A:1027374931887 10.1016/S0021-9258(19)36959-5 10.1016/S0378-4274(02)00280-1 10.1046/j.1432-1033.2003.03529.x 10.1002/(SICI)1097-0061(19980315)14:4<347::AID-YEA226>3.0.CO;2-9 10.1073/pnas.83.11.3820 10.1007/s00438-006-0175-z 10.1074/jbc.M105296200 10.1089/152308602753625915 10.1016/j.bbrc.2006.11.100 10.1016/S0891-5849(03)00434-9 10.1023/A:1005626712319 10.1083/jcb.200402120 10.1074/jbc.M602165200 10.1074/jbc.M200949200 10.1016/j.bbrc.2005.02.183 10.1074/jbc.M111686200 10.1074/jbc.M411062200 10.1128/MCB.19.12.8180 10.1074/jbc.274.10.6366 10.1074/jbc.M106846200 10.1006/bbrc.1998.9864 10.1128/MCB.14.9.5832 10.1111/j.0031-9317.2004.0193.x 10.1074/jbc.M303542200 10.1128/EC.3.5.1076-1087.2004 10.1074/jbc.M307760200 10.1111/j.1348-0421.2003.tb03376.x 10.1113/jphysiol.2003.049478 10.1002/(SICI)1097-0061(199812)14:16<1511::AID-YEA356>3.0.CO;2-S 10.1016/S0891-5849(03)00307-1 10.1179/135100005X83707 10.1091/mbc.01-10-0517 10.1042/bj1560435 10.1046/j.1365-2958.2002.03020.x 10.1074/jbc.274.21.15151 10.1111/j.1365-2958.2004.04065.x 10.1007/s00253-003-1421-5 10.1128/EC.2.3.381-389.2003 10.1128/IAI.72.4.2390-2394.2004 10.1038/sj.bjp.0705776 10.1016/j.bbrc.2006.06.067 10.1128/IAI.73.8.5022-5030.2005 10.1128/EC.00098-06 10.1016/j.cell.2004.05.002 10.1042/bst0311308 10.1089/ars.2005.7.327 10.1111/j.1432-1033.1991.tb15775.x 10.1515/BC.2006.166 10.1046/j.1365-2958.2000.01783.x 10.1007/s00018-007-6554-8 10.1016/S0021-9258(18)31570-9 10.1074/jbc.271.21.12275 10.1074/jbc.M502757200 10.1146/annurev.cellbio.17.1.701 10.1006/bbrc.1997.7812 10.1016/j.bbrc.2004.09.158 10.1128/EC.00098-07 10.1128/MCB.21.18.6139-6150.2001 10.1016/0304-4173(73)90001-3 10.1016/j.femsyr.2005.03.004 10.1074/jbc.M513346200 10.1091/mbc.11.12.4241 10.1091/mbc.7.11.1805 10.1074/jbc.275.8.5723 10.1074/jbc.M402095200 10.1016/0378-1119(93)90513-3 10.1146/annurev.micro.54.1.439 10.1016/j.freeradbiomed.2006.10.042 10.1016/j.febslet.2004.03.091 10.1038/nature03887 10.1016/j.bbamcr.2006.09.006 10.1074/jbc.M105672200 10.1016/S0014-5793(02)03220-9 10.1038/35088500 10.1093/oxfordjournals.jbchem.a022387 10.1016/j.febslet.2006.03.037 10.1128/jb.173.18.5918-5920.1991 10.1038/nature02790 10.1128/EC.4.2.392-400.2005 10.1079/BJN2000296 10.1099/00221287-143-5-1649 10.1093/genetics/150.2.613 10.1016/j.mrfmmm.2004.09.006 10.1196/annals.1395.042 10.1111/j.1567-1364.2006.00065.x 10.1161/01.RES.0000234780.06115.2c 10.1146/annurev.bi.64.070195.000525 10.1146/annurev.biophys.27.1.133 10.1146/annurev.pharmtox.45.120403.095857 10.1007/s00438-004-1015-7 10.1016/j.freeradbiomed.2007.04.007 10.1042/BJ20060034 10.1074/jbc.M201225200 10.1074/jbc.M504716200 10.1016/S0021-9258(19)61523-1 10.1074/jbc.M601354200 10.1091/mbc.E05-06-0520 10.1074/jbc.M313773200 10.1016/S0021-9258(19)74369-5 10.1016/j.febslet.2004.05.077 10.1089/ars.2005.7.348 10.1016/S0968-0004(02)00003-8 10.1016/S0006-291X(88)80602-8 10.1042/BST20051378 10.1099/mic.0.28132-0 10.1046/j.1365-2958.2002.03216.x 10.1042/bj3200061 10.1074/jbc.M404849200 10.1074/jbc.275.3.1902 10.1073/pnas.78.11.6858 10.1016/S0966-842X(02)02462-9 10.1038/nature05292 10.1091/mbc.11.7.2335 10.1128/MCB.19.12.8302 10.1016/j.sbi.2004.09.012 10.1128/IAI.71.1.173-180.2003 10.1038/nature02026 10.1016/S0092-8674(02)01048-6 10.1126/science.273.5271.59 10.1074/jbc.273.35.22480 10.1128/MMBR.69.2.262-291.2005 10.1146/annurev.pharmtox.47.120505.105122 10.1091/mbc.E05-06-0501 10.1016/S0168-9525(03)00167-7 10.1099/00221287-148-11-3705 10.1074/jbc.M008708200 10.1007/s00018-007-6558-4 10.1046/j.1365-2958.2000.01948.x 10.1093/emboj/16.7.1710 10.1074/jbc.275.21.16296 10.1046/j.1365-2958.2001.02255.x 10.1089/ars.2005.7.560 10.1016/j.femsyr.2005.06.001 10.1074/jbc.M201688200 10.1091/mbc.10.5.1395 10.1038/sj.embor.embor729 10.1091/mbc.01-12-0568 10.1016/S0891-5849(02)01328-X 10.1128/EC.00216-06 10.1073/pnas.0503251102 10.1016/j.bbapap.2004.08.010 10.1073/pnas.1632471100 10.1016/j.freeradbiomed.2006.12.027 10.1074/jbc.M910401199 10.1093/emboj/cdg446 10.1146/annurev.genet.32.1.163 10.1091/mbc.E02-08-0499 10.1074/jbc.M202557200 10.1080/10715760410001717327 10.1007/s00726-003-0011-2 10.1128/EC.4.8.1396-1402.2005 10.1016/S0968-0004(00)01674-1 10.1016/j.freeradbiomed.2005.02.026 10.1074/jbc.M303477200 10.1002/yea.835 10.1038/sj.emboj.7600276 10.1046/j.1365-2958.2002.02795.x 10.1016/j.tcb.2005.04.003 10.1128/JB.182.10.2823-2830.2000 10.1046/j.1365-2958.1996.403940.x 10.1016/S0169-409X(01)00128-4 10.1182/blood-2007-02-072520 10.1016/S0021-9258(18)71625-6 10.1111/j.1365-2958.2005.04771.x 10.1515/BC.2006.174 10.1074/jbc.M600790200 10.1016/j.bcp.2005.10.044 10.1091/mbc.E03-03-0179 10.1038/nature00829 10.1179/135100006X154987 10.1073/pnas.090083597 10.1128/IAI.01680-06 10.1016/S0168-6445(03)00017-2 10.1074/jbc.274.23.16040 |
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References | Carmel-Harel, Stearman, Gash, Botstein, Brown, Storz (bib211) 2001; 39 Bearden, Perry (bib131) 1999; 32 Singh, Chauhan, Ghosh, Dixon, Calderone (bib204) 2004; 72 Kox, Gladyshev (bib189) 2007; 1100 Turrens (bib19) 1997; 17 Furukawa, Fu, Deng, Siddique, O'Halloran (bib74) 2006; 103 Vilella, Herrero, Torres, de la Torre-Ruiz (bib254) 2005; 280 Collister, Didmon, MacIsaac, Stark, MacDonald, Keyse (bib251) 2002; 527 Overkamp, Bakker, Kötter, van Tuijl, de Vries, van Dijken, Pronk (bib25) 2000; 182 Outten, Culotta (bib178) 2004; 279 Moskovitz (bib187) 2005; 1703 Orrenius, Gogvadze, Zhivotovsky (bib42) 2007; 47 Davidson, Schiestl (bib26) 2001; 21 Demasi, Pereira, Netto (bib112) 2006; 273 Halliwell, Gutteridge (bib7) 2007 Camaschella, Campanella, De Falco, Boschetto, Merlini, Silvestri, Levi, Iolascon (bib173) 2007; 110 Gulshan, Rovinsky, Coleman, Moye-Rowley (bib226) 2005; 280 Nguyen, Shiozaki (bib241) 1999; 13 Mukhopadhyay, Shi, Rosen (bib156) 2000; 275 Han, Williams, Cadenas (bib64) 2001; 353 Toledano, Kumar, Le Moan, Spector, Tacnet (bib149) 2007; 581 Porras, Padilla, Krayl, Voos, Bárcena (bib151) 2006; 281 Chung, Kim, Roe (bib177) 2005; 330 Moye-Rowley (bib203) 2003; 2 Coleman, Epping, Steggerda, Moye-Rowley (bib224) 1999; 19 Kudo, Taoka, Toda, Yoshida, Horinouchi (bib236) 1999; 274 Molin, Renault, Lagniel, Pin, Toledano, Labarre (bib221) 2007; 43 Choi, Kim, Mukhopadhyay, Cho, Woo, Storz, Ryu (bib210) 2001; 105 Dinis-Oliveira, Remiao, Carmo, Duarte, Navarro, Bastos, Carvalho (bib37) 2006; 27 Martin, Flandez, Nombela, Molina (bib255) 2005; 58 Reverter-Branchat, Cabiscol, Tamarit, Ros (bib46) 2004; 279 Enjalbert, Cornell, Alam, Nicholls, Brown, Quinn (bib101) 2006; 17 Avery, Avery (bib91) 2001; 276 Fridovich (bib60) 1995; 64 Bozonet, Findlay, Day, Cameron, Veal, Morgan (bib239) 2005; 280 Hanbauer, Moskovitz (bib193) 2006; 40 Lin, Kaeberlein, Andalis, Sturtz, Defossez, Culotta, Fink, Guarente (bib45) 2002; 418 Chen, Toone, Mata, Lyne, Burns, Kivinen, Brazma, Jones, Bahler (bib231) 2003; 14 Pujol-Carrión, Bellí, Herrero, Bogues, de la Torre-Ruiz (bib161) 2006; 119 Rodríguez-Manzaneque, Ros, Cabiscol, Sorribas, Herrero (bib168) 1999; 19 Wormley, Heinrich, Millar, Perfect, Cox (bib205) 2005; 73 Fox, Shafiq, Briggs, Knowles, Collister, Didmon, Makrantoni, Dickinson, Hanrahan, Totty, Stark, Keyse, McDonald (bib249) 2007; 447 Muller (bib183) 1996; 7 Greenall, Hadcroft, Malakasi, Jones, Morgan, Hoffman, Whitehall (bib246) 2002; 13 Irazusta, Cabiscol, Reverter-Branchat, Ros, Tamarit (bib128) 2006; 281 Teixeira, Telo, Duarte, Sá-Correia (bib154) 2004; 324 Westwater, McLaren, Dormer, Jamieson (bib217) 2002; 19 Molina-Navarro, Casas, Piedrafita, Bellí, Herrero (bib170) 2006; 580 Oien, Moskovitz (bib192) 2007; 32 Rhee, Chae, Kim (bib105) 2005; 38 Trotter, Grant (bib182) 2003; 4 Ostergaard, Tachibana, Winther (bib180) 2004; 166 Mukai, Kohno, Ishizu (bib124) 1988; 155 Drakulic, Temple, Guido, Jarolim, Breitenbach, Attfield, Dawes (bib181) 2005; 5 Izawa, Inoue, Kimura (bib78) 1996; 320 Wu, Moye-Rowley (bib213) 1994; 14 Lopreiato, Facchin, Sartori, Arrigoni, Casonato, Ruzzene, Pinna, Carignani (bib158) 2004; 377 Toledano, Delaunay, Monceau, Tacnet (bib228) 2004; 29 Sturtz, Diekert, Jensen, Lill, Culotta (bib62) 2001; 276 Kuge, Arita, Murayama, Maeta, Izawa, Inoue, Nomoto (bib223) 2001; 21 De Vries, Marres (bib27) 1987; 895 Kuge, Jones (bib212) 1994; 13 Toone, Kuge, Samuels, Morgan, Toda, Jones (bib235) 1998; 12 Slekar, Kosman, Culotta (bib71) 1996; 271 Hahn, Thiele (bib250) 2002; 277 Pedrajas, Kosmidou, Miranda-Vizuete, Gustaffson, Wright, Spyrou (bib138) 1999; 274 Rouhier, Couturier, Jacquot (bib163) 2006; 57 Cheng, Liu, Brock, Nelson, Hirschi (bib171) 2006; 281 Yamamoto, Ueda, Yamamoto, Hashikawa, Sakurai (bib207) 2007; 6 Huh, Falvo, Gerke, Carroll, Howson, Weissman, O'Shea (bib95) 2003; 425 Rand, Grant (bib148) 2006; 17 Whitbread, Masoumi, Tetlow, Schmuck, Coggan, Board (bib185) 2005; 401 Marres, De Vries, Grivell (bib23) 1991; 195 Barja (bib21) 1999; 31 Wheeler, Grant (bib134) 2004; 120 Field, Furukawa, O'Halloran, Culotta (bib63) 2003 Gunkel, Veenhuis, van der Klei (bib48) 2005; 5 Singer, Kahana, Wolf, Meisinger, Peterson, Goggin, Mahowald, Gottschling (bib117) 1998; 150 Tamarit, Bellí, Cabiscol, Herrero, Ros (bib176) 2003; 278 Nohl, Kozlov, Gille, Staniek (bib16) 2003; 31 Lee, Godon, Lagniel, Spector, Garin, Labarre, Toledano (bib199) 1999; 274 Osorio, Carvalho, del Valle, Gunther Sillero, Moradas-Ferreira, Sillero (bib36) 2003; 270 Stadtman, Van Remmen, Richardson, Wehr, Levine (bib188) 2005; 1703 Grant (bib5) 2001; 39 Camier, Ma, Leroy, Pruvost, Toledano, Marsolier-Kergoat (bib141) 2007; 42 Filipits, Simon, Rapatz, Hamilton, Ruis (bib49) 1993; 132 Filipits, Simon, Rapatz, Hamilton, Ruis (bib77) 1993 Lambert, Brand (bib32) 2004; 279 Salmeen, Barford (bib248) 2005; 7 Larsson, Pahlman, Ansell, Rigoulet, Adler, Gustafsson (bib28) 1998; 14 Vivancos, Castillo, Biteau, Nicot, Ayte, Toledano, Hidalgo (bib240) 2005; 102 Mühlenhoff, Gerber, Richhardt, Lill (bib167) 2003; 22 Cabiscol, Piulats, Echave, Herrero, Ros (bib35) 2000; 275 Stadtman, Levine (bib52) 2003; 25 Enjalbert, MacCallum, Odds, Brown (bib84) 2007; 75 Moskovitz, Berlett, Poston, Stadtman (bib190) 1997; 94 Guidot, McCord, Wright, Repine (bib66) 1993; 268 Bakker, Overkamp, van Maris, Kötter, Luttik, van Dijken, Pronk (bib22) 2001; 25 Wood, Storz, Tjandra (bib227) 2004; 430 Zuin, Vivancos, Sansó, Takatsume, Ayte, Inoue, Hidalgo (bib238) 2005; 280 Herrero, Barja (bib31) 2000; 32 Brihelius-Flohe (bib89) 2006; 387 Wu, Bird, Winge, Eide (bib113) 2007; 282 Koc, Mathews, Wheeler, Gross, Merrill (bib142) 2006; 281 Pinson, Sagot, Daignan-Fornier (bib218) 2000; 36 Pollegioni, Piubelli, Sacchi, Pilone, Molla (bib50) 2007; 64 Longo, Gralla, Valentine (bib70) 1996; 271 Raitt, Johnson, Erkine, Makino, Morgan, Gross, Johnston (bib201) 2000; 11 Barford (bib208) 2004; 14 Halliwell, Whiteman (bib18) 2004; 142 Jeong, Cha, Kim, Kang, Yang, Kim, Yoon, Oh, Bernecker, Sakata, Le, Cui, Lee, Kim do, Woo, Liao, Hajjar, Park (bib165) 2006; 99 Lewinska, Bartosz (bib54) 2006; 11 Liu, Zeng, Hausladen, Heitman, Stamler (bib59) 2000; 97 Ames, Cathcart, Schwiers, Hochstein (bib51) 1981; 78 by oxidative stress is mediated by Yap1 and Skn7, FEBS Lett. 565 (2004) 148–154. Park, Cha, Jeong, Kim (bib106) 2000; 275 Turrens (bib17) 2003; 552 Urban, Xiong, Sohn, Schröpel, Brunner, Rupp (bib119) 2005; 57 Ghezzi (bib10) 2005; 33 Raspor, Plesnicar, Gazdag, Pesti, Miklavcic, Lah, Logar-Marinsek, Poljsak (bib125) 2005; 29 Le Moan, Clement, Le Maout, Tacnet, Toledano (bib146) 2006; 281 Witte, Villalba, Bi, Liu, Isakov, Altman (bib164) 2000; 275 Hayes, Flanagan, Jowsey (bib153) 2005; 45 Wood, Schroder, Harris, Poole (bib104) 2003; 28 Barreto, Garcerá, Jansson, Sunnerhagen, Herrero (bib186) 2006; 5 Shelton, Chock, Mieyal (bib13) 2005; 7 Gralla, Valentine (bib68) 1991; 173 Jang, Lee, Chi, Jung, Park, Park, Lee, Lee, Moon, Yun, Choi, Kim, Kang, Cheong, Yun, Rhee, Cho, Lee (bib115) 2004; 117 Nohl, Staniek, Kozlov (bib58) 2005; 10 Munhoz, Netto (bib109) 2004; 279 Pedrajas, Miranda-Vizuete, Javanmardy, Gustafsson, Spyrou (bib110) 2000; 275 Delaunay, Isnard, Toledano (bib225) 2000; 19 Castello, David, McClure, Crook, Poyton (bib57) 2006; 3 Quinn, Findlay, Dawson, Millar, Jones, Morgan, Toone (bib232) 2002; 13 Nguyen, Alarco, Raymond (bib216) 2001; 276 Ohmiya, Kato, Yamada, Aiba, Mizuno (bib245) 1999; 125 Summer, Shanmuganathan, Sideri, Willetts, Houghton, Avery (bib191) 2005; 151 Luk, Carroll, Baker, Culotta (bib129) 2003; 100 Gaits, Russell (bib244) 1999; 10 Inoue, Matsuda, Sugiyama, Izawa, Kimura (bib90) 1999; 274 Muller (bib139) 1991; 266 Godon, Lagniel, Lee, Buhler, Kieffer, Perror, Boucherie, Toledano, Labarre (bib198) 1998; 273 Giustarini, Rossi, Milzani, Colombo, Dalle-Donne (bib53) 2004; 8 Alic, Higgins, Pichova, Breitenbach, Dawes (bib253) 2003; 278 Fernandes, Fladvad, Berndt, Andrésen, Lillig, Neubauer, Sunnerhagen, Holmgren, Vlamis-Gardikas (bib174) 2005; 280 Cotgreave, Gerdes (bib9) 1998; 242 Fernandes, Holmgren (bib15) 2004; 6 Rahlfs, Fischer, Becker (bib175) 2001; 276 Liu, Fiskum, Schubert (bib33) 2002; 80 Jeffery (bib116) 2003; 19 Martin (bib136) 1995; 3 Barford, Das, Egloff (bib247) 1998; 27 Costa, Amorim, Reis, Quintanilha, Moradas-Ferreira (bib67) 1997; 143 Izawa, Ikeda, Ohdate, Inoue (bib80) 2007; 352 Fang, Beattie (bib29) 2003; 34 Wong, Zhou, Ng, Kung, Jin (bib107) 2002; 277 Cabiscol, Ros (bib8) 2006 Molina, Bellí, de la Torre, Rodríguez-Manzaneque, Herrero (bib159) 2004; 279 Janakiraman, Slauch (bib132) 2000; 35 Izawa, Kuroki, Inoue (bib118) 2004; 64 Grant, MacIver, Dawes (bib179) 1996; 29 Ocón-Garrido, Grant (bib144) 2002; 43 Ojeda, Keller, Mühlenhoff, Rutherford, Lill, Winge (bib160) 2006; 281 Tanaka, Izawa, Inoue (bib98) 2005; 280 Hiltunen, Mursula, Rottensteiner, Wierenga, Kastaniotis, Gurvitz (bib76) 2003; 27 Luikenhuis, Perrone, Dawes, Grant (bib150) 1998; 9 Jamieson (bib4) 1998; 14 Martchenko, Alarco, Harcus, Whiteway (bib87) 2004; 15 Bellí, Polaina, Tamarit, de la Torre, Rodríguez-Manzaneque, Ros, Herrero (bib169) 2002; 277 Ohnishi (bib24) 1973; 301 Delaunay, Pflieger, Barrault, Vinh, Toledano (bib94) 2002; 111 Garcerá, Barreto, Piedrafita, Tamarit, Herrero (bib100) 2006; 398 Biswas, Chida, Rahman (bib11) 2006; 71 Vivancos, Jara, Zuin, Sansó, Hidalgo (bib234) 2006; 276 Giles, Stajich, Nichols, Gerrald, Alspaugh, Dietrich, Perfect (bib81) 2006; 5 Carroll, Outten, Proescher, Rosenfeld, Watson, Whitson, Hart, Jensen, Culotta (bib75) 2006; 281 Purdue, Lazarow (bib47) 2001; 17 Raha, Robinson (bib20) 2000; 25 Ikner, Shiozaki (bib196) 2005; 569 Temple, Perrone, Dawes (bib197) 2005; 15 Levin (bib252) 2005; 69 Rodriguez-Gabriel, Russell (bib242) 2005; 4 Guo, Lemire (bib40) 2003; 278 Tsuzi, Maeta, Takatsume, Izawa, Inoue (bib97) 2004; 569 Rodríguez-Manzaneque, Tamarit, Bellí, Ros, Herrero (bib166) 2002; 13 Moye-Rowley (bib214) 2002; 4 Ogusucu, Rettori, Munhoz, Netto, Augusto (bib108) 2007; 42 Gasch, Spellman, Kao (bib195) 2000; 11 Carmel-Harel, Storz (bib133) 2000; 54 Nakagawa, Kanbe, Mizuguchi (bib82) 2003; 47 Draculic, Dawes, Grant (bib155) 2000; 36 Morgan, Banks, Toone, Arit, Kuge, Johnston Carlioz (10.1016/j.bbagen.2007.12.004_bib127) 1986; 5 Singh (10.1016/j.bbagen.2007.12.004_bib204) 2004; 72 Okazaki (10.1016/j.bbagen.2007.12.004_bib230) 2005; 7 Filipits (10.1016/j.bbagen.2007.12.004_bib49) 1993; 132 Salmeen (10.1016/j.bbagen.2007.12.004_bib248) 2005; 7 Vivancos (10.1016/j.bbagen.2007.12.004_bib240) 2005; 102 Singer (10.1016/j.bbagen.2007.12.004_bib117) 1998; 150 Porras (10.1016/j.bbagen.2007.12.004_bib151) 2006; 281 Kho (10.1016/j.bbagen.2007.12.004_bib194) 2006; 348 Turrens (10.1016/j.bbagen.2007.12.004_bib19) 1997; 17 Rodríguez-Manzaneque (10.1016/j.bbagen.2007.12.004_bib168) 1999; 19 Veal (10.1016/j.bbagen.2007.12.004_bib229) 2003; 278 Longo (10.1016/j.bbagen.2007.12.004_bib70) 1996; 271 Furukawa (10.1016/j.bbagen.2007.12.004_bib74) 2006; 103 Demasi (10.1016/j.bbagen.2007.12.004_bib112) 2006; 273 Pinson (10.1016/j.bbagen.2007.12.004_bib218) 2000; 36 Irazusta (10.1016/j.bbagen.2007.12.004_bib128) 2006; 281 Tanaka (10.1016/j.bbagen.2007.12.004_bib98) 2005; 280 Whitbread (10.1016/j.bbagen.2007.12.004_bib185) 2005; 401 Turrens (10.1016/j.bbagen.2007.12.004_bib17) 2003; 552 Liu (10.1016/j.bbagen.2007.12.004_bib69) 1992; 267 Vilella (10.1016/j.bbagen.2007.12.004_bib254) 2005; 280 Jung (10.1016/j.bbagen.2007.12.004_bib38) 2001; 49 Cox (10.1016/j.bbagen.2007.12.004_bib86) 2003; 71 Alic (10.1016/j.bbagen.2007.12.004_bib253) 2003; 278 Fang (10.1016/j.bbagen.2007.12.004_bib29) 2003; 34 Delaunay (10.1016/j.bbagen.2007.12.004_bib94) 2002; 111 Maeta (10.1016/j.bbagen.2007.12.004_bib220) 2004; 24 Enjalbert (10.1016/j.bbagen.2007.12.004_bib84) 2007; 75 Lambert (10.1016/j.bbagen.2007.12.004_bib32) 2004; 279 Filipits (10.1016/j.bbagen.2007.12.004_bib77) 1993 Drakulic (10.1016/j.bbagen.2007.12.004_bib181) 2005; 5 Liu (10.1016/j.bbagen.2007.12.004_bib59) 2000; 97 Gralla (10.1016/j.bbagen.2007.12.004_bib68) 1991; 173 Teixeira (10.1016/j.bbagen.2007.12.004_bib154) 2004; 324 Scherens (10.1016/j.bbagen.2007.12.004_bib2) 2004; 5 Wood (10.1016/j.bbagen.2007.12.004_bib227) 2004; 430 Outten (10.1016/j.bbagen.2007.12.004_bib178) 2004; 279 Barford (10.1016/j.bbagen.2007.12.004_bib208) 2004; 14 Gan (10.1016/j.bbagen.2007.12.004_bib137) 1991; 266 Luk (10.1016/j.bbagen.2007.12.004_bib129) 2003; 100 Grant (10.1016/j.bbagen.2007.12.004_bib5) 2001; 39 Ostergaard (10.1016/j.bbagen.2007.12.004_bib180) 2004; 166 Wong (10.1016/j.bbagen.2007.12.004_bib111) 2004; 279 Nohl (10.1016/j.bbagen.2007.12.004_bib16) 2003; 31 Bellí (10.1016/j.bbagen.2007.12.004_bib169) 2002; 277 Hahn (10.1016/j.bbagen.2007.12.004_bib250) 2002; 277 Mukhopadhyay (10.1016/j.bbagen.2007.12.004_bib156) 2000; 275 Lin (10.1016/j.bbagen.2007.12.004_bib45) 2002; 418 Ohnishi (10.1016/j.bbagen.2007.12.004_bib24) 1973; 301 Vivancos (10.1016/j.bbagen.2007.12.004_bib234) 2006; 276 Cabiscol (10.1016/j.bbagen.2007.12.004_bib35) 2000; 275 Enjalbert (10.1016/j.bbagen.2007.12.004_bib83) 2003; 14 Summer (10.1016/j.bbagen.2007.12.004_bib191) 2005; 151 Moradas-Ferreira (10.1016/j.bbagen.2007.12.004_bib3) 1996; 19 Izawa (10.1016/j.bbagen.2007.12.004_bib78) 1996; 320 Larsson (10.1016/j.bbagen.2007.12.004_bib28) 1998; 14 Brombacher (10.1016/j.bbagen.2007.12.004_bib145) 2006; 23 Pedrajas (10.1016/j.bbagen.2007.12.004_bib110) 2000; 275 Martin (10.1016/j.bbagen.2007.12.004_bib136) 1995; 3 Toledano (10.1016/j.bbagen.2007.12.004_bib6) 2003; vol. 1 Gaits (10.1016/j.bbagen.2007.12.004_bib244) 1999; 10 Temple (10.1016/j.bbagen.2007.12.004_bib197) 2005; 15 Zheng (10.1016/j.bbagen.2007.12.004_bib209) 2000; 59 Halliwell (10.1016/j.bbagen.2007.12.004_bib18) 2004; 142 Bakker (10.1016/j.bbagen.2007.12.004_bib22) 2001; 25 Park (10.1016/j.bbagen.2007.12.004_bib106) 2000; 275 Molina-Navarro (10.1016/j.bbagen.2007.12.004_bib170) 2006; 580 Liu (10.1016/j.bbagen.2007.12.004_bib33) 2002; 80 Yamaguchi-Iwai (10.1016/j.bbagen.2007.12.004_bib162) 2002; 277 Gulshan (10.1016/j.bbagen.2007.12.004_bib226) 2005; 280 Ocón-Garrido (10.1016/j.bbagen.2007.12.004_bib144) 2002; 43 Hiltunen (10.1016/j.bbagen.2007.12.004_bib76) 2003; 27 Ghezzi (10.1016/j.bbagen.2007.12.004_bib10) 2005; 33 Cabiscol (10.1016/j.bbagen.2007.12.004_bib8) 2006 Bronzetti (10.1016/j.bbagen.2007.12.004_bib126) 2001; 496 Hancock (10.1016/j.bbagen.2007.12.004_bib123) 2000; 186 Martínez-Pastor (10.1016/j.bbagen.2007.12.004_bib79) 1996; 15 Ojeda (10.1016/j.bbagen.2007.12.004_bib160) 2006; 281 Biswas (10.1016/j.bbagen.2007.12.004_bib11) 2006; 71 Witte (10.1016/j.bbagen.2007.12.004_bib164) 2000; 275 Martin (10.1016/j.bbagen.2007.12.004_bib255) 2005; 58 van Loon (10.1016/j.bbagen.2007.12.004_bib65) 1986; 83 Zuin (10.1016/j.bbagen.2007.12.004_bib238) 2005; 280 Rodriguez-Gabriel (10.1016/j.bbagen.2007.12.004_bib242) 2005; 4 Furukawa (10.1016/j.bbagen.2007.12.004_bib73) 2004; 23 Wong (10.1016/j.bbagen.2007.12.004_bib107) 2002; 277 Izawa (10.1016/j.bbagen.2007.12.004_bib118) 2004; 64 Bearden (10.1016/j.bbagen.2007.12.004_bib131) 1999; 32 Field (10.1016/j.bbagen.2007.12.004_bib63) 2003 Enjalbert (10.1016/j.bbagen.2007.12.004_bib101) 2006; 17 Camaschella (10.1016/j.bbagen.2007.12.004_bib173) 2007; 110 Kanadia (10.1016/j.bbagen.2007.12.004_bib56) 1998; 45 Oien (10.1016/j.bbagen.2007.12.004_bib192) 2007; 32 Kox (10.1016/j.bbagen.2007.12.004_bib189) 2007; 1100 Carmel-Harel (10.1016/j.bbagen.2007.12.004_bib211) 2001; 39 Tamarit (10.1016/j.bbagen.2007.12.004_bib176) 2003; 278 Levin (10.1016/j.bbagen.2007.12.004_bib252) 2005; 69 Janakiraman (10.1016/j.bbagen.2007.12.004_bib132) 2000; 35 Schrader (10.1016/j.bbagen.2007.12.004_bib55) 2006; 1763 Castello (10.1016/j.bbagen.2007.12.004_bib57) 2006; 3 Martchenko (10.1016/j.bbagen.2007.12.004_bib87) 2004; 15 Molin (10.1016/j.bbagen.2007.12.004_bib221) 2007; 43 Hanbauer (10.1016/j.bbagen.2007.12.004_bib193) 2006; 40 Wingert (10.1016/j.bbagen.2007.12.004_bib172) 2005; 436 Purdue (10.1016/j.bbagen.2007.12.004_bib47) 2001; 17 Guo (10.1016/j.bbagen.2007.12.004_bib40) 2003; 278 Grant (10.1016/j.bbagen.2007.12.004_bib179) 1996; 29 Brihelius-Flohe (10.1016/j.bbagen.2007.12.004_bib89) 2006; 387 Le Moan (10.1016/j.bbagen.2007.12.004_bib146) 2006; 281 De Vries (10.1016/j.bbagen.2007.12.004_bib27) 1987; 895 Yamamoto (10.1016/j.bbagen.2007.12.004_bib207) 2007; 6 Jensen (10.1016/j.bbagen.2007.12.004_bib72) 2004; 279 Carroll (10.1016/j.bbagen.2007.12.004_bib75) 2006; 281 Toone (10.1016/j.bbagen.2007.12.004_bib235) 1998; 12 Giustarini (10.1016/j.bbagen.2007.12.004_bib53) 2004; 8 Overkamp (10.1016/j.bbagen.2007.12.004_bib25) 2000; 182 Grant (10.1016/j.bbagen.2007.12.004_bib88) 1998; 253 Ohmiya (10.1016/j.bbagen.2007.12.004_bib245) 1999; 125 Avery (10.1016/j.bbagen.2007.12.004_bib91) 2001; 276 Evans (10.1016/j.bbagen.2007.12.004_bib120) 2001; 85 Ikner (10.1016/j.bbagen.2007.12.004_bib196) 2005; 569 Forsburg (10.1016/j.bbagen.2007.12.004_bib1) 2001; 2 Lorenz (10.1016/j.bbagen.2007.12.004_bib102) 2003; 3 Krzepilko (10.1016/j.bbagen.2007.12.004_bib121) 2004; 38 Collinson (10.1016/j.bbagen.2007.12.004_bib152) 2002; 277 Toledano (10.1016/j.bbagen.2007.12.004_bib228) 2004; 29 Nguyen (10.1016/j.bbagen.2007.12.004_bib216) 2001; 276 Barreto (10.1016/j.bbagen.2007.12.004_bib186) 2006; 5 Potamitou (10.1016/j.bbagen.2007.12.004_bib143) 2002; 277 Han (10.1016/j.bbagen.2007.12.004_bib64) 2001; 353 Rodríguez-Manzaneque (10.1016/j.bbagen.2007.12.004_bib166) 2002; 13 Moskovitz (10.1016/j.bbagen.2007.12.004_bib190) 1997; 94 Kuge (10.1016/j.bbagen.2007.12.004_bib223) 2001; 21 Barros (10.1016/j.bbagen.2007.12.004_bib39) 2003; 35 Horsburgh (10.1016/j.bbagen.2007.12.004_bib130) 2002; 10 Azevedo (10.1016/j.bbagen.2007.12.004_bib219) 2003; 35 Choi (10.1016/j.bbagen.2007.12.004_bib210) 2001; 105 Greenall (10.1016/j.bbagen.2007.12.004_bib246) 2002; 13 Avery (10.1016/j.bbagen.2007.12.004_bib92) 2004; 279 Rahlfs (10.1016/j.bbagen.2007.12.004_bib175) 2001; 276 Muller (10.1016/j.bbagen.2007.12.004_bib183) 1996; 7 Wheeler (10.1016/j.bbagen.2007.12.004_bib134) 2004; 120 Wu (10.1016/j.bbagen.2007.12.004_bib213) 1994; 14 Fernandes (10.1016/j.bbagen.2007.12.004_bib15) 2004; 6 Moye-Rowley (10.1016/j.bbagen.2007.12.004_bib203) 2003; 2 Koc (10.1016/j.bbagen.2007.12.004_bib142) 2006; 281 Castillo (10.1016/j.bbagen.2007.12.004_bib237) 2002; 45 Collinson (10.1016/j.bbagen.2007.12.004_bib99) 2002; 277 Rand (10.1016/j.bbagen.2007.12.004_bib148) 2006; 17 Raha (10.1016/j.bbagen.2007.12.004_bib20) 2000; 25 Marres (10.1016/j.bbagen.2007.12.004_bib23) 1991; 195 Osorio (10.1016/j.bbagen.2007.12.004_bib36) 2003; 270 Munhoz (10.1016/j.bbagen.2007.12.004_bib109) 2004; 279 Gaits (10.1016/j.bbagen.2007.12.004_bib243) 1998; 12 Wormley (10.1016/j.bbagen.2007.12.004_bib205) 2005; 73 Halliwell (10.1016/j.bbagen.2007.12.004_bib7) 2007 Trotter (10.1016/j.bbagen.2007.12.004_bib147) 2002; 46 Gasch (10.1016/j.bbagen.2007.12.004_bib195) 2000; 11 Nguyen (10.1016/j.bbagen.2007.12.004_bib241) 1999; 13 Garcerá (10.1016/j.bbagen.2007.12.004_bib100) 2006; 398 Fridovich (10.1016/j.bbagen.2007.12.004_bib60) 1995; 64 Lewinska (10.1016/j.bbagen.2007.12.004_bib54) 2006; 11 Hayes (10.1016/j.bbagen.2007.12.004_bib153) 2005; 45 Ames (10.1016/j.bbagen.2007.12.004_bib51) 1981; 78 Collister (10.1016/j.bbagen.2007.12.004_bib251) 2002; 527 Orrenius (10.1016/j.bbagen.2007.12.004_bib42) 2007; 47 Lin (10.1016/j.bbagen.2007.12.004_bib43) 2006; 443 Lopreiato (10.1016/j.bbagen.2007.12.004_bib158) 2004; 377 Kuge (10.1016/j.bbagen.2007.12.004_bib212) 1994; 13 Vivancos (10.1016/j.bbagen.2007.12.004_bib233) 2004; 52 Slekar (10.1016/j.bbagen.2007.12.004_bib71) 1996; 271 Lee (10.1016/j.bbagen.2007.12.004_bib199) 1999; 274 Monteiro (10.1016/j.bbagen.2007.12.004_bib122) 2007; 104 Mukai (10.1016/j.bbagen.2007.12.004_bib124) 1988; 155 Stadtman (10.1016/j.bbagen.2007.12.004_bib188) 2005; 1703 Trotter (10.1016/j.bbagen.2007.12.004_bib140) 2005; 4 Dinis-Oliveira (10.1016/j.bbagen.2007.12.004_bib37) 2006; 27 Jeffery (10.1016/j.bbagen.2007.12.004_bib116) 2003; 19 Coleman (10.1016/j.bbagen.2007.12.004_bib224) 1999; 19 Schmitt (10.1016/j.bbagen.2007.12.004_bib41) 1996; 93 Vido (10.1016/j.bbagen.2007.12.004_bib200) 2001; 276 Chung (10.1016/j.bbagen.2007.12.004_bib177) 2005; 330 Wu (10.1016/j.bbagen.2007.12.004_bib113) 2007; 282 Stadtman (10.1016/j.bbagen.2007.12.004_bib52) 2003; 25 Nohl (10.1016/j.bbagen.2007.12.004_bib58 |
References_xml | – volume: 4 start-page: 123 year: 2002 end-page: 140 ident: bib214 article-title: Transcription factors regulating the response to oxidative stress in yeast publication-title: Antioxid. Redox Signal. – volume: 271 start-page: 28831 year: 1996 end-page: 28836 ident: bib71 article-title: The yeast Cu,Zn superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection publication-title: J. Biol. Chem. – volume: 277 start-page: 18914 year: 2002 end-page: 18918 ident: bib162 article-title: Subcellular localisation of Aft1 transcription factor responds to iron status in publication-title: J. Biol. Chem. – volume: 352 start-page: 750 year: 2007 end-page: 755 ident: bib80 article-title: Msn2p/Msn4p-activation is essential for the recovery from freezing stress in yeast publication-title: Biochem. Biophys. Res. Commun. – volume: 5 start-page: 1215 year: 2005 end-page: 1228 ident: bib181 article-title: Involvement of oxidative stress response genes in redox homeostasis, the level of reactive oxygen species, and ageing in publication-title: FEMS Yeast Res. – volume: 64 start-page: 1518 year: 2007 end-page: 1530 ident: bib157 article-title: Monothiol glutaredoxins: a common domain for multiple functions publication-title: Cell. Mol. Life Sci. – volume: 94 start-page: 9585 year: 1997 end-page: 9589 ident: bib190 article-title: The yeast peptide–methionine sulfoxide reductase functions as an antioxidant in vivo publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 268 start-page: 26699 year: 1993 end-page: 26703 ident: bib66 article-title: Absence of electron transport (Rho publication-title: J. Biol. Chem. – volume: 5 start-page: 1037 year: 2005 end-page: 1045 ident: bib48 article-title: Protein translocation machineries: how organelles bring in matrix proteins publication-title: FEMS Yeast Res. – volume: 71 start-page: 551 year: 2006 end-page: 564 ident: bib11 article-title: Redox modifications of protein thiols: emerging roles in cell signalling publication-title: Biochem. Pharmacol. – volume: 111 start-page: 471 year: 2002 end-page: 481 ident: bib94 article-title: A thiol peroxidase is an H publication-title: Cell – volume: 6 start-page: 1373 year: 2007 end-page: 1379 ident: bib207 article-title: Role of heat shock transcription factor in publication-title: Eukaryot. Cell – volume: 13 start-page: 1109 year: 2002 end-page: 1121 ident: bib166 article-title: Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes publication-title: Mol. Biol. Cell – volume: 19 start-page: 415 year: 2003 end-page: 417 ident: bib116 article-title: Moonlighting proteins: old proteins learning new tricks publication-title: Trends Genet. – volume: 40 start-page: 1391 year: 2006 end-page: 1396 ident: bib193 article-title: The yeast cytosolic thioredoxins are involved in the regulation of methionine sulfoxide reductase A publication-title: Free Rad. Biol. Med. – volume: 72 start-page: 2390 year: 2004 end-page: 2394 ident: bib204 article-title: SKN7 of publication-title: Infect. Immun. – volume: 83 start-page: 3820 year: 1986 end-page: 3824 ident: bib65 article-title: A yeast mutant lacking mitochondrial manganese–superoxide dismutase is hypersensitive to oxygen publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 173 start-page: 5918 year: 1991 end-page: 5920 ident: bib68 article-title: Null mutants of publication-title: J. Bacteriol. – volume: 580 start-page: 2273 year: 2006 end-page: 2280 ident: bib170 article-title: Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria publication-title: FEBS Lett. – volume: 273 start-page: 22480 year: 1998 end-page: 22489 ident: bib198 article-title: The H publication-title: J. Biol. Chem. – volume: 14 start-page: 679 year: 2004 end-page: 686 ident: bib208 article-title: The role of cysteine residues as redox-sensitive regulatory switches publication-title: Curr. Op. Struct. Biol. – volume: 4 start-page: 184 year: 2003 end-page: 188 ident: bib182 article-title: Non-reciprocal regulation of the redox state of the glutathione–glutaredoxin and thioredoxin systems publication-title: EMBO Rep. – volume: 569 start-page: 301 year: 2004 end-page: 306 ident: bib97 article-title: Distinct regulatory mechanism of yeast publication-title: FEBS Lett. – volume: 1763 start-page: 747 year: 2006 end-page: 758 ident: bib61 article-title: Activation of superoxide dismutases: putting the metal to the pedal publication-title: Biochim. Biophys. Acta – volume: 14 start-page: 5832 year: 1994 end-page: 5839 ident: bib213 publication-title: Mol. Cell. Biol. – volume: 22 start-page: 4815 year: 2003 end-page: 4825 ident: bib167 article-title: Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p publication-title: EMBO J. – reference: by oxidative stress is mediated by Yap1 and Skn7, FEBS Lett. 565 (2004) 148–154. – volume: 2 start-page: 659 year: 2001 end-page: 668 ident: bib1 article-title: The art and design of genetic screens: yeast publication-title: Nature Rev. Genet. – volume: 443 start-page: 787 year: 2006 end-page: 795 ident: bib43 article-title: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases publication-title: Nature – volume: 21 start-page: 8483 year: 2001 end-page: 8489 ident: bib26 article-title: Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in publication-title: Mol. Cell. Biol. – volume: 32 start-page: 403 year: 1999 end-page: 414 ident: bib131 article-title: The Yfe system of publication-title: Mol. Microbiol. – volume: 52 start-page: 1427 year: 2004 end-page: 1435 ident: bib233 article-title: Activation of the redox sensor Pap1 by hydrogen peroxide requires modulation of the intracellular oxidant concentration publication-title: Mol. Microbiol. – volume: 25 start-page: 15 year: 2001 end-page: 17 ident: bib22 article-title: Stoichiometry and compartmentation of NADH metabolism in publication-title: FEMS Microbiol. Rev. – volume: 527 start-page: 186 year: 2002 end-page: 192 ident: bib251 publication-title: FEBS Lett. – volume: 552 start-page: 335 year: 2003 end-page: 344 ident: bib17 article-title: Mitochondrial formation of reactive oxygen species publication-title: J. Physiol. – volume: 15 start-page: 456 year: 2004 end-page: 467 ident: bib87 article-title: Superoxide dismutases in publication-title: Mol. Biol. Cell – volume: 16 start-page: 1035 year: 1997 end-page: 1044 ident: bib202 article-title: The Skn7 response regulator controls gene expressión in the oxidative stress response of the budding yeast publication-title: EMBO J. – volume: 5 start-page: 623 year: 1986 end-page: 630 ident: bib127 article-title: Isolation of superoxide dismutase mutants in publication-title: EMBO J. – volume: 282 start-page: 2184 year: 2007 end-page: 2195 ident: bib113 article-title: Regulation of the yeast TSA1 peroxiredoxin by ZAP1 is an adaptive response to the oxidative stress of zinc deficiency publication-title: J. Biol. Chem. – volume: 430 start-page: 917 year: 2004 end-page: 921 ident: bib227 article-title: Structural basis for redox regulation of Yap1 transcription factor localization publication-title: Nature – volume: 35 start-page: 179 year: 2003 end-page: 188 ident: bib39 article-title: H publication-title: Free Radic. Biol. Med. – volume: 47 start-page: 143 year: 2007 end-page: 183 ident: bib42 article-title: Mitochondrial oxidative stress: implications for cell death publication-title: Annu. Rev. Pharmacol. Toxicol. – volume: 21 start-page: 6139 year: 2001 end-page: 6150 ident: bib223 article-title: Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation publication-title: Mol. Cell. Biol. – volume: 73 start-page: 5022 year: 2005 end-page: 5030 ident: bib205 article-title: Identification and characterization of an publication-title: Infect. Immun. – volume: 273 start-page: 805 year: 2006 end-page: 816 ident: bib112 article-title: Yeast oxidative stress response: influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state publication-title: FEBS J. – volume: 29 start-page: 511 year: 1996 end-page: 515 ident: bib179 article-title: Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast publication-title: Curr. Genet. – volume: 279 start-page: 46652 year: 2004 end-page: 46658 ident: bib92 article-title: Genetic dissection of the phospholipids hydroperoxidase activity of yeast Gpx3 reveals its functional importance publication-title: J. Biol. Chem. – volume: 280 start-page: 40524 year: 2005 end-page: 40533 ident: bib226 article-title: Oxidant-specific folding of Yap1p regulates both transcriptional activation and nuclear localization publication-title: J. Biol. Chem. – volume: 277 start-page: 18561 year: 2002 end-page: 18567 ident: bib143 article-title: Protein levels of publication-title: J. Biol. Chem. – volume: 42 start-page: 1008 year: 2007 end-page: 1016 ident: bib141 article-title: Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast publication-title: Free Rad. Biol. Med. – volume: 242 start-page: 1 year: 1998 end-page: 9 ident: bib9 article-title: Recent trends in glutathione biochemistry-glutathione–protein interactions: a molecular link between oxidative stress and cell proliferation? publication-title: Biochem. Biophys. Res. Commun. – volume: 387 start-page: 1385 year: 2006 end-page: 1397 ident: bib12 article-title: Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways publication-title: Biol. Chem. – volume: 279 start-page: 23207 year: 2004 end-page: 23213 ident: bib111 article-title: Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable publication-title: J. Biol. Chem. – volume: 25 start-page: 207 year: 2003 end-page: 218 ident: bib52 article-title: Free radical-mediated oxidation of free amino acids and amino acid residues in proteins publication-title: Amino Acids – volume: 275 start-page: 1902 year: 2000 end-page: 1909 ident: bib164 article-title: Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interaction protein with a thioredoxin homology domain publication-title: J. Biol. Chem. – volume: 43 start-page: 136 year: 2007 end-page: 144 ident: bib221 article-title: Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast publication-title: Free Rad. Biol. Med. – volume: 5 start-page: 1748 year: 2006 end-page: 1759 ident: bib186 article-title: A peroxisomal glutathione transferase of publication-title: Eukaryot. Cell – volume: 270 start-page: 1578 year: 2003 end-page: 1589 ident: bib36 article-title: H publication-title: Eur. J. Biochem. – volume: 398 start-page: 187 year: 2006 end-page: 196 ident: bib100 publication-title: Biochem. J. – volume: 278 start-page: 25745 year: 2003 end-page: 25751 ident: bib176 article-title: Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin publication-title: J. Biol. Chem. – year: 2007 ident: bib7 article-title: Free Radicals in Biology and Medicine – volume: 45 start-page: 51 year: 2005 end-page: 88 ident: bib153 article-title: Glutathione transferases publication-title: Annu. Rev. Pharmacol. Toxicol. – volume: 186 start-page: 245 year: 2000 end-page: 250 ident: bib123 article-title: Biosynthesis of publication-title: FEMS Microbiol. Lett. – volume: 3 start-page: 1076 year: 2003 end-page: 1087 ident: bib102 article-title: Transcriptional response of publication-title: Eukaryot. Cell – volume: 110 start-page: 1353 year: 2007 end-page: 1358 ident: bib173 article-title: The human counterpart of zebrafish publication-title: Blood – volume: 11 start-page: 2335 year: 2000 end-page: 2347 ident: bib201 article-title: The Skn7 response regulator of publication-title: Mol. Biol. Cell – volume: 7 start-page: 560 year: 2005 end-page: 577 ident: bib248 article-title: Functions and mechanisms of redox regulation of cysteine-based phosphatases publication-title: Antioxid. Redox Signal. – volume: 17 start-page: 3 year: 1997 end-page: 8 ident: bib19 article-title: Superoxide production by the mitochondrial respiratory chain publication-title: Biosci. Rep. – volume: 279 start-page: 29938 year: 2004 end-page: 29943 ident: bib72 article-title: Mutations in publication-title: J. Biol. Chem. – volume: 13 start-page: 655 year: 1994 end-page: 664 ident: bib212 publication-title: EMBO J. – volume: 277 start-page: 16712 year: 2002 end-page: 16717 ident: bib152 article-title: Role of yeast glutaredoxins as glutathione publication-title: J. Biol. Chem. – volume: 16 start-page: 1710 year: 1997 end-page: 1720 ident: bib215 article-title: Regulation of yAP-1 nuclear localization in response to oxidative stress publication-title: EMBO J. – volume: 6 start-page: 652 year: 2006 end-page: 661 ident: bib206 article-title: The Skn7 response regulator of publication-title: FEMS Yeast Res. – volume: 280 start-page: 23319 year: 2005 end-page: 23327 ident: bib239 article-title: Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide publication-title: J. Biol. Chem. – volume: 5 start-page: 229 year: 2004 ident: bib2 article-title: The uses of genome-wide mutant collections publication-title: Genome Biol. – volume: 34 start-page: 478 year: 2003 end-page: 488 ident: bib29 article-title: External alternative NADH dehydrogenase of publication-title: Free Radic. Biol. Med. – volume: 29 start-page: 351 year: 2004 end-page: 357 ident: bib228 article-title: Microbial H publication-title: Trends Biochem. Sci. – volume: 254 start-page: 13963 year: 1989 end-page: 13966 ident: bib14 article-title: Thioredoxin and glutaredoxin systems publication-title: J. Biol. Chem. – volume: 401 start-page: 77 year: 2005 end-page: 99 ident: bib185 article-title: Characterization of the Omega-class of glutathione transferases publication-title: Methods Enzymol. – volume: 281 start-page: 16551 year: 2006 end-page: 16562 ident: bib151 article-title: One single in-frame AUG codon is responsible for a diversity of subcellular localizations for glutaredoxin 2 in publication-title: J. Biol. Chem. – volume: 104 start-page: 4886 year: 2007 end-page: 4891 ident: bib122 article-title: Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 32 start-page: 603 year: 2007 end-page: 606 ident: bib192 article-title: Protein-carbonyl accumulation in the non-replicative senescence of the methionine sulfoxide reductase A ( publication-title: Amino Acids – volume: 31 start-page: 1308 year: 2003 end-page: 1311 ident: bib16 article-title: Cell respiration and formation of reactive oxygen species: facts and artefacts publication-title: Biochem. Soc. Trans. – volume: 253 start-page: 893 year: 1998 end-page: 898 ident: bib88 article-title: Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast publication-title: Biochem. Biophys. Res. Commun. – volume: 46 start-page: 869 year: 2002 end-page: 878 ident: bib147 article-title: Thioredoxins are required for protection against a reductive stress in the yeast publication-title: Mol. Microbiol. – volume: 1703 start-page: 135 year: 2005 end-page: 140 ident: bib188 article-title: Methionine oxidation and aging publication-title: Biochim. Biophys. Acta – volume: 17 start-page: 701 year: 2001 end-page: 752 ident: bib47 article-title: Peroxisome biogenesis publication-title: Annu. Rev. Cell Dev. Biol. – volume: 38 start-page: 1543 year: 2005 end-page: 1552 ident: bib105 article-title: Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signalling publication-title: Free Rad. Biol. Med. – volume: 32 start-page: 163 year: 1998 end-page: 184 ident: bib135 article-title: The genetics of disulphide bond metabolism publication-title: Annu. Rev. Genet. – volume: 155 start-page: 1046 year: 1988 end-page: 1050 ident: bib124 article-title: Kinetic study of the reaction between vitamin E radical and alkyl hydroperoxides in solution publication-title: Biochem. Biophys. Res. Commun. – volume: 275 start-page: 16296 year: 2000 end-page: 16301 ident: bib110 article-title: Mitochondria of publication-title: J. Biol. Chem. – volume: 57 start-page: 1318 year: 2005 end-page: 1341 ident: bib119 article-title: The moonlighting protein Tsa1p is implicated in oxidative stress response and in cell wall biogenesis in publication-title: Mol. Microbiol. – volume: 279 start-page: 31983 year: 2004 end-page: 31989 ident: bib46 article-title: Oxidative damage to specific proteins in replicative and chronological-aged publication-title: J. Biol. Chem. – volume: 276 start-page: 1138 year: 2001 end-page: 1145 ident: bib216 article-title: Multiple Yap1p-binding sites mediate induction of the yeast major facilitator FLR1 gene in response to drugs, oxidants, and alkylating agents publication-title: J. Biol. Chem. – volume: 97 start-page: 4672 year: 2000 end-page: 4676 ident: bib59 article-title: Protection from nitrosative stress by yeast flavohemoglobin publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 11 start-page: 4241 year: 2000 end-page: 4257 ident: bib195 article-title: Genomic expression programs in the response of yeast cells to environmental changes publication-title: Mol. Biol. Cell – volume: 25 start-page: 502 year: 2000 end-page: 508 ident: bib20 article-title: Mitochondria, oxygen free radicals, disease and ageing publication-title: Trends Biochem. Sci. – volume: 195 start-page: 857 year: 1991 end-page: 862 ident: bib23 article-title: Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from publication-title: Eur. J. Biochem. – volume: 279 start-page: 7785 year: 2004 end-page: 7791 ident: bib178 article-title: Alternative start sites in the publication-title: J. Biol. Chem. – volume: 27 start-page: 1110 year: 2006 end-page: 1122 ident: bib37 article-title: Paraquat exposure as an etiological factor of Parkinson's disease publication-title: Neurotoxicology – volume: 42 start-page: 326 year: 2007 end-page: 334 ident: bib108 article-title: Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics publication-title: Free Rad. Biol. Med. – volume: 348 start-page: 25 year: 2006 end-page: 35 ident: bib194 article-title: Glutathione peroxidase 3 of publication-title: Biochem. Biophys. Res. Commun. – volume: 100 start-page: 10353 year: 2003 end-page: 10357 ident: bib129 article-title: Manganese activation of superoxide dismutase 2 in publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 281 start-page: 17661 year: 2006 end-page: 17669 ident: bib160 article-title: Role of glutaredoxin-3 and glutaredoxin-4 in the iron-regulation of the Aft1 transcriptional activator in publication-title: J. Biol. Chem. – volume: 12 start-page: 1453 year: 1998 end-page: 1463 ident: bib235 article-title: Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (exportin) and the stress-activated MAP kinase Sty1/Spc1 publication-title: Genes Dev. – volume: 43 start-page: 993 year: 2002 end-page: 1003 ident: bib144 article-title: Role of thioredoxins in the response of publication-title: Mol. Microbiol. – volume: 279 start-page: 51923 year: 2004 end-page: 51930 ident: bib159 article-title: Nuclear monothiol glutaredoxins of publication-title: J. Biol. Chem. – volume: 102 start-page: 8875 year: 2005 end-page: 8880 ident: bib240 article-title: A cysteine–sulfinic acid in peroxiredoxin regulates H publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 279 start-page: 39414 year: 2004 end-page: 39420 ident: bib32 article-title: Inhibitors of the quinone binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) publication-title: J. Biol. Chem. – volume: 28 start-page: 32 year: 2003 end-page: 40 ident: bib104 article-title: Structure, mechanism and regulation of peroxiredoxins publication-title: Trends Biochem. Sci. – volume: 36 start-page: 679 year: 2000 end-page: 687 ident: bib218 article-title: Identification of genes affecting selenite toxicity and resistance in publication-title: Mol. Microbiol. – volume: 266 start-page: 9194 year: 1991 end-page: 9202 ident: bib139 article-title: Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle publication-title: J. Biol. Chem. – volume: 425 start-page: 686 year: 2003 end-page: 691 ident: bib95 article-title: Global analysis of protein localization in budding yeast publication-title: Nature – volume: 27 start-page: 35 year: 2003 end-page: 64 ident: bib76 article-title: The biochemistry of peroxisomal beta-oxidation in the yeast publication-title: FEMS Microbiol. Rev. – volume: 281 start-page: 12227 year: 2006 end-page: 12232 ident: bib128 article-title: Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia publication-title: J. Biol. Chem. – volume: 45 start-page: 243 year: 2002 end-page: 254 ident: bib237 article-title: Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues publication-title: Mol. Microbiol. – volume: 278 start-page: 41849 year: 2003 end-page: 41855 ident: bib253 article-title: Lipid hydroperoxides activate the mitogen-activated protein kinase Mpk1p in publication-title: J. Biol. Chem. – volume: 125 start-page: 1061 year: 1999 end-page: 1066 ident: bib245 article-title: A fission yeast gene ( publication-title: J. Biochem. – volume: 387 start-page: 1329 year: 2006 end-page: 1335 ident: bib89 article-title: Glutathione peroxidases and redox-regulated transcription factors publication-title: Biol. Chem. – volume: 5 start-page: 1447 year: 2006 end-page: 1459 ident: bib81 article-title: The publication-title: Eukaryot. Cell – volume: 274 start-page: 27002 year: 1999 end-page: 27009 ident: bib90 article-title: Genetic analysis of glutathione peroxidase in oxidative stress response of publication-title: J. Biol. Chem. – volume: 19 start-page: 651 year: 1996 end-page: 658 ident: bib3 article-title: The molecular defences against reactive oxygen species in yeast publication-title: Mol. Microbiol. – volume: 99 start-page: 307 year: 2006 end-page: 314 ident: bib165 article-title: PICOT inhibits cardiac hypertrophy and enhances ventricular function and cardiomyocyte contractility publication-title: Circ. Res. – volume: 274 start-page: 16040 year: 1999 end-page: 16046 ident: bib199 article-title: Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast publication-title: J. Biol. Chem. – volume: 14 start-page: 1511 year: 1998 end-page: 1527 ident: bib4 article-title: Oxidative stress responses of yeast publication-title: Yeast – volume: 119 start-page: 4554 year: 2006 end-page: 4564 ident: bib161 article-title: Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in publication-title: J. Cell Sci. – volume: 179 start-page: 9 year: 2003 end-page: 16 ident: bib34 article-title: Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation publication-title: Exp. Neurol. – volume: 275 start-page: 24800 year: 2000 end-page: 24806 ident: bib184 article-title: Identification, characterization, and crystal structure of the omega class glutathione transferases publication-title: J. Biol. Chem. – volume: 64 start-page: 97 year: 1995 end-page: 112 ident: bib60 article-title: Superoxide radical and superoxide dismutases publication-title: Annu. Rev. Biochem. – volume: 6 start-page: 63 year: 2004 end-page: 74 ident: bib15 article-title: Glutaredoxins: glutathione-dependent redox enzymes with functions as far beyond a simple thioredoxin backup system publication-title: Antioxid. Redox Signal – volume: 271 start-page: 627 year: 2004 end-page: 637 ident: bib93 article-title: Reverse genetic analysis of the glutathione metabolic pathway suggests a novel role of publication-title: Mol. Gen. Genomics – volume: 14 start-page: 214 year: 2003 end-page: 229 ident: bib231 article-title: Global transcriptional responses of fission yeast to environmental stress publication-title: Mol. Biol. Cell – volume: 23 start-page: 741 year: 2006 end-page: 750 ident: bib145 article-title: The role of Yap1p and Skn7p-mediated oxidative stress response in the defence of publication-title: Yeast – volume: 156 start-page: 435 year: 1976 end-page: 444 ident: bib30 article-title: Role of ubiquinone in the mitochondrial generation of hydrogen peroxide publication-title: Biochem. J. – volume: 17 start-page: 1018 year: 2006 end-page: 1032 ident: bib101 article-title: Role of the Hog1 stress-activated protein kinase in the global transcriptional response to stress in the fungal pathogen publication-title: Mol. Biol. Cell – volume: 10 start-page: 1395 year: 1999 end-page: 1407 ident: bib244 article-title: Active nucleocytoplasmic shuttling required for function and regulation of stress-activated kinase Spc1/StyI in fission yeast publication-title: Mol. Biol. Cell – volume: 10 start-page: 281 year: 2005 end-page: 286 ident: bib58 article-title: The existence and significance of a mitochondrial nitrite reductase publication-title: Redox Rep. – volume: 85 start-page: S67 year: 2001 end-page: S74 ident: bib120 article-title: Micronutrients: oxidant/antioxidant status publication-title: Br. J. Nutr. – volume: 281 start-page: 10420 year: 2006 end-page: 10430 ident: bib146 article-title: The publication-title: J. Biol. Chem. – volume: 57 start-page: 1685 year: 2006 end-page: 1696 ident: bib163 article-title: Genome-wide analysis of plant glutaredoxin systems publication-title: J. Exp. Bot. – volume: 277 start-page: 37590 year: 2002 end-page: 37596 ident: bib169 article-title: Structure–function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein publication-title: J. Biol. Chem. – volume: 275 start-page: 21149 year: 2000 end-page: 21157 ident: bib156 article-title: Purification and characterization of Acr2p, the publication-title: J. Biol. Chem. – volume: 2 start-page: 381 year: 2003 end-page: 389 ident: bib203 article-title: Regulation of the transcriptional response to oxidative stress in fungi: similarities and differences publication-title: Eukaryot. Cell – volume: 120 start-page: 12 year: 2004 end-page: 20 ident: bib134 article-title: Regulation of redox homeostasis in the yeast publication-title: Physiol. Plant. – volume: 151 start-page: 2573 year: 2005 end-page: 2581 ident: bib103 article-title: Two glutathione peroxidases in the fungal pathogen publication-title: Microbiology – volume: 280 start-page: 9149 year: 2005 end-page: 9159 ident: bib254 article-title: Pkc1 and the upstream elements of the cell integrity pathway in publication-title: J. Biol. Chem. – volume: 23 start-page: 2872 year: 2004 end-page: 2881 ident: bib73 article-title: Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS publication-title: EMBO J. – volume: 142 start-page: 231 year: 2004 end-page: 255 ident: bib18 article-title: Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? publication-title: Br. J. Pharmacol. – start-page: 247 year: 2006 end-page: 281 ident: bib8 publication-title: Oxidative Damage to Proteins: Structural Modifications and Consequences in Cell Function, Redox Proteomics – volume: 35 start-page: 1146 year: 2000 end-page: 1155 ident: bib132 article-title: The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of publication-title: Mol. Microbiol. – volume: 17 start-page: 387 year: 2006 end-page: 401 ident: bib148 article-title: The thioredoxin system protects ribosomes against stress-induced aggregation publication-title: Mol. Biol. Cell – volume: 14 start-page: 1460 year: 2003 end-page: 1467 ident: bib83 article-title: Stress-induced gene expression in publication-title: Mol. Biol. Cell – volume: 447 start-page: 487 year: 2007 end-page: 492 ident: bib249 article-title: Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases publication-title: Nature – volume: 274 start-page: 15151 year: 1999 end-page: 15158 ident: bib236 article-title: A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1 publication-title: J. Biol. Chem. – volume: 496 start-page: 105 year: 2001 end-page: 115 ident: bib126 article-title: Protective effects of vitamins and selenium compounds in yeast publication-title: Mutat. Res. – volume: 274 start-page: 6566 year: 1999 end-page: 6573 ident: bib138 article-title: Identification and functional characterization of a novel mitochondrial thioredoxin system in publication-title: J. Biol. Chem. – volume: 278 start-page: 47629 year: 2003 end-page: 47635 ident: bib40 article-title: The ubiquinone-binding site of the publication-title: J. Biol. Chem. – start-page: 28052 year: 2003 end-page: 28059 ident: bib63 article-title: Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria publication-title: J. Biol. Chem. – volume: 436 start-page: 1035 year: 2005 end-page: 1039 ident: bib172 article-title: Deficiency of glutaredoxin 5 reveals Fe–S clusters are required for vertebrate haem synthesis publication-title: Nature – volume: 59 start-page: 1 year: 2000 end-page: 6 ident: bib209 article-title: Redox sensing by prokaryotic transcription factors publication-title: Biochem. Pharmacol. – volume: 581 start-page: 3598 year: 2007 end-page: 3607 ident: bib149 article-title: The system biology of thiol redox system in publication-title: FEBS Lett. – volume: 280 start-page: 36708 year: 2005 end-page: 36713 ident: bib238 article-title: The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in publication-title: J. Biol. Chem. – volume: 9 start-page: 1081 year: 1998 end-page: 1091 ident: bib150 article-title: The yeast publication-title: Mol. Biol. Cell – volume: 324 start-page: 1101 year: 2004 end-page: 1107 ident: bib154 article-title: The herbicide 2,4-dichlorophenoxyacetic acid induces the generation of free-radicals and associated oxidative stress responses in yeast publication-title: Biochem. Biophys. Res. Commun. – volume: 277 start-page: 5385 year: 2002 end-page: 5394 ident: bib107 article-title: Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress publication-title: J. Biol. Chem. – volume: 19 start-page: 8180 year: 1999 end-page: 8190 ident: bib168 article-title: Grx5 glutaredoxin plays a central role in protection against oxidative damage in publication-title: Mol. Cell. Biol. – volume: 11 start-page: 231 year: 2006 end-page: 239 ident: bib54 article-title: Yeast flavohemoglobin protects against nitrosative stress and controls ferric reductase activity publication-title: Redox Rep. – volume: 105 start-page: 103 year: 2001 end-page: 113 ident: bib210 article-title: Structural basis of the redox switch in the OxyR transcription factor publication-title: Cell – volume: 78 start-page: 6858 year: 1981 end-page: 6862 ident: bib51 article-title: Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 271 start-page: 12275 year: 1996 end-page: 12280 ident: bib70 article-title: Superoxide dismutase activity is essential for stationary phase survival in publication-title: J. Biol. Chem. – volume: 24 start-page: 8753 year: 2004 end-page: 8764 ident: bib220 article-title: Activity of the Yap1 transcription factor in publication-title: Mol. Cell. Biol. – volume: 1100 start-page: 383 year: 2007 end-page: 386 ident: bib189 article-title: Methionine sulfoxide reduction and the aging process publication-title: Ann. N.Y. Acad. Sci. – volume: 275 start-page: 27393 year: 2000 end-page: 27398 ident: bib35 article-title: Oxidative stress promotes specific protein damage in publication-title: J. Biol. Chem. – volume: 15 start-page: 319 year: 2005 end-page: 326 ident: bib197 article-title: Complex cellular responses to reactive oxygen species publication-title: Trends Cell Biol. – volume: 3 start-page: 277 year: 2006 end-page: 287 ident: bib57 article-title: Mitochondrial cytochrome oxidase produces nitric oxide under hypoxic conditions: implications for oxygen sensing and hypoxic signalling in eukaryotes publication-title: Cell Metab. – reference: D. Tsuzi, K. Maeta, Y. Takatsume, S. Igawa, Y. Inoue, Regulation of the yeast phospholipid hydroperoxide glutathione peroxidase – volume: 13 start-page: 2977 year: 2002 end-page: 2989 ident: bib246 article-title: Role of fission yeast Tup1-like repressors and Prr1 transcription factor in response to salt stress publication-title: Mol. Biol. Cell – volume: 32 start-page: 609 year: 2000 end-page: 615 ident: bib31 article-title: Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria publication-title: J. Bioenerg. Biomembr. – volume: 80 start-page: 780 year: 2002 end-page: 787 ident: bib33 article-title: Generation of reactive oxygen species by the mitochondrial electron transport publication-title: J. Neurochem. – volume: 27 start-page: 133 year: 1998 end-page: 164 ident: bib247 article-title: The structure and mechanism of protein phosphatases: insights into catalysis and regulation publication-title: Annu. Rev. Biophys. Biomol. Struct. – volume: 895 start-page: 205 year: 1987 end-page: 239 ident: bib27 article-title: The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism publication-title: Biochim. Biophys. Acta – volume: 1763 start-page: 1755 year: 2006 end-page: 1766 ident: bib55 article-title: Peroxisomes and oxidative stress publication-title: Biochim. Biophys. Acta – volume: 103 start-page: 7148 year: 2006 end-page: 7153 ident: bib74 article-title: Disulfide cross-linked protein represents a significant fraction of ALS-associated SOD1 aggregates in spinal cords of model mice publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 54 start-page: 439 year: 2000 end-page: 461 ident: bib133 article-title: Roles of the glutathione- and thioredoxin-dependent systems in the publication-title: Annu. Rev. Microbiol. – volume: 4 start-page: 1396 year: 2005 end-page: 1402 ident: bib242 article-title: Distinct signaling pathways respond to arsenite and reactive oxygen species in publication-title: Eukaryot. Cell – volume: 277 start-page: 21278 year: 2002 end-page: 21284 ident: bib250 article-title: Regulation of the publication-title: J. Biol. Chem. – volume: 280 start-page: 42078 year: 2005 end-page: 42087 ident: bib98 publication-title: J. Biol. Chem. – volume: 7 start-page: 348 year: 2005 end-page: 366 ident: bib13 article-title: Glutaredoxin: role in reversible protein publication-title: Antioxid. Redox Signal. – volume: 58 start-page: 6 year: 2005 end-page: 16 ident: bib255 article-title: Protein phosphatases in MAPK signalling: we keep learning from yeast publication-title: Mol. Microbiol. – volume: 19 start-page: 5157 year: 2000 end-page: 5166 ident: bib225 article-title: H2O2 sensing through oxidation of the Yap1 transcription factor publication-title: EMBO J. – volume: 4 start-page: 392 year: 2005 end-page: 400 ident: bib140 article-title: Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast publication-title: Eukaryot. Cell – volume: 569 start-page: 13 year: 2005 end-page: 27 ident: bib196 article-title: Yeast signalling pathways in the oxidative stress response publication-title: Mutat. Res. – volume: 276 start-page: 8469 year: 2001 end-page: 8474 ident: bib200 article-title: A proteome analysis of the cadmium response in publication-title: J. Biol. Chem. – volume: 275 start-page: 5723 year: 2000 end-page: 5732 ident: bib106 article-title: Distinct physiological functions of thiol peroxidase isoenzymes in publication-title: J. Biol. Chem. – volume: vol. 1 start-page: 241 year: 2003 end-page: 303 ident: bib6 publication-title: Oxidative Stress Responses in Yeast, Topics in Current Genetics, Yeast Stress Responses – volume: 377 start-page: 395 year: 2004 end-page: 405 ident: bib158 article-title: Analysis of the interaction between piD261/Bud32, an evolutionary conserved protein kinase of publication-title: Biochem. J. – volume: 38 start-page: 1019 year: 2004 end-page: 1024 ident: bib121 article-title: Ascorbate restores lifespan of superoxide–dismutase deficient yeast publication-title: Free Radic. Res. – volume: 3 start-page: 245 year: 1995 end-page: 250 ident: bib136 article-title: Thioredoxin—a fold for all reasons publication-title: Structure – volume: 33 start-page: 1378 year: 2005 end-page: 1381 ident: bib10 article-title: Oxidoreduction of protein thiols in redox regulation publication-title: Biochem. Soc. Trans. – volume: 36 start-page: 1167 year: 2000 end-page: 1174 ident: bib155 article-title: A single glutaredoxin or thioredoxin is essential for viability in the yeast publication-title: Mol. Microbiol. – volume: 49 start-page: 87 year: 2001 end-page: 105 ident: bib38 article-title: Mitochondria as subcellular targets for clinically useful anthracyclines publication-title: Adv. Drug Deliv. Rev. – volume: 35 start-page: 889 year: 2003 end-page: 900 ident: bib219 article-title: Two redox centers within Yap1 for H publication-title: Free Radic. Biol. Med. – volume: 117 start-page: 625 year: 2004 end-page: 635 ident: bib115 article-title: Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function publication-title: Cell – volume: 12 start-page: 1464 year: 1998 end-page: 1473 ident: bib243 article-title: Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast publication-title: Genes Dev. – volume: 31 start-page: 347 year: 1999 end-page: 366 ident: bib21 article-title: Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity and relation to aging and longevity publication-title: Bioenerg. Biomembr. – volume: 278 start-page: 30896 year: 2003 end-page: 30904 ident: bib229 article-title: Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor publication-title: J. Biol. Chem. – volume: 277 start-page: 16712 year: 2002 end-page: 16717 ident: bib99 article-title: The yeast glutaredoxins are active as glutathione peroxidases publication-title: J. Biol. Chem. – volume: 135 start-page: 219 year: 2002 end-page: 228 ident: bib114 article-title: Alkyl hydroperoxide reductase 1 protects publication-title: Toxicol. Lett. – volume: 150 start-page: 613 year: 1998 end-page: 632 ident: bib117 article-title: Identification of high-copy disrupters of telomeric silencing in publication-title: Genetics – volume: 64 start-page: 1373 year: 2007 end-page: 1394 ident: bib50 article-title: Physiological functions of publication-title: Cell. Mol. Life Sci. – volume: 281 start-page: 28648 year: 2006 end-page: 28656 ident: bib75 article-title: The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase publication-title: J. Biol. Chem. – volume: 64 start-page: 120 year: 2004 end-page: 124 ident: bib118 article-title: Nuclear thioredoxin peroxidase Dot5 in publication-title: Appl. Microbiol. Biotechnol. – volume: 266 start-page: 1692 year: 1991 end-page: 1696 ident: bib137 article-title: Yeast thioredoxin genes publication-title: J. Biol. Chem. – volume: 8 start-page: 201 year: 2004 end-page: 212 ident: bib53 publication-title: J. Cell. Mol. Med. – volume: 320 start-page: 61 year: 1996 end-page: 67 ident: bib78 article-title: Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasemic publication-title: J. Biochem. – volume: 1703 start-page: 213 year: 2005 end-page: 219 ident: bib187 article-title: Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases publication-title: Biochim. Biophys. Acta – volume: 71 start-page: 173 year: 2003 end-page: 180 ident: bib86 article-title: Superoxide dismutase influences the virulence of publication-title: Infect. Immun. – volume: 151 start-page: 1939 year: 2005 end-page: 1948 ident: bib191 article-title: Oxidative protein damage causes chromium toxicity in yeast publication-title: Microbiology – volume: 69 start-page: 262 year: 2005 end-page: 291 ident: bib252 article-title: Cell wall integrity signaling in publication-title: Microbiol. Mol. Biol. Rev. – volume: 13 start-page: 1653 year: 1999 end-page: 1663 ident: bib241 article-title: Heat–shock-induced activation of stress MAP kinase is regulated by threonine- and tyrosine-specific phosphatases publication-title: Genes Dev. – volume: 7 start-page: 1805 year: 1996 end-page: 1813 ident: bib183 article-title: A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth publication-title: Mol. Biol. Cell – volume: 276 start-page: 495 year: 2006 end-page: 502 ident: bib234 article-title: Oxidative stress in publication-title: Mol. Genet. Genomics – volume: 17 start-page: 7416 year: 1998 end-page: 7429 ident: bib222 article-title: Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor publication-title: EMBO J. – volume: 143 start-page: 1649 year: 1997 end-page: 1656 ident: bib67 article-title: Mitochondrial superoxide dismutase is essential for ethanol tolerance of publication-title: Microbiology – volume: 15 start-page: 2227 year: 1996 end-page: 2235 ident: bib79 article-title: The publication-title: EMBO J. – volume: 132 start-page: 49 year: 1993 end-page: 55 ident: bib49 article-title: A publication-title: Gene – volume: 273 start-page: 59 year: 1996 end-page: 63 ident: bib44 article-title: Oxidative stress, caloric restriction, and aging publication-title: Science – volume: 353 start-page: 411 year: 2001 end-page: 416 ident: bib64 article-title: Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space publication-title: Biochem. J. – volume: 10 start-page: 496 year: 2002 end-page: 501 ident: bib130 article-title: Manganese: elemental defence for a life with oxygen publication-title: Trends Microbiol. – volume: 39 start-page: 533 year: 2001 end-page: 541 ident: bib5 article-title: Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions publication-title: Mol. Microbiol. – volume: 166 start-page: 337 year: 2004 end-page: 345 ident: bib180 article-title: Monitoring disulfide bond formation in the eukaryotic cytosol publication-title: J. Cell Biol. – volume: 276 start-page: 37133 year: 2001 end-page: 37140 ident: bib175 publication-title: J. Biol. Chem. – volume: 7 start-page: 327 year: 2005 end-page: 334 ident: bib230 article-title: Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast publication-title: Antioxid. Redox Signal. – volume: 14 start-page: 347 year: 1998 end-page: 357 ident: bib28 article-title: The importance of the glycerol 3-phosphate shuttle during aerobic growth of publication-title: Yeast – volume: 93 start-page: 5777 year: 1996 end-page: 5782 ident: bib41 article-title: Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response in publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 29 start-page: 57 year: 2005 end-page: 63 ident: bib125 article-title: Prevention of intracellular oxidation in yeast: the role of vitamin E analogue, Trolox (6-hydroxy-2,5,7,8-tetramethylkroman-2-carboxyl acid) publication-title: Cell Biol. Int. – volume: 75 start-page: 2143 year: 2007 end-page: 2151 ident: bib84 article-title: Niche-specific activation of the oxidative stress response by the pathogenic fungus publication-title: Infect. Immun. – volume: 19 start-page: 233 year: 2002 end-page: 239 ident: bib217 article-title: The adaptive response of publication-title: Yeast – volume: 267 start-page: 18298 year: 1992 end-page: 18302 ident: bib69 article-title: Yeast lacking superoxide dismutase: isolation of genetic suppressors publication-title: J. Biol. Chem. – volume: 276 start-page: 33730 year: 2001 end-page: 33735 ident: bib91 publication-title: J. Biol. Chem. – volume: 330 start-page: 604 year: 2005 end-page: 610 ident: bib177 article-title: Localization and function of three monothiol glutaredoxins in publication-title: Biochem. Biophys. Res. Commun. – start-page: 49 year: 1993 end-page: 55 ident: bib77 article-title: A publication-title: Gene – volume: 281 start-page: 26280 year: 2006 end-page: 26288 ident: bib171 article-title: AtGRXcp, an publication-title: J. Biol. Chem. – volume: 281 start-page: 15058 year: 2006 end-page: 15063 ident: bib142 article-title: Thioredoxin is required for deoxyribonucleotide pool maintenance during S phase publication-title: J. Biol. Chem. – volume: 39 start-page: 595 year: 2001 end-page: 605 ident: bib211 article-title: Role of thioredoxin reductase in the Yap1-dependent response to oxidative stress in publication-title: Mol. Microbiol. – volume: 13 start-page: 805 year: 2002 end-page: 816 ident: bib232 article-title: Distinct regulatory proteins control the graded transcriptional response to increasing H publication-title: Mol. Biol. Cell – volume: 182 start-page: 2823 year: 2000 end-page: 2830 ident: bib25 article-title: In vivo analysis of the mechanisms for oxidation of cytosolic NADH by publication-title: J. Bacteriol. – volume: 418 start-page: 344 year: 2002 end-page: 348 ident: bib45 article-title: Calorie restriction extends publication-title: Nature – volume: 47 start-page: 395 year: 2003 end-page: 403 ident: bib82 article-title: Disruption of the human pathogenic yeast publication-title: Microbiol. Immunol. – volume: 279 start-page: 35219 year: 2004 end-page: 35227 ident: bib109 article-title: Cytosolic thioredoxin peroxidases I and II are important defenses of yeast against organic hydroperoxide insult publication-title: J. Biol. Chem. – volume: 19 start-page: 8302 year: 1999 end-page: 8313 ident: bib224 article-title: Yap1p activates gene transcription in an oxidant-specific fashion publication-title: Mol. Cell. Biol. – volume: 148 start-page: 3705 year: 2002 end-page: 3713 ident: bib85 article-title: Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of publication-title: Microbiology – volume: 276 start-page: 38084 year: 2001 end-page: 38089 ident: bib62 article-title: A fraction of yeast Cu,Zn–superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria: a physiological role for SOD1 in guarding against mitochondrial oxidative damage publication-title: J. Biol. Chem. – volume: 301 start-page: 105 year: 1973 end-page: 128 ident: bib24 article-title: Mechanism of electron transport and energy conservation in the site I region of the respiratory chain publication-title: Biochim. Biophys. Acta – volume: 280 start-page: 24544 year: 2005 end-page: 24552 ident: bib174 article-title: A novel monothiol glutaredoxin (Grx4) from publication-title: J. Biol. Chem. – volume: 45 start-page: 1081 year: 1998 end-page: 1087 ident: bib56 article-title: Constitutive nitric oxide synthase in publication-title: Biochem. Mol. Biol. Int. – volume: 103 start-page: 7148 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib74 article-title: Disulfide cross-linked protein represents a significant fraction of ALS-associated SOD1 aggregates in spinal cords of model mice publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0602048103 – volume: 5 start-page: 623 year: 1986 ident: 10.1016/j.bbagen.2007.12.004_bib127 article-title: Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? publication-title: EMBO J. doi: 10.1002/j.1460-2075.1986.tb04256.x – volume: 14 start-page: 1460 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib83 article-title: Stress-induced gene expression in Candida albicans: absence of a general stress response publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E02-08-0546 – volume: 1763 start-page: 747 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib61 article-title: Activation of superoxide dismutases: putting the metal to the pedal publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2006.05.003 – volume: 32 start-page: 603 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib192 article-title: Protein-carbonyl accumulation in the non-replicative senescence of the methionine sulfoxide reductase A (msrA) knockout yeast strain publication-title: Amino Acids doi: 10.1007/s00726-006-0448-1 – volume: 151 start-page: 1939 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib191 article-title: Oxidative protein damage causes chromium toxicity in yeast publication-title: Microbiology doi: 10.1099/mic.0.27945-0 – volume: 377 start-page: 395 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib158 article-title: Analysis of the interaction between piD261/Bud32, an evolutionary conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin publication-title: Biochem. J. doi: 10.1042/bj20030638 – volume: 29 start-page: 511 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib179 article-title: Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae publication-title: Curr. Genet. doi: 10.1007/BF02426954 – start-page: 247 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib8 – volume: 279 start-page: 51923 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib159 article-title: Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins publication-title: J. Biol. Chem. doi: 10.1074/jbc.M410219200 – volume: 279 start-page: 7785 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib178 article-title: Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M312421200 – volume: 271 start-page: 28831 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib71 article-title: The yeast Cu,Zn superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.46.28831 – volume: 279 start-page: 46652 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib92 article-title: Genetic dissection of the phospholipids hydroperoxidase activity of yeast Gpx3 reveals its functional importance publication-title: J. Biol. Chem. doi: 10.1074/jbc.M408340200 – volume: 57 start-page: 1685 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib163 article-title: Genome-wide analysis of plant glutaredoxin systems publication-title: J. Exp. Bot. doi: 10.1093/jxb/erl001 – volume: 279 start-page: 39414 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib32 article-title: Inhibitors of the quinone binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) publication-title: J. Biol. Chem. doi: 10.1074/jbc.M406576200 – volume: 39 start-page: 533 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib5 article-title: Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2001.02283.x – volume: 21 start-page: 8483 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib26 article-title: Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.21.24.8483-8489.2001 – volume: 280 start-page: 42078 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib98 article-title: GPX2, encoding a phospholipid hydroperoxide glutathione peroxidase homologue, codes for an atypical 2-Cys peroxiredoxin in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M508622200 – volume: 27 start-page: 1110 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib37 article-title: Paraquat exposure as an etiological factor of Parkinson's disease publication-title: Neurotoxicology doi: 10.1016/j.neuro.2006.05.012 – volume: 13 start-page: 805 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib232 article-title: Distinct regulatory proteins control the graded transcriptional response to increasing H2O2 levels in fission yeast Schizosaccharomyces pombe publication-title: Mol. Biol. Cell doi: 10.1091/mbc.01-06-0288 – volume: 281 start-page: 28648 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib75 article-title: The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M600138200 – volume: 276 start-page: 1138 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib216 article-title: Multiple Yap1p-binding sites mediate induction of the yeast major facilitator FLR1 gene in response to drugs, oxidants, and alkylating agents publication-title: J. Biol. Chem. doi: 10.1074/jbc.M008377200 – volume: 179 start-page: 9 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib34 article-title: Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation publication-title: Exp. Neurol. doi: 10.1006/exnr.2002.8072 – volume: 31 start-page: 347 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib21 article-title: Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity and relation to aging and longevity publication-title: Bioenerg. Biomembr. doi: 10.1023/A:1005427919188 – volume: 13 start-page: 655 year: 1994 ident: 10.1016/j.bbagen.2007.12.004_bib212 article-title: YAP1-dependent activation of TRX2 is essential for the response of S. cerevisiae to oxidative stress by hydroperoxides publication-title: EMBO J. doi: 10.1002/j.1460-2075.1994.tb06304.x – volume: 119 start-page: 4554 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib161 article-title: Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae publication-title: J. Cell Sci. doi: 10.1242/jcs.03229 – volume: 280 start-page: 24544 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib174 article-title: A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M500678200 – volume: 5 start-page: 229 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib2 article-title: The uses of genome-wide mutant collections publication-title: Genome Biol. doi: 10.1186/gb-2004-5-7-229 – volume: 3 start-page: 245 year: 1995 ident: 10.1016/j.bbagen.2007.12.004_bib136 article-title: Thioredoxin—a fold for all reasons publication-title: Structure doi: 10.1016/S0969-2126(01)00154-X – start-page: 28052 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib63 article-title: Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria publication-title: J. Biol. Chem. doi: 10.1074/jbc.M304296200 – volume: 40 start-page: 1391 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib193 article-title: The yeast cytosolic thioredoxins are involved in the regulation of methionine sulfoxide reductase A publication-title: Free Rad. Biol. Med. doi: 10.1016/j.freeradbiomed.2005.12.017 – volume: 496 start-page: 105 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib126 article-title: Protective effects of vitamins and selenium compounds in yeast publication-title: Mutat. Res. doi: 10.1016/S1383-5718(01)00213-3 – volume: 278 start-page: 47629 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib40 article-title: The ubiquinone-binding site of the Saccharomyces cerevisiae succinate–ubiquinone oxidoreductase is a source of superoxide publication-title: J. Biol. Chem. doi: 10.1074/jbc.M306312200 – volume: 12 start-page: 1453 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib235 article-title: Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (exportin) and the stress-activated MAP kinase Sty1/Spc1 publication-title: Genes Dev. doi: 10.1101/gad.12.10.1453 – volume: 58 start-page: 6 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib255 article-title: Protein phosphatases in MAPK signalling: we keep learning from yeast publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.2005.04822.x – volume: 279 start-page: 29938 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib72 article-title: Mutations in Saccharomyces cerevisiae iron–sulfur cluster assembly gens and oxidative stress relevant to Cu,Zn superoxide dismutase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M402795200 – volume: 17 start-page: 7416 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib222 article-title: Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor publication-title: EMBO J. doi: 10.1093/emboj/17.24.7416 – volume: 281 start-page: 15058 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib142 article-title: Thioredoxin is required for deoxyribonucleotide pool maintenance during S phase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M601968200 – volume: 13 start-page: 1653 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib241 article-title: Heat–shock-induced activation of stress MAP kinase is regulated by threonine- and tyrosine-specific phosphatases publication-title: Genes Dev. doi: 10.1101/gad.13.13.1653 – volume: 59 start-page: 1 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib209 article-title: Redox sensing by prokaryotic transcription factors publication-title: Biochem. Pharmacol. doi: 10.1016/S0006-2952(99)00289-0 – volume: 36 start-page: 679 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib218 article-title: Identification of genes affecting selenite toxicity and resistance in Saccharomyces cerevisiae publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2000.01890.x – volume: 581 start-page: 3598 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib149 article-title: The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis publication-title: FEBS Lett. doi: 10.1016/j.febslet.2007.07.002 – volume: 276 start-page: 37133 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib175 article-title: Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain publication-title: J. Biol. Chem. doi: 10.1074/jbc.M105524200 – volume: 3 start-page: 277 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib57 article-title: Mitochondrial cytochrome oxidase produces nitric oxide under hypoxic conditions: implications for oxygen sensing and hypoxic signalling in eukaryotes publication-title: Cell Metab. doi: 10.1016/j.cmet.2006.02.011 – volume: 280 start-page: 36708 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib238 article-title: The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe publication-title: J. Biol. Chem. doi: 10.1074/jbc.M508400200 – volume: 266 start-page: 1692 year: 1991 ident: 10.1016/j.bbagen.2007.12.004_bib137 article-title: Yeast thioredoxin genes publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)52350-4 – volume: 353 start-page: 411 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib64 article-title: Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space publication-title: Biochem. J. doi: 10.1042/0264-6021:3530411 – volume: 24 start-page: 8753 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib220 article-title: Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.24.19.8753-8764.2004 – volume: 23 start-page: 741 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib145 article-title: The role of Yap1p and Skn7p-mediated oxidative stress response in the defence of Saccharomyces cerevisiae against singlet oxygen publication-title: Yeast doi: 10.1002/yea.1392 – volume: 1703 start-page: 213 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib187 article-title: Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2004.09.003 – volume: 15 start-page: 2227 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib79 article-title: The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress-response element (STRE) publication-title: EMBO J. doi: 10.1002/j.1460-2075.1996.tb00576.x – volume: 6 start-page: 63 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib15 article-title: Glutaredoxins: glutathione-dependent redox enzymes with functions as far beyond a simple thioredoxin backup system publication-title: Antioxid. Redox Signal doi: 10.1089/152308604771978354 – volume: 273 start-page: 805 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib112 article-title: Yeast oxidative stress response: influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state publication-title: FEBS J. doi: 10.1111/j.1742-4658.2006.05116.x – volume: 281 start-page: 12227 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib128 article-title: Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia publication-title: J. Biol. Chem. doi: 10.1074/jbc.M511649200 – volume: 16 start-page: 1035 year: 1997 ident: 10.1016/j.bbagen.2007.12.004_bib202 article-title: The Skn7 response regulator controls gene expressión in the oxidative stress response of the budding yeast Saccharomyces cerevisiae publication-title: EMBO J. doi: 10.1093/emboj/16.5.1035 – volume: 447 start-page: 487 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib249 article-title: Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases publication-title: Nature doi: 10.1038/nature05804 – volume: 29 start-page: 351 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib228 article-title: Microbial H2O2 sensors as archetypical redox signaling modules publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2004.05.005 – volume: 8 start-page: 201 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib53 article-title: S-glutathionylation: from redox regulation of protein functions to human diseases publication-title: J. Cell. Mol. Med. doi: 10.1111/j.1582-4934.2004.tb00275.x – volume: 29 start-page: 57 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib125 article-title: Prevention of intracellular oxidation in yeast: the role of vitamin E analogue, Trolox (6-hydroxy-2,5,7,8-tetramethylkroman-2-carboxyl acid) publication-title: Cell Biol. Int. doi: 10.1016/j.cellbi.2004.11.010 – volume: 274 start-page: 27002 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib90 article-title: Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.38.27002 – volume: 19 start-page: 5157 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib225 article-title: H2O2 sensing through oxidation of the Yap1 transcription factor publication-title: EMBO J. doi: 10.1093/emboj/19.19.5157 – volume: 104 start-page: 4886 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib122 article-title: Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0700481104 – volume: 94 start-page: 9585 year: 1997 ident: 10.1016/j.bbagen.2007.12.004_bib190 article-title: The yeast peptide–methionine sulfoxide reductase functions as an antioxidant in vivo publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.94.18.9585 – volume: 93 start-page: 5777 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib41 article-title: Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response in Saccharomyces cerevisiae publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.93.12.5777 – volume: 105 start-page: 103 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib210 article-title: Structural basis of the redox switch in the OxyR transcription factor publication-title: Cell doi: 10.1016/S0092-8674(01)00300-2 – volume: 282 start-page: 2184 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib113 article-title: Regulation of the yeast TSA1 peroxiredoxin by ZAP1 is an adaptive response to the oxidative stress of zinc deficiency publication-title: J. Biol. Chem. doi: 10.1074/jbc.M606639200 – volume: 80 start-page: 780 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib33 article-title: Generation of reactive oxygen species by the mitochondrial electron transport publication-title: J. Neurochem. doi: 10.1046/j.0022-3042.2002.00744.x – volume: 895 start-page: 205 year: 1987 ident: 10.1016/j.bbagen.2007.12.004_bib27 article-title: The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism publication-title: Biochim. Biophys. Acta doi: 10.1016/S0304-4173(87)80003-4 – volume: 32 start-page: 403 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib131 article-title: The Yfe system of Yersinia pestis transports iron and manganese and is required for full virulence of plague publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1999.01360.x – volume: 9 start-page: 1081 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib150 article-title: The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species publication-title: Mol. Biol. Cell doi: 10.1091/mbc.9.5.1081 – volume: 25 start-page: 15 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib22 article-title: Stoichiometry and compartmentation of NADH metabolism in Saccharomyces cerevisiae publication-title: FEMS Microbiol. Rev. doi: 10.1111/j.1574-6976.2001.tb00570.x – volume: 275 start-page: 24800 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib184 article-title: Identification, characterization, and crystal structure of the omega class glutathione transferases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M001706200 – volume: 12 start-page: 1464 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib243 article-title: Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast publication-title: Genes Dev. doi: 10.1101/gad.12.10.1464 – volume: 17 start-page: 3 year: 1997 ident: 10.1016/j.bbagen.2007.12.004_bib19 article-title: Superoxide production by the mitochondrial respiratory chain publication-title: Biosci. Rep. doi: 10.1023/A:1027374931887 – volume: 267 start-page: 18298 year: 1992 ident: 10.1016/j.bbagen.2007.12.004_bib69 article-title: Yeast lacking superoxide dismutase: isolation of genetic suppressors publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)36959-5 – volume: 135 start-page: 219 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib114 article-title: Alkyl hydroperoxide reductase 1 protects Saccharomyces cerevisiae against metal ion toxicity and glutathione depletion publication-title: Toxicol. Lett. doi: 10.1016/S0378-4274(02)00280-1 – volume: 270 start-page: 1578 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib36 article-title: H2O2, but not menadione, provokes a decrease in the ATP and an increase in the inosine levels in Saccharomyces cerevisiae. An experimental and theoretical approach publication-title: Eur. J. Biochem. doi: 10.1046/j.1432-1033.2003.03529.x – volume: 14 start-page: 347 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib28 article-title: The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae publication-title: Yeast doi: 10.1002/(SICI)1097-0061(19980315)14:4<347::AID-YEA226>3.0.CO;2-9 – volume: 83 start-page: 3820 year: 1986 ident: 10.1016/j.bbagen.2007.12.004_bib65 article-title: A yeast mutant lacking mitochondrial manganese–superoxide dismutase is hypersensitive to oxygen publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.83.11.3820 – year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib7 – volume: 276 start-page: 495 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib234 article-title: Oxidative stress in Schizosaccharomyces pombe: different H2O2 levels, different response pathways publication-title: Mol. Genet. Genomics doi: 10.1007/s00438-006-0175-z – volume: 276 start-page: 38084 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib62 article-title: A fraction of yeast Cu,Zn–superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria: a physiological role for SOD1 in guarding against mitochondrial oxidative damage publication-title: J. Biol. Chem. doi: 10.1074/jbc.M105296200 – volume: 4 start-page: 123 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib214 article-title: Transcription factors regulating the response to oxidative stress in yeast publication-title: Antioxid. Redox Signal. doi: 10.1089/152308602753625915 – volume: 352 start-page: 750 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib80 article-title: Msn2p/Msn4p-activation is essential for the recovery from freezing stress in yeast publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2006.11.100 – volume: 35 start-page: 889 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib219 article-title: Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signalling publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(03)00434-9 – volume: 32 start-page: 609 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib31 article-title: Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria publication-title: J. Bioenerg. Biomembr. doi: 10.1023/A:1005626712319 – volume: 166 start-page: 337 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib180 article-title: Monitoring disulfide bond formation in the eukaryotic cytosol publication-title: J. Cell Biol. doi: 10.1083/jcb.200402120 – volume: 45 start-page: 1081 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib56 article-title: Constitutive nitric oxide synthase in Saccharomyces cerevisiae publication-title: Biochem. Mol. Biol. Int. – volume: 281 start-page: 17661 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib160 article-title: Role of glutaredoxin-3 and glutaredoxin-4 in the iron-regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M602165200 – volume: 277 start-page: 18914 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib162 article-title: Subcellular localisation of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M200949200 – volume: 330 start-page: 604 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib177 article-title: Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2005.02.183 – volume: 277 start-page: 16712 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib99 article-title: The yeast glutaredoxins are active as glutathione peroxidases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111686200 – volume: 280 start-page: 9149 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib254 article-title: Pkc1 and the upstream elements of the cell integrity pathway in Saccharomyces cerevisiae, Rom2 and Mtl1, are required for cellular responses to oxidative stress publication-title: J. Biol. Chem. doi: 10.1074/jbc.M411062200 – volume: 19 start-page: 8180 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib168 article-title: Grx5 glutaredoxin plays a central role in protection against oxidative damage in Saccharomyces cerevisiae publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.19.12.8180 – volume: 277 start-page: 16712 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib152 article-title: Role of yeast glutaredoxins as glutathione S-transferases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111686200 – volume: 274 start-page: 6566 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib138 article-title: Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.10.6366 – volume: 277 start-page: 5385 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib107 article-title: Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress publication-title: J. Biol. Chem. doi: 10.1074/jbc.M106846200 – volume: 253 start-page: 893 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib88 article-title: Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1998.9864 – volume: 14 start-page: 5832 year: 1994 ident: 10.1016/j.bbagen.2007.12.004_bib213 article-title: GSH1, which encodes γ-glutamylcysteine synthetase, is a target gene for yAP-1 transcriptional regulator publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.14.9.5832 – volume: 120 start-page: 12 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib134 article-title: Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae publication-title: Physiol. Plant. doi: 10.1111/j.0031-9317.2004.0193.x – volume: 278 start-page: 30896 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib229 article-title: Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M303542200 – volume: 3 start-page: 1076 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib102 article-title: Transcriptional response of Candida albicans upon internalization by macrophages publication-title: Eukaryot. Cell doi: 10.1128/EC.3.5.1076-1087.2004 – volume: 278 start-page: 41849 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib253 article-title: Lipid hydroperoxides activate the mitogen-activated protein kinase Mpk1p in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M307760200 – volume: 47 start-page: 395 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib82 article-title: Disruption of the human pathogenic yeast Candida albicans catalase gene decreases survival in mouse-model infection and elevates susceptibility to higher temperature and to detergents publication-title: Microbiol. Immunol. doi: 10.1111/j.1348-0421.2003.tb03376.x – volume: 552 start-page: 335 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib17 article-title: Mitochondrial formation of reactive oxygen species publication-title: J. Physiol. doi: 10.1113/jphysiol.2003.049478 – volume: 14 start-page: 1511 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib4 article-title: Oxidative stress responses of yeast Saccharomyces cerevisiae publication-title: Yeast doi: 10.1002/(SICI)1097-0061(199812)14:16<1511::AID-YEA356>3.0.CO;2-S – volume: 35 start-page: 179 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib39 article-title: H2O2 generation in Saccharomyces cerevisiae respiratory pet mutants: effect of cytochrome c publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(03)00307-1 – volume: 10 start-page: 281 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib58 article-title: The existence and significance of a mitochondrial nitrite reductase publication-title: Redox Rep. doi: 10.1179/135100005X83707 – volume: 13 start-page: 1109 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib166 article-title: Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes publication-title: Mol. Biol. Cell doi: 10.1091/mbc.01-10-0517 – volume: 156 start-page: 435 year: 1976 ident: 10.1016/j.bbagen.2007.12.004_bib30 article-title: Role of ubiquinone in the mitochondrial generation of hydrogen peroxide publication-title: Biochem. J. doi: 10.1042/bj1560435 – volume: 45 start-page: 243 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib237 article-title: Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2002.03020.x – volume: 274 start-page: 15151 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib236 article-title: A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.21.15151 – volume: 52 start-page: 1427 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib233 article-title: Activation of the redox sensor Pap1 by hydrogen peroxide requires modulation of the intracellular oxidant concentration publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.2004.04065.x – volume: vol. 1 start-page: 241 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib6 – volume: 64 start-page: 120 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib118 article-title: Nuclear thioredoxin peroxidase Dot5 in Saccharomyces cerevisiae: roles in oxidative stress response and disruption of telomeric silencing publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-003-1421-5 – volume: 2 start-page: 381 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib203 article-title: Regulation of the transcriptional response to oxidative stress in fungi: similarities and differences publication-title: Eukaryot. Cell doi: 10.1128/EC.2.3.381-389.2003 – volume: 72 start-page: 2390 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib204 article-title: SKN7 of Candida albicans: mutant construction and phenotype analysis publication-title: Infect. Immun. doi: 10.1128/IAI.72.4.2390-2394.2004 – volume: 142 start-page: 231 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib18 article-title: Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? publication-title: Br. J. Pharmacol. doi: 10.1038/sj.bjp.0705776 – volume: 348 start-page: 25 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib194 article-title: Glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox-dependent way publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2006.06.067 – volume: 73 start-page: 5022 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib205 article-title: Identification and characterization of an SKN7 homologue in Cryptococcus neoformans publication-title: Infect. Immun. doi: 10.1128/IAI.73.8.5022-5030.2005 – volume: 5 start-page: 1447 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib81 article-title: The Cryptococcus neoformans catalase gene family and its role in antioxidant defense publication-title: Eukaryot. Cell doi: 10.1128/EC.00098-06 – volume: 117 start-page: 625 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib115 article-title: Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function publication-title: Cell doi: 10.1016/j.cell.2004.05.002 – volume: 31 start-page: 1308 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib16 article-title: Cell respiration and formation of reactive oxygen species: facts and artefacts publication-title: Biochem. Soc. Trans. doi: 10.1042/bst0311308 – volume: 7 start-page: 327 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib230 article-title: Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast publication-title: Antioxid. Redox Signal. doi: 10.1089/ars.2005.7.327 – volume: 195 start-page: 857 year: 1991 ident: 10.1016/j.bbagen.2007.12.004_bib23 article-title: Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1991.tb15775.x – volume: 387 start-page: 1329 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib89 article-title: Glutathione peroxidases and redox-regulated transcription factors publication-title: Biol. Chem. doi: 10.1515/BC.2006.166 – volume: 35 start-page: 1146 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib132 article-title: The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2000.01783.x – volume: 64 start-page: 1518 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib157 article-title: Monothiol glutaredoxins: a common domain for multiple functions publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-007-6554-8 – volume: 266 start-page: 9194 year: 1991 ident: 10.1016/j.bbagen.2007.12.004_bib139 article-title: Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)31570-9 – volume: 271 start-page: 12275 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib70 article-title: Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic species in vivo publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.21.12275 – volume: 280 start-page: 23319 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib239 article-title: Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide publication-title: J. Biol. Chem. doi: 10.1074/jbc.M502757200 – volume: 17 start-page: 701 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib47 article-title: Peroxisome biogenesis publication-title: Annu. Rev. Cell Dev. Biol. doi: 10.1146/annurev.cellbio.17.1.701 – volume: 242 start-page: 1 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib9 article-title: Recent trends in glutathione biochemistry-glutathione–protein interactions: a molecular link between oxidative stress and cell proliferation? publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.7812 – volume: 324 start-page: 1101 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib154 article-title: The herbicide 2,4-dichlorophenoxyacetic acid induces the generation of free-radicals and associated oxidative stress responses in yeast publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2004.09.158 – volume: 6 start-page: 1373 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib207 article-title: Role of heat shock transcription factor in Saccharomyces cerevisiae oxidative stress response publication-title: Eukaryot. Cell doi: 10.1128/EC.00098-07 – volume: 21 start-page: 6139 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib223 article-title: Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.21.18.6139-6150.2001 – volume: 301 start-page: 105 year: 1973 ident: 10.1016/j.bbagen.2007.12.004_bib24 article-title: Mechanism of electron transport and energy conservation in the site I region of the respiratory chain publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4173(73)90001-3 – volume: 5 start-page: 1037 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib48 article-title: Protein translocation machineries: how organelles bring in matrix proteins publication-title: FEMS Yeast Res. doi: 10.1016/j.femsyr.2005.03.004 – volume: 281 start-page: 10420 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib146 article-title: The Saccharomyces cerevisiae proteome of oxidized protein thiols publication-title: J. Biol. Chem. doi: 10.1074/jbc.M513346200 – volume: 11 start-page: 4241 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib195 article-title: Genomic expression programs in the response of yeast cells to environmental changes publication-title: Mol. Biol. Cell doi: 10.1091/mbc.11.12.4241 – volume: 7 start-page: 1805 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib183 article-title: A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth publication-title: Mol. Biol. Cell doi: 10.1091/mbc.7.11.1805 – volume: 275 start-page: 5723 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib106 article-title: Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.8.5723 – volume: 279 start-page: 23207 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib111 article-title: Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable publication-title: J. Biol. Chem. doi: 10.1074/jbc.M402095200 – start-page: 49 year: 1993 ident: 10.1016/j.bbagen.2007.12.004_bib77 article-title: A Saccharomyces cerevisiae upstream activating sequence mediates induction of peroxisome proliferation by fatty acids publication-title: Gene doi: 10.1016/0378-1119(93)90513-3 – volume: 54 start-page: 439 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib133 article-title: Roles of the glutathione- and thioredoxin-dependent systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress publication-title: Annu. Rev. Microbiol. doi: 10.1146/annurev.micro.54.1.439 – volume: 42 start-page: 326 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib108 article-title: Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics publication-title: Free Rad. Biol. Med. doi: 10.1016/j.freeradbiomed.2006.10.042 – ident: 10.1016/j.bbagen.2007.12.004_bib96 doi: 10.1016/j.febslet.2004.03.091 – volume: 436 start-page: 1035 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib172 article-title: Deficiency of glutaredoxin 5 reveals Fe–S clusters are required for vertebrate haem synthesis publication-title: Nature doi: 10.1038/nature03887 – volume: 1763 start-page: 1755 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib55 article-title: Peroxisomes and oxidative stress publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2006.09.006 – volume: 276 start-page: 33730 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib91 article-title: Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M105672200 – volume: 527 start-page: 186 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib251 article-title: YIL113w encodes a functional dual-specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae publication-title: FEBS Lett. doi: 10.1016/S0014-5793(02)03220-9 – volume: 2 start-page: 659 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib1 article-title: The art and design of genetic screens: yeast publication-title: Nature Rev. Genet. doi: 10.1038/35088500 – volume: 125 start-page: 1061 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib245 article-title: A fission yeast gene (prr1+) that encodes a response regulator implicated in oxidative stress response publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a022387 – volume: 580 start-page: 2273 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib170 article-title: Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria publication-title: FEBS Lett. doi: 10.1016/j.febslet.2006.03.037 – volume: 173 start-page: 5918 year: 1991 ident: 10.1016/j.bbagen.2007.12.004_bib68 article-title: Null mutants of Saccharomyces cerevisiae Cu,Zn superoxide dismutase: characterization and spontaneous mutation rates publication-title: J. Bacteriol. doi: 10.1128/jb.173.18.5918-5920.1991 – volume: 430 start-page: 917 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib227 article-title: Structural basis for redox regulation of Yap1 transcription factor localization publication-title: Nature doi: 10.1038/nature02790 – volume: 4 start-page: 392 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib140 article-title: Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae publication-title: Eukaryot. Cell doi: 10.1128/EC.4.2.392-400.2005 – volume: 85 start-page: S67 issue: Suppl 2 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib120 article-title: Micronutrients: oxidant/antioxidant status publication-title: Br. J. Nutr. doi: 10.1079/BJN2000296 – volume: 143 start-page: 1649 year: 1997 ident: 10.1016/j.bbagen.2007.12.004_bib67 article-title: Mitochondrial superoxide dismutase is essential for ethanol tolerance of Saccharomyces cerevisiae in the post-diauxic phase publication-title: Microbiology doi: 10.1099/00221287-143-5-1649 – volume: 150 start-page: 613 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib117 article-title: Identification of high-copy disrupters of telomeric silencing in Saccharomyces cerevisiae publication-title: Genetics doi: 10.1093/genetics/150.2.613 – volume: 569 start-page: 13 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib196 article-title: Yeast signalling pathways in the oxidative stress response publication-title: Mutat. Res. doi: 10.1016/j.mrfmmm.2004.09.006 – volume: 1100 start-page: 383 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib189 article-title: Methionine sulfoxide reduction and the aging process publication-title: Ann. N.Y. Acad. Sci. doi: 10.1196/annals.1395.042 – volume: 6 start-page: 652 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib206 article-title: The Skn7 response regulator of Cryptococcus neoformans is involved in oxidative stress signalling and augments intracellular survival in endothelium publication-title: FEMS Yeast Res. doi: 10.1111/j.1567-1364.2006.00065.x – volume: 99 start-page: 307 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib165 article-title: PICOT inhibits cardiac hypertrophy and enhances ventricular function and cardiomyocyte contractility publication-title: Circ. Res. doi: 10.1161/01.RES.0000234780.06115.2c – volume: 64 start-page: 97 year: 1995 ident: 10.1016/j.bbagen.2007.12.004_bib60 article-title: Superoxide radical and superoxide dismutases publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.bi.64.070195.000525 – volume: 27 start-page: 133 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib247 article-title: The structure and mechanism of protein phosphatases: insights into catalysis and regulation publication-title: Annu. Rev. Biophys. Biomol. Struct. doi: 10.1146/annurev.biophys.27.1.133 – volume: 45 start-page: 51 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib153 article-title: Glutathione transferases publication-title: Annu. Rev. Pharmacol. Toxicol. doi: 10.1146/annurev.pharmtox.45.120403.095857 – volume: 271 start-page: 627 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib93 article-title: Reverse genetic analysis of the glutathione metabolic pathway suggests a novel role of PHGPX and URE2 genes in aluminium resistance in Saccharomyces cerevisiae publication-title: Mol. Gen. Genomics doi: 10.1007/s00438-004-1015-7 – volume: 401 start-page: 77 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib185 article-title: Characterization of the Omega-class of glutathione transferases publication-title: Methods Enzymol. – volume: 43 start-page: 136 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib221 article-title: Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast publication-title: Free Rad. Biol. Med. doi: 10.1016/j.freeradbiomed.2007.04.007 – volume: 398 start-page: 187 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib100 article-title: Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases active as 1-Cys thiol transferases publication-title: Biochem. J. doi: 10.1042/BJ20060034 – volume: 277 start-page: 18561 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib143 article-title: Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase and function publication-title: J. Biol. Chem. doi: 10.1074/jbc.M201225200 – volume: 280 start-page: 40524 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib226 article-title: Oxidant-specific folding of Yap1p regulates both transcriptional activation and nuclear localization publication-title: J. Biol. Chem. doi: 10.1074/jbc.M504716200 – volume: 275 start-page: 27393 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib35 article-title: Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)61523-1 – volume: 281 start-page: 26280 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib171 article-title: AtGRXcp, an Arabidopsis chloroplastic/plastidic glutaredoxin is critical for protection against protein oxidative damage publication-title: J. Biol. Chem. doi: 10.1074/jbc.M601354200 – volume: 17 start-page: 387 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib148 article-title: The thioredoxin system protects ribosomes against stress-induced aggregation publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E05-06-0520 – volume: 279 start-page: 35219 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib109 article-title: Cytosolic thioredoxin peroxidases I and II are important defenses of yeast against organic hydroperoxide insult publication-title: J. Biol. Chem. doi: 10.1074/jbc.M313773200 – volume: 268 start-page: 26699 year: 1993 ident: 10.1016/j.bbagen.2007.12.004_bib66 article-title: Absence of electron transport (Rho0 state) restores growth of a manganese–superoxide dismutase-deficient Saccharomyces cerevisiae in hyperoxia publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)74369-5 – volume: 569 start-page: 301 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib97 article-title: Distinct regulatory mechanism of yeast GPX2 encoding phospholipids hydroperoxide glutathione peroxidase by oxidative stress and a calcineurin/Crz1-mediated Ca2+ signalling pathway publication-title: FEBS Lett. doi: 10.1016/j.febslet.2004.05.077 – volume: 7 start-page: 348 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib13 article-title: Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation publication-title: Antioxid. Redox Signal. doi: 10.1089/ars.2005.7.348 – volume: 28 start-page: 32 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib104 article-title: Structure, mechanism and regulation of peroxiredoxins publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(02)00003-8 – volume: 155 start-page: 1046 year: 1988 ident: 10.1016/j.bbagen.2007.12.004_bib124 article-title: Kinetic study of the reaction between vitamin E radical and alkyl hydroperoxides in solution publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(88)80602-8 – volume: 33 start-page: 1378 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib10 article-title: Oxidoreduction of protein thiols in redox regulation publication-title: Biochem. Soc. Trans. doi: 10.1042/BST20051378 – volume: 151 start-page: 2573 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib103 article-title: Two glutathione peroxidases in the fungal pathogen Cryptococcus neoformans are expressed in the presence of specific substrates publication-title: Microbiology doi: 10.1099/mic.0.28132-0 – volume: 46 start-page: 869 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib147 article-title: Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2002.03216.x – volume: 320 start-page: 61 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib78 article-title: Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasemic Saccharomyces cerevisiae publication-title: J. Biochem. doi: 10.1042/bj3200061 – volume: 279 start-page: 31983 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib46 article-title: Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction publication-title: J. Biol. Chem. doi: 10.1074/jbc.M404849200 – volume: 275 start-page: 1902 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib164 article-title: Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interaction protein with a thioredoxin homology domain publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.3.1902 – volume: 78 start-page: 6858 year: 1981 ident: 10.1016/j.bbagen.2007.12.004_bib51 article-title: Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.78.11.6858 – volume: 10 start-page: 496 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib130 article-title: Manganese: elemental defence for a life with oxygen publication-title: Trends Microbiol. doi: 10.1016/S0966-842X(02)02462-9 – volume: 443 start-page: 787 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib43 article-title: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases publication-title: Nature doi: 10.1038/nature05292 – volume: 11 start-page: 2335 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib201 article-title: The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsf1 in vivo and is required for the induction of heat shock genes by oxidative stress publication-title: Mol. Biol. Cell doi: 10.1091/mbc.11.7.2335 – volume: 19 start-page: 8302 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib224 article-title: Yap1p activates gene transcription in an oxidant-specific fashion publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.19.12.8302 – volume: 14 start-page: 679 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib208 article-title: The role of cysteine residues as redox-sensitive regulatory switches publication-title: Curr. Op. Struct. Biol. doi: 10.1016/j.sbi.2004.09.012 – volume: 71 start-page: 173 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib86 article-title: Superoxide dismutase influences the virulence of Cryptococcus neoformans by affecting growth within macrophages publication-title: Infect. Immun. doi: 10.1128/IAI.71.1.173-180.2003 – volume: 425 start-page: 686 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib95 article-title: Global analysis of protein localization in budding yeast publication-title: Nature doi: 10.1038/nature02026 – volume: 111 start-page: 471 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib94 article-title: A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation publication-title: Cell doi: 10.1016/S0092-8674(02)01048-6 – volume: 273 start-page: 59 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib44 article-title: Oxidative stress, caloric restriction, and aging publication-title: Science doi: 10.1126/science.273.5271.59 – volume: 273 start-page: 22480 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib198 article-title: The H2O2 stimulon in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.35.22480 – volume: 69 start-page: 262 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib252 article-title: Cell wall integrity signaling in Saccharomyces cerevisiae publication-title: Microbiol. Mol. Biol. Rev. doi: 10.1128/MMBR.69.2.262-291.2005 – volume: 47 start-page: 143 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib42 article-title: Mitochondrial oxidative stress: implications for cell death publication-title: Annu. Rev. Pharmacol. Toxicol. doi: 10.1146/annurev.pharmtox.47.120505.105122 – volume: 17 start-page: 1018 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib101 article-title: Role of the Hog1 stress-activated protein kinase in the global transcriptional response to stress in the fungal pathogen Candida albicans publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E05-06-0501 – volume: 19 start-page: 415 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib116 article-title: Moonlighting proteins: old proteins learning new tricks publication-title: Trends Genet. doi: 10.1016/S0168-9525(03)00167-7 – volume: 148 start-page: 3705 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib85 article-title: Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence publication-title: Microbiology doi: 10.1099/00221287-148-11-3705 – volume: 276 start-page: 8469 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib200 article-title: A proteome analysis of the cadmium response in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M008708200 – volume: 64 start-page: 1373 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib50 article-title: Physiological functions of d-amino acid oxidases: from yeast to humans publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-007-6558-4 – volume: 36 start-page: 1167 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib155 article-title: A single glutaredoxin or thioredoxin is essential for viability in the yeast Saccharomyces cerevisiae publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2000.01948.x – volume: 16 start-page: 1710 year: 1997 ident: 10.1016/j.bbagen.2007.12.004_bib215 article-title: Regulation of yAP-1 nuclear localization in response to oxidative stress publication-title: EMBO J. doi: 10.1093/emboj/16.7.1710 – volume: 275 start-page: 16296 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib110 article-title: Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.21.16296 – volume: 39 start-page: 595 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib211 article-title: Role of thioredoxin reductase in the Yap1-dependent response to oxidative stress in Saccharomyces cerevisiae publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2001.02255.x – volume: 7 start-page: 560 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib248 article-title: Functions and mechanisms of redox regulation of cysteine-based phosphatases publication-title: Antioxid. Redox Signal. doi: 10.1089/ars.2005.7.560 – volume: 5 start-page: 1215 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib181 article-title: Involvement of oxidative stress response genes in redox homeostasis, the level of reactive oxygen species, and ageing in Saccharomyces cerevisiae publication-title: FEMS Yeast Res. doi: 10.1016/j.femsyr.2005.06.001 – volume: 277 start-page: 37590 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib169 article-title: Structure–function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein publication-title: J. Biol. Chem. doi: 10.1074/jbc.M201688200 – volume: 10 start-page: 1395 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib244 article-title: Active nucleocytoplasmic shuttling required for function and regulation of stress-activated kinase Spc1/StyI in fission yeast publication-title: Mol. Biol. Cell doi: 10.1091/mbc.10.5.1395 – volume: 4 start-page: 184 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib182 article-title: Non-reciprocal regulation of the redox state of the glutathione–glutaredoxin and thioredoxin systems publication-title: EMBO Rep. doi: 10.1038/sj.embor.embor729 – volume: 13 start-page: 2977 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib246 article-title: Role of fission yeast Tup1-like repressors and Prr1 transcription factor in response to salt stress publication-title: Mol. Biol. Cell doi: 10.1091/mbc.01-12-0568 – volume: 34 start-page: 478 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib29 article-title: External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(02)01328-X – volume: 5 start-page: 1748 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib186 article-title: A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism publication-title: Eukaryot. Cell doi: 10.1128/EC.00216-06 – volume: 102 start-page: 8875 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib240 article-title: A cysteine–sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0503251102 – volume: 1703 start-page: 135 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib188 article-title: Methionine oxidation and aging publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2004.08.010 – volume: 100 start-page: 10353 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib129 article-title: Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1632471100 – volume: 42 start-page: 1008 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib141 article-title: Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast publication-title: Free Rad. Biol. Med. doi: 10.1016/j.freeradbiomed.2006.12.027 – volume: 275 start-page: 21149 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib156 article-title: Purification and characterization of Acr2p, the Saccharomyces cerevisiae arsenate reductase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M910401199 – volume: 22 start-page: 4815 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib167 article-title: Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p publication-title: EMBO J. doi: 10.1093/emboj/cdg446 – volume: 32 start-page: 163 year: 1998 ident: 10.1016/j.bbagen.2007.12.004_bib135 article-title: The genetics of disulphide bond metabolism publication-title: Annu. Rev. Genet. doi: 10.1146/annurev.genet.32.1.163 – volume: 132 start-page: 49 year: 1993 ident: 10.1016/j.bbagen.2007.12.004_bib49 article-title: A Saccharomyces cerevisiae upstream activating sequence mediates induction of peroxisome proliferation by fatty acids publication-title: Gene doi: 10.1016/0378-1119(93)90513-3 – volume: 14 start-page: 214 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib231 article-title: Global transcriptional responses of fission yeast to environmental stress publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E02-08-0499 – volume: 277 start-page: 21278 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib250 article-title: Regulation of the Saccharomyces cerevisiae Slt2 kinase pathway by the stress-inducible Sdp1 dual specificity phosphatase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M202557200 – volume: 38 start-page: 1019 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib121 article-title: Ascorbate restores lifespan of superoxide–dismutase deficient yeast publication-title: Free Radic. Res. doi: 10.1080/10715760410001717327 – volume: 25 start-page: 207 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib52 article-title: Free radical-mediated oxidation of free amino acids and amino acid residues in proteins publication-title: Amino Acids doi: 10.1007/s00726-003-0011-2 – volume: 4 start-page: 1396 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib242 article-title: Distinct signaling pathways respond to arsenite and reactive oxygen species in Schizosaccharomyces pombe publication-title: Eukaryot. Cell doi: 10.1128/EC.4.8.1396-1402.2005 – volume: 25 start-page: 502 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib20 article-title: Mitochondria, oxygen free radicals, disease and ageing publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(00)01674-1 – volume: 38 start-page: 1543 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib105 article-title: Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signalling publication-title: Free Rad. Biol. Med. doi: 10.1016/j.freeradbiomed.2005.02.026 – volume: 278 start-page: 25745 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib176 article-title: Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin publication-title: J. Biol. Chem. doi: 10.1074/jbc.M303477200 – volume: 19 start-page: 233 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib217 article-title: The adaptive response of Saccharomyces cerevisiae to mercury exposure publication-title: Yeast doi: 10.1002/yea.835 – volume: 23 start-page: 2872 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib73 article-title: Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS publication-title: EMBO J. doi: 10.1038/sj.emboj.7600276 – volume: 43 start-page: 993 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib144 article-title: Role of thioredoxins in the response of Saccharomyces cerevisiae to oxidative stress induced by hydroperoxides publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2002.02795.x – volume: 15 start-page: 319 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib197 article-title: Complex cellular responses to reactive oxygen species publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2005.04.003 – volume: 182 start-page: 2823 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib25 article-title: In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria publication-title: J. Bacteriol. doi: 10.1128/JB.182.10.2823-2830.2000 – volume: 19 start-page: 651 year: 1996 ident: 10.1016/j.bbagen.2007.12.004_bib3 article-title: The molecular defences against reactive oxygen species in yeast publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1996.403940.x – volume: 49 start-page: 87 year: 2001 ident: 10.1016/j.bbagen.2007.12.004_bib38 article-title: Mitochondria as subcellular targets for clinically useful anthracyclines publication-title: Adv. Drug Deliv. Rev. doi: 10.1016/S0169-409X(01)00128-4 – volume: 110 start-page: 1353 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib173 article-title: The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload publication-title: Blood doi: 10.1182/blood-2007-02-072520 – volume: 254 start-page: 13963 year: 1989 ident: 10.1016/j.bbagen.2007.12.004_bib14 article-title: Thioredoxin and glutaredoxin systems publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)71625-6 – volume: 57 start-page: 1318 year: 2005 ident: 10.1016/j.bbagen.2007.12.004_bib119 article-title: The moonlighting protein Tsa1p is implicated in oxidative stress response and in cell wall biogenesis in Candida albicans publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.2005.04771.x – volume: 387 start-page: 1385 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib12 article-title: Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways publication-title: Biol. Chem. doi: 10.1515/BC.2006.174 – volume: 281 start-page: 16551 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib151 article-title: One single in-frame AUG codon is responsible for a diversity of subcellular localizations for glutaredoxin 2 in Saccharomyces cerevisiae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M600790200 – volume: 71 start-page: 551 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib11 article-title: Redox modifications of protein thiols: emerging roles in cell signalling publication-title: Biochem. Pharmacol. doi: 10.1016/j.bcp.2005.10.044 – volume: 15 start-page: 456 year: 2004 ident: 10.1016/j.bbagen.2007.12.004_bib87 article-title: Superoxide dismutases in Candida albicans: transcriptional regulation and functional characterization of the hyphal-induced SOD5 gene publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E03-03-0179 – volume: 418 start-page: 344 year: 2002 ident: 10.1016/j.bbagen.2007.12.004_bib45 article-title: Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration publication-title: Nature doi: 10.1038/nature00829 – volume: 11 start-page: 231 year: 2006 ident: 10.1016/j.bbagen.2007.12.004_bib54 article-title: Yeast flavohemoglobin protects against nitrosative stress and controls ferric reductase activity publication-title: Redox Rep. doi: 10.1179/135100006X154987 – volume: 97 start-page: 4672 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib59 article-title: Protection from nitrosative stress by yeast flavohemoglobin publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.090083597 – volume: 186 start-page: 245 year: 2000 ident: 10.1016/j.bbagen.2007.12.004_bib123 article-title: Biosynthesis of l-ascorbic acid (vitamin C) by Saccharomyces cerevisiae publication-title: FEMS Microbiol. Lett. – volume: 75 start-page: 2143 year: 2007 ident: 10.1016/j.bbagen.2007.12.004_bib84 article-title: Niche-specific activation of the oxidative stress response by the pathogenic fungus Candida albicans publication-title: Infect. Immun. doi: 10.1128/IAI.01680-06 – volume: 27 start-page: 35 year: 2003 ident: 10.1016/j.bbagen.2007.12.004_bib76 article-title: The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae publication-title: FEMS Microbiol. Rev. doi: 10.1016/S0168-6445(03)00017-2 – volume: 274 start-page: 16040 year: 1999 ident: 10.1016/j.bbagen.2007.12.004_bib199 article-title: Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.23.16040 |
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SubjectTerms | Antioxidants - metabolism Catalase Glutaredoxin Humans Oxidation-Reduction Oxidative Stress Pancreatitis-Associated Proteins Peroxidase Reactive Oxygen Species - metabolism Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Superoxide dismutase Thioredoxin Yap1 |
Title | Redox control and oxidative stress in yeast cells |
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