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Volumn 10, Issue 12, 2011, Pages

Protein expression regulation under oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; OXIDOREDUCTASE; PROTEINASE; PROTEOME; RNA BINDING PROTEIN; TRANSCRIPTOME; PEROXIDASE; SACCHAROMYCES CEREVISIAE PROTEIN; TSA1 PROTEIN, S CEREVISIAE;

EID: 83055163866     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.009217     Document Type: Article
Times cited : (118)

References (103)
  • 2
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • Sohal, R. S. (2002) Role of oxidative stress and protein oxidation in the aging process. Free Radic. Biol. Med. 33, 37-44
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 3
    • 34248583109 scopus 로고    scopus 로고
    • Protein oxidation, repair mechanisms and proteolysis in Saccharomyces cerevisiae
    • DOI 10.1080/15216540701225958, PII 778715388
    • Costa, V., Quintanilha, A., and Moradas-Ferreira, P. (2007) Protein oxidation, repair mechanisms and proteolysis in Saccharomyces cerevisiae. IUBMB Life 59, 293-298 (Pubitemid 46763761)
    • (2007) IUBMB Life , vol.59 , Issue.4-5 , pp. 293-298
    • Costa, V.1    Quintanilha, A.2    Moradas-Ferreira, P.3
  • 4
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • DOI 10.1023/A:1016175429877
    • Oyadomari, S., Araki, E., and Mori, M. (2002) Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Apoptosis 7, 335-345 (Pubitemid 34832258)
    • (2002) Apoptosis , vol.7 , Issue.4 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 6
    • 65649118144 scopus 로고    scopus 로고
    • Protein degradation in Parkinson disease revisited: It's complex
    • Li, H., and Guo, M. (2009) Protein degradation in Parkinson disease revisited: It's complex. J. Clin. Invest. 119, 442-445
    • (2009) J. Clin. Invest. , vol.119 , pp. 442-445
    • Li, H.1    Guo, M.2
  • 7
    • 0037176975 scopus 로고    scopus 로고
    • Heat shock proteins, inflammation, and cardiovascular disease
    • Pockley, A. G. (2002) Heat shock proteins, inflammation, and cardiovascular disease. Circulation 105, 1012-1017
    • (2002) Circulation , vol.105 , pp. 1012-1017
    • Pockley, A.G.1
  • 8
    • 43249125918 scopus 로고    scopus 로고
    • The neuronal ubiquitin-proteasome system: Murine models and their neurological phenotype
    • van Tijn, P., Hol, E. M., van Leeuwen, F. W., and Fischer, D. F. (2008) The neuronal ubiquitin-proteasome system: murine models and their neurological phenotype. Prog. Neurobiol. 85, 176-193
    • (2008) Prog. Neurobiol. , vol.85 , pp. 176-193
    • Van Tijn, P.1    Hol, E.M.2    Van Leeuwen, F.W.3    Fischer, D.F.4
  • 9
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • DOI 10.1016/j.biocel.2004.04.020, PII S1357272504001670
    • Grune, T., Jung, T., Merker, K., and Davies, K. J. (2004) Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36, 2519-2530 (Pubitemid 39119763)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.12 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.A.4
  • 10
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman, E. R. (2006) Protein oxidation and aging. Free Radic. Res. 40, 1250-1258
    • (2006) Free Radic. Res. , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 11
    • 62149149998 scopus 로고    scopus 로고
    • New insights on oxidative stress in cancer
    • Visconti, R., and Grieco, D. (2009) New insights on oxidative stress in cancer. Curr. Opin. Drug Discov. Dev. 12, 240-245
    • (2009) Curr. Opin. Drug Discov. Dev. , vol.12 , pp. 240-245
    • Visconti, R.1    Grieco, D.2
  • 15
    • 27144465421 scopus 로고    scopus 로고
    • Global gene expression profiling reveals widespread yet distinctive translational responses to different eukaryotic translation initiation factor 2B-targeting stress pathways
    • DOI 10.1128/MCB.25.21.9340-9349.2005
    • Smirnova, J. B., Selley, J. N., Sanchez-Cabo, F., Carroll, K., Eddy, A. A., McCarthy, J. E., Hubbard, S. J., Pavitt, G. D., Grant, C. M., and Ashe, M. P. (2005) Global gene expression profiling reveals widespread yet distinctive translational responses to different eukaryotic translation initiation factor 2B-targeting stress pathways. Mol. Cell Biol. 25, 9340-9349 (Pubitemid 41507835)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.21 , pp. 9340-9349
    • Smirnova, J.B.1    Selley, J.N.2    Sanchez-Cabo, F.3    Carroll, K.4    Eddy, A.A.5    McCarthy, J.E.G.6    Hubbard, S.J.7    Pavitt, G.D.8    Grant, C.M.9    Ashe, M.P.10
  • 17
    • 0034714288 scopus 로고    scopus 로고
    • Purification and kinetic analysis of eIF2B from Saccharomyces cerevisiae
    • Nika, J., Yang, W., Pavitt, G. D., Hinnebusch, A. G., and Hannig, E. M. (2000) Purification and kinetic analysis of eIF2B from Saccharomyces cerevisiae. J. Biol. Chem. 275, 26011-26017
    • (2000) J. Biol. Chem. , vol.275 , pp. 26011-26017
    • Nika, J.1    Yang, W.2    Pavitt, G.D.3    Hinnebusch, A.G.4    Hannig, E.M.5
  • 19
    • 40149096226 scopus 로고    scopus 로고
    • Posttranscriptional gene regulation by RNA-binding proteins during oxidative stress: Implications for cellular senescence
    • DOI 10.1515/BC.2008.022
    • Abdelmohsen, K., Kuwano, Y., Kim, H. H., and Gorospe, M. (2008) Post-transcriptional gene regulation by RNA-binding proteins during oxidative stress: Implications for cellular senescence. Biol. Chem. 389, 243-255 (Pubitemid 351329020)
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 243-255
    • Abdelmohsen, K.1    Kuwano, Y.2    Kim, H.H.3    Gorospe, M.4
  • 20
    • 40149100476 scopus 로고    scopus 로고
    • Regulation of proteasome-mediated protein degradation during oxidative stress and aging
    • DOI 10.1515/BC.2008.029
    • Breusing, N., and Grune, T. (2008) Regulation of proteasome-mediated protein degradation during oxidative stress and aging. Biol. Chem. 389, 203-209 (Pubitemid 351329027)
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 203-209
    • Breusing, N.1    Grune, T.2
  • 21
    • 0037401688 scopus 로고    scopus 로고
    • Targeted disruption of specific steps of the ubiquitin-proteasome pathway by oxidation in lens epithelial cells
    • DOI 10.1016/S1357-2725(02)00397-7
    • Hosler, M. R., Wang-Su, S. T., and Wagner, B. J. (2003) Targeted disruption of specific steps of the ubiquitin-proteasome pathway by oxidation in lens epithelial cells. Int. J. Biochem. Cell Biol. 35, 685-697 (Pubitemid 36369516)
    • (2003) International Journal of Biochemistry and Cell Biology , vol.35 , Issue.5 , pp. 685-697
    • Hosler, M.R.1    Wang-Su, S.-T.2    Wagner, B.J.3
  • 24
    • 33845422079 scopus 로고    scopus 로고
    • Protein-RNA cross-linking in the ribosomes of yeast under oxidative stress
    • DOI 10.1021/pr060337l
    • Mirzaei, H., and Regnier, F. (2006) Protein-RNA cross-linking in the ribosomes of yeast under oxidative stress. J. Proteome Res. 5, 3249-3259 (Pubitemid 44904316)
    • (2006) Journal of Proteome Research , vol.5 , Issue.12 , pp. 3249-3259
    • Mirzaei, H.1    Regnier, F.2
  • 25
    • 33947403221 scopus 로고    scopus 로고
    • Proteomic analysis of the oxidative stress response in Candida albicans
    • DOI 10.1002/pmic.200600575
    • Kusch, H., Engelmann, S., Albrecht, D., Morschhäuser, J., and Hecker, M. (2007) Proteomic analysis of the oxidative stress response in Candida albicans. Proteomics 7, 686-697 (Pubitemid 46450647)
    • (2007) Proteomics , vol.7 , Issue.5 , pp. 686-697
    • Kusch, H.1    Engelmann, S.2    Albrecht, D.3    Morschhauser, J.4    Hecker, M.5
  • 26
    • 77952045719 scopus 로고    scopus 로고
    • Proteomic analysis of the oxidative stress response in Kluyveromyces lactis and effect of glutathione reductase depletion
    • García-Leiro, A., Cerdán, M. E., and González-Siso, M. I. (2010) Proteomic analysis of the oxidative stress response in Kluyveromyces lactis and effect of glutathione reductase depletion. J. Proteome Res. 9, 2358-2376
    • (2010) J. Proteome Res. , vol.9 , pp. 2358-2376
    • García-Leiro, A.1    Cerdán, M.E.2    González-Siso, M.I.3
  • 27
    • 33845590717 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of the budding yeast cell cycle using acid-cleavable isotope-coded affinity tag reagents
    • DOI 10.1002/pmic.200600159
    • Flory, M. R., Lee, H., Bonneau, R., Mallick, P., Serikawa, K., Morris, D. R., and Aebersold, R. (2006) Quantitative proteomic analysis of the budding yeast cell cycle using acid-cleavable isotope-coded affinity tag reagents. Proteomics 6, 6146-6157 (Pubitemid 44935504)
    • (2006) Proteomics , vol.6 , Issue.23 , pp. 6146-6157
    • Flory, M.R.1    Lee, H.2    Bonneau, R.3    Mallick, P.4    Serikawa, K.5    Morris, D.R.6    Aebersold, R.7
  • 29
    • 53949098609 scopus 로고    scopus 로고
    • Transient transcriptional responses to stress are generated by opposing effects of mRNA production and degradation
    • Shalem, O., Dahan, O., Levo, M., Martinez, M. R., Furman, I., Segal, E., and Pilpel, Y. (2008) Transient transcriptional responses to stress are generated by opposing effects of mRNA production and degradation. Mol. Syst. Biol. 4, 223
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 223
    • Shalem, O.1    Dahan, O.2    Levo, M.3    Martinez, M.R.4    Furman, I.5    Segal, E.6    Pilpel, Y.7
  • 30
    • 65249176527 scopus 로고    scopus 로고
    • Stress-dependent coordination of transcriptome and translatome in yeast
    • Halbeisen, R. E., and Gerber, A. P. (2009) Stress-dependent coordination of transcriptome and translatome in yeast. PLoS Biol. 7, e105
    • (2009) PLoS Biol. , vol.7
    • Halbeisen, R.E.1    Gerber, A.P.2
  • 32
    • 73449116050 scopus 로고    scopus 로고
    • Loss of yeast peroxiredoxin Tsa1p induces genome instability through activation of the DNA damage checkpoint and elevation of dNTP levels
    • Tang, H. M., Siu, K. L., Wong, C. M., and Jin, D. Y. (2009) Loss of yeast peroxiredoxin Tsa1p induces genome instability through activation of the DNA damage checkpoint and elevation of dNTP levels. PLoS Genet. 5, e1000697
    • (2009) PLoS Genet. , vol.5
    • Tang, H.M.1    Siu, K.L.2    Wong, C.M.3    Jin, D.Y.4
  • 33
    • 67651202633 scopus 로고    scopus 로고
    • Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiae
    • Iraqui, I., Kienda, G., Soeur, J., Faye, G., Baldacci, G., Kolodner, R. D., and Huang, M. E. (2009) Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiae. PLoS Genet. 5, e1000524
    • (2009) PLoS Genet. , vol.5
    • Iraqui, I.1    Kienda, G.2    Soeur, J.3    Faye, G.4    Baldacci, G.5    Kolodner, R.D.6    Huang, M.E.7
  • 34
    • 77950881235 scopus 로고    scopus 로고
    • Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast
    • Sideri, T. C., Stojanovski, K., Tuite, M. F., and Grant, C. M. (2010) Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast. Proc. Natl. Acad. Sci. U.S.A. 107, 6394-6399
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 6394-6399
    • Sideri, T.C.1    Stojanovski, K.2    Tuite, M.F.3    Grant, C.M.4
  • 35
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • DOI 10.1038/nbt1270, PII NBT1270
    • Lu, P., Vogel, C., Wang, R., Yao, X., and Marcotte, E. M. (2007) Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat. Biotechnol. 25, 117-124 (Pubitemid 46087910)
    • (2007) Nature Biotechnology , vol.25 , Issue.1 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 37
    • 84155179192 scopus 로고    scopus 로고
    • RNA polymerase mapping during stress responses reveals widespread nonproductive transcription in yeast
    • Kim, T. S., Liu, C. L., Yassour, M., Holik, J., Friedman, N., Buratowski, S., and Rando, O. J. (2010) RNA polymerase mapping during stress responses reveals widespread nonproductive transcription in yeast. Genome Biol. 11, R75
    • (2010) Genome Biol. , vol.11
    • Kim, T.S.1    Liu, C.L.2    Yassour, M.3    Holik, J.4    Friedman, N.5    Buratowski, S.6    Rando, O.J.7
  • 39
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • DOI 10.1021/ac025747h
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392 (Pubitemid 35215372)
    • (2002) Analytical Chemistry , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 40
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • DOI 10.1021/ac0341261
    • Nesvizhskii, A. I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658 (Pubitemid 37082259)
    • (2003) Analytical Chemistry , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 41
    • 51649124498 scopus 로고    scopus 로고
    • Calculating absolute and relative protein abundance from mass spectrometry-based protein expression data
    • Vogel, C., and Marcotte, E. M. (2008) Calculating absolute and relative protein abundance from mass spectrometry-based protein expression data. Nat. Protoc. 3, 1444-1451
    • (2008) Nat. Protoc. , vol.3 , pp. 1444-1451
    • Vogel, C.1    Marcotte, E.M.2
  • 44
    • 0347513219 scopus 로고    scopus 로고
    • Characterizing gene sets with FuncAssociate
    • DOI 10.1093/bioinformatics/btg363
    • Berriz, G. F., King, O. D., Bryant, B., Sander, C., and Roth, F. P. (2003) Characterizing gene sets with FuncAssociate. Bioinformatics 19, 2502-2504 (Pubitemid 38016661)
    • (2003) Bioinformatics , vol.19 , Issue.18 , pp. 2502-2504
    • Berriz, G.F.1    King, O.D.2    Bryant, B.3    Sander, C.4    Roth, F.P.5
  • 46
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey, T. L., and Elkan, C. (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol. 2, 28-36
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 47
    • 77954636295 scopus 로고    scopus 로고
    • There is a steady-state transcriptome in exponentially growing yeast cells
    • Pelechano, V., and Pérez-Ortín, J. E. (2010) There is a steady-state transcriptome in exponentially growing yeast cells. Yeast 27, 413-422
    • (2010) Yeast , vol.27 , pp. 413-422
    • Pelechano, V.1    Pérez-Ortín, J.E.2
  • 48
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • DOI 10.1126/science.1163581
    • Gsponer, J., Futschik, M. E., Teichmann, S. A., and Babu, M. M. (2008) Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 322, 1365-1368 (Pubitemid 352775246)
    • (2008) Science , vol.322 , Issue.5906 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 49
    • 34249875986 scopus 로고    scopus 로고
    • Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation
    • DOI 10.1038/nsmb1249, PII NSMB1249
    • Liao, B., Hu, Y., and Brewer, G. (2007) Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation. Nat. Struct. Mol. Biol. 14, 511-518 (Pubitemid 46871812)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.6 , pp. 511-518
    • Liao, B.1    Hu, Y.2    Brewer, G.3
  • 51
    • 0032535451 scopus 로고    scopus 로고
    • A role for the yeast La protein in U6 snRNP assembly: Evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts
    • DOI 10.1093/emboj/17.24.7442
    • Pannone, B. K., Xue, D., and Wolin, S. L. (1998) A role for the yeast La protein in U6 snRNP assembly: Evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts. EMBO J. 17, 7442-7453 (Pubitemid 29002711)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7442-7453
    • Pannone, B.K.1    Xue, D.2    Wolin, S.L.3
  • 52
    • 0347717583 scopus 로고    scopus 로고
    • Identification of Lhp1p-associated RNAs by microarray analysis in Saccharomyces cerevisiae reveals association with coding and noncoding RNAs
    • DOI 10.1073/pnas.0307425100
    • Inada, M., and Guthrie, C. (2004) Identification of Lhp1p-associated RNAs by microarray analysis in Saccharomyces cerevisiae reveals association with coding and noncoding RNAs. Proc. Natl. Acad. Sci. U.S.A. 101, 434-439 (Pubitemid 38084654)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.2 , pp. 434-439
    • Inada, M.1    Guthrie, C.2
  • 53
    • 55549092781 scopus 로고    scopus 로고
    • Distinct roles for Khd1p in the localization and expression of bud-localized mRNAs in yeast
    • Hasegawa, Y., Irie, K., and Gerber, A. P. (2008) Distinct roles for Khd1p in the localization and expression of bud-localized mRNAs in yeast. RNA 14, 2333-2347
    • (2008) RNA , vol.14 , pp. 2333-2347
    • Hasegawa, Y.1    Irie, K.2    Gerber, A.P.3
  • 54
    • 54949148332 scopus 로고    scopus 로고
    • Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system
    • Hogan, D. J., Riordan, D. P., Gerber, A. P., Herschlag, D., and Brown, P. O. (2008) Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system. PLoS Biol. 6, e255
    • (2008) PLoS Biol. , vol.6
    • Hogan, D.J.1    Riordan, D.P.2    Gerber, A.P.3    Herschlag, D.4    Brown, P.O.5
  • 55
    • 36248971198 scopus 로고    scopus 로고
    • How arginine-rich domains coordinate mRNA maturation events
    • Godin, K. S., and Varani, G. (2007) How arginine-rich domains coordinate mRNA maturation events. RNA Biol. 4, 69-75 (Pubitemid 350127831)
    • (2007) RNA Biology , vol.4 , Issue.2 , pp. 69-75
    • Godin, K.S.1    Varani, G.2
  • 56
    • 0031972645 scopus 로고    scopus 로고
    • RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G
    • Kessler, S. H., and Sachs, A. B. (1998) RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 18, 51-57 (Pubitemid 28021016)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.1 , pp. 51-57
    • Kessler, S.H.1    Sachs, A.B.2
  • 57
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • Swisher, K. D., and Parker, R. (2010) Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae. PLoS ONE 5, e10006
    • (2010) PLoS ONE , vol.5
    • Swisher, K.D.1    Parker, R.2
  • 58
    • 34548535363 scopus 로고    scopus 로고
    • Cap-independent translation is required for starvation-induced differentiation in yeast
    • Gilbert, W. V., Zhou, K., Butler, T. K., and Doudna, J. A. (2007) Cap-independent translation is required for starvation-induced differentiation in yeast. Science 317, 1224-1227
    • (2007) Science , vol.317 , pp. 1224-1227
    • Gilbert, W.V.1    Zhou, K.2    Butler, T.K.3    Doudna, J.A.4
  • 59
    • 19044361932 scopus 로고    scopus 로고
    • Acquisition of tolerance against oxidative damage in Saccharomyces cerevisiae
    • Pereira, M. D., Eleutherio, E. C., and Panek, A. D. (2001) Acquisition of tolerance against oxidative damage in Saccharomyces cerevisiae. BMC Microbiol. 1, 11
    • (2001) BMC Microbiol. , vol.1 , pp. 11
    • Pereira, M.D.1    Eleutherio, E.C.2    Panek, A.D.3
  • 62
    • 0026563230 scopus 로고
    • Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress
    • Terada, T., Oshida, T., Nishimura, M., Maeda, H., Hara, T., Hosomi, S., Mizoguchi, T., and Nishihara, T. (1992) Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress. J. Biochem. 111, 688-692
    • (1992) J. Biochem. , vol.111 , pp. 688-692
    • Terada, T.1    Oshida, T.2    Nishimura, M.3    Maeda, H.4    Hara, T.5    Hosomi, S.6    Mizoguchi, T.7    Nishihara, T.8
  • 63
    • 18244385536 scopus 로고    scopus 로고
    • Protein glutathionylation: Coupling and uncoupling of glutathione to protein thiol groups in lymphocytes under oxidative stress and HIV infection
    • DOI 10.1016/S0161-5890(01)00114-6, PII S0161589001001146
    • Ghezzi, P., Romines, B., Fratelli, M., Eberini, I., Gianazza, E., Casagrande, S., Laragione, T., Mengozzi, M., and Herzenberg, L. A. (2002) Protein glutathionylation: Coupling and uncoupling of glutathione to protein thiol groups in lymphocytes under oxidative stress and HIV infection. Mol. Immunol. 38, 773-780 (Pubitemid 34158880)
    • (2002) Molecular Immunology , vol.38 , Issue.10 , pp. 773-780
    • Ghezzi, P.1    Romines, B.2    Fratelli, M.3    Eberini, I.4    Gianazza, E.5    Casagrande, S.6    Laragione, T.7    Mengozzi, M.8    Herzenberg, L.A.9    Herzenberg, L.A.10
  • 64
    • 69249208411 scopus 로고    scopus 로고
    • Activation of translation via reduction by thioredoxin-thioredoxin reductase in Saccharomyces cerevisiae
    • Jun, K. O., Song, C. H., Kim, Y. B., An, J., Oh, J. H., and Choi, S. K. (2009) Activation of translation via reduction by thioredoxin-thioredoxin reductase in Saccharomyces cerevisiae. FEBS Lett. 583, 2804-2810
    • (2009) FEBS Lett. , vol.583 , pp. 2804-2810
    • Jun, K.O.1    Song, C.H.2    Kim, Y.B.3    An, J.4    Oh, J.H.5    Choi, S.K.6
  • 65
    • 76849107684 scopus 로고    scopus 로고
    • Structure and function of yeast glutaredoxin 2 depend on postranslational processing and are related to subcellular distribution
    • Porras, P., McDonagh, B., Pedrajas, J. R., Bárcena, J. A., and Padilla, C. A. (2010) Structure and function of yeast glutaredoxin 2 depend on postranslational processing and are related to subcellular distribution. Biochim. Biophys. Acta 1804, 839-845
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 839-845
    • Porras, P.1    McDonagh, B.2    Pedrajas, J.R.3    Bárcena, J.A.4    Padilla, C.A.5
  • 66
    • 0031719952 scopus 로고    scopus 로고
    • The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species
    • Luikenhuis, S., Perrone, G., Dawes, I. W., and Grant, C. M. (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol. Biol. Cell 9, 1081-1091 (Pubitemid 28457301)
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.5 , pp. 1081-1091
    • Luikenhuis, S.1    Perrone, G.2    Dawes, I.W.3    Grant, C.M.4
  • 68
    • 0033956380 scopus 로고    scopus 로고
    • Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae
    • DOI 10.1016/S0167-4781(99)00234-1, PII S0167478199002341
    • Grant, C. M., Luikenhuis, S., Beckhouse, A., Soderbergh, M., and Dawes, I. W. (2000) Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1490, 33-42 (Pubitemid 30070131)
    • (2000) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1490 , Issue.1-2 , pp. 33-42
    • Grant, C.M.1    Luikenhuis, S.2    Beckhouse, A.3    Soderbergh, M.4    Dawes, I.W.5
  • 69
    • 0035131144 scopus 로고    scopus 로고
    • Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions
    • Grant, C. M. (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol. Microbiol. 39, 533-541
    • (2001) Mol. Microbiol. , vol.39 , pp. 533-541
    • Grant, C.M.1
  • 72
    • 0029828902 scopus 로고    scopus 로고
    • The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection
    • DOI 10.1074/jbc.271.46.28831
    • Slekar, K. H., Kosman, D. J., and Culotta, V. C. (1996) The yeast copper/ zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J. Biol. Chem. 271, 28831-28836 (Pubitemid 26382581)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.46 , pp. 28831-28836
    • Slekar, K.H.1    Kosman, D.J.2    Culotta, V.C.3
  • 73
    • 55449088127 scopus 로고    scopus 로고
    • Folding free energies of 5′-UTRs impact post-transcriptional regulation on a genomic scale in yeast
    • Ringnér, M., and Krogh, M. (2005) Folding free energies of 5′-UTRs impact post-transcriptional regulation on a genomic scale in yeast. PLoS Comput. Biol. 1, e72
    • (2005) PLoS Comput. Biol. , vol.1
    • Ringnér, M.1    Krogh, M.2
  • 74
    • 0036591853 scopus 로고    scopus 로고
    • Protein turnover by the proteasome in aging and disease
    • DOI 10.1016/S0891-5849(02)00824-9, PII S0891584902008249
    • Shringarpure, R., and Davies, K. J. (2002) Protein turnover by the proteasome in aging and disease. Free Radic. Biol. Med. 32, 1084-1089 (Pubitemid 34603346)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1084-1089
    • Shringarpure, R.1    Davies, K.J.A.2
  • 75
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • DOI 10.1074/jbc.M206279200
    • Shringarpure, R., Grune, T., Mehlhase, J., and Davies, K. J. (2003) Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J. Biol. Chem. 278, 311-318 (Pubitemid 36043578)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 77
    • 33750616737 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis
    • DOI 10.1515/BC.2006.169, PII BCHM38710111351
    • Bader, N., and Grune, T. (2006) Protein oxidation and proteolysis. Biol. Chem. 387, 1351-1355 (Pubitemid 44691414)
    • (2006) Biological Chemistry , vol.387 , Issue.10-11 , pp. 1351-1355
    • Bader, N.1    Grune, T.2
  • 78
    • 57649146490 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes
    • Zong, C., Young, G. W., Wang, Y., Lu, H., Deng, N., Drews, O., and Ping, P. (2008) Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes. Proteomics 8, 5025-5037
    • (2008) Proteomics , vol.8 , pp. 5025-5037
    • Zong, C.1    Young, G.W.2    Wang, Y.3    Lu, H.4    Deng, N.5    Drews, O.6    Ping, P.7
  • 79
    • 0037414784 scopus 로고    scopus 로고
    • 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • DOI 10.1074/jbc.M209282200
    • Demasi, M., Silva, G. M., and Netto, L. E. (2003) 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J. Biol. Chem. 278, 679-685 (Pubitemid 36043622)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.S.3
  • 80
    • 0028797005 scopus 로고
    • Degradation of proteasomes by lysosomes in rat liver
    • Cuervo, A. M., Palmer, A., Rivett, A. J., and Knecht, E. (1995) Degradation of proteasomes by lysosomes in rat liver. Eur. J. Biochem. 227, 792-800
    • (1995) Eur. J. Biochem. , vol.227 , pp. 792-800
    • Cuervo, A.M.1    Palmer, A.2    Rivett, A.J.3    Knecht, E.4
  • 81
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the brain 26S proteasome and its interacting proteins
    • Tai, H. C., Besche, H., Goldberg, A. L., and Schuman, E. M. (2010) Characterization of the brain 26S proteasome and its interacting proteins. Front. Mol. Neurosci. 3, 12
    • (2010) Front. Mol. Neurosci. , vol.3 , pp. 12
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4
  • 83
    • 0037313537 scopus 로고    scopus 로고
    • Genome-wide analysis of RNA-protein interactions illustrates specificity of the mRNA export machinery
    • DOI 10.1038/ng1080
    • Hieronymus, H., and Silver, P. A. (2003) Genome-wide analysis of RNA-protein interactions illustrates specificity of the mRNA export machinery. Nat. Genet. 33, 155-161 (Pubitemid 36177066)
    • (2003) Nature Genetics , vol.33 , Issue.2 , pp. 155-161
    • Hieronymus, H.1    Silver, P.A.2
  • 85
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell
    • Gong, Y., Kakihara, Y., Krogan, N., Greenblatt, J., Emili, A., Zhang, Z., and Houry, W. A. (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell. Mol. Syst. Biol. 5, 275
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5    Zhang, Z.6    Houry, W.A.7
  • 86
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • DOI 10.1038/nrm1618
    • Holcik, M., and Sonenberg, N. (2005) Translational control in stress and apoptosis. Nat. Rev. Mol. Cell Biol. 6, 318-327 (Pubitemid 40516898)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 87
    • 4143074740 scopus 로고    scopus 로고
    • 2 by yeast
    • DOI 10.1074/jbc.M313773200
    • Munhoz, D. C., and Netto, L. E. (2004) Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: Catalases and peroxiredoxins cooperate in the decomposition of H2O2 by yeast. J. Biol. Chem. 279, 35219-35227 (Pubitemid 39100518)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35219-35227
    • Munhoz, D.C.1    Netto, L.E.S.2
  • 88
    • 0035861895 scopus 로고    scopus 로고
    • Cytosolic thioredoxin peroxidase I is essential for the antioxidant defense of yeast with dysfunctional mitochondria
    • DOI 10.1016/S0014-5793(01)03215-X, PII S001457930103215X
    • Demasi, A. P., Pereira, G. A., and Netto, L. E. (2001) Cytosolic thioredoxin peroxidase I is essential for the antioxidant defense of yeast with dysfunctional mitochondria. FEBS Lett. 509, 430-434 (Pubitemid 34031973)
    • (2001) FEBS Letters , vol.509 , Issue.3 , pp. 430-434
    • Demasi, A.P.D.1    Pereira, G.A.G.2    Netto, L.E.S.3
  • 89
    • 55449104987 scopus 로고    scopus 로고
    • Stress-activated genomic expression changes serve a preparative role for impending stress in yeast
    • Berry, D. B., and Gasch, A. P. (2008) Stress-activated genomic expression changes serve a preparative role for impending stress in yeast. Mol. Biol. Cell 19, 4580-4587
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4580-4587
    • Berry, D.B.1    Gasch, A.P.2
  • 91
    • 10044282898 scopus 로고    scopus 로고
    • A systems view of mRNP biology
    • DOI 10.1101/gad.1256904
    • Hieronymus, H., and Silver, P. A. (2004) A systems view of mRNP biology. Genes Dev 18, 2845-2860 (Pubitemid 39602303)
    • (2004) Genes and Development , vol.18 , Issue.23 , pp. 2845-2860
    • Hieronymus, H.1    Silver, P.A.2
  • 93
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • Rice, P., Longden, I., and Bleasby, A. (2000) EMBOSS: The European Molecular Biology Open Software Suite. Trends Genet. 16, 276-277
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 94
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: Implications for structural proteomics
    • DOI 10.1016/j.str.2003.10.002
    • Linding, R., Jensen, L. J., Diella, F., Bork, P., Gibson, T. J., and Russell, R. B. (2003) Protein disorder prediction: Implications for structural proteomics. Structure 11, 1453-1459 (Pubitemid 37412427)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5    Russell, R.B.6
  • 95
    • 17844395239 scopus 로고    scopus 로고
    • Dissecting eukaryotic translation and its control by ribosome density mapping
    • DOI 10.1093/nar/gki331
    • Arava, Y., Boas, F. E., Brown, P. O., and Herschlag, D. (2005) Dissecting eukaryotic translation and its control by ribosome density mapping. Nucleic Acids Res. 33, 2421-2432 (Pubitemid 41511261)
    • (2005) Nucleic Acids Research , vol.33 , Issue.8 , pp. 2421-2432
    • Arava, Y.1    Boas, F.E.2    Brown, P.O.3    Herschlag, D.4
  • 99
  • 100
    • 34548093996 scopus 로고    scopus 로고
    • A catalog of stability-associated sequence elements in 3′ UTRs of yeast mRNAs
    • Shalgi, R., Lapidot, M., Shamir, R., and Pilpel, Y. (2005) A catalog of stability-associated sequence elements in 3′ UTRs of yeast mRNAs. Genome Biol. 6, R86
    • (2005) Genome Biol. , vol.6
    • Shalgi, R.1    Lapidot, M.2    Shamir, R.3    Pilpel, Y.4


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