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Volumn 43, Issue 2, 2009, Pages 223-231

Expression regulation of the proteasomal genes in eukaryotes

Author keywords

Proteasome; Rpn4p; Saccharomyces cerevisiae; Transcription regulation; Ubiquitin

Indexed keywords

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 65349124297     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893309020058     Document Type: Article
Times cited : (2)

References (55)
  • 2
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • S. Rogers R. Wells M. Rechstiener 1986 Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis Science 234 364 368 (Pubitemid 17181385)
    • (1986) Science , vol.234 , Issue.4774 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 3
    • 0029790893 scopus 로고    scopus 로고
    • The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe
    • H. Yamano J. Gannon T. Hunt 1996 The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe EMBO J. 15 5268 5279 (Pubitemid 26336210)
    • (1996) EMBO Journal , vol.15 , Issue.19 , pp. 5268-5279
    • Yamano, H.1    Gannon, J.2    Hunt, T.3
  • 4
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • DOI 10.1093/embo-reports/kve246
    • S. Murata Y. Minami M. Minami T. Chiba K. Tanaka 2001 CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein EMBO Rep. 2 1133 1138 (Pubitemid 34055961)
    • (2001) EMBO Reports , vol.2 , Issue.12 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 5
    • 0029036680 scopus 로고
    • P53 in complex with DNA is resistant to ubiquitin-dependent proteolysis in the presence of HPV-16 E6
    • M. Molinari J. Milner 1995 p53 in complex with DNA is resistant to ubiquitin-dependent proteolysis in the presence of HPV-16 E6 Oncogene 10 1849 1854
    • (1995) Oncogene , vol.10 , pp. 1849-1854
    • Molinari, M.1    Milner, J.2
  • 6
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • DOI 10.1016/0092-8674(93)90384-3
    • M. Scheffner J. Huibregste R.D. Vierstra P.M. Howley 1993 The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53 Cell 75 495 505 (Pubitemid 23335075)
    • (1993) Cell , vol.75 , Issue.3 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 7
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • DOI 10.1146/annurev.biochem.70.1.503
    • C.M. Pickart 2001 Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 503 533 (Pubitemid 32663902)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 9
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: A family of natural gene fusions
    • E. Ozkaynak D. Finley M.J. Solomon A. Varshavky 1987 The yeast ubiquitin genes: A family of natural gene fusions EMBO J. 6 1429 1439
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavky, A.4
  • 13
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • DOI 10.1038/416763a
    • Y. Lam T.G. Lowson M. Velayutham J.L. Zweier C.M. Pickart 2002 A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal Nature 18 763 767 (Pubitemid 34429155)
    • (2002) Nature , vol.416 , Issue.6882 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweler, J.L.4    Pickart, C.M.5
  • 14
    • 0035841193 scopus 로고    scopus 로고
    • Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome
    • G. Cagney P. Uetz S. Fields 2001 Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome Physiol. Genomics. 7 27 34
    • (2001) Physiol. Genomics. , vol.7 , pp. 27-34
    • Cagney, G.1    Uetz, P.2    Fields, S.3
  • 15
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • DOI 10.1126/science.1075898
    • R. Verma L. Aravind R. Oania W.H. [tmp] McDonald J.R. Yates E.V. Koonin R.J. Deshaies 2002 Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome Science 298 611 615 (Pubitemid 35215317)
    • (2002) Science , vol.298 , Issue.5593 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates Iii, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 16
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • DOI 10.1038/386463a0
    • M. Groll L. Ditzel J. Löwe D. Stock M. Bochtler H.D. Bartunik R. Huber 1997 Structure of 20S proteasome from yeast at a 2.4 A resolution Nature 386 463 471 (Pubitemid 27164066)
    • (1997) Nature , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5    Bartunik, H.D.6    Huber, R.7
  • 17
    • 0025123346 scopus 로고
    • The multicatalytic proteinase complex, a major extralysosomal proteolytic system
    • M. Orlowski 1990 The multicatalitic proteinase complex: A major extralysosomal proteolytic system Biochemistry 29 10289 10297 (Pubitemid 20384536)
    • (1990) Biochemistry , vol.29 , Issue.45 , pp. 10289-10297
    • Orlowski, M.1
  • 18
    • 0033004441 scopus 로고    scopus 로고
    • Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast
    • DOI 10.1016/S0014-5793(99)00467-6, PII S0014579399004676
    • G. Mannhaupt R. Schnall V. Karpov I. Vetter H. Feldmann 1999 Rpn4 acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast FEBS Lett. 450 27 34 (Pubitemid 29206706)
    • (1999) FEBS Letters , vol.450 , Issue.1-2 , pp. 27-34
    • Mannhaupt, G.1    Schnall, R.2    Karpov, V.3    Vetter, I.4    Feldmann, H.5
  • 20
    • 0033772765 scopus 로고    scopus 로고
    • Regulatory networks revealed by transcriptional profiling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes
    • S.A. Jelinsky P. Estep G.M. Church L.D. Samson 2000 Regulatory networks revealed by transcriptional profiling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes Mol. Cell Biol. 20 8157 8167
    • (2000) Mol. Cell Biol. , vol.20 , pp. 8157-8167
    • Jelinsky, S.A.1    Estep, P.2    Church, G.M.3    Samson, L.D.4
  • 21
    • 0027230956 scopus 로고
    • Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
    • M.K. Nelson T. Kurihara P.A. Silver 1993 Extragenic suppressors of mutations in the cytoplasmic C terminus of Sec63 define five genes in Saccharomyces cerevisae Genetics 134 159 173 (Pubitemid 23127219)
    • (1993) Genetics , vol.134 , Issue.1 , pp. 159-173
    • Nelson, M.K.1    Kurihara, T.2    Silver, P.A.3
  • 22
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • E. Johnston C. Ma M. Ota A. Varshavsky 1995 A proteolytic pathway that recognizes ubiquitin as a degradation signal J. Biol. Chem. 270 17442 17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnston, E.1    Ma, C.2    Ota, M.3    Varshavsky, A.4
  • 24
    • 0032548779 scopus 로고    scopus 로고
    • Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae
    • DOI 10.1016/S0014-5793(98)00084-2, PII S0014579398000842
    • M. Fujimuro K. Tanaka H. Yokosawa A. Toh-e 1998 Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae FEBS Lett. 423 149 154 (Pubitemid 28343199)
    • (1998) FEBS Letters , vol.423 , Issue.2 , pp. 149-154
    • Fujimuro, M.1    Tanaka, K.2    Yokosawa, H.3    Toh-E, A.4
  • 25
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • DOI 10.1105/tpc.12.3.319
    • R. Verma S. Chen R. Feldman D. Schieltz J. Yates R.J. Dohmen R.J. Deshaies 2000 Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes Mol. Biol. Cell. 11 3425 3439 (Pubitemid 30186303)
    • (2000) Plant Cell , vol.12 , Issue.3 , pp. 319-341
    • Peltier, J.-B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nilsson, F.5    Adamska, I.6    Van Wijk, K.J.7
  • 28
    • 2942620845 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome
    • DOI 10.1016/j.febslet.2004.04.078, PII S001457930400554X
    • M.K. London B.I. Keck P.C. Ramos R.J. Dohmen 2004 Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome FEBS Lett. 567 259 264 (Pubitemid 38748402)
    • (2004) FEBS Letters , vol.567 , Issue.2-3 , pp. 259-264
    • London, M.K.1    Keck, B.I.2    Ramos, P.C.3    Dohmen, R.J.4
  • 29
    • 3543037588 scopus 로고    scopus 로고
    • Homeostatic regulation of the proteasome via an Rpn4-dependent feedback circuit
    • DOI 10.1016/j.bbrc.2004.06.105, PII S0006291X04013853
    • D. Ju L. Wang X. Mao Y. Xie 2004 Homeostatic regulation of the proteasome via an Rpn4-dependent feedback circuit Biochem. Biophys. Res. Commun. 321 51 57 (Pubitemid 39055604)
    • (2004) Biochemical and Biophysical Research Communications , vol.321 , Issue.1 , pp. 51-57
    • Ju, D.1    Wang, L.2    Mao, X.3    Xie, Y.4
  • 30
    • 0036226237 scopus 로고    scopus 로고
    • Control of 26S proteasome expression by transcription factors regulating multidrug resistance in Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2002.02823.x
    • G. Owsianik L. Balzil M. Ghislain 2002 Control of 26S proteasome expression by transcription factors regulating multidrug resistance in Saccharomyces cerevisiae Mol. Microbiol. 43 1295 1308 (Pubitemid 34304544)
    • (2002) Molecular Microbiology , vol.43 , Issue.5 , pp. 1295-1308
    • Owsianik, G.1    Balzi, L.2    Ghislain, M.3
  • 31
    • 33644843117 scopus 로고    scopus 로고
    • A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor
    • DOI 10.1111/j.1365-2958.2006.05097.x
    • J.S. Hahn D.W. Neef D.J. Thiele 2006 A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor Mol. Microbiol. 60 240 251 (Pubitemid 43363302)
    • (2006) Molecular Microbiology , vol.60 , Issue.1 , pp. 240-251
    • Hahn, J.-S.1    Neef, D.W.2    Thiele, D.J.3
  • 32
    • 2642560445 scopus 로고    scopus 로고
    • Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent
    • DOI 10.1074/jbc.C400111200
    • D. Ju Y. Xie 2004 Proteasomal degradation of RPN4 via two distinct mechanisms: Ubiquitin-dependent and - independent J. Biol. Chem. 279 23851 23854 (Pubitemid 38725239)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 23851-23854
    • Ju, D.1    Xie, Y.2
  • 33
    • 33744960697 scopus 로고    scopus 로고
    • Identification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4
    • DOI 10.1074/jbc.M513790200
    • D. Ju Y. Xie 2006 Identification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4 J. Biol. Cell. 281 10657 10662 (Pubitemid 43855486)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.16 , pp. 10657-10662
    • Ju, D.1    Xie, Y.2
  • 34
    • 11244343965 scopus 로고    scopus 로고
    • Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase
    • DOI 10.1074/jbc.M410085200
    • L. Wang X. Mao D. Ju Y. Xie 2004 Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase J. Biol. Chem. 279 55218 55223 (Pubitemid 40066517)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55218-55223
    • Wang, L.1    Mao, X.2    Ju, D.3    Xie, Y.4
  • 35
    • 35548985701 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal
    • DOI 10.1016/j.bbamcr.2007.04.012, PII S0167488907000961
    • D. Ju H. Xu X. Wang Y. Xie 2007 Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal Biochim. Biophys. Acta. 1773 1672 1680 (Pubitemid 350018908)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.11 , pp. 1672-1680
    • Ju, D.1    Xu, H.2    Wang, X.3    Xie, Y.4
  • 36
    • 38949119689 scopus 로고    scopus 로고
    • Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation
    • D. Ju X. Wang H. Xu Y. Xie 2008 Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation Mol. Cell. Biol. 28 1404 1412
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1404-1412
    • Ju, D.1    Wang, X.2    Xu, H.3    Xie, Y.4
  • 37
    • 52149085445 scopus 로고    scopus 로고
    • Rpn4p is a positive and negative transcriptional regulatior of the ubiquitin-proteasome system
    • D.S. Karpov S.A. Osipov O.V. Preobrazhenskaya V.L. Karpov 2008 Rpn4p is a positive and negative transcriptional regulatior of the ubiquitin-proteasome system Mol. Biol. 42 518 525
    • (2008) Mol. Biol. , vol.42 , pp. 518-525
    • Karpov, D.S.1    Osipov, S.A.2    Preobrazhenskaya, O.V.3    Karpov, V.L.4
  • 38
    • 52149083053 scopus 로고    scopus 로고
    • Mapping of the Rpn4p regions responsible for transcriptional activation of proteasome genes
    • D.S. Karpov V.V. Tyutyaeva S.F. Beresten' V.L. Karpov 2008 Mapping of the Rpn4p regions responsible for transcriptional activation of proteasome genes Mol. Biol. 42 526 532
    • (2008) Mol. Biol. , vol.42 , pp. 526-532
    • Karpov, D.S.1    Tyutyaeva, V.V.2    Beresten, S.F.3    Karpov, V.L.4
  • 39
    • 53049085515 scopus 로고    scopus 로고
    • Mapping of yeast Rpn4p transactivation domains
    • D.S. Karpov V.V. Tutyaeva V.L. Karpov 2008 Mapping of yeast Rpn4p transactivation domains FEBS Lett. 582 3459 3464
    • (2008) FEBS Lett. , vol.582 , pp. 3459-3464
    • Karpov, D.S.1    Tutyaeva, V.V.2    Karpov, V.L.3
  • 40
    • 4844219971 scopus 로고    scopus 로고
    • Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-directional promoter element
    • DOI 10.1093/nar/gkh838
    • Y. Zhu W. Xiao 2004 Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-directional promoter element Nucleic Acids Res. 32 5066 5075 (Pubitemid 39445493)
    • (2004) Nucleic Acids Research , vol.32 , Issue.17 , pp. 5066-5075
    • Zhu, Y.1    Xiao, W.2
  • 42
    • 36148943839 scopus 로고    scopus 로고
    • Genomic evolution of the proteasome system among hemiascomycetous yeasts
    • DOI 10.1007/s00239-007-9031-y
    • G. Mannhaupt H. Feldmann 2007 Genomic evolution of the proteasome system among hemiascomycetous yeasts J. Mol. Evol. 65 529 540 (Pubitemid 350115435)
    • (2007) Journal of Molecular Evolution , vol.65 , Issue.5 , pp. 529-540
    • Mannhaupt, G.1    Feldmann, H.2
  • 43
    • 14044252090 scopus 로고    scopus 로고
    • Conservation and evolution of cis-regulatory systems in ascomycete fungi
    • DOI 10.1371/journal.pbio.0020398
    • A.P. Gasch A.M. Moses D.Y. Chiang H.B. Fraser M. Berardini M.B. Eisen 2004 Conservation and evolution of cis-regulatory systems in Ascomycete fungi PLoS Biol. 2 e398 (Pubitemid 40280524)
    • (2004) PLoS Biology , vol.2 , Issue.12
    • Gasch, A.P.1    Moses, A.M.2    Chiang, D.Y.3    Fraser, H.B.4    Berardini, M.5    Eisen, M.B.6
  • 44
    • 0042091963 scopus 로고    scopus 로고
    • Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13
    • DOI 10.1128/MCB.23.15.5320-5330.2003
    • J. Lundgren P. Masson C.A. Realini P. Young 2003 Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13 Mol. Cell Biol. 23 5320 5330 (Pubitemid 36950887)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.15 , pp. 5320-5330
    • Lundgren, J.1    Masson, P.2    Realini, C.A.3    Young, P.4
  • 45
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • DOI 10.1074/jbc.M301032200
    • S. Meiners D. Heyken A. Weller A. Ludwig K. Stangl P.M. Kloetzel E. Kruger 2003 Inhibition of proteasome activity induces concerted expression of proteasome genes and denovo formation of mammalian proteasomes J. Biol. Chem. 278 21517 21525 (Pubitemid 36792549)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.-M.6    Kruger, E.7
  • 46
    • 17144414925 scopus 로고    scopus 로고
    • 5 subunit increases the amount of assembled proteasome and confers ameliorated response to oxidative stress and higher survival rates
    • DOI 10.1074/jbc.M413007200
    • N. Chondrogianni C. Tzavelas A.J. Pemberton I.P. Nezis A.J. Rivett E.S. Gonos 2005 Overexpression of proteasome beta 5 subunit increases amount of assembled proteasome andconfers ameliorated response to oxidative stress and higher survival rates J. Biol. Chem. 280 11840 11850 (Pubitemid 40418498)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11840-11850
    • Chondrogianni, N.1    Tzavelas, C.2    Pemberton, A.J.3    Nezis, I.P.4    Rivett, A.J.5    Gonos, E.S.6
  • 47
    • 0842266786 scopus 로고    scopus 로고
    • Interferon-gamma: An overview of signals, mechanisms and functions
    • DOI 10.1189/jlb.0603252
    • K. Schroder P.J. Hertzog T. Ravasi D.A. Hume 2004 Interferon-γ: An overview of signals, mechanisms and functions J. Leukoc. Biol. 75 163 189 (Pubitemid 38174573)
    • (2004) Journal of Leukocyte Biology , vol.75 , Issue.2 , pp. 163-189
    • Schroder, K.1    Hertzog, P.J.2    Ravasi, T.3    Hume, D.A.4
  • 48
    • 0034254726 scopus 로고    scopus 로고
    • How Stat1 mediates constitutive gene expression: A complex of unphosphorylated Stat1 and IRF1 supports transcription of the LMP2 gene
    • M. Chatterjee-Kishore K.L. Wright J.P. Ting G.R. Stark 2000 How Stat1 mediates constitutive gene expression: A complex of unphosphorylated STAT1 and IRF1supports transcription of the LMP2 gene EMBO J. 19 4111 4122 (Pubitemid 30608549)
    • (2000) EMBO Journal , vol.19 , Issue.15 , pp. 4111-4122
    • Chatterjee-Kishore, M.1    Wright, K.L.2    Ting, J.P.-Y.3    Stark, G.R.4
  • 49
    • 0042346327 scopus 로고    scopus 로고
    • Central role of the proteasome in senescence and survival of human fibroblasts. Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
    • DOI 10.1074/jbc.M301048200
    • N. Chondrogianni F.L. Stratford I.P. Trougakos B. Friguet A.J. Rivett E.S. Gonos 2003 Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation J. Biol. Chem. 278 28026 28037 (Pubitemid 36899999)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 28026-28037
    • Chondrogianni, N.1    Stratford, F.L.L.2    Trougakos, I.P.3    Friguet, B.4    Rivett, A.J.5    Gonos, E.S.6
  • 50
    • 27744490852 scopus 로고    scopus 로고
    • HDACs and the senescent phenotype of WI-38 cells
    • DOI 10.1186/1471-2121-6-37
    • R.F. Place E.J. Noonan C. Giardia 2005 HDACs and the senescent phenotype of WI-38 cells BMC Cell Biol. 6 37 (Pubitemid 41601344)
    • (2005) BMC Cell Biology , vol.6 , pp. 37
    • Place, R.F.1    Noonan, E.J.2    Giardina, C.3
  • 51
    • 18944392199 scopus 로고    scopus 로고
    • Identification and characterization of a Drosophila proteasome regulatory network
    • DOI 10.1128/MCB.25.11.4662-4675.2005
    • J. Lundgren P. Masson Z. Mirzaei P. Young 2005 Identification and characterization of a Drosophila proteasome regulatory network Mol. Cell. Biol. 25 4662 4675 (Pubitemid 40705769)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.11 , pp. 4662-4675
    • Lundgren, J.1    Masson, P.2    Mirzaei, Z.3    Young, P.4
  • 52
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants Enhance Mammalian Proteasome Expression through the Keap1-Nrf2 Signaling Pathway
    • DOI 10.1128/MCB.23.23.8786-8794.2003
    • M.K. Kwak N. Wakabayashi J.L. Greenlaw M. Yamamoto T.W. Kensler 2003 Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway Mol. Cell. Biol. 23 8786 8794 (Pubitemid 37433379)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.23 , pp. 8786-8794
    • Kwak, M.-K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 53
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element: Degradation of Nrf2 by the 26 S proteasome
    • DOI 10.1074/jbc.M207293200
    • T. Nguyen P.J. Sherratt H.C. Huang C.S. Yang C.B. Pickett 2003 Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26S proteasome J. Biol. Chem. 278 4536 4541 (Pubitemid 36800950)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.-C.3    Yang, C.S.4    Pickett, C.B.5
  • 54
    • 10844247029 scopus 로고    scopus 로고
    • The transcriptional response to a peroxisome proliferator-activated receptor alpha agonist includes increased expression of proteome maintenance genes
    • DOI 10.1074/jbc.M409347200
    • S.P. Anderson P. Howroyd J. Liu X. Qian R. Bahnemann C. Swanson M.K. Kwak T.W. Kensler J.C. Corton 2004 The transcriptional response to a peroxisome proliferators-activated receptor alpha agonist includes increased expression of proteome maintenance genes J. Biol. Chem. 279 52390 52398 (Pubitemid 39662730)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52390-52398
    • Anderson, S.P.1    Howroyd, P.2    Liu, J.3    Qian, X.4    Bahnemann, R.5    Swanson, C.6    Kwak, M.-K.7    Kensler, T.W.8    Corton, J.C.9
  • 55
    • 26944432044 scopus 로고    scopus 로고
    • Proteasome activity or expression is not altered by activation of the heat shock transcription factor Hsf1 in cultured fibroblasts or myoblasts
    • DOI 10.1379/CSC-119R.1
    • D.M. Taylor E. Kabashi J.N. Agar S. Minotti H.D. Durham 2005 Proteasome activity or expression is not altered by activation of the heat shock transcription factor Hsf1 in cultured fibroblasts or myoblasts Cell Stress Chaperones 10 230 241 (Pubitemid 41813370)
    • (2005) Cell Stress and Chaperones , vol.10 , Issue.3 , pp. 230-241
    • Taylor, D.M.1    Kabashi, E.2    Agar, J.N.3    Minotti, S.4    Durham, H.D.5


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