메뉴 건너뛰기




Volumn 2, Issue 8, 2012, Pages 943-959

Loss of a 20S proteasome activator in saccharomyces cerevisiae downregulates genes important for genomic integrity, increases DNA damage, and selectively sensitizes cells to agents with diverse mechanisms of action

Author keywords

20S proteasome activator; BLM10 PA200; DNA damage; Molecular chaperones; UBP3 BLM3

Indexed keywords

ANTINEOPLASTIC AGENT; BLM10 PROTEIN, S CEREVISIAE; CHAPERONE; OXIDIZING AGENT; PROTEASOME; PROTEINASE; SACCHAROMYCES CEREVISIAE PROTEIN; UBP3 PROTEIN, S CEREVISIAE;

EID: 84883572040     PISSN: None     EISSN: 21601836     Source Type: Journal    
DOI: 10.1534/g3.112.003376     Document Type: Article
Times cited : (25)

References (101)
  • 1
    • 0842282564 scopus 로고    scopus 로고
    • A genomewide screen in Saccharomyces cerevisiae reveals altered transport as a mechanism of resistance to the anticancer drug bleomycin
    • Aouida, M., N. Page, A. Leduc, M. Peter, and D. Ramotar, 2004 A genomewide screen in Saccharomyces cerevisiae reveals altered transport as a mechanism of resistance to the anticancer drug bleomycin. Cancer Res. 64: 1102-1109.
    • (2004) Cancer Res. , vol.64 , pp. 1102-1109
    • Aouida, M.1    Page, N.2    Leduc, A.3    Peter, M.4    Ramotar, D.5
  • 2
    • 22144443549 scopus 로고    scopus 로고
    • Upregulation of heat shock protein expression by proteasome inhibition: an antiapoptotic mechanism in the lens
    • Awasthi, N., and B. J. Wagner, 2005 Upregulation of heat shock protein expression by proteasome inhibition: an antiapoptotic mechanism in the lens. Invest. Ophthalmol. Vis. Sci. 46: 2082-2091.
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 2082-2091
    • Awasthi, N.1    Wagner, B.J.2
  • 3
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., D. Finley, and A. Varshavsky, 1986 In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 5
    • 0031821736 scopus 로고    scopus 로고
    • Isolation of UBP3, encoding a deubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S
    • Baxter, B. K., and E. A. Craig, 1998 Isolation of UBP3, encoding a deubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae. Curr. Genet. 33: 412-419.
    • (1998) cerevisiae. Curr. Genet. , vol.33 , pp. 412-419
    • Baxter, B.K.1    Craig, E.A.2
  • 6
    • 0027155371 scopus 로고
    • Bleomycin affects cell wall anchorage of mannoproteins in Saccharomyces cerevisiae
    • Beaudouin, R., S. T. Lim, J. A. Steide, M. Powell, J. McKoy et al., 1993 Bleomycin affects cell wall anchorage of mannoproteins in Saccharomyces cerevisiae. Antimicrob. Agents Chemother. 37: 1264-1269.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1264-1269
    • Beaudouin, R.1    Lim, S.T.2    Steide, J.A.3    Powell, M.4    McKoy, J.5
  • 8
    • 34447549100 scopus 로고    scopus 로고
    • Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation
    • Blickwedehl, J., S. McEvoy, I. Wong, P. Kousis, J. Clements et al., 2007 Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation. Radiat. Res. 167: 663-674.
    • (2007) Radiat. Res. , vol.167 , pp. 663-674
    • Blickwedehl, J.1    McEvoy, S.2    Wong, I.3    Kousis, P.4    Clements, J.5
  • 9
    • 55849123303 scopus 로고    scopus 로고
    • Role for proteasome activator PA200 and postglutamyl proteasome activity in genomic stability
    • Blickwedehl, J., M. Agarwal, C. Seong, R. K. Pandita, T. Melendy et al., 2008 Role for proteasome activator PA200 and postglutamyl proteasome activity in genomic stability. Proc. Natl. Acad. Sci. USA 105: 16165-16170.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16165-16170
    • Blickwedehl, J.1    Agarwal, M.2    Seong, C.3    Pandita, R.K.4    Melendy, T.5
  • 10
    • 18244376808 scopus 로고    scopus 로고
    • Homeostatic adjustment and metabolic remodeling in glucoselimited yeast cultures
    • Brauer, M. J., A. J. Saldanha, K. Dolinski, and D. Botstein, 2005 Homeostatic adjustment and metabolic remodeling in glucoselimited yeast cultures. Mol. Biol. Cell 16: 2503-2517.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2503-2517
    • Brauer, M.J.1    Saldanha, A.J.2    Dolinski, K.3    Botstein, D.4
  • 11
    • 38749112941 scopus 로고    scopus 로고
    • Coordination of growth rate, cell cycle, stress response, and metabolic activity in yeast
    • Brauer, M. J., C. Huttenhower, E. M. Airoldi, R. Rosenstein, J. C. Matese et al., 2008 Coordination of growth rate, cell cycle, stress response, and metabolic activity in yeast. Mol. Biol. Cell 19: 352-367.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 352-367
    • Brauer, M.J.1    Huttenhower, C.2    Airoldi, E.M.3    Rosenstein, R.4    Matese, J.C.5
  • 12
    • 0036862055 scopus 로고    scopus 로고
    • The yeast ubiquitin protease, Ubp3p, promotes protein stability
    • Brew, C. T., and T. C. Huffaker, 2002 The yeast ubiquitin protease, Ubp3p, promotes protein stability. Genetics 162: 1079-1089.
    • (2002) Genetics , vol.162 , pp. 1079-1089
    • Brew, C.T.1    Huffaker, T.C.2
  • 14
    • 0034708356 scopus 로고    scopus 로고
    • A genome-wide screening in Saccharomyces cerevisiae for genes that confer resistance to the anticancer agent cisplatin
    • Burger, H., A. Capelloa, P. W. Schenka, G. Stotera, J. Brouwerb et al., 2000 A genome-wide screening in Saccharomyces cerevisiae for genes that confer resistance to the anticancer agent cisplatin. Biochem. Biophys. Res. Commun. 269: 767-774.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 767-774
    • Burger, H.1    Capelloa, A.2    Schenka, P.W.3    Stotera, G.4    Brouwerb, J.5
  • 15
    • 33645121980 scopus 로고    scopus 로고
    • Microarray analysis of bleomycin-exposed lymphoblastoid cells for identifying cancer susceptibility genes
    • Cloos, J., W. P. De Boer, M. H. Snel, P. Van Den Ijssel, B. Ylstra et al., 2006 Microarray analysis of bleomycin-exposed lymphoblastoid cells for identifying cancer susceptibility genes. Mol. Cancer Res. 4: 71-77.
    • (2006) Mol. Cancer Res. , vol.4 , pp. 71-77
    • Cloos, J.1    De Boer, W.P.2    Snel, M.H.3    Van Den Ijssel, P.4    Ylstra, B.5
  • 17
    • 83355169695 scopus 로고    scopus 로고
    • Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism
    • Dange, T., D. Smith, T. Noy, P. C. Rommel, L. Jurzitza et al., 2011 Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. J. Biol. Chem. 286: 42830-42839.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42830-42839
    • Dange, T.1    Smith, D.2    Noy, T.3    Rommel, P.C.4    Jurzitza, L.5
  • 18
    • 0036829476 scopus 로고    scopus 로고
    • Impaired mitochondrial function protects against free radicalmediated cell death
    • Davermann, D., M. Martinez, J. McKoy, N. Patel, D. Averbeck et al., 2002 Impaired mitochondrial function protects against free radicalmediated cell death. Free Radic. Biol. Med. 33: 1209-1220.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1209-1220
    • Davermann, D.1    Martinez, M.2    McKoy, J.3    Patel, N.4    Averbeck, D.5
  • 19
    • 79959635260 scopus 로고    scopus 로고
    • Mitomycin C DNA interstrand crosslink repair and cancer
    • Deans, A. J., and S. C. West, 2011 Mitomycin C DNA interstrand crosslink repair and cancer. Nat. Rev. Cancer 11: 467-480.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 467-480
    • Deans, A.J.1    West, S.C.2
  • 20
    • 34249085552 scopus 로고    scopus 로고
    • Proteasomes: machines for all reasons
    • Demartino, G. N., and T. G. Gillette, 2007 Proteasomes: machines for all reasons. Cell 129: 659-662.
    • (2007) Cell , vol.129 , pp. 659-662
    • Demartino, G.N.1    Gillette, T.G.2
  • 21
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: enzymology and biology
    • Demple, B., and L. Harrison, 1994 Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63: 915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 22
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M., 2003 Protein folding and misfolding. Nature 426: 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 23
    • 6344289159 scopus 로고    scopus 로고
    • Expression of the expanded YFL007w ORF and assignment of the gene name BLM10
    • Doherty, K., A. Pramanik, L. Pride, J. Lukose, and C. W. Moore, 2004 Expression of the expanded YFL007w ORF and assignment of the gene name BLM10. Yeast 21: 1021-1023.
    • (2004) Yeast , vol.21 , pp. 1021-1023
    • Doherty, K.1    Pramanik, A.2    Pride, L.3    Lukose, J.4    Moore, C.W.5
  • 24
    • 65649154116 scopus 로고    scopus 로고
    • Myeloma cells exhibit an increase in proteasome activity and an enhanced response to proteasome inhibition in the bone marrow microenvironment in vivo
    • Edwards, C. M., S. T. Lwin, J. A. Fowler, B. O. Oyajobi, J. Zhuang et al., 2009 Myeloma cells exhibit an increase in proteasome activity and an enhanced response to proteasome inhibition in the bone marrow microenvironment in vivo. Am. J. Hematol. 84: 268-272.
    • (2009) Am. J. Hematol. , vol.84 , pp. 268-272
    • Edwards, C.M.1    Lwin, S.T.2    Fowler, J.A.3    Oyajobi, B.O.4    Zhuang, J.5
  • 25
    • 0035524343 scopus 로고    scopus 로고
    • The novel BLM3 gene encodes a protein that protects against lethal effects of oxidative damage
    • Febres, D. E., A. Pramanik, M. Caton, K. Doherty, J. McKoy et al., 2001 The novel BLM3 gene encodes a protein that protects against lethal effects of oxidative damage. Cell Mol Biol (Noisy-le-grand) 47: 1149-1162.
    • (2001) Cell Mol Biol (Noisy-le-grand) , vol.47 , pp. 1149-1162
    • Febres, D.E.1    Pramanik, A.2    Caton, M.3    Doherty, K.4    McKoy, J.5
  • 26
    • 0242522904 scopus 로고    scopus 로고
    • Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
    • Fehlker, M., P. Wendler, A. Lehmann, and C. Enenkel, 2003 Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 4: 959-963.
    • (2003) EMBO Rep. , vol.4 , pp. 959-963
    • Fehlker, M.1    Wendler, P.2    Lehmann, A.3    Enenkel, C.4
  • 27
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D., 2009 Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78: 477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 30
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Academic Press, Inc., San Diego, California
    • Gietz, R. D., and R. A. Woods, 2002 Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method, pp. 87-96 in Methods in Enzymology, edited by C. Guthrie, and G. R. Fink. Academic Press, Inc., San Diego, California.
    • (2002) Methods in Enzymology, edited by C. Guthrie, and G. R. Fink , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 31
    • 0242522907 scopus 로고    scopus 로고
    • The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its function
    • Gilbert, C. S., M. Van Den Bosch, C. M. Green, J. E. Vialard, M. Grenon et al., 2003 The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its function. EMBO Rep. 4: 953-958.
    • (2003) EMBO Rep. , vol.4 , pp. 953-958
    • Gilbert, C.S.1    Van Den Bosch, M.2    Green, C.M.3    Vialard, J.E.4    Grenon, M.5
  • 32
    • 20444384416 scopus 로고    scopus 로고
    • Proteasome plasticity
    • Glickman, M. H., and D. Raveh, 2005 Proteasome plasticity. FEBS Lett. 579: 3214-3223.
    • (2005) FEBS Lett. , vol.579 , pp. 3214-3223
    • Glickman, M.H.1    Raveh, D.2
  • 33
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L., 2003 Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 35
    • 0033592983 scopus 로고    scopus 로고
    • Rapamycin-modulated transcription defines the subset of nutri-ent-sensitive signaling pathways directly controlled by the Tor proteins
    • Hardwick, J. S., F. G. Kuruvilla, J. K. Tong, A. F. Shamji, and S. L. Schreiber, 1999 Rapamycin-modulated transcription defines the subset of nutri-ent-sensitive signaling pathways directly controlled by the Tor proteins. Proc. Natl. Acad. Sci. USA 96: 14866-14870.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14866-14870
    • Hardwick, J.S.1    Kuruvilla, F.G.2    Tong, J.K.3    Shamji, A.F.4    Schreiber, S.L.5
  • 36
    • 0033977579 scopus 로고    scopus 로고
    • Increased coverage of protein families with the blocks database servers
    • Henikoff, J. G., E. A. Greene, S. Pietrokovski, and S. Henikoff, 2000 Increased coverage of protein families with the blocks database servers. Nucleic Acids Res. 28: 228-230.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 228-230
    • Henikoff, J.G.1    Greene, E.A.2    Pietrokovski, S.3    Henikoff, S.4
  • 37
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima, T., P. Richardson, D. Chauhan, V. J. Palombella, P. J. Elliott et al., 2001 The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res. 61: 3071-3076.
    • (2001) Cancer Res. , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5
  • 38
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y., A. Gruhler, A. Heilbut, G. D. Bader, L. Moore et al., 2002 Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5
  • 39
    • 77952543134 scopus 로고    scopus 로고
    • Protein complexes/aggregates as potential cancer biomarkers revealed by a nanoparticle aggregation immunoassay
    • Huo, Q., 2010 Protein complexes/aggregates as potential cancer biomarkers revealed by a nanoparticle aggregation immunoassay. Colloids Surf. B Biointerfaces 78: 259-265.
    • (2010) Colloids Surf. B Biointerfaces , vol.78 , pp. 259-265
    • Huo, Q.1
  • 40
    • 33749265270 scopus 로고    scopus 로고
    • Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes
    • Iwanczyk, J., K. Sadre-Bazzaz, K. Ferrell, E. Kondrashkina, T. Formosa et al., 2006 Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. J. Mol. Biol. 363: 648-659.
    • (2006) J. Mol. Biol. , vol.363 , pp. 648-659
    • Iwanczyk, J.1    Sadre-Bazzaz, K.2    Ferrell, K.3    Kondrashkina, E.4    Formosa, T.5
  • 41
    • 33847380754 scopus 로고    scopus 로고
    • Circulating proteasome levels are an independent prognostic factor for survival in multiple myeloma
    • Jakob, C., K. Egerer, P. Liebisch, S. Turkmen, I. Zavrski et al., 2007 Circulating proteasome levels are an independent prognostic factor for survival in multiple myeloma. Blood 109: 2100-2105.
    • (2007) Blood , vol.109 , pp. 2100-2105
    • Jakob, C.1    Egerer, K.2    Liebisch, P.3    Turkmen, S.4    Zavrski, I.5
  • 42
    • 1942489340 scopus 로고    scopus 로고
    • New HEAT-like repeat motifs in proteins regulating proteasome structure and function
    • Kajava, A. V., C. Gorbea, J. Ortega, M. Rechsteiner, and A. C. Steven, 2004 New HEAT-like repeat motifs in proteins regulating proteasome structure and function. J. Struct. Biol. 146: 425-430.
    • (2004) J. Struct. Biol. , vol.146 , pp. 425-430
    • Kajava, A.V.1    Gorbea, C.2    Ortega, J.3    Rechsteiner, M.4    Steven, A.C.5
  • 44
    • 19944388882 scopus 로고    scopus 로고
    • Proteasome involvement in the repair of DNA double-strand breaks
    • Krogan, N. J., M. H. Lam, J. Fillingham, M. C. Keogh, M. Gebbia et al., 2004 Proteasome involvement in the repair of DNA double-strand breaks. Mol. Cell 16: 1027-1034.
    • (2004) Mol. Cell , vol.16 , pp. 1027-1034
    • Krogan, N.J.1    Lam, M.H.2    Fillingham, J.3    Keogh, M.C.4    Gebbia, M.5
  • 46
    • 57049135155 scopus 로고    scopus 로고
    • Blm10 binds to pre-activated proteasome core particles with open gate conformation
    • Lehmann, A., K. Jechow, and C. Enenkel, 2008 Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep. 9: 1237-1243.
    • (2008) EMBO Rep. , vol.9 , pp. 1237-1243
    • Lehmann, A.1    Jechow, K.2    Enenkel, C.3
  • 47
    • 0034733497 scopus 로고    scopus 로고
    • Tying up loose ends: nonhomologous end-joining in Saccharomyces cerevisiae
    • Lewis, L. K., and M. A. Resnick, 2000 Tying up loose ends: nonhomologous end-joining in Saccharomyces cerevisiae. Mutat. Res. 451: 71-89.
    • (2000) Mutat. Res. , vol.451 , pp. 71-89
    • Lewis, L.K.1    Resnick, M.A.2
  • 48
    • 34247617365 scopus 로고    scopus 로고
    • beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint
    • Li, X., A. R. Kusmierczyk, P. Wong, A. Emili, and M. Hochstrasser, 2007 beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J. 26: 2339-2349.
    • (2007) EMBO J. , vol.26 , pp. 2339-2349
    • Li, X.1    Kusmierczyk, A.R.2    Wong, P.3    Emili, A.4    Hochstrasser, M.5
  • 49
    • 79952342817 scopus 로고    scopus 로고
    • Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10
    • Lopez, A. D., K. Tar, U. Krügel, T. Dange, I. G. Ros et al., 2011 Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10. Mol. Biol. Cell 22: 528-540.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 528-540
    • Lopez, A.D.1    Tar, K.2    Krügel, U.3    Dange, T.4    Ros, I.G.5
  • 50
    • 0029741095 scopus 로고    scopus 로고
    • A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae
    • Ma, X. J., Q. Lu, and M. Grunstein, 1996 A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae. Genes Dev. 10: 1327-1340.
    • (1996) Genes Dev. , vol.10 , pp. 1327-1340
    • Ma, X.J.1    Lu, Q.2    Grunstein, M.3
  • 51
    • 78549277226 scopus 로고    scopus 로고
    • Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation
    • Mao, P., and M. J. Smerdon, 2010 Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation. J. Biol. Chem. 285: 37542-37550.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37542-37550
    • Mao, P.1    Smerdon, M.J.2
  • 52
    • 36849024844 scopus 로고    scopus 로고
    • The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation
    • Marques, A. J., C. Glanemann, P. C. Ramos, and R. J. Dohmen, 2007 The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation. J. Biol. Chem. 282: 34869-34876.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34869-34876
    • Marques, A.J.1    Glanemann, C.2    Ramos, P.C.3    Dohmen, R.J.4
  • 53
    • 0033612287 scopus 로고    scopus 로고
    • Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast
    • Martin, S. G., T. Laroche, N. Suka, M. Grunstein, and S. M. Gasser, 1999 Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast. Cell 97: 621-633.
    • (1999) Cell , vol.97 , pp. 621-633
    • Martin, S.G.1    Laroche, T.2    Suka, N.3    Grunstein, M.4    Gasser, S.M.5
  • 54
    • 0033527694 scopus 로고    scopus 로고
    • A biochemical genomics approach for identifying genes by the activity of their products
    • Martzen, M. R., S. M. McCraith, S. L. Spinelli, F. M. Torres, S. Fields et al., 1999 A biochemical genomics approach for identifying genes by the activity of their products. Science 286: 1153-1155.
    • (1999) Science , vol.286 , pp. 1153-1155
    • Martzen, M.R.1    McCraith, S.M.2    Spinelli, S.L.3    Torres, F.M.4    Fields, S.5
  • 55
    • 0029935849 scopus 로고    scopus 로고
    • Construction of a CUP1 promoter-based vector to modulate gene expression in Saccharomyces cerevisiae
    • Mascorro-Gallardo, J. O., A. A. Covarrubias, and R. Gaxiola, 1996 Construction of a CUP1 promoter-based vector to modulate gene expression in Saccharomyces cerevisiae. Gene 172: 169-170.
    • (1996) Gene , vol.172 , pp. 169-170
    • Mascorro-Gallardo, J.O.1    Covarrubias, A.A.2    Gaxiola, R.3
  • 56
    • 33749244672 scopus 로고    scopus 로고
    • blm3-1 is an allele of UBP3, a ubiquitin protease that appears to act during transcription of damaged DNA
    • McCullock, S., T. Kinard, L. McCullough, and T. Formosa, 2006 blm3-1 is an allele of UBP3, a ubiquitin protease that appears to act during transcription of damaged DNA. J. Mol. Biol. 363: 660-672.
    • (2006) J. Mol. Biol. , vol.363 , pp. 660-672
    • McCullock, S.1    Kinard, T.2    McCullough, L.3    Formosa, T.4
  • 58
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S
    • Moazed, D., and D. Johnson, 1996 A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86: 667-677.
    • (1996) cerevisiae. Cell , vol.86 , pp. 667-677
    • Moazed, D.1    Johnson, D.2
  • 59
    • 0017820581 scopus 로고
    • Responses of radiation-sensitive mutants of Saccharomyces cerevisiae to lethal effects of bleomycin
    • Moore, C. W., 1978 Responses of radiation-sensitive mutants of Saccharomyces cerevisiae to lethal effects of bleomycin. Mutat. Res. 51: 165-180.
    • (1978) Mutat. Res. , vol.51 , pp. 165-180
    • Moore, C.W.1
  • 60
    • 0020054324 scopus 로고
    • Control of in vivo (cellular) phleomycin sensitivity by nuclear genotype, growth phase, and metal ions
    • Moore, C. W., 1982 Control of in vivo (cellular) phleomycin sensitivity by nuclear genotype, growth phase, and metal ions. Cancer Res. 42: 929-933.
    • (1982) Cancer Res. , vol.42 , pp. 929-933
    • Moore, C.W.1
  • 61
    • 0024240419 scopus 로고
    • Internucleosomal cleavage and chromosomal degradation by bleomycin and phleomycin in yeast
    • Moore, C. W., 1988 Internucleosomal cleavage and chromosomal degradation by bleomycin and phleomycin in yeast. Cancer Res. 48: 6837-6843.
    • (1988) Cancer Res. , vol.48 , pp. 6837-6843
    • Moore, C.W.1
  • 62
    • 0025190891 scopus 로고
    • Degradation of DNA and structure-activity relationship between bleomycins A2 and B2 in the absence of DNA repair
    • Moore, C. W., 1990 Degradation of DNA and structure-activity relationship between bleomycins A2 and B2 in the absence of DNA repair. Biochemistry 29: 1342-1347.
    • (1990) Biochemistry , vol.29 , pp. 1342-1347
    • Moore, C.W.1
  • 63
    • 0025878391 scopus 로고
    • Further characterizations of bleomycin-sensitive (blm) mutants of Saccharomyces cerevisiae with implications for a radiomimetic model
    • Moore, C. W., 1991 Further characterizations of bleomycin-sensitive (blm) mutants of Saccharomyces cerevisiae with implications for a radiomimetic model. J. Bacteriol. 173: 3605-3608.
    • (1991) J. Bacteriol. , vol.173 , pp. 3605-3608
    • Moore, C.W.1
  • 65
    • 0026437665 scopus 로고
    • Lesions and preferential initial localization of [S-methyl-3H] bleomycin A2 on Saccharomyces cerevisiae cell walls and membranes
    • Moore, C. W., R. Del Valle, J. McKoy, A. Pramanik, and R. E. Gordon, 1992 Lesions and preferential initial localization of [S-methyl-3H] bleomycin A2 on Saccharomyces cerevisiae cell walls and membranes. Antimicrob. Agents Chemother. 36: 2497-2505.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 2497-2505
    • Moore, C.W.1    Del Valle, R.2    McKoy, J.3    Pramanik, A.4    Gordon, R.E.5
  • 66
    • 0034100331 scopus 로고    scopus 로고
    • DNA damage-inducible and RAD52-independent repair of DNA double-strand breaks in Saccharomyces cerevisiae
    • Moore, C. W., J. McKoy, M. Dardalhon, D. Davermann, M. Martinez et al., 2000 DNA damage-inducible and RAD52-independent repair of DNA double-strand breaks in Saccharomyces cerevisiae. Genetics 154: 1085-1099.
    • (2000) Genetics , vol.154 , pp. 1085-1099
    • Moore, C.W.1    McKoy, J.2    Dardalhon, M.3    Davermann, D.4    Martinez, M.5
  • 68
  • 69
    • 33745113181 scopus 로고    scopus 로고
    • Discovery of biological networks from diverse functional genomic data
    • Myers, C. L., D. Robson, A. Wible, M. A. Hibbs, C. Chiriac et al., 2005 Discovery of biological networks from diverse functional genomic data. Genome Biol. 6: R114.
    • (2005) Genome Biol. , vol.6
    • Myers, C.L.1    Robson, D.2    Wible, A.3    Hibbs, M.A.4    Chiriac, C.5
  • 70
    • 77954998449 scopus 로고    scopus 로고
    • Proteomics: a strategy to understand the novel targets in protein misfolding and cancer therapy
    • Nagaraj, N. S., O. V. Singh, and N. B. Merchant, 2010 Proteomics: a strategy to understand the novel targets in protein misfolding and cancer therapy. Expert Rev. Proteomics 7: 613-623.
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 613-623
    • Nagaraj, N.S.1    Singh, O.V.2    Merchant, N.B.3
  • 72
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: lessons from the first decade
    • Orlowski, R. Z., and D. J. Kuhn, 2008 Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin. Cancer Res. 14: 1649-1657.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 73
    • 13844280355 scopus 로고    scopus 로고
    • The axial channel of the 20S proteasome opens upon binding of the PA200 activator
    • Ortega, J., J. B. Heymann, A. V. Kajava, V. Ustrell, M. Rechsteiner et al., 2005 The axial channel of the 20S proteasome opens upon binding of the PA200 activator. J. Mol. Biol. 346: 1221-1227.
    • (2005) J. Mol. Biol. , vol.346 , pp. 1221-1227
    • Ortega, J.1    Heymann, J.B.2    Kajava, A.V.3    Ustrell, V.4    Rechsteiner, M.5
  • 74
    • 33644778778 scopus 로고    scopus 로고
    • A DNA integrity network in the yeast Saccharomyces cerevisiae
    • Pan, X., P. Ye, D. S. Yuan, X. Wang, J. S. Bader et al., 2006 A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell 124: 1069-1081.
    • (2006) Cell , vol.124 , pp. 1069-1081
    • Pan, X.1    Ye, P.2    Yuan, D.S.3    Wang, X.4    Bader, J.S.5
  • 75
    • 0347473810 scopus 로고    scopus 로고
    • Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways
    • Parsons, A. B., R. L. Brost, H. Ding, Z. Li, C. Zhang et al., 2004 Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways. Nat. Biotechnol. 22: 62-69.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 62-69
    • Parsons, A.B.1    Brost, R.L.2    Ding, H.3    Li, Z.4    Zhang, C.5
  • 76
    • 0034680759 scopus 로고    scopus 로고
    • A novel strategy for constructing N-terminal chromosomal fusions to green fluorescent protein in the yeast Saccharomyces cerevisiae
    • Prein, B., K. Natter, and S. D. Kohlwein, 2000 A novel strategy for constructing N-terminal chromosomal fusions to green fluorescent protein in the yeast Saccharomyces cerevisiae. FEBS Lett. 485: 29-34.
    • (2000) FEBS Lett. , vol.485 , pp. 29-34
    • Prein, B.1    Natter, K.2    Kohlwein, S.D.3
  • 77
    • 0036081709 scopus 로고    scopus 로고
    • Proteasome inhibitors induce heat shock response and increase IL-6 expression in human intestinal epithelial cells
    • Pritts, T. A., E. S. Hungness, D. D. Hershko, B. W. Robb, X. Sun et al., 2002 Proteasome inhibitors induce heat shock response and increase IL-6 expression in human intestinal epithelial cells. Am. J. Physiol. Regul. Integr. Comp. Physiol. 282: R1016-R1026.
    • (2002) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.282
    • Pritts, T.A.1    Hungness, E.S.2    Hershko, D.D.3    Robb, B.W.4    Sun, X.5
  • 78
    • 0018126018 scopus 로고
    • A comparative study of ethidium bromide complexes with dinucleotides and DNA: direct evidence for intercalation and nucleic acid sequence preferences
    • Reinhardt, C. G., and T. R. Krugh, 1978 A comparative study of ethidium bromide complexes with dinucleotides and DNA: direct evidence for intercalation and nucleic acid sequence preferences. Biochemistry 17: 4845-4854.
    • (1978) Biochemistry , vol.17 , pp. 4845-4854
    • Reinhardt, C.G.1    Krugh, T.R.2
  • 79
    • 0020645053 scopus 로고
    • Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast
    • Rose, M., and D. Botstein, 1983 Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast. Methods Enzymol. 101: 167-180.
    • (1983) Methods Enzymol. , vol.101 , pp. 167-180
    • Rose, M.1    Botstein, D.2
  • 80
    • 0025975312 scopus 로고
    • Cloning genes by complementation in yeast
    • Rose, M. D., and J. R. Broach, 1991 Cloning genes by complementation in yeast. Methods Enzymol. 194: 195-230.
    • (1991) Methods Enzymol. , vol.194 , pp. 195-230
    • Rose, M.D.1    Broach, J.R.2
  • 81
  • 82
    • 0033618256 scopus 로고    scopus 로고
    • Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast
    • Russell, S. J., K. A. Steger, and S. A. Johnston, 1999 Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast. J. Biol. Chem. 274: 21943-21952.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21943-21952
    • Russell, S.J.1    Steger, K.A.2    Johnston, S.A.3
  • 83
    • 77649243592 scopus 로고    scopus 로고
    • Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening
    • Sadre-Bazzaz, K., F. G. Whitby, H. Robinson, T. Formosa, and C. P. Hill, 2010 Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol. Cell 37: 728-735.
    • (2010) Mol. Cell , vol.37 , pp. 728-735
    • Sadre-Bazzaz, K.1    Whitby, F.G.2    Robinson, H.3    Formosa, T.4    Hill, C.P.5
  • 84
    • 0035206628 scopus 로고    scopus 로고
    • Hydroxyurea induces site-specific DNA damage via formation of hydrogen peroxide and nitric oxide
    • Sakano, K., S. Oikawa, K. Hasegawa, and S. Kawanishi, 2001 Hydroxyurea induces site-specific DNA damage via formation of hydrogen peroxide and nitric oxide. Jpn. J. Cancer Res. 92: 1166-1174.
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 1166-1174
    • Sakano, K.1    Oikawa, S.2    Hasegawa, K.3    Kawanishi, S.4
  • 86
    • 18744391955 scopus 로고    scopus 로고
    • The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle
    • Schmidt, M., W. Haas, B. Crosas, P. G. Santamaria, S. P. Gygi et al., 2005a The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat. Struct. Mol. Biol. 12: 294-303.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 294-303
    • Schmidt, M.1    Haas, W.2    Crosas, B.3    Santamaria, P.G.4    Gygi, S.P.5
  • 87
    • 26844433577 scopus 로고    scopus 로고
    • Proteasomeassociated proteins: regulation of a proteolytic machine
    • Schmidt, M., J. Hanna, S. Elsasser, and D. Finley, 2005b Proteasomeassociated proteins: regulation of a proteolytic machine. Biol. Chem. 386: 725-737.
    • (2005) Biol. Chem. , vol.386 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 90
    • 49549122021 scopus 로고    scopus 로고
    • SGD Project, Available at
    • SGD Project, 2010 Saccharomyces Genome Database. Available at: http://www.yeastgenome.org/July14,.
    • (2010) Saccharomyces Genome Database
  • 91
    • 77956400468 scopus 로고    scopus 로고
    • Laterally attached kinetochores recruit the checkpoint protein Bub1, but satisfy the spindle checkpoint
    • Shimogawa, M. M., M. M. Wargacki, E. G. Muller, and T. N. Davis, 2010 Laterally attached kinetochores recruit the checkpoint protein Bub1, but satisfy the spindle checkpoint. Cell Cycle 9: 3619-3628.
    • (2010) Cell Cycle , vol.9 , pp. 3619-3628
    • Shimogawa, M.M.1    Wargacki, M.M.2    Muller, E.G.3    Davis, T.N.4
  • 93
    • 0025642866 scopus 로고
    • Detection of free radicals during the cellular metabolism of adriamycin
    • Turner, M., D. Everman, S. Ellington, and C. Fields, 1990 Detection of free radicals during the cellular metabolism of adriamycin. Free Radic. Biol. Med. 9: 415-421.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 415-421
    • Turner, M.1    Everman, D.2    Ellington, S.3    Fields, C.4
  • 94
    • 0036646488 scopus 로고    scopus 로고
    • PA200, a nuclear proteasome activator involved in DNA repair
    • Ustrell, V., L. Hoffman, G. Pratt, and M. Rechsteiner, 2002 PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21: 3516-3525.
    • (2002) EMBO J. , vol.21 , pp. 3516-3525
    • Ustrell, V.1    Hoffman, L.2    Pratt, G.3    Rechsteiner, M.4
  • 95
    • 3843078831 scopus 로고    scopus 로고
    • Remodelling the Rad9 checkpoint complex: preparing Rad53 for action
    • Van Den Bosch, M., and N. F. Lowndes, 2004 Remodelling the Rad9 checkpoint complex: preparing Rad53 for action. Cell Cycle 3: 119-122.
    • (2004) Cell Cycle , vol.3 , pp. 119-122
    • Van Den Bosch, M.1    Lowndes, N.F.2
  • 96
    • 33144469102 scopus 로고    scopus 로고
    • The proteasome and proteasome inhibitors in cancer therapy
    • Voorhees, P. M., and R. Z. Orlowski, 2006 The proteasome and proteasome inhibitors in cancer therapy. Annu. Rev. Pharmacol. Toxicol. 46: 189-213.
    • (2006) Annu. Rev. Pharmacol. Toxicol. , vol.46 , pp. 189-213
    • Voorhees, P.M.1    Orlowski, R.Z.2
  • 97
    • 0027480969 scopus 로고
    • Serum concentration and localization in tumor cells of proteasomes in patients with hematologic malignancy and their pathophysiologic significance
    • Wada, M., M. Kosaka, S. Saito, T. Sano, K. Tanaka et al., 1993 Serum concentration and localization in tumor cells of proteasomes in patients with hematologic malignancy and their pathophysiologic significance. J. Lab. Clin. Med. 121: 215-223.
    • (1993) J. Lab. Clin. Med. , vol.121 , pp. 215-223
    • Wada, M.1    Kosaka, M.2    Saito, S.3    Sano, T.4    Tanaka, K.5
  • 98
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach, A., J. Carmichael, J. Swartz, R. A. Furlong, Y. Narain et al., 2000 Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl. Acad. Sci. USA 97: 2898-2903.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5
  • 99
    • 58149295169 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome system for cancer therapy
    • Yang, Y., J. Kitagaki, H. Wang, D. X. Hou, and A. O. Perantoni, 2009 Targeting the ubiquitin-proteasome system for cancer therapy. Cancer Sci. 100: 24-28.
    • (2009) Cancer Sci. , vol.100 , pp. 24-28
    • Yang, Y.1    Kitagaki, J.2    Wang, H.3    Hou, D.X.4    Perantoni, A.O.5
  • 100
    • 10144255831 scopus 로고    scopus 로고
    • Mutations in the homologous ZDS1 and ZDS2 genes affect cell cycle progression
    • Yu, Y., Y. W. Jiang, R. J. Wellinger, K. Carlson, J. M. Roberts et al., 1996 Mutations in the homologous ZDS1 and ZDS2 genes affect cell cycle progression. Mol. Cell. Biol. 16: 5254-5263.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5254-5263
    • Yu, Y.1    Jiang, Y.W.2    Wellinger, R.J.3    Carlson, K.4    Roberts, J.M.5
  • 101
    • 32944454483 scopus 로고    scopus 로고
    • Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors
    • Zaarur, N., V. L. Gabai, J. A. Porco Jr, S. Calderwood, and M. Y. Sherman, 2006 Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors. Cancer Res. 66: 1783-1791.
    • (2006) Cancer Res. , vol.66 , pp. 1783-1791
    • Zaarur, N.1    Gabai, V.L.2    Porco Jr., J.A.3    Calderwood, S.4    Sherman, M.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.