메뉴 건너뛰기




Volumn 22, Issue 11, 2012, Pages 576-583

A prescription for 'stress' - the role of Hsp90 in genome stability and cellular adaptation

Author keywords

Adaptation; Cell stress; Chaperone; Genome instability; Hsp90

Indexed keywords

BRCA2 PROTEIN; DNA BINDING PROTEIN; DNA POLYMERASE; GELDANAMYCIN; GENOMIC DNA; HEAT SHOCK PROTEIN 90; MULTIPROTEIN COMPLEX; PIWI PROTEIN; PROTEASOME; PROTEOME; RAD51 PROTEIN;

EID: 84867860444     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.08.006     Document Type: Review
Times cited : (39)

References (83)
  • 1
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto R.I. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 2008, 22:1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 2
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance
    • Sangster T.A., et al. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays 2004, 26:348-362.
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1
  • 3
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms
    • Jarosz D.F., et al. Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu. Rev. Genet. 2010, 44:189-216.
    • (2010) Annu. Rev. Genet. , vol.44 , pp. 189-216
    • Jarosz, D.F.1
  • 4
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford S.L., Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 1998, 396:336-342.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 5
    • 35148834805 scopus 로고    scopus 로고
    • Mutation as a stress response and the regulation of evolvability
    • Galhardo R.S., et al. Mutation as a stress response and the regulation of evolvability. Crit. Rev. Biochem. Mol. Biol. 2007, 42:399-435.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 399-435
    • Galhardo, R.S.1
  • 6
    • 76349117871 scopus 로고    scopus 로고
    • Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons
    • Specchia V., et al. Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons. Nature 2010, 463:662-665.
    • (2010) Nature , vol.463 , pp. 662-665
    • Specchia, V.1
  • 7
    • 77955716080 scopus 로고    scopus 로고
    • Hsp90 modulates CAG repeat instability in human cells
    • Mittelman D., et al. Hsp90 modulates CAG repeat instability in human cells. Cell Stress Chaperones 2010, 15:753-759.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 753-759
    • Mittelman, D.1
  • 8
    • 80052563657 scopus 로고    scopus 로고
    • Stress alters rates and types of loss of heterozygosity in Candida albicans
    • Forche A., et al. Stress alters rates and types of loss of heterozygosity in Candida albicans. MBio 2011, 2:e00129-e211.
    • (2011) MBio , vol.2
    • Forche, A.1
  • 9
    • 84862777815 scopus 로고    scopus 로고
    • Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy
    • Chen G., et al. Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy. Nature 2012, 482:246-250.
    • (2012) Nature , vol.482 , pp. 246-250
    • Chen, G.1
  • 10
    • 84857053558 scopus 로고    scopus 로고
    • The role of Hsp90 in protein complex assembly
    • Makhnevych T., Houry W.A. The role of Hsp90 in protein complex assembly. Biochim. Biophys. Acta 2012, 1823:674-682.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 674-682
    • Makhnevych, T.1    Houry, W.A.2
  • 11
    • 33845959149 scopus 로고    scopus 로고
    • Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p
    • Catlett M., Kaplan K. Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J. Biol. Chem. 2006, 281:33739-33748.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33739-33748
    • Catlett, M.1    Kaplan, K.2
  • 13
    • 0031127737 scopus 로고    scopus 로고
    • Cdc37: a protein kinase chaperone?
    • Hunter T., Poon R.Y. Cdc37: a protein kinase chaperone?. Trends Cell Biol. 1997, 7:157-161.
    • (1997) Trends Cell Biol. , vol.7 , pp. 157-161
    • Hunter, T.1    Poon, R.Y.2
  • 14
    • 0030745769 scopus 로고    scopus 로고
    • Cdc37 is a molecular chaperone with specific functions in signal transduction
    • Kimura Y., et al. Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes Dev. 1997, 11:1775-1785.
    • (1997) Genes Dev. , vol.11 , pp. 1775-1785
    • Kimura, Y.1
  • 15
    • 84857058279 scopus 로고    scopus 로고
    • Expanding the cellular molecular chaperone network through the ubiquitous cochaperones
    • Echtenkamp F.J., Freeman B.C. Expanding the cellular molecular chaperone network through the ubiquitous cochaperones. Biochim. Biophys. Acta 2012, 1823:668-673.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 668-673
    • Echtenkamp, F.J.1    Freeman, B.C.2
  • 16
    • 19444383801 scopus 로고    scopus 로고
    • Trading places: how do DNA polymerases switch during translesion DNA synthesis?
    • Friedberg E.C., et al. Trading places: how do DNA polymerases switch during translesion DNA synthesis?. Mol. Cell 2005, 18:499-505.
    • (2005) Mol. Cell , vol.18 , pp. 499-505
    • Friedberg, E.C.1
  • 17
    • 78449261906 scopus 로고    scopus 로고
    • Simultaneous disruption of two DNA polymerases, Polη and Polζ, in avian DT40 cells unmasks the role of Polη in cellular response to various DNA lesions
    • Hirota K., et al. Simultaneous disruption of two DNA polymerases, Polη and Polζ, in avian DT40 cells unmasks the role of Polη in cellular response to various DNA lesions. PLoS Genet. 2010, 6:e1001151.
    • (2010) PLoS Genet. , vol.6
    • Hirota, K.1
  • 18
    • 36048999739 scopus 로고    scopus 로고
    • The spectrum of spontaneous mutations caused by deficiency in proteasome maturase Ump1 in Saccharomyces cerevisiae
    • McIntyre J., et al. The spectrum of spontaneous mutations caused by deficiency in proteasome maturase Ump1 in Saccharomyces cerevisiae. Curr. Genet. 2007, 52:221-228.
    • (2007) Curr. Genet. , vol.52 , pp. 221-228
    • McIntyre, J.1
  • 19
    • 30944459035 scopus 로고    scopus 로고
    • Analysis of the spontaneous mutator phenotype associated with 20S proteasome deficiency in S. cerevisiae
    • McIntyre J., et al. Analysis of the spontaneous mutator phenotype associated with 20S proteasome deficiency in S. cerevisiae. Mutat. Res. 2006, 593:153-163.
    • (2006) Mutat. Res. , vol.593 , pp. 153-163
    • McIntyre, J.1
  • 20
    • 33846640580 scopus 로고    scopus 로고
    • Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae
    • Skoneczna A., et al. Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae. J. Mol. Biol. 2007, 366:1074-1086.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1074-1086
    • Skoneczna, A.1
  • 21
    • 74049129007 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 regulates accumulation of DNA polymerase eta at replication stalling sites in UV-irradiated cells
    • Sekimoto T., et al. The molecular chaperone Hsp90 regulates accumulation of DNA polymerase eta at replication stalling sites in UV-irradiated cells. Mol. Cell 2010, 37:79-89.
    • (2010) Mol. Cell , vol.37 , pp. 79-89
    • Sekimoto, T.1
  • 22
    • 79961165129 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 regulates REV1-mediated mutagenesis
    • Pozo F.M., et al. Molecular chaperone Hsp90 regulates REV1-mediated mutagenesis. Mol. Cell. Biol. 2011, 31:3396-3409.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3396-3409
    • Pozo, F.M.1
  • 23
    • 10044266718 scopus 로고    scopus 로고
    • Cellular functions of DNA polymerase zeta and Rev1 protein
    • Lawrence C.W. Cellular functions of DNA polymerase zeta and Rev1 protein. Adv. Protein Chem. 2004, 69:167-203.
    • (2004) Adv. Protein Chem. , vol.69 , pp. 167-203
    • Lawrence, C.W.1
  • 24
    • 0345732688 scopus 로고    scopus 로고
    • Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis
    • Guo C., et al. Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. EMBO J. 2003, 22:6621-6630.
    • (2003) EMBO J. , vol.22 , pp. 6621-6630
    • Guo, C.1
  • 25
    • 4544251295 scopus 로고    scopus 로고
    • Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein
    • Tissier A., et al. Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. DNA Repair (Amst.) 2004, 3:1503-1514.
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1503-1514
    • Tissier, A.1
  • 26
    • 3042812439 scopus 로고    scopus 로고
    • Interaction of hREV1 with three human Y-family DNA polymerases
    • Ohashi E., et al. Interaction of hREV1 with three human Y-family DNA polymerases. Genes Cells 2004, 9:523-531.
    • (2004) Genes Cells , vol.9 , pp. 523-531
    • Ohashi, E.1
  • 27
    • 84862777927 scopus 로고    scopus 로고
    • Regulation of Rev1 by the Fanconi anemia core complex
    • Kim H., et al. Regulation of Rev1 by the Fanconi anemia core complex. Nat. Struct. Mol. Biol. 2012, 19:164-170.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 164-170
    • Kim, H.1
  • 28
    • 82755184119 scopus 로고    scopus 로고
    • The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA
    • Crossan G.P., Patel K.J. The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA. J. Pathol. 2012, 226:326-337.
    • (2012) J. Pathol. , vol.226 , pp. 326-337
    • Crossan, G.P.1    Patel, K.J.2
  • 29
    • 79960688447 scopus 로고    scopus 로고
    • Fanconi anaemia: from a monogenic disease to sporadic cancer
    • Valeri A., et al. Fanconi anaemia: from a monogenic disease to sporadic cancer. Clin. Transl. Oncol. 2011, 13:215-221.
    • (2011) Clin. Transl. Oncol. , vol.13 , pp. 215-221
    • Valeri, A.1
  • 30
    • 67349227137 scopus 로고    scopus 로고
    • Replication stress induces sister-chromatid bridging at fragile site loci in mitosis
    • Chan K., et al. Replication stress induces sister-chromatid bridging at fragile site loci in mitosis. Nat. Cell Biol. 2009, 11:753-760.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 753-760
    • Chan, K.1
  • 31
    • 34249727193 scopus 로고    scopus 로고
    • Hsp90 regulates the Fanconi anemia DNA damage response pathway
    • Oda T., et al. Hsp90 regulates the Fanconi anemia DNA damage response pathway. Blood 2007, 109:5016-5026.
    • (2007) Blood , vol.109 , pp. 5016-5026
    • Oda, T.1
  • 32
    • 77955716080 scopus 로고    scopus 로고
    • Hsp90 modulates CAG repeat instability in human cells
    • Mittelman D., et al. Hsp90 modulates CAG repeat instability in human cells. Cell Stress Chaperones 2010, 15:753-759.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 753-759
    • Mittelman, D.1
  • 33
    • 33750696349 scopus 로고    scopus 로고
    • Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin
    • Noguchi M., et al. Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Biochem. Biophys. Res. Commun. 2006, 351:658-663.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 658-663
    • Noguchi, M.1
  • 34
    • 0347993069 scopus 로고    scopus 로고
    • Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress
    • Arlander S.J.H., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J. Biol. Chem. 2003, 278:52572-52577.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52572-52577
    • Arlander, S.J.H.1
  • 35
    • 65549090186 scopus 로고    scopus 로고
    • DDB1 targets Chk1 to the Cul4 E3 ligase complex in normal cycling cells and in cells experiencing replication stress
    • Leung-Pineda V., et al. DDB1 targets Chk1 to the Cul4 E3 ligase complex in normal cycling cells and in cells experiencing replication stress. Cancer Res. 2009, 69:2630-2637.
    • (2009) Cancer Res. , vol.69 , pp. 2630-2637
    • Leung-Pineda, V.1
  • 36
    • 24044476837 scopus 로고    scopus 로고
    • Genotoxic stress targets human Chk1 for degradation by the ubiquitin-proteasome pathway
    • Zhang Y.-W., et al. Genotoxic stress targets human Chk1 for degradation by the ubiquitin-proteasome pathway. Mol. Cell 2005, 19:607-618.
    • (2005) Mol. Cell , vol.19 , pp. 607-618
    • Zhang, Y.-W.1
  • 37
    • 49649103587 scopus 로고    scopus 로고
    • Expanded roles for Chk1 in genome maintenance
    • Enders G.H. Expanded roles for Chk1 in genome maintenance. J. Biol. Chem. 2008, 283:17749-17752.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17749-17752
    • Enders, G.H.1
  • 38
    • 0035432062 scopus 로고    scopus 로고
    • The role of selfish genetic elements in eukaryotic evolution
    • Hurst G.D., Werren J.H. The role of selfish genetic elements in eukaryotic evolution. Nat. Rev. Genet. 2001, 2:597-606.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 597-606
    • Hurst, G.D.1    Werren, J.H.2
  • 39
    • 80755169456 scopus 로고    scopus 로고
    • Uniting germline and stem cells: the function of Piwi proteins and the piRNA pathway in diverse organisms
    • Juliano C., et al. Uniting germline and stem cells: the function of Piwi proteins and the piRNA pathway in diverse organisms. Annu. Rev. Genet. 2011, 45:447-469.
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 447-469
    • Juliano, C.1
  • 40
    • 0037228526 scopus 로고    scopus 로고
    • Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution
    • Sollars V., et al. Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution. Nat. Genet. 2003, 33:70-74.
    • (2003) Nat. Genet. , vol.33 , pp. 70-74
    • Sollars, V.1
  • 41
    • 79251560849 scopus 로고    scopus 로고
    • Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation
    • Gangaraju V.K., et al. Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation. Nat. Genet. 2011, 43:153-158.
    • (2011) Nat. Genet. , vol.43 , pp. 153-158
    • Gangaraju, V.K.1
  • 42
    • 84855199318 scopus 로고    scopus 로고
    • The R2TP complex: discovery and functions
    • Kakihara Y., Houry W.A. The R2TP complex: discovery and functions. Biochim. Biophys. Acta 2012, 1823:101-107.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 101-107
    • Kakihara, Y.1    Houry, W.A.2
  • 43
    • 0026013226 scopus 로고
    • A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere
    • Lechner J., Carbon J. A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere. Cell 1991, 64:717-725.
    • (1991) Cell , vol.64 , pp. 717-725
    • Lechner, J.1    Carbon, J.2
  • 44
    • 0345255913 scopus 로고    scopus 로고
    • Structure, function, and regulation of budding yeast kinetochores
    • McAinsh A.D., et al. Structure, function, and regulation of budding yeast kinetochores. Annu. Rev. Cell Dev. Biol. 2003, 19:519-539.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 519-539
    • McAinsh, A.D.1
  • 45
    • 0030662073 scopus 로고    scopus 로고
    • Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation
    • Kaplan K.B., et al. Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation. Cell 1997, 91:491-500.
    • (1997) Cell , vol.91 , pp. 491-500
    • Kaplan, K.B.1
  • 46
    • 3042842156 scopus 로고    scopus 로고
    • Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function
    • Rodrigo-Brenni M.C., et al. Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function. Mol. Biol. Cell 2004, 15:3366-3378.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3366-3378
    • Rodrigo-Brenni, M.C.1
  • 47
    • 0037173049 scopus 로고    scopus 로고
    • Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore
    • Stemmann O., et al. Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:8585-8590.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8585-8590
    • Stemmann, O.1
  • 48
    • 0033166694 scopus 로고    scopus 로고
    • SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex
    • Kitagawa K., et al. SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Mol. Cell 1999, 4:21-33.
    • (1999) Mol. Cell , vol.4 , pp. 21-33
    • Kitagawa, K.1
  • 49
    • 4744356146 scopus 로고    scopus 로고
    • The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly
    • Lingelbach L., Kaplan K. The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly. Mol. Cell. Biol. 2004, 24:8938-8950.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8938-8950
    • Lingelbach, L.1    Kaplan, K.2
  • 50
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 1999, 15:435-467.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 51
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman R.M., et al. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 1997, 91:221-230.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1
  • 52
    • 34948857409 scopus 로고    scopus 로고
    • A Bir1p Sli15p kinetochore passenger complex regulates septin organization during anaphase
    • Thomas S., Kaplan K.B. A Bir1p Sli15p kinetochore passenger complex regulates septin organization during anaphase. Mol. Biol. Cell 2007, 18:3820-3834.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3820-3834
    • Thomas, S.1    Kaplan, K.B.2
  • 53
    • 28544442597 scopus 로고    scopus 로고
    • A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis
    • Gillis A., et al. A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis. J. Cell Biol. 2005, 171:773-784.
    • (2005) J. Cell Biol. , vol.171 , pp. 773-784
    • Gillis, A.1
  • 54
    • 79955499722 scopus 로고    scopus 로고
    • Chromosome passenger complexes control anaphase duration and spindle elongation via a kinesin-5 brake
    • Rozelle D.K., et al. Chromosome passenger complexes control anaphase duration and spindle elongation via a kinesin-5 brake. J. Cell Biol. 2011, 193:285-294.
    • (2011) J. Cell Biol. , vol.193 , pp. 285-294
    • Rozelle, D.K.1
  • 55
    • 65549149069 scopus 로고    scopus 로고
    • Protein architecture of the human kinetochore microtubule attachment site
    • Wan X., et al. Protein architecture of the human kinetochore microtubule attachment site. Cell 2009, 137:672-684.
    • (2009) Cell , vol.137 , pp. 672-684
    • Wan, X.1
  • 56
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubule-binding site of the kinetochore
    • Cheeseman I., et al. The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell 2006, 127:983-997.
    • (2006) Cell , vol.127 , pp. 983-997
    • Cheeseman, I.1
  • 57
    • 77951198477 scopus 로고    scopus 로고
    • Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites
    • Davies A.E., Kaplan K.B. Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites. J. Cell Biol. 2010, 189:261-274.
    • (2010) J. Cell Biol. , vol.189 , pp. 261-274
    • Davies, A.E.1    Kaplan, K.B.2
  • 58
    • 78649758292 scopus 로고    scopus 로고
    • Adapt or die: how eukaryotic cells respond to prolonged activation of the spindle assembly checkpoint
    • Rossio V., et al. Adapt or die: how eukaryotic cells respond to prolonged activation of the spindle assembly checkpoint. Biochem. Soc. Trans. 2010, 38:1645-1649.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1645-1649
    • Rossio, V.1
  • 59
    • 80053364894 scopus 로고    scopus 로고
    • Chromosome segregation errors as a cause of DNA damage and structural chromosome aberrations
    • Janssen A., et al. Chromosome segregation errors as a cause of DNA damage and structural chromosome aberrations. Science 2011, 333:1895-1898.
    • (2011) Science , vol.333 , pp. 1895-1898
    • Janssen, A.1
  • 60
    • 84856424908 scopus 로고    scopus 로고
    • DNA breaks and chromosome pulverization from errors in mitosis
    • Crasta K., et al. DNA breaks and chromosome pulverization from errors in mitosis. Nature 2012, 482:53-58.
    • (2012) Nature , vol.482 , pp. 53-58
    • Crasta, K.1
  • 61
    • 84857192718 scopus 로고    scopus 로고
    • Causes and consequences of aneuploidy in cancer
    • Gordon D.J., et al. Causes and consequences of aneuploidy in cancer. Nat. Rev. Genet. 2012, 13:189-203.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 189-203
    • Gordon, D.J.1
  • 62
    • 78650033928 scopus 로고    scopus 로고
    • Somatic genome variations in health and disease
    • Iourov I.Y., et al. Somatic genome variations in health and disease. Curr. Genomics 2010, 11:387-396.
    • (2010) Curr. Genomics , vol.11 , pp. 387-396
    • Iourov, I.Y.1
  • 63
    • 78649636162 scopus 로고    scopus 로고
    • Dr Jekyll and Mr Hyde: role of aneuploidy in cellular adaptation and cancer
    • Pavelka N., et al. Dr Jekyll and Mr Hyde: role of aneuploidy in cellular adaptation and cancer. Curr. Opin. Cell Biol. 2010, 22:809-815.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 809-815
    • Pavelka, N.1
  • 64
    • 4944234694 scopus 로고    scopus 로고
    • Chromosome transfer induced aneuploidy results in complex dysregulation of the cellular transcriptome in immortalized and cancer cells
    • Upender M.B., et al. Chromosome transfer induced aneuploidy results in complex dysregulation of the cellular transcriptome in immortalized and cancer cells. Cancer Res. 2004, 64:6941-6949.
    • (2004) Cancer Res. , vol.64 , pp. 6941-6949
    • Upender, M.B.1
  • 65
    • 34547433234 scopus 로고    scopus 로고
    • Chromosome instability, chromosome transcriptome, and clonal evolution of tumor cell populations
    • Gao C., et al. Chromosome instability, chromosome transcriptome, and clonal evolution of tumor cell populations. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:8995-9000.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 8995-9000
    • Gao, C.1
  • 66
    • 17444446946 scopus 로고    scopus 로고
    • Widespread aneuploidy revealed by DNA microarray expression profiling
    • Hughes T.R., et al. Widespread aneuploidy revealed by DNA microarray expression profiling. Nat. Genet. 2000, 25:333-337.
    • (2000) Nat. Genet. , vol.25 , pp. 333-337
    • Hughes, T.R.1
  • 67
    • 76549103412 scopus 로고    scopus 로고
    • Reflections on studies of gene expression in aneuploids
    • Birchler J.A. Reflections on studies of gene expression in aneuploids. Biochem. J. 2010, 426:119-123.
    • (2010) Biochem. J. , vol.426 , pp. 119-123
    • Birchler, J.A.1
  • 68
    • 78149423336 scopus 로고    scopus 로고
    • Aneuploidy confers quantitative proteome changes and phenotypic variation in budding yeast
    • Pavelka N., et al. Aneuploidy confers quantitative proteome changes and phenotypic variation in budding yeast. Nature 2010, 468:321-325.
    • (2010) Nature , vol.468 , pp. 321-325
    • Pavelka, N.1
  • 69
    • 77952254077 scopus 로고    scopus 로고
    • A general lack of compensation for gene dosage in yeast
    • Springer M., et al. A general lack of compensation for gene dosage in yeast. Mol. Syst. Biol. 2010, 6:368.
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 368
    • Springer, M.1
  • 70
    • 77957237291 scopus 로고    scopus 로고
    • Identification of aneuploidy-tolerating mutations
    • Torres E.M., et al. Identification of aneuploidy-tolerating mutations. Cell 2010, 143:71-83.
    • (2010) Cell , vol.143 , pp. 71-83
    • Torres, E.M.1
  • 71
    • 56349088536 scopus 로고    scopus 로고
    • Aneuploidy underlies rapid adaptive evolution of yeast cells deprived of a conserved cytokinesis motor
    • Rancati G., et al. Aneuploidy underlies rapid adaptive evolution of yeast cells deprived of a conserved cytokinesis motor. Cell 2008, 135:879-893.
    • (2008) Cell , vol.135 , pp. 879-893
    • Rancati, G.1
  • 72
    • 33746506280 scopus 로고    scopus 로고
    • Aneuploidy and isochromosome formation in drug-resistant Candida albicans
    • Selmecki A., et al. Aneuploidy and isochromosome formation in drug-resistant Candida albicans. Science 2006, 313:367-370.
    • (2006) Science , vol.313 , pp. 367-370
    • Selmecki, A.1
  • 73
    • 73449107205 scopus 로고    scopus 로고
    • Acquisition of aneuploidy provides increased fitness during the evolution of antifungal drug resistance
    • Selmecki A.M., et al. Acquisition of aneuploidy provides increased fitness during the evolution of antifungal drug resistance. PLoS Genet. 2009, 5:e1000705.
    • (2009) PLoS Genet. , vol.5
    • Selmecki, A.M.1
  • 74
    • 77954047286 scopus 로고    scopus 로고
    • Cryptococcus neoformans overcomes stress of azole drugs by formation of disomy in specific multiple chromosomes
    • Sionov E., et al. Cryptococcus neoformans overcomes stress of azole drugs by formation of disomy in specific multiple chromosomes. PLoS Pathog. 2010, 6:e1000848.
    • (2010) PLoS Pathog. , vol.6
    • Sionov, E.1
  • 75
    • 81755183013 scopus 로고    scopus 로고
    • Deletion of Cryptococcus neoformans AIF ortholog promotes chromosome aneuploidy and fluconazole-resistance in a metacaspase-independent manner
    • Semighini C.P., et al. Deletion of Cryptococcus neoformans AIF ortholog promotes chromosome aneuploidy and fluconazole-resistance in a metacaspase-independent manner. PLoS Pathog. 2011, 7:e1002364.
    • (2011) PLoS Pathog. , vol.7
    • Semighini, C.P.1
  • 76
    • 58149161888 scopus 로고    scopus 로고
    • Heat shock induces chromosomal instability in near-tetraploid embryonal carcinoma cells
    • Gupta R.K., Srinivas U.K. Heat shock induces chromosomal instability in near-tetraploid embryonal carcinoma cells. Cancer Biol. Ther. 2008, 7:1471-1480.
    • (2008) Cancer Biol. Ther. , vol.7 , pp. 1471-1480
    • Gupta, R.K.1    Srinivas, U.K.2
  • 77
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A., et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 78
    • 84857044092 scopus 로고    scopus 로고
    • Post-translational modifications of Hsp90 and their contributions to chaperone regulation
    • Mollapour M., Neckers L. Post-translational modifications of Hsp90 and their contributions to chaperone regulation. Biochim. Biophys. Acta 2012, 1823:648-655.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 648-655
    • Mollapour, M.1    Neckers, L.2
  • 79
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata Y., Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol. Cell. Biol. 2004, 24:4065-4074.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 80
    • 67650539066 scopus 로고    scopus 로고
    • Sgt1 dimerization is negatively regulated by protein kinase CK2-mediated phosphorylation at Ser361
    • Bansal P.K., et al. Sgt1 dimerization is negatively regulated by protein kinase CK2-mediated phosphorylation at Ser361. J. Biol. Chem. 2009, 284:18692-18698.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18692-18698
    • Bansal, P.K.1
  • 81
    • 25844530060 scopus 로고    scopus 로고
    • Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi
    • Cowen L.E., Lindquist S. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 2005, 309:2185-2189.
    • (2005) Science , vol.309 , pp. 2185-2189
    • Cowen, L.E.1    Lindquist, S.2
  • 82
    • 84857039457 scopus 로고    scopus 로고
    • Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers
    • Jhaveri K., et al. Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers. Biochim. Biophys. Acta 2012, 1823:742-755.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 742-755
    • Jhaveri, K.1
  • 83
    • 81255179936 scopus 로고    scopus 로고
    • The 26S proteasome complex: an attractive target for cancer therapy
    • Frankland-Searby S., Bhaumik S.R. The 26S proteasome complex: an attractive target for cancer therapy. Biochim. Biophys. Acta 2012, 1825:64-76.
    • (2012) Biochim. Biophys. Acta , vol.1825 , pp. 64-76
    • Frankland-Searby, S.1    Bhaumik, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.