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Volumn 10, Issue 10, 2012, Pages 693-704

Fungal Hsp90: A biological transistor that tunes cellular outputs to thermal inputs

Author keywords

[No Author keywords available]

Indexed keywords

CASPOFUNGIN; CELL CYCLE PROTEIN 37; CHAPERONE; CYCLOSPORIN; FLUCONAZOLE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE SLT2; TACROLIMUS; UNCLASSIFIED DRUG;

EID: 84867827357     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro2875     Document Type: Review
Times cited : (81)

References (141)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa, F. A new puffing pattern induced by temperature shock and DNP in Drosophila. Cell. Mol. Life Sci. 18, 571-573 (1962).
    • (1962) Cell. Mol. Life Sci. , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 2
    • 0019433557 scopus 로고
    • Regulation of protein synthesis during heat shock
    • DOI 10.1038/293311a0
    • Lindquist, S. Regulation of protein synthesis during heat shock. Nature 293, 311-314 (1981). (Pubitemid 11016267)
    • (1981) Nature , vol.293 , Issue.5830 , pp. 311-314
    • Lindquist, S.1
  • 3
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist, S. The heat-shock response. Annu. Rev. Biochem. 55, 1151-1191 (1986). (Pubitemid 16070798)
    • (1986) Annual Review of Biochemistry , vol.VOL. 55 , pp. 1151-1191
    • Lindquist, S.1
  • 6
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang, D., Liberek, K., Skowyra, D., Zylicz, M. & Georgopoulos, C. Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266, 24233-24236 (1991). (Pubitemid 21908929)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.36 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 9
    • 64249092397 scopus 로고    scopus 로고
    • Phylogenetic diversity of stress signalling pathways in fungi
    • Nikolaou, E. et al. Phylogenetic diversity of stress signalling pathways in fungi. BMC Evol. Biol. 9, 44 (2009).
    • (2009) BMC Evol. Biol. , vol.9 , pp. 44
    • Nikolaou, E.1
  • 10
    • 70449568487 scopus 로고    scopus 로고
    • Role of the heat shock transcription factor, Hsf1, in a major fungal pathogen that is obligately associated with warm-blooded animals
    • Nicholls, S., Leach, M. D., Priest, C. L. & Brown, A. J. Role of the heat shock transcription factor, Hsf1, in a major fungal pathogen that is obligately associated with warm-blooded animals. Mol. Microbiol. 74, 844-861 (2009).
    • (2009) Mol. Microbiol. , vol.74 , pp. 844-861
    • Nicholls, S.1    Leach, M.D.2    Priest, C.L.3    Brown, A.J.4
  • 12
    • 78751627330 scopus 로고    scopus 로고
    • Activation of the heat shock transcription factor Hsf1 is essential for the full virulence of the fungal pathogen Candida albicans
    • Nicholls, S. et al. Activation of the heat shock transcription factor Hsf1 is essential for the full virulence of the fungal pathogen Candida albicans. Fungal Genet. Biol. 48, 297-305 (2011).
    • (2011) Fungal Genet. Biol. , vol.48 , pp. 297-305
    • Nicholls, S.1
  • 13
    • 84858665548 scopus 로고    scopus 로고
    • Modelling the regulation of thermal adaptation in Candida albicans, a major fungal pathogen of humans
    • Leach, M. D., Tyc, K. M., Brown, A. J. P. & Klipp, E. Modelling the regulation of thermal adaptation in Candida albicans, a major fungal pathogen of humans. PLoS ONE 7, e32467 (2012).
    • (2012) PLoS ONE , vol.7
    • Leach, M.D.1    Tyc, K.M.2    Brown, A.J.P.3    Klipp, E.4
  • 14
    • 0024421221 scopus 로고
    • Hsp82 Is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J. & Lindquist, S. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9, 3919-3930 (1989). (Pubitemid 19216285)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 15
    • 0028876053 scopus 로고
    • Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans
    • Swoboda, R. K. et al. Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans. Infect. Immun. 63, 4506-4514 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 4506-4514
    • Swoboda, R.K.1
  • 16
    • 77953255163 scopus 로고    scopus 로고
    • Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe
    • Kim, D.-U. et al. Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe. Nature Biotech. 28, 617-623 (2010).
    • (2010) Nature Biotech. , vol.28 , pp. 617-623
    • Kim, D.U.1
  • 17
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale, M., Jarosz, D. F. & Lindquist, S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nature Rev. Mol. Cell Biol. 11, 515-528 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 18
    • 78650644709 scopus 로고    scopus 로고
    • Hsp90 and environmental stress transform the adaptive value of natural genetic variation
    • Jarosz, D. F. & Lindquist, S. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 330, 1820-1824 (2010).
    • (2010) Science , vol.330 , pp. 1820-1824
    • Jarosz, D.F.1    Lindquist, S.2
  • 19
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • DOI 10.1038/24550
    • Rutherford, S. L. & Lindquist, S. Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342 (1998). (Pubitemid 28557387)
    • (1998) Nature , vol.396 , Issue.6709 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 20
    • 25844530060 scopus 로고    scopus 로고
    • Cell biology: Hsp90 potentiates the rapid evolution of new traits: Drug resistance in diverse fungi
    • DOI 10.1126/science.1118370
    • Cowen, L. E. & Lindquist, S. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 309, 2185-2189 (2005). (Pubitemid 41396062)
    • (2005) Science , vol.309 , Issue.5744 , pp. 2185-2189
    • Cowen, L.E.1    Lindquist, S.2
  • 21
    • 84862777815 scopus 로고    scopus 로고
    • Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy
    • Chen, G., Bradford, W. D., Seidel, C. W. & Li, R. Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy. Nature 482, 246-250 (2012).
    • (2012) Nature , vol.482 , pp. 246-250
    • Chen, G.1    Bradford, W.D.2    Seidel, C.W.3    Li, R.4
  • 23
    • 84857042271 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
    • Li, J., Soroka, J. & Buchner, J. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochim. Biophys. Acta 1823, 624-635 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 624-635
    • Li, J.1    Soroka, J.2    Buchner, J.3
  • 24
    • 0033951278 scopus 로고    scopus 로고
    • Structure and in vivo function of Hsp90
    • DOI 10.1016/S0959-440X(99)00047-0
    • Pearl, L. H. & Prodromou, C. Structure and in vivo function of Hsp90. Curr. Opin. Struct. Biol. 10, 46-51 (2000). (Pubitemid 30099326)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 46-51
    • Pearl, L.H.1    Prodromou, C.2
  • 25
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali, M. M. et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440, 1013-1017 (2006).
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1
  • 26
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • DOI 10.1042/BJ20071640
    • Pearl, L. H., Prodromou, C. & Workman, P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410, 439-453 (2008). (Pubitemid 351429015)
    • (2008) Biochemical Journal , vol.410 , Issue.3 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 27
    • 56849131626 scopus 로고    scopus 로고
    • Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
    • Southworth, D. R. & Agard, D. A. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol. Cell 32, 631-640 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 631-640
    • Southworth, D.R.1    Agard, D.A.2
  • 31
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E. et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997). (Pubitemid 27199896)
    • (1997) Cell , vol.89 , Issue.2 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 34
    • 76749131138 scopus 로고    scopus 로고
    • Integrative analysis of the heat shock response in Aspergillus fumigatus
    • Albrecht, D., Guthke, R., Brakhage, A. A. & Kniemeyer, O. Integrative analysis of the heat shock response in Aspergillus fumigatus. BMC Genomics 11, 32 (2010).
    • (2010) BMC Genomics , vol.11 , pp. 32
    • Albrecht, D.1    Guthke, R.2    Brakhage, A.A.3    Kniemeyer, O.4
  • 35
    • 0025997535 scopus 로고
    • The intron-containing hsp82 gene of the dimorphic pathogenic fungus Histoplasma capsulatum is properly spliced in severe heat shock conditions
    • Minchiotti, G., Gargano, S. & Maresca, B. The intron-containing hsp82 gene of the dimorphic pathogenic fungus Histoplasma capsulatum is properly spliced in severe heat shock conditions. Mol. Cell. Biol. 11, 5624-5630 (1991). (Pubitemid 21895329)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.11 , pp. 5624-5630
    • Minchiotti, G.1    Gargano, S.2    Maresca, B.3
  • 36
    • 0025755922 scopus 로고
    • Heat shock factor and the heat shock response
    • Sorger, P. K. Heat shock factor and the heat shock response. Cell 65, 363-366 (1991). (Pubitemid 121002045)
    • (1991) Cell , vol.65 , Issue.3 , pp. 363-366
    • Sorger, P.K.1
  • 37
    • 0029564954 scopus 로고
    • Heat shock transcription factors: Structure and regulation
    • Wu, C. Heat shock transcription factors: structure and regulation. Annu. Rev. Cell Dev. Biol. 11, 441-469 (1995). (Pubitemid 26019611)
    • (1995) Annual Review of Cell and Developmental Biology , vol.11 , pp. 441-469
    • Wu, C.1
  • 38
    • 0024282788 scopus 로고
    • Isolation of the gene encoding the S. cerevisiae heat shock transcription factor
    • Wiederrecht, G., Seto, D. & Parker, C. S. Isolation of the gene encoding the S. cerevisiae heat shock transcription factor. Cell 54, 841-853 (1988).
    • (1988) Cell , vol.54 , pp. 841-853
    • Wiederrecht, G.1    Seto, D.2    Parker, C.S.3
  • 39
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger, P. K. & Pelham, H. R. B. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54, 855-864 (1988).
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 40
    • 80052264688 scopus 로고    scopus 로고
    • Regulation of chaperone gene expression by heat shock transcription factor in Saccharomyces cerevisiae: Importance in normal cell growth, stress resistance, and longevity
    • Sakurai, H. & Ota, A. Regulation of chaperone gene expression by heat shock transcription factor in Saccharomyces cerevisiae: importance in normal cell growth, stress resistance, and longevity. FEBS Lett. 585, 2744-2748 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 2744-2748
    • Sakurai, H.1    Ota, A.2
  • 41
    • 0023701108 scopus 로고
    • Constitutive binding of yeast heat shock factor to DNA in vivo
    • Jakobsen, B. K. & Pelham, H. R. Constitutive binding of yeast heat shock factor to DNA in vivo. Mol. Cell. Biol. 8, 5040-5042 (1988). (Pubitemid 18261577)
    • (1988) Molecular and Cellular Biology , vol.8 , Issue.11 , pp. 5040-5042
    • Jakobsen, B.K.1    Pelham, H.R.B.2
  • 43
    • 0024852809 scopus 로고
    • Trimerization of the yeast transcriptional activator via a coiled-coil motif
    • DOI 10.1016/0092-8674(89)90604-1
    • Sorger, P. K. & Nelson, H. C. M. Trimerization of a yeast transcriptional activator via a coiled-coil motif. Cell 59, 807-813 (1989). (Pubitemid 20022371)
    • (1989) Cell , vol.59 , Issue.5 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.M.2
  • 44
    • 0025678738 scopus 로고
    • Genomic footprinting of the yeast HSP82 promoter reveals marked distortion of the DNA helix and constitutive occupancy of heat shock and TATA elements
    • Gross, D. S., English, K. E., Collins, K. W. & Lee, S. W. Genomic footprinting of the yeast HSP82 promoter reveals marked distortion of the DNA helix and constitutive occupancy of heat shock and TATA elements. J. Mol. Biol. 216, 611-631 (1990). (Pubitemid 120037394)
    • (1990) Journal of Molecular Biology , vol.216 , Issue.3 , pp. 611-631
    • Gross, D.S.1    English, K.E.2    Collins, K.W.3    Lee, S.4
  • 45
    • 0028886503 scopus 로고
    • Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance
    • Sewell, A. K. et al. Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance. J. Biol. Chem. 270, 25079-25086 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25079-25086
    • Sewell, A.K.1
  • 46
    • 0029664413 scopus 로고    scopus 로고
    • Oxidative stress induced heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription
    • Liu, X. D. & Thiele, D. J. Oxidative stress induced heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription. Genes Dev. 10, 592-603 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 592-603
    • Liu, X.D.1    Thiele, D.J.2
  • 47
    • 0025122831 scopus 로고
    • The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions
    • Nieto-Sotelo, J., Wiederrecht, G., Okuda, A. & Parker, C. S. The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions. Cell 62, 807-817 (1990).
    • (1990) Cell , vol.62 , pp. 807-817
    • Nieto-Sotelo, J.1    Wiederrecht, G.2    Okuda, A.3    Parker, C.S.4
  • 48
    • 0023643235 scopus 로고
    • Heat shock factor is regulated differently in yeast and HeLa cells
    • Sorger, P. K., Lewis, M. J. & Pelham, H. R. Heat shock factor is regulated differently in yeast and HeLa cells. Nature 329, 81-84 (1987). (Pubitemid 17125900)
    • (1987) Nature , vol.328 , Issue.6134 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, R.B.3
  • 49
    • 0032931842 scopus 로고    scopus 로고
    • A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress
    • Morano, K. A., Santoro, N., Koch, K. A. & Thiele, D. J. A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress. Mol. Cell. Biol. 19, 402-411 (1999). (Pubitemid 29018442)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 402-411
    • Morano, K.A.1    Santoro, N.2    Koch, K.A.3    Thiele, D.J.4
  • 50
    • 0019325433 scopus 로고
    • Varying patterns of protein synthesis in Drosophila during heat shock: Implications for regulation
    • Lindquist, S. Varying patterns of protein synthesis in Drosophila during heat shock: implications for regulation. Dev. Biol. 77, 463-479 (1980).
    • (1980) Dev. Biol. , vol.77 , pp. 463-479
    • Lindquist, S.1
  • 51
    • 0020409205 scopus 로고
    • The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels
    • DiDomenico, B. J., Bugaisky, G. E. & Lindquist, S. The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels. Cell 31, 593-603 (1982). (Pubitemid 13223944)
    • (1982) Cell , vol.31 , Issue.3 , pp. 593-603
    • DiDomenico, B.J.1    Bugaisky, G.E.2    Lindquist, S.3
  • 52
    • 0026665975 scopus 로고
    • The human heat shock protein Hsp70 interacts with Hsf1, the transcription factor that regulates heat shock gene expression
    • Abravaya, K., Myers, M. P., Murphy, S. P. & Morimoto, R. I. The human heat shock protein Hsp70 interacts with Hsf1, the transcription factor that regulates heat shock gene expression. Genes Dev. 6, 1153-1164 (1992).
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 53
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • Baler, R., Welch, W. J. & Voellmy, R. Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor. J. Cell Biol. 117, 1151-1159 (1992).
    • (1992) J. Cell Biol. , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 54
    • 0027202273 scopus 로고
    • The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70
    • Mosser, D. D., Duchaine, J. & Massie, B. The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by Hsp70. Mol. Cell. Biol. 13, 5427-5438 (1993). (Pubitemid 23260646)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.9 , pp. 5427-5438
    • Mosser, D.D.1    Duchaine, J.2    Massie, B.3
  • 56
    • 0033578875 scopus 로고    scopus 로고
    • The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
    • Liu, X.-D., Morano, K. A. & Thiele, D. J. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J. Biol. Chem. 274, 26654-26660 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 26654-26660
    • Liu, X.D.1    Morano, K.A.2    Thiele, D.J.3
  • 57
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou, J., Guo, Y., Guettouche, T., Smith, D. F. & Voellmy, R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94, 471-480 (1998). (Pubitemid 28391863)
    • (1998) Cell , vol.94 , Issue.4 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 58
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo, Y. et al. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J. Biol. Chem. 276, 45791-45799 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 45791-45799
    • Guo, Y.1
  • 59
    • 0032563195 scopus 로고    scopus 로고
    • Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response
    • DOI 10.1074/jbc.273.30.18974
    • Duina, A. A., Kalton, H. M. & Gaber, R. F. Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J. Biol. Chem. 273, 18974-18978 (1998). (Pubitemid 28366287)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18974-18978
    • Duina, A.A.1    Kalton, H.M.2    Gaber, R.F.3
  • 60
    • 0026648827 scopus 로고
    • The effects of 5Ŷ-capping, 3Ŷ-polyadenylation and leader composition upon the translation and stability of mRNA in a cell-free extract derived from the yeast Saccharomyces cerevisiae
    • Gerstel, B., Tuite, M. F. & McCarthy, J. E. G. The effects of 5Ŷ-capping, 3Ŷ-polyadenylation and leader composition upon the translation and stability of mRNA in a cell-free extract derived from the yeast Saccharomyces cerevisiae. Mol. Microbiol. 6, 2339-2348 (1992).
    • (1992) Mol. Microbiol. , vol.6 , pp. 2339-2348
    • Gerstel, B.1    Tuite, M.F.2    McCarthy, J.E.G.3
  • 61
    • 75949112264 scopus 로고    scopus 로고
    • Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function
    • Mollapour, M. et al. Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol. Cell 37, 333-343 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 333-343
    • Mollapour, M.1
  • 62
    • 0020403812 scopus 로고
    • Phosphorylation in vivo of chicken oviduct progesterone receptor
    • Dougherty, J. J., Puri, R. K. & Toft, D. O. Phosphorylation in vivo of chicken oviduct progesterone receptor. J. Biol. Chem. 257, 14226-14230 (1982). (Pubitemid 13141304)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.23 , pp. 14226-14230
    • Dougherty, J.J.1    Puri, R.K.2    Toft, D.O.3
  • 63
    • 0023068568 scopus 로고
    • Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors
    • DOI 10.1016/0167-4889(87)90067-X
    • Dougherty, J. J., Rabideau, D. A., Iannotti, A. M., Sullivan, W. P. & Toft, D. O. Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors. Biochim. Biophys. Acta 927, 74-80 (1987). (Pubitemid 17232096)
    • (1987) Biochimica et Biophysica Acta - Molecular Cell Research , vol.927 , Issue.1 , pp. 74-80
    • Dougherty, J.J.1    Rabideau, D.A.2    Iannotti, A.M.3
  • 64
    • 31444454302 scopus 로고    scopus 로고
    • The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
    • DOI 10.1038/sj.emboj.7600930, PII 7600930
    • Wandinger, S. K., Suhre, M. H., Wegele, H. & Buchner, J. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. 25, 367-376 (2006). (Pubitemid 43152857)
    • (2006) EMBO Journal , vol.25 , Issue.2 , pp. 367-376
    • Wandinger, S.K.1    Suhre, M.H.2    Wegele, H.3    Buchner, J.4
  • 65
    • 79952665421 scopus 로고    scopus 로고
    • Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects Its chaperone activity
    • Mollapour, M. et al. Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects Its chaperone activity. Mol. Cell 41, 672-681 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 672-681
    • Mollapour, M.1
  • 66
    • 35348858091 scopus 로고    scopus 로고
    • Post-translational modification of heat-shock protein 90: Impact on chaperone function
    • DOI 10.1517/17460441.2.10.1403
    • Scroggins, B. T. & Neckers, L. Post-translational modification of heat-shock protein 90: impact on chaperone function. Expert Opin. Drug Discov. 2, 1403-1414 (2007). (Pubitemid 47591277)
    • (2007) Expert Opinion on Drug Discovery , vol.2 , Issue.10 , pp. 1403-1414
    • Scroggins, B.T.1    Neckers, L.2
  • 67
    • 84859223051 scopus 로고    scopus 로고
    • Mapping the Hsp90 genetic interaction network in Candida albicans reveals environmental contingency and rewired circuitry
    • Diezmann, S., Michaut, M., Shapiro, R. S., Bader, G. D. & Cowen, L. E. Mapping the Hsp90 genetic interaction network in Candida albicans reveals environmental contingency and rewired circuitry. PLoS Genet. 8, e1002562 (2012).
    • (2012) PLoS Genet , vol.8
    • Diezmann, S.1    Michaut, M.2    Shapiro, R.S.3    Bader, G.D.4    Cowen, L.E.5
  • 68
    • 70449710842 scopus 로고    scopus 로고
    • Hsp90 is regulated by a switch point in the C-terminal domain
    • Retzlaff, M. et al. Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep. 10, 1147-1153 (2009).
    • (2009) EMBO Rep. , vol.10 , pp. 1147-1153
    • Retzlaff, M.1
  • 74
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
    • DOI 10.1074/jbc.M206566200
    • Hernandez, M. P., Sullivan, W. P. & Toft, D. O. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J. Biol. Chem. 277, 38294-38304 (2002). (Pubitemid 35154683)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 76
    • 0037593900 scopus 로고    scopus 로고
    • Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
    • DOI 10.1074/jbc.M212761200
    • Lotz, G. P., Lin, H., Harst, A. & Obermann, W. M. J. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. 278, 17228-17235 (2003). (Pubitemid 36799604)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 17228-17235
    • Lotz, G.P.1    Lin, H.2    Harst, A.3    Obermann, W.M.J.4
  • 77
    • 0034329452 scopus 로고    scopus 로고
    • Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    • Young, J. C. & Hartl, F. U. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19, 5930-5940 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5930-5940
    • Young, J.C.1    Hartl, F.U.2
  • 80
    • 0042357461 scopus 로고    scopus 로고
    • Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M304315200
    • Tesic, M., Marsh, J. A., Cullinan, S. B. & Gaber, R. F. Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae. J. Biol. Chem. 278, 32692-32701 (2003). (Pubitemid 37055708)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 32692-32701
    • Tesic, M.1    Marsh, J.A.2    Cullinan, S.B.3    Gaber, R.F.4
  • 81
    • 33845959149 scopus 로고    scopus 로고
    • Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p
    • DOI 10.1074/jbc.M603847200
    • Catlett, M. G. & Kaplan, K. B. Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J. Biol. Chem. 281, 33739-33748 (2006). (Pubitemid 46036752)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.44 , pp. 33739-33748
    • Catlett, M.G.1    Kaplan, K.B.2
  • 82
    • 0034602390 scopus 로고    scopus 로고
    • Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties
    • Mayr, C., Richter, K., Lilie, H. & Buchner, J. Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J. Biol. Chem. 275, 34140-34146 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34140-34146
    • Mayr, C.1    Richter, K.2    Lilie, H.3    Buchner, J.4
  • 84
    • 1542298244 scopus 로고    scopus 로고
    • Candida albicans Cdc37 interacts with the Crk1 kinase and is required for Crk1 production
    • DOI 10.1016/S0014-5793(04)00172-3, PII S0014579304001723
    • Ni, J., Gao, Y., Liu, H. & Chen, J. Candida albicans Cdc37 interacts with the Crk1 kinase and is required for Crk1 production. FEBS Lett. 561, 223-230 (2004). (Pubitemid 38317326)
    • (2004) FEBS Letters , vol.561 , Issue.1-3 , pp. 223-230
    • Ni, J.1    Gao, Y.2    Liu, H.3    Chen, J.4
  • 85
    • 4444291856 scopus 로고    scopus 로고
    • Sgt1 associates with Hsp90: An initial step of assembly of the core kinetochore complex
    • DOI 10.1128/MCB.24.18.8069-8079.2004
    • Bansal, P. K., Abdulle, R. & Kitagawa, K. Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex. Mol. Cell. Biol. 24, 8069-8079 (2004). (Pubitemid 39167457)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.18 , pp. 8069-8079
    • Bansal, P.K.1    Abdulle, R.2    Kitagawa, K.3
  • 86
    • 77957816357 scopus 로고    scopus 로고
    • The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity
    • Eckert, K. et al. The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J. Biol. Chem. 285, 31304-31312 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 31304-31312
    • Eckert, K.1
  • 87
    • 58149271606 scopus 로고    scopus 로고
    • Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
    • Johnson, J. & Brown, C. Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 14, 83-94 (2009).
    • (2009) Cell Stress Chaperones , vol.14 , pp. 83-94
    • Johnson, J.1    Brown, C.2
  • 88
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • DOI 10.1038/nrc1716
    • Whitesell, L. & Lindquist, S. L. HSP90 and the chaperoning of cancer. Nature Rev. Cancer 5, 761-772 (2005). (Pubitemid 41400776)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 89
    • 66149125584 scopus 로고    scopus 로고
    • Targeting HSP90 for cancer therapy
    • Mahalingam, D. et al. Targeting HSP90 for cancer therapy. Br. J. Cancer 100, 1523-1529 (2009).
    • (2009) Br. J. Cancer , vol.100 , pp. 1523-1529
    • Mahalingam, D.1
  • 90
    • 79958167192 scopus 로고    scopus 로고
    • Heat shock and awe
    • Dolgin, E. & Motluk, A. Heat shock and awe. Nature Med. 17, 646-649 (2011).
    • (2011) Nature Med. , vol.17 , pp. 646-649
    • Dolgin, E.1    Motluk, A.2
  • 91
    • 18944365231 scopus 로고    scopus 로고
    • A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)
    • DOI 10.1128/EC.4.5.849-860.2005
    • Millson, S. H. et al. A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot. Cell 4, 849-860 (2005). (Pubitemid 40697749)
    • (2005) Eukaryotic Cell , vol.4 , Issue.5 , pp. 849-860
    • Millson, S.H.1    Truman, A.W.2    King, V.3    Prodromou, C.4    Pearl, L.H.5    Piper, P.W.6
  • 92
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the hsp90 molecular chaperone uncovered using systems approaches
    • DOI 10.1016/j.cell.2007.07.036, PII S0092867407009749
    • McClellan, A. J. et al. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131, 121-135 (2007). (Pubitemid 47498528)
    • (2007) Cell , vol.131 , Issue.1 , pp. 121-135
    • McClellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5    Frydman, J.6
  • 93
    • 84862323158 scopus 로고    scopus 로고
    • Systematic identification of the HSP90 candidate regulated proteome
    • Wu, Z., Moghaddas Gholami, A. & Kuster, B. Systematic identification of the HSP90 candidate regulated proteome. Mol. Cell. Proteomics 11, M111.016675 (2012).
    • (2012) Mol. Cell. Proteomics , vol.11
    • Wu, Z.1    Moghaddas Gholami, A.2    Kuster, B.3
  • 94
    • 78651328883 scopus 로고    scopus 로고
    • The BioGRID interaction database: 2011 update
    • Stark, C. et al. The BioGRID Interaction Database: 2011 update. Nucleic Acids Res. 39, D698-D704 (2011).
    • (2011) Nucleic Acids Res. , vol.39
    • Stark, C.1
  • 95
    • 80053976720 scopus 로고    scopus 로고
    • An interaction network predicted from public data as a discovery tool: Application to the Hsp90 molecular chaperone machine
    • Echeverría, P. C., Bernthaler, A., Dupuis, P., Mayer, B. & Picard, D. An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS ONE 6, e26044 (2011).
    • (2011) PLoS ONE , vol.6
    • Echeverría, P.C.1    Bernthaler, A.2    Dupuis, P.3    Mayer, B.4    Picard, D.5
  • 96
    • 70049109583 scopus 로고    scopus 로고
    • Hsp90 governs echinocandin resistance in the pathogenic yeast Candida albicans via calcineurin
    • Singh, S. D. et al. Hsp90 governs echinocandin resistance in the pathogenic yeast Candida albicans via calcineurin. PLoS Pathog. 5, e1000532 (2009).
    • (2009) PLoS Pathog , vol.5
    • Singh, S.D.1
  • 97
    • 0034458959 scopus 로고    scopus 로고
    • Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin
    • DOI 10.1128/MCB.20.24.9262-9270.2000
    • Imai, J. & Yahara, I. Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin. Mol. Cell. Biol. 20, 9262-9270 (2000). (Pubitemid 32246112)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.24 , pp. 9262-9270
    • Imai, J.1    Yahara, I.2
  • 98
    • 0036032124 scopus 로고    scopus 로고
    • Antifungal activity in Saccharomyces cerevisiae is modulated by calcium signalling
    • DOI 10.1046/j.1365-2958.2002.03165.x
    • Edlind, T., Smith, L., Henry, K., Katiyar, S. & Nickels, J. Antifungal activity in Saccharomyces cerevisiae is modulated by calcium signalling. Mol. Microbiol. 46, 257-268 (2002). (Pubitemid 35231962)
    • (2002) Molecular Microbiology , vol.46 , Issue.1 , pp. 257-268
    • Edlind, T.1    Smith, L.2    Henry, K.3    Katiyar, S.4    Nickels, J.5
  • 99
    • 0038016755 scopus 로고    scopus 로고
    • Calcineurin A of Candida albicans: Involvement in antifungal tolerance, cell morphogenesis and virulence
    • DOI 10.1046/j.1365-2958.2003.03495.x
    • Sanglard, D., Ischer, F., Marchetti, O., Entenza, J. & Bille, J. Calcineurin A of Candida albicans: involvement in antifungal tolerance, cell morphogenesis and virulence. Mol. Microbiol. 48, 959-976 (2003). (Pubitemid 36628262)
    • (2003) Molecular Microbiology , vol.48 , Issue.4 , pp. 959-976
    • Sanglard, D.1    Ischer, F.2    Marchetti, O.3    Entenza, J.4    Bille, J.5
  • 100
    • 33845608850 scopus 로고    scopus 로고
    • Genetic architecture of Hsp90-dependent drug resistance
    • DOI 10.1128/EC.00274-06
    • Cowen, L. E., Carpenter, A. E., Matangkasombut, O., Fink, G. R. & Lindquist, S. Genetic architecture of Hsp90-dependent drug resistance. Eukaryot. Cell 5, 2184-2188 (2006). (Pubitemid 44956829)
    • (2006) Eukaryotic Cell , vol.5 , Issue.12 , pp. 2184-2188
    • Cowen, L.E.1    Carpenter, A.E.2    Matangkasombut, O.3    Fink, G.R.4    Lindquist, S.5
  • 101
    • 77958121046 scopus 로고    scopus 로고
    • PKC signaling regulates drug resistance of the fungal pathogen Candida albicans via circuitry comprised of Mkc1, calcineurin, and Hsp90
    • LaFayette, S. L. et al. PKC signaling regulates drug resistance of the fungal pathogen Candida albicans via circuitry comprised of Mkc1, calcineurin, and Hsp90. PLoS Pathog. 6, e1001069 (2010).
    • (2010) PLoS Pathog , vol.6
    • Lafayette, S.L.1
  • 102
    • 62449104891 scopus 로고    scopus 로고
    • Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease
    • Cowen, L. E. et al. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc. Natl Acad. Sci. USA 106, 2818-2823 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 2818-2823
    • Cowen, L.E.1
  • 103
    • 0030957532 scopus 로고    scopus 로고
    • Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway
    • Watanabe, Y., Takaesu, G., Hagiwara, M., Irie, K. & Matsumoto, K. Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway. Mol. Cell. Biol. 17, 2615-2623 (1997). (Pubitemid 27175143)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.5 , pp. 2615-2623
    • Watanabe, Y.1    Takaesu, G.2    Hagiwara, M.3    Irie, K.4    Matsumoto, K.5
  • 104
    • 0033009538 scopus 로고    scopus 로고
    • The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.1999.01375.x
    • Heinisch, J. J., Lorberg, A., Schmitz, H. P. & Jacoby, J. J. The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae. Mol. Microbiol. 32, 671-680 (1999). (Pubitemid 29241509)
    • (1999) Molecular Microbiology , vol.32 , Issue.4 , pp. 671-680
    • Heinisch, J.J.1    Lorberg, A.2    Schmitz, H.-P.3    Jacoby, J.J.4
  • 105
    • 10144237210 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans
    • San Jose, C., Monge, R. A., Perez-Diaz, R., Pla, J. & Nombela, C. The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans. J. Bacteriol. 178, 5850-5852 (1996). (Pubitemid 26327699)
    • (1996) Journal of Bacteriology , vol.178 , Issue.19 , pp. 5850-5852
    • Jose, C.S.1    Monge, R.A.2    Perez-Diaz, R.3    Pla, J.4    Nombela, C.5
  • 106
    • 0031717526 scopus 로고    scopus 로고
    • Stress-activated signalling pathways in yeast
    • DOI 10.1046/j.1365-2443.1998.00211.x
    • Toone, W. M. & Jones, N. Stress-activated signalling pathways in yeast. Genes Cells 3, 485-498 (1998). (Pubitemid 28475319)
    • (1998) Genes to Cells , vol.3 , Issue.8 , pp. 485-498
    • Toone, W.M.1    Jones, N.2
  • 107
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • DOI 10.1128/MMBR.66.2.300-372.2002
    • Hohmann, S. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev. 66, 300-372 (2002). (Pubitemid 34625712)
    • (2002) Microbiology and Molecular Biology Reviews , vol.66 , Issue.2 , pp. 300-372
    • Hohmann, S.1
  • 108
    • 4344587177 scopus 로고    scopus 로고
    • A conserved stress-activated protein kinase regulates a core stress response in the human pathogen Candida albicans
    • DOI 10.1091/mbc.E04-03-0181
    • Smith, D. A., Nicholls, S., Morgan, B. A., Brown, A. J. & Quinn, J. A conserved stress-activated protein kinase regulates a core stress response in the human pathogen Candida albicans. Mol. Biol. Cell 15, 4179-4190 (2004). (Pubitemid 39122021)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.9 , pp. 4179-4190
    • Smith, D.A.1    Nicholls, S.2    Morgan, B.A.3    Brown, A.J.P.4    Quinn, J.5
  • 109
    • 77950499351 scopus 로고    scopus 로고
    • Stress signalling to fungal stress-activated protein kinase pathways
    • Smith, D. A., Morgan, B. A. & Quinn, J. Stress signalling to fungal stress-activated protein kinase pathways. FEMS Microbiol. Lett. 306, 1-8 (2010).
    • (2010) FEMS Microbiol. Lett. , vol.306 , pp. 1-8
    • Smith, D.A.1    Morgan, B.A.2    Quinn, J.3
  • 111
    • 33947633366 scopus 로고    scopus 로고
    • Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)
    • DOI 10.1128/EC.00343-06
    • Hawle, P. et al. Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p). Eukaryot. Cell 6, 521-532 (2007). (Pubitemid 46492340)
    • (2007) Eukaryotic Cell , vol.6 , Issue.3 , pp. 521-532
    • Hawle, P.1    Horst, D.2    Bebelman, J.P.3    Yang, X.X.4    Siderius, M.5    Van Der Vies, S.M.6
  • 112
    • 0033166271 scopus 로고    scopus 로고
    • Heat shock-induced activation of stress MAP kinase is regulated by threonine-and tyrosine-specific phosphatases
    • Nguyen, A. N. & Shiozaki, K. Heat shock-induced activation of stress MAP kinase is regulated by threonine-and tyrosine-specific phosphatases. Genes Dev. 13, 1653-1663 (1999). (Pubitemid 29325871)
    • (1999) Genes and Development , vol.13 , Issue.13 , pp. 1653-1663
    • Nguyen, A.N.1    Shiozaki, K.2
  • 113
  • 114
    • 84855879659 scopus 로고    scopus 로고
    • Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans
    • Senn, H., Shapiro, R. S. & Cowen, L. E. Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans. Mol. Biol. Cell 23, 268-283 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 268-283
    • Senn, H.1    Shapiro, R.S.2    Cowen, L.E.3
  • 115
    • 65049086509 scopus 로고    scopus 로고
    • Hsp90 orchestrates temperature-dependent Candida albicans morphogenesis via Ras1-PKA signaling
    • Shapiro, R. S. et al. Hsp90 orchestrates temperature-dependent Candida albicans morphogenesis via Ras1-PKA signaling. Curr. Biol. 19, 621-629 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 621-629
    • Shapiro, R.S.1
  • 116
    • 33644873184 scopus 로고    scopus 로고
    • BioGRID: A general repository for interaction datasets
    • Stark, C. et al. BioGRID: a general repository for interaction datasets. Nucleic Acids Res. 34, D535-D539 (2006).
    • (2006) Nucleic Acids Res. , vol.34
    • Stark, C.1
  • 118
    • 23444449142 scopus 로고    scopus 로고
    • Integrative model of the response of yeast to osmotic shock
    • DOI 10.1038/nbt1114
    • Klipp, E., Nordlander, B., Kruger, R., Gennemark, P. & Hohmann, S. Integrative model of the response of yeast to osmotic shock. Nature Biotech. 23, 975-982 (2005). (Pubitemid 41114031)
    • (2005) Nature Biotechnology , vol.23 , Issue.8 , pp. 975-982
    • Klipp, E.1    Nordlander, B.2    Kruger, R.3    Gennemark, P.4    Hohmann, S.5
  • 119
    • 80053228416 scopus 로고    scopus 로고
    • Time-dependent quantitative multicomponent control of the G1-S network by the stress-activated protein kinase Hog1 upon osmostress
    • Adrover, M. A. et al. Time-dependent quantitative multicomponent control of the G1-S network by the stress-activated protein kinase Hog1 upon osmostress. Sci. Signal. 4, ra63 (2011).
    • (2011) Sci. Signal. , vol.4
    • Adrover, M.A.1
  • 120
    • 80055081144 scopus 로고    scopus 로고
    • Heat shock partially dissociates the overlapping modules of the yeast protein-protein interaction network: A systems level model of adaptation
    • Mihalik, Á. & Csermely, P. Heat shock partially dissociates the overlapping modules of the yeast protein-protein interaction network: a systems level model of adaptation. PLoS Computat. Biol. 7, e1002187 (2011).
    • (2011) PLoS Computat. Biol. , vol.7
    • Mihalik, Á.1    Csermely, P.2
  • 121
    • 81055145456 scopus 로고    scopus 로고
    • Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes
    • Ebong, I.-o. et al. Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes. Proc. Natl Acad. Sci. USA 108, 17939-17944 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 17939-17944
    • Ebong, I.-O.1
  • 122
    • 79960337702 scopus 로고    scopus 로고
    • Modelling the role of the Hsp70/Hsp90 system in the maintenance of protein homeostasis
    • Proctor, C. J. & Lorimer, I. A. J. Modelling the role of the Hsp70/Hsp90 system in the maintenance of protein homeostasis. PLoS ONE 6, e22038 (2011).
    • (2011) PLoS ONE , vol.6
    • Proctor, C.J.1    Lorimer, I.A.J.2
  • 123
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90
    • Aligue, R., Akhavan-Niak, H. & Russell, P. A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90. EMBO J. 13, 6099-6106 (1994).
    • (1994) EMBO J. , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 124
    • 84858703485 scopus 로고    scopus 로고
    • Pho85, Pcl1, and Hms1 signaling governs Candida albicans morphogenesis induced by high temperature or Hsp90 compromise
    • Shapiro, R. S. et al. Pho85, Pcl1, and Hms1 signaling governs Candida albicans morphogenesis induced by high temperature or Hsp90 compromise. Curr. Biol. 22, 461-470 (2012).
    • (2012) Curr. Biol. , vol.22 , pp. 461-470
    • Shapiro, R.S.1
  • 126
    • 0025896441 scopus 로고
    • In vitro production of tumor necrosis factor by murine splenic macrophages stimulated with mannoprotein constituents of Candida albicans cell wall
    • Vecchiarelli, A., Puliti, M., Torosantucci, A., Cassone, A. & Bistoni, F. In vitro production of tumor necrosis factor by murine splenic macrophages stimulated with mannoprotein constituents of Candida albicans cell wall. Cell. Immunol. 134, 65-76 (1991).
    • (1991) Cell. Immunol. , vol.134 , pp. 65-76
    • Vecchiarelli, A.1    Puliti, M.2    Torosantucci, A.3    Cassone, A.4    Bistoni, F.5
  • 127
    • 0028012419 scopus 로고
    • Secretion of TNF-α by alveolar macrophages in response to Candida albicans mannan
    • Garner, R., Rubanowice, K., Sawyer, R. & Hudson, J. Secretion of TNF-α by alveolar macrophages in response to Candida albicans mannan. J. Leukoc. Biol. 55, 161-168 (1994). (Pubitemid 24066338)
    • (1994) Journal of Leukocyte Biology , vol.55 , Issue.2 , pp. 161-168
    • Garner, R.E.1    Rubanowice, K.2    Sawyer, R.T.3    Hudson, J.A.4
  • 128
    • 33644853912 scopus 로고    scopus 로고
    • Candida albicans mannoprotein influences the biological function of dendritic cells
    • DOI 10.1111/j.1462-5822.2005.00651.x
    • Pietrella, D., Bistoni, G., Corbucci, C., Perito, S. & Vecchiarelli, A. Candida albicans mannoprotein influences the biological function of dendritic cells. Cell. Microbiol. 8, 602-612 (2006). (Pubitemid 43372739)
    • (2006) Cellular Microbiology , vol.8 , Issue.4 , pp. 602-612
    • Pietrella, D.1    Bistoni, G.2    Corbucci, C.3    Perito, S.4    Vecchiarelli, A.5
  • 129
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: Principles and mechanisms
    • Jarosz, D. F., Taipale, M. & Lindquist, S. Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu. Rev. Genet. 44, 189-216 (2010).
    • (2010) Annu. Rev. Genet. , vol.44 , pp. 189-216
    • Jarosz, D.F.1    Taipale, M.2    Lindquist, S.3
  • 130
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • DOI 10.1038/nature749
    • Queitsch, C., Sangster, T. A. & Lindquist, S. Hsp90 as a capacitor of phenotypic variation. Nature 417, 618-624 (2002). (Pubitemid 34614814)
    • (2002) Nature , vol.417 , Issue.6889 , pp. 618-624
    • Queitsch, C.1    Sangstert, T.A.2    Lindquist, S.3
  • 131
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
    • DOI 10.1002/bies.20020
    • Sangster, T. A., Lindquist, S. & Queitsch, C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays 26, 348-362 (2004). (Pubitemid 38468577)
    • (2004) BioEssays , vol.26 , Issue.4 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 134
    • 0037228526 scopus 로고    scopus 로고
    • Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution
    • DOI 10.1038/ng1067
    • Sollars, V. et al. Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution. Nature Genet. 33, 70-74 (2003). (Pubitemid 36068685)
    • (2003) Nature Genetics , vol.33 , Issue.1 , pp. 70-74
    • Sollars, V.1    Lu, X.2    Xiao, L.3    Wang, X.4    Garfinkel, M.D.5    Ruden, D.M.6
  • 135
    • 39149087719 scopus 로고    scopus 로고
    • The evolution of fungal drug resistance: Modulating the trajectory from genotype to phenotype
    • DOI 10.1038/nrmicro1835, PII NRMICRO1835
    • Cowen, L. E. The evolution of fungal drug resistance: modulating the trajectory from genotype to phenotype. Nature Rev. Microbiol. 6, 187-198 (2008). (Pubitemid 351256314)
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.3 , pp. 187-198
    • Cowen, L.E.1
  • 137
    • 84855478341 scopus 로고    scopus 로고
    • Fitness trade-offs and environmentally induced mutation buffering in isogenic C. elegans
    • Casanueva, M. O., Burga, A. & Lehner, B. Fitness trade-offs and environmentally induced mutation buffering in isogenic C. elegans. Science 335, 82-85 (2012).
    • (2012) Science , vol.335 , pp. 82-85
    • Casanueva, M.O.1    Burga, A.2    Lehner, B.3
  • 139
    • 53749085229 scopus 로고    scopus 로고
    • A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology
    • Herrgard, M. J. et al. A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology. Nature Biotech. 26, 1155-1160 (2008).
    • (2008) Nature Biotech. , vol.26 , pp. 1155-1160
    • Herrgard, M.J.1
  • 141
    • 0031755018 scopus 로고    scopus 로고
    • Cns1 is an essential protein associated with the Hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells
    • Marsh, J. A., Kalton, H. M. & Gaber, R. F. Cns1 is an essential protein associated with the Hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells. Mol. Cell. Biol. 18, 7353-7359 (1998). (Pubitemid 28533055)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.12 , pp. 7353-7359
    • Marsh, J.A.1    Kalton, H.M.2    Gaber, R.F.3


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