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Volumn 18, Issue 6, 2017, Pages 345-360

The HSP90 chaperone machinery

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; DIMER; HEAT SHOCK PROTEIN 90; TETRATRICOPEPTIDE REPEAT PROTEIN; PROTEIN BINDING;

EID: 85019166473     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm.2017.20     Document Type: Review
Times cited : (1095)

References (200)
  • 1
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa, F. Discovery of the heat shock response. Cell Stress Chaperones 1, 97-98 (1996
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 2
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein, and immunophilin chaperones
    • Pratt, W. B., & Toft, D. O. Steroid receptor interactions with heat shock protein, and immunophilin chaperones. Endocr. Rev. 18, 306-360 (1997
    • (1997) Endocr. Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 3
    • 0017745268 scopus 로고
    • Identification of a transformation-specific antigen induced by an avian sarcoma virus
    • Brugge, J. S., & Erikson, R. L. Identification of a transformation-specific antigen induced by an avian sarcoma virus. Nature 269, 346-348 (1977
    • (1977) Nature , vol.269 , pp. 346-348
    • Brugge, J.S.1    Erikson, R.L.2
  • 4
    • 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
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 5
    • 0030748520 scopus 로고    scopus 로고
    • Essential role of the first intron in the transcription of hsp90β gene
    • Shen, Y., et al. Essential role of the first intron in the transcription of hsp90β gene. FEBS Lett. 413, 92-98 (1997
    • (1997) FEBS Lett , vol.413 , pp. 92-98
    • Shen, Y.1
  • 6
    • 0032588963 scopus 로고    scopus 로고
    • Regulation of human hsp90alpha gene expression
    • Zhang, S. L., et al. Regulation of human hsp90alpha gene expression. FEBS Lett. 444, 130-135 (1999
    • (1999) FEBS Lett , vol.444 , pp. 130-135
    • Zhang, S.L.1
  • 7
    • 33746660802 scopus 로고    scopus 로고
    • Comparative genomics, and evolution of the HSP90 family of genes across all kingdoms of organisms
    • Chen, B., Zhong, D., & Monteiro, A. Comparative genomics, and evolution of the HSP90 family of genes across all kingdoms of organisms. BMC Genomics 7, 156 (2006
    • (2006) BMC Genomics , vol.7 , pp. 156
    • Chen, B.1    Zhong, D.2    Monteiro, A.3
  • 8
    • 84857048585 scopus 로고    scopus 로고
    • Evolution and function of diverse Hsp90 homologs, and cochaperone proteins
    • Johnson, J. L. Evolution, and function of diverse Hsp90 homologs, and cochaperone proteins. Biochim. Biophys. Acta 1823, 607-613 (2012
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 607-613
    • Johnson, J.L.1
  • 9
    • 0034603178 scopus 로고    scopus 로고
    • The hsp90 related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • Felts, S. J., et al. The hsp90 related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275, 3305-3312 (2000
    • (2000) J. Biol. Chem , vol.275 , pp. 3305-3312
    • Felts, S.J.1
  • 10
    • 33644666048 scopus 로고    scopus 로고
    • HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii
    • Willmund, F., & Schroda, M. HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii. Plant Physiol. 138, 2310-2322 (2005
    • (2005) Plant Physiol , vol.138 , pp. 2310-2322
    • Willmund, F.1    Schroda, M.2
  • 11
    • 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 396, 336-342 (1998
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 12
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch, C., Sangster, T. A., & Lindquist, S. Hsp90 as a capacitor of phenotypic variation. Nature 417, 618-624 (2002
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 13
    • 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
  • 14
    • 84890110060 scopus 로고    scopus 로고
    • Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish
    • Rohner, N., et al. Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish. Science 342, 1372-1375 (2013
    • (2013) Science , vol.342 , pp. 1372-1375
    • Rohner, N.1
  • 15
    • 84926021668 scopus 로고    scopus 로고
    • Hsp90: Breaking the symmetry
    • Mayer, M. P., & Le Breton, L. Hsp90: breaking the symmetry. Mol. Cell 58, 8-20 (2015
    • (2015) Mol. Cell , vol.58 , pp. 8-20
    • Mayer, M.P.1    Le Breton, L.2
  • 16
    • 36849083947 scopus 로고    scopus 로고
    • Dimerization of Hsp90 is required for in vivo function design, and analysis of monomers, and dimers
    • Wayne, N., & Bolon, D. N. Dimerization of Hsp90 is required for in vivo function. Design, and analysis of monomers, and dimers. J. Biol. Chem. 282, 35386-35395 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 35386-35395
    • Wayne, N.1    Bolon, D.N.2
  • 17
    • 0031444238 scopus 로고    scopus 로고
    • Identification, and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., et al. Identification, and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75 (1997
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1
  • 18
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris, S. F., Shiau, A. K., & Agard, D. A. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12, 1087-1097 (2004
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 19
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90, & co - A holding for folding
    • Buchner, J. Hsp90, & co. - a holding for folding. Trends Biochem. Sci. 24, 136-141 (1999
    • (1999) Trends Biochem. Sci , vol.24 , pp. 136-141
    • Buchner, J.1
  • 20
    • 69249130057 scopus 로고    scopus 로고
    • The charged linker region is an important regulator of Hsp90 function
    • Hainzl, O., Lapina, M. C., Buchner, J., & Richter, K. The charged linker region is an important regulator of Hsp90 function. J. Biol. Chem. 284, 22559-22567 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 22559-22567
    • Hainzl, O.1    Lapina, M.C.2    Buchner, J.3    Richter, K.4
  • 21
    • 84918567953 scopus 로고    scopus 로고
    • The charged linker of the molecular chaperone Hsp90 modulates domain contacts, and biological function
    • Jahn, M., et al. The charged linker of the molecular chaperone Hsp90 modulates domain contacts, and biological function. Proc. Natl Acad. Sci. USA 111, 17881-17886 (2014
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 17881-17886
    • Jahn, M.1
  • 22
    • 84863878440 scopus 로고    scopus 로고
    • Chaperoning the chaperone: A role for the co chaperone Cpr7 in modulating hsp90 function in saccharomyces cerevisiae
    • Zuehlke, A. D., & Johnson, J. L. Chaperoning the chaperone: a role for the co chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics 191, 805-814 (2012
    • (2012) Genetics , vol.191 , pp. 805-814
    • Zuehlke, A.D.1    Johnson, J.L.2
  • 23
    • 84863116734 scopus 로고    scopus 로고
    • Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity
    • Tsutsumi, S., et al. Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity. Proc. Natl Acad. Sci. USA 109, 2937-2942 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 2937-2942
    • Tsutsumi, S.1
  • 24
    • 33750008686 scopus 로고    scopus 로고
    • Structural analysis of e coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • Shiau, A. K., Harris, S. F., Southworth, D. R., & Agard, D. A. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 127, 329-340 (2006
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 25
    • 34948893963 scopus 로고    scopus 로고
    • Structures of GRP94 nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
    • Dollins, D. E., Warren, J. J., Immormino, R. M., & Gewirth, D. T. Structures of GRP94 nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol. Cell 28, 41-56 (2007
    • (2007) Mol. Cell , vol.28 , pp. 41-56
    • Dollins, D.E.1    Warren, J.J.2    Immormino, R.M.3    Gewirth, D.T.4
  • 26
    • 85002489634 scopus 로고    scopus 로고
    • Multidomain structure, and correlated dynamics determined by self-consistent FRET networks
    • Hellenkamp, B., Wortmann, P., Kandzia, F., Zacharias, M., & Hugel, T. Multidomain structure, and correlated dynamics determined by self-consistent FRET networks. Nat. Methods 14, 174-180 (2017
    • (2017) Nat. Methods , vol.14 , pp. 174-180
    • Hellenkamp, B.1    Wortmann, P.2    Kandzia, F.3    Zacharias, M.4    Hugel, T.5
  • 27
    • 84867051420 scopus 로고    scopus 로고
    • From a ratchet mechanism to
    • random fluctuations evolution of Hsp90?s mechanochemical cycle
    • Ratzke, C., Nguyen, M. N., Mayer, M. P., & Hugel, T. From a ratchet mechanism to random fluctuations evolution of Hsp90?s mechanochemical cycle. J. Mol. Biol. 423, 462-471 (2012
    • (2012) J. Mol. Biol , vol.423 , pp. 462-471
    • Ratzke, C.1    Nguyen, M.N.2    Mayer, M.P.3    Hugel, T.4
  • 28
    • 61949212626 scopus 로고    scopus 로고
    • The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
    • Mickler, M., Hessling, M., Ratzke, C., Buchner, J., & Hugel, T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat. Struct. Mol. Biol. 16, 281-286 (2009
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 281-286
    • Mickler, M.1    Hessling, M.2    Ratzke, C.3    Buchner, J.4    Hugel, T.5
  • 29
    • 62049084010 scopus 로고    scopus 로고
    • Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
    • Graf, C., Stankiewicz, M., Kramer, G., & Mayer, M. P. Spatially, and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J. 28, 602-613 (2009
    • (2009) EMBO J. , vol.28 , pp. 602-613
    • Graf, C.1    Stankiewicz, M.2    Kramer, G.3    Mayer, M.P.4
  • 30
    • 0033985080 scopus 로고    scopus 로고
    • GHKL an emergent ATPase/kinase superfamily
    • Dutta, R., & Inouye, M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 25, 24-28 (2000
    • (2000) Trends Biochem. Sci , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 31
    • 0030752373 scopus 로고    scopus 로고
    • ATP-binding properties of human Hsp90
    • Scheibel, T., et al. ATP-binding properties of human Hsp90. J. Biol. Chem. 272, 18608-18613 (1997
    • (1997) J. Biol. Chem , vol.272 , pp. 18608-18613
    • Scheibel, T.1
  • 32
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human hsp90 by a client protein
    • McLaughlin, S. H., Smith, H. W., & Jackson, S. E. Stimulation of the weak ATPase activity of human hsp90 by a client protein. J. Mol. Biol. 315, 787-798 (2002
    • (2002) J. Mol. Biol , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 33
    • 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
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1
  • 34
    • 61949349758 scopus 로고    scopus 로고
    • Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
    • Hessling, M., Richter, K., & Buchner, J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 16, 287-293 (2009
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 287-293
    • Hessling, M.1    Richter, K.2    Buchner, J.3
  • 35
    • 0034663806 scopus 로고    scopus 로고
    • The ATPase cycle of Hsp90 drives a molecular ?Clamp? Via transient dimerization of the N terminal domains
    • Prodromou, C., et al. The ATPase cycle of Hsp90 drives a molecular ?clamp? via transient dimerization of the N terminal domains. EMBO J. 19, 4383-4392 (2000
    • (2000) EMBO J. , vol.19 , pp. 4383-4392
    • Prodromou, C.1
  • 36
    • 51049093018 scopus 로고    scopus 로고
    • Intra-and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90
    • Cunningham, C. N., Krukenberg, K. A., & Agard, D. A. Intra-and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J. Biol. Chem. 283, 21170-21178 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 21170-21178
    • Cunningham, C.N.1    Krukenberg, K.A.2    Agard, D.A.3
  • 37
    • 0037352446 scopus 로고    scopus 로고
    • Structural, and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis, and client protein, and cochaperone interactions
    • Meyer, P., et al. Structural, and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis, and client protein, and cochaperone interactions. Mol. Cell 11, 647-658 (2003
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1
  • 38
  • 39
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding, and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B., et al. ATP binding, and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829-4836 (1998
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1
  • 40
    • 84892840819 scopus 로고    scopus 로고
    • Designed Hsp90 heterodimers reveal an asymmetric ATPase-driven mechanism in vivo
    • Mishra, P., & Bolon, D. N. Designed Hsp90 heterodimers reveal an asymmetric ATPase-driven mechanism in vivo. Mol. Cell 53, 344-350 (2014
    • (2014) Mol. Cell , vol.53 , pp. 344-350
    • Mishra, P.1    Bolon, D.N.2
  • 41
    • 84990951672 scopus 로고    scopus 로고
    • Importance of cycle timing for the function of the molecular chaperone Hsp90
    • Zierer, B. K., et al. Importance of cycle timing for the function of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 23, 1020-1028 (2016
    • (2016) Nat. Struct. Mol. Biol , vol.23 , pp. 1020-1028
    • Zierer, B.K.1
  • 42
    • 85006891206 scopus 로고    scopus 로고
    • Mechanisms of Hsp90 regulation
    • Prodromou, C. Mechanisms of Hsp90 regulation. Biochem. J. 473, 2439-2452 (2016
    • (2016) Biochem. J. , vol.473 , pp. 2439-2452
    • Prodromou, C.1
  • 43
    • 84992390642 scopus 로고    scopus 로고
    • Defining the essential function of yeast Hsf1 reveals a compact transcriptional program for maintaining eukaryotic proteostasis
    • Solis, E. J., et al. Defining the essential function of yeast Hsf1 reveals a compact transcriptional program for maintaining eukaryotic proteostasis. Mol. Cell 63, 60-71 (2016
    • (2016) Mol. Cell , vol.63 , pp. 60-71
    • Solis, E.J.1
  • 44
    • 84934440933 scopus 로고    scopus 로고
    • Chaperone regulation of the heat shock protein response
    • Voellmy, R., & Boellmann, F. Chaperone regulation of the heat shock protein response. Adv. Exp. Med. Biol. 594, 89-99 (2007
    • (2007) Adv. Exp. Med. Biol , vol.594 , pp. 89-99
    • Voellmy, R.1    Boellmann, F.2
  • 45
    • 84876707777 scopus 로고    scopus 로고
    • The chaperone Hsp90: Changing partners for demanding clients
    • Rohl, A., Rohrberg, J., & Buchner, J. The chaperone Hsp90: changing partners for demanding clients. Trends Biochem. Sci. 38, 253-262 (2013
    • (2013) Trends Biochem. Sci , vol.38 , pp. 253-262
    • Rohl, A.1    Rohrberg, J.2    Buchner, J.3
  • 46
    • 35348858091 scopus 로고    scopus 로고
    • Post-translational modification of heat-shock protein 90: Impact on chaperone function
    • 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
    • (2007) Expert Opin. Drug Discov , vol.2 , pp. 1403-1414
    • Scroggins, B.T.1    Neckers, L.2
  • 47
    • 84857390643 scopus 로고    scopus 로고
    • Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation
    • Soroka, J., et al. Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Mol. Cell 45, 517-528 (2012
    • (2012) Mol. Cell , vol.45 , pp. 517-528
    • Soroka, J.1
  • 48
    • 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 1823, 648-655 (2012
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 648-655
    • Mollapour, M.1    Neckers, L.2
  • 49
    • 0035980061 scopus 로고    scopus 로고
    • Hsp90 phosphorylation is linked to its chaperoning function assembly of the reovirus cell attachment protein
    • Zhao, Y. G., et al. Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein. J. Biol. Chem. 276, 32822-32827 (2001
    • (2001) J. Biol. Chem , vol.276 , pp. 32822-32827
    • Zhao, Y.G.1
  • 50
    • 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
  • 51
    • 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
  • 52
    • 31444454302 scopus 로고    scopus 로고
    • The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
    • 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
    • (2006) EMBO J. , vol.25 , pp. 367-376
    • Wandinger, S.K.1    Suhre, M.H.2    Wegele, H.3    Buchner, J.4
  • 53
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation, and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs, J. J., et al. HDAC6 regulates Hsp90 acetylation, and chaperone-dependent activation of glucocorticoid receptor. Mol. Cell 18, 601-607 (2005
    • (2005) Mol. Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1
  • 54
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates, and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali, P., et al. Inhibition of histone deacetylase 6 acetylates, and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 280, 26729-26734 (2005
    • (2005) J. Biol. Chem , vol.280 , pp. 26729-26734
    • Bali, P.1
  • 55
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins, B. T., et al. An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol. Cell 25, 151-159 (2007
    • (2007) Mol. Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1
  • 56
    • 0009621605 scopus 로고    scopus 로고
    • Dynamic activation of endothelial nitric oxide synthase by Hsp90
    • Garcia-Cardena, G., et al. Dynamic activation of endothelial nitric oxide synthase by Hsp90. Nature 392, 821-824 (1998
    • (1998) Nature , vol.392 , pp. 821-824
    • Garcia-Cardena, G.1
  • 57
    • 20844444338 scopus 로고    scopus 로고
    • S Nitrosylation of Hsp90 promotes the inhibition of its ATPase, and endothelial nitric oxide synthase regulatory activities
    • Martinez-Ruiz, A., et al. S Nitrosylation of Hsp90 promotes the inhibition of its ATPase, and endothelial nitric oxide synthase regulatory activities. Proc. Natl Acad. Sci. USA 102, 8525-8530 (2005
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8525-8530
    • Martinez-Ruiz, A.1
  • 58
    • 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
  • 59
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein protein interactions
    • Das, A. K., Cohen, P. W., & Barford, D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein protein interactions. EMBO J. 17, 1192-1199 (1998
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 60
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70 Hsp90 multichaperone machine
    • Scheufler, C., et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70 Hsp90 multichaperone machine. Cell 101, 199-210 (2000
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1
  • 61
    • 84858763945 scopus 로고    scopus 로고
    • The architecture of functional modules in the Hsp90 co chaperone Sti1/Hop
    • Schmid, A. B., et al. The architecture of functional modules in the Hsp90 co chaperone Sti1/Hop. EMBO J. 31, 1506-1517 (2012
    • (2012) EMBO J. , vol.31 , pp. 1506-1517
    • Schmid, A.B.1
  • 62
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates Hsp70/Hsp90 interactions in protein folding
    • Johnson, B. D., Schumacher, R. J., Ross, E. D., & Toft, D. O. Hop modulates Hsp70/Hsp90 interactions in protein folding. J. Biol. Chem. 273, 3679-3686 (1998
    • (1998) J. Biol. Chem , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 64
    • 78650983812 scopus 로고    scopus 로고
    • Mixed Hsp90 cochaperone complexes are important for the progression of the reaction cycle
    • Li, J., Richter, K., & Buchner, J. Mixed Hsp90 cochaperone complexes are important for the progression of the reaction cycle. Nat. Struct. Mol. Biol. 18, 61-66 (2011
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 61-66
    • Li, J.1    Richter, K.2    Buchner, J.3
  • 66
    • 0033081968 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co chaperones
    • Prodromou, C., et al. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co chaperones. EMBO J. 18, 754-762 (1999
    • (1999) EMBO J. , vol.18 , pp. 754-762
    • Prodromou, C.1
  • 67
    • 84926615158 scopus 로고    scopus 로고
    • Hsp90 regulates the dynamics of its cochaperone Sti1, and the transfer of Hsp70 between modules
    • Rohl, A., et al. Hsp90 regulates the dynamics of its cochaperone Sti1, and the transfer of Hsp70 between modules. Nat. Commun. 6, 6655 (2015
    • (2015) Nat. Commun , vol.6 , pp. 6655
    • Rohl, A.1
  • 68
    • 84862816993 scopus 로고    scopus 로고
    • Dynamics of the regulation of hsp90 by the co chaperone sti1
    • Lee, C. T., Graf, C., Mayer, F. J., Richter, S. M., & Mayer, M. P. Dynamics of the regulation of Hsp90 by the co chaperone Sti1. EMBO J. 31, 1518-1528 (2012
    • (2012) EMBO J. , vol.31 , pp. 1518-1528
    • Lee, C.T.1    Graf, C.2    Mayer, F.J.3    Richter, S.M.4    Mayer, M.P.5
  • 69
    • 84923372470 scopus 로고    scopus 로고
    • Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop
    • Alvira, S., et al. Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. Nat. Commun. 5, 5484 (2014
    • (2014) Nat. Commun , vol.5 , pp. 5484
    • Alvira, S.1
  • 70
    • 84922254182 scopus 로고    scopus 로고
    • Hop/Sti1 phosphorylation inhibits its co chaperone function
    • Rohl, A., et al. Hop/Sti1 phosphorylation inhibits its co chaperone function. EMBO Rep. 16, 240-249 (2015
    • (2015) EMBO Rep , vol.16 , pp. 240-249
    • Rohl, A.1
  • 71
    • 84883352804 scopus 로고    scopus 로고
    • Stress-inducible phosphoprotein 1 has unique cochaperone activity during development, and regulates cellular response to ischemia via the prion protein
    • Beraldo, F. H., et al. Stress-inducible phosphoprotein 1 has unique cochaperone activity during development, and regulates cellular response to ischemia via the prion protein. FASEB J. 27, 3594-3607 (2013
    • (2013) FASEB J. , vol.27 , pp. 3594-3607
    • Beraldo, F.H.1
  • 72
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 cochaperone Sti1 p60
    • Chang, H. C., Nathan, D. F., & Lindquist, S. In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol. Cell. Biol. 17, 318-325 (1997
    • (1997) Mol. Cell. Biol , Issue.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 73
    • 84948397326 scopus 로고    scopus 로고
    • Hsp70, and Hsp90 of e coli directly interact for collaboration in protein remodeling
    • Genest, O., Hoskins, J. R., Kravats, A. N., Doyle, S. M., & Wickner, S. Hsp70, and Hsp90 of E. coli directly interact for collaboration in protein remodeling. J. Mol. Biol. 427, 3877-3889 (2015
    • (2015) J. Mol. Biol , vol.427 , pp. 3877-3889
    • Genest, O.1    Hoskins, J.R.2    Kravats, A.N.3    Doyle, S.M.4    Wickner, S.5
  • 74
    • 52249108496 scopus 로고    scopus 로고
    • Hsp90 dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37
    • Vaughan, C. K., et al. Hsp90 dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol. Cell 31, 886-895 (2008
    • (2008) Mol. Cell , vol.31 , pp. 886-895
    • Vaughan, C.K.1
  • 75
    • 37549067731 scopus 로고    scopus 로고
    • Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling
    • Riggs, D. L., et al. Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling. Mol. Cell. Biol. 27, 8658-8669 (2007
    • (2007) Mol. Cell. Biol , vol.27 , pp. 8658-8669
    • Riggs, D.L.1
  • 76
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90 associated proteins
    • Bose, S., Weikl, T., Bugl, H., & Buchner, J. Chaperone function of Hsp90 associated proteins. Science 274, 1715-1717 (1996
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 77
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin CYP 40, and the steroid aporeceptor-associated protein p23
    • Freeman, B. C., Toft, D. O., & Morimoto, R. I. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp 40, and the steroid aporeceptor-associated protein p23. Science 274, 1718-1720 (1996
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 78
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37
    • Roe, S. M., et al. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116, 87-98 (2004
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1
  • 79
    • 0037036458 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by the co chaperone Cdc37p/p50cdc37
    • Siligardi, G., et al. Regulation of Hsp90 ATPase activity by the co chaperone Cdc37p/p50cdc37. J. Biol. Chem. 277, 20151-20159 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 20151-20159
    • Siligardi, G.1
  • 80
    • 84976318037 scopus 로고    scopus 로고
    • Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps, and stabilizes an unfolded kinase
    • Verba, K. A., et al. Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps, and stabilizes an unfolded kinase. Science 352, 1542-1547 (2016
    • (2016) Science , vol.352 , pp. 1542-1547
    • Verba, K.A.1
  • 81
    • 84878392353 scopus 로고    scopus 로고
    • Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N terminal, and middle domain binding sites
    • Eckl, J. M., et al. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N terminal, and middle domain binding sites. J. Biol. Chem. 288, 16032-16042 (2013
    • (2013) J. Biol. Chem , vol.288 , pp. 16032-16042
    • Eckl, J.M.1
  • 82
    • 84951760190 scopus 로고    scopus 로고
    • Hsp90 Cdc37 complexes with protein kinases form cooperatively with multiple distinct interaction sites
    • Eckl, J. M., et al. Hsp90 Cdc37 complexes with protein kinases form cooperatively with multiple distinct interaction sites. J. Biol. Chem. 290, 30843-30854 (2015
    • (2015) J. Biol. Chem , vol.290 , pp. 30843-30854
    • Eckl, J.M.1
  • 83
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1
    • Panaretou, B., et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell 10, 1307-1318 (2002
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 84
    • 10744221887 scopus 로고    scopus 로고
    • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
    • Meyer, P., et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 23, 1402-1410 (2004
    • (2004) EMBO J. , vol.23 , pp. 1402-1410
    • Meyer, P.1
  • 85
    • 75949106173 scopus 로고    scopus 로고
    • Asymmetric activation of the hsp90 dimer by its cochaperone aha1
    • Retzlaff, M., et al. Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol. Cell 37, 344-354 (2010
    • (2010) Mol. Cell , vol.37 , pp. 344-354
    • Retzlaff, M.1
  • 86
    • 77949438155 scopus 로고    scopus 로고
    • Biological, and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis
    • Koulov, A. V., et al. Biological, and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Mol. Biol. Cell 21, 871-884 (2010
    • (2010) Mol. Biol. Cell , vol.21 , pp. 871-884
    • Koulov, A.V.1
  • 87
    • 84875225582 scopus 로고    scopus 로고
    • Integration of the accelerator aha1 in the hsp90 co chaperone cycle
    • Li, J., Richter, K., Reinstein, J., & Buchner, J. Integration of the accelerator Aha1 in the Hsp90 co chaperone cycle. Nat. Struct. Mol. Biol. 20, 326-331 (2013
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 326-331
    • Li, J.1    Richter, K.2    Reinstein, J.3    Buchner, J.4
  • 88
    • 84896405318 scopus 로고    scopus 로고
    • Modulation of the hsp90 chaperone cycle by a stringent client protein
    • Lorenz, O. R., et al. Modulation of the hsp90 chaperone cycle by a stringent client protein. Mol. Cell 53, 941-953 (2014
    • (2014) Mol. Cell , vol.53 , pp. 941-953
    • Lorenz, O.R.1
  • 89
    • 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
  • 90
    • 4444291743 scopus 로고    scopus 로고
    • The co chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • Richter, K., Walter, S., & Buchner, J. The co chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 342, 1403-1413 (2004
    • (2004) J. Mol. Biol , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3
  • 91
    • 0028027504 scopus 로고
    • A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23
    • Johnson, J. L., & Toft, D. O. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J. Biol. Chem. 269, 24989-24993 (1994
    • (1994) J. Biol. Chem , vol.269 , pp. 24989-24993
    • Johnson, J.L.1    Toft, D.O.2
  • 92
    • 0034725641 scopus 로고    scopus 로고
    • Crystal structure, and activity of human p23, a heat shock protein 90 co chaperone
    • Weaver, A. J., Sullivan, W. P., Felts, S. J., Owen, B. A., & Toft, D. O. Crystal structure, and activity of human p23, a heat shock protein 90 co chaperone. J. Biol. Chem. 275, 23045-23052 (2000
    • (2000) J. Biol. Chem , vol.275 , pp. 23045-23052
    • Weaver, A.J.1    Sullivan, W.P.2    Felts, S.J.3    Owen, B.A.4    Toft, D.O.5
  • 93
    • 0032760261 scopus 로고    scopus 로고
    • An unstructured C terminal region of the Hsp90 co chaperone p23 is important for its chaperone function
    • Weikl, T., Abelmann, K., & Buchner, J. An unstructured C terminal region of the Hsp90 co chaperone p23 is important for its chaperone function. J. Mol. Biol. 293, 685-691 (1999
    • (1999) J. Mol. Biol , vol.293 , pp. 685-691
    • Weikl, T.1    Abelmann, K.2    Buchner, J.3
  • 94
    • 84869086668 scopus 로고    scopus 로고
    • The p23 molecular chaperone, and GCN5 acetylase jointly modulate protein-DNA dynamics, and open chromatin status
    • Zelin, E., Zhang, Y., Toogun, O. A., Zhong, S., & Freeman, B. C. The p23 molecular chaperone, and GCN5 acetylase jointly modulate protein-DNA dynamics, and open chromatin status. Mol. Cell 48, 459-470 (2012
    • (2012) Mol. Cell , vol.48 , pp. 459-470
    • Zelin, E.1    Zhang, Y.2    Toogun, O.A.3    Zhong, S.4    Freeman, B.C.5
  • 95
    • 79960452274 scopus 로고    scopus 로고
    • Global functional map of the p23 molecular chaperone reveals an extensive cellular network
    • Echtenkamp, F. J., et al. Global functional map of the p23 molecular chaperone reveals an extensive cellular network. Mol. Cell 43, 229-241 (2011
    • (2011) Mol. Cell , vol.43 , pp. 229-241
    • Echtenkamp, F.J.1
  • 96
    • 85003691529 scopus 로고    scopus 로고
    • Hsp90, and p23 molecular chaperones control chromatin architecture by maintaining the functional pool of the RSC chromatin remodeler
    • Echtenkamp, F. J., et al. Hsp90, and p23 molecular chaperones control chromatin architecture by maintaining the functional pool of the RSC chromatin remodeler. Mol. Cell 64, 888-899 (2016
    • (2016) Mol. Cell , vol.64 , pp. 888-899
    • Echtenkamp, F.J.1
  • 97
    • 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., Skowyra, D., Elledge, S. J., Harper, J. W., & Hieter, P. SGT1 encodes an essential component of the yeast kinetochore assembly pathway, and a novel subunit of the SCF ubiquitin ligase complex. Mol. Cell 4, 21-33 (1999
    • (1999) Mol. Cell , vol.4 , pp. 21-33
    • Kitagawa, K.1    Skowyra, D.2    Elledge, S.J.3    Harper, J.W.4    Hieter, P.5
  • 98
    • 33845959149 scopus 로고    scopus 로고
    • Sgt1p is a unique co chaperone that acts as a client adaptor to link Hsp90 to Skp1p
    • 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
    • (2006) J. Biol. Chem , vol.281 , pp. 33739-33748
    • Catlett, M.G.1    Kaplan, K.B.2
  • 99
    • 34247265509 scopus 로고    scopus 로고
    • A crucial function of SGT1, and HSP90 in inflammasome activity links mammalian, and plant innate immune responses
    • Mayor, A., Martinon, F., De Smedt, T., Petrilli, V., & Tschopp, J. A crucial function of SGT1, and HSP90 in inflammasome activity links mammalian, and plant innate immune responses. Nat. Immunol. 8, 497-503 (2007
    • (2007) Nat. Immunol , vol.8 , pp. 497-503
    • Mayor, A.1    Martinon, F.2    De Smedt, T.3    Petrilli, V.4    Tschopp, J.5
  • 100
    • 54349122449 scopus 로고    scopus 로고
    • Structural, and functional coupling of Hsp90-and Sgt1 centred multi-protein complexes
    • Zhang, M., et al. Structural, and functional coupling of Hsp90-and Sgt1 centred multi-protein complexes. EMBO J. 27, 2789-2798 (2008
    • (2008) EMBO J. , vol.27 , pp. 2789-2798
    • Zhang, M.1
  • 101
    • 0031756340 scopus 로고    scopus 로고
    • CNS1 encodes an essential p60/Sti1 homolog in saccharomyces cerevisiae that suppresses cyclophilin 40 mutations, and interacts with Hsp90
    • Dolinski, K. J., Cardenas, M. E., & Heitman, J. CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations, and interacts with Hsp90. Mol. Cell. Biol. 18, 7344-7352 (1998
    • (1998) Mol. Cell. Biol , vol.18 , pp. 7344-7352
    • Dolinski, K.J.1    Cardenas, M.E.2    Heitman, J.3
  • 102
    • 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 cpr7Delta 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 cpr7Delta cells. Mol. Cell. Biol. 18, 7353-7359 (1998
    • (1998) Mol. Cell. Biol , vol.18 , pp. 7353-7359
    • Marsh, J.A.1    Kalton, H.M.2    Gaber, R.F.3
  • 103
    • 0042357461 scopus 로고    scopus 로고
    • Functional interactions between Hsp90, and the co chaperones Cns1, and Cpr7 in saccharomyces cerevisiae
    • 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
    • (2003) J. Biol. Chem , vol.278 , pp. 32692-32701
    • Tesic, M.1    Marsh, J.A.2    Cullinan, S.B.3    Gaber, R.F.4
  • 104
    • 2542453964 scopus 로고    scopus 로고
    • Cns1 is an activator of the Ssa1 ATPase activity
    • Hainzl, O., Wegele, H., Richter, K., & Buchner, J. Cns1 is an activator of the Ssa1 ATPase activity. J. Biol. Chem. 279, 23267-23273 (2004
    • (2004) J. Biol. Chem , vol.279 , pp. 23267-23273
    • Hainzl, O.1    Wegele, H.2    Richter, K.3    Buchner, J.4
  • 105
    • 39049143941 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
    • Zhao, R., et al. Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180, 563-578 (2008
    • (2008) J. Cell Biol , vol.180 , pp. 563-578
    • Zhao, R.1
  • 106
    • 38649104452 scopus 로고    scopus 로고
    • Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos
    • Du, S. J., Li, H., Bian, Y., & Zhong, Y. Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos. Proc. Natl Acad. Sci. USA 105, 554-559 (2008
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 554-559
    • Du, S.J.1    Li, H.2    Bian, Y.3    Zhong, Y.4
  • 107
    • 84963815649 scopus 로고    scopus 로고
    • Remodeled Hsp90 molecular chaperone ensemble with the novel cochaperone Aarsd1 is required for muscle differentiation
    • Echeverria, P. C., Briand, P. A., & Picard, D. A. Remodeled Hsp90 molecular chaperone ensemble with the novel cochaperone Aarsd1 is required for muscle differentiation. Mol. Cell. Biol. 36, 1310-1321 (2016
    • (2016) Mol. Cell. Biol , vol.36 , pp. 1310-1321
    • Echeverria, P.C.1    Briand, P.A.2    Picard, D.A.3
  • 108
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 14, 422-434 (2000
    • (2000) Genes Dev , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 109
    • 84857475033 scopus 로고    scopus 로고
    • Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone
    • Liu, B., et al. Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Nat. Commun. 1, 79 (2010
    • (2010) Nat. Commun , vol.1 , pp. 79
    • Liu, B.1
  • 110
    • 70350130802 scopus 로고    scopus 로고
    • Efficient IgM assembly, and secretion require the plasma cell induced endoplasmic reticulum protein pERp1
    • van Anken, E., et al. Efficient IgM assembly, and secretion require the plasma cell induced endoplasmic reticulum protein pERp1. Proc. Natl Acad. Sci. USA 106, 17019-17024 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17019-17024
    • Van Anken, E.1
  • 111
    • 84901767455 scopus 로고    scopus 로고
    • MZB1 is a GRP94 cochaperone that enables proper immunoglobulin heavy chain biosynthesis upon ER stress
    • Rosenbaum, M., et al. MZB1 is a GRP94 cochaperone that enables proper immunoglobulin heavy chain biosynthesis upon ER stress. Genes Dev. 28, 1165-1178 (2014
    • (2014) Genes Dev , vol.28 , pp. 1165-1178
    • Rosenbaum, M.1
  • 112
    • 70350129433 scopus 로고    scopus 로고
    • PERp1 is significantly up regulated during plasma cell differentiation, and contributes to the oxidative folding of immunoglobulin
    • Shimizu, Y., Meunier, L., & Hendershot, L. M. pERp1 is significantly up regulated during plasma cell differentiation, and contributes to the oxidative folding of immunoglobulin. Proc. Natl Acad. Sci. USA 106, 17013-17018 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17013-17018
    • Shimizu, Y.1    Meunier, L.2    Hendershot, L.M.3
  • 113
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90, and hsp70
    • Chen, S., Prapapanich, V., Rimerman, R. A., Honore, B., & Smith, D. F. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90, and hsp70. Mol. Endocrinol. 10, 682-693 (1996
    • (1996) Mol. Endocrinol , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honore, B.4    Smith, D.F.5
  • 115
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of HSP90 client interactions reveals principles of substrate recognition
    • Taipale, M., et al. Quantitative analysis of HSP90 client interactions reveals principles of substrate recognition. Cell 150, 987-1001 (2012
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1
  • 116
    • 84904547311 scopus 로고    scopus 로고
    • A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways
    • Taipale, M., et al. A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158, 434-448 (2014
    • (2014) Cell , vol.158 , pp. 434-448
    • Taipale, M.1
  • 117
    • 84892857095 scopus 로고    scopus 로고
    • Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two step ATP hydrolysis mechanism
    • Lavery, L. A., et al. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two step ATP hydrolysis mechanism. Mol. Cell 53, 330-343 (2014
    • (2014) Mol. Cell , vol.53 , pp. 330-343
    • Lavery, L.A.1
  • 118
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S., et al. Global analysis of protein expression in yeast. Nature 425, 737-741 (2003
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 119
    • 79551666466 scopus 로고    scopus 로고
    • N Terminal domain of human Hsp90 triggers binding to the cochaperone p23
    • Karagoz, G. E., et al. N Terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc. Natl Acad. Sci. USA 108, 580-585 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 580-585
    • Karagoz, G.E.1
  • 120
    • 79959344309 scopus 로고    scopus 로고
    • Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo em structure of the human Hsp90: Hop complex
    • Southworth, D. R., & Agard, D. A. Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo EM structure of the human Hsp90: Hop complex. Mol. Cell 42, 771-781 (2011
    • (2011) Mol. Cell , vol.42 , pp. 771-781
    • Southworth, D.R.1    Agard, D.A.2
  • 121
    • 84892847945 scopus 로고    scopus 로고
    • Asymmetric Hsp90 N domain SUMOylation recruits Aha1, and ATP-competitive inhibitors
    • Mollapour, M., et al. Asymmetric Hsp90 N domain SUMOylation recruits Aha1, and ATP-competitive inhibitors. Mol. Cell 53, 317-329 (2014
    • (2014) Mol. Cell , vol.53 , pp. 317-329
    • Mollapour, M.1
  • 122
    • 80053976720 scopus 로고    scopus 로고
    • An interaction network predicted from public data as a discovery tool: Application to the Hsp90 molecular chaperone machine
    • Echeverria, 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 , pp. e26044
    • Echeverria, P.C.1    Bernthaler, A.2    Dupuis, P.3    Mayer, B.4    Picard, D.5
  • 123
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • Picard, D. Chaperoning steroid hormone action. Trends Endocrinol. Metab. 17, 229-235 (2006
    • (2006) Trends Endocrinol. Metab , vol.17 , pp. 229-235
    • Picard, D.1
  • 124
    • 0027291238 scopus 로고
    • Heat-shock protein hsp90 governs the activity of pp60v src kinase
    • Xu, Y., & Lindquist, S. Heat-shock protein hsp90 governs the activity of pp60v src kinase. Proc. Natl Acad. Sci. USA 90, 7074-7078 (1993
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 125
    • 0025175208 scopus 로고
    • Reduced levels of hsp90 compromise steroid receptor action in vivo
    • Picard, D., et al. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348, 166-168 (1990
    • (1990) Nature , vol.348 , pp. 166-168
    • Picard, D.1
  • 126
    • 84987900173 scopus 로고    scopus 로고
    • Regulation of ubiquitin-like with plant homeodomain, and RING finger domain 1 (UHRF1) protein stability by heat shock protein 90 chaperone machinery
    • Ding, G., et al. Regulation of ubiquitin-like with plant homeodomain, and RING finger domain 1 (UHRF1) protein stability by heat shock protein 90 chaperone machinery. J. Biol. Chem. 291, 20125-20135 (2016
    • (2016) J. Biol. Chem , vol.291 , pp. 20125-20135
    • Ding, G.1
  • 127
    • 0035146685 scopus 로고    scopus 로고
    • The co chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell, P., et al. The co chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3, 93-96 (2001
    • (2001) Nat. Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1
  • 128
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W., et al. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl Acad. Sci. USA 99, 12847-12852 (2002
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12847-12852
    • Xu, W.1
  • 129
    • 73249143709 scopus 로고    scopus 로고
    • Identification of residues on Hsp70, and Hsp90 ubiquitinated by the cochaperone CHIP
    • Kundrat, L., & Regan, L. Identification of residues on Hsp70, and Hsp90 ubiquitinated by the cochaperone CHIP. J. Mol. Biol. 395, 587-594 (2010
    • (2010) J. Mol. Biol , vol.395 , pp. 587-594
    • Kundrat, L.1    Regan, L.2
  • 130
    • 73949114912 scopus 로고    scopus 로고
    • Regulation of Hsp90 client proteins by a Cullin5 RING E3 ubiquitin ligase
    • Ehrlich, E. S., et al. Regulation of Hsp90 client proteins by a Cullin5 RING E3 ubiquitin ligase. Proc. Natl Acad. Sci. USA 106, 20330-20335 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20330-20335
    • Ehrlich, E.S.1
  • 131
    • 84935009324 scopus 로고    scopus 로고
    • Conformational processing of oncogenic v Src kinase by the molecular chaperone Hsp90
    • Boczek, E. E., et al. Conformational processing of oncogenic v Src kinase by the molecular chaperone Hsp90. Proc. Natl Acad. Sci. USA 112, E3189-E3198 (2015
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E3189-E3198
    • Boczek, E.E.1
  • 132
    • 0031871101 scopus 로고    scopus 로고
    • Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly
    • Pratt, W. B., & Dittmar, K. D. Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly. Trends Endocrinol. Metab. 9, 244-252 (1998
    • (1998) Trends Endocrinol. Metab , vol.9 , pp. 244-252
    • Pratt, W.B.1    Dittmar, K.D.2
  • 133
    • 84903149823 scopus 로고    scopus 로고
    • Glucocorticoid receptor function regulated by coordinated action of the Hsp90, and Hsp70 chaperone cycles
    • Kirschke, E., Goswami, D., Southworth, D., Griffin, P. R., & Agard, D. A. Glucocorticoid receptor function regulated by coordinated action of the Hsp90, and Hsp70 chaperone cycles. Cell 157, 1685-1697 (2014
    • (2014) Cell , vol.157 , pp. 1685-1697
    • Kirschke, E.1    Goswami, D.2    Southworth, D.3    Griffin, P.R.4    Agard, D.A.5
  • 134
    • 84864720613 scopus 로고    scopus 로고
    • Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO active enzyme
    • Ghosh, A., & Stuehr, D. J. Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO active enzyme. Proc. Natl Acad. Sci. USA 109, 12998-13003 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 12998-13003
    • Ghosh, A.1    Stuehr, D.J.2
  • 135
    • 84930643471 scopus 로고    scopus 로고
    • Defining fundamental steps in the assembly of the Drosophila RNAi enzyme complex
    • Iwasaki, S., et al. Defining fundamental steps in the assembly of the Drosophila RNAi enzyme complex. Nature 521, 533-536 (2015
    • (2015) Nature , vol.521 , pp. 533-536
    • Iwasaki, S.1
  • 136
    • 37549046440 scopus 로고    scopus 로고
    • The hsp90 molecular chaperone modulates multiple telomerase activities
    • Toogun, O. A., Dezwaan, D. C., & Freeman, B. C. The hsp90 molecular chaperone modulates multiple telomerase activities. Mol. Cell. Biol. 28, 457-467 (2008
    • (2008) Mol. Cell. Biol , vol.28 , pp. 457-467
    • Toogun, O.A.1    Dezwaan, D.C.2    Freeman, B.C.3
  • 137
    • 67650337568 scopus 로고    scopus 로고
    • The Hsp82 molecular chaperone promotes a switch between unextendable, and extendable telomere states
    • DeZwaan, D. C., Toogun, O. A., Echtenkamp, F. J., & Freeman, B. C. The Hsp82 molecular chaperone promotes a switch between unextendable, and extendable telomere states. Nat. Struct. Mol. Biol. 16, 711-716 (2009
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 711-716
    • De Zwaan, D.C.1    Toogun, O.A.2    Echtenkamp, F.J.3    Freeman, B.C.4
  • 138
    • 84963818046 scopus 로고    scopus 로고
    • Molecular mechanism of protein kinase recognition, and sorting by the Hsp90 kinome-specific cochaperone Cdc37
    • Keramisanou, D., et al. Molecular mechanism of protein kinase recognition, and sorting by the Hsp90 kinome-specific cochaperone Cdc37. Mol. Cell 62, 260-271 (2016
    • (2016) Mol. Cell , vol.62 , pp. 260-271
    • Keramisanou, D.1
  • 140
    • 0027359404 scopus 로고
    • Isolation of Hsp90 mutants by screening for decreased steroid receptor function
    • Bohen, S. P., & Yamamoto, K. R. Isolation of Hsp90 mutants by screening for decreased steroid receptor function. Proc. Natl Acad. Sci. USA 90, 11424-11428 (1993
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11424-11428
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 141
    • 84873420281 scopus 로고    scopus 로고
    • Uncovering a region of heat shock protein 90 important for client binding in e coli, and chaperone function in yeast
    • Genest, O., et al. Uncovering a region of heat shock protein 90 important for client binding in E. coli, and chaperone function in yeast. Mol. Cell 49, 464-473 (2013
    • (2013) Mol. Cell , vol.49 , pp. 464-473
    • Genest, O.1
  • 142
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor, and a protein kinase
    • Nathan, D. F., & Lindquist, S. Mutational analysis of Hsp90 function: interactions with a steroid receptor, and a protein kinase. Mol. Cell. Biol. 15, 3917-3925 (1995
    • (1995) Mol. Cell. Biol , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 143
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny, M. V., Toretsky, J., Bohen, S., & Neckers, L. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc. Natl Acad. Sci. USA 93, 8379-8383 (1996
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 144
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehrnia, B., Paz, I. B., Dasgupta, G., & Momand, J. Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J. Biol. Chem. 271, 15084-15090 (1996
    • (1996) J. Biol. Chem , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 145
    • 0033613434 scopus 로고    scopus 로고
    • The stabilization mechanism of mutant-type p53 by impaired ubiquitination: The loss of wild-type p53 function, and the hsp90 association
    • Nagata, Y., et al. The stabilization mechanism of mutant-type p53 by impaired ubiquitination: the loss of wild-type p53 function, and the hsp90 association. Oncogene 18, 6037-6049 (1999
    • (1999) Oncogene , vol.18 , pp. 6037-6049
    • Nagata, Y.1
  • 146
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by Geldanamycin, an hsp90 binding agent
    • Whitesell, L., Sutphin, P. D., Pulcini, E. J., Martinez, J. D., & Cook, P. H. The physical association of multiple molecular chaperone proteins with mutant p53 is altered by Geldanamycin, an hsp90 binding agent. Mol. Cell. Biol. 18, 1517-1524 (1998
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinez, J.D.4    Cook, P.H.5
  • 147
    • 10344243547 scopus 로고    scopus 로고
    • Hsp90 regulates the activity of wild type p53 under physiological, and elevated temperatures
    • Muller, L., Schaupp, A., Walerych, D., Wegele, H., & Buchner, J. Hsp90 regulates the activity of wild type p53 under physiological, and elevated temperatures. J. Biol. Chem. 279, 48846-48854 (2004
    • (2004) J. Biol. Chem , vol.279 , pp. 48846-48854
    • Muller, L.1    Schaupp, A.2    Walerych, D.3    Wegele, H.4    Buchner, J.5
  • 148
    • 0037449734 scopus 로고    scopus 로고
    • Phosphorylation and hsp90 binding mediate heat shock stabilization of p53
    • Wang, C. G., & Chen, J. D. Phosphorylation, and hsp90 binding mediate heat shock stabilization of p53. J. Biol. Chem. 278, 2066-2071 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 2066-2071
    • Wang, C.G.1    Chen, J.D.2
  • 149
    • 10344239940 scopus 로고    scopus 로고
    • Hsp90 chaperones wild-type p53 tumor suppressor protein
    • Walerych, D., et al. Hsp90 chaperones wild-type p53 tumor suppressor protein. J. Biol. Chem. 279, 48836-48845 (2004
    • (2004) J. Biol. Chem , vol.279 , pp. 48836-48845
    • Walerych, D.1
  • 150
    • 80455155014 scopus 로고    scopus 로고
    • Structural analysis of the interaction between Hsp90, and the tumor suppressor protein p53
    • Hagn, F., et al. Structural analysis of the interaction between Hsp90, and the tumor suppressor protein p53. Nat. Struct. Mol. Biol. 18, 1086-1093 (2011
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1086-1093
    • Hagn, F.1
  • 151
    • 79955642720 scopus 로고    scopus 로고
    • The client protein p53 adopts a molten globule-like state in the presence of Hsp90
    • Park, S. J., Borin, B. N., Martinez-Yamout, M. A., & Dyson, H. J. The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat. Struct. Mol. Biol. 18, 537-541 (2011
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 537-541
    • Park, S.J.1    Borin, B.N.2    Martinez-Yamout, M.A.3    Dyson, H.J.4
  • 152
    • 79960698348 scopus 로고    scopus 로고
    • Dynamic interaction of Hsp90 with its client protein p53
    • Park, S. J., Kostic, M., & Dyson, H. J. Dynamic interaction of Hsp90 with its client protein p53. J. Mol. Biol. 411, 158-173 (2011
    • (2011) J. Mol. Biol , vol.411 , pp. 158-173
    • Park, S.J.1    Kostic, M.2    Dyson, H.J.3
  • 153
    • 0037143625 scopus 로고    scopus 로고
    • CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90
    • Rudiger, S., Freund, S. M. V., Veprintsev, D. B., & Fersht, A. R. CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. Proc. Natl Acad. Sci. USA 99, 11085-11090 (2002
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11085-11090
    • Rudiger, S.1    Freund, S.M.V.2    Veprintsev, D.B.3    Fersht, A.R.4
  • 154
    • 84896837095 scopus 로고    scopus 로고
    • Hsp90 Tau complex reveals molecular basis for specificity in chaperone action
    • Karagoz, G. E., et al. Hsp90 Tau complex reveals molecular basis for specificity in chaperone action. Cell 156, 963-974 (2014
    • (2014) Cell , vol.156 , pp. 963-974
    • Karagoz, G.E.1
  • 155
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: An ensemble of conformations trapped in a locally encoded topological space
    • Shortle, D. The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space. Adv. Protein Chem. 62, 1-23 (2002
    • (2002) Adv. Protein Chem , vol.62 , pp. 1-23
    • Shortle, D.1
  • 156
    • 79953308070 scopus 로고    scopus 로고
    • Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone
    • Street, T. O., Lavery, L. A., & Agard, D. A. Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol. Cell 42, 96-105 (2011
    • (2011) Mol. Cell , vol.42 , pp. 96-105
    • Street, T.O.1    Lavery, L.A.2    Agard, D.A.3
  • 157
    • 77951610740 scopus 로고    scopus 로고
    • HtpG the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium synechococcus elongatus PCC 7942
    • Sato, T., Minagawa, S., Kojima, E., Okamoto, N., & Nakamoto, H. HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942. Mol. Microbiol. 76, 576-589 (2010
    • (2010) Mol. Microbiol , vol.76 , pp. 576-589
    • Sato, T.1    Minagawa, S.2    Kojima, E.3    Okamoto, N.4    Nakamoto, H.5
  • 158
    • 84879098944 scopus 로고    scopus 로고
    • ATP-competitive inhibitors block protein kinase recruitment to the Hsp90 Cdc37 system
    • Polier, S., et al. ATP-competitive inhibitors block protein kinase recruitment to the Hsp90 Cdc37 system. Nat. Chem. Biol. 9, 307-312 (2013
    • (2013) Nat. Chem. Biol , vol.9 , pp. 307-312
    • Polier, S.1
  • 159
    • 84988983027 scopus 로고    scopus 로고
    • Nucleotide-free sB raf is preferentially bound by Hsp90, and Cdc37 in vitro
    • Eckl, J. M., Daake, M., Schwartz, S., & Richter, K. Nucleotide-free sB raf is preferentially bound by Hsp90, and Cdc37 in vitro. J. Mol. Biol. 428, 4185-4196 (2016
    • (2016) J. Mol. Biol , vol.428 , pp. 4185-4196
    • Eckl, J.M.1    Daake, M.2    Schwartz, S.3    Richter, K.4
  • 160
    • 0033524442 scopus 로고    scopus 로고
    • Maturation of the tyrosine kinase c src as a kinase, and as a substrate depends on the molecular chaperone Hsp90
    • Xu, Y., Singer, M. A., & Lindquist, S. Maturation of the tyrosine kinase c src as a kinase, and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl Acad. Sci. USA 96, 109-114 (1999
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 109-114
    • Xu, Y.1    Singer, M.A.2    Lindquist, S.3
  • 161
    • 84995902636 scopus 로고    scopus 로고
    • Bipartite role of heat shock protein 90 (Hsp90) keeps CRAF kinase poised for activation
    • Mitra, S., Ghosh, B., Gayen, N., Roy, J., & Mandal, A. K. Bipartite role of heat shock protein 90 (Hsp90) keeps CRAF kinase poised for activation. J. Biol. Chem. 291, 24579-24593 (2016
    • (2016) J. Biol. Chem , vol.291 , pp. 24579-24593
    • Mitra, S.1    Ghosh, B.2    Gayen, N.3    Roy, J.4    Mandal, A.K.5
  • 163
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman, B. C., & Yamamoto, K. R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296, 2232-2235 (2002
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 164
    • 84982924098 scopus 로고    scopus 로고
    • Structural, and functional basis of protein phosphatase 5 substrate specificity
    • Oberoi, J., et al. Structural, and functional basis of protein phosphatase 5 substrate specificity. Proc. Natl Acad. Sci. USA 113, 9009-9014 (2016
    • (2016) Proc. Natl Acad. Sci. USA , vol.113 , pp. 9009-9014
    • Oberoi, J.1
  • 165
    • 84951161372 scopus 로고    scopus 로고
    • Unusual suspects in the twilight zone between the Hsp90 interactome, and carcinogenesis
    • Vartholomaiou, E., Echeverria, P. C., & Picard, D. Unusual suspects in the twilight zone between the Hsp90 interactome, and carcinogenesis. Adv. Cancer Res. 129, 1-30 (2016
    • (2016) Adv. Cancer Res , vol.129 , pp. 1-30
    • Vartholomaiou, E.1    Echeverria, P.C.2    Picard, D.3
  • 166
    • 34248195608 scopus 로고    scopus 로고
    • High HSP90 expression is associated with decreased survival in breast cancer
    • Pick, E., et al. High HSP90 expression is associated with decreased survival in breast cancer. Cancer Res. 67, 2932-2937 (2007
    • (2007) Cancer Res , vol.67 , pp. 2932-2937
    • Pick, E.1
  • 167
    • 0033194732 scopus 로고    scopus 로고
    • Disruption of functions of wild-type p53 by hetero-oligomerization
    • Deb, D., Chakraborti, A. S., Lanyi, A., Troyer, D. A., & Deb, S. Disruption of functions of wild-type p53 by hetero-oligomerization. Int. J. Oncol. 15, 413-422 (1999
    • (1999) Int. J. Oncol , vol.15 , pp. 413-422
    • Deb, D.1    Chakraborti, A.S.2    Lanyi, A.3    Troyer, D.A.4    Deb, S.5
  • 168
    • 84937604711 scopus 로고    scopus 로고
    • Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatment
    • Alexandrova, E. M., et al. Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatment. Nature 523, 352-356 (2015
    • (2015) Nature , vol.523 , pp. 352-356
    • Alexandrova, E.M.1
  • 169
    • 33845302853 scopus 로고    scopus 로고
    • Tumor selectivity of Hsp90 inhibitors: The explanation remains elusive
    • Chiosis, G., & Neckers, L. Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive. ACS Chem. Biol. 1, 279-284 (2006
    • (2006) ACS Chem. Biol , vol.1 , pp. 279-284
    • Chiosis, G.1    Neckers, L.2
  • 170
    • 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 425, 407-410 (2003
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 171
    • 84992436568 scopus 로고    scopus 로고
    • The epichaperome is an integrated chaperome network that facilitates tumour survival
    • Rodina, A., et al. The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature 538, 397-401 (2016
    • (2016) Nature , vol.538 , pp. 397-401
    • Rodina, A.1
  • 172
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90 CHIP complex recognizes, and selectively degrades phosphorylated tau client proteins
    • Dickey, C. A., et al. The high-affinity HSP90 CHIP complex recognizes, and selectively degrades phosphorylated tau client proteins. J. Clin. Invest. 117, 648-658 (2007
    • (2007) J. Clin. Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1
  • 173
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70, and 90 inhibit early stages of amyloid beta 1-42) aggregation in vitro
    • Evans, C. G., Wisen, S., & Gestwicki, J. E. Heat shock proteins 70, and 90 inhibit early stages of amyloid beta (1-42) aggregation in vitro. J. Biol. Chem. 281, 33182-33191 (2006
    • (2006) J. Biol. Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 174
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70, and prevents alpha-synuclein aggregation, and toxicity in vitro
    • McLean, P. J., Klucken, J., Shin, Y., & Hyman, B. T. Geldanamycin induces Hsp70, and prevents alpha-synuclein aggregation, and toxicity in vitro. Biochem. Biophys. Res. Commun. 321, 665-669 (2004
    • (2004) Biochem. Biophys. Res. Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 176
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang, X., et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127, 803-815 (2006
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1
  • 177
    • 84857049091 scopus 로고    scopus 로고
    • Broad action of Hsp90 as a host chaperone required for viral replication
    • Geller, R., Taguwa, S., & Frydman, J. Broad action of Hsp90 as a host chaperone required for viral replication. Biochim. Biophys. Acta 1823, 698-706 (2012
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 698-706
    • Geller, R.1    Taguwa, S.2    Frydman, J.3
  • 179
    • 84874543845 scopus 로고    scopus 로고
    • Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus
    • Geller, R., Andino, R., & Frydman, J. Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus. PLoS ONE 8, e56762 (2013
    • (2013) Plos One , vol.8 , pp. e56762
    • Geller, R.1    Andino, R.2    Frydman, J.3
  • 180
    • 84930872782 scopus 로고    scopus 로고
    • Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest
    • Hombach, A., Ommen, G., Sattler, V., & Clos, J. Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest. Cell Stress Chaperones 20, 673-685 (2015
    • (2015) Cell Stress Chaperones , vol.20 , pp. 673-685
    • Hombach, A.1    Ommen, G.2    Sattler, V.3    Clos, J.4
  • 181
    • 0035203992 scopus 로고    scopus 로고
    • Heat shock protein 90 homeostasis controls stage differentiation in leishmania donovani
    • Wiesgigl, M., & Clos, J. Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani. Mol. Biol. Cell 12, 3307-3316 (2001
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3307-3316
    • Wiesgigl, M.1    Clos, J.2
  • 182
    • 85012870279 scopus 로고    scopus 로고
    • HSP90 shapes the consequences of human genetic variation
    • Karras. G.I., et al. HSP90 shapes the consequences of human genetic variation. Cell 168, 856-866 (2017)
    • (2017) Cell , vol.168 , pp. 856-866
    • Karras, G.I.1
  • 183
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90 pp60v src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. Inhibition of heat shock protein HSP90 pp60v src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl Acad. Sci. USA 91, 8324-8328 (1994
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 184
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol, and geldanamycin
    • Roe, S. M., et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol, and geldanamycin. J. Med. Chem. 42, 260-266 (1999
    • (1999) J. Med. Chem , vol.42 , pp. 260-266
    • Roe, S.M.1
  • 185
    • 0029813620 scopus 로고    scopus 로고
    • Destabilization of Raf 1 by geldanamycin leads to disruption of the Raf 1 MEK-mitogen-activated protein kinase signalling pathway
    • Schulte, T. W., et al. Destabilization of Raf 1 by geldanamycin leads to disruption of the Raf 1 MEK-mitogen-activated protein kinase signalling pathway. Mol. Cell. Biol. 16, 5839-5845 (1996
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5839-5845
    • Schulte, T.W.1
  • 187
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma, S. V., Agatsuma, T., & Nakano, H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 16, 2639-2645 (1998
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 188
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells, and induce the degradation of Her2 tyrosine kinase
    • Chiosis, G., Lucas, B., Shtil, A., Huezo, H., & Rosen, N. Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells, and induce the degradation of Her2 tyrosine kinase. Bioorg. Med. Chem. 10, 3555-3564 (2002
    • (2002) Bioorg. Med. Chem , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Lucas, B.2    Shtil, A.3    Huezo, H.4    Rosen, N.5
  • 189
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu, M. G., Chadli, A., Bouhouche, I., Catelli, M., & Neckers, L. M. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275, 37181-37186 (2000
    • (2000) J. Biol. Chem , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 190
    • 25844519550 scopus 로고    scopus 로고
    • HSP90, and the chaperoning of cancer
    • Whitesell, L., & Lindquist, S. L. HSP90, and the chaperoning of cancer. Nat. Rev. Cancer 5, 761-772 (2005
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 191
    • 84957927619 scopus 로고    scopus 로고
    • Anticancer inhibitors of Hsp90 function: Beyond the usual suspects
    • Garg, G., Khandelwal, A., & Blagg, B. S. Anticancer inhibitors of Hsp90 function: beyond the usual suspects. Adv. Cancer Res. 129, 51-88 (2016
    • (2016) Adv. Cancer Res , vol.129 , pp. 51-88
    • Garg, G.1    Khandelwal, A.2    Blagg, B.S.3
  • 193
    • 66249138886 scopus 로고    scopus 로고
    • Hsp90 inhibitor PU H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models
    • Caldas-Lopes, E., et al. Hsp90 inhibitor PU H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models. Proc. Natl Acad. Sci. USA 106, 8368-8373 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8368-8373
    • Caldas-Lopes, E.1
  • 194
    • 84958183525 scopus 로고    scopus 로고
    • HSP90 inhibitor-SN 38 conjugate strategy for targeted delivery of topoisomerase i inhibitor to tumors
    • Proia, D. A., et al. HSP90 inhibitor-SN 38 conjugate strategy for targeted delivery of topoisomerase I inhibitor to tumors. Mol. Cancer Ther. 14, 2422-2432 (2015
    • (2015) Mol. Cancer Ther , vol.14 , pp. 2422-2432
    • Proia, D.A.1
  • 195
    • 84994076451 scopus 로고    scopus 로고
    • STA 8666, a novel HSP90 inhibitor/SN 38 drug conjugate, causes complete tumor regression in preclinical mouse models of pediatric sarcoma
    • Heske, C. M., et al. STA 8666, a novel HSP90 inhibitor/SN 38 drug conjugate, causes complete tumor regression in preclinical mouse models of pediatric sarcoma. Oncotarget 7, 65540-65552 (2016
    • (2016) Oncotarget , vol.7 , pp. 65540-65552
    • Heske, C.M.1
  • 196
    • 51849155552 scopus 로고    scopus 로고
    • Targeting Hsp90 prevents escape of breast cancer cells from tyrosine kinase inhibition
    • Pashtan, I., Tsutsumi, S., Wang, S. Q., Xu, W. P., & Neckers, L. Targeting Hsp90 prevents escape of breast cancer cells from tyrosine kinase inhibition. Cell Cycle 7, 2936-2941 (2008
    • (2008) Cell Cycle , vol.7 , pp. 2936-2941
    • Pashtan, I.1    Tsutsumi, S.2    Wang, S.Q.3    Xu, W.P.4    Neckers, L.5
  • 197
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90 progesterone receptor binding, and the disactivation loop model for steroid receptor complexes
    • Smith, D. F. Dynamics of heat shock protein 90 progesterone receptor binding, and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7, 1418-1429 (1993
    • (1993) Mol. Endocrinol , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 198
    • 84878873702 scopus 로고    scopus 로고
    • Regulation of organismal proteostasis by transcellular chaperone signaling
    • van Oosten-Hawle, P., Porter, R. S., & Morimoto, R. I. Regulation of organismal proteostasis by transcellular chaperone signaling. Cell 153, 1366-1378 (2013
    • (2013) Cell , vol.153 , pp. 1366-1378
    • Van Oosten-Hawle, P.1    Porter, R.S.2    Morimoto, R.I.3
  • 199
    • 33845215386 scopus 로고    scopus 로고
    • The Hsp90 cochaperone p23 is essential for perinatal survival
    • Grad, I., et al. The Hsp90 cochaperone p23 is essential for perinatal survival. Mol. Cell. Biol. 26, 8976-8983 (2006
    • (2006) Mol. Cell. Biol , vol.26 , pp. 8976-8983
    • Grad, I.1
  • 200
    • 84875325305 scopus 로고    scopus 로고
    • Hsp90, an unlikely ally in the war on cancer
    • Barrott, J. J., & Haystead, T. A. Hsp90, an unlikely ally in the war on cancer. FEBS J. 280, 1381-1396 (2013
    • (2013) FEBS J. , vol.280 , pp. 1381-1396
    • Barrott, J.J.1    Haystead, T.A.2


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