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Volumn 7, Issue 9, 2012, Pages 1556-1564

Pharmacological tuning of heat shock protein 70 modulates polyglutamine toxicity and aggregation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CE 12; ETHYL 4 (2,4 DICHLOROPHENYL) 2,7,7 TRIMETHYL 5 OXO 1,4,5,6,7,8 HEXAHYDROQUINOLINE 3 CARBOXYLATE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 INHIBITOR; POLYGLUTAMINE; PROTEIN INHIBITOR; SW 02; UNCLASSIFIED DRUG;

EID: 84868142926     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300166p     Document Type: Article
Times cited : (31)

References (60)
  • 1
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • DOI 10.1001/archneurol.2007.56
    • Soto, C., and Estrada, L. D. (2008) Protein misfolding and neurodegeneration. Arch. Neurol. 65, 184-189. (Pubitemid 351240778)
    • (2008) Archives of Neurology , vol.65 , Issue.2 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 3
    • 70450192073 scopus 로고    scopus 로고
    • Transcriptional dysregulation of coding and non-coding genes in cellular models of Huntington's disease
    • Bithell, A., Johnson, R., and Buckley, N. J. (2009) Transcriptional dysregulation of coding and non-coding genes in cellular models of Huntington's disease. Biochem. Soc. Trans. 37, 1270-1275.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1270-1275
    • Bithell, A.1    Johnson, R.2    Buckley, N.J.3
  • 4
    • 35348980793 scopus 로고    scopus 로고
    • Nucleocytoplasmic trafficking and transcription effects of huntingtin in Huntington's disease
    • DOI 10.1016/j.pneurobio.2006.11.004, PII S0301008206001547, Chromatin Dysfunction in Huntington's Disease
    • Truant, R., Atwal, R. S., and Burtnik, A. (2007) Nucleocytoplasmic trafficking and transcription effects of huntingtin in Huntington's disease. Prog. Neurobiol. 83, 211-227. (Pubitemid 47595404)
    • (2007) Progress in Neurobiology , vol.83 , Issue.4 , pp. 211-227
    • Truant, R.1    Atwal, R.S.2    Burtnik, A.3
  • 5
    • 79955955066 scopus 로고    scopus 로고
    • Proteasomal dysfunction in aging and Huntington disease
    • Li, X. J., and Li, S. (2011) Proteasomal dysfunction in aging and Huntington disease. Neurobiol. Dis. 43, 4-8.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 4-8
    • Li, X.J.1    Li, S.2
  • 6
    • 77955844171 scopus 로고    scopus 로고
    • Chaperone networks: Tipping the balance in protein folding diseases
    • Voisine, C., Pedersen, J. S., and Morimoto, R. I. (2010) Chaperone networks: tipping the balance in protein folding diseases. Neurobiol. Dis 40, 12-20.
    • (2010) Neurobiol. Dis , vol.40 , pp. 12-20
    • Voisine, C.1    Pedersen, J.S.2    Morimoto, R.I.3
  • 7
    • 78650827764 scopus 로고    scopus 로고
    • Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease
    • Vidal, R., Caballero, B., Couve, A., and Hetz, C. (2011) Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease. Curr. Mol. Med 11, 1-12.
    • (2011) Curr. Mol. Med , vol.11 , pp. 1-12
    • Vidal, R.1    Caballero, B.2    Couve, A.3    Hetz, C.4
  • 8
    • 71849095133 scopus 로고    scopus 로고
    • Cause and consequence: Mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases
    • Gibson, G. E., Starkov, A., Blass, J. P., Ratan, R. R., and Beal, M. F. (2010) Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases. Biochim. Biophys. Acta 1802, 122-134.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 122-134
    • Gibson, G.E.1    Starkov, A.2    Blass, J.P.3    Ratan, R.R.4    Beal, M.F.5
  • 9
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch, W. E., Morimoto, R. I., Dillin, A., and Kelly, J. W. (2008) Adapting proteostasis for disease intervention. Science 319, 916-919. (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 10
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., and Balch, W. E. (2009) Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem. 78, 959-991.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4    Balch, W.E.5
  • 11
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 13
    • 77952851112 scopus 로고    scopus 로고
    • Chaperone-assisted degradation: Multiple paths to destruction
    • Kettern, N., Dreiseidler, M., Tawo, R., and Hohfeld, J. (2010) Chaperone-assisted degradation: multiple paths to destruction. Biol. Chem. 391, 481-489.
    • (2010) Biol. Chem. , vol.391 , pp. 481-489
    • Kettern, N.1    Dreiseidler, M.2    Tawo, R.3    Hohfeld, J.4
  • 14
    • 77950600645 scopus 로고    scopus 로고
    • Mechanisms of the Hsp70 chaperone system
    • Young, J. C. (2010) Mechanisms of the Hsp70 chaperone system. Biochem. Cell Biol. 88, 291-300.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 291-300
    • Young, J.C.1
  • 15
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H. H., Craig, E. A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity, Nat. Rev. Mol. Cell Biol. 11, 579-592.
    • Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 16
    • 77954377096 scopus 로고    scopus 로고
    • Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)
    • Chang, L., Thompson, A. D., Ung, P., Carlson, H. A., and Gestwicki, J. E. (2010) Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK). J. Biol. Chem. 285, 21282-21291.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21282-21291
    • Chang, L.1    Thompson, A.D.2    Ung, P.3    Carlson, H.A.4    Gestwicki, J.E.5
  • 19
    • 41649104650 scopus 로고    scopus 로고
    • Activation of heat shock and antioxidant responses by the natural product celastrol: Transcriptional signatures of a thiol-targeted molecule
    • DOI 10.1091/mbc.E07-10-1004
    • Trott, A., West, J. D., Klaic, L., Westerheide, S. D., Silverman, R. B., Morimoto, R. I., and Morano, K. A. (2008) Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thiol-targeted molecule. Mol. Biol. Cell 19, 1104-1112. (Pubitemid 351481823)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.3 , pp. 1104-1112
    • Trott, A.1    West, J.D.2    Klaic, L.3    Westerheide, S.D.4    Silverman, R.B.5    Morimoto, R.I.6    Morano, K.A.7
  • 20
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings, C. J., Sun, Y., Opal, P., Antalffy, B., Mestril, R., Orr, H. T., Dillmann, W. H., and Zoghbi, H. Y. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10, 1511-1518. (Pubitemid 32684893)
    • (2001) Human Molecular Genetics , vol.10 , Issue.14 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 22
    • 77953734857 scopus 로고    scopus 로고
    • Heat shock protein 70 (hsp70) as an emerging drug target
    • Evans, C. G., Chang, L., and Gestwicki, J. E. (2010) Heat shock protein 70 (hsp70) as an emerging drug target. J. Med. Chem. 53, 4585-4602.
    • (2010) J. Med. Chem. , vol.53 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 24
    • 78650143677 scopus 로고    scopus 로고
    • High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer
    • Miyata, Y., Chang, L., Bainor, A., McQuade, T. J., Walczak, C. P., Zhang, Y., Larsen, M. J., Kirchhoff, P., and Gestwicki, J. E. (2010) High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer. J Biomol Screen 15, 1211-1219.
    • (2010) J Biomol Screen , vol.15 , pp. 1211-1219
    • Miyata, Y.1    Chang, L.2    Bainor, A.3    McQuade, T.J.4    Walczak, C.P.5    Zhang, Y.6    Larsen, M.J.7    Kirchhoff, P.8    Gestwicki, J.E.9
  • 26
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • Wadhwa, R., Sugihara, T., Yoshida, A., Nomura, H., Reddel, R. R., Simpson, R., Maruta, H., and Kaul, S. C. (2000) Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res. 60, 6818-6821. (Pubitemid 32059144)
    • (2000) Cancer Research , vol.60 , Issue.24 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6    Maruta, H.7    Kaul, S.C.8
  • 27
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • Leu, J. I., Pimkina, J., Frank, A., Murphy, M. E., and George, D. L. (2009) A small molecule inhibitor of inducible heat shock protein 70. Mol. Cell 36, 15-27.
    • (2009) Mol. Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 28
    • 0035847010 scopus 로고    scopus 로고
    • Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis
    • DOI 10.1074/jbc.M008535200
    • Fewell, S. W., Day, B. W., and Brodsky, J. L. (2001) Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis. J. Biol. Chem. 276, 910-914. (Pubitemid 32096508)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 910-914
    • Fewell, S.W.1    Day, B.W.2    Brodsky I, J.L.3
  • 29
    • 79951837256 scopus 로고    scopus 로고
    • Chemical screens against a reconstituted multiprotein complex: Myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism
    • Chang, L., Miyata, Y., Ung, P. M., Bertelsen, E. B., McQuade, T. J., Carlson, H. A., Zuiderweg, E. R., and Gestwicki, J. E. (2011) Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism. Chem. Biol. 18, 210-221.
    • (2011) Chem. Biol. , vol.18 , pp. 210-221
    • Chang, L.1    Miyata, Y.2    Ung, P.M.3    Bertelsen, E.B.4    McQuade, T.J.5    Carlson, H.A.6    Zuiderweg, E.R.7    Gestwicki, J.E.8
  • 30
    • 39149117364 scopus 로고    scopus 로고
    • Identification of small molecules that modify the protein folding activity of heat shock protein 70
    • Wisen, S., and Gestwicki, J. E. (2008) Identification of small molecules that modify the protein folding activity of heat shock protein 70. Anal. Biochem. 374, 371-377.
    • (2008) Anal. Biochem. , vol.374 , pp. 371-377
    • Wisen, S.1    Gestwicki, J.E.2
  • 31
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • DOI 10.1016/j.ab.2007.08.020, PII S0003269707005416
    • Chang, L., Bertelsen, E. B., Wisen, S., Larsen, E. M., Zuiderweg, E. R., and Gestwicki, J. E. (2008) High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Anal. Biochem. 372, 167-176. (Pubitemid 350116767)
    • (2008) Analytical Biochemistry , vol.372 , Issue.2 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisen, S.3    Larsen, E.M.4    Zuiderweg, E.R.P.5    Gestwicki, J.E.6
  • 32
    • 67650286836 scopus 로고    scopus 로고
    • Enantioselective organocatalytic Hantzsch synthesis of polyhydroquinolines
    • Evans, C. G., and Gestwicki, J. E. (2009) Enantioselective organocatalytic Hantzsch synthesis of polyhydroquinolines. Org. Lett. 11, 2957-2959.
    • (2009) Org. Lett. , vol.11 , pp. 2957-2959
    • Evans, C.G.1    Gestwicki, J.E.2
  • 35
    • 67849092349 scopus 로고    scopus 로고
    • Exploiting yeast genetics to inform therapeutic strategies for Huntington's disease
    • Giorgini, F., and Muchowski, P. J. (2009) Exploiting yeast genetics to inform therapeutic strategies for Huntington's disease. Methods Mol. Biol. 548, 161-174.
    • (2009) Methods Mol. Biol. , vol.548 , pp. 161-174
    • Giorgini, F.1    Muchowski, P.J.2
  • 36
    • 0037053566 scopus 로고    scopus 로고
    • Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • DOI 10.1083/jcb.200112104
    • Meriin, A. B., Zhang, X., He, X., Newnam, G. P., Chernoff, Y. O., and Sherman, M. Y. (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 157, 997-1004. (Pubitemid 34839774)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 37
    • 3242723420 scopus 로고    scopus 로고
    • A cell-based screen for drugs to treat Huntington's disease
    • DOI 10.1016/j.nbd.2004.04.001, PII S0969996104000828
    • Aiken, C. T., Tobin, A. J., and Schweitzer, E. S. (2004) A cellbased screen for drugs to treat Huntington's disease. Neurobiol. Dis. 16, 546-555. (Pubitemid 38942987)
    • (2004) Neurobiology of Disease , vol.16 , Issue.3 , pp. 546-555
    • Aiken, C.T.1    Tobin, A.J.2    Schweitzer, E.S.3
  • 39
    • 37549046818 scopus 로고    scopus 로고
    • Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase
    • Wisen, S., Androsavich, J., Evans, C. G., Chang, L., and Gestwicki, J. E. (2008) Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase. Bioorg. Med. Chem. Lett. 18, 60-65.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 60-65
    • Wisen, S.1    Androsavich, J.2    Evans, C.G.3    Chang, L.4    Gestwicki, J.E.5
  • 40
    • 66149188136 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of conformationally constrained cis-amide Hsp90 inhibitors
    • Duerfeldt, A. S., Brandt, G. E., and Blagg, B. S. (2009) Design, synthesis, and biological evaluation of conformationally constrained cis-amide Hsp90 inhibitors. Org. Lett. 11, 2353-2356.
    • (2009) Org. Lett. , vol.11 , pp. 2353-2356
    • Duerfeldt, A.S.1    Brandt, G.E.2    Blagg, B.S.3
  • 41
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist, S. (1986) The heat-shock response. Annu. Rev. Biochem. 55, 1151-1191. (Pubitemid 16070798)
    • (1986) Annual Review of Biochemistry , vol.VOL. 55 , pp. 1151-1191
    • Lindquist, S.1
  • 42
    • 0035064786 scopus 로고    scopus 로고
    • Hsf1p and Msn2/4p cooperate in the expression of Saccharomyces cerevisiae genes HSP26 and HSP104 in a gene- and stress type-dependent manner
    • DOI 10.1046/j.1365-2958.2001.02339.x
    • Amoros, M., and Estruch, F. (2001) Hsf1p and Msn2/4p cooperate in the expression of Saccharomyces cerevisiae genes HSP26 and HSP104 in a gene- and stress type-dependent manner. Mol. Microbiol. 39, 1523-1532. (Pubitemid 32269749)
    • (2001) Molecular Microbiology , vol.39 , Issue.6 , pp. 1523-1532
    • Amoros, M.1    Estruch, F.2
  • 43
    • 0024294370 scopus 로고
    • Transcriptional activation by the SV40 AP-1 recognition element in yeast is mediated by a factor similar to AP-1 that is distinct from GCN4
    • Harshman, K. D., Moye-Rowley, W. S., and Parker, C. S. (1988) Transcriptional activation by the SV40 AP-1 recognition element in yeast is mediated by a factor similar to AP-1 that is distinct from GCN4. Cell 53, 321-330.
    • (1988) Cell , vol.53 , pp. 321-330
    • Harshman, K.D.1    Moye-Rowley, W.S.2    Parker, C.S.3
  • 44
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • DOI 10.1016/S0092-8674(00)81360-4
    • Cox, J. S., and Walter, P. (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87, 391-404. (Pubitemid 26374314)
    • (1996) Cell , vol.87 , Issue.3 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 45
    • 83755183685 scopus 로고    scopus 로고
    • Polyglutamine misfolding in yeast: Toxic and protective aggregation
    • Duennwald, M. L. (2011) Polyglutamine misfolding in yeast: Toxic and protective aggregation. Prion 5, 285-290.
    • (2011) Prion , vol.5 , pp. 285-290
    • Duennwald, M.L.1
  • 46
    • 80053564708 scopus 로고    scopus 로고
    • Amyloid in neurodegenerative diseases: Friend or foe?
    • Wolfe, K. J., and Cyr, D. M. (2011) Amyloid in neurodegenerative diseases: Friend or foe? Semin. Cell. Dev. Biol., 476-481.
    • (2011) Semin. Cell. Dev. Biol. , pp. 476-481
    • Wolfe, K.J.1    Cyr, D.M.2
  • 47
    • 81755172428 scopus 로고    scopus 로고
    • Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes
    • Walter, G. M., Smith, M. C., Wisen, S., Basrur, V., Elenitoba- Johnson, K. S., Duennwald, M. L., Kumar, A., and Gestwicki, J. E. (2011) Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. J. Biol. Chem. 286, 40486-40493.
    • (2011) J. Biol. Chem. , vol.286 , pp. 40486-40493
    • Walter, G.M.1    Smith, M.C.2    Wisen, S.3    Basrur, V.4    Elenitoba-Johnson, K.S.5    Duennwald, M.L.6    Kumar, A.7    Gestwicki, J.E.8
  • 48
    • 84868129517 scopus 로고    scopus 로고
    • Protein aggregates in Huntington's disease
    • Arrasate, M., and Finkbeiner, S. (2002) Protein aggregates in Huntington's disease. Exp. Neurol. 84, 273-278.
    • (2002) Exp. Neurol. , vol.84 , pp. 273-278
    • Arrasate, M.1    Finkbeiner, S.2
  • 49
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., and Finkbeiner, S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810. (Pubitemid 39434070)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 50
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutaminemediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick, J. M., Chan, H. Y., Gray-Board, G. L., Chai, Y., Paulson, H. L., and Bonini, N. M. (1999) Suppression of polyglutaminemediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. 23, 425-428.
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 51
    • 18144374138 scopus 로고    scopus 로고
    • NMR investigations of allosteric processes in a two-domain thermus thermophilus Hsp70 molecular chaperone
    • DOI 10.1016/j.jmb.2005.03.033, PII S0022283605003141
    • Revington, M., Zhang, Y., Yip, G. N., Kurochkin, A. V., and Zuiderweg, E. R. (2005) NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone. J. Mol. Biol. 349, 163-183. (Pubitemid 40616456)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.1 , pp. 163-183
    • Revington, M.1    Zhang, Y.2    Yip, G.N.B.3    Kurochkin, A.V.4    Zuiderweg, E.R.P.5
  • 52
    • 0037044301 scopus 로고    scopus 로고
    • Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state
    • Slepenkov, S. V., and Witt, S. N. (2002) Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state. Biochemistry 41, 12224-12235.
    • (2002) Biochemistry , vol.41 , pp. 12224-12235
    • Slepenkov, S.V.1    Witt, S.N.2
  • 53
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 Chaperone Ligands Control Domain Association via an Allosteric Mechanism Mediated by the Interdomain Linker
    • DOI 10.1016/j.molcel.2007.02.020, PII S1097276507001207
    • Swain, J. F., Dinler, G., Sivendran, R., Montgomery, D. L., Stotz, M., and Gierasch, L. M. (2007) Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell 26, 27-39. (Pubitemid 46550933)
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 55
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • DOI 10.1016/j.ab.2007.08.020, PII S0003269707005416
    • Chang, L., Bertelsen, E. B., Wisén, S., Larsen, E. M., Zuiderweg, E. R., and Gestwicki, J. E. (2008) High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Anal. Biochem. 372, 167-176. (Pubitemid 350116767)
    • (2008) Analytical Biochemistry , vol.372 , Issue.2 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisen, S.3    Larsen, E.M.4    Zuiderweg, E.R.P.5    Gestwicki, J.E.6
  • 56
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation: HSP26 alteks the nature of protein aggregates to facilitate reactivation by HSP104
    • DOI 10.1074/jbc.M502854200
    • Cashikar, A. G., Duennwald, M., and Lindquist, S. L. (2005) A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 280, 23869-23875. (Pubitemid 40884874)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 57
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald, M. L., and Lindquist, S. (2008) Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 22, 3308-3319.
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 59
    • 79952191022 scopus 로고    scopus 로고
    • Monitoring polyglutamine toxicity in yeast
    • Duennwald, M. L. (2011) Monitoring polyglutamine toxicity in yeast. Methods 53, 232-237.
    • (2011) Methods , vol.53 , pp. 232-237
    • Duennwald, M.L.1
  • 60
    • 80055112289 scopus 로고    scopus 로고
    • Screening for amyloid aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
    • 10.3791/838
    • Halfmann, R., and Lindquist, S. (2008) Screening for amyloid aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis. J. Vis. Exp. 17, No. 10.3791/838.
    • (2008) J. Vis. Exp. , vol.17
    • Halfmann, R.1    Lindquist, S.2


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