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Volumn 694, Issue , 2010, Pages 138-159

Protein homeostasis in models of aging and age-related conformational disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; ANSAMYCIN DERIVATIVE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CELASTROL; CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90 INHIBITOR; LACTACYSTIN; NONSTEROID ANTIINFLAMMATORY AGENT; POLYGLUTAMINE; PROTEASOME INHIBITOR; PROTEINASE INHIBITOR; RADICICOL; SERINE PROTEINASE INHIBITOR; TANESPIMYCIN; TAU PROTEIN; TRIPTOLIDE; PROTEIN;

EID: 78049383942     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-7002-2_11     Document Type: Article
Times cited : (152)

References (175)
  • 1
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • DOI 10.1038/24550
    • Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 1998; 396:336-342. (Pubitemid 28557387)
    • (1998) Nature , vol.396 , Issue.6709 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 2
    • 0033215279 scopus 로고    scopus 로고
    • Pathogenic light chains and the B-cell repertoire
    • DOI 10.1016/S0167-5699(99)01502-9, PII S0167569999015029
    • Stevens FJ, Argon Y. Pathogenic light chains and the B-cell repertoire. Immunol Today 1999; 20:451-457. (Pubitemid 29476074)
    • (1999) Immunology Today , vol.20 , Issue.10 , pp. 451-457
    • Stevens, F.J.1    Argon, Y.2
  • 3
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • DOI 10.1126/science.1124514
    • Gidalevitz T, Ben-Zvi A, Ho KH et al. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 2006; 311:1471-1474. (Pubitemid 43376703)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 4
    • 34047237073 scopus 로고    scopus 로고
    • Hsp90 selectively modulates phenotype in vertebrate development
    • Yeyati PL, Bancewicz RM, Maule J et al. Hsp90 selectively modulates phenotype in vertebrate development. PLoS Genet 2007; 3:e43.
    • (2007) PLoS Genet , vol.3
    • Yeyati, P.L.1    Bancewicz, R.M.2    Maule, J.3
  • 6
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 1993; 27:437-496. (Pubitemid 24011359)
    • (1993) Annual Review of Genetics , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 7
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch WE, Morimoto RI, Dillin A et al. Adapting proteostasis for disease intervention. Science 2008; 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
  • 8
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging : a theory based on free radical and radiation chemistry. J Gerontol 1956; 11:298-300.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 9
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal RS, Weindruch R. Oxidative stress, caloric restriction and aging. Science 1996; 273:59-63. (Pubitemid 26255420)
    • (1996) Science , vol.273 , Issue.5271 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 10
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • DOI 10.1074/jbc.272.33.20313
    • Berlett BS, Stadtman ER. Protein oxidation in aging, disease and oxidative stress. J Biol Chem 1997; 272:20313-20316. (Pubitemid 27355575)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 11
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins: Physiological consequences
    • Stadtman ER, Oliver CN. Metal-catalyzed oxidation of proteins. Physiological consequences. J Biol Chem 1991; 266:2005-2008. (Pubitemid 21909019)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.4 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 13
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. Protein oxidation and aging. Science 1992; 257:1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 14
    • 14044251043 scopus 로고    scopus 로고
    • Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity
    • DOI 10.1074/jbc.M410973200
    • Ahmed N, Dobler D, Dean M et al. Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J Biol Chem 2005; 280:5724-5732. (Pubitemid 40280052)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5724-5732
    • Ahmed, N.1    Dobler, D.2    Dean, M.3    Thornalley, P.J.4
  • 15
    • 0028605299 scopus 로고
    • Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine and N alpha-acetyllysine and bovine serum albumin
    • Lo TW, Westwood ME, McLellan AC et al. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine and N alpha-acetyllysine and bovine serum albumin. J Biol Chem 1994; 269:32299-32305.
    • (1994) J Biol Chem , vol.269 , pp. 32299-32305
    • Lo, T.W.1    Westwood, M.E.2    McLellan, A.C.3
  • 16
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms - Chemistry, biochemistry, toxicology and biological implications
    • DOI 10.1016/S0378-4274(99)00160-5, PII S0378427499001605
    • Kalapos MP. Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol Lett 1999; 110:145-175. (Pubitemid 29528251)
    • (1999) Toxicology Letters , vol.110 , Issue.3 , pp. 145-175
    • Kalapos, M.P.1
  • 17
    • 33751330181 scopus 로고    scopus 로고
    • Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimer's disease brains
    • DOI 10.1016/j.neurobiolaging.2005.11.007, PII S0197458005004057
    • Kuhla B, Boeck K, Schmidt A et al. Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimer's disease brains. Neurobiol Aging 2007; 28:29-41. (Pubitemid 44802915)
    • (2007) Neurobiology of Aging , vol.28 , Issue.1 , pp. 29-41
    • Kuhla, B.1    Boeck, K.2    Schmidt, A.3    Ogunlade, V.4    Arendt, T.5    Munch, G.6    Luth, H.-J.7
  • 18
    • 28344445558 scopus 로고    scopus 로고
    • On the mechanisms of ageing suppression by dietary restriction - Is persistent glycolysis the problem?
    • DOI 10.1016/j.mad.2005.09.006, PII S0047637405002241
    • Hipkiss AR. On the mechanisms of ageing suppression by dietary restriction-is persistent glycolysis the problem? Mech Ageing Dev 2006; 127:8-15. (Pubitemid 41715230)
    • (2006) Mechanisms of Ageing and Development , vol.127 , Issue.1 , pp. 8-15
    • Hipkiss, A.R.1
  • 20
    • 17844372715 scopus 로고    scopus 로고
    • Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival
    • DOI 10.2174/1381612053507846
    • Moskovitz J. Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival. Curr Pharm Des 2005; 11:1451-1457. (Pubitemid 40590193)
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.11 , pp. 1451-1457
    • Moskovitz, J.1
  • 21
    • 33646578189 scopus 로고    scopus 로고
    • Oxidized protein degradation and repair in ageing and oxidative stress
    • DOI 10.1016/j.febslet.2006.03.028, PII S0014579306003309
    • Friguet B. Oxidized protein degradation and repair in ageing and oxidative stress. FEBS Lett 2006; 580:2910-2916. (Pubitemid 43729157)
    • (2006) FEBS Letters , vol.580 , Issue.12 , pp. 2910-2916
    • Friguet, B.1
  • 22
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 1993; 62:797-821. (Pubitemid 23237888)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 23
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson SR, Hasan A, Smith DL et al. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp Eye Res 2000; 71:195-207.
    • (2000) Exp Eye Res , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3
  • 24
    • 40149100476 scopus 로고    scopus 로고
    • Regulation of proteasome-mediated protein degradation during oxidative stress and aging
    • DOI 10.1515/BC.2008.029
    • Breusing N, Grune T. Regulation of proteasome-mediated protein degradation during oxidative stress and aging. Biol Chem 2008; 389:203-209. (Pubitemid 351329027)
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 203-209
    • Breusing, N.1    Grune, T.2
  • 25
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001; 83:301-310.
    • (2001) Biochimie , vol.83 , Issue.301-310
    • Davies, K.J.1
  • 26
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • DOI 10.1074/jbc.M206279200
    • Shringarpure R, Grune T, Mehlhase J et al. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 2003; 278:311-318. (Pubitemid 36043578)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 27
    • 0034769477 scopus 로고    scopus 로고
    • Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway
    • DOI 10.1006/exer.2001.1029
    • Shang F, Nowell TR Jr, Taylor A. Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp Eye Res 2001; 73:229-238. (Pubitemid 32977953)
    • (2001) Experimental Eye Research , vol.73 , Issue.2 , pp. 229-238
    • Shang, F.1    Nowell Jr., T.R.2    Taylor, A.3
  • 28
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • DOI 10.1038/ncb836
    • Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 2002; 4:674-680. (Pubitemid 34993703)
    • (2002) Nature Cell Biology , vol.4 , Issue.9 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.A.2
  • 29
    • 0033648814 scopus 로고    scopus 로고
    • The measurement of protein degradation in response to oxidative stress
    • Reinheckel T, Grune T, Davies KJ. The measurement of protein degradation in response to oxidative stress. Methods Mol Biol 2000; 99:49-60.
    • (2000) Methods Mol Biol , vol.99 , pp. 49-60
    • Reinheckel, T.1    Grune, T.2    Davies, K.J.3
  • 30
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • DOI 10.1091/mbc.E04-06-0477
    • Kiffin R, Christian C, Knecht E et al. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell 2004; 15:4829-4840. (Pubitemid 39392200)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 31
    • 0022537857 scopus 로고
    • Site-saturation studies of β-lactamase: Production and characterization of mutant β-lactamases with all possible amino acid substitutions at residue 71
    • Schultz SC, Richards JH. Site-saturation studies of beta-lactamase: production and characterization of mutant beta-lactamases with all possible amino acid substitutions at residue 71. Proc Natl Acad Sci USA 1986; 83:1588-1592. (Pubitemid 16018609)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.6 , pp. 1588-1592
    • Schultz, S.C.1    Richards, J.H.2
  • 32
    • 0024792699 scopus 로고
    • Genetic analysis of protein stability and function
    • Pakula AA, Sauer RT. Genetic analysis of protein stability and function. Annu Rev Genet 1989; 23:289-310. (Pubitemid 20033405)
    • (1989) Annual Review of Genetics , vol.23 , pp. 289-310
    • Pakula, A.A.1    Sauer, R.T.2
  • 33
    • 33750353461 scopus 로고    scopus 로고
    • Predicting the effects of amino acid substitutions on protein function
    • DOI 10.1146/annurev.genom.7.080505.115630
    • Ng PC, Henikoff S. Predicting the effects of amino acid substitutions on protein function. Annu Rev Genomics Hum Genet 2006; 7:61-80. (Pubitemid 44627922)
    • (2006) Annual Review of Genomics and Human Genetics , vol.7 , pp. 61-80
    • Ng, P.C.1    Henikoff, S.2
  • 34
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: A biophysical view of protein evolution
    • DOI 10.1038/nrg1672
    • DePristo MA, Weinreich DM, Hartl DL. Missense meanderings in sequence space: a biophysical view of protein evolution. Nat Rev Genet 2005; 6:678-687. (Pubitemid 41192319)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.9 , pp. 678-687
    • DePristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 35
    • 2342519701 scopus 로고    scopus 로고
    • Genetic studies of the Lac repressor XV: 4000 single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure
    • DOI 10.1006/jmbi.1996.0479
    • Suckow J, Markiewicz P, Kleina LG et al. Genetic studies of the Lac repressor. XV: 4000 single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure. J Mol Biol 1996; 261:509-523. (Pubitemid 26335943)
    • (1996) Journal of Molecular Biology , vol.261 , Issue.4 , pp. 509-523
    • Suckow, J.1    Markiewicz, P.2    Kleina, L.G.3    Miller, J.4    Kisters-Woike, B.5    Muller-Hill, B.6
  • 37
    • 47549097539 scopus 로고    scopus 로고
    • Mistranslation-Induced Protein Misfolding as a Dominant Constraint on Coding-Sequence Evolution
    • DOI 10.1016/j.cell.2008.05.042, PII S0092867408007058
    • Drummond DA, Wilke CO. Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell 2008; 134:341-352. (Pubitemid 352010328)
    • (2008) Cell , vol.134 , Issue.2 , pp. 341-352
    • Drummond, D.A.1    Wilke, C.O.2
  • 38
    • 62149129690 scopus 로고    scopus 로고
    • Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity
    • Gidalevitz T, Krupinski T, Garcia S et al. Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity. PLoS Genet 2009; 5:e1000399.
    • (2009) PLoS Genet , vol.5
    • Gidalevitz, T.1    Krupinski, T.2    Garcia, S.3
  • 39
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • DOI 10.1007/s00109-003-0464-5
    • Stefani M, Dobson CM. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 2003; 81:678-699. (Pubitemid 37491594)
    • (2003) Journal of Molecular Medicine , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 43
    • 33645879820 scopus 로고    scopus 로고
    • Oxidative damage and age-related functional declines
    • Martin I, Grotewiel MS. Oxidative damage and age-related functional declines. Mech Ageing Dev 2006; 127:411-423.
    • (2006) Mech Ageing Dev , vol.127 , pp. 411-423
    • Martin, I.1    Grotewiel, M.S.2
  • 44
    • 70349507340 scopus 로고    scopus 로고
    • The shock of aging: Molecular chaperones and the heat shock response in longevity and aginga mini-review
    • Calderwood SK, Murshid A, Prince T. The Shock of Aging: Molecular Chaperones and the Heat Shock Response in Longevity and Aging-A Mini-Review. Gerontology 2009.
    • (2009) Gerontology
    • Calderwood, S.K.1    Murshid, A.2    Prince, T.3
  • 45
    • 9144223729 scopus 로고    scopus 로고
    • Inefficient degradation of truncated polyglutamine proteins by the proteasome
    • DOI 10.1038/sj.emboj.7600426
    • Holmberg CI, Staniszewski KE, Mensah KN et al. Inefficient degradation of truncated polyglutamine proteins by the proteasome. EMBO J 2004; 23:4307-4318. (Pubitemid 39546168)
    • (2004) EMBO Journal , vol.23 , Issue.21 , pp. 4307-4318
    • Holmberg, C.I.1    Staniszewski, K.E.2    Mensah, K.N.3    Matouschek, A.4    Morimoto, R.I.5
  • 46
    • 0036797242 scopus 로고    scopus 로고
    • Polyglutamine protein aggregates are dynamic
    • Kim S, Nollen EA, Kitagawa K et al. Polyglutamine protein aggregates are dynamic. Nat Cell Biol 2002; 4:826-831.
    • (2002) Nat Cell Biol , vol.4 , pp. 826-831
    • Kim, S.1    Nollen, E.A.2    Kitagawa, K.3
  • 48
    • 34147116715 scopus 로고    scopus 로고
    • Most rare missense alleles are deleterious in humans: Implications for complex disease and association studies
    • DOI 10.1086/513473
    • Kryukov GV, Pennacchio LA, Sunyaev SR. Most rare missense alleles are deleterious in humans: implications for complex disease and association studies. Am J Hum Genet 2007; 80:727-739. (Pubitemid 46564409)
    • (2007) American Journal of Human Genetics , vol.80 , Issue.4 , pp. 727-739
    • Kryukov, G.V.1    Pennacchio, L.A.2    Sunyaev, S.R.3
  • 49
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • DOI 10.1074/jbc.R500010200
    • Westerheide SD, Morimoto RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 2005; 280:33097-33100. (Pubitemid 41397104)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 50
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8:519-529. (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 51
    • 0021685483 scopus 로고
    • Heat shock-induced translational control of HSP70 and globin synthesis in chicken reticulocytes
    • Banerji SS, Theodorakis NG, Morimoto RI. Heat shock-induced translational control of HSP70 and globin synthesis in chicken reticulocytes. Mol Cell Biol 1984; 4:2437-2448. (Pubitemid 15212259)
    • (1984) Molecular and Cellular Biology , vol.4 , Issue.11 , pp. 2437-2448
    • Banerji, S.S.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 52
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • DOI 10.1093/emboj/18.21.5943
    • Xiao X, Zuo X, Davis AA et al. HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 1999; 18:5943-5952. (Pubitemid 29515671)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    McMillan, D.R.4    Curry, B.B.5    Richardson, J.A.6    Benjamin, I.J.7
  • 53
    • 2942525558 scopus 로고    scopus 로고
    • Enlarged ventricles, astrogliosis and neurodegeneration in heat shock factor 1 null mouse brain
    • DOI 10.1016/j.neuroscience.2004.03.023, PII S0306452204002106
    • Santos SD, Saraiva MJ. Enlarged ventricles, astrogliosis and neurodegeneration in heat shock factor 1 null mouse brain. Neuroscience 2004; 126:657-663. (Pubitemid 38759259)
    • (2004) Neuroscience , vol.126 , Issue.3 , pp. 657-663
    • Santos, S.D.1    Saraiva, M.J.2
  • 54
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • DOI 10.1128/MCB.22.11.3864-3874.2002
    • Zhang P, McGrath B, Li S et al. The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth and the function and viability of the pancreas. Mol Cell Biol 2002; 22:3864-3874. (Pubitemid 34525227)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.11 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6    Gannon, M.7    Ma, K.8    McNaughton, K.9    Cavener, D.R.10
  • 57
    • 0032837196 scopus 로고    scopus 로고
    • Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality
    • Elefant F, Palter KB. Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality. Mol Biol Cell 1999; 10:2101-2117. (Pubitemid 29343122)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.7 , pp. 2101-2117
    • Elefant, F.1    Palter, K.B.2
  • 58
    • 0026645957 scopus 로고
    • The consequences of expressing hsp70 in Drosophila cells at normal temperatures
    • Feder JH, Rossi JM, Solomon J et al. The consequences of expressing hsp70 in Drosophila cells at normal temperatures. Genes Dev 1992; 6:1402-1413.
    • (1992) Genes Dev , vol.6 , pp. 1402-1413
    • Feder, J.H.1    Rossi, J.M.2    Solomon, J.3
  • 60
    • 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 EG, De Costa B et al. 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 1994; 91:8324-8328.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3
  • 61
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • DOI 10.1038/nrc1716
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005; 5:761-772. (Pubitemid 41400776)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 63
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley JF, Brignull HR, Weyers JJ et al. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci USA 2002; 99:10417-10422.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3
  • 64
    • 0029768753 scopus 로고    scopus 로고
    • A phosphatidylinositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans
    • DOI 10.1038/382536a0
    • Morris JZ, Tissenbaum HA, Ruvkun G. A phosphatidylinositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans. Nature 1996; 382:536-539. (Pubitemid 26260694)
    • (1996) Nature , vol.382 , Issue.6591 , pp. 536-539
    • Morris, J.Z.1    Tissenbaum, H.A.2    Ruvkun, G.3
  • 65
    • 0030657540 scopus 로고    scopus 로고
    • Daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans
    • DOI 10.1126/science.278.5341.1319
    • Lin K, Dorman JB, Rodan A et al. daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans. Science 1997; 278:1319-1322. (Pubitemid 27495748)
    • (1997) Science , vol.278 , Issue.5341 , pp. 1319-1322
    • Lin, K.1    Dorman, J.B.2    Rodan, A.3    Kenyon, C.4
  • 66
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of Longevity in Caenorhabditis elegans by Heat Shock Factor and Molecular Chaperones
    • DOI 10.1091/mbc.E03-07-0532
    • Morley JF, Morimoto RI. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 2004; 15:657-664. (Pubitemid 38146482)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 67
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • DOI 10.1126/science.1083701
    • Hsu AL, Murphy CT, Kenyon C. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 2003; 300:1142-1145. (Pubitemid 36583098)
    • (2003) Science , vol.300 , Issue.5622 , pp. 1142-1145
    • Hsu, A.-L.1    Murphy, C.T.2    Kenyon, C.3
  • 68
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • DOI 10.1126/science.1124646
    • Cohen E, Bieschke J, Perciavalle RM et al. Opposing activities protect against age-onset proteotoxicity. Science 2006; 313:1604-1610. (Pubitemid 44414028)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 69
    • 0029123058 scopus 로고
    • Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress
    • Lithgow GJ, White TM, Melov S et al. Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress. Proc Natl Acad Sci USA 1995; 92:7540-7544.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7540-7544
    • Lithgow, G.J.1    White, T.M.2    Melov, S.3
  • 74
    • 44049095652 scopus 로고    scopus 로고
    • Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons
    • DOI 10.1126/science.1156093
    • Prahlad V, Cornelius T, Morimoto RI. Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons. Science 2008; 320:811-814. (Pubitemid 351929633)
    • (2008) Science , vol.320 , Issue.5877 , pp. 811-814
    • Prahlad, V.1    Cornelius, T.2    Morimoto, R.I.3
  • 76
    • 0023550048 scopus 로고
    • Selective induction of a heat shock gene in fibre tracts and cerebellar neurons of the rabbit brain detected by in situ hybridization
    • DOI 10.1016/0169-328X(87)90049-0
    • Sprang GK, Brown IR. Selective induction of a heat shock gene in fibre tracts and cerebellar neurons of the rabbit brain detected by in situ hybridization. Brain Res 1987; 427:89-93. (Pubitemid 18015567)
    • (1987) Molecular Brain Research , vol.3 , Issue.1 , pp. 89-93
    • Sprang, G.K.1    Brown, I.R.2
  • 77
    • 8344262275 scopus 로고    scopus 로고
    • Novel regulatory factors of HSF-1 activation: Facts and perspectives regarding their involvement in the age-associated attenuation of the heat shock response
    • DOI 10.1016/j.mad.2004.07.006, PII S0047637404001678
    • Shamovsky I, Gershon D. Novel regulatory factors of HSF-1 activation: facts and perspectives regarding their involvement in the age-associated attenuation of the heat shock response. Mech Ageing Dev 2004; 125:767-775. (Pubitemid 39482405)
    • (2004) Mechanisms of Ageing and Development , vol.125 , Issue.10-11 SPEC. ISSUE , pp. 767-775
    • Shamovsky, I.1    Gershon, D.2
  • 79
    • 0030048735 scopus 로고    scopus 로고
    • Regulatory differences in the stress response of hippocampal neurons and glial cells after heat shock
    • Marcuccilli CJ, Mathur SK, Morimoto RI et al. Regulatory differences in the stress response of hippocampal neurons and glial cells after heat shock. J Neurosci 1996; 16:478-485. (Pubitemid 26028808)
    • (1996) Journal of Neuroscience , vol.16 , Issue.2 , pp. 478-485
    • Marcuccilli, C.J.1    Mathur, S.K.2    Morimoto, R.I.3    Miller, R.J.4
  • 81
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • DOI 10.1038/nrn1587
    • Muchowski PJ, Wacker JL. Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005; 6:11-22. (Pubitemid 40052135)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 82
    • 0041507039 scopus 로고    scopus 로고
    • Lifespan extension in C. elegans by a molecular chaperone dependent upon insulin-like signals
    • Walker GA, Lithgow GJ. Lifespan extension in C. elegans by a molecular chaperone dependent upon insulin-like signals. Aging Cell 2003; 2:131-139.
    • (2003) Aging Cell , vol.2 , pp. 131-139
    • Walker, G.A.1    Lithgow, G.J.2
  • 83
    • 0037051942 scopus 로고    scopus 로고
    • Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot-2 (mortalin)/mthsp70/Grp75
    • DOI 10.1016/S0014-5793(02)02470-5, PII S0014579302024705
    • YYokoyama K, Fukumoto K, Murakami T et al. Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot-2 (mortalin)/mthsp70/Grp75. FEBS Lett 2002; 516:53-57. (Pubitemid 34311932)
    • (2002) FEBS Letters , vol.516 , Issue.1-3 , pp. 53-57
    • Yokoyama, K.1    Fukumoto, K.2    Murakami, T.3    Harada, S.-I.4    Hosono, R.5    Wadhwa, R.6    Mitsui, Y.7    Ohkuma, S.8
  • 85
    • 67650757278 scopus 로고    scopus 로고
    • Expression of hsp22 and hsp70 transgenes is partially predictive of drosophila survival under normal and stress conditions
    • Yang J, Tower J. Expression of hsp22 and hsp70 transgenes is partially predictive of drosophila survival under normal and stress conditions. J Gerontol A Biol Sci Med Sci 2009; 64:828-838.
    • (2009) J Gerontol A Biol Sci Med Sci , vol.64 , pp. 828-838
    • Yang, J.1    Tower, J.2
  • 88
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide SD, Anckar J, Stevens SM et al. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 2009; 323:1063-1066.
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3
  • 89
    • 0037466652 scopus 로고    scopus 로고
    • DAF-16 target genes that control C. elegans Life-span and metabolism
    • DOI 10.1126/science.1083614
    • Lee SS, Kennedy S, Tolonen AC et al. DAF-16 target genes that control C. elegans life-span and metabolism. Science 2003; 300:644-647. (Pubitemid 36520589)
    • (2003) Science , vol.300 , Issue.5619 , pp. 644-647
    • Lee, S.S.1    Kennedy, S.2    Tolonen, A.C.3    Ruvkun, G.4
  • 91
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid and human disease. Annu Rev Biochem 2006; 75:333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 92
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • DOI 10.1016/S0092-8674(00)81200-3
    • Warrick JM, Paulson HL, Gray-Board GL et al. Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 1998; 93:939-949. (Pubitemid 28280788)
    • (1998) Cell , vol.93 , Issue.6 , pp. 939-949
    • Warrick, J.M.1    Paulson, H.L.2    Gray-Board, G.L.3    Bui, Q.T.4    Fischbeck, K.H.5    Pittman, R.N.6    Bonini, N.M.7
  • 94
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • DOI 10.1038/35006074
    • Feany MB, Bender WW. A Drosophila model of Parkinson's disease. Nature 2000; 404:394-398. (Pubitemid 30164341)
    • (2000) Nature , vol.404 , Issue.6776 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 95
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • DOI 10.1073/pnas.97.4.1589
    • Krobitsch S, Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci USA 2000; 97:1589-1594. (Pubitemid 30118486)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.4 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 98
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL et al. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 1999; 23:425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3
  • 99
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • DOI 10.1126/science.287.5459.1837
    • Kazemi-Esfarjani P, Benzer S. Genetic suppression of polyglutamine toxicity in Drosophila. Science 2000; 287:1837-1840. (Pubitemid 30143971)
    • (2000) Science , vol.287 , Issue.5459 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 101
    • 36248980418 scopus 로고    scopus 로고
    • Neuronal signaling modulates protein homeostasis in Caenorhabditis elegans post-synaptic muscle cells
    • DOI 10.1101/gad.1575307
    • Garcia SM, Casanueva MO, Silva MC et al. Neuronal signaling modulates protein homeostasis in Caenorhabditis elegans postsynaptic muscle cells. Genes Dev 2007; 21:3006-3016. (Pubitemid 350133446)
    • (2007) Genes and Development , vol.21 , Issue.22 , pp. 3006-3016
    • Garcia, S.M.1    Casanueva, M.O.2    Silva, M.C.3    Amara, M.D.4    Morimoto, R.I.5
  • 102
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • DOI 10.1016/S0896-6273(00)80573-5
    • Jackson GR, Salecker I, Dong X et al. Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 1998; 21:633-642. (Pubitemid 28475514)
    • (1998) Neuron , vol.21 , Issue.3 , pp. 633-642
    • Jackson, G.R.1    Salecker, I.2    Dong, X.3    Yao, X.4    Arnheim, N.5    Faber, P.W.6    MacDonald, M.E.7    Zipursky, S.L.8
  • 103
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model
    • DOI 10.1523/JNEUROSCI.0990-06.2006
    • Brignull HR, Moore FE, Tang SJ et al. Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model. J Neurosci 2006; 26:7597-7606. (Pubitemid 44315179)
    • (2006) Journal of Neuroscience , vol.26 , Issue.29 , pp. 7597-7606
    • Brignull, H.R.1    Moore, F.E.2    Tang, S.J.3    Morimoto, R.I.4
  • 105
    • 0028981288 scopus 로고
    • Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans
    • Link CD. Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc Natl Acad Sci USA 1995; 92:9368-9372.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9368-9372
    • Link, C.D.1
  • 106
    • 3242809725 scopus 로고    scopus 로고
    • A model for studying Alzheimer's Aβ42-induced toxicity in Drosophila melanogaster
    • DOI 10.1016/j.mcn.2004.03.001, PII S1044743104000521
    • Finelli A, Kelkar A, Song HJ et al. A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster. Mol Cell Neurosci 2004; 26:365-375. (Pubitemid 38968431)
    • (2004) Molecular and Cellular Neuroscience , vol.26 , Issue.3 , pp. 365-375
    • Finelli, A.1    Kelkar, A.2    Song, H.-J.3    Yang, H.4    Konsolaki, M.5
  • 109
    • 0030768929 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease
    • DOI 10.1093/hmg/6.10.1687
    • Nussbaum RL, Polymeropoulos MH. Genetics of Parkinson's disease. Hum Mol Genet 1997; 6:1687-1691. (Pubitemid 27401611)
    • (1997) Human Molecular Genetics , vol.6 , Issue.10 REV. ISSUE , pp. 1687-1691
    • Nussbaum, R.L.1    Polymeropoulos, M.H.2
  • 110
    • 0030821967 scopus 로고    scopus 로고
    • A gene for Parkinson disease
    • Chase TN. A gene for Parkinson disease. Arch Neurol 1997; 54:1156-1157. (Pubitemid 27396484)
    • (1997) Archives of Neurology , vol.54 , Issue.9 , pp. 1156-1157
    • Chase, T.N.1
  • 112
    • 41949097891 scopus 로고    scopus 로고
    • C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging
    • van Ham TJ, Thijssen KL, Breitling R et al. C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging. PLoS Genet 2008; 4:e1000027.
    • (2008) PLoS Genet , vol.4
    • Van Ham, T.J.1    Thijssen, K.L.2    Breitling, R.3
  • 113
    • 0027164824 scopus 로고
    • Erratum: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis (Nature (1993) 362 (59-62))
    • Rosen DR. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993; 364:362. (Pubitemid 23265284)
    • (1993) Nature , vol.364 , Issue.6435 , pp. 362
    • Rosen, D.R.1
  • 114
    • 54049142949 scopus 로고    scopus 로고
    • A drosophila model for amyotrophic lateral sclerosis reveals motor neuron damage by human SOD1
    • Watson MR, Lagow RD, Xu K et al. A drosophila model for amyotrophic lateral sclerosis reveals motor neuron damage by human SOD1. J Biol Chem 2008; 283:24972-24981.
    • (2008) J Biol Chem , vol.283 , pp. 24972-24981
    • Watson, M.R.1    Lagow, R.D.2    Xu, K.3
  • 115
    • 59249098430 scopus 로고    scopus 로고
    • An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
    • Wang J, Farr GW, Hall DH et al. An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. PLoS Genet 2009; 5:e1000350.
    • (2009) PLoS Genet , vol.5
    • Wang, J.1    Farr, G.W.2    Hall, D.H.3
  • 116
    • 0037442768 scopus 로고    scopus 로고
    • Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
    • DOI 10.1101/gad.1044503
    • Ahn SG, Thiele DJ. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes Dev 2003; 17:516-528. (Pubitemid 36258765)
    • (2003) Genes and Development , vol.17 , Issue.4 , pp. 516-528
    • Ahn, S.-G.1    Thiele, D.J.2
  • 117
    • 1242294502 scopus 로고    scopus 로고
    • Activation of the Saccharomyces cerevisiae Heat Shock Transcription Factor under Glucose Starvation Conditions by Snf1 Protein Kinase
    • DOI 10.1074/jbc.M311005200
    • Hahn JS, Thiele DJ. Activation of the Saccharomyces cerevisiae heat shock transcription factor under glucose starvation conditions by Snf1 protein kinase. J Biol Chem 2004; 279:5169-5176. (Pubitemid 38220534)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5169-5176
    • Hahn, J.-S.1    Thiele, D.J.2
  • 118
    • 4344592639 scopus 로고    scopus 로고
    • Distinct stimulus-specific histone modifications at Hsp70 chromatin targeted by the transcription factor heat shock factor-1
    • DOI 10.1016/j.molcel.2004.08.002, PII S1097276504004484
    • Thomson S, Hollis A, Hazzalin CA et al. Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1. Mol Cell 2004; 15:585-594. (Pubitemid 39141785)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 585-594
    • Thomson, S.1    Hollis, A.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 119
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan J, Goldberg AL, Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 1986; 232:522-524. (Pubitemid 16052371)
    • (1986) Science , vol.232 , Issue.4749 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 120
    • 0022552545 scopus 로고
    • Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes
    • Hiromi Y, Okamoto H, Gehring WJ et al. Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes. Cell 1986; 44:293-301. (Pubitemid 16048215)
    • (1986) Cell , vol.44 , Issue.2 , pp. 293-301
    • Hiromi, Y.1    Okamoto, H.2    Gehring, W.J.3    Hotta, Y.4
  • 121
    • 0024709959 scopus 로고
    • Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation
    • Parsell DA, Sauer RT. Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes Dev 1989; 3:1226-1232.
    • (1989) Genes Dev , vol.3 , pp. 1226-1232
    • Parsell, D.A.1    Sauer, R.T.2
  • 123
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones and negative regulators. Genes Dev 1998; 12:3788-3796. (Pubitemid 29024840)
    • (1998) Genes and Development , vol.12 , Issue.24 , pp. 3788-3796
    • Morimoto, R.I.1
  • 124
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: Regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto RI, Kline MP, Bimston DN et al. The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem 1997; 32:17-29. (Pubitemid 127470399)
    • (1997) Essays in Biochemistry , vol.32 , pp. 17-29
    • Morimoto, R.I.1    Kline, M.P.2    Bimston, D.N.3    Cotto, J.J.4
  • 125
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996; 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 126
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • DOI 10.1016/S0092-8674(00)80928-9
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998; 92:351-366. (Pubitemid 28093013)
    • (1998) Cell , vol.92 , Issue.3 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 127
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 2003; 228:111-133. (Pubitemid 36187918)
    • (2003) Experimental Biology and Medicine , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 128
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125:443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 130
    • 0035900779 scopus 로고    scopus 로고
    • Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations
    • Katayama T, Imaizumi K, Honda A et al. Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations. J Biol Chem 2001; 276:43446-43454.
    • (2001) J Biol Chem , vol.276 , pp. 43446-43454
    • Katayama, T.1    Imaizumi, K.2    Honda, A.3
  • 131
    • 0038039288 scopus 로고    scopus 로고
    • Polyglutamine protein aggregation and toxicity are linked to the cellular stress response
    • Cowan KJ, Diamond MI, Welch WJ. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum Mol Genet 2003; 12:1377-1391. (Pubitemid 36758451)
    • (2003) Human Molecular Genetics , vol.12 , Issue.12 , pp. 1377-1391
    • Cowan, K.J.1    Diamond, M.I.2    Welch, W.J.3
  • 134
    • 0037494974 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 27 in neuronal cells and nonneuronal cells expressing mutant ataxin-3
    • Wen FC, Li YH, Tsai HF et al. Down-regulation of heat shock protein 27 in neuronal cells and nonneuronal cells expressing mutant ataxin-3. FEBS Lett 2003; 546:307-314.
    • (2003) FEBS Lett , vol.546 , pp. 307-314
    • Wen, F.C.1    Li, Y.H.2    Tsai, H.F.3
  • 135
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y, Koppenhafer SL, Bonini NM et al. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 1999; 19:10338-10347. (Pubitemid 30228041)
    • (1999) Journal of Neuroscience , vol.19 , Issue.23 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 137
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • DOI 10.1126/science.292.5521.1552
    • Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001; 292:1552-1555. (Pubitemid 32493425)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 139
    • 0028958208 scopus 로고
    • Scrapie prions selectively modify the stress response in neuroblastoma cells
    • Tatzelt J, Zuo J, Voellmy R et al. Scrapie prions selectively modify the stress response in neuroblastoma cells. Proc Natl Acad Sci USA 1995; 92:2944-2948.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2944-2948
    • Tatzelt, J.1    Zuo, J.2    Voellmy, R.3
  • 140
    • 0024439338 scopus 로고
    • Demonstration by genetic suppression of interaction of GroE products with many proteins
    • DOI 10.1038/342451a0
    • Van Dyk TK, Gatenby AA, LaRossa RA. Demonstration by genetic suppression of interaction of GroE products with many proteins. Nature 1989; 342:451-453. (Pubitemid 19277524)
    • (1989) Nature , vol.342 , Issue.6248 , pp. 451-453
    • Van Dyk, T.K.1    Gatenby, A.A.2    LaRossa, R.A.3
  • 142
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • DOI 10.1371/journal.pgen.0030177
    • Bilen J, Bonini NM. Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genet 2007; 3:1950-1964. (Pubitemid 350072059)
    • (2007) PLoS Genetics , vol.3 , Issue.10 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 143
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • Ben-Zvi A, Miller EA, Morimoto RI. Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc Natl Acad Sci USA 2009.
    • (2009) Proc Natl Acad Sci USA
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 144
    • 0034676457 scopus 로고    scopus 로고
    • Functional genomic analysis of C. elegans chromosome I by systematic RNA interference
    • Fraser AG, Kamath RS, Zipperlen P et al. Functional genomic analysis of C. elegans chromosome I by systematic RNA interference. Nature 2000; 408:325-330.
    • (2000) Nature , vol.408 , pp. 325-330
    • Fraser, A.G.1    Kamath, R.S.2    Zipperlen, P.3
  • 145
    • 0035229245 scopus 로고    scopus 로고
    • Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans
    • RESEARCH0002
    • Kamath RS, Martinez-Campos M, Zipperlen P et al. Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans. Genome Biol 2001; 2:RESEARCH0002.
    • (2001) Genome Biol , vol.2
    • Kamath, R.S.1    Martinez-Campos, M.2    Zipperlen, P.3
  • 146
    • 5744248243 scopus 로고    scopus 로고
    • Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases
    • DOI 10.1093/hmg/ddh214
    • Ghosh S, Feany MB. Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases. Hum Mol Genet 2004; 13:2011-2018. (Pubitemid 39377825)
    • (2004) Human Molecular Genetics , vol.13 , Issue.18 , pp. 2011-2018
    • Ghosh, S.1    Feany, M.B.2
  • 149
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • DOI 10.1038/ncb1477, PII NCB1477
    • Tam S, Geller R, Spiess C et al. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 2006; 8:1155-1162. (Pubitemid 44473612)
    • (2006) Nature Cell Biology , vol.8 , Issue.10 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 150
    • 33646133424 scopus 로고    scopus 로고
    • Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans
    • Kraemer BC, Burgess JK, Chen JH et al. Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans. Hum Mol Genet 2006; 15:1483-1496.
    • (2006) Hum Mol Genet , vol.15 , pp. 1483-1496
    • Kraemer, B.C.1    Burgess, J.K.2    Chen, J.H.3
  • 152
    • 0346361872 scopus 로고    scopus 로고
    • Genetic Modifiers of Tauopathy in Drosophila
    • Shulman JM, Feany MB. Genetic modifiers of tauopathy in Drosophila. Genetics 2003; 165:1233-1242. (Pubitemid 38020245)
    • (2003) Genetics , vol.165 , Issue.3 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 153
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
    • DOI 10.1126/science.1067389
    • Auluck PK, Chan HY, Trojanowski JQ et al. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 2002; 295:865-868. (Pubitemid 34118369)
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.E.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4    Bonini, N.M.5
  • 155
    • 0345189365 scopus 로고    scopus 로고
    • Yeast Genes that Enhance the Toxicity of a Mutant Huntingtin Fragment or α-Synuclein
    • DOI 10.1126/science.1090389
    • Willingham S, Outeiro TF, DeVit MJ et al. Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 2003; 302:1769-1772. (Pubitemid 37505741)
    • (2003) Science , vol.302 , Issue.5651 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5
  • 157
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers ET, Morimoto RI, Dillin A et al. Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 2009; 78:959-991.
    • (2009) Annu Rev Biochem , vol.78 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3
  • 158
    • 33646900838 scopus 로고    scopus 로고
    • Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death
    • DOI 10.1074/jbc.M512044200
    • Westerheide SD, Kawahara TL, Orton K et al. Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death. J Biol Chem 2006; 281:9616-9622. (Pubitemid 43864680)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9616-9622
    • Westerheide, S.D.1    Kawahara, T.L.A.2    Orton, K.3    Morimoto, R.I.4
  • 159
    • 0031841818 scopus 로고    scopus 로고
    • Heat shock response and protein degradation: Regulation of HSF2 by the ubiquitin-proteasome pathway
    • Mathew A, Mathur SK, Morimoto RI. Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway. Mol Cell Biol 1998; 18:5091-5098. (Pubitemid 28388092)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.9 , pp. 5091-5098
    • Mathew, A.1    Mathur, S.K.2    Morimoto, R.I.3
  • 160
    • 0032569013 scopus 로고    scopus 로고
    • Activation of the heat shock factor 1 by serine protease inhibitors. An effect associated with nuclear factor-κB inhibition
    • DOI 10.1074/jbc.273.26.16446
    • Rossi A, Elia G, Santoro MG. Activation of the heat shock factor 1 by serine protease inhibitors. An effect associated with nuclear factor-kappaB inhibition. J Biol Chem 1998; 273:16446-16452. (Pubitemid 28311427)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16446-16452
    • Rossi, A.1    Elia, G.2    Santoro, M.G.3
  • 162
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • Bagatell R, Whitesell L. Altered Hsp90 function in cancer: a unique therapeutic opportunity. MolCancer Ther 2004; 3:1021-1030. (Pubitemid 39199597)
    • (2004) Molecular Cancer Therapeutics , vol.3 , Issue.8 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 163
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich DA, Sistonen L, Kroes RA et al. Effect of sodium salicylate on the human heat shock response. Science 1992; 255:1243-1245.
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3
  • 164
    • 0029161913 scopus 로고
    • Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage
    • Lee BS, Chen J, Angelidis C et al. Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage. Proc Natl Acad Sci USA 1995; 92:7207-7211.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7207-7211
    • Lee, B.S.1    Chen, J.2    Angelidis, C.3
  • 165
    • 0026627948 scopus 로고
    • Antiproliferative prostaglandins activate heat shock transcription factor
    • Amici C, Sistonen L, Santoro MG et al. Antiproliferative prostaglandins activate heat shock transcription factor. Proc Natl Acad Sci USA 1992; 89:6227-6231.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6227-6231
    • Amici, C.1    Sistonen, L.2    Santoro, M.G.3
  • 168
    • 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 JD, Klaié L et al. Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thiol-targeted molecule. Mol Biol Cell. 2008;19(3):1104-12. Epub 2008 Jan 16. (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
  • 170
    • 36849044616 scopus 로고    scopus 로고
    • Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
    • DOI 10.1007/s00109-007-0251-9, Special Issue (Ed. G. Semenza): Hypoxia and Human Disease
    • Zhang YQ, Sarge KD. Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response. J Mol Med 2007; 85:1421-1428. (Pubitemid 350234097)
    • (2007) Journal of Molecular Medicine , vol.85 , Issue.12 , pp. 1421-1428
    • Zhang, Y.-Q.1    Sarge, K.D.2
  • 172
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • Parker JA, Arango M, Abderrahmane S et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat Genet 2005; 37:349-350.
    • (2005) Nat Genet , vol.37 , pp. 349-350
    • Parker, J.A.1    Arango, M.2    Abderrahmane, S.3
  • 173
    • 35548950179 scopus 로고    scopus 로고
    • Identification of potential therapeutic drugs for huntington's disease using Caenorhabditis elegans
    • Voisine C, Varma H, Walker N et al. Identification of potential therapeutic drugs for huntington's disease using Caenorhabditis elegans. PLoS ONE 2007; 2:e504.
    • (2007) PLoS ONE , vol.2
    • Voisine, C.1    Varma, H.2    Walker, N.3


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