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Home All issues Volume 21 / No 6-7 (Juin–Juillet 2005) Med Sci (Paris), 21 6-7 (2005) 619-625 References
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Issue
Med Sci (Paris)
Volume 21, Number 6-7, Juin–Juillet 2005
Page(s) 619 - 625
Section M/S revues
DOI https://doi.org/10.1051/medsci/2005216-7619
Published online 15 June 2005
  1. Ritossa FM. Experimental activation of specific loci in polytene chromosomes of Drosophila. Exp Cell Res 1964; 35 : 601–7. [Google Scholar]
  2. Schiller P, Amin J, Ananthan J, et al. Cis-acting elements involved in the regulated expression of a human HSP70 gene. J Mol Biol 1988; 203 : 97–105. [Google Scholar]
  3. Ananthan J, Goldberg AL, Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 1986; 232 : 522–4. [Google Scholar]
  4. 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 : 3788–96. [Google Scholar]
  5. Ellis RJ, Van der Vies SM, Hemmingsen SM. The molecular chaperone concept. Biochem Soc Symp 1989; 55 : 145–53. [Google Scholar]
  6. Young JC, Agashe VR, Siegers K, Hartl FU. Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol 2004; 5 ; 781–91. [Google Scholar]
  7. Ehrnsperger M, Lilie H, Gaestel M, Buchner J. The dynamics of hsp25 quaternary structure. Structure and function of different oligomeric species. J Biol Chem 1999; 274 : 14867–74. [Google Scholar]
  8. McDonough H, Patterson C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 2003; 8 : 303–8. [Google Scholar]
  9. Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994; 79 : 13–21. [Google Scholar]
  10. Arrigo AP, Tanaka K, Goldberg AL, Welch WJ. Identity of the 19S ’prosome’ particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature 1988; 331 : 192–4. [Google Scholar]
  11. Peters JM. Proteasomes: protein degradation machines of the cell. Trends Biochem Sci 1994; 19 : 377–82. [Google Scholar]
  12. Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001; 83 : 301–10. [Google Scholar]
  13. Demasi M, Davies KJ. Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism. FEBS Lett 2003; 542 : 89–94. [Google Scholar]
  14. Lee MH, Hyun DH, Jenner P, Halliwell B. Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production. J Neurochem 2001; 78 : 32–41. [Google Scholar]
  15. Robertson JD, Datta K, Biswal SS, Kehrer JP. Heat-shock protein 70 antisense oligomers enhance proteasome inhibitor-induced apoptosis. Biochem J 1999; 344 : 477–85. [Google Scholar]
  16. Agarwal S, Sohal RS. Aging and protein oxidative damage. Mech Ageing Dev 1994; 75 : 11–9. [Google Scholar]
  17. Grune T, Shringarpure R, Sitte N, Davies K. Age-related changes in protein oxidation and proteolysis in mammalian cells. J Gerontol A Biol Sci Med Sci 2001; 56 : B459–67. [Google Scholar]
  18. Carrard G, Bulteau A, Petropoulos I, Friguet B. Impairment of proteasome structure and function in aging. Int J Biochem Cell Biol 2002; 34 : 1461–70. [Google Scholar]
  19. Conconi M, Petropoulos I, Emod I, et al. Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90. Biochem J 1998; 333 : 407–15. [Google Scholar]
  20. De Maio, A. Heat shock proteins: facts, thoughts, and dreams. Shock 1999; 11 : 1–12. [Google Scholar]
  21. Mestril R. The use of transgenic mice to study cytoprotection by the stress proteins. Methods 2005; 35 : 165–9. [Google Scholar]
  22. Deshaies RJ, Koch BD, Schekman R. The role of stress proteins in membrane biogenesis. Trends Biochem Sci 1988; 13 : 384–8. [Google Scholar]
  23. Beckmann RP, Mizzen LE, Welch WJ. Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 1990; 248 : 850–4. [Google Scholar]
  24. Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 2002; 59 : 1640–8. [Google Scholar]
  25. Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 1998; 396 : 336–42. [Google Scholar]
  26. Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998; 92 : 351–66. [Google Scholar]
  27. Arrigo AP. In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation. J Cell Biochem 2005; 94 : 241–6. [Google Scholar]
  28. Mehlen P, Mehlen A, Godet J, Arrigo AP. Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells. J Biol Chem 1997; 272 : 31657–65. [Google Scholar]
  29. Mehlen P, Schulze-Osthoff K, Arrigo AP. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J Biol Chem 1996; 271 : 16510–4. [Google Scholar]
  30. Bruey JM, Ducasse C, Bonniaud P, et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2 : 645–52. [Google Scholar]
  31. Paul C, Manero F, Gonin S, et al. Hsp27 as a negative regulator of cytochrome c release. Mol Cell Biol 2002; 22 : 816–34. [Google Scholar]
  32. Halliwell B. Hypothesis. Proteasomal dysfunction: a primary event in neurogeneration that leads to nitrative and oxidative stress and subsequent cell death. Ann NY Acad Sci 2002; 962 : 182–94. [Google Scholar]
  33. Bates G. Huntingtin aggregation and toxicity in Huntington’s disease. Lancet 2003; 361 : 1642–4. [Google Scholar]
  34. Biasini E, Fioriti L, Ceglia I, et al. Proteasome inhibition and aggregation in Parkinson’s disease: a comparative study in untransfected and transfected cells. J Neurochem 2004; 88 : 545–53. [Google Scholar]
  35. Venkatraman R, Wetzel P, Tanaka M, et al. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 2004; 14 : 95–104. [Google Scholar]
  36. Wyttenbach A. Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis. J Mol Neurosci 2004; 23 : 69–96. [Google Scholar]
  37. Wyttenbach A, Sauvageot O, Carmichael J, et al. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 2002; 11 : 1137–51. [Google Scholar]
  38. Ravikumar B, Vacher C, Berger Z, et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004; 36 : 585–95. [Google Scholar]
  39. Jaattela M. Escaping cell death: survival proteins in cancer. Exp Cell Res 1999; 248 : 30–43. [Google Scholar]
  40. Chiosis G, Vilenchik M, Kim J, Solit D. Hsp90: the vulnerable chaperone. Drug Discov Today 2004; 9 : 881–8. [Google Scholar]

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