Accès gratuit
Numéro
Med Sci (Paris)
Volume 18, Numéro 8-9, Août–Septembre 2002
Page(s) 841 - 852
Section M/S Revues : Articles De Synthèse
DOI https://doi.org/10.1051/medsci/20021889841
Publié en ligne 15 août 2002
  1. Vogt C. Untersuchungen über die Entwicklungsgeschichte der Geburtshelferkröte (Alytes obstreticans). Solothurn 1842. [Google Scholar]
  2. Kerr JF, Wyllie AH, Currie AR. Apoptosis : a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26 : 239–57. [Google Scholar]
  3. Wyllie AH, Golstein P. More than one way to go. Proc Natl Acad Sci USA 2001; 98 : 11–3. [Google Scholar]
  4. Leist M, Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol 2001; 2 : 589–98. [Google Scholar]
  5. Horvitz HR. Genetic control of programmed cell death in the nematode Caenorhabditis elegans. Cancer Res 1999; 59 (suppl) : 1701–6. [Google Scholar]
  6. Yuan J, Shaham S, Ledoux S, Ellis H, Horvitz H. The C. elegans cell-death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta converting enzyme. Cell 1993; 75 : 641–52. [Google Scholar]
  7. Budihardjo I, Oliver H, Lutter M, Luo X, Wang X. Biochemical pathways of caspase activation during apoptosis. Annu Rev Cell Biol 1999; 15 : 269–90. [Google Scholar]
  8. Thornberry NA, Lazebnik Y. Caspases : enemies within. Science 1998; 281 : 1312–6. [Google Scholar]
  9. Marzo I, Brenner C, Zamzami N, et al. The permeability transition pore complex: a target for apoptosis regulation by caspases and bcl-2-related proteins. J Exp Med 1998; 187 : 1261–71. [Google Scholar]
  10. Zamzami N, Kroemer G. The mitochondrion in apoptosis: how Pandora’s box opens. Nat Rev Mol Cell Biol 2001; 2 : 67–71. [Google Scholar]
  11. Martinou JC, Desagher S, Antonsson B. Cytochrome c release from mitochondria: all or nothing. Nat Cell Biol 2000; 2 : E41–3. [Google Scholar]
  12. Zou H, Li Y, Liu X, Wang X. An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem 1999; 274 : 11549–56. [Google Scholar]
  13. Susin SA, Lorenzo HK, Zamzami N, et al. Molecular characterization of mitochondrial apoptosisinducing factor. Nature 1999; 397 : 441–6. [Google Scholar]
  14. Locksley RM, Killeen N, Lenardo MJ. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 2001; 104 : 487–501. [Google Scholar]
  15. Siegel RM, Chan FK, Chun HJ, Lenardo MJ. The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity. Nat Immunol 2000; 1 : 469–74. [Google Scholar]
  16. Kischkel FC, Hellbardt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995; 14 : 5579–88. [Google Scholar]
  17. Orlinick JR, Vaishnaw A, Elkon KB, Chao MV. Requirement of cysteinerich repeats of the Fas receptor for binding by the Fas ligand. J Biol Chem 1997; 272 : 28889–94. [Google Scholar]
  18. Siegel RM, Frederiksen JK, Zacharias DA, et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 2000; 288 : 2354–7. [Google Scholar]
  19. Papoff G, Hausler P, Eramo A, et al. Identification and characterization of a ligand-independent oligomerization domain in the extracellular region of the CD95 death receptor. J Biol Chem 1999; 274 : 38241–50. [Google Scholar]
  20. Scaffidi C, Fulda S, Srinivasan A, et al. Two CD95 (APO-1/Fas) signaling pathways. EMBO J 1998; 17 : 1675–87. [Google Scholar]
  21. Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94 : 481–90. [Google Scholar]
  22. Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000; 20 : 929–35. [Google Scholar]
  23. Zhang H, Xu Q, Krajewski S, et al. BAR: an apoptosis regulator at the intersection of caspases and Bcl-2 family proteins. Proc Natl Acad Sci USA 2000; 97 : 2597–602. [Google Scholar]
  24. Feldman M, Taylor P, Paleolog E, Brennan FM, Maini RN. Anti-TNF alpha therapy is useful in rheumatoid arthritis and Crohn’s disease: analysis of the mechanism of action predicts utility in other diseases. Transplant Proc 1998; 30 : 4126–7. [Google Scholar]
  25. Jenkins M, Keir M, McCune JM. A membrane-bound Fas decoy receptor expressed by human thymocytes. J Biol Chem 2000; 275 : 7988–93. [Google Scholar]
  26. Pitti RM, Marsters SA, Lawrence DA, et al. Genomic amplification of a decoy receptor for Fas ligand in lung and colon cancer. Nature 1998; 396 : 699–703. [Google Scholar]
  27. Hueber AO, Bernard AM, Hérincs Z, Couzinet A, He HT. An essential role of membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes. EMBO Rep 2002; 3 : 190–6. [Google Scholar]
  28. Irmler M, Thome M, Hahne M, et al. Inhibition of death receptor signals by cellular FLIP. Nature 1997; 388 : 190–5. [Google Scholar]
  29. Krueger A, Schmitz I, Baumann S, Krammer PH, Kirchhoff S. Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex. J Biol Chem 2001; 276 : 20633–40. [Google Scholar]
  30. Jiang Y, Woronicz JD, Liu W, Goeddel DV. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 1999; 283 : 543–6. [Google Scholar]
  31. Adams JM, Cory S. The Bcl-2 protein family: arbiters of cell survival. Science 1998; 281 : 1322–6. [Google Scholar]
  32. Crompton M. Bax, Bid and the permeabilization of the mitochondrial outer membrane in apoptosis. Curr Opin Cell Biol 2000; 12 : 414–9. [Google Scholar]
  33. Schendel SL, Montal M, Reed JC. Bcl-2 family proteins as ion-channels. Cell Death Differ 1998; 5 : 372–80. [Google Scholar]
  34. Fesik SW, Shi Y. Structural biology. Controlling the caspases. Science 2001; 294 : 1477–8. [Google Scholar]
  35. Holcik M, Gibson H, Korneluk RG. XIAP: apoptotic brake and promising therapeutic target. Apoptosis 2001; 6 : 253–61. [Google Scholar]
  36. Ferri KF, Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol 2001; 3 : E255–63. [Google Scholar]
  37. Jacobson MD, Burne JF, Raff MC. Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J 1994; 13 : 1899–910. [Google Scholar]
  38. Wang ZG, Delva L, Gaboli M, et al. Role of PML in cell growth and the retinoic acid pathway. Science 1998; 279 : 1547–51. [Google Scholar]
  39. Yang X, Khosravi-Far R, Chang H, Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 1997; 89 : 1067–76. [Google Scholar]
  40. Chang HY, Nishitoh H, Yang X, Ichijo H, Baltimore D. Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. Science 1998; 281 : 1860–3. [Google Scholar]
  41. Li H, Leo C, Zhu J, et al. Sequestration and inhibition of Daxxmediated transcriptional repression by PML. Mol Cell Biol 2000; 20 : 1784–96. [Google Scholar]
  42. Torii S, Egan DA, Evans RA, Reed JC. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J 1999; 18 : 6037–49. [Google Scholar]
  43. Zhong S, Salomoni P, Ronchetti S, Guo A, Ruggero D, Pandolfi PP.. Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med 2000; 191 : 631–40. [Google Scholar]
  44. Charette SJ, Lavoie JN, Lambert H, Landry J. Inhibition of Daxxmediated apoptosis by heat shock protein 27. Mol Cell Biol 2000; 20 : 7602–12. [Google Scholar]
  45. Rochat-Steiner V, Becker K, Micheau O, Schneider P, Burns K, Tschopp J. FIST/HIPK3: a Fas/FADDinteracting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH(2)-terminal kinase activation. J Exp Med 2000; 192 : 1165–74. [Google Scholar]
  46. Liston P, Fong WG, Kelly NL, et al. Identification of XAF1 as an antagonist of XIAP anti-caspase activity. Nat Cell Biol 2001; 3 : 128–33. [Google Scholar]
  47. Stegh AH, Schickling O, Ehret A, et al. DEDD, a novel death effector domaincontaining protein, targeted to the nucleolus. EMBO J 1998; 17 : 5974–86. [Google Scholar]
  48. Schickling O, Stegh AH, Byrd J, Peter ME. Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription. Cell Death Differ 2001; 8 : 1157–68. [Google Scholar]
  49. Zheng L, Schickling O, Peter ME, Lenardo MJ. The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm. J Biol Chem 2001; 276 : 31945–52. [Google Scholar]

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