Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


BIR3 Domain Plasma Membrane Calcium ATPase Permeability Transition Pore Complex Deoxyadenosine Triphosphate Apoptosis Figure 
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References and Further Reading

General References

  1. Igney FH, and Krammer PH [2002]. Death and anti-death: Tumor resistance to apoptosis. Nature Rev. Cancer, 2: 277–288.CrossRefGoogle Scholar
  2. Johnstone RW, Ruefli AA, and Lowe SW [2002]. Apoptosis: A link between cancer genetics and chemotherapy. Cell, 108: 153–164.CrossRefGoogle Scholar
  3. Mattson MP [2000]. Apoptosis in neurodegenerative disorders. Nature Rev. Mol. Cell Biol., 1: 120–129.CrossRefGoogle Scholar
  4. Meier P, Finch A, and Evan G [2000]. Apoptosis in development. Nature, 407: 796–801.CrossRefADSGoogle Scholar
  5. Vila M, and Przedborski S [2003]. Targeting programmed cell death in neurodegenerative diseases. Nature Rev. Neurosci., 4: 1–11.Google Scholar


  1. Boatright KM, et al. [2003]. A unified model for apical caspase activation. Mol. Cell, 11: 529–541.CrossRefGoogle Scholar
  2. Chai JJ, et al. [2001]. Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding. Cell, 107: 399–407.CrossRefGoogle Scholar
  3. Chang DW, et al. [2003]. Interdimer processing mechanism of procaspase-8 activation. EMBO J., 22: 4132–4142.CrossRefGoogle Scholar
  4. Shi YG [2002]. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell, 9: 459–479.CrossRefGoogle Scholar
  5. Stennicke HR, and Salvesen GS [2000]. Caspases—Controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta, 1477: 299–306.CrossRefGoogle Scholar

Bcl-2 Proteins

  1. Cheng EHYA, et al. [2001]. Bcl-2, BclxL sequester BH3 domain only molecules preventing BAX-and BAK-mediated mitochondrial apoptosis. Mol. Cell, 8: 705–711.CrossRefGoogle Scholar
  2. Cory S, and Adams JM [2002]. The Bcl-2 family: Regulators of the cellular life-or-death switch. Nature Rev. Cancer, 2: 647–656.CrossRefGoogle Scholar
  3. Gross A, McDonnell JM, and Korsmeyer SJ [1999]. Bcl-2 family members and the mitochondria in apoptosis. Genes Dev., 13: 1899–1911.CrossRefGoogle Scholar
  4. Letai A, et al. [2002]. Distinct BH3 only domain either sensitize or activate mitochondrial apoptosis, serving as prototypes cancer therapeutics. Cancer Cell, 2: 183–192.CrossRefGoogle Scholar
  5. Moreau C, et al. [2003]. Minimal BH3 peptides promote cell death by antagonizing anti-apoptotic proteins. J. Biol. Chem., 278: 19426–19435.CrossRefGoogle Scholar
  6. Scorrano L, et al. [2002]. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev. Cell, 2: 55–67.CrossRefGoogle Scholar

DISC Signaling

  1. Enari M, et al. [1998]. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature, 391: 43–50.CrossRefADSGoogle Scholar
  2. Nagata S [1997]. Apoptosis by death factor. Cell, 88: 355–365.CrossRefGoogle Scholar
  3. Scaffidi C, et al. [1998]. Two CD95 (APO-1/Fas) signaling pathways. EMBO J., 17: 1675–1687.CrossRefGoogle Scholar
  4. Weber CH, and Vincenz C [2001]. The death domain superfamily: A tale of two interfaces? Trends Biochem. Sci., 26: 475–481.CrossRefGoogle Scholar

Regulation of the Apoptotic Signaling Pathways by NF-κB

  1. Karin M, and Lin A [2002]. NF-κB at the crossroads of life and death. Nature Immunology, 3: 221–227.CrossRefGoogle Scholar
  2. Mayo CY, et al. [1998]. NF-κB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase 8 activation. Science, 281: 1680–1683.CrossRefADSGoogle Scholar

Permeability Transition Pore Complex

  1. Crompton M [1999]. The mitochondrial permeability transition pore and its role in cell death. Biochem. J., 341, pt. 2: 233–249.CrossRefGoogle Scholar
  2. Ott M, et al. [2002]. Cytochrome c release from mitochondria proceeds by a two-step process. Proc. Natl. Acad. Sci. USA, 99: 1259–1263.CrossRefADSGoogle Scholar
  3. Susin SA, Zamzami N, and Kroemer G [1998]. Mitochondria as regulators of apoptosis: Doubt no more. Biochim. Biophys. Acta., 1366: 151–165.CrossRefGoogle Scholar

Apoptosome Assembly

  1. Acehan D, et al. [2002]. Three-dimensional structure of the apoptosome: Implications for assembly, pro-caspase-9 binding, and activation. Mol. Cell, 9: 423–432.CrossRefGoogle Scholar
  2. Bratton SB, et al. [2001]. Recruitment, activation and retention of caspase-9 and-3 by Apaf-1 apoptosome and associated XIAP complexes. EMBO J., 20: 998–1009.CrossRefGoogle Scholar

Inhibitor of Apoptosis Proteins

  1. Huang HK, et al. [2000]. The inhibitor of apoptosis, cIAP2, functions as a ubiquitinprotein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J. Biol. Chem., 275: 26661–26664.Google Scholar
  2. Salvesen GS, and Duckett CS [2002]. IAP proteins: Blocking the road to death’s door. Nature Rev. Mol. Cell Biol., 3: 401–410.CrossRefGoogle Scholar
  3. Suzuki Y, Nakabayashi Y, and Takahashi R [2001]. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteosomal degradation and caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. Proc. Natl. Acad. Sci. USA, 98: 8662–8667.CrossRefADSGoogle Scholar
  4. Yang Y, et al. [2000]. Ubiquitin protein ligase activity of IAPs and their degradation in proteosomes in response to apoptotic stimuli. Science, 288: 874–877.CrossRefADSGoogle Scholar

IAP Counterregulators Smac/DIABLO and Omi/HtrA2

  1. Holley CL, et al. [2002]. Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition. Nature Cell Biol., 4: 439–444.CrossRefADSGoogle Scholar
  2. Nicholson DW [2002]. Baiting death inhibitors. Nature, 410: 33–34.CrossRefADSGoogle Scholar
  3. Srinivasula SM, et al. [2001]. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase acytivity and apoptosis. Nature, 410: 112–116.CrossRefADSGoogle Scholar
  4. Yoo SJ, et al. [2002]. Hid, Ror and Grim negatively regulate DIAP1 levels through distinct mechanisms. Nature Cell Biol., 4: 416–424.CrossRefGoogle Scholar

Mitochondrial Physiology

  1. Duchen MR [2000]. Mitochondria and calcium: From cell signaling to cell death. J. Physiol., 529: 57–68.CrossRefADSGoogle Scholar
  2. Jacobson J, and Duchen MR [2002]. Mitochondrial oxidative stress and cell death in astrocytes—Requirement for stored Ca2+ and sustained opening of the permeability transition pore. J. Cell Sci., 115: 1175-1188.Google Scholar
  3. Kowaltowski AJ, Castilho RF, and Vercesi AE [2001]. Mitochondrial permeability transition and oxidative stress. FEBS Lett., 495: 12–15.CrossRefGoogle Scholar
  4. Marchetti P [1997]. Redox regulation of apoptosis: Impact of thiol oxidation status on mitochondrial function. Eur. J. Immunol., 27: 289–296.CrossRefGoogle Scholar
  5. Ricci JE, Gottlieb RA, and Green DR [2003]. Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis. J. Cell Biol., 160: 65–75.CrossRefGoogle Scholar

ER and Calcium Signals to the Mitochondria

  1. Boehning D, et al. [2003]. Cytochrome c binds to inositol (1,4,5) triphosphate receptors, amplifying calcium-dependent apoptosis. Nature Cell Biol., 5: 1051–1061.CrossRefGoogle Scholar
  2. Li C, et al. [2002]. Bcl-xL affects Ca2+ homeostasis by altering expression of inositol 1,4,5-triphosphate receptors. Proc. Natl. Acad. Sci. USA, 99: 9830–9835.CrossRefADSGoogle Scholar
  3. Nutt LK. et al. [2002]. Bax-mediated Ca2+ mobilization promotes cytochrome c release during apoptosis. J. Biol. Chem., 277: 20301–20308.CrossRefGoogle Scholar
  4. Orrenius S, Zhivotovsky B, and Nicotera P [2003]. Regulation of cell death: The calcium-apoptosis link. Nature Rev. Mol. Cell Biol., 4: 552–565.CrossRefGoogle Scholar
  5. Scorrano L, et al. [2003]. BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis. Science, 300: 135–139.CrossRefADSGoogle Scholar

p53 Regulation

  1. Flores ER [2002]. p63 and p73 are required for p53-dependent apoptosis in response to DNA damage. Nature, 416: 560–564.CrossRefADSGoogle Scholar
  2. Mihara M, et al. [2003]. p53 has a direct apoptogenic role at the mitochondria. Mol. Cell, 11: 577–590.CrossRefGoogle Scholar
  3. Vousden KH, and Lu X [2002]. Live or let die: The cell’s response to p53. Nature Rev. Cancer, 2: 594–604.CrossRefGoogle Scholar

Cancer Therapy

  1. Herr I, and Debatin KM [2001]. Cellular stress response and apoptosis in cancer therapy. Blood, 98: 2603–2614.CrossRefGoogle Scholar
  2. Johnstone RW, Ruefli AA, and Lowe SW [2002]. Apoptosis: A link between cancer genetics and chemotherapy. Cell, 108: 153–164.CrossRefGoogle Scholar
  3. Kaufmann SH, and Earnshaw WC [2000]. Induction of apoptosis by cancer chemotherapy. Exp. Cell Res., 256: 42–49.CrossRefGoogle Scholar
  4. Nicholson DW [2000]. From bench to clinic with apoptosis-based therapeutic agents. Nature, 407: 810–816.CrossRefADSGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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