Molecular Biology of Conformational Diseases

  • Claude Reiss
  • Thierry Lesnik
  • Hasan Parvez
  • Simone Parvez
  • Ricardo Ehrlich
Part of the Advances in Behavioral Biology book series (ABBI, volume 53)


An important family of diseases is characterized by the presence of a disease-specific protein that accumulates as “amyloid” fibers and thereby becomes toxic to the cell. Although the protein has the authentic primary sequence (except in familial cases), it adopts a non-native conformation which resists proteolysis, allowing the protein to accumulate and form fibers. Non-familial amyloid conditions are clearly epigenetic.


Misfolded Protein Prion Disease Synonymous Codon Translation Rate Nascent Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Kelly J.W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8 101–106.PubMedCrossRefGoogle Scholar
  2. 2.
    Schubert U., Anton L.C., Gibbs J., Norbury C.C., Yewdell J.W. and Bennink J.R. (2000) Rapid degradation of a large fraction of newly synthesized proteins by proteasomes, Nature 404 770–773.PubMedCrossRefGoogle Scholar
  3. 3.
    Kopito R.R.(1997) ER quality control: the cytoplasmic connection. Cell 88 427–430.PubMedCrossRefGoogle Scholar
  4. 4.
    Solomovici J., Lesnik T. and Reiss R (1997) Does E.coli optimize the economics of the translation process. J. Theor. Biol. 185.511–521.PubMedCrossRefGoogle Scholar
  5. 5.
    Thanaraj T.A. and Argos P. (1996) Protein secondary structural types are differentially encoded in mRNA. Prot. Sci. 5 1973–1983.CrossRefGoogle Scholar
  6. 6.
    Lesnik T., Solomovici J., Deana A., Ehrlich R. and Reiss T (2000) Ribosome traffic in E.coli and regulation of gene expression. J. Theor. Biol. 202 175–185.PubMedCrossRefGoogle Scholar
  7. 7.
    Rüdiger S., Germeroth L., Schneider-Mergener J. and Bukau B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries EMBO J. 16 1501–1507.PubMedCrossRefGoogle Scholar
  8. 8.
    Komar A.A., Lesnik T. and Reiss C. (1999) Synonymous codon substitution affect ribosome traffic and protein folding during in vitro tarnslation FEBS Lett. (1999) 462 p387–391.PubMedCrossRefGoogle Scholar
  9. 9.
    Komar A.A., Lesnik T., Cullin C, Guillemet E., Ehrlich R. and Reiss T (1997) Differential resistance to proteinase T digestion of the yeast prion-like (Ure2p) protein synthesized in vitro in wheat germ extract and rabbit reticulocyte cell-free translation systems. FEBS Lett. 415 6–10.PubMedCrossRefGoogle Scholar
  10. 10.
    Emilsson V. and Kurland C.G. (1990) Growth rate dependence of transfer RNA abundance in E.coli? EMBO J. 94 359–4366.Google Scholar
  11. 11.
    Baumeister W., Walz J., Ziihl F., and Seemüller E. (1998) The Proteasome: paradigm of a self-compartmentalizing protease Cell 92 367–380.PubMedCrossRefGoogle Scholar
  12. 12.
    Hershko A. and Ciechanover A. (1998) The ubiquitin system In Ann Rev. Biochem, Richardson C.C. editor 67 425–480.Google Scholar

Copyright information

© Springer Science+Business Media New York 2002

Authors and Affiliations

  • Claude Reiss
    • 1
  • Thierry Lesnik
    • 1
  • Hasan Parvez
    • 2
  • Simone Parvez
    • 3
  • Ricardo Ehrlich
    • 4
  1. 1.Alzheim’R&DGifFrance
  2. 2.CNRS IAF GifFrance
  3. 3.Reims UniversityFrance
  4. 4.University of the RepublicMontevideo

Personalised recommendations