Biochemistry Online: An Approach Based on Chemical Logic

Biochemistry Online




Last Update:  03/10/16

Learning Goals/Objectives for Chapter 2H:  After class and this reading, students will be able to

  • describe experimental evidence to show that protein misfolding and aggregation depends on the amino acid sequence and the environment in which folding occurs.
  • describe conditions in vitro that may promote aggregation and how these might be minimized in vivo
  • describe alternative conformations of prion proteins and relate them to a energy topology landscape
  • explain how prion diseases may be transmitted in the absence of genetic material

H4.  Recent Links and References

  1. Wasmer, C. Amyloid Fibrils of the HET-s(218-289) Prion Form a b Solenoid with a Triangular Hydrophobic Core.  Science.  319, 1523 (2008)

  2. Balch, W. et al.  Adapting Proteostasis for Disease Intervention.  Science.  319, 916 (2008)

  3. Krishnan and Linquist, Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature, 435, 765 (2005)

  4. Ritter et al. Correlation of structural elements and infectivity of the HET-s prion. Nature, 435, 844 (2005)
  5. Nelson, R. et al. Structure of the cross-b spine of amyloid-like fibrils.  Nature 435, 773 (2005).
  6. Hardy and Selkoe. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics. Science 297, pg 353 (2002)
  7. Pepys et al. Targeted Pharmacological Depletion of Serum Amyloid P Component for Treatment of human amyloidosis.  Nature. 254, 231 and 254 (2002)
  8. Bucciantini et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416, pgs. 483, 507 (2002)
  9. Walsh et al. Naturally secreted oligomers of amyloid b protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416, pgs. 483, 535 (2002)
  10. Esler et al., A Portrait of Alzheimer Secretases - New Features and Familiar Faces. . Science. 293, pg 1449 (2001)
  11. Happarstrom et al. Trans-Suppression of Misfolding in an Amyloid Disease.  Science 293 pg 2459 (2001)
  12. An Inflammatory Drug Prospect (for Alzheimers). Nature. 414, pg 199 (2001)
  13. Saborio et al. Sensitive Detection of Pathological prion protein by cyclic amplification of protein misfolding.  Nature. 411, pg 810 (2001) 
  14. Bence et al. Impairment of the Ubiquitin-Proteasome System by Protein Aggregation. Science. 292, pg 1552 (2001)
  15. Cao et al. Elusive Protein Auditions for Several Roles (about APP in neural cells) Science. 293, pg 28, 115 (2001)
  16. Serio et al. Nucleated Conformational Conversion and the Replication of Conformational Information by a prion determinant.  Science. 289, pg 1317 (2000)
  17. Chien and Weissman. the Shape of a species barrier (in prion conformation transformation). Nature. 410, pg 161. 223 (2001)


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