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H4. Recent Links and References

  • Page ID
    4796
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    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)

    This page titled H4. Recent Links and References is shared under a CC BY-NC-SA license and was authored, remixed, and/or curated by Henry Jakubowski.

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