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Vol. 50, Issue 4, 493-514, December 1998
Department of Pharmacology (D.F.S.), University of
Nebraska Medical Center, Omaha, Nebraska;
Department of Pediatrics
(L.W., E.K.), Steele Memorial Children's Research Center, University
of Arizona, Tucson, Arizona
I. Protein Folding in the Cell
II. Molecular and Chemical Chaperones
A. Heat Shock Response and Heat Shock Proteins
B. Chaperone-Mediated Nascent Chain Folding
C. Cytoplasmic Co-chaperones
D. Endoplasmic Reticulum: A Special Folding Environment
E. Cellular Chemicals That Favor Protein Folding
III. Chaperone-Mediated Regulation of Signal Transduction Pathways
IV. Protein Misfolding in Disease
A. Cancer and Inactive or Inappropriately Acting Mutant Proteins
B. Cystic Fibrosis and Diversion in Folding Pathways
C. Amyloid Diseases and Protein Aggregation
1. Alzheimer's disease.
2. Huntington's disease.
3. Prion diseases.
V. Natural Products That Bind Chaperone Components
A. Molecules That Bind Immunophilins
B. Molecules That Bind Hsp70
1. Background.
2. Hsp70-15-deoxyspergualin interactions.
3. 15-Deoxyspergualin biological activities.
C. Molecules That Bind Hsp90
1. Background.
2. Hsp90-15-deoxyspergualin interactions.
3. Hsp90-benzoquinone ansamycin interactions.
4. Hsp90-radicicol interactions.
5. Biological activities.
VI. Prospective Therapeutic Rationales That Involve Chaperones
A. Drugs Targeting Specific Chaperone Activities
1. Immunophilins.
2. Hsp70.
3. Hsp90.
B. Induction of Protein and Chemical Chaperones
1. Background.
2. Mechanisms for inducing chaperone activity.
3. Injury protection.
4. Enhanced utilization of mutant proteins.
C. Chaperones as Immunological Adjuvants
VII. Summary
Acknowledgments
References
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