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Previous Volume 353:1489-1501 October 6, 2005 Number 14 Next

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Cells maintain a complete set of functionally competent proteins normally and in the face of injury or stress with the use of various mechanisms, including systems of proteins called molecular chaperones.¹ The typical function of a chaperone is to assist a nascent polypeptide chain to attain a functional conformation as a new protein and then to assist the protein's arrival at the site in the cell where the protein carries out its functions. It has become increasingly clear that disruption of chaperoning mechanisms contributes to aging and disease. This review outlines the involvement of defective chaperones in senescence and in . . . [Full Text of this Article]

Protein Quality Control and Antistress Mechanisms

Cellular Stress and Protein Damage

Heat-Shock Proteins and Chaperones

Chaperoning Machines

Chaperonopathies

Acquired Chaperonopathies

Acquired Chaperonopathies Associated with Aging and Disease

Hsp70 and Hsp90 in Aging

Crystallins in Neurodegenerative Diseases, Myositis, Cataracts, and Retinopathy

            Neurodegenerative Disease

            Inclusion-Body Myositis

            Cataracts

            Retinopathy

Other Pathologic Conditions Involving Chaperones

Von Hippel–Lindau Disease

Autoantibodies against Chaperones

Chaperonopathies and Malfunction of the Immune System

Chaperone-Gene Polymorphisms

Genetic Chaperonopathies

Prospects for the Future

Source Information

From the Wadsworth Center, Division of Molecular Medicine, New York State Department of Health (A.J.L.M., E.C.M.); and the Department of Biomedical Sciences, School of Public Health, State University of New York at Albany (A.J.L.M.) — both in Albany.

Address reprint requests to Dr. A.J.L. Macario at the Wadsworth Center, Room B-749, Division of Molecular Medicine, New York State Department of Health, Empire State Plaza, P.O. Box 509, Albany, NY 12201-0509, or at macario@wadsworth.org.

Related Letters:

Chaperones and Disease
Adewoye A. H., McMahon L., Mavropoulos J. C., Fields T. A., Pizzo S. V., Levy Y., Gorshtein A., Macario A. J.L., de Macario E. C.
Extract | Full Text | PDF  
N Engl J Med 2005; 353:2821-2822, Dec 29, 2005. Correspondence

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