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Science 329 (5988): 154-155

Copyright © 2010 by the American Association for the Advancement of Science


Clearing Conformational Disease

Richard N. Sifers

Research focused on defining the underlying characteristics of a disease can often lead to new treatment strategies. This is certainly the case for a rapidly expanding group of inherited diseases characterized by the toxic accumulation of a misfolded protein (1). Identifying, and then targeting, the cellular machinery responsible for orchestrating the degradation of these aberrant molecules, rather than correcting the mutations that cause them, represents a paradigm shift from the conventional wisdom associated with gene therapy. On page 229 of this issue, Hidvegi et al. (2) describe how a compound that stimulates autophagy—the process by which a cell destroys its own organelles through lysosomal compartments—can successfully eliminate the toxic effects of misfolded {alpha}1-antitrypsin protein in a preclinical mouse model of the associated liver disease (3).

Department of Pathology and Immunology, Baylor College of Medicine, Houston, TX 77030, USA.

E-mail: rsifers{at}

Histone Deacetylase Inhibitor (HDACi) Suberoylanilide Hydroxamic Acid (SAHA)-mediated Correction of {alpha}1-Antitrypsin Deficiency.
M. Bouchecareilh, D. M. Hutt, P. Szajner, T. R. Flotte, and W. E. Balch (2012)
J. Biol. Chem. 287, 38265-38278
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