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Clinical Implications of Basic Research
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Volume 357:1150-1152 September 13, 2007 Number 11
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On Prions, Proteasomes, and Mad Cows
Alfred L. Goldberg, Ph.D.

Since this article has no abstract, we have provided an extract of the first 100 words of the full text and any section headings.

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All cells have the capacity to selectively degrade misfolded intracellular proteins, which, if they accumulated, could interfere with normal function and could be toxic. Such proteins may arise by mutation, errors in gene expression, failure to fold correctly, spontaneous denaturation, or postsynthetic damage (for example, by oxygen radicals). How often such events occur in cells is uncertain, largely because the ubiquitin–proteasome pathway rapidly degrades such aberrant proteins, including those that cause various inherited diseases, such as cystic fibrosis and certain hemoglobinopathies.1

This pathway also protects against neurodegenerative diseases.1,2 The hallmarks of amyotrophic lateral sclerosis, Parkinson's disease, Lewy-body dementia, Huntington's disease, . . . [Full Text of this Article]


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From the Department of Cell Biology, Harvard Medical School, Boston.



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