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Previous Volume 356:79-81 January 4, 2007 Number 1 Next

	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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The p53 tumor-suppressor protein is dysfunctional in most human cancers. Even when p53 is not itself mutant, its regulators — such as p14^ARF — are often altered. Moreover, for any given cancer type, p53 dysfunction generally correlates with poor treatment response and poor prognosis, so restoration of p53 function is a potential avenue for therapeutic development.

The p53 protein is a key responder to a variety of stresses, including DNA damage, hypoxia, and cell-cycle aberrations. The specific molecular pathways that activate p53 depend on the nature of the stress and the cell type. These, in turn, determine the specific downstream . . . [Full Text of this Article]

Source Information

From the Department of Genetics and the Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill School of Medicine, Chapel Hill.

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