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Interaction of Tumor Suppressor p53 with DNA and Proteins

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p53, a tumor suppressor and a transcription factor, binds DNA in a sequence-specific manner. In more than half of human cancers, p53 has been found to be mutated with the loss of DNA-binding ability. In this review, we focus on the sensitive detection of interaction of tumor suppressor p53 with double-stranded DNA bearing the consensus sequence and proteins, such as monoclonal antibodies recognizing the p53 protein and metalloprotein. Relying on the specific binding of p53 to DNA and antibodies, quantitative determination of wild-type and mutant p53 proteins in normal and cancer cell lysates has been achieved.

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Keywords: DNA; Interaction; cell lysates; consensus sequence; metalloprotein; monoclonal antibodies; p53

Document Type: Research Article

Publication date: 2010-01-01

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  • Current Pharmaceutical Biotechnology aims to cover all the latest and outstanding developments in Pharmaceutical Biotechnology. Each issue of the journal contains a series of timely in-depth reviews written by leaders in the field covering a range of current topics in both pre-clinical and clinical areas of Pharmaceutical Biotechnology. Current Pharmaceutical Biotechnology is an essential journal for academic, clinical, government and pharmaceutical scientists who wish to be kept informed and up-to-date with the latest and most important developments.
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