Title : p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes.

Pub. Date : 2000 Oct 1

PMID : 10998350






6 Functional Relationships(s)
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1 p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes. pyrrolidine dithiocarbamic acid tumor protein p53 Homo sapiens
2 p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes. pyrrolidine dithiocarbamic acid tumor protein p53 Homo sapiens
3 p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes. pyrrolidine dithiocarbamic acid tumor protein p53 Homo sapiens
4 Treatment of MCF7 breast cancer cells with pyrrolidine dithiocarbamate (PDTC), a metal chelator, resulted in a minimum of 25% oxidation of p53. pyrrolidine dithiocarbamic acid tumor protein p53 Homo sapiens
5 Treatment of MCF7 breast cancer cells with pyrrolidine dithiocarbamate (PDTC), a metal chelator, resulted in a minimum of 25% oxidation of p53. pyrrolidine dithiocarbamic acid tumor protein p53 Homo sapiens
6 However, when cells were simultaneously treated with PDTC and actinomycin D, p53 accumulated in both the nucleus and the cytoplasm. pyrrolidine dithiocarbamic acid tumor protein p53 Homo sapiens