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Biochem Biophys Res Commun. 1992 Dec 30;189(3):1701-8.

Phosphorylation-associated conformation shift of anti-oncogene phosphoprotein p53 in concanavalin-A activated human T lymphocytes.

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Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030.


A new radioimmunoassay for p53, employing an anti-peptide antibody directed against conserved Domain V, exhibited specificity for a relatively dephosphorylated form of p53. This form, correlated with the monoclonal antibody PAB421+ conformation, appeared transiently in the cytosol of cycloheximide-treated T cells undergoing activation by concanavalin-A/serum. Concurrently, there were decreased levels of p53 in the nucleus that correlated with increased phosphorylation of p53. After 90 min nuclear levels of p53 increased steadily above levels of unstimulated cells. Anti-p53 antibodies introduced into cells prior to stimulation enhanced cell proliferation in response to mitogens.

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