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. 1987 Feb;7(2):961–963. doi: 10.1128/mcb.7.2.961

Primary structure polymorphism at amino acid residue 72 of human p53.

G J Matlashewski, S Tuck, D Pim, P Lamb, J Schneider, L V Crawford
PMCID: PMC365159  PMID: 3547088

Abstract

We analyzed p53 cDNA and genomic clones from a variety of normal and transformed cells. Sequence analysis of these clones revealed that amino acid residue 72 can be an arginine, proline, or cysteine. This single codon difference results in electrophoretically distinct forms of human p53 seen in normal and transformed cells.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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