Primary structure polymorphism at amino acid residue 72 of human p53.
Open Access
- 1 February 1987
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 7 (2) , 961-963
- https://doi.org/10.1128/mcb.7.2.961
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.This publication has 18 references indexed in Scilit:
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