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.
Dates
Type | When |
---|---|
Created | 9 years, 10 months ago (Sept. 30, 2015, 3:40 p.m.) |
Deposited | 2 years, 8 months ago (Dec. 15, 2022, 8:53 a.m.) |
Indexed | 1 month ago (July 23, 2025, 8:51 a.m.) |
Issued | 38 years, 6 months ago (Feb. 1, 1987) |
Published | 38 years, 6 months ago (Feb. 1, 1987) |
Published Online | 38 years, 6 months ago (Feb. 1, 1987) |
Published Print | 38 years, 6 months ago (Feb. 1, 1987) |
@article{Matlashewski_1987, title={Primary structure polymorphism at amino acid residue 72 of human p53.}, volume={7}, ISSN={1098-5549}, url={http://dx.doi.org/10.1128/mcb.7.2.961}, DOI={10.1128/mcb.7.2.961}, number={2}, journal={Molecular and Cellular Biology}, publisher={Informa UK Limited}, author={Matlashewski, G J and Tuck, S and Pim, D and Lamb, P and Schneider, J and Crawford, L V}, year={1987}, month=feb, pages={961–963} }