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Science 8 November 1996:
Vol. 274. no. 5289, pp. 921 - 922
DOI: 10.1126/science.274.5289.921

Research News

Elizabeth Pennisi

Because the p53 protein plays a critical role in protecting cells against cancer, researchers want to understand all aspects of its structure and function. In work reported in this issue (p. 948), researchers have now solved the three-dimensional structure of one previously unvisualized section of the protein--a key regulatory region in association with its regulator, a protein called MDM2. In an accompanying paper (p. 1001), they also take a look at p53's interaction with another protein that may be involved in controlling the tumor suppressor's activity.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
NMR Spectroscopy Reveals the Solution Dimerization Interface of p53 Core Domains Bound to Their Consensus DNA.
C. Klein, E. Planker, T. Diercks, H. Kessler, K.-P. Kunkele, K. Lang, S. Hansen, and M. Schwaiger (2001)
J. Biol. Chem. 276, 49020-49027
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Science. ISSN 0036-8075 (print), 1095-9203 (online)