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- W2048489955 abstract "A crucial mechanism by which p53 transcription function is regulated appears to operate through control of its DNA-binding properties. Allosteric/conformational and steric mechanisms of latency and activation of p53 DNA-binding function have been proposed. Both are inconsistent with recent data obtained by NMR and fluorescence correlation spectroscopy. This article presents the two-binding sites mechanism, which postulates that p53 is not a latent DNA-binding factor but is involved in multiple interactions with DNA via its core- and C-terminal domains, and that in the p53 tetramer–DNA complexes, binding of the C-terminal-domain to DNA prevents interactions of the core domain with target DNA elements but not with nonspecific DNA sequences. We also discuss whether the conformations assumed by p53 when bound to structurally diverse target DNAs are crucial determinants of interaction with co-activators and co-repressors of transcription." @default.
- W2048489955 created "2016-06-24" @default.
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- W2048489955 date "2002-12-01" @default.
- W2048489955 modified "2023-09-30" @default.
- W2048489955 title "p53 latency – out of the blind alley" @default.
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- W2048489955 doi "https://doi.org/10.1016/s0968-0004(02)02209-0" @default.
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