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Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization

We have measured the stability and stoichiometry of variants of the human p53 tetramerization domain to assess the effects of mutation on homo- and hetero-oligomerization. The residues chosen for mutation were those in the hydrophobic core that we had previously found to be critical for its stabilit...

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Bibliografiset tiedot
Julkaisussa:Proc Natl Acad Sci U S A
Päätekijät: Mateu, Mauricio G., Fersht, Alan R.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 1999
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Linkit:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC22339/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10097082/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.7.3595
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