Structure–function–rescue: the diverse nature of common p53 cancer mutants
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cancer Research,Genetics,Molecular Biology
Link
http://www.nature.com/articles/1210291.pdf
Reference124 articles.
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2. Ang HC, Joerger AC, Mayer S, Fersht AR . (2006). Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains. J Biol Chem 281: 21934–21941.
3. Balagurumoorthy P, Sakamoto H, Lewis MS, Zambrano N, Clore GM, Gronenborn AM et al. (1995). Four p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA. Proc Natl Acad Sci USA 92: 8591–8595.
4. Baroni TE, Wang T, Qian H, Dearth LR, Truong LN, Zeng J et al. (2004). A global suppressor motif for p53 cancer mutants. Proc Natl Acad Sci USA 101: 4930–4935.
5. Bell S, Klein C, Muller L, Hansen S, Buchner J . (2002). p53 contains large unstructured regions in its native state. J Mol Biol 322: 917–927.
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