Mutant p53 Aggregates into Prion-like Amyloid Oligomers and Fibrils: IMPLICATIONS FOR CANCER

Over 50% of all human cancers lose p53 function. To evaluate the role of aggregation in cancer, we asked whether wild-type (WT) p53 and the hot-spot mutant R248Q could aggregate as amyloids under physiological conditions and whether the mutant could seed aggregation of the wild-type form. The centra...

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Detalles Bibliográficos
Autores principales: Ano Bom, Ana P. D., Rangel, Luciana P., Costa, Danielly C. F., de Oliveira, Guilherme A. P., Sanches, Daniel, Braga, Carolina A., Gava, Lisandra M., Ramos, Carlos H. I., Cepeda, Ana O. T., Stumbo, Ana C., De Moura Gallo, Claudia V., Cordeiro, Yraima, Silva, Jerson L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2012
Materias:
Protein Structure and Folding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431633/
https://www.ncbi.nlm.nih.gov/pubmed/22715097
http://dx.doi.org/10.1074/jbc.M112.340638

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431633/
https://www.ncbi.nlm.nih.gov/pubmed/22715097
http://dx.doi.org/10.1074/jbc.M112.340638

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