L
Luciana P. Rangel
Researcher at Federal University of Rio de Janeiro
Publications - 31
Citations - 1131
Luciana P. Rangel is an academic researcher from Federal University of Rio de Janeiro. The author has contributed to research in topics: Protein aggregation & Cancer. The author has an hindex of 15, co-authored 28 publications receiving 855 citations. Previous affiliations of Luciana P. Rangel include Claude Bernard University Lyon 1 & University of Lyon.
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Journal ArticleDOI
Mutant p53 Aggregates into Prion-like Amyloid Oligomers and Fibrils IMPLICATIONS FOR CANCER
Ana Paula Dinis Ano Bom,Luciana P. Rangel,Danielly C. Ferraz da Costa,Guilherme A. P. de Oliveira,Daniel Sanches,Carolina A. Braga,Lisandra M. Gava,Lisandra M. Gava,Carlos H.I. Ramos,Carlos H.I. Ramos,Ana Oliva Tiroli Cepeda,Ana Carolina Stumbo,Claudia V. De Moura Gallo,Claudia V. De Moura Gallo,Yraima Cordeiro,Jerson L. Silva +15 more
TL;DR: It is concluded that aggregation of p53 into a mixture of oligomers and fibrils sequestrates the native protein into an inactive conformation that is typical of a prionoid.
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Prion-like aggregation of mutant p53 in cancer
Jerson L. Silva,Claudia V. De Moura Gallo,Claudia V. De Moura Gallo,Danielly C. Ferraz da Costa,Luciana P. Rangel +4 more
TL;DR: The shared properties of cancer and neurodegenerative diseases are discussed and how the prion-like properties of p53 aggregates offer potential targets for drug development.
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The aggregation of mutant p53 produces prion-like properties in cancer.
TL;DR: The prion-like behavior of oncogenic p53 mutants is reviewed that provides an explanation for their dominant-negative and gain-of-function properties and for the high metastatic potential of cancers bearing p53 mutations.
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Aggregation and Prion-Like Properties of Misfolded Tumor Suppressors: Is Cancer a Prion Disease?
Danielly C. Ferraz da Costa,Guilherme A. P. de Oliveira,Elio A. Cino,Iaci N. Soares,Luciana P. Rangel,Jerson L. Silva +5 more
TL;DR: The prion-like behavior of oncogenic p53 mutants provides an explanation for its dominant-negative and GoF properties, including the high metastatic potential of cancer cells carrying p53 mutations.
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Expanding the prion concept to cancer biology: dominant-negative effect of aggregates of mutant p53 tumour suppressor.
Jerson L. Silva,Luciana P. Rangel,Danielly C. Ferraz da Costa,Yraima Cordeiro,Claudia V. De Moura Gallo,Claudia V. De Moura Gallo +5 more
TL;DR: It is proposed that if p53 aggregation occurred, it would be a crucial aspect of cancer development, as p53 would lose its WT functions in an aggregated state, leading into gain of function in addition to the loss of tumour suppressor function.