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Modulation of p53 and prion protein aggregation by RNA

Biochimica Et Biophysica Acta. Proteins and Proteomics

Mar 4, 2019

Yraima CordeiroJerson L Silva

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Abstract

Several RNA-binding proteins undergo reversible liquid-liquid phase transitions, which, in pathological conditions, might evolve into transitions to solid-state phases, giving rise to amyloid structures. Amyloidogenic and prion-like proteins, such as the tumor suppressor protein p53 and...read more

Mentioned in this Paper

Major Prion Protein
Mutant Proteins
TP53
Amyloid Proteins
Protein Aggregation, Pathological
Amyloid
Binding (Molecular Function)
Structure
Malignant Neoplasms
RNA-Binding Proteins
3
19
Paper Details
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Modulation of p53 and prion protein aggregation by RNA

Biochimica Et Biophysica Acta. Proteins and Proteomics

Mar 4, 2019

Yraima CordeiroJerson L Silva

PMID: 30826454

DOI: 10.1016/j.bbapap.2019.02.006

Abstract

Several RNA-binding proteins undergo reversible liquid-liquid phase transitions, which, in pathological conditions, might evolve into transitions to solid-state phases, giving rise to amyloid structures. Amyloidogenic and prion-like proteins, such as the tumor suppressor protein p53 and...read more

Mentioned in this Paper

Major Prion Protein
Mutant Proteins
TP53
Amyloid Proteins
Protein Aggregation, Pathological
Amyloid
Binding (Molecular Function)
Structure
Malignant Neoplasms
RNA-Binding Proteins
3
19

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ALS: Prions

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The aggregation of mutant p53 produces prion-like properties in cancer

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Biochemical and Biophysical Research Communications

Dual role of p53 amyloid formation in cancer; loss of function and gain of toxicity

Biochemical and Biophysical Research CommunicationsDecember 25, 2012
Cristian A Lasagna-ReevesRakez Kayed
Paper Details
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  • finger pointing at paper

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