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Modulation of p53 and prion protein aggregation by RNA
Univ Fed Rio de Janeiro, Fac Pharm, BR-21941902 Rio De Janeiro, Brazil.
Univ Fed Rio de Janeiro, Inst Bioquim Med Leopoldo Meis, Inst Nacl Ciencia Tecnol Biol Estrutural & Bioima, BR-21941902 Rio De Janeiro, Brazil.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Biology.ORCID iD: 0000-0003-4448-6447
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Biology.ORCID iD: 0000-0002-7124-792X
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2019 (English)In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1867, no 10, p. 933-940Article, review/survey (Refereed) Published
Abstract [en]

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 the mammalian prion protein (PrP), bind RNAs specifically or nonspecifically, resulting in changes in their propensity to undergo aggregation. Mutant p53 aggregation seems to play a crucial role in cancer through loss of function, negative dominance and gain of function. PrP conversion modulated by RNA results in highly toxic aggregates. Here, we review data on the modulatory action of RNAs on the aggregation of both proteins.

Place, publisher, year, edition, pages
2019. Vol. 1867, no 10, p. 933-940
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-393757DOI: 10.1016/j.bbapap.2019.02.006ISI: 000480375700008PubMedID: 30826454OAI: oai:DiVA.org:uu-393757DiVA, id: diva2:1355283
Available from: 2019-09-27 Created: 2019-09-27 Last updated: 2019-09-27Bibliographically approved

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Kovachev, Petar StefanovSanyal, Suparna

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