Evidence map›Paper›PMID 28420731›Full record

ArticleThe Journal of biological chemistry2017

Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.

Petar Stefanov Kovachev, Debapriya Banerjee, Luciana Pereira Rangel, Jonny Eriksson, Murilo M Pedrote, Mafalda Maria D C Martins-Dinis, Katarina Edwards, Yraima Cordeiro, Jerson L Silva, Suparna Sanyal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 58 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Petar Stefanov KovachevFrom the Department of Cell and Molecular Biology, Uppsala University, Uppsala, Box-596, 75124, Sweden.ORCID 0000-0003-4448-6447
Debapriya BanerjeeFrom the Department of Cell and Molecular Biology, Uppsala University, Uppsala, Box-596, 75124, Sweden.
Luciana Pereira RangelFaculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21941-902, Brazil.ORCID 0000-0002-6154-0815
Jonny ErikssonDepartment of Chemistry, Uppsala University, Uppsala, 75124, Sweden, and.
Murilo M PedroteInstituto de Bioquímica Médica Leopoldo de Meis, Instituto Nacional de Ciência Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Mafalda Maria D C Martins-DinisInstituto de Bioquímica Médica Leopoldo de Meis, Instituto Nacional de Ciência Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Katarina EdwardsDepartment of Chemistry, Uppsala University, Uppsala, 75124, Sweden, and.ORCID 0000-0003-0674-2219
Yraima CordeiroFaculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21941-902, Brazil.ORCID 0000-0003-4278-212X
Jerson L SilvaInstituto de Bioquímica Médica Leopoldo de Meis, Instituto Nacional de Ciência Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.ORCID 0000-0001-9523-9441
Suparna SanyalFrom the Department of Cell and Molecular Biology, Uppsala University, Uppsala, Box-596, 75124, Sweden, suparna.sanyal@icm.uu.se.ORCID 0000-0002-7124-792X
Universidade Federal do Rio de Janeiro · BRUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inactivation of the tumor suppressor protein p53 by mutagenesis, chemical modification, protein-protein interaction, or aggregation has been associated with different human cancers. Although DNA is the typical substrate of p53, numerous studies have reported p53 interactions with RNA. Here, we have examined the effects of RNA of varied sequence, length, and origin on the mechanism of aggregation of the core domain of p53 (p53C) using light scattering, intrinsic fluorescence, transmission electron microscopy, thioflavin-T binding, seeding, and immunoblot assays. Our results are the first to demonstrate that RNA can modulate the aggregation of p53C and full-length p53. We found bimodal behavior of RNA in p53C aggregation. A low RNA:protein ratio (∼1:50) facilitates the accumulation of large amorphous aggregates of p53C. By contrast, at a high RNA:protein ratio (≥1:8), the amorphous aggregation of p53C is clearly suppressed. Instead, amyloid p53C oligomers are formed that can act as seeds nucleating

Indexed as

Protein AggregatesHumansProtein DomainsRNATumor Suppressor Protein p53Protein AggregatesRNATP53 protein, humanTumor Suppressor Protein p53amyloiddomain V of 23S rRNAfluorescencekineticsp53p53Cprionprotein aggregationprotein foldingRNA

Identifiers

PMID28420731
PMCPMC5454114
OpenAlexW2606102701

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.