Evidence map›Paper›PMID 35155881›Full record

ReviewACS omega2022

P53: Stability from the Ubiquitin-Proteasome System and Specific 26S Proteasome Inhibitors.

Andressa Barban do Patrocinio, Vanderlei Rodrigues, Lizandra Guidi Magalhães

Open access · goldAbstract readReview
In one paragraph

Review in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 29 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

3 authors at 2 institutions in 1 country.

Andressa Barban do PatrocinioResearch Group on Natural Products (Center for Research in Sciences and Technology), Universidade de Franca, Av. Dr. Armando de Sales Oliveira, 201 - Parque Universitário, Franca, São Paulo 14404-600, Brazil.ORCID https://orcid.org/0000-0002-1734-7620
Vanderlei RodriguesDepartment of Biochemistry and Immunology, Ribeirão Preto Medical School, Universidade de São Paulo, Avenida Bandeirantes 3900, Ribeirão Preto, São Paulo 14049-900, Brazil.
Lizandra Guidi MagalhãesResearch Group on Natural Products (Center for Research in Sciences and Technology), Universidade de Franca, Av. Dr. Armando de Sales Oliveira, 201 - Parque Universitário, Franca, São Paulo 14404-600, Brazil.ORCID https://orcid.org/0000-0003-2959-6752
Universidade de Franca · BRUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein p53 is degraded by the 26S proteasome, a protein complex that breaks down cellular proteins. Degradation begins with activation of the protein ubiquitin (Ub) by the ubiquitin-activating E1 enzymes, ubiquitin-conjugating E2 enzymes, and ubiquitin E3 ligases, linking Ub or the polyubiquitin chain to p53 and marking it for degradation by the 26S proteasome. E3 ubiquitin ligases participate in this process and regulate p53 stability. There are compounds that inhibit the 26S proteasome and interfere at the p53 level, and some of these inhibitors are used to treat cancer and other diseases and can stabilize tumor suppressor proteins through the p53 pathway. This review discusses how the ubiquitin-proteasome system, p53, and these compounds are related.

Identifiers

PMID35155881
PMCPMC8829948
OpenAlexW4210342072

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.