Evidence map›Paper›PMID 36232329›Full record

ReviewInternational journal of molecular sciences2022

Anticancer Therapeutic Strategies Targeting p53 Aggregation.

Giulia D S Ferretti, Julia Quarti, Gileno Dos Santos, Luciana P Rangel, Jerson L Silva

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Big versus small: The impact of aggregate size in disease.Protein science : a publication of the Protein Society · 2023
    Review
  11. Article
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

5 authors at 1 institution in 1 country.

Giulia D S FerrettiInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.
Julia QuartiInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.
Gileno Dos SantosInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.ORCID 0000-0002-2668-8670
Luciana P RangelFaculty of Pharmacy, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.ORCID 0000-0002-6154-0815
Jerson L SilvaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.ORCID 0000-0001-9523-9441
Universidade Federal do Rio de Janeiro · BR

Funding

Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro 202840/2018Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro 210008/2018National Council for Scientific and Technological Development 408046/2021-0National Council for Scientific and Technological Development 465395/2014-7
6 · The paper itself

Abstract

p53 is a tumor suppressor protein that is mutated in more than 50% of cancer cases. When mutated, it frequently results in p53 oncogenic gain of function (GOF), resulting in a greater tendency to aggregate in the phase separation and phase transition pathway. GOFs related to p53 aggregation include chemoresistance, which makes therapy even more difficult. The therapies available for the treatment of cancer are still quite limited, so the study of new molecules and therapeutic targets focusing on p53 aggregates is a promising strategy against cancer. In this review, we classify anticancer molecules with antiaggregation properties into four categories: thiol alkylating agents, designed peptides, agents with chaperone-based mechanisms that inhibit p53 aggregation, and miscellaneous compounds with anti-protein aggregation properties that have been studied in neurodegenerative diseases. Furthermore, we highlight autophagy as a possible degradation pathway for aggregated p53. Here, considering cancer as a protein aggregation disease, we review strategies that have been used to disrupt p53 aggregates, leading to cancer regression.

Indexed as

NeoplasmsTumor Suppressor Protein p53Alkylating AgentsHumansMutationPeptidesSulfhydryl CompoundsTumor Suppressor ProteinsAlkylating AgentsPeptidesSulfhydryl CompoundsTumor Suppressor Protein p53Tumor Suppressor Proteinscancerp53protein aggregation

Identifiers

PMID36232329
PMCPMC9569952
OpenAlexW4296741805

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.