Evidence map›Paper›PMID 38927053›Full record

ReviewBiomolecules2024

Recent Advances on Mutant p53: Unveiling Novel Oncogenic Roles, Degradation Pathways, and Therapeutic Interventions.

Marco Cordani, Alessia Garufi, Rossella Benedetti, Marco Tafani, Michele Aventaggiato, Gabriella D'Orazi, Mara Cirone

Abstract readReview
In one paragraph

Review in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Decoding the NRF2-NOTCH Crosstalk in Lung Cancer-An Update.Antioxidants (Basel, Switzerland) · 2025
    Review
  8. Article
  9. Drug Target Investigation ofAntioxidants (Basel, Switzerland) · 2024
    Article
  10. Covalent Modification of p53 by (ACS pharmacology & translational science · 2024
    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

7 authors.

Marco CordaniDepartment of Biochemistry and Molecular Biology, Faculty of Biological Sciences, Complutense University of Madrid, 28040 Madrid, Spain.ORCID 0000-0001-9342-4862
Alessia GarufiUnit of Cellular Networks and Molecular Therapeutic Targets, IRCCS Regina Elena National Cancer Institute, 00144 Rome, Italy.
Rossella BenedettiDepartment of Experimental Medicine, University La Sapienza, 00161 Rome, Italy.ORCID 0000-0002-1825-9112
Marco TafaniDepartment of Experimental Medicine, University La Sapienza, 00161 Rome, Italy.ORCID 0000-0001-7128-810X
Michele AventaggiatoDepartment of Experimental Medicine, University La Sapienza, 00161 Rome, Italy.ORCID 0000-0002-9466-0047
Gabriella D'OraziUnit of Cellular Networks and Molecular Therapeutic Targets, IRCCS Regina Elena National Cancer Institute, 00144 Rome, Italy.ORCID 0000-0001-6876-9105
Mara CironeDepartment of Experimental Medicine, University La Sapienza, 00161 Rome, Italy.ORCID 0000-0002-2207-9624

Funding

European Union NextGenerationEU/PRTR RYC2021-031003IItalian Association for Cancer Research grant IG 2019-23040MICIU/AEI/10.13039/501100011033 RYC2021-031003ISapienza University of Rome Grant Ateneo 2023
6 · The paper itself

Abstract

The p53 protein is the master regulator of cellular integrity, primarily due to its tumor-suppressing functions. Approximately half of all human cancers carry mutations in the TP53 gene, which not only abrogate the tumor-suppressive functions but also confer p53 mutant proteins with oncogenic potential. The latter is achieved through so-called gain-of-function (GOF) mutations that promote cancer progression, metastasis, and therapy resistance by deregulating transcriptional networks, signaling pathways, metabolism, immune surveillance, and cellular compositions of the microenvironment. Despite recent progress in understanding the complexity of mutp53 in neoplastic development, the exact mechanisms of how mutp53 contributes to cancer development and how they escape proteasomal and lysosomal degradation remain only partially understood. In this review, we address recent findings in the field of oncogenic functions of mutp53 specifically regarding, but not limited to, its implications in metabolic pathways, the secretome of cancer cells, the cancer microenvironment, and the regulating scenarios of the aberrant proteasomal degradation. By analyzing proteasomal and lysosomal protein degradation, as well as its connection with autophagy, we propose new therapeutical approaches that aim to destabilize mutp53 proteins and deactivate its oncogenic functions, thereby providing a fundamental basis for further investigation and rational treatment approaches for TP53-mutated cancers.

Indexed as

NeoplasmsProteolysisTumor MicroenvironmentTumor Suppressor Protein p53AnimalsAutophagyCarcinogenesisHumansLysosomesMutationProteasome Endopeptidase ComplexProteasome Endopeptidase ComplexTP53 protein, humanTumor Suppressor Protein p53cancer secretomechaperone-mediated autophagy (CMA)extracellular vesiclesheat shock proteins (HSP)MDM2mutant p53proteasometumor microenvironmentubiquitination

Identifiers

PMID38927053
PMCPMC11201733

What OpenQuestion holds

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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.