Evidence map›Paper›PMID 36230470›Full record

ReviewCancers2022

Regulating the p53 Tumor Suppressor Network at PML Biomolecular Condensates.

Magdalena C Liebl, Thomas G Hofmann

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Disulfide cross-linked redox-sensitive peptide condensates are efficient cell delivery vehicles of molecular cargo.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Anticancer Activity ofBiomolecules · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Discovery of a 6-Aminobenzo[ACS pharmacology & translational science · 2024
    Article
  8. Article
  9. Article
  10. Cellular senescence: Neither irreversible nor reversible.The Journal of experimental medicine · 2024
    Article
  11. Review
  12. Article
  13. The PML hub: An emerging actor of leukemia therapies.The Journal of experimental medicine · 2023
    Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

Magdalena C LieblInstitute of Toxicology, University Medical Center Mainz, Johannes Gutenberg University, 55131 Mainz, Germany.ORCID 0000-0002-0685-7107
Thomas G HofmannInstitute of Toxicology, University Medical Center Mainz, Johannes Gutenberg University, 55131 Mainz, Germany.ORCID 0000-0003-0547-2720
Johannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By forming specific functional entities, nuclear biomolecular condensates play an important function in guiding biological processes. PML biomolecular condensates, also known as PML nuclear bodies (NBs), are macro-molecular sub-nuclear organelles involved in central biological processes, including anti-viral response and cell fate control upon genotoxic stress. PML condensate formation is stimulated upon cellular stress, and relies on protein-protein interactions establishing a PML protein meshwork capable of recruiting the tumor suppressor p53, along with numerous modifiers of p53, thus balancing p53 posttranslational modifications and activity. This stress-regulated process appears to be controlled by liquid-liquid phase separation (LLPS), which may facilitate regulated protein-unmixing of p53 and its regulators into PML nuclear condensates. In this review, we summarize and discuss the molecular mechanisms underlying PML nuclear condensate formation, and how these impact the biological function of p53 in driving the cell death and senescence responses. In addition, by using an in silico approach, we identify 299 proteins which share PML and p53 as binding partners, thus representing novel candidate proteins controlling p53 function and cell fate decision-making at the level of PML nuclear biocondensates.

Indexed as

biomolecular condensatescell deathcellular senescenceDNA damageliquid–liquid phase separationnuclear bodyp53PMLSUMO

Identifiers

PMID36230470
PMCPMC9558958
OpenAlexW4296468177

What OpenQuestion 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 OpenQuestion graph.