Evidence map›Paper›PMID 30739016›Full record

ArticleiScience2019

Anomalous Dense Liquid Condensates Host the Nucleation of Tumor Suppressor p53 Fibrils.

Mohammad S Safari, Zhiqing Wang, Kunaal Tailor, Anatoly B Kolomeisky, Jacinta C Conrad, Peter G Vekilov

Abstract read
In one paragraph

Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

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  20. Protein conformation and biomolecular condensates.Current research in structural biology · 2022
    Review
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

6 authors.

Mohammad S SafariDepartment of Chemical and Biomolecular Engineering, University of Houston, 4726 Calhoun Road, Houston, TX 77204-4004, USA; Department of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, USA.
Zhiqing WangDepartment of Chemical and Biomolecular Engineering, University of Houston, 4726 Calhoun Road, Houston, TX 77204-4004, USA.
Kunaal TailorDepartment of Chemical and Biomolecular Engineering, University of Houston, 4726 Calhoun Road, Houston, TX 77204-4004, USA.
Anatoly B KolomeiskyDepartment of Chemistry, Rice University, P.O. Box 1892, MS 60, Houston, TX 77251-1892, USA. Electronic address: tolya@rice.edu.
Jacinta C ConradDepartment of Chemical and Biomolecular Engineering, University of Houston, 4726 Calhoun Road, Houston, TX 77204-4004, USA. Electronic address: jcconrad@uh.edu.
Peter G VekilovDepartment of Chemical and Biomolecular Engineering, University of Houston, 4726 Calhoun Road, Houston, TX 77204-4004, USA; Department of Chemistry, University of Houston, 3585 Cullen Boulevard, Houston, TX 77204-5003, USA. Electronic address: vekilov@uh.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

About half of human cancers are associated with mutations of the tumor suppressor p53. Gained oncogenic functions of the mutants have been related to aggregation behaviors of wild-type and mutant p53. The thermodynamic and kinetic mechanisms of p53 aggregation are poorly understood. Here we find that wild-type p53 forms an anomalous liquid phase. The liquid condensates exhibit several behaviors beyond the scope of classical phase transition theories: their size, ca. 100 nm, is independent of the p53 concentration and decoupled from the protein mass held in the liquid phase. Furthermore, the liquid phase lacks constant solubility. The nucleation of p53 fibrils deviates from the accepted mechanism of sequential association of single solute molecules. We find that the liquid condensates serve as pre-assembled precursors of high p53 concentration that facilitate fibril assembly. Fibril nucleation hosted by precursors represents a novel biological pathway, which opens avenues to suppress protein fibrillation in aggregation diseases.

Indexed as

Biological SciencesBiophysicsChemistry

Identifiers

PMID30739016
PMCPMC6369220

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Registered trials

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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.