Evidence map›Paper›PMID 33860088›Full record

ArticleMolecular & cellular oncology2021

Cell-to-cell transmission of p53 aggregates: a novel player in oncology?

Naoyuki Iwahashi, Midori Ikezaki, Hiroyuki Saito, Kenji Uchimura, Kazuchika Nishitsuji

Abstract read
In one paragraph

Article in Molecular & cellular oncology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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.

Naoyuki IwahashiDepartment of Obstetrics and Gynecology, Wakayama Medical University, Wakayama, Japan.ORCID https://orcid.org/0000-0002-6422-325X
Midori IkezakiDepartment of Biochemistry, Wakayama Medical University, Wakayama, Japan.ORCID https://orcid.org/0000-0003-3629-3629
Hiroyuki SaitoDepartment of Biophysical Chemistry, Kyoto Pharmaceutical University, Kyoto, Japan.
Kenji UchimuraUnité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Université de Lille, Villeneuve d'Ascq, France.ORCID https://orcid.org/0000-0003-3009-248X
Kazuchika NishitsujiDepartment of Biochemistry, Wakayama Medical University, Wakayama, Japan.ORCID https://orcid.org/0000-0003-3056-8310

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mutants of the tumor suppressor protein p53 form protein aggregates. It has been proposed that these aggregates propagate like prions, albeit the detailed mechanism of the propagation is unclear. Our recent study revealed that sulfated glycosaminoglycans, especially highly sulfated domains of heparan sulfate (heparan sulfate S-domains), participate in cancer pathology by mediating transcellular propagation of p53 aggregates.

Indexed as

glycosaminoglycanheparan sulfatep53prionprotein aggregates

Identifiers

PMID33860088
PMCPMC8018399

What OpenQuestion holds

Textmetadata
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.