Evidence map›Paper›PMID 33268817›Full record

ArticleBritish journal of cancer2021

Phosphatase, pseudo-phosphatase, or both? Understanding PRL oncogenicity.

Kalle Gehring, Hiroaki Miki

Erratum issuedOpen access · hybridAbstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in British journal of cancer, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. The Roles of Pseudophosphatases in Disease.International journal of molecular sciences · 2021
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Kalle GehringDepartment of Biochemistry and Centre de Recherche en Biologie Structurale, McGill University, Montreal, QC, Canada. kalle.gehring@mcgill.ca.ORCID http://orcid.org/0000-0001-6500-1184
Hiroaki MikiDepartment of Cellular Regulation, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
McGill University · CAThe University of Osaka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphatases of regenerating liver (PRL1-3) are among the most oncogenic protein phosphatases but their mechanism of action is poorly understood. Multiple substrates have been proposed as well as a non-catalytic function regulating magnesium transport. Our recent identification of a catalytically inactive PRL mutant that retains oncogenicity in a mouse model promises to resolve the question of whether PRLs act as phosphatases or pseudo-phosphatases in different cancer models.

Indexed as

Oncogene ProteinsProtein Tyrosine PhosphatasesAnimalsMiceOncogene ProteinsProtein Tyrosine Phosphatases

Identifiers

PMID33268817
PMCPMC7960985
OpenAlexW3106721187

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.