Evidence map›Paper›PMID 36497033›Full record

ArticleCells2022

Prolyl Isomerase, Pin1, Controls Meiotic Progression in Mouse Oocytes.

Yumi Hoshino, Takafumi Uchida

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 88% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. 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

2 authors at 2 institutions in 1 country.

Yumi HoshinoLaboratory of Animal Reproduction, Graduate School of Integrated Science for Life, Hiroshima University, Hiroshima 739-8528, Japan.ORCID 0000-0002-9364-132X
Takafumi UchidaLaboratory of Molecular Enzymology, Department of Molecular Cell Science, Graduate School of Agricultural Science, Tohoku University, Miyagi 981-8555, Japan.ORCID 0000-0003-3665-4906
Hiroshima University · JPTohoku University · JP

Funding

Japan Society for the Promotion of Science 19K06369Japan Society for the Promotion of Science 26712022
6 · The paper itself

Abstract

During meiotic maturation, accurate progression of meiosis is ensured by multiple protein kinases and by signal transduction pathways they are involved in. However, the mechanisms regulating the functions of phosphorylated proteins are unclear. Herein, we investigated the role of Pin1, a peptidyl-prolyl cis-trans isomerase family member that regulates protein functions by altering the structure of the peptide bond of proline in phosphorylated proteins in meiosis. First, we analyzed changes in the expression of Pin1 during meiotic maturation and found that although its levels were constant, its localization was dynamic in different stages of meiosis. Furthermore, we confirmed that the spindle rotates near the cortex when Pin1 is inhibited by juglone during meiotic maturation, resulting in an error in the extrusion of the first polar body. In Pin1

Indexed as

NIMA-Interacting Peptidylprolyl IsomeraseOocytesAnimalsFemaleMeiosisMiceMicrotubulesPhosphorylationNIMA-Interacting Peptidylprolyl IsomerasePin1 protein, mousemeiotic maturationmouseoocytephosphorylationPin1

Identifiers

PMID36497033
PMCPMC9739419
OpenAlexW4310211456

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.