Evidence map›Paper›PMID 25279558›Full record

ArticlePloS one2014

JMY functions as actin nucleation-promoting factor and mediator for p53-mediated DNA damage in porcine oocytes.

Zili Lin, Yong-Nan Xu, Suk Namgoong, Nam-Hyung Kim

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Zili LinDepartment of Animal Sciences, Chungbuk National University, Cheongju, Korea.
Yong-Nan XuDepartment of Animal Sciences, Chungbuk National University, Cheongju, Korea.
Suk NamgoongDepartment of Animal Sciences, Chungbuk National University, Cheongju, Korea.
Nam-Hyung KimDepartment of Animal Sciences, Chungbuk National University, Cheongju, Korea.
Chungbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Junction-mediating and regulatory protein(JMY) is a multifunctional protein with roles in the transcriptional co-activation of p53 and the regulation of actin nucleation promoting factors and, hence, cell migration; however, its role in the maturation of porcine oocytes is unclear. In the current study, we investigated functional roles of JMY in porcine oocytes. Porcine oocytes expressed JMY mRNA and protein, and the mRNA expression level decreased during oocyte maturation. Knockdown of JMY by RNA interference decreased the rate of polar body extrusion, validating its role in the asymmetric division of porcine oocytes. JMY knockdown also down-regulated the mRNA and protein levels of actin and Arp2/3. Furthermore, JMY accumulated in the nucleus in response to DNA damage, and JMY knockdown suppressed DNA damage-mediated p53 activation. In conclusion, our results show that JMY has important roles in oocyte maturation as a regulator of actin nucleation-promoting factors and an activator of p53 during DNA damage during DNA damages in porcine oocytes.

Indexed as

Actin-Related Protein 2-3 ComplexActinsAnimalsDNA DamageFemaleGene Knockdown TechniquesMeiosisModels, GeneticNuclear ProteinsOocytesPolar BodiesSwineTrans-ActivatorsTubulinTumor Suppressor Protein p53Actin-Related Protein 2-3 ComplexActinsNuclear ProteinsTrans-ActivatorsTubulinTumor Suppressor Protein p53

Identifiers

PMID25279558
PMCPMC4184845
OpenAlexW2072797961

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.