Evidence map›Paper›PMID 28754007›Full record

ArticleGenes2017

Developmental Expression of HSP60 and HSP10 in the Coilia nasus Testis during Upstream Spawning Migration.

Di-An Fang, Yan-Feng Zhou, Min-Ying Zhang, Dong-Po Xu, Kai Liu, Jin-Rong Duan

Open access · goldAbstract read
In one paragraph

Article in Genes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. 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

6 authors at 1 institution in 1 country.

Di-An FangFreshwater Fisheries Research Center, Chinese Academy of Fishery Sciences, Shanshui Road 9, Wuxi 214000, Jiangsu, China. fangda@ffrc.cn.
Yan-Feng ZhouFreshwater Fisheries Research Center, Chinese Academy of Fishery Sciences, Shanshui Road 9, Wuxi 214000, Jiangsu, China. zhouyf@ffrc.cn.
Min-Ying ZhangFreshwater Fisheries Research Center, Chinese Academy of Fishery Sciences, Shanshui Road 9, Wuxi 214000, Jiangsu, China. zhangmy@ffrc.cn.
Dong-Po XuFreshwater Fisheries Research Center, Chinese Academy of Fishery Sciences, Shanshui Road 9, Wuxi 214000, Jiangsu, China. xudp@ffrc.cn.
Kai LiuFreshwater Fisheries Research Center, Chinese Academy of Fishery Sciences, Shanshui Road 9, Wuxi 214000, Jiangsu, China. liuk@ffrc.cn.
Jin-Rong DuanFreshwater Fisheries Research Center, Chinese Academy of Fishery Sciences, Shanshui Road 9, Wuxi 214000, Jiangsu, China. duanjr@ffrc.cn.
Chinese Academy of Fishery Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein 60 (HSP60) and heat shock protein 10 (HSP10) are important chaperones, which have been proven to have essential roles in mediating the correct folding of nuclear encoded proteins imported to mitochondria. Mitochondria are known as the power house of the cell, with which it produces energy and respires aerobically. In this regard, the obtained HSP60 and HSP10 have typical characteristics of the HSP60/10 family signature. Their mRNA transcripts detected were highest during the developmental phase (in April), while the lowest levels were found in the resting phase (after spawning in late July). Additionally, the strongest immunolabeling positive signals were found in the primary spermatocyte, with lower positive staining in secondary sperm cells, and a weak or absent level in the mature sperm. At the electron microscopic level, immunogold particles were localized in the mitochondrial matrix. Data indicated that HSP10 and HSP60 were inducible and functional in the Coilia nasus testis development and migration process, suggesting their essential roles in this process. The results also indicated that HSP60 may be one indicator of properly working mitochondrial import and refolding in the fish testis. This study also provides an expanded perspective on the role of heat shock protein families in spawning migration biology.

Indexed as

Coilia nasusHeat shock protein 10Heat shock protein 60Spawning Migration

Identifiers

PMID28754007
PMCPMC5541322
OpenAlexW2736352191

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.