Evidence map›Paper›PMID 23543141›Full record

ArticleFish physiology and biochemistry2013

Cloning, molecular characterization and expression analysis of heat shock cognate 70 (Hsc70) cDNA from turbot (Scophthalmus maximus).

T T Wang, N Wang, X L Liao, L Meng, Y Liu, S L Chen

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Article in Fish physiology and biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

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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

4 citing papers in PubMed, 9 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

6 authors at 1 institution in 1 country.

T T WangYellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, 106 Nanjing Road, Qingdao, 266071, China.
N Wang
X L Liao
L Meng
Y Liu
S L Chen
Chinese Academy of Fishery Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As an essential member of the HSP70 family, heat shock cognate 70 (Hsc70) is a constitutively expressed molecular chaperone involved in protein metabolism. In this paper, turbot Hsc70 was cloned and the expression profile was also analyzed. The full-length cDNA of the turbot Hsc70 was 2,292 bp in length, including a 113-bp 5' UTR, a 223-bp 3' UTR and a 1,956-bp open reading frame coding a protein with 651 amino acid residues. Comparison of amino acid sequence revealed the existence of three classical HSP70 family signature motifs, a signature nonapeptide and one repeat of tetrapeptide in turbot Hsc70. The turbot Hsc70-deduced amino acids sequence exhibited 75.4-96.8 % homology with Hsp70s/Hsc70s of 24 other known sequences. In particular, the strongest homology was found with the cognate members of Hsc70 subfamily and the highest identity was found with Japanese flounder Hsc70. Semi-quantitative RT-PCR revealed that turbot Hsc70 transcripts were stably expressed in all tested tissues under normal physiological condition, while the expression levels also increased (~1.5-fold to ~threefold) after heat shock and bacterial infection. In addition, Hsc70 transcripts were detected throughout embryonic development and in turbot embryonic cell line (TEC) in the absence of any stress. Meanwhile, it was also heat inducible, but not cold inducible in TEC. These results suggest that Hsc70 gene may be involved in embryogenesis and cellular protection events under normal and stress condition.

Indexed as

Amino Acid SequenceAnimalsBase SequenceEmbryonic DevelopmentFlatfishesGene Expression Regulation, DevelopmentalHSC70 Heat-Shock ProteinsMolecular Sequence DataSequence Analysis, DNASequence Homology, Amino AcidHSC70 Heat-Shock Proteins

Identifiers

PMID23543141
OpenAlexW2000453673

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Registered trials

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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.