Evidence map›Paper›PMID 15610066›Full record

ArticleThe Biochemical journal2005

A new class of glutathione S-transferase from the hepatopancreas of the red sea bream Pagrus major.

Takafumi Konishi, Keitaro Kato, Toshiyoshi Araki, Kentaro Shiraki, Masahiro Takagi, Yutaka Tamaru

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Purification and properties of glutathione S-transferase from the pike liver.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2013
    Article
  11. Article
  12. Article
  13. Molecular mechanisms of microcystin toxicity in animal cells.International journal of molecular sciences · 2010
    Review
  14. Article
  15. Crystallization and preliminary X-ray diffraction analysis of a glutathione S-transferase from Xylella fastidiosa.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  16. Article
  17. Marine glutathione S-transferases.Marine biotechnology (New York, N.Y.)
    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

6 authors at 4 institutions in 1 country.

Takafumi KonishiDepartment of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, Mie 514-8507, Japan.
Keitaro Kato
Toshiyoshi Araki
Kentaro Shiraki
Masahiro Takagi
Yutaka Tamaru
Japan Advanced Institute of Science and Technology · JPMie University · JPKindai University · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To elucidate drug deposition and metabolism in cultured marine fishes, in a previous study we isolated and purified the GSTs (glutathione S-transferases) from the hepatopancreas of the red sea bream Pagrus major that contained 25 and 28 kDa GST subunits. The 25 kDa GST subunits encoded by two genes (GSTA1 and GSTA2) have been identified as Alpha-class GSTs. In the present study, we performed the molecular cloning and characterization of the GSTR1 gene encoding the 28 kDa GST subunit from the Pa. major hepatopancreas. The nucleotide sequence of GSTR1 was composed of an ORF (open reading frame) of 675 bp encoding a protein of 225 residues with a predicted molecular mass of 25.925 Da. A search of the BLAST protein database revealed that the deduced amino acid sequence of GSTR1 was structurally similar to that of GSTs derived from other fishes such as largemouth bass (Micropterus salmoides) and plaice (Pleuronectes platessa). The genomic DNA containing the GSTR1 gene was found to consist of six exons and five introns quite distinct from mammalian Theta-class GSTs. We have purified and characterized the recombinant GSTR1 enzyme (pmGSTR1-1) which showed activity only towards 1-chloro-2,4-dinitrobenzene, although it had no detectable activity towards cumene hydroperoxide, 1,2-dichloro-4-nitrobenzene, ethacrynic acid, 4-hydroxynonenal and p-nitrobenzyl chloride. Moreover, pmGSTR1-1 revealed remarkable heat instability (melting temperature Tm=30.3+/-0.11 degrees C). Collectively, our results indicated that the characteristic GST genes including GSTR1 have been conserved and functional in fishes. Therefore we designate them 'Rho-class', a new class of GSTs.

Indexed as

Amino Acid SequenceAnimalsBase SequenceEnzyme StabilityFemaleGlutathione TransferaseHepatopancreasHydrogen-Ion ConcentrationMolecular Sequence DataPerciformesProtein DenaturationSequence Homology, Amino AcidTemperatureGlutathione Transferase

Identifiers

PMID15610066
PMCPMC1186719
OpenAlexW2019473255

What OpenQuestion holds

Textmetadata
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.