Evidence map›Paper›PMID 15717864›Full record

ArticleThe Biochemical journal2005

Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme.

Rungrutai Udomsinprasert, Saengtong Pongjaroenkit, Jantana Wongsantichon, Aaron J Oakley, La-aied Prapanthadara, Matthew C J Wilce, Albert J Ketterman

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 42 papers, 5 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 5 pooled it
1.1field-weighted citation impact, top 24% 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

42 citing papers in PubMed, 5 syntheses or guidelines pooled it, 101 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Quantitative assessment of the effect of glutathione S-transferase genes GSTM1 and GSTT1 on hepatocellular carcinoma risk.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Pooled it
  4. Pooled it
  5. Pooled it
  6. Article
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  17. Dynamics of Oxidative Stress inDiagnostics (Basel, Switzerland) · 2022
    Article
  18. Review
  19. Association ofCanadian respiratory journal · 2022
    Article
  20. 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

7 authors at 4 institutions in 2 countries.

Rungrutai UdomsinprasertInstitute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, 25/25 Putthamonthol Road 4, Salaya, Nakon Pathom 73170, Thailand.
Saengtong Pongjaroenkit
Jantana Wongsantichon
Aaron J Oakley
La-aied Prapanthadara
Matthew C J Wilce
Albert J Ketterman
Mahidol University · THUniversity of Western Australia · AUChiang Mai University · THMaejo University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.

Indexed as

Amino Acid SequenceAnimalsAnophelesBase SequenceBinding SitesCrystallography, X-RayDNA, ComplementaryGenomicsGlutathione TransferaseIsoenzymesKineticsModels, MolecularMolecular Sequence DataPromoter Regions, GeneticProtein ConformationRecombinant ProteinsDNA, ComplementaryGlutathione TransferaseIsoenzymesRecombinant Proteins

Identifiers

PMID15717864
PMCPMC1183455
OpenAlexW2108893450

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.