Evidence map›Paper›PMID 17682821›Full record

ReviewMarine biotechnology (New York, N.Y.)

Marine glutathione S-transferases.

Brian Blanchette, Xia Feng, Bal Ram Singh

Abstract readReview
PubMed Publisher
In one paragraph

Review in Marine biotechnology (New York, N.Y.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 212 citations in OpenAlex.

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  9. FirstFrontiers in microbiology · 2019
    Article
  10. Molecular Cloning and Expression ofInternational journal of molecular sciences · 2018
    Article
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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

3 authors at 1 institution in 1 country.

Brian BlanchetteDepartment of Chemistry and Biochemistry, University of Massachusetts Dartmouth, Dartmouth, MA 02747, USA.
Xia Feng
Bal Ram Singh
University of Massachusetts Dartmouth · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aquatic environment is generally affected by the presence of environmental xenobiotic compounds. One of the major xenobiotic detoxifying enzymes is glutathione S-transferase (GST), which belongs to a family of multifunctional enzymes involved in catalyzing nucleophilic attack of the sulfur atom of glutathione (gamma-glutamyl-cysteinylglycine) to an electrophilic group on metabolic products or xenobiotic compounds. Because of the unique nature of the aquatic environment and the possible pollution therein, the biochemical evolution in terms of the nature of GSTs could by uniquely expressed. The full complement of GSTs has not been studied in marine organisms, as very few aquatic GSTs have been fully characterized. The focus of this article is to present an overview of the GST superfamily and their critical role in the survival of organisms in the marine environment, emphasizing the critical roles of GSTs in the detoxification of marine organisms and the unique characteristics of their GSTs compared to those from non-marine organisms.

Indexed as

AnimalsFishesGlutathione TransferaseInvertebratesMarine BiologyPhylogenyProtein ConformationSeawaterWater Pollutants, ChemicalWater Pollution, ChemicalGlutathione TransferaseWater Pollutants, Chemical

Identifiers

PMID17682821
OpenAlexW2086534923

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.