Evidence map›Paper›PMID 8645150›Full record

ArticleThe Biochemical journal1996

Purification and characterization of a recombinant human Theta-class glutathione transferase (GSTT2-2).

K L Tan, P G Board

Abstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Glutathione transferases.The arabidopsis book · 2010
    Article
  10. Article
  11. Article
  12. Article
  13. Evolution of highly active enzymes by homology-independent recombination.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  14. Article
  15. Article
  16. Article
  17. 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

2 authors.

K L TanDivision of Molecular Medicine, John Curtin School of Medical Research, Australian National University, Canberra, Australia.
P G Board

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A cDNA encoding the human Theta-class glutathione transferase GSTT2-2 was expressed in Escherichia coli as a ubiquitin fusion protein. The co-translational removal of the ubiquitin by a cloned ubiquitin-specific protease, Ubp1, generates enzymically active GSTT2-2 without any additional N-terminal residues. The recombinant isoenzyme was purified to apparent homogeneity by DEAE anion-exchange, gel filtration, dye ligand chromatography and high resolution anion-exchange chromatography on Mono Q FPLC. The recombinant enzyme had significant activity with a range of substrates, including cumene hydroperoxide and 1-menapthyl sulphate. The activity of GSTT2-2 with a range of secondary lipid peroxidation products such as the trans,trans-alka-2,4-dienals and trans-alk-2-enals, as well as its glutathione peroxidase activity with organic hydroperoxides, suggest that it may play a significant role in protection against the products of lipid peroxidation.

Indexed as

Base SequenceDNA, ComplementaryDNA PrimersEscherichia coliGenetic VectorsGlutathione TransferaseHumansIn Vitro TechniquesIsoenzymesMolecular Sequence DataRecombinant Fusion ProteinsSubstrate SpecificityUbiquitinsDNA, ComplementaryDNA PrimersGlutathione TransferaseGSTT2 protein, humanIsoenzymesRecombinant Fusion ProteinsUbiquitins

Identifiers

PMID8645150
PMCPMC1217267

What OpenQuestion holds

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Read underepoch 390

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.