Evidence map›Paper›PMID 18539744›Full record

ArticleJournal of bacteriology2008

Glutathione and transition-metal homeostasis in Escherichia coli.

Kerstin Helbig, Corinna Bleuel, Gerd J Krauss, Dietrich H Nies

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
7.2field-weighted citation impact, top 3% 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

104 citing papers in PubMed, 212 citations in OpenAlex.

  1. Article
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  5. TheJournal of proteome research · 2026
    Article
  6. The glutathione pathway is required for biofilm formation inCurrent research in microbial sciences · 2026
    Article
  7. Article
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  9. ABCC1 promotes GSH-dependent iron transport and resistance to Fe(II) and Cu(II) chelators.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
    Article
  10. Article
  11. Bacteria Under Metal Stress-Molecular Mechanisms of Metal Tolerance.International journal of molecular sciences · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Article
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  17. Article
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44 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Kerstin HelbigInstitute for Biology, Life Science Faculty, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str 3, 06099 Halle, Germany.
Corinna Bleuel
Gerd J Krauss
Dietrich H Nies
Institute for Medical Biology · PLMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutathione (GSH) and its derivative phytochelatin are important binding factors in transition-metal homeostasis in many eukaryotes. Here, we demonstrate that GSH is also involved in chromate, Zn(II), Cd(II), and Cu(II) homeostasis and resistance in Escherichia coli. While the loss of the ability to synthesize GSH influenced metal tolerance in wild-type cells only slightly, GSH was important for residual metal resistance in cells without metal efflux systems. In mutant cells without the P-type ATPase ZntA, the additional deletion of the GSH biosynthesis system led to a strong decrease in resistance to Cd(II) and Zn(II). Likewise, in mutant cells without the P-type ATPase CopA, the removal of GSH led to a strong decrease of Cu(II) resistance. The precursor of GSH, gamma-glutamylcysteine (gammaEC), was not able to compensate for a lack of GSH. On the contrary, gammaEC-containing cells were less copper and cadmium tolerant than cells that contained neither gammaEC nor GSH. Thus, GSH may play an important role in trace-element metabolism not only in higher organisms but also in bacteria.

Indexed as

HomeostasisAdenosine TriphosphatasesAnti-Bacterial AgentsCadmiumCopperDipeptidesDrug Resistance, BacterialEscherichia coliGene DeletionGlutathioneMetals, HeavyMutagenesis, InsertionalSulfhydryl CompoundsZincAdenosine TriphosphatasesAnti-Bacterial AgentsCadmiumCopperDipeptidesgamma-glutamylcysteineGlutathioneMetals, HeavySulfhydryl CompoundsZincZn(II)-translocating P-type ATPase

Identifiers

PMID18539744
PMCPMC2493246
OpenAlexW2171672250

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.