Evidence map›Paper›PMID 20712413›Full record

ReviewAntioxidants & redox signaling2011

Bacillithiol, a new player in bacterial redox homeostasis.

John D Helmann

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The glutathione pathway is required for biofilm formation inCurrent research in microbial sciences · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Liquid Phase Electron Microscopy of Bacterial Ultrastructure.Small (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Structure of BrxA from Staphylococcus aureus, a bacilliredoxin involved in redox homeostasis in Firmicutes.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  16. Article
  17. CaninePathogens (Basel, Switzerland) · 2022
    Article
  18. Article
  19. Article
  20. 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

1 author at 1 institution in 1 country.

John D HelmannDepartment of Microbiology, Cornell University, Ithaca, New York 14853-8101, USA. jdh9@cornell.edu
Cornell University · US

Funding

Zinc Homeostasis in Bacillus subtilisR01GM059323 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HELMANN, JOHN D · 2000 to 2017
$4.5M
NIGMS NIH HHS GM059323
6 · The paper itself

Abstract

Bacillithiol (BSH), the α-anomeric glycoside of l-cysteinyl-d-glucosamine with l-malic acid, plays a dominant role in the cytosolic thiol redox chemistry of the low guanine and cytosine (GC) Gram-positive bacteria (phylum Firmicutes). BSH is functionally analogous to glutathione (GSH) but differs sufficiently in chemical structure that cells have evolved a distinct set of enzymes that use BSH as cofactor. BSH was discovered in Bacillus subtilis as a mixed disulfide with the redox-sensing repressor OhrR and in B. anthracis by biochemical analysis of pools of labeled thiols. The structure of BSH was determined after purification from Deinococcus radiodurans. Similarities in structure between BSH and mycothiol (MSH) facilitated the identification of biosynthetic genes for BSH in the model organism B. subtilis. Phylogenomic analyses have identified several candidate BSH-using or associated proteins, including a BSH reductase, glutaredoxin-like thiol-dependent oxidoreductases (bacilliredoxins), and a BSH-S-transferase (FosB) involved in resistance to the epoxide antibiotic fosfomycin. Preliminary results implicate BSH in cellular processes to maintain cytosolic redox balance and for adaptation to reactive oxygen, nitrogen, and electrophilic species. BSH also is predicted to chelate metals avidly, in part due to the appended malate moiety, although the implications of BSH for metal ion homeostasis have yet to be explored in detail.

Indexed as

CysteineGlucosamineHomeostasisModels, BiologicalOxidation-ReductionSulfhydryl CompoundsbacillithiolCysteineGlucosamineSulfhydryl Compounds

Identifiers

PMID20712413
PMCPMC3110096
OpenAlexW2084563469

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.