Evidence map›Paper›PMID 20018758›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.

Rachel J Dutton, April Wayman, Jun-Rong Wei, Eric J Rubin, Jon Beckwith, Dana Boyd

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.7field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Distinct enzymatic strategies forCritical reviews in biochemistry and molecular biology · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Disulfide bond formation in prokaryotes.Nature microbiology · 2018
    Review
  17. Review
  18. Structural basis for catalysis at the membrane-water interface.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  19. 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

6 authors at 1 institution in 1 country.

Rachel J DuttonDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
April Wayman
Jun-Rong Wei
Eric J Rubin
Jon Beckwith
Dana Boyd
Harvard University · US

Funding

Drug Targets for TuberculosisR01AI071881 · NIAID · HARVARD SCHOOL OF PUBLIC HEALTH · PI RUBIN, ERIC J. · 2009 to 2010
$802k
NIAID NIH HHS AI071881NIAID NIH HHS R01 AI071881PHS HHS GMO41883
6 · The paper itself

Abstract

Blood coagulation in humans requires the activity of vitamin K epoxide reductase (VKOR), the target of the anticoagulant warfarin (Coumadin). Bacterial homologs of VKOR were recently found to participate in a pathway leading to disulfide bond formation in secreted proteins of many bacteria. Here we show that the VKOR homolog from the bacterium Mycobacterium tuberculosis, the causative agent of human tuberculosis, is inhibited by warfarin and that warfarin-resistant mutations of mycobacterial VKOR appear in similar locations to mutations found in human patients who require higher doses of warfarin. Deletion of VKOR results in a severe growth defect in mycobacteria, and the growth of M. tuberculosis is inhibited by warfarin. The bacterial VKOR homolog may represent a target for antibiotics and a model for genetic studies of human VKOR. We present a simple assay in Escherichia coli, based on a disulfide-sensitive beta-galactosidase, which can be used to screen for stronger inhibitors of the M. tuberculosis VKOR homolog.

Indexed as

Amino Acid SequenceAnimalsAnticoagulantsBacterial ProteinsDisulfidesEscherichia coliHumansMixed Function OxygenasesMolecular Sequence DataMolecular StructureMutationMycobacterium tuberculosisOxidation-ReductionSequence AlignmentVitamin K Epoxide ReductasesWarfarinAnticoagulantsBacterial ProteinsDisulfidesMixed Function OxygenasesVitamin K Epoxide ReductasesWarfarin

Identifiers

PMID20018758
PMCPMC2806739
OpenAlexW2100104025

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.