Evidence map›Paper›PMID 25531939›Full record

ArticleACS chemical biology2015

Inactivation of multiple bacterial histidine kinases by targeting the ATP-binding domain.

Kaelyn E Wilke, Samson Francis, Erin E Carlson

Abstract read
In one paragraph

Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Development of covalent inhibitors for bacterial histidine kinases.Chemical communications (Cambridge, England) · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Evaluation of Expanded 2-Aminobenzothiazole Library for Inhibition ofbioRxiv : the preprint server for biology · 2024
    Article
  12. Chemical and biomolecular insights into theIsrael journal of chemistry · 2023
    Article
  13. Targeting multidrug resistantChemical science · 2023
    Article
  14. Overview on Strategies and Assays for Antibiotic Discovery.Pharmaceuticals (Basel, Switzerland) · 2022
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Role of Two-Component System Networks in Pseudomonas aeruginosa Pathogenesis.Advances in experimental medicine and biology · 2022
    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

3 authors.

Kaelyn E WilkeDepartment of Chemistry, Indiana University , 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.
Samson Francis
Erin E Carlson

Funding

Targeted natural product diversification to identify novel antibacterial agentsDP2OD008592 · OD · UNIVERSITY OF MINNESOTA · PI CARLSON, ERIN ELIZABETH · 2011 to 2011
$2.2M
NIH HHS DP2 OD008592NIH HHS DP2OD008592
6 · The paper itself

Abstract

Antibacterial agents that exploit new targets will be required to combat the perpetual rise of bacterial resistance to current antibiotics. We are exploring the inhibition of histidine kinases, constituents of two-component systems. Two-component systems are the primary signaling pathways that bacteria utilize to respond to their environment. They are ubiquitous in bacteria and trigger various pathogenic mechanisms. To attenuate these signaling pathways, we sought to broadly target the histidine kinase family by focusing on their highly conserved ATP-binding domain. Development of a fluorescence polarization displacement assay facilitated high-throughput screening of ∼53 000 diverse small molecules for binding to the ATP-binding pocket. Of these compounds, nine inhibited the catalytic activity of two or more histidine kinases. These scaffolds could provide valuable starting points for the design of broadly effective HK inhibitors, global reduction of bacterial signaling, and ultimately, a class of antibiotics that function by a new mechanism of action.

Indexed as

Anti-Bacterial AgentsProtein Kinase InhibitorsAdenosine TriphosphateAnimalsBacillus subtilisCatalytic DomainCell SurvivalChlorocebus aethiopsDose-Response Relationship, DrugDrug DiscoveryEscherichia coliFluorescence PolarizationHigh-Throughput Screening AssaysHistidine KinaseProtein BindingProtein KinasesAdenosine TriphosphateAnti-Bacterial AgentsHistidine KinaseProtein Kinase InhibitorsProtein KinasesSmall Molecule Libraries

Identifiers

PMID25531939
PMCPMC4301073

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.