Evidence map›Paper›PMID 22606938›Full record

ArticleJournal of the American Chemical Society2012

Activity-based probe for histidine kinase signaling.

Kaelyn E Wilke, Samson Francis, Erin E Carlson

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

  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. Evaluation of Expanded 2-Aminobenzothiazole Library for Inhibition ofbioRxiv : the preprint server for biology · 2024
    Article
  11. Review
  12. Article
  13. An Overview of the Factors Involved in Biofilm Production by theInternational journal of molecular sciences · 2023
    Review
  14. Targeting multidrug resistantChemical science · 2023
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  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

3 authors at 1 institution in 1 country.

Kaelyn E WilkeDepartment of Chemistry, Indiana University, Bloomington, 47405, United States.
Samson Francis
Erin E Carlson
Indiana University Bloomington · US

Funding

Targeted natural product diversification to identify novel antibacterial agentsDP2OD008592 · OD · UNIVERSITY OF MINNESOTA · PI CARLSON, ERIN ELIZABETH · 2011 to 2011
$2.2M
Innovative Technologies for Metabolite Profiling and Natural Products DiscoveryR00GM082983 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CARLSON, ERIN ELIZABETH · 2008 to 2010
$744k
NIGMS NIH HHS R00 GM082983NIGMS NIH HHS R00GM82983NIH HHS DP2 OD008592NIH HHS DP2OD008592
6 · The paper itself

Abstract

Bacterial two-component systems (TCSs) are signaling pathways composed of two proteins: a histidine kinase (HK) and a response regulator (RR). Upon stimulation, the HK autophosphorylates at a conserved histidine. The phosphoryl group is subsequently transferred to an aspartate on an RR, eliciting an adaptive response, often up- or downregulation of gene expression. TCS signaling controls many functions in bacteria, including development, virulence, and antibiotic resistance, making the proteins involved in these systems potential therapeutic targets. Efficient methods for the profiling of HKs are currently lacking. For direct readout of HK activity, we sought to design a probe that enables detection of the phosphotransfer event; however, analysis of the phosphohistidine species is made difficult by the instability of the P-N bond. We anticipated that use of a γ-thiophosphorylated ATP analogue, which would yield a thiophosphorylated histidine intermediate, could overcome this challenge. We determined that the fluorophore-conjugated probe, BODIPY-FL-ATPγS, labels active HK proteins and is competitive for the ATP binding site. This activity-based probe provides a new strategy for analysis of TCSs and other HK-mediated processes and will facilitate both functional studies and inhibitor identification.

Indexed as

Signal TransductionBacterial Physiological PhenomenaFluorescent DyesHistidine KinaseProtein KinasesFluorescent DyesHistidine KinaseProtein Kinases

Identifiers

PMID22606938
PMCPMC3415608
OpenAlexW2024960866

What OpenQuestion holds

Textmetadata
LicenceTDM
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.