Evidence map›Paper›PMID 33932730›Full record

ReviewCurrent opinion in microbiology2021

Targeting a highly conserved domain in bacterial histidine kinases to generate inhibitors with broad spectrum activity.

Conrad A Fihn, Erin E Carlson

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.5field-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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Development of covalent inhibitors for bacterial histidine kinases.Chemical communications (Cambridge, England) · 2026
    Article
  7. Article
  8. Article
  9. Novel Antibacterial Approaches and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Anti-quorum sensing activity of poly-amidoamine dendrimer generation 5 dendrimer loaded kinase inhibitor peptide against methicillin-resistantSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
    Article
  16. Evaluation of Expanded 2-Aminobenzothiazole Library for Inhibition ofbioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Review
  19. Article
  20. Sensing of Antibiotic-Bacteria Interactions.Antibiotics (Basel, Switzerland) · 2023
    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

2 authors at 1 institution in 1 country.

Conrad A FihnDepartment of Medicinal Chemistry, University of Minnesota, 308 Harvard Street SE, Minneapolis, MN 55454, United States.
Erin E CarlsonDepartment of Medicinal Chemistry, University of Minnesota, 308 Harvard Street SE, Minneapolis, MN 55454, United States; Department of Chemistry, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, United States; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, 321 Church St SE, Minneapolis, MN 55454, United States; Department of Pharmacology, University of Minnesota, 321 Church St SE, Minneapolis, MN 55454, United States. Electronic address: carlsone@umn.edu.
University of Minnesota · US

Funding

Discovery of New Antibacterial Targets: Probes and Inhibitors of Histidine Kinase ProteinsR01GM134538 · NIGMS · UNIVERSITY OF MINNESOTA · PI CARLSON, ERIN ELIZABETH · 2020 to 2023
$1.2M
NIGMS NIH HHS R01 GM134538
6 · The paper itself

Abstract

With the rise in antimicrobial resistance and the dearth of effective strategies to combat this threat, the development of novel therapies is of utmost importance. Targeting of bacterial signaling through their the two-component systems (TCSs) may be a viable strategy. TCSs are comprised of a sensory histidine kinase (HK), of which a bacterium can have up to 160 distinct proteins, and a cognate response regulator (RR). The TCSs are generally non-essential for life, but control many virulence and antibiotic-resistance mechanisms. This, along with their absence in animals makes the TCSs an attractive target for antimicrobial therapy, whether as a stand-alone treatments or adjuvants for existing therapies. This review focuses on progress in the development of inhibitors that target the HK ATP-binding domain. Because this domain is highly conserved, it may be feasible to disrupt multiple TCSs within a single organism to increase effectiveness and reduce pressure for the evolution of resistance.

Indexed as

BacteriaHistidineAnimalsBacterial ProteinsHistidine KinaseSignal TransductionVirulenceBacterial ProteinsHistidineHistidine Kinase

Identifiers

PMID33932730
PMCPMC8189720
OpenAlexW3158164589

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.