Evidence map›Paper›PMID 38918599›Full record

ArticleThe Journal of antibiotics2024

Synthesis and biochemical characterization of naphthoquinone derivatives targeting bacterial histidine kinases.

Teruhiko Ishikawa, Yoko Eguchi, Masayuki Igarashi, Toshihide Okajima, Kohei Mita, Yuri Yamasaki, Kaho Sumikura, Taisei Okumura, Yuna Tabuchi, Chigusa Hayashi and 8 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of antibiotics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

18 authors.

Teruhiko Ishikawa *Graduate School of Education, Okayama University, Okayama, Japan. teruhiko@cc.okayama-u.ac.jp.
Yoko Eguchi *Department of Science and Technology on Food Safety, Faculty of Biology-Oriented Science and Technology, Kindai University, Wakayama, Japan.
Masayuki Igarashi *Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.ORCID 0000-0002-1562-6685
Toshihide Okajima *SANKEN (The Institute of Scientific and Industrial Research), Osaka University, Osaka, Japan.ORCID 0000-0003-1733-9580
Kohei MitaGraduate School of Education, Okayama University, Okayama, Japan.
Yuri YamasakiGraduate School of Education, Okayama University, Okayama, Japan.
Kaho SumikuraGraduate School of Education, Okayama University, Okayama, Japan.
Taisei OkumuraGraduate School of Education, Okayama University, Okayama, Japan.
Yuna TabuchiGraduate School of Education, Okayama University, Okayama, Japan.
Chigusa HayashiInstitute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.
Martina PasquaIstituto Pasteur Italy, Department of Biology and Biotechnology, "C. Darwin", Sapienza University of Rome, Rome, Italy.
Marco ColucciaIstituto Pasteur Italy, Department of Biology and Biotechnology, "C. Darwin", Sapienza University of Rome, Rome, Italy.
Gianni ProssedaIstituto Pasteur Italy, Department of Biology and Biotechnology, "C. Darwin", Sapienza University of Rome, Rome, Italy.
Bianca ColonnaIstituto Pasteur Italy, Department of Biology and Biotechnology, "C. Darwin", Sapienza University of Rome, Rome, Italy.
Chie KohayakawaDepartment of Lead Exploration Units, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Akiyoshi TaniCompound Library Screening Center, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Jun-Ichi HarutaDepartment of Lead Exploration Units, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Ryutaro Utsumi *SANKEN (The Institute of Scientific and Industrial Research), Osaka University, Osaka, Japan. utsumi@sanken.osaka-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Waldiomycin is an inhibitor of histidine kinases (HKs). Although most HK inhibitors target the ATP-binding region, waldiomycin binds to the intracellular dimerization domain (DHp domain) with its naphthoquinone moiety presumed to interact with the conserved H-box region. To further develop inhibitors targeting the H-box, various 2-aminonaphthoquinones with cyclic, aliphatic, or aromatic amino groups and naphtho [2,3-d] isoxazole-4,9-diones were synthesized. These compounds were tested for their inhibitory activity (IC

Indexed as

Anti-Bacterial AgentsBacillus subtilisHistidine KinaseMicrobial Sensitivity TestsNaphthoquinonesBacterial ProteinsGene Expression Regulation, BacterialProtein Kinase InhibitorsQuinonesStructure-Activity RelationshipAnti-Bacterial AgentsBacterial ProteinsHistidine KinaseNaphthoquinonesProtein Kinase InhibitorsQuinoneswaldiomycin

Identifiers

PMID38918599
PMCPMC11284088

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.