Evidence map›Paper›PMID 31521478›Full record

ArticleBioorganic & medicinal chemistry letters2019

Antibacterial activity of 2-amino-4-hydroxypyrimidine-5-carboxylates and binding to Burkholderia pseudomallei 2-C-methyl-d-erythritol-2,4-cyclodiphosphate synthase.

Sydney M Watkins, Debarati Ghose, Joy M Blain, Dakota L Grote, Chi-Hao Luan, Michael Clare, R Meganathan, James R Horn, Timothy J Hagen

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2019. 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
0.1field-weighted citation impact, top 52% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  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

9 authors at 2 institutions in 1 country.

Sydney M WatkinsDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA.
Debarati GhoseDepartment of Biological Sciences, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA.
Joy M BlainDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA.
Dakota L GroteDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA.
Chi-Hao LuanHigh Throughput Analysis Laboratory and Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Michael ClareClare Associates LLC, Skokie, IL 60077, USA.
R MeganathanDepartment of Biological Sciences, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA.
James R HornDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA.
Timothy J HagenDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy., DeKalb, IL 60115, USA. Electronic address: thagen@niu.edu.
Northern Illinois University · USNorthwestern University · US

Funding

Echo Acoustic Liquid Handler for High Throughput Analysis LabS10OD023681 · OD · NORTHWESTERN UNIVERSITY · PI WEISS, ERIC LYLE · 2018 to 2018
$550k
Design and Study of IspF Inhibitors as Antibacterial AgentsR15AI113653 · NIAID · NORTHERN ILLINOIS UNIVERSITY · PI HAGEN, TIMOTHY JOSEPH · 2014 to 2014
$356k
NIAID NIH HHS R15 AI113653NIH HHS S10 OD023681
6 · The paper itself

Abstract

Enzymes in the methylerythritol phosphate pathway make attractive targets for antibacterial activity due to their importance in isoprenoid biosynthesis and the absence of the pathway in mammals. The fifth enzyme in the pathway, 2-C-methyl-d-erythritol-2,4-cyclodiphosphate synthase (IspF), contains a catalytically important zinc ion in the active site. A series of de novo designed compounds containing a zinc binding group was synthesized and evaluated for antibacterial activity and interaction with IspF from Burkholderia pseudomallei, the causative agent of Whitmore's disease. The series demonstrated antibacterial activity as well as protein stabilization in fluorescence-based thermal shift assays. Finally, the binding of one compound to Burkholderia pseudomallei IspF was evaluated through group epitope mapping by saturation transfer difference NMR.

Indexed as

Anti-Bacterial AgentsBacterial ProteinsBurkholderia pseudomalleiCatalysisCatalytic DomainCrystallography, X-RayErythritolHumansKineticsMolecular StructurePhosphorus-Oxygen LyasesProtein BindingPyrimidinesSignal TransductionZinc2-methyl-butan-1,2,3,4-tetraol-2,4-cyclopyrophosphateAnti-Bacterial AgentsBacterial ProteinsErythritolPhosphorus-Oxygen LyasespyrimidinePyrimidinesZincAntibacterial activityBurkholderia pseudomallei IspFFluorescence-based thermal shiftKirby Bauer disk diffusionMEP pathwaySTD-NMR

Identifiers

PMID31521478
PMCPMC7006361
OpenAlexW2971812439

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.