Evidence map›Paper›PMID 29551481›Full record

ArticleBioorganic & medicinal chemistry letters2018

The identification of inhibitory compounds of Rickettsia prowazekii methionine aminopeptidase for antibacterial applications.

Travis R Helgren, Elif S Seven, Congling Chen, Thomas E Edwards, Bart L Staker, Jan Abendroth, Peter J Myler, James R Horn, Timothy J Hagen

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. ACS infectious diseases · 2022
    Article
  2. 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

9 authors at 3 institutions in 1 country.

Travis R HelgrenDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy, DeKalb, IL 60115, USA.
Elif S SevenDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy, DeKalb, IL 60115, USA.
Congling ChenDepartment of Chemistry and Biochemistry, Northern Illinois University, 1425 W. Lincoln Hwy, DeKalb, IL 60115, USA.
Thomas E EdwardsBeryllium Discovery Corp., 7869 NE Day Road West, Bainbridge Island, WA 98110, USA; Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, USA.
Bart L StakerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, USA; Center for Infectious Disease Research, Formerly Seattle Biomedical Research Institute, 307 Westlake Avenue N., Seattle, WA 98109, USA.
Jan AbendrothBeryllium Discovery Corp., 7869 NE Day Road West, Bainbridge Island, WA 98110, USA; Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, USA.
Peter J MylerSeattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA, USA; Center for Infectious Disease Research, Formerly Seattle Biomedical Research Institute, 307 Westlake Avenue N., Seattle, WA 98109, 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 · USCenter for Infectious Disease Research · USBeryllium (United States) · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
NIAID NIH HHS HHSN272200700057CNIAID NIH HHS HHSN272201200025CNIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

Methionine aminopeptidase (MetAP) is a dinuclear metalloprotease responsible for the cleavage of methionine initiator residues from nascent proteins. MetAP activity is necessary for bacterial proliferation and is therefore a projected novel antibacterial target. A compound library consisting of 294 members containing metal-binding functional groups was screened against Rickettsia prowazekii MetAP to determine potential inhibitory motifs. The compounds were first screened against the target at a concentration of 10 µM and potential hits were determined to be those exhibiting greater than 50% inhibition of enzymatic activity. These hit compounds were then rescreened against the target in 8-point dose-response curves and 11 compounds were found to inhibit enzymatic activity with IC

Indexed as

Anti-Bacterial AgentsCatalytic DomainEnzyme AssaysMetalloproteasesMethionyl AminopeptidasesMolecular Docking SimulationProtease InhibitorsRickettsia prowazekiiSmall Molecule LibrariesAnti-Bacterial AgentsMetalloproteasesMethionyl AminopeptidasesProtease InhibitorsSmall Molecule Libraries

Identifiers

PMID29551481
PMCPMC5908248
OpenAlexW2794178257

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.