Evidence map›Paper›PMID 28745975›Full record

ArticleSLAS discovery : advancing life sciences R & D2018

Identification of Chemical Compounds That Inhibit the Function of Histidyl-tRNA Synthetase from Pseudomonas aeruginosa.

Yanmei Hu, Stephanie O Palmer, Sara T Robles, Tahyra Resto, Frank B Dean, James M Bullard

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

Article in SLAS discovery : advancing life sciences R & D, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  2. A Systematic Strategy to Find Potential Therapeutic Targets forFrontiers in molecular biosciences · 2021
    Article
  3. Review
  4. 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

6 authors at 1 institution in 1 country.

Yanmei Hu1 Chemistry Department, The University of Texas-RGV, Edinburg, TX, USA.
Stephanie O Palmer1 Chemistry Department, The University of Texas-RGV, Edinburg, TX, USA.
Sara T Robles1 Chemistry Department, The University of Texas-RGV, Edinburg, TX, USA.
Tahyra Resto1 Chemistry Department, The University of Texas-RGV, Edinburg, TX, USA.
Frank B Dean1 Chemistry Department, The University of Texas-RGV, Edinburg, TX, USA.
James M Bullard1 Chemistry Department, The University of Texas-RGV, Edinburg, TX, USA.
The University of Texas Rio Grande Valley · US

Funding

Construction of a Protein Synthesis System from Pseudomonas aeruginosa for Screening for Antibacterial CandidatesSC3GM098173 · NIGMS · UNIVERSITY OF TEXAS RIO GRANDE VALLEY · PI BULLARD, JAMES M · 2012 to 2019
$861k
NIGMS NIH HHS SC3 GM098173
6 · The paper itself

Abstract

Pseudomonas aeruginosa histidyl-tRNA synthetase (HisRS) was selected as a target for antibiotic drug development. The HisRS protein was overexpressed in Escherichia coli and kinetically evaluated. The K

Indexed as

Drug DiscoveryAmino Acid SequenceAnti-Bacterial AgentsDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsGene ExpressionHistidine-tRNA LigaseHumansInhibitory Concentration 50Microbial Sensitivity TestsMolecular StructurePseudomonas aeruginosaAnti-Bacterial AgentsEnzyme InhibitorsHistidine-tRNA Ligaseantibioticdrug discoveryhistidyl-tRNA synthetaseprotein synthesisPseudomonas aeruginosatRNA aminoacylation

Identifiers

PMID28745975
PMCPMC5794219
OpenAlexW3004676436

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.