Evidence map›Paper›PMID 24755430›Full record

ArticleBioorganic & medicinal chemistry letters2014

Discovery of novel bacterial elongation condensing enzyme inhibitors by virtual screening.

Zhong Zheng, Joshua B Parsons, Rajendra Tangallapally, Weixing Zhang, Charles O Rock, Richard E Lee

Abstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2014. 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
–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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Ureadepsipeptides as ClpP Activators.ACS infectious diseases · 2019
    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.

Zhong ZhengDepartment of Chemical Biology and Therapeutics, St Jude Children's Research Hospital, Memphis, TN 38105, USA.
Joshua B ParsonsDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, TN 38105, USA.
Rajendra TangallapallyDepartment of Chemical Biology and Therapeutics, St Jude Children's Research Hospital, Memphis, TN 38105, USA.
Weixing ZhangDepartment of Structural Biology, St Jude Children's Research Hospital, Memphis, TN 38105, USA.
Charles O RockDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, TN 38105, USA.
Richard E LeeDepartment of Chemical Biology and Therapeutics, St Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address: richard.lee@stjude.org.

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
REGULATION OF LIPID METABOLISM IN E COLIR01GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 1985 to 2022
$9.2M
Targeting the PlsX/Y pathway for novel antimicrobialsR01AI079653 · NIAID · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI LEE, RICHARD E., ROCK, CHARLES O · 2009 to 2010
$1.1M
NCI NIH HHS CA21765NCI NIH HHS P30 CA021765NIAID NIH HHS R01 AI079653NIGMS NIH HHS 5R01GM034496NIGMS NIH HHS R01 GM034496
6 · The paper itself

Abstract

The elongation condensing enzymes in the bacterial fatty acid biosynthesis pathway represent desirable targets for the design of novel, broad-spectrum antimicrobial agents. A series of substituted benzoxazolinones was identified in this study as a novel class of elongation condensing enzyme (FabB and FabF) inhibitors using a two-step virtual screening approach. Structure activity relationships were developed around the benzoxazolinone scaffold showing that N-substituted benzoxazolinones were most active. The benzoxazolinone scaffold has high chemical tractability making this chemotype suitable for further development of bacterial fatty acid synthesis inhibitors.

Indexed as

Drug Evaluation, Preclinical3-Oxoacyl-(Acyl-Carrier-Protein) SynthaseAnti-Bacterial AgentsBenzoxazolesDose-Response Relationship, DrugEnzyme InhibitorsEscherichia coliEscherichia coli ProteinsFatty Acid Synthase, Type IIMicrobial Sensitivity TestsModels, MolecularMolecular StructureStructure-Activity Relationship3-Oxoacyl-(Acyl-Carrier-Protein) SynthaseAnti-Bacterial AgentsBenzoxazolesEnzyme InhibitorsEscherichia coli ProteinsFabB protein, E coliFatty Acid Synthase, Type IIAntibioticsCondensing enzymesFatty acid synthesisVirtual screening

Identifiers

PMID24755430
PMCPMC4425204

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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.