Evidence map›Paper›PMID 27607918›Full record

ArticleBiochemistry2016

Targeting Bacterial Nitric Oxide Synthase with Aminoquinoline-Based Inhibitors.

Jeffrey K Holden, Matthew C Lewis, Maris A Cinelli, Ziad Abdullatif, Anthony V Pensa, Richard B Silverman, Thomas L Poulos

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. The nitric oxide synthase gene negatively regulates biofilm formation inFrontiers in cellular and infection microbiology · 2022
    Article
  5. A Novel Thiazolyl Schiff Base: Antibacterial and Antifungal Effects andOxidative medicine and cellular longevity · 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

7 authors.

Jeffrey K HoldenDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.
Matthew C LewisDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.
Maris A CinelliDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.
Ziad AbdullatifDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.
Anthony V PensaDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.
Richard B SilvermanDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.
Thomas L PoulosDepartment of Molecular Biology and Biochemistry, ‡Department of Pharmaceutical Sciences, and §Department of Chemistry, University of California , Irvine, California 92697-3900, United States.

Funding

STRUCTURAL STUDIES ON NITRIC OXIDE SYNTHASER01GM057353 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI POULOS, THOMAS L · 1998 to 2018
$6.8M
Selective inhibition of nitric oxide synthase for multiple indicationsR01GM049725 · NIGMS · NORTHWESTERN UNIVERSITY · PI SILVERMAN, RICHARD B · 1994 to 2018
$6.0M
Design, Synthesis, and Biology of Inhibitors of Neuronal Nitric Oxide SynthaseF32GM109667 · NIGMS · NORTHWESTERN UNIVERSITY · PI CINELLI, MARIS A · 2014 to 2015
$109k
NIGMS NIH HHS F32 GM109667NIGMS NIH HHS R01 GM049725NIGMS NIH HHS R01 GM057353
6 · The paper itself

Abstract

Nitric oxide is produced in Gram-positive pathogens Bacillus anthracis and Staphylococcus aureus by the bacterial isoform of nitric oxide synthase (NOS). Inhibition of bacterial nitric oxide synthase (bNOS) has been identified as a promising antibacterial strategy for targeting methicillin-resistant S. aureus [Holden, J. K., et al. (2015) Chem. Biol. 22, 785-779]. One class of NOS inhibitors that demonstrates antimicrobial efficacy utilizes an aminoquinoline scaffold. Here we report on a variety of aminoquinolines that target the bacterial NOS active site, in part, by binding to a hydrophobic patch that is unique to bNOS. Through mutagenesis and crystallographic studies, our findings demonstrate that aminoquinolines are an excellent scaffold for further aiding in the development of bNOS specific inhibitors.

Indexed as

AminoquinolinesBacillus anthracisCrystallography, X-RayEnzyme InhibitorsNitric Oxide SynthaseStaphylococcus aureusAminoquinolinesEnzyme InhibitorsNitric Oxide Synthase

Identifiers

PMID27607918
PMCPMC5283056

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Registered trials

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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.