ArticleJournal of medicinal chemistry2015
Structure-based design of bacterial nitric oxide synthase inhibitors.
Article in Journal of medicinal chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Simple monocyclic pyrimidine analogs as microtubule targeting agents binding to the colchicine site.Bioorganic & medicinal chemistry · 2023Article
- Synthesis, DFT investigations, antioxidant, antibacterial activity and SAR-study of novel thiophene-2-carboxamide derivatives.BMC chemistry · 2023Article
- Potential of substituted quinazolines to interact with multiple targets in the treatment of cancer.Bioorganic & medicinal chemistry · 2021Article
- Staphylococcus aureus nitric oxide synthase (saNOS) modulates aerobic respiratory metabolism and cell physiology.Molecular microbiology · 2017Article
- Secretome of IntestinalFrontiers in microbiology · 2017Review
- Article
- Elucidating nitric oxide synthase domain interactions by molecular dynamics.Protein science : a publication of the Protein Society · 2016Article
- Inhibitor Bound Crystal Structures of Bacterial Nitric Oxide Synthase.Biochemistry · 2015Article
- Nitric Oxide Synthase as a Target for Methicillin-Resistant Staphylococcus aureus.Chemistry & biology · 2015Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Inhibition of bacterial nitric oxide synthase (bNOS) has the potential to improve the efficacy of antimicrobials used to treat infections by Gram-positive pathogens Staphylococcus aureus and Bacillus anthracis. However, inhibitor specificity toward bNOS over the mammalian NOS (mNOS) isoforms remains a challenge because of the near identical NOS active sites. One key structural difference between the NOS isoforms is the amino acid composition of the pterin cofactor binding site that is adjacent to the NOS active site. Previously, we demonstrated that a NOS inhibitor targeting both the active and pterin sites was potent and functioned as an antimicrobial ( Holden , , Proc. Natl. Acad. Sci. U.S.A. 2013 , 110 , 18127 ). Here we present additional crystal structures, binding analyses, and bacterial killing studies of inhibitors that target both the active and pterin sites of a bNOS and function as antimicrobials. Together, these data provide a framework for continued development of bNOS inhibitors, as each molecule represents an excellent chemical scaffold for the design of isoform selective bNOS inhibitors.
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