ArticleACS chemical biology2012
Comparison of small molecule inhibitors of the bacterial cell division protein FtsZ and identification of a reliable cross-species inhibitor.
Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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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.
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Who cites it
40 citing papers in PubMed, 78 citations in OpenAlex.
- Mechanistic inhibition of FtsZ-driven bacterial cytokinesis by natural products: an integrated machine learning and advanced drug discovery approach.Molecular diversity · 2026Article
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Isoleucyl-tRNA synthetase depletion reveals vulnerabilities in Mycobacterium abscessus and Mycobacterium marinum.Communications biology · 2025Article
- The study of honokiol as a natural product-based antimicrobial agent and its potential interaction with FtsZ protein.Frontiers in microbiology · 2024Article
- A mechanism of salt bridge-mediated resistance to FtsZ inhibitor PC190723 revealed by a cell-based screen.Molecular biology of the cell · 2023Article
- The performance of plant essential oils against lactic acid bacteria and adverse microorganisms in silage production.Frontiers in plant science · 2023Review
- A novel and dual digestive symbiosis scales up the nutrition and immune system of the holobiont Rimicaris exoculata.Microbiome · 2022Article
- Covalent Proteomimetic Inhibitor of the Bacterial FtsQB Divisome Complex.Journal of the American Chemical Society · 2022Article
- The Search for Antibacterial Inhibitors Targeting Cell Division Protein FtsZ at Its Nucleotide and Allosteric Binding Sites.Biomedicines · 2022Review
- Discovery of FtsZ inhibitors by virtual screening as antibacterial agents and study of the inhibition mechanism.RSC medicinal chemistry · 2022Article
- Traditional Chinese Medicine Tanreqing Targets Both Cell Division and Virulence inFrontiers in cellular and infection microbiology · 2022Article
- Prospects for Antibacterial Discovery and Development.Journal of the American Chemical Society · 2021Article
- Targeting the FtsZ Allosteric Binding Site with a Novel Fluorescence Polarization Screen, Cytological and Structural Approaches for Antibacterial Discovery.Journal of medicinal chemistry · 2021Article
- FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics.Antibiotics (Basel, Switzerland) · 2021Review
- Compound Uptake intoACS infectious diseases · 2021Article
- Synthesis of 9-Dechlorochrysophaentin A Enables Studies Revealing Bacterial Cell Wall Biosynthesis Inhibition Phenotype inJournal of the American Chemical Society · 2020Article
- Viriditoxin Stabilizes Microtubule Polymers in SK-OV-3 Cells and Exhibits Antimitotic and Antimetastatic Potential.Marine drugs · 2020Article
- A key bacterial cytoskeletal cell division protein FtsZ as a novel therapeutic antibacterial drug target.Bosnian journal of basic medical sciences · 2020Review
- Targeting Bacterial Cell Division: A Binding Site-Centered Approach to the Most Promising Inhibitors of the Essential Protein FtsZ.Antibiotics (Basel, Switzerland) · 2020Review
- Inhibition ofFrontiers in microbiology · 2019Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
FtsZ is a guanosine triphosphatase (GTPase) that mediates cytokinesis in bacteria. FtsZ is homologous in structure to eukaryotic tubulin and polymerizes in a similar head-to-tail fashion. The study of tubulin's function in eukaryotic cells has benefited greatly from specific and potent small molecule inhibitors, including colchicine and taxol. Although many small molecule inhibitors of FtsZ have been reported, none has emerged as a generally useful probe for modulating bacterial cell division. With the goal of establishing a useful and reliable small molecule inhibitor of FtsZ, a broad biochemical cross-comparison of reported FtsZ inhibitors was undertaken. Several of these molecules, including phenolic natural products, are unselective inhibitors that seem to derive their activity from the formation of microscopic colloids or aggregates. Other compounds, including the natural product viriditoxin and the drug development candidate PC190723, exhibit no inhibition of GTPase activity using protocols in this work or under published conditions. Of the compounds studied, only zantrin Z3 exhibits good levels of inhibition, maintains activity under conditions that disrupt small molecule aggregates, and provides a platform for exploration of structure-activity relationships (SAR). Preliminary SAR studies have identified slight modifications to the two side chains of this structure that modulate the inhibitory activity of zantrin Z3. Collectively, these studies will help focus future investigations toward the establishment of probes for FtsZ that fill the roles of colchicine and taxol in studies of tubulin.
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