ReviewFuture medicinal chemistry2010
Discovery of anti-TB agents that target the cell-division protein FtsZ.
Review in Future medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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.
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.
Who cites it
36 citing papers in PubMed.
- Pharmacophore-based virtual screening, molecular docking, MD simulation, MM-GBSA energy calculation and DFT analysis for theRSC advances · 2026Article
- Mechanistic inhibition of FtsZ-driven bacterial cytokinesis by natural products: an integrated machine learning and advanced drug discovery approach.Molecular diversity · 2026Article
- In-silico screening of marine fungal metabolites identifies potential FtsZ inhibitors against MDR-tuberculosis through docking and molecular dynamics analysis.Scientific reports · 2026Article
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- In Silico Development of a Chimeric Multi-Epitope Vaccine TargetingPharmaceuticals (Basel, Switzerland) · 2025Article
- The geneAntimicrobial agents and chemotherapy · 2025Article
- Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development.Molecular diversity · 2024Review
- Implementation of a mycobacterial CRISPRi platform in Mycobacterium abscessus and demonstration of the essentiality of ftsZTuberculosis (Edinburgh, Scotland) · 2023Article
- Evybactin is a DNA gyrase inhibitor that selectively kills Mycobacterium tuberculosis.Nature chemical biology · 2022Article
- Investigating the Antituberculosis Activity of Selected Commercial Essential Oils and Identification of Active Constituents Using a Biochemometrics Approach and In Silico Modeling.Antibiotics (Basel, Switzerland) · 2022Article
- Filamentous Thermosensitive Mutant Z: An Appealing Target for Emerging Pathogens and a Trek on Its Natural Inhibitors.Biology · 2022Review
- Overcoming the Prokaryote/Eukaryote Barrier in Tuberculosis Treatment: A Prospect for the Repurposing and Use of Antiparasitic Drugs.Microorganisms · 2021Review
- Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Strategic incorporation of fluorine in the drug discovery of new-generation antitubercular agents targeting bacterial cell division protein FtsZ.Journal of fluorine chemistry · 2017Article
- Recent advances in the discovery and development of antibacterial agents targeting the cell-division protein FtsZ.Bioorganic & medicinal chemistry · 2016Review
- Targeting the Bacterial Division Protein FtsZ.Journal of medicinal chemistry · 2016Review
- Article
- Streptomyces: a screening tool for bacterial cell division inhibitors.Journal of biomolecular screening · 2015Article
- NDK Interacts with FtsZ and Converts GDP to GTP to Trigger FtsZ Polymerisation--A Novel Role for NDK.PloS one · 2015Article
- Drug discovery targeting cell division proteins, microtubules and FtsZ.Bioorganic & medicinal chemistry · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The emergence of multidrug-resistant Mycobacterium tuberculosis strains has made many of the currently available anti-tuberculosis (TB) drugs ineffective. Accordingly, there is a pressing need to identify new drug targets. Filamentous temperature-sensitive protein Z (FtsZ), a bacterial tubulin homologue, is an essential cell-division protein that polymerizes in a GTP-dependent manner, forming a highly dynamic cytokinetic ring, designated as the Z ring, at the septum site. Other cell-division proteins are recruited to the Z ring and, upon resolution of the septum, two daughter cells are produced. Since inactivation of FtsZ or alteration of FtsZ assembly results in the inhibition of Z-ring and septum formation, FtsZ is a very promising target for novel antimicrobial drug development. This review describes the function and dynamic behaviors of FtsZ and the recent development of FtsZ inhibitors as potential anti-TB agents.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.