ArticleScience advances2015
Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline.
Article in Science advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.
What it found
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Who cites it
132 citing papers in PubMed, 286 citations in OpenAlex.
- Targeting Latent Tuberculosis Using Hypoxia-Activated Prodrugs of Bedaquiline Analogues.ACS medicinal chemistry letters · 2026Article
- Article
- A Multi-Scale Computational Framework for Anti-Persister Tuberculosis Drug Discovery.Chemical biology & drug design · 2026Review
- The Antimycobacterial Activity, Toxicity and Chemical Composition of South African Propolis.Chemistry & biodiversity · 2026Article
- Bedaquiline inhibits the ATP synthase leak channel and prevents glutamate-induced neuronal death.Biophysical reports · 2026Article
- A Case of Transmission of Bedaquiline- and Linezolid-Resistant Tuberculosis.International journal of molecular sciences · 2026Article
- Ensemble learning-guided discovery of anti-tuberculosis phytochemicals: computational prediction and mechanistic insights.Journal of computer-aided molecular design · 2026Article
- Bedaquiline, Pretomanid, Linezolid, and Moxifloxacin: Mechanisms of Action, Drug Interactions, Adverse Effects and Use in Special Situations.Microorganisms · 2026Review
- ADME/drug-likeness and functional properties of Punica granatum seeds supported with molecular docking, GC-MS and LC-MS/MS analysis.Scientific reports · 2026Article
- Secondary metabolites fromRSC advances · 2026Article
- Bedaquiline inhibits the ATP synthase leak channel and prevents glutamate-induced neuronal death.bioRxiv : the preprint server for biology · 2026Article
- Investigation of mitochondrial inner membrane ion conductance by planar lipid bilayer electrophysiology.Frontiers in physiology · 2026Article
- Drug Exposure Dictates Evolutionary Dynamics of Drug-Resistant Tuberculosis: A Longitudinal Cohort Study in Beijing, China.Infection and drug resistance · 2026Article
- Combating Drug Resistance inBioinformatics and biology insights · 2026Article
- Remission spectroscopy resolves the mechanism of action of bedaquiline within living mycobacteria.Nature communications · 2025Article
- Mycobacterium tuberculosis curli pili facilitates pathogenicity by modulating central carbon metabolism.Metabolomics : Official journal of the Metabolomic Society · 2025Article
- ATP synthesis driven by atmospheric hydrogen concentrations.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- An improved catalogue for whole-genome sequencing prediction of bedaquiline resistance inMicrobial genomics · 2025Article
- Structure and assembly of the MmpL5/MmpS5 efflux transporter from Mycobacterium tuberculosis.Nature communications · 2025Article
- Quinoline ATP Synthase Inhibitors with Activity Against Multidrug Resistant Acinetobacter baumannii and Pseudomonas aeruginosa.ChemMedChem · 2025Article
72 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug-resistant tuberculosis (MDR-TB) is more prevalent today than at any other time in human history. Bedaquiline (BDQ), a novel Mycobacterium-specific adenosine triphosphate (ATP) synthase inhibitor, is the first drug in the last 40 years to be approved for the treatment of MDR-TB. This bactericidal compound targets the membrane-embedded rotor (c-ring) of the mycobacterial ATP synthase, a key metabolic enzyme required for ATP generation. We report the x-ray crystal structures of a mycobacterial c9 ring without and with BDQ bound at 1.55- and 1.7-Å resolution, respectively. The structures and supporting functional assays reveal how BDQ specifically interacts with the rotor ring via numerous interactions and thereby completely covers the c-ring's ion-binding sites. This prevents the rotor ring from acting as an ion shuttle and stalls ATP synthase operation. The structures explain how diarylquinoline chemicals specifically inhibit the mycobacterial ATP synthase and thus enable structure-based drug design of next-generation ATP synthase inhibitors against Mycobacterium tuberculosis and other bacterial pathogens.
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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.