ArticleProceedings of the National Academy of Sciences of the United States of America2017
MmpL3 is the flippase for mycolic acids in mycobacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.
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119 citing papers in PubMed, 196 citations in OpenAlex.
- Structure, assembly, and mechanism of the MmpL family of transporters.Microbiology and molecular biology reviews : MMBR · 2026Review
- Article
- Polar growth factor PgfA regulates polar peptidoglycan synthesis as well as mycolate synthesis inJournal of bacteriology · 2026Article
- Integrating computational and biological approaches for the discovery of putative MmpL3 inhibitors against Mycobacterium tuberculosis.Molecular diversity · 2026Article
- Gaining insights into MmpL3: combining structural and computational approaches to unlock transport and inhibitor-binding mechanisms.Acta crystallographica. Section D, Structural biology · 2026Article
- Combined computational and classical medicinal chemistry procedure to disclose novel pyrrole-based compounds as potential antituberculosis agents.Journal of computer-aided molecular design · 2026Article
- Bacterial cell envelope-targeting antibiotics.Nature reviews. Microbiology · 2026Review
- Exquisite specificity of Pks13 defines the essentiality of trehalose in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Protective mechanism of action of the antifungal drug naftifine againstAntimicrobial agents and chemotherapy · 2026Article
- Structural elucidation of the hexameric MmpS4-MmpL4 complex frombioRxiv : the preprint server for biology · 2026Article
- Carboxamide: A Privileged Pharmacophore for the Development of Anti-infectious and Anti-cancer Drugs.Current topics in medicinal chemistry · 2026Review
- The Biosynthetic Pathway of Mycolic Acids: Dual-Function Targets for Tuberculosis Therapeutics and Green Steroid Drugs Biomanufacturing.Pharmaceutics · 2025Review
- A bioluminescence-based chemical screen identifies a bactericidal naphthalene scaffold targeting MmpL3 inbioRxiv : the preprint server for biology · 2025Article
- Microbiological evidence for the trisubstituted benzimidazoles targeting MmpL3 inAntimicrobial agents and chemotherapy · 2025Article
- Common Biological Properties ofACS infectious diseases · 2025Article
- A potent phenylalkylamine disrupts mycobacterial membrane bioenergetics and augments bactericidal activity of bedaquiline.iScience · 2025Article
- A coiled-coil domain triggers oligomerization of MmpL10, the mycobacterial transporter of trehalose polyphleate precursor.FEBS letters · 2025Article
- Investigating the unbinding mechanisms and kinetics of MmpL3 inhibitors: A computational study.Protein science : a publication of the Protein Society · 2025Article
- Tailored phenyl ureas eradicate drug-resistantChemical science · 2025Article
- Verapamil and its metabolite norverapamil inhibit theProceedings of the National Academy of Sciences of the United States of America · 2025Article
59 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The defining feature of the mycobacterial outer membrane (OM) is the presence of mycolic acids (MAs), which, in part, render the bilayer extremely hydrophobic and impermeable to external insults, including many antibiotics. Although the biosynthetic pathway of MAs is well studied, the mechanism(s) by which these lipids are transported across the cell envelope is(are) much less known. Mycobacterial membrane protein Large 3 (MmpL3), an essential inner membrane (IM) protein, is implicated in MA transport, but its exact function has not been elucidated. It is believed to be the cellular target of several antimycobacterial compounds; however, evidence for direct inhibition of MmpL3 activity is also lacking. Here, we establish that MmpL3 is the MA flippase at the IM of mycobacteria and is the molecular target of BM212, a 1,5-diarylpyrrole compound. We develop assays that selectively access mycolates on the surface of
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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.