ArticleNature communications2019
Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
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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.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
- Structural basis of allosteric activation of Mycobacterium tuberculosis isocitrate lyase 2.Communications biology · 2026Article
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- Characterization of the Biological Effect Mediated by Mycobacterial Kinase PknG on Protein Phosphorylation and Acetylation.ACS omega · 2025Article
- The Effect of Erythromycin in Macrolide-resistantCurrent pharmaceutical biotechnology · 2025Article
- An integrated structural and biophysical approach to study carbon metabolism inQRB discovery · 2025Review
- Gene Regulatory Mechanism of Mycobacterium Tuberculosis during Dormancy.Current issues in molecular biology · 2024Review
- Temporal genome-wide fitness analysis ofmSystems · 2024Article
- Proteomic study of the inhibitory effects of tannic acid on MRSA biofilm.Frontiers in pharmacology · 2024Article
- The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.Molecular biomedicine · 2022Review
- GATA-type transcriptional factor SpGAT1 interacts with SpMIG1 and promotes lipid accumulation in the oleaginous yeastBiotechnology for biofuels and bioproducts · 2022Article
- Comparative Genomic Analysis Reveals Potential Pathogenicity and Slow-Growth Characteristics of GenusMicrobiology spectrum · 2022Article
- Engineering the glyoxylate cycle for chemical bioproduction.Frontiers in bioengineering and biotechnology · 2022Review
- Regulation of theJournal of bacteriology · 2021Article
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- Itaconate is a covalent inhibitor of theRSC medicinal chemistry · 2021Article
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- Truncation of C-Terminal Intrinsically Disordered Region of Mycobacterial Rv1915 Facilitates Production of "Difficult-to-Purify" Recombinant Drug Target.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isocitrate lyase is important for lipid utilisation by Mycobacterium tuberculosis but its ICL2 isoform is poorly understood. Here we report that binding of the lipid metabolites acetyl-CoA or propionyl-CoA to ICL2 induces a striking structural rearrangement, substantially increasing isocitrate lyase and methylisocitrate lyase activities. Thus, ICL2 plays a pivotal role regulating carbon flux between the tricarboxylic acid (TCA) cycle, glyoxylate shunt and methylcitrate cycle at high lipid concentrations, a mechanism essential for bacterial growth and virulence.
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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.