ArticleNature2005
Regulation of Mycobacterium tuberculosis cell envelope composition and virulence by intramembrane proteolysis.
Article in Nature, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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
59 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.
- Identification of gene targets against dormant phase Mycobacterium tuberculosis infections.BMC infectious diseases · 2007Pooled it
- Bacterial zinc metalloproteases as facilitators of pathogenic success: a review.Archives of microbiology · 2026Review
- Cryo-EM structure of the bacterial intramembrane metalloprotease RseP in the substrate-bound state.Science advances · 2025Article
- Genomic variations in Mycobacterium tuberculosis from the lungs and blood of HIV-infected individuals in Uganda: insights into compartmentalization.African health sciences · 2024Article
- The Balance between Protealysin and Its Substrate, the Outer Membrane Protein OmpX, RegulatesInternational journal of molecular sciences · 2024Review
- Iron-related gene mutations driving global Mycobacterium tuberculosis transmission revealed by whole-genome sequencing.BMC genomics · 2024Article
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
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- The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.microLife · 2023Review
- Integrated sensing of host stresses by inhibition of a cytoplasmic two-component system controlseLife · 2021Article
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- RskA Is a Dual Function Activator-Inhibitor That Controls SigK Activity Across Distinct Bacterial Genera.Frontiers in microbiology · 2020Article
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- Disorder-to-order transition in PE-PPE proteins of Mycobacterium tuberculosis augments the pro-pathogen immune response.FEBS open bio · 2020Article
- In Vivo Methods to Study Protein-Protein Interactions as Key Players inPathogens (Basel, Switzerland) · 2019Review
- MmpL8Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Characterising resuscitation promoting factor fluorescent-fusions in mycobacteria.BMC microbiology · 2018Article
- Article
- Chemical Genetic Interaction Profiling Reveals Determinants of Intrinsic Antibiotic Resistance in Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mycobacterium tuberculosis infection is a continuing global health crisis that kills 2 million people each year. Although the structurally diverse lipids of the M. tuberculosis cell envelope each have non-redundant roles in virulence or persistence, the molecular mechanisms regulating cell envelope composition in M. tuberculosis are undefined. In higher eukaryotes, membrane composition is controlled by site two protease (S2P)-mediated cleavage of sterol regulatory element binding proteins, membrane-bound transcription factors that control lipid biosynthesis. S2P is the founding member of a widely distributed family of membrane metalloproteases that cleave substrate proteins within transmembrane segments. Here we show that a previously uncharacterized M. tuberculosis S2P homologue (Rv2869c) regulates M. tuberculosis cell envelope composition, growth in vivo and persistence in vivo. These results establish that regulated intramembrane proteolysis is a conserved mechanism controlling membrane composition in prokaryotes and show that this proteolysis is a proximal regulator of cell envelope virulence determinants in M. tuberculosis.
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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.