ArticleNature structural & molecular biology2014
Structure of a pathogenic type 3 secretion system in action.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 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
107 citing papers in PubMed.
- From gut colonization to recurrence:Gut microbes · 2026Review
- Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026Article
- Reprogramming of bacterial virulence by lysine acetylation.Nature communications · 2026Article
- Tumor-specific cytokine therapy mediated by engineered Salmonella with a synthetic protein delivery system.Scientific reports · 2026Article
- A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.bioRxiv : the preprint server for biology · 2026Article
- The Salmonella pathogenicity island 1 injectisome reprograms host cell translation to evade the inflammatory response.Nature communications · 2025Article
- Yersinia actively downregulates type III secretion and adhesion at higher cell densities.PLoS pathogens · 2025Article
- A high throughput assay for measuring secreted protein based on a de novo fluorescent reporter reveals regulatory and structural insights in Salmonella type three secretion system.Protein science : a publication of the Protein Society · 2025Article
- Targeting Type III Secretion System usingIndian journal of microbiology · 2025Review
- Review
- Exploitation of Biodiversity in Bioeconomy: Examples, Opportunities, and Challenges.Advances in biochemical engineering/biotechnology · 2025Review
- Genomic analysis of multidrug-resistantFrontiers in microbiology · 2025Article
- The T4bSS of Legionella features a two-step secretion pathway with an inner membrane intermediate for secretion of transmembrane effectors.PLoS pathogens · 2024Article
- Cytosolic delivery of monobodies using the bacterial type III secretion system inhibits oncogenic BCR: ABL1 signaling.Cell communication and signaling : CCS · 2024Article
- Overexpression of T3SS translocation signals inInfection and immunity · 2024Article
- Exploring the comparative genome of rice pathogenFrontiers in plant science · 2024Article
- MakC and MakD are two proteins associated with a tripartite toxin ofFrontiers in microbiology · 2024Article
- Visualizing the invisible: novel approaches to visualizing bacterial proteins and host-pathogen interactions.Frontiers in bioengineering and biotechnology · 2024Review
- Organelles are miscommunicating: Membrane contact sites getting hijacked by pathogens.Virulence · 2023Review
- An Outbreak ofAnimals : an open access journal from MDPI · 2023Article
47 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
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type 3 secretion systems use 3.5-megadalton syringe-like, membrane-embedded 'injectisomes', each containing an ~800-Å-long needle complex to connect intracellular compartments of infectious bacteria and hosts. Here we identify requirements for substrate association with, transport through and exit from the injectisome of Salmonella enterica serovar Typhimurium. This guided the design of substrates that become trapped within the secretion path and enabled visualization of injectisomes in action in situ. We used cryo-EM to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport. Furthermore, trapping of a heterologous substrate in the needle prevents secretion of natural bacterial effectors. Together, the data reveal the path of protein secretion across multiple membranes and show that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.
Indexed as
Identifiers
24317488What 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.