ArticleJournal of bacteriology2015
The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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Who cites it
7 citing papers in PubMed.
- Visualizing the invisible: novel approaches to visualizing bacterial proteins and host-pathogen interactions.Frontiers in bioengineering and biotechnology · 2024Review
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens.Veterinary research · 2021Review
- Delivery of Heterologous Proteins, Enzymes, and Antigens via the Bacterial Type III Secretion System.Microorganisms · 2020Review
- Regulation of Effector Delivery by Type III Secretion Chaperone Proteins inFrontiers in microbiology · 2018Article
- Methods to Illuminate the Role ofFrontiers in cellular and infection microbiology · 2017Review
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Bacteria hijack eukaryotic cells by injecting virulence effectors into host cytosol with a type III secretion system (T3SS). Effectors are targeted with their cognate chaperones to hexameric T3SS ATPase at the bacterial membrane's cytosolic face. In this issue of the Journal of Bacteriology, Roblin et al. (P. Roblin, F. Dewitte, V. Villeret, E. G. Biondi, and C. Bompard, J Bacteriol 197:688-698, 2015, http://dx.doi.org/10.1128/JB.02294-14) show that the T3SS chaperone SigE of Salmonella can form hexameric rings rather than dimers when bound to its cognate effector, SopB, implying a novel multimeric association for chaperone/effector complexes with their ATPase.
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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.