ArticleThe Journal of biological chemistry2019
Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded by
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 12 citations in OpenAlex.
- From gut colonization to recurrence:Gut microbes · 2026Review
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- Deciphering the role of SsaE in biofilm regulation and T3SS-dependent virulence of Salmonella Typhimurium.World journal of microbiology & biotechnology · 2025Article
- Beyond Antibiotics: What the Future Holds.Antibiotics (Basel, Switzerland) · 2024Review
- RyhB Paralogs Downregulate the Expressions of Multiple Survival-Associated Genes and Attenuate the Survival ofMicroorganisms · 2023Article
- Article
- Orf1B controls secretion of T3SS proteins and contributes to Edwardsiella piscicida adhesion to epithelial cells.Veterinary research · 2022Article
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- CesL Regulates Type III Secretion Substrate Specificity of the EnteropathogenicMicroorganisms · 2021Article
- Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.Biomolecules · 2021Review
- A Reporter System for Fast Quantitative Monitoring of Type 3 Protein Secretion in EnteropathogenicMicroorganisms · 2020Article
- Article
- Identification of an Integrase That Responsible for Precise Integration and Excision ofFrontiers in microbiology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial type III secretion system (T3SS) delivers virulence proteins, called effectors, into eukaryotic cells. T3SS comprises a transmembrane secretion apparatus and a complex network of specialized chaperones that target protein substrates to this secretion apparatus. However, the regulation of secretion switching from early (needle and inner rod) to middle (tip/filament and translocators) substrates is incompletely understood. Here, we investigated chaperone-mediated secretion switching from early to middle substrates in the T3SS encoded by
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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.