ArticleNature structural & molecular biology2010
Structure of the cholera toxin secretion channel in its closed state.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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.
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Who cites it
78 citing papers in PubMed, 138 citations in OpenAlex.
- Molecular evolution and adaptations ofFrontiers in cellular and infection microbiology · 2026Review
- The GspCD-dependent type II secretion system promotes necrotizing soft tissue infection caused byFrontiers in cellular and infection microbiology · 2026Article
- Secretins of type-two secretion systems are necessary for exopolymeric slime secretion in cyanobacteria and myxobacteria.Nature communications · 2025Article
- The activity of the quorum sensing regulator HapR is modulated by the bacterial extracellular vesicle (BEV)-associated protein ObfA of Vibrio cholerae.Journal of extracellular vesicles · 2024Article
- UsingBiochemistry · 2024Article
- UsingbioRxiv : the preprint server for biology · 2023Article
- Membrane translocation process revealed by in situ structures of type II secretion system secretins.Nature communications · 2023Article
- Characterization and utility of two monoclonal antibodies to cholera toxin B subunit.Scientific reports · 2023Article
- Structural basis for the toxin-coregulated pilus-dependent secretion ofScience advances · 2022Article
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- In-Depth Characterization of a Re-Engineered Cholera Toxin Manufacturing Process Using Growth-Decoupled Production inToxins · 2022Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- Core architecture of a bacterial type II secretion system.Nature communications · 2019Article
- Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system.PLoS pathogens · 2019Article
- Cholera Toxin Encapsulated within SeveralToxins · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- A Hybrid Secretion System Facilitates Bacterial Sporulation: A Structural Perspective.Microbiology spectrum · 2019Review
- Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion.The Journal of biological chemistry · 2018Article
- Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa.Scientific reports · 2018Article
- Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.PLoS pathogens · 2018Article
18 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
4 authors at 2 institutions in 1 country.
Funding
Abstract
The type II secretion system (T2SS) is a macromolecular complex spanning the inner and outer membranes of Gram-negative bacteria. Remarkably, the T2SS secretes folded proteins, including multimeric assemblies such as cholera toxin and heat-labile enterotoxin from Vibrio cholerae and enterotoxigenic Escherichia coli, respectively. The major outer membrane T2SS protein is the 'secretin' GspD. Cryo-EM reconstruction of the V. cholerae secretin at 19-Å resolution reveals a dodecameric structure reminiscent of a barrel, with a large channel at its center that contains a closed periplasmic gate. The GspD periplasmic domain forms a vestibule with a conserved constriction, and it binds to a pentameric exoprotein and to the trimeric tip of the T2SS pseudopilus. By combining our results with structures of the cholera toxin and T2SS pseudopilus tip, we provide a structural basis for a possible secretion mechanism of the T2SS.
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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.