![4 Schematic model for the secretion pathway of RTX toxins. Proposed... | Download Scientific Diagram 4 Schematic model for the secretion pathway of RTX toxins. Proposed... | Download Scientific Diagram](https://www.researchgate.net/publication/280085087/figure/fig3/AS:582308714553344@1515844624050/Schematic-model-for-the-secretion-pathway-of-RTX-toxins-Proposed-model-for-the-secretion.png)
4 Schematic model for the secretion pathway of RTX toxins. Proposed... | Download Scientific Diagram
![Identification of a Vibrio cholerae RTX toxin gene cluster that is tightly linked to the cholera toxin prophage | PNAS Identification of a Vibrio cholerae RTX toxin gene cluster that is tightly linked to the cholera toxin prophage | PNAS](https://www.pnas.org/cms/10.1073/pnas.96.3.1071/asset/a20e8d96-505c-4609-b2f3-b9f7610abd3b/assets/graphic/pq0394623001.jpeg)
Identification of a Vibrio cholerae RTX toxin gene cluster that is tightly linked to the cholera toxin prophage | PNAS
![In vivo covalent cross‐linking of cellular actin by the Vibrio cholerae RTX toxin | The EMBO Journal In vivo covalent cross‐linking of cellular actin by the Vibrio cholerae RTX toxin | The EMBO Journal](https://www.embopress.org/cms/asset/77208a59-3540-45dd-98cb-e31328be5fb2/embj7593346-fig-0003-m.jpg)
In vivo covalent cross‐linking of cellular actin by the Vibrio cholerae RTX toxin | The EMBO Journal
![RTX proteins: a highly diverse family secreted by a common mechanism - Linhartová - 2010 - FEMS Microbiology Reviews - Wiley Online Library RTX proteins: a highly diverse family secreted by a common mechanism - Linhartová - 2010 - FEMS Microbiology Reviews - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/64062d9c-c47b-4468-8133-b324fa1ffad8/fmr_231_f2.gif)
RTX proteins: a highly diverse family secreted by a common mechanism - Linhartová - 2010 - FEMS Microbiology Reviews - Wiley Online Library
![The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives. | Semantic Scholar The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/bc7631811ed777efcfa17b3c0d7a084c9bf96bd1/6-Figure2-1.png)
The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives. | Semantic Scholar
![Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore* - Journal of Biological Chemistry Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore* - Journal of Biological Chemistry](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/attachment/ce70b7d1-8c26-41a1-80d5-110c46608484/gr1_lrg.jpg)
Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore* - Journal of Biological Chemistry
![Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin - Journal of Biological Chemistry Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin - Journal of Biological Chemistry](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/attachment/81cbcf96-8701-4051-8147-062b73baee2f/gr1_lrg.jpg)
Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin - Journal of Biological Chemistry
![His-859 Is an Essential Residue for the Activity and pH Dependence of Escherichia coli RTX Toxin α-Hemolysin* - Journal of Biological Chemistry His-859 Is an Essential Residue for the Activity and pH Dependence of Escherichia coli RTX Toxin α-Hemolysin* - Journal of Biological Chemistry](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/asset/3e978e76-51cf-45d2-af04-f1c14492a927/gr1.jpg)
His-859 Is an Essential Residue for the Activity and pH Dependence of Escherichia coli RTX Toxin α-Hemolysin* - Journal of Biological Chemistry
![Channel formation by RTX-toxins of pathogenic bacteria: Basis of their biological activity - ScienceDirect Channel formation by RTX-toxins of pathogenic bacteria: Basis of their biological activity - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S000527361500365X-gr1.jpg)
Channel formation by RTX-toxins of pathogenic bacteria: Basis of their biological activity - ScienceDirect
Structural basis for antibody binding to adenylate cyclase toxin reveals RTX linkers as neutralization-sensitive epitopes | PLOS Pathogens
![Frontiers | Accessory Toxins of Vibrio Pathogens and Their Role in Epithelial Disruption During Infection Frontiers | Accessory Toxins of Vibrio Pathogens and Their Role in Epithelial Disruption During Infection](https://www.frontiersin.org/files/Articles/407174/fmicb-09-02248-HTML/image_m/fmicb-09-02248-g002.jpg)
Frontiers | Accessory Toxins of Vibrio Pathogens and Their Role in Epithelial Disruption During Infection
Toxins MDPI on Twitter: "Structure–Function Relationships of the Repeat Domains of #RTX Toxins https://t.co/JZ5sS9O77e #calcium; #proteinfolding; #tertiarystructure #mdpitoxins https://t.co/49AAZ478C5" / Twitter
![Templated folding of the RTX domain of the bacterial toxin adenylate cyclase revealed by single molecule force spectroscopy | Nature Communications Templated folding of the RTX domain of the bacterial toxin adenylate cyclase revealed by single molecule force spectroscopy | Nature Communications](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41467-022-30448-8/MediaObjects/41467_2022_30448_Fig1_HTML.png)
Templated folding of the RTX domain of the bacterial toxin adenylate cyclase revealed by single molecule force spectroscopy | Nature Communications
![Vibrio cholerae Strains with Mutations in an Atypical Type I Secretion System Accumulate RTX Toxin Intracellularly | Journal of Bacteriology Vibrio cholerae Strains with Mutations in an Atypical Type I Secretion System Accumulate RTX Toxin Intracellularly | Journal of Bacteriology](https://journals.asm.org/cms/10.1128/JB.186.23.8137-8143.2004/asset/1e1ae25b-b2ed-430b-af3a-490c046cb4f2/assets/graphic/zjb0230442370005.jpeg)