![Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members - ScienceDirect Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0005273615001157-fx1.jpg)
Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members - ScienceDirect
Membrane localization of the Repeats-in-Toxin (RTX) Leukotoxin (LtxA) produced by Aggregatibacter actinomycetemcomitans | PLOS ONE
![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/6dbc96c2-851e-45da-9a5f-fda886a55999/fmr_231_f1.jpg)
RTX proteins: a highly diverse family secreted by a common mechanism - Linhartová - 2010 - FEMS Microbiology Reviews - Wiley Online Library
![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
![Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins | Scientific Reports Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-021-99112-3/MediaObjects/41598_2021_99112_Fig3_HTML.png)
Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins | Scientific Reports
![The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives | Future Microbiology The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives | Future Microbiology](https://www.futuremedicine.com/cms/10.2217/fmb.12.131/asset/images/medium/figure2.gif)
The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives | Future Microbiology
![2 Schematic organization of HlyA and CyaA RTX toxins. The different... | Download Scientific Diagram 2 Schematic organization of HlyA and CyaA RTX toxins. The different... | Download Scientific Diagram](https://www.researchgate.net/publication/280085087/figure/fig1/AS:582308710760448@1515844623694/Schematic-organization-of-HlyA-and-CyaA-RTX-toxins-The-different-domains-of-the-proteins.png)
2 Schematic organization of HlyA and CyaA RTX toxins. The different... | Download Scientific Diagram
![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-gr2.jpg)
Channel formation by RTX-toxins of pathogenic bacteria: Basis of their biological activity - ScienceDirect
![Single Molecule Force Spectroscopy Reveals the Mechanical Design Governing the Efficient Translocation of the Bacterial Toxin Protein RTX | Journal of the American Chemical Society Single Molecule Force Spectroscopy Reveals the Mechanical Design Governing the Efficient Translocation of the Bacterial Toxin Protein RTX | Journal of the American Chemical Society](https://pubs.acs.org/cms/10.1021/jacs.9b11281/asset/images/large/ja9b11281_0005.jpeg)
Single Molecule Force Spectroscopy Reveals the Mechanical Design Governing the Efficient Translocation of the Bacterial Toxin Protein RTX | Journal of the American Chemical Society
![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-g001.jpg)
Frontiers | Accessory Toxins of Vibrio Pathogens and Their Role in Epithelial Disruption During Infection
![Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins - ScienceDirect Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0022283620305143-ga1.jpg)
Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins - ScienceDirect
![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
![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
![The Vibrio cholerae MARTX toxin simultaneously induces actin collapse while silencing the inflammatory response to cytoskeletal damage | bioRxiv The Vibrio cholerae MARTX toxin simultaneously induces actin collapse while silencing the inflammatory response to cytoskeletal damage | bioRxiv](https://www.biorxiv.org/content/biorxiv/early/2019/09/09/526616/F1.large.jpg)
The Vibrio cholerae MARTX toxin simultaneously induces actin collapse while silencing the inflammatory response to cytoskeletal damage | bioRxiv
![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)
Vibrio cholerae Strains with Mutations in an Atypical Type I Secretion System Accumulate RTX Toxin Intracellularly | Journal of Bacteriology
![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/bc7631811ed777efcfa17b3c0d7a084c9bf96bd1/3-Figure1-1.png)