![Xf (Temecula) RTX proteins. a Schematic of the Temecula RTX proteins... | Download Scientific Diagram Xf (Temecula) RTX proteins. a Schematic of the Temecula RTX proteins... | Download Scientific Diagram](https://www.researchgate.net/publication/324963528/figure/fig3/AS:962507430711314@1606491062769/Xf-Temecula-RTX-proteins-a-Schematic-of-the-Temecula-RTX-proteins-delimited-into-the.gif)
Xf (Temecula) RTX proteins. a Schematic of the Temecula RTX proteins... | Download Scientific Diagram
![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
![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
![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
![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/095b5d8f-d9cf-45e1-96f3-512d7aeccf34/fmr_231_f5.gif)
RTX proteins: a highly diverse family secreted by a common mechanism - Linhartová - 2010 - FEMS Microbiology Reviews - Wiley Online Library
![Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts - ScienceDirect Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S1097276516300016-gr1.jpg)
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts - ScienceDirect
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![Use of a simple RTX building unit in generation of complex biological... | Download Scientific Diagram Use of a simple RTX building unit in generation of complex biological... | Download Scientific Diagram](https://www.researchgate.net/publication/44654763/figure/fig7/AS:272650622730249@1442016382262/Use-of-a-simple-RTX-building-unit-in-generation-of-complex-biological-functionalities-By.png)
Use of a simple RTX building unit in generation of complex biological... | Download Scientific Diagram
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RTX Adhesins are Key Bacterial Surface Megaproteins in the Formation of Biofilms: Trends in Microbiology
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Type 1 Does the Two-Step: Type 1 Secretion Substrates with a Functional Periplasmic Intermediate | Journal of Bacteriology
![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)