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Bacterial RTX Toxins Allow Acute ATP Release from Human Erythrocytes Directly through the Toxin Pore* - Journal of Biological Chemistry
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Toxins | Free Full-Text | Structure–Function Relationships of the Repeat Domains of RTX Toxins | HTML
Structural basis for antibody binding to adenylate cyclase toxin reveals RTX linkers as neutralization-sensitive epitopes | PLOS Pathogens
Membrane localization of the Repeats-in-Toxin (RTX) Leukotoxin (LtxA) produced by Aggregatibacter actinomycetemcomitans | PLOS ONE
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Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins | Scientific Reports
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Channel formation by RTX-toxins of pathogenic bacteria: Basis of their biological activity - ScienceDirect
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Coordinated delivery and function of bacterial MARTX toxin effectors - Woida - 2018 - Molecular Microbiology - Wiley Online Library
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Identification of a Vibrio cholerae RTX toxin gene cluster that is tightly linked to the cholera toxin prophage | PNAS
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Channel formation by RTX-toxins of pathogenic bacteria: Basis of their biological activity - ScienceDirect
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In vivo covalent cross‐linking of cellular actin by the Vibrio cholerae RTX toxin | The EMBO Journal
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The Vibrio cholerae MARTX toxin simultaneously induces actin collapse while silencing the inflammatory response to cytoskeletal damage | bioRxiv
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Templated folding of the RTX domain of the bacterial toxin adenylate cyclase revealed by single molecule force spectroscopy | Nature Communications
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