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UnknownRapid Purification of Endotoxin-Free RTX Toxins.
Not available
S-EPMC6628407 | biostudies-literature
UnknownStructure-Function Relationships of the Repeat Domains of RTX Toxins.
Not available
S-EPMC6891781 | biostudies-literature
ProteomicsA conserved tryptophan in the acylated segment controls β2- integrin-independent cell penetration of RTX toxins
The post-translationally acylated Repeats in ToXins (RTX) leukotoxins, such as the adenylate cyclase (CyaA) or α-hemolysin (HlyA), bind β2-integrins of leukocytes, but also penetrate cells lacking these receptors. We show that the indole of conserved tryptophans within the acylated segments, e.g. W8...
ORGANISM(S): Bordetella pertussis 
2023-07-11 | PXD041207 | Pride
Hydrogen-deuterium exchange Tryptophan residue Adenylate cyclase toxin Α-hemolysin Trp-pro interaction Thermal stability Β2-integrins Rtx toxin Acylated segment Cytotoxicity 
UnknownKingella kingae RtxA Cytotoxin in the Context of Other RTX Toxins.
Not available
S-EPMC8953716 | biostudies-literature
ProteomicsNovel calcium-binding sites in the acylated segment control the folding and membrane penetration of RTX toxins
The Repeats in ToXin (RTX) domain of RTX cytolysins harbors numerous hexacoordinated Ca2+-binding sites that facilitate cooperative and vectorial folding of the RTX β-rolls. Recent study identified Ca2+-binding sites in the acylated N-terminal extension of the RTX domain of Bordetella pertussis aden...
ORGANISM(S): Bordetella pertussis 
2026-04-22 | PXD058094 | Pride
Membrane penetration H/d exchange Rtx toxin Folding Calcium binding site Acylated segment 
UnknownMembrane Interaction Characteristics of the RTX Toxins and the Cholesterol-Dependence of Their Cytolytic/Cytotoxic Activity.
Not available
S-EPMC10970614 | biostudies-literature
ProteomicsSelection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins
Numerous proteins synthesized in cells ranging from bacteria to humans have to be posttranslationally acylated to become biologically active. Bacterial Repeats in ToXin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo a posttranslational acyl...
ORGANISM(S): Escherichia coli Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2020-05-20 | PXD018859 | Pride
Fatty acyl Rtx toxin Acyltransferase Acylation Cytotoxicity 
UnknownDifferent roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins.
Not available
S-EPMC8494930 | biostudies-literature
UnknownNew Insights into the Type II Toxins from the Sea Anemone Heteractis crispa.
Not available
S-EPMC7020476 | biostudies-literature
ProteomicsTwo pairs of back-to-back α-helices of Kingella kingae RtxA toxin are crucial for the formation of a membrane pore
The RtxA cytotoxin, a member of the RTX (Repeats in ToXin) family of pore-forming toxins, is the primary virulence factor of the paediatric facultative pathogen Kingella kingae. Although structure-function studies of RTX toxins have defined their characteristic domains and features, the exact membra...
ORGANISM(S): Kingella sp. (in: b-proteobacteria) 
2025-02-18 | PXD060913 | Pride
Rtx toxins Kingella kingae 
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