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The protective antigen component of anthrax toxin forms functional octameric complexes.
The assembly of bacterial toxins and virulence factors is critical to their function, but the regulation of assembly during infection has not been studied. We begin to address this question usingExpand
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Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
The protein transporter anthrax lethal toxin is composed of protective antigen (PA), a transmembrane translocase, and lethal factor (LF), a cytotoxic enzyme. After its assembly into holotoxinExpand
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Rapid induction of inflammatory lipid mediators by the inflammasome in vivo
Detection of microbial products by host inflammasomes is an important mechanism of innate immune surveillance. Inflammasomes activate the caspase-1 (CASP1) protease, which processes the cytokinesExpand
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Structure, inhibition, and regulation of two-pore channel TPC1 from Arabidopsis thaliana
Two-pore channels (TPCs) comprise a subfamily (TPC1-3) of eukaryotic voltage- and ligand-gated cation channels that contain two non-equivalent tandem pore-forming subunits that then dimerize to formExpand
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Structure, inhibition, and regulatory sites of TPC1 from Arabidopsis thaliana
Two-pore channels (TPCs) comprise a subfamily (TPC1–3) of eukaryotic voltage- and ligand-gated cation channels with two non-equivalent tandem pore-forming subunits that dimerize to formExpand
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Anthrax Toxin Receptor Drives Protective Antigen Oligomerization and Stabilizes the Heptameric and Octameric Oligomer by a Similar Mechanism
Background Anthrax toxin is comprised of protective antigen (PA), lethal factor (LF), and edema factor (EF). These proteins are individually nontoxic; however, when PA assembles with LF and EF, itExpand
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Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions
The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization wereExpand
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Role of the protective antigen octamer in the molecular mechanism of anthrax lethal toxin stabilization in plasma.
Anthrax is caused by strains of Bacillus anthracis that produce two key virulence factors, anthrax toxin (Atx) and a poly-gamma-D-glutamic acid capsule. Atx is comprised of three proteins: protectiveExpand
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Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations
The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). LowExpand
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Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen.
The three protein components of anthrax toxin are nontoxic individually, but they form active holotoxin complexes upon assembly. The role of the protective antigen (PA) component of the toxin is toExpand
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