Increased Stability upon Heptamerization of the Pore-forming Toxin Aerolysin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Aerolysin - the ins and outs of a model channel-forming toxin
2. Membrane insertion: The strategies of toxins (Review)
3. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
4. Dimerization stabilizes the pore-forming toxin aerolysin in solution.
5. Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation
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1. Aerolysin nanopore structure revealed at high resolution in lipid environment;2024-08-12
2. Electrical Sensing and Discrimination of Different States of Myoglobin Through Solid-State Nanopore;Nanoscience and Nanotechnology Letters;2019-09-01
3. An IL‐2 proaerolysin fusion toxin that selectively eliminates regulatory t cells to enhance antitumor immune response;The Prostate;2019-05-06
4. Dynamics of a polyelectrolyte through aerolysin channel as a function of applied voltage and concentration⋆;The European Physical Journal E;2018-05
5. Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family;Scientific Reports;2017-10-24
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