Lysenin is a pore-forming toxin extracted from earthworms, which inserts large conducting channels in both artificial and natural lipid membranes. Unlike any other pore-forming toxin, Lysenin presents asymmetrical voltage induced gating at depolarizing membrane potentials. Lysenin behaves similar to ion channels by presenting two states, open and closed, and their occupancy is described by a Boltzmann distribution. However, our recordings at high-depolarizing potentials indicate a biphasic response to external voltages, which suggests significant dynamic changes in the energy landscape elicited by channel gating. We associated this unusual response to a potential electromechanical coupling between the voltage domain sensor and the lipid mem...
Lysenin is a pore-forming toxin, which self-inserts open channels into sphingomyelin containing memb...
Transmembrane protein transporters possessing binding sites for ions, toxins, pharmaceutical drugs, ...
This work focuses on understanding the interactions between lysenin, a pore-forming toxin, and ATP. ...
Lysenin, a pore forming toxin (PFT) extracted from Eisenia fetida, inserts voltage-regulated channel...
Lysenin, a Pore Forming Toxin extracted from the earthworm E. foetida, inserts uniform and large con...
AbstractLysenin, a 297 amino acid pore-forming protein extracted from the coelomic fluid of the eart...
The electrochemical gradients established across cell membranes are paramount for the execution of b...
This research work was undertaken to demonstrate that the composition of the lipid environment, modu...
Lysenin, a 297 amino acid pore-forming protein extracted from the coelomic fluid of the earthworm E....
Lysenin, a pore forming toxin extracted from the red earthworm E. fetida, self assembles as a large ...
Memory in physical systems is often viewed as a property of electronic components and computers. How...
The selectivity of ion channels is intrinsic to biological activity in any cell. However, other pore...
All cell membranes are packed with proteins. The ability to investigate the regulatory mechanisms of...
The pore-forming toxin lysenin self-inserts to form conductance channels in natural and artificial l...
Non-specific ion conductance channels can be formed in lipid membranes by the poreforming toxin lyse...
Lysenin is a pore-forming toxin, which self-inserts open channels into sphingomyelin containing memb...
Transmembrane protein transporters possessing binding sites for ions, toxins, pharmaceutical drugs, ...
This work focuses on understanding the interactions between lysenin, a pore-forming toxin, and ATP. ...
Lysenin, a pore forming toxin (PFT) extracted from Eisenia fetida, inserts voltage-regulated channel...
Lysenin, a Pore Forming Toxin extracted from the earthworm E. foetida, inserts uniform and large con...
AbstractLysenin, a 297 amino acid pore-forming protein extracted from the coelomic fluid of the eart...
The electrochemical gradients established across cell membranes are paramount for the execution of b...
This research work was undertaken to demonstrate that the composition of the lipid environment, modu...
Lysenin, a 297 amino acid pore-forming protein extracted from the coelomic fluid of the earthworm E....
Lysenin, a pore forming toxin extracted from the red earthworm E. fetida, self assembles as a large ...
Memory in physical systems is often viewed as a property of electronic components and computers. How...
The selectivity of ion channels is intrinsic to biological activity in any cell. However, other pore...
All cell membranes are packed with proteins. The ability to investigate the regulatory mechanisms of...
The pore-forming toxin lysenin self-inserts to form conductance channels in natural and artificial l...
Non-specific ion conductance channels can be formed in lipid membranes by the poreforming toxin lyse...
Lysenin is a pore-forming toxin, which self-inserts open channels into sphingomyelin containing memb...
Transmembrane protein transporters possessing binding sites for ions, toxins, pharmaceutical drugs, ...
This work focuses on understanding the interactions between lysenin, a pore-forming toxin, and ATP. ...