|
ALO
(Anthrolysin O) |
 |
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
|
ALO
(Anthrolysin O) |
|
Belongs to cholesterol-dependent cytolysin (CDC). CDCs are pore-forming toxins, which require cholesterol in the membrane to form pores with a mechanism not completely clarified. It is generally known that monomers oligomerize into a prepore complex and that this step is followed by a large conformational change in each oligomer, resulting in the insertion into the membrane. ... |
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