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Tertiary structural changes of the alpha-hemolysin from Staphylococcus aureus on association with liposome membranes
(Academic Press Inc., 1998-03-01)
The interaction of alpha-hemolysin (also called alpha-toxin) from Staphylococcus aureus with mixed egg-yolk phosphatidylcholine/cholesterol liposomes has been investigated using the intrinsic tryptophan fluorescence emission ...
Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins
(Elsevier B.V., 2019-01-01)
Sticholysin I and II (Sts: St I and St II) are proteins of biomedical interest that form pores upon the insertion of their N-terminus in the plasma membrane. Peptides spanning the N-terminal residues of StI (StI(1-31)) or ...
Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
(Nature Publishing Group, 2018-12)
The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, ...
Exaptation of two ancient immune proteins into a new dimeric pore-forming toxin in snails
(Academic Press Inc Elsevier Science, 2020-08-01)
The Membrane Attack Complex-Perforin (MACPF) family is ubiquitously found in all kingdoms. They have diverse cellular roles, however MACPFs with pore-forming toxic function in venoms and poisons are very rare in animals. ...
Obtaining structural data of the pore-forming region of the Shaker potassium channel using the scorpion toxin Agitoxin2
(Universisdad de Chile, 1995)
Los canales de K+ constituyen el grupo mas diverso
dentro de la familia de los canales iónicos. Ellos se
activan en respuesta a cambios en el potencial de membrana,
a segundos mensajeros como AMPc o Ca2+ y vía proteína ...