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Conjugation of manganese ferrite nanoparticles to an anti Sticholysin monoclonal antibody and conjugate applications
(Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2013-01-16)
Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins
(Elsevier B.V., 2007-12-15)
Sticholysins I and II (St I and St II) are cytolysins produced by the sea anemone Stichodactyla helianthus. In spite of their 93% sequence homology, St II is more hemolytic against human erythrocytes than St 1. In order ...
Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins
(Elsevier B.V., 2007-12-15)
Sticholysins I and II (St I and St II) are cytolysins produced by the sea anemone Stichodactyla helianthus. In spite of their 93% sequence homology, St II is more hemolytic against human erythrocytes than St 1. In order ...
The pore forming capacity of Sticholysin I in dipalmitoyl phosphatidyl vesicles is tuned by osmotic stress
(Elsevier, 2017)
The osmotic condition modulates the properties of liposomes, particularly those related to their
stability and response to external agents such as membrane-active proteins or peptides. In a
previous work, we have ...
The pore forming capacity of Sticholysin I in dipalmitoyl phosphatidyl vesicles is tuned by osmotic stress
(Elsevier, 2017)
The osmotic condition modulates the properties of liposomes, particularly those related to their
stability and response to external agents such as membrane-active proteins or peptides. In a
previous work, we have ...
The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition
(Indian Acad Sciences, 2011-12-01)
The sea anemone Stichodactyla helianthus produces two pore-forming proteins, sticholysins I and II (St I and St II). Despite their high identity (93%), these toxins exhibit differences in hemolytic activity that can be ...
Cys mutants in functional regions of Sticholysin I clarify the participation of these residues in pore formation
(PERGAMON-ELSEVIER SCIENCE LTD, 2011)
Experimental evidence shows that the mechanism of pore formation by actinoporins is a multistep process, involving binding of the water-soluble monomer to the membrane and subsequent oligomerization on the membrane surface, ...
Functional and Topological Studies with Trp-Containing Analogs of the Peptide StII(1-30) Derived From the N-Terminus of the Pore Forming Toxin Sticholysin II: Contribution to Understand its Orientation in Membrane
(Wiley-Blackwell, 2013-07-01)
Sticholysin II (St II) is the most potent cytolysin produced by the sea anemone Stichodactyla helianthus, exerting hemolytic activity via pore formation in membranes. The toxin's N-terminus contains an amphipathic alpha-helix ...
Cys mutants in functional regions of Sticholysin I clarify the participation of these residues in pore formation
(2011)
Experimental evidence shows that the mechanism of pore formation by actinoporins is a multistep process, involving binding of the water-soluble monomer to the membrane and subsequent oligomerization on the membrane surface, ...