Bioactive peptides from marine sources: pharmacological properties and isolation procedures

A Aneiros, A Garateix - Journal of Chromatography B, 2004 - Elsevier
Marine organisms represent a valuable source of new compounds. The biodiversity of the
marine environment and the associated chemical diversity constitute a practically unlimited …

Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)

G Anderluh, P Maček - toxicon, 2002 - Elsevier
More than 32 species of sea anemones have been reported to produce lethal cytolytic
peptides and proteins. Based on their primary structure and functional properties, cytolysins …

[HTML][HTML] Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus

CA Valcarcel, M Dalla Serra, C Potrich, I Bernhart… - Biophysical journal, 2001 - cell.com
Abstract Sticholysin I and II (St I and St II), two basic cytolysins purified from the Caribbean
sea anemone Stichodactyla helianthus, efficiently permeabilize lipid vesicles by forming …

Molecular mechanism of pore formation by actinoporins

KČ Kristan, G Viero, M Dalla Serra, P Maček… - Toxicon, 2009 - Elsevier
Actinoporins are effective pore-forming toxins produced by sea anemones. These extremely
potent, basic 20kDa proteins readily form pores in membranes that contain sphingomyelin …

[HTML][HTML] Sticholysins, two pore-forming toxins produced by the Caribbean Sea anemone Stichodactyla helianthus: their interaction with membranes

C Alvarez, JM Mancheno, D Martínez, M Tejuca… - Toxicon, 2009 - Elsevier
Sticholysins (Sts) I and II (StI/II) are pore-forming toxins (PFTs) produced by the Caribbean
Sea anemone Stichodactyla helianthus belonging to the actinoporin family, a unique class …

Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation

MG Hinds, W Zhang, G Anderluh, PE Hansen… - Journal of molecular …, 2002 - Elsevier
Sea anemones produce a family of 18–20 kDa proteins, the actinoporins, that lyse cells by
forming pores in cell membranes. Sphingomyelin plays an important role in their lytic activity …

Sizing the Radius of the Pore Formed in Erythrocytes and Lipid Vesicles by the Toxin Sticholysin I from the Sea Anemone Stichodactyla helianthus

M Tejuca, M Dalla Serra, C Potrich, C Alvarez… - The Journal of …, 2001 - Springer
The radius of the pore formed by sticholysin I and II (StI, StII) in erythrocytes and sticholysin I
in lipid vesicles was investigated. The rate of colloid osmotic lysis of human erythrocytes …

[HTML][HTML] Binding specificity of sea anemone toxins to Nav 1.1-1.6 sodium channels: unexpected contributions from differences in the IV/S3-S4 outer loop

JS Oliveira, E Redaelli, AJ Zaharenko… - Journal of Biological …, 2004 - ASBMB
Sea anemones are an important source of various biologically active peptides, and it is
known that ATX-II from Anemonia sulcata slows sodium current inactivation. Using six …

[HTML][HTML] Damage of eukaryotic cells by the pore-forming toxin sticholysin II: Consequences of the potassium efflux

S Cabezas, S Ho, U Ros, ME Lanio, C Alvarez… - … et Biophysica Acta (BBA …, 2017 - Elsevier
Pore-forming toxins (PFTs) form holes in membranes causing one of the most catastrophic
damages to a target cell. Target organisms have evolved a regulated response against PFTs …

Development of a rational nomenclature for naming peptide and protein toxins from sea anemones

JS Oliveira, D Fuentes-Silva, GF King - Toxicon, 2012 - Elsevier
Sea anemone toxins are predominantly peptide and proteins that act mainly on sodium and
potassium channels, as well as in a variety of target cells causing lysis. Over recent years …