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Stichodactyla helianthus Ellis 1768
2012Published as part of Gonzalez-Muñoz, Ricardo, Simões, Nuno, Sanchez-Rodriguez, Judith, Rodriguez, Estefania & Segura-Puertas, Lourdes, 2012, First Inventory of Sea Anemones (Cnidaria: Actiniaria) of the Mexican Caribbean, pp.
Gonzalez-Muñoz, Ricardo +4 more
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Toxicon, 1995
A peptide toxin, ShK, that blocks voltage-dependent potassium channels was isolated from the whole body extract of the Caribbean sea anemone Stichodactyla helianthus. It competes with dendrotoxin I and alpha-dendrotoxin for binding to synaptosomal membranes of rat brain, facilities acetylcholine release at an avian neuromuscular junction and suppresses
Castañeda, O +8 more
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A peptide toxin, ShK, that blocks voltage-dependent potassium channels was isolated from the whole body extract of the Caribbean sea anemone Stichodactyla helianthus. It competes with dendrotoxin I and alpha-dendrotoxin for binding to synaptosomal membranes of rat brain, facilities acetylcholine release at an avian neuromuscular junction and suppresses
Castañeda, O +8 more
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Toxicon, 2002
Stichodactyla helianthus is a sea anemone relatively abundant along Cuban coasts appearing in two morphos with different colors in their tentacles: green or brownish, probably due to their association with algal symbionts. Traditionally, the brownish morpho has been used as a source of sticholysins I and II, the most characterized cytolysins from this ...
Diana, Martínez +8 more
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Stichodactyla helianthus is a sea anemone relatively abundant along Cuban coasts appearing in two morphos with different colors in their tentacles: green or brownish, probably due to their association with algal symbionts. Traditionally, the brownish morpho has been used as a source of sticholysins I and II, the most characterized cytolysins from this ...
Diana, Martínez +8 more
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Chemical synthesis of a neurotoxic polypeptide from the sea anemoneStichodactyla helianthus+
International Journal of Peptide and Protein Research, 1990The sea anemoneStichodactyla helianthusneurotoxin I, a 48‐residue polypeptide, was synthesized by automated solid phase methodology. The fully reduced polypeptide was subsequently refolded in the presence of a glutathione oxidoreduction buffer to the biologically active species containing three disulfide bonds.
M W, Pennington +3 more
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An ouabain-sensitive Na+,K+-ATPase in tentacles of the sea anemone Stichodactyla helianthus
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995Tentacles of Stichodactyla helianthus contain an ouabain-inhibitable, (Na+,K+)-stimulated ATPase. The K0.5 for Na+ was 24 mM and for K+, 3.2 mM. The apparent affinity for ouabain was low, I50 = 10(-4) M. The order of cation affinities was Rb+ > K+ > NH4+ = Cs+.
S C, Specht +3 more
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Sticholysin I (St-I) and sticholysin II (St-II) are cytolysins purified from the sea anemone Stichodactyla helianthus with a high degree of sequence identity (93%) but clearly differenced in their hemolytic activity. In order to go further into the structural determinants for the different behavior of St-I and St-II, we report here the complete amino ...
Vivian Huerta +9 more
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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 of eukaryotic PFTs exclusively found in sea anemones. As for the rest of the members of this family, Sts are cysteine-less proteins, with molecular weights around 20 kDa ...
Carlos Álvarez +5 more
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ShK is a potassium channel blocker from the Caribbean sea anemone Stichodactyla helianthus
Olga Castañeda +4 more
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Actinaria cytolysins are very potent basic toxins isolated from the venom of sea anemones, which are supposed to exert their toxic activity through formation of oligomeric pores in the host plasma membrane. To gain insight into their mechanism of action, the interaction of Stichodactyla helianthus sticholysin I (St-I) with lipid bilayers was studied ...
Mayra Tejuca +4 more
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The major protease inhibitor from the sea anemone Stichodactyla helianthus (ShPI-1) is a non-specific inhibitor that binds trypsin and other trypsin-like enzymes, as well as chymotrypsin, and human neutrophil elastase. We performed site-directed mutagenesis of ShPI-1 to produce two variants (rShPI-1/K13L and rShPI/Y15S) that were expressed in Pichia ...
Rossana García‐Fernández +8 more
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