Results 31 to 40 of about 461 (139)
Marine Drugs, 2015 Actinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members.
Sara García-Linares +5 more
doaj +1 more source
Properties of St I and St II, two isotoxins isolated from Stichodactyla helianthus: a comparison
Toxicon, 2001 Sticholysins I and II are two highly hemolytic polypeptides purified from the Caribbean Sea anemone Stichodactyla helianthus. Their high sequence homology (93%) indicates that they correspond to isoforms of the same hemolysin. The spectroscopic measurements show a close similarity in the secondary structure content, conformation and stability of both ...
Martinez, D +9 more
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The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels
Toxins, 2016 The bovine pancreatic trypsin inhibitor (BPTI)-Kunitz-type protein ShPI-1 (UniProt: P31713) is the major protease inhibitor from the sea anemone Stichodactyla helianthus.
Rossana García-Fernández +6 more
doaj +1 more source
Toxicon, 1989 The ability of a purified sea anemone (Stichodactyla helianthus) protein cytolysin to interact with a variety of interfaces was investigated by means of the Wilhemy plate method. At the air:water and lipid:water interfaces, the toxin lowered the surface pressure most readily as the aqueous phase pH increased towards the isoelectric point (9.8) of the ...
Department of Pharmacology and Therapeutics, College of Medicine, University of Florida, Gainesville, FL 32610, U.S.A. ( host institution ) +3 more
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Development of Highly Selective Kv1.3-Blocking Peptides Based on the Sea Anemone Peptide ShK
Marine Drugs, 2015 ShK, from the sea anemone Stichodactyla helianthus, is a 35-residue disulfide-rich peptide that blocks the voltage-gated potassium channel Kv1.3 at ca. 10 pM and the related channel Kv1.1 at ca. 16 pM.
Michael W. Pennington +7 more
doaj +1 more source
Toxicon, 2009 Sticholysin II (St II) is a toxin from the sea anemona Stichodactyla helianthus that produces erythrocytes lysis at low concentration and its activity depends on the presence of calcium. Calcium may act modifying toxin interaction with erythrocyte membranes or activating cellular processes which may result in a modified St II lytic action.
Celedon, Gloria +9 more
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Proteins: Structure, Function, and Bioinformatics, Volume 92, Issue 2, Page 192-205, February 2024.Abstract Diverse structural scaffolds have been described in peptides from sea anemones, with the ShKT domain being a common scaffold first identified in ShK toxin from Stichodactyla helianthus. ShK is a potent blocker of voltage‐gated potassium channels (KV1.x), and an analog, ShK‐186 (dalazatide), has completed Phase 1 clinical trials in plaque ...
Karoline Sanches +9 more
wiley +1 more source
Toxicon, 2006 Sticholysins I and II (Sts I and II) are two potent cytolysins from the sea anemone Stichodactyla helianthus. These isoforms present 13 substitutions, with three non-conservative located at the N-terminus. St II is considerably more hemolytic than St I in human red blood cells, a result explained by the smaller number of negatively charged groups ...
Pazos, F. +15 more
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Anales de la Academia de Ciencias de Cuba, 2021 Introducción: Las estrategias vacunales para potenciar respuestas de linfocitos T CD8+ citotóxicos (CTL) constituyen un reto debido a la necesidad de favorecer la presentación cruzada de antígenos (Ag) exógenos por las células presentadoras de antígenos (
María Eliana Lanio Ruiz +9 more
doaj
FEBS Letters, 1999 Sticholysin II (Stn‐II) is a pore‐forming cytolysin. Stn‐II interacts with several supports for size exclusion chromatography, which results in an abnormal retardation precluding molecular mass calculations. Sedimentation equilibrium analysis has revealed that the protein is an associating system at neutral pH.
de los Rı́os, Vivian +6 more
openaire +2 more sources