Results 11 to 20 of about 1,026 (176)

Two-dimensional crystallization on lipid monolayers and three-dimensional structure of sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus. [PDF]

Biophys J, 2000
Sticholysin II (Stn II), a potent cytolytic protein isolated from the sea anemone Stichodactyla helianthus, has been crystallized on lipid monolayers. With Fourier-based methods, a three-dimensional (3D) model of Stn II, up to a resolution of 15 A, has been determined. The two-sided plane group is p22(1)2, with dimensions a = 98 A, b = 196 A.
Martín-Benito J, Gavilanes F, de Los Ríos V, Mancheño JM, Fernández JJ, Gavilanes JG.   +5 more
europepmc   +5 more sources

Recombinant Analogs of Sea Anemone Kunitz-Type Peptides Influence P2X7 Receptor Activity in Neuro-2a Cells. [PDF]

Mar Drugs, 2023
Purinergic P2X7 receptors (P2X7) have now been proven to play an important role and represent an important therapeutic target in many pathological conditions including neurodegeneration.
Pislyagin EA, Menchinskaya ES, Gladkikh IN, Kvetkina AN, Sintsova OV, Popkova DV, Kozlovskiy SA, Gorpenchenko TY, Likhatskaya GN, Kaluzhskiy LA, Ivanov AS, Andreev YA, Kozlov SA, Dmitrenok PS, Aminin DL, Leychenko EV.   +15 more
europepmc   +3 more sources

Efecto agregante plaquetario de 2 citolisinas: Sti y Stii purificadas de la anémona marina Stichodactyla Helianthus Platelet aggregating effect of 2 cytolysins: StI and StII purified from the sea anemone Stichodactyla helianthus

Revista Cubana de Hematología, Inmunología y Hemoterapia, 1999
Las citolisinas Sticholysina I (St I) y Sticholysina II (St II) inducen la agregación plaquetaria en el plasma rico en plaquetas en el rango de concentraciones ensayadas (0,5 a 10 µg/mL).
Alina Díaz Concepción, Alberto Brito Martínez, Mayra Tejuca Martínez, Carlos Álvarez Valcárcel, María E Lanio, Delfina Almagro Vázquez, Marianela Estrada del Cueto   +6 more
doaj   +2 more sources

Structural and functional characterization of Sticholysin III: A newly discovered actinoporin within the venom of the sea anemone Stichodactyla helianthus. [PDF]

Archives of Biochemistry and Biophysics, 2020
Actinoporins are a family of pore-forming toxins produced by sea anemones as part of their venomous cocktail. These proteins remain soluble and stably folded in aqueous solution, but when interacting with sphingomyelin-containing lipid membranes, they ...
Garb, Jessica E., Gavilanes, José G., Martínez del Pozo, Álvaro, Palacios Ortega, Juan, Rivera de Torre, Esperanza, Slotte, J. Peter   +5 more
core   +6 more sources

Sticholysin II, a cytolysin from the sea anemoneStichodactyla helianthus, is a monomer‐tetramer associating protein [PDF]

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.
Vivian de los Rı́os, José M. Mancheño, Álvaro Martínez‐del‐Pozo, Carlos Alfonso, Germán Rivas, Mercedes Oñaderra, José G. Gavilanes   +6 more
openalex   +3 more sources

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 ...
Diana Martínez Hernández, A. M. Campos, Fabiola Pazos, Carlos Álvarez, María E. Lanio, Fábio Casallanovo, Shirley Schreier, Roberto Köpke Salinas, Cecilia Vergara, E. A. Lissi   +9 more
openalex   +6 more sources

Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus

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 ...
Fabiola Pazos, Aisel Valle Garay, Diana Martínez Hernández, Angel Rafael Ramirez-Ramirez, Lesly Calderón, Amaury Pupo, Mayra Tejuca, Vivian Morera, Javier Campos, Rafael Fando, Fábio Henrique Dyszy, Shirley Schreier, E. Horjales, Carlos Álvarez, María E. Lanio, E. A. Lissi   +15 more
openalex   +6 more sources

The NMR solution structure of a Kunitz‐type proteinase inhibitor from the sea anemone Stichodactyla helianthus [PDF]

European Journal of Biochemistry, 1993
The solution structure of a 55‐amino‐acid Kunitz‐type proteinase inhibitor, ShPI, purified from the Caribbean sea anemone Stichodactyla helianthus, was determined by NMR spectroscopy. Nearly complete sequence‐specific 1H‐NMR assignments were obtained at pH 4.6 and 36°C, and stereospecific assignments were determined for 23 pairs of diastereotopic ...
Walfrido Antuch, Kurt D. Berndt, María Á. Chávez, Julieta Delfín, Kurt Wüthrich   +4 more
openalex   +3 more sources

Effect of calcium on the hemolytic activity of Stichodactyla helianthus toxin sticholysin II on human erythrocytes

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.
Gloria Celedón, Gustavo González, E. A. Lissi, Tania Cerda, Diana Martínez Hernández, Carmen Soto, Mario Pupo-Meriño, Fabiola Pazos, María E. Lanio, Carlos Álvarez   +9 more
openalex   +6 more sources

Sticholysin I–II oligomerization in the absence of membranes

FEBS Letters, Volume 596, Issue 8, Page 1029-1036, April 2022., 2022
In this study, the oligomerization in solution of StnI and StnII, two pore‐forming toxins produced by Stichodactyla helianthus, has been studied using analytical ultracentrifugation. Our results show that while StnI is more prone to oligomerize than StnII when assayed independently, the addition of a small amount of StnII favours oligomerization ...
Sara García‐Linares, Rafael Amigot‐Sánchez, Carmen García‐Montoya, Diego Heras‐Márquez, Carlos Alfonso, Juan Román Luque‐Ortega, José G. Gavilanes, Álvaro Martínez‐del‐Pozo, Juan Palacios‐Ortega   +8 more
wiley   +1 more source