Results 31 to 40 of about 1,026 (176)

Pharmacological characterization of cnidarian extracts from the Caribbean Sea: evaluation of anti-snake venom and antitumor properties

Journal of Venomous Animals and Toxins including Tropical Diseases, 2018
Background Cnidarians produce toxins, which are composed of different polypeptides that induce pharmacological effects of biotechnological interest, such as antitumor, antiophidic and anti-clotting activities.
Cláudia S. Oliveira, Cleópatra A. S. Caldeira, Rafaela Diniz-Sousa, Dolores L. Romero, Silvana Marcussi, Laura A. Moura, André L. Fuly, Cicília de Carvalho, Walter L. G. Cavalcante, Márcia Gallacci, Maeli Dal Pai, Juliana P. Zuliani, Leonardo A. Calderon, Andreimar M. Soares   +13 more
doaj   +1 more source

Toxin-induced pore formation is hindered by intermolecular hydrogen bonding in sphingomyelin bilayers [PDF]

, 2016
Sticholysin I and II (StnI and StnII) are pore-forming toxins that use sphingomyelin (SM) for membrane binding. We examined how hydrogen bonding among membrane SMs affected the StnI- and StnII-induced pore formation process, resulting in bilayer ...
García Linares, Sara, Gavilanes, José G., Martínez del Pozo, Álvaro, Palacios Ortega, Juan, Slotte, J. Peter, Yasuda, Tomokazu, Åstrand, Mia   +6 more
core   +2 more sources

Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assembly. [PDF]

PLoS ONE, 2014
The use of pore-forming toxins in the construction of immunotoxins against tumour cells is an alternative for cancer therapy. In this protein family one of the most potent toxins are the actinoporins, cytolysins from sea anemones.
Valeria Antonini, Victor Pérez-Barzaga, Silvia Bampi, David Pentón, Diana Martínez, Mauro Dalla Serra, Mayra Tejuca   +6 more
doaj   +1 more source

ESTICOLISINA II, UNA CITOLISINA AISLADA DEL ANÉMONA DEL MAR CARIBE Stichodactyla helianthus, INTERACTÚA CON LIPOPROTEÍNAS SÉRICAS, FREUND ANTICUERPOS ADYUVANTES Y ESPECÍFICOS A ESTA PROTEÍNA

Revista de Investigaciones Marinas, 2023
Sticholisina II (St II) es una citolisina aislada de la anémona marina Stichodactyla helianthus. Esta proteína hidrofilica forma poros en las membranas celulares, lo que provoca el desbalance osmótico que conduce a la lisis celular.
Ariel Basulto Perdomo, Isis Casadelvalle Pérez, Anselmo Otero González, María C. Pico Beltrán   +3 more
doaj  

Reproductive biology of the sea anemone shrimp Periclimenes rathbunae (Caridea, Palaemonidae, Pontoniinae), from the Caribbean coast of Costa Rica

ZooKeys, 2014
Caridean shrimps are a highly diverse group and many species form symbiotic relationships with different marine invertebrates. Periclimenes rathbunae is a brightly colored shrimp that lives predominantly in association with sea anemones.
Juan Carlos Azofeifa-Solano, Marcelo Elizondo-Coto, Ingo Wehrtmann   +2 more
doaj   +1 more source

Calorimetric scrutiny of lipid binding by sticholysin II toxin mutants [PDF]

, 2008
The mechanisms by which pore-forming toxins are able to insert into lipid membranes are a subject of the highest interest in the field of lipid–protein interaction.
Alegre Cebollada, Jorge, Cunietti, Michela, Gavilanes, José G., Herrero Galán, Elías, Martínez del Pozo, Álvaro   +4 more
core   +2 more sources

Pharmacological effects of two cytolysins isolated from the sea anemone Stichodactyla helianthus

Journal of Biosciences, 2009
Sticholysins I and II (St I/II) are cytolysins purified from the sea anemone Stichodactyla helianthus. In this study, we show their pharmacological action on guinea-pig and snail models in native and pH-denatured conditions in order to correlate the pharmacological findings with the pore-forming activity of both isoforms.
T, García, D, Martinez, A, Palmero, C, Soto, M, Tejuca, F, Pazos, R, Menéndez, C, Alvarez, A, Garateix   +8 more
openaire   +2 more sources

Sea Anemones: Quiet Achievers in the Field of Peptide Toxins

Toxins, 2018
Sea anemones have been understudied as a source of peptide and protein toxins, with relatively few examined as a source of new pharmacological tools or therapeutic leads. This is surprising given the success of some anemone peptides that have been tested,
Peter J. Prentis, Ana Pavasovic, Raymond S. Norton   +2 more
doaj   +1 more source

Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1)using GST affinity purification and SILAC-based quantitative proteomics [PDF]

, 2017
Hydra actinoporin-like toxin-1 (HALT-1) is a 20.8 kDa pore-forming toxin isolated from Hydra magnipapillata. HALT-1 shares structural similarity with actinoporins, a family that is well known for its haemolytic and cytolytic activity.
Ameirika, ., Hong, Xi Sha, Hwang, Jung Shan *   +2 more
core   +1 more source

Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals [PDF]

, 2013
The Kunitz-type protease inhibitors are the best-characterized family of serine protease inhibitors, probably due to their abundance in several organisms.
Mourão, Caroline Barbosa Farias, Schwartz, Elisabeth Nogueira Ferroni   +1 more
core   +3 more sources