Results 61 to 70 of about 157 (83)

Tissue damaging toxins in snake venoms: mechanisms of action, pathophysiology and treatment strategies. [PDF]

open access: yesCommun Biol
Bittenbinder MA   +6 more
europepmc   +1 more source

Dermonecrosis caused by a spitting cobra snakebite results from toxin potentiation and is prevented by the repurposed drug varespladib. [PDF]

open access: yesProc Natl Acad Sci U S A
Bartlett KE   +13 more
europepmc   +1 more source

Varespladib Inhibits the Phospholipase A<sub>2</sub> and Coagulopathic Activities of Venom Components from Hemotoxic Snakes. [PDF]

open access: yesBiomedicines, 2020
Xie C   +9 more
europepmc   +1 more source

Articles You May Have Missed. [PDF]

open access: yesJ Med Toxicol, 2018
Goodnough R   +3 more
europepmc   +1 more source
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Varespladib (LY315920) prevents neuromuscular blockage and myotoxicity induced by crotoxin on mouse neuromuscular preparations

Toxicon, 2021
Varespladib (LY315920) is a synthetic phospholipase A2 (PLA2) inhibitor that has been demonstrating antiophidic potential against snake venoms that present PLA2 neurotoxins. In this study, we evaluate the capacity of Varespladib to inhibit the neuromuscular effects of crotoxin (CTX), the main toxic component of Crotalus durissus terrificus snake venom,
Walter Cavalcante   +2 more
exaly   +3 more sources

Varespladib (LY315920) inhibits neuromuscular blockade induced by Oxyuranus scutellatus venom in a nerve-muscle preparation

Toxicon, 2020
The phospholipase A2 (PLA2) inhibitors varespladib (LY315920) and its orally available derivative methyl-varespladib (LY333013) have been proposed as potential therapies for the treatment of snakebite envenomings in which toxicity depends on the action of PLA2s.
José Maria Gutierrez   +2 more
exaly   +3 more sources

Varespladib (LY315920) neutralises phospholipase A2 mediated prothrombinase-inhibition induced by Bitis snake venoms

Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology, 2020
Anticoagulant toxicity is a common function of venoms produced by species within the Bitis genus. Potent inhibition of the prothrombinase complex is an identified mechanism of action for the dwarf species B. cornuta and B. xeropaga, along with some localities of B. atropos and B. caudalis.
Bryan Fry   +2 more
exaly   +6 more sources

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