Inhibition of a Snake Venom Metalloproteinase by the Flavonoid Myricetin [PDF]
Molecules, 2018 Most of the snakebite envenomations in Central and South America are caused by species belonging to Bothrops genus. Their venom is composed mainly by zinc-dependent metalloproteinases, responsible of the hemorrhage characteristic of these envenomations ...
Lina María Preciado +4 more
doaj +8 more sources
Snakebite drug discovery: high-throughput screening to identify novel snake venom metalloproteinase toxin inhibitors. [PDF]
Front Pharmacol, 2023 Snakebite envenoming results in ∼100,000 deaths per year, with close to four times as many victims left with life-long sequelae. Current antivenom therapies have several limitations including high cost, variable cross-snake species efficacy and a ...
Clare RH +10 more
europepmc +2 more sources
Data on global expression of non-coding RNome in mice gastrocnemius muscle exposed to jararhagin, snake venom metalloproteinase [PDF]
Data in Brief, 2016 This article describes the data on the global expression profile of small RNA (smRNAs) molecules in mice gastrocnemius muscle exposed to jararhagin, snake venom metalloproteinase.
Patricia Bianca Clissa +4 more
doaj +3 more sources
Complement System Inhibition Modulates the Pro-Inflammatory Effects of a Snake Venom Metalloproteinase. [PDF]
Front Immunol, 2019 Envenomation by Bothrops snakes causes prominent local effects, including pain, oedema, local bleeding, blistering and necrosis, and systemic manifestations, such as hemorrhage, hypotension, shock and acute renal failure.
Luchini LSG +3 more
europepmc +2 more sources
Potential of Matrix Metalloproteinase Inhibitors for the Treatment of Local Tissue Damage Induced by a Type P-I Snake Venom Metalloproteinase. [PDF]
Toxins (Basel), 2019 Snake bite envenoming is a public health problem that was recently included in the list of neglected tropical diseases of the World Health Organization.
Preciado LM, Pereañez JA, Comer J.
europepmc +2 more sources
Comprehensive Study of the Proteome and Transcriptome of the Venom of the Most Venomous European Viper: Discovery of a New Subclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived Proteins. [PDF]
J Proteome Res, 2019 The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes (Vaa), in particular, is, medically, one of the most relevant snakes in Europe.
Leonardi A +3 more
europepmc +2 more sources
Interactions between Triterpenes and a P-I Type Snake Venom Metalloproteinase: Molecular Simulations and Experiments. [PDF]
Toxins (Basel), 2018 Small molecule inhibitors of snake venom metalloproteinases (SVMPs) could provide a means to rapidly halt the progression of local tissue damage following viperid snake envenomations.
Preciado LM +3 more
europepmc +2 more sources
Corrigendum: Complement System Inhibition Modulates the Pro-Inflammatory Effects of a Snake Venom Metalloproteinase. [PDF]
Front Immunol, 2019 [This corrects the article DOI: 10.3389/fimmu.2019.01137.].
Luchini LSG +3 more
europepmc +2 more sources
Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase. [PDF]
Toxins (Basel), 2017 Hemorrhage is the most prominent effect of snake venom metalloproteinases (SVMPs) in human envenomation. The capillary injury is a multifactorial effect caused by hydrolysis of the components of the basement membrane (BM).
Freitas-de-Sousa LA +4 more
europepmc +2 more sources
P-I snake venom metalloproteinase is able to activate the complement system by direct cleavage of central components of the cascade. [PDF]
PLoS Neglected Tropical Diseases, 2013 BACKGROUND: Snake Venom Metalloproteinases (SVMPs) are amongst the key enzymes that contribute to the high toxicity of snake venom. We have recently shown that snake venoms from the Bothrops genus activate the Complement system (C) by promoting direct ...
Giselle Pidde-Queiroz +7 more
doaj +2 more sources