Results 1 to 10 of about 32,635 (169)

Inhibition of a Snake Venom Metalloproteinase by the Flavonoid Myricetin [PDF]

open access: yesMolecules, 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   +7 more sources

Inflammatory effects of snake venom metalloproteinases [PDF]

open access: yesMemorias do Instituto Oswaldo Cruz, 2005
Metalloproteinases are abundant enzymes in crotaline and viperine snake venoms. They are relevant in the pathophysiology of envenomation, being responsible for local and systemic hemorrhage frequently observed in the victims.
Catarina de Fátima Pereira Teixeira   +3 more
doaj   +4 more sources

Preliminary Insights into Geographic Variation in Venom Profiles and Functional Activities of Nigerian Snakes, Bitis arietans and Naja nigricollis [PDF]

open access: yesToxins
Snakebite envenoming is a major yet neglected tropical disease in sub-Saharan Africa, where antivenom efficacy is critically limited by intraspecific venom variation shaped by local ecological pressures. Nigeria’s sharply contrasting Sudan Savanna (North)
Akindele Oluwatosin Adeyi   +11 more
doaj   +2 more sources

Snake Venom Metalloproteinases (SVMPs): A structure-function update

open access: yesToxicon: X, 2020
Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation of fibrinogen and fibrin, induction of apoptosis and inhibition
Olamide Tosin Olaoba   +3 more
doaj   +3 more sources

Transcriptomic Insights Into the Evolution of Snake Venom: Mechanisms, Diversity, and Adaptation. [PDF]

open access: yesScientifica (Cairo)
Snake venoms are evolutionarily refined biochemical arsenals composed of diverse toxins with complex functional roles in predation, defense, and competition. Over the past 2 decades, transcriptomic approaches have transformed venom research by enabling high‐resolution insights into gene expression dynamics, molecular diversity, and the evolutionary ...
Sofyantoro F   +13 more
europepmc   +2 more sources

Animal Venom Pharmacological Resources: Exploiting Bioactive Peptides to Target Multi-Drug-Resistant Bacteria. [PDF]

open access: yesBiochem Res Int
Background The escalating rise of multi–drug‐resistant (MDR) bacterial strains significantly threatens global health, creating a “silent pandemic” prompted by natural selection, gene mutation, and horizontal gene transfer. This crisis is worsened by the deficit in the development of new treatments, necessitating the innovative discovery of new potent ...
Jaber R   +5 more
europepmc   +2 more sources

Purified zymogens reveal mechanisms of snake venom metalloproteinase auto-activation [PDF]

open access: yeseLife
Snake venoms contain diverse mixtures of toxins that evolved to incapacitate prey, but in humans, they cause extensive pathology following snakebite envenomation. In viper venom, some of the most potent toxins are the haemorrhagic and coagulopathic snake
Sophie Hall   +17 more
doaj   +2 more sources

Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom [PDF]

open access: yesToxins, 2016
Russell’s viper bites are potentially fatal from severe bleeding, renal failure and capillary leakage. Snake venom metalloproteinases (SVMPs) are attributed to these effects.
Khin Than Yee   +4 more
doaj   +2 more sources

Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan [PDF]

open access: yesMolecules, 2017
Snake venom metalloproteinases (SVMP) are widely distributed among the venoms of Crotalinae and Viperidae, and are organized into three classes (P-I, P-II and P-III) according to their size and domain structure.
Etsuko Oyama, Hidenobu Takahashi
doaj   +3 more sources

Jararhagin, a hemorrhagic snake venom metalloproteinase from Bothrops jararaca

open access: yesToxicon, 2012
Jararhagin is a metalloproteinase isolated from Bothrops jararaca snake venom, which has been extensively studied. These studies showed its involvement on most of the systemic and local damaging effects of snakebite envenomings. In this review we comment on the major targets of jararhagin as the vascular endothelium, platelets and coagulation factors ...
Ana Maria Moura-Da-Silva
exaly   +3 more sources

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