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From Venom to Vein: Factor VII Activation as a Major Pathophysiological Target for Procoagulant Australian Elapid Snake Venoms [PDF]

open access: yesToxins
Australian elapid snake venoms are uniquely procoagulant, utilizing blood clotting enzyme Factor Xa (FXa) as a toxin, which evolved as a basal trait in this clade.
Uthpala Chandrasekara   +5 more
doaj   +4 more sources

Differential Effects of Marimastat and Prinomastat on the Metalloprotease Activity of Various Snake Venoms [PDF]

open access: yesToxins
Snakebite envenoming is a neglected tropical disease, responsible for approximately 140,000 deaths globally each year. Vipers and elapid snakes represent the most significant snake families in medical contexts, exhibiting a variety of venom components ...
Mahtab Khatibi   +6 more
doaj   +2 more sources

Heterologous expression, protein folding and antibody recognition of a neurotoxin from the Mexican coral snake Micrurus laticorallis [PDF]

open access: yesJournal of Venomous Animals and Toxins including Tropical Diseases, 2016
Background The cysteine-rich neurotoxins from elapid venoms are primarily responsible for human and animal envenomation; however, their low concentration in the venom may hamper the production of efficient elapid antivenoms.
Herlinda Clement   +5 more
doaj   +2 more sources

Profiling cytotoxicity of nanofractionated elapid snake venoms in human cell lines representing different tissues [PDF]

open access: yesJournal of Pharmaceutical Analysis
Elapid snakebites cause severe toxicity, predominantly neurotoxicity and general cytotoxicity. However, the specific cellular impacts of individual venom toxins remain largely underexplored.
Haifeng Xu   +5 more
doaj   +2 more sources

Venom Down Under: Dynamic Evolution of Australian Elapid Snake Toxins [PDF]

open access: yesToxins, 2013
Despite the unparalleled diversity of venomous snakes in Australia, research has concentrated on a handful of medically significant species and even of these very few toxins have been fully sequenced.
Timothy N. W. Jackson   +9 more
doaj   +4 more sources

Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom. [PDF]

open access: yesPLoS ONE, 2012
Snake venoms are rich sources of biologically active proteins and polypeptides. Three-finger toxins are non-enzymatic proteins present in elapid (cobras, kraits, mambas and sea snakes) and colubrid venoms.
Vallerinteavide Mavelli Girish   +5 more
doaj   +11 more sources

A polygeneric immunogen composed of 22 venoms from sub-Saharan African snakes to expand the neutralization scope of the EchiTAb-plus-ICP antivenom [PDF]

open access: yesToxicon: X
Recent research suggests that a polygeneric immunogen made from the venoms of the most medically important viperid and elapid snakes in sub-Saharan Africa could elicit a broader antibody response in horses compared to the current EchiTAb-plus-ICP ...
Andrés Sánchez   +16 more
doaj   +2 more sources

X Marks the Clot: Evolutionary and Clinical Implications of Divergences in Procoagulant Australian Elapid Snake Venoms [PDF]

open access: yesToxins
Australian elapid snakes possess potent procoagulant venoms, capable of inducing severe venom-induced consumption coagulopathy (VICC) in snakebite victims through rapid activation of the coagulation cascade by converting the FVII and prothrombin zymogens
Holly Morecroft   +5 more
doaj   +2 more sources

Heating up the Blunts: Prothrombin Activation, with Factor Va as an Obligate Cofactor, Is the Dominant Procoagulant Mechanism of Blunt-Nosed Viper Venoms (Macrovipera Species) [PDF]

open access: yesToxins
Venoms of the Palearctic vipers in the Macrovipera genus cause severe procoagulant clinical effects, yet the precise molecular targets remain incompletely defined. To fill this toxicological knowledge gap, we tested five Macrovipera venoms—M.
Patrick S. Champagne   +2 more
doaj   +2 more sources

Assessing the Utility of Broad-Acting Inhibitors as Therapeutics in Diverse Venoms [PDF]

open access: yesToxins
Examination of venom constituent bioactivities from diverse venomous animals shows certain highly conserved classes, including enzymes (e.g., phospholipases and metalloproteinases) and pore-forming proteins.
Raechel Kadler   +2 more
doaj   +2 more sources

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