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Snake venom proteins" is a generic term for the **diverse set of enzymatic and non-enzymatic proteins and peptides** found in the venom of snakes belonging to multiple families (notably Elapidae, Viperidae, and others)[1][2][3]. These proteins include several major families such as **phospholipase A2, metalloproteases, serine proteases, and three-finger toxins**, among others, each responsible for specific biological effects like neurotoxicity, cytotoxicity, hemotoxicity, and prey immobilization[1][2][3]. Each snake species expresses a distinct cocktail of these proteins, with the relative abundance and presence of specific families varying across taxonomic groups[1][2]. While these proteins are **the direct cause of symptoms seen in snakebite envenomation**, including bleeding, tissue necrosis, coagulation disorders, paralysis, and death, they also represent a toolbox for drug discovery and pathophysiological research[1][2][3]. **Important note:** "Snake venom proteins" is not a single, well-defined molecule or target, but a heterogeneous mix of biomolecules, each with distinct modes of action and potential as individual drug targets or toxins. Therefore, this entry is **too broad for typical structured molecular target curation and is not itself a therapeutic target, but rather a category or mixture**[1]. **Correction:** For structured data curation, focus on individual protein families or specific toxins (e.g., "Snake venom phospholipase A2," "Three-finger toxin," or "Snake venom metalloprotease"), not on the category "snake venom proteins" as a whole.
Block neuromuscular transmission (three-finger toxins and β-bungarotoxins); Hydrolyze phospholipids in cell membranes (phospholipase A2); Proteolytic cleavage of clotting factors and extracellular matrix (metalloproteases, serine proteases); Inhibit platelet aggregation or promote thrombosis (C-type lectins, disintegrins); Cause direct cell lysis (L-amino acid oxidase, others)
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