Crotalus durissus terrificus snake venom activates 3T3-L1 preadipocytes to release PGE<sub>2</sub>, which depends on COX-2 expression and is modulated by PGE<sub>2</sub> EP2 receptor. [PDF]
Arch ToxicolTeixeira DS, Maia-Marques R, Teixeira C.
europepmc +1 more source
Isolation and Pharmacological Characterisation of Pre-Synaptic Neurotoxins from Thai and Javanese Russell's Viper (Daboia siamensis) Venoms. [PDF]
Toxins (Basel)Lay M, Hodgson WC.
europepmc +1 more source
Comparative Analysis of the Enzymatic, Coagulant, and Neuromuscular Activities of Two Variants of Crotalus durissus ruruima Venom and Antivenom Efficacy. [PDF]
Pharmaceuticals (Basel)Demico PJ +17 more
europepmc +1 more source
Venom-Derived Enzyme Inhibitors as Anticancer Agents: Structure-Activity Relationships, Molecular Targets and Mechanistic Insights. [PDF]
MoleculesOgundele AV +4 more
europepmc +1 more source
Targeting Key Enzymatic Snake Venom Proteins Using Repurposed Small Molecule Inhibitors: Emerging Adjuncts to Antivenom Therapy. [PDF]
Int J Mol SciReghu N +8 more
europepmc +1 more source
Related searches:
The crotoxin complex is identified as the primary lethal toxin in various species of rattlesnakes. It comprises two subunits: CtxA, a non-toxic protein, and CtxB, a minimally toxic enzymatic phospholipase A2.
Miguel Angel Mejía Sánchez +8 more
semanticscholar +3 more sources
Biochemistry and pharmacology of the crotoxin complex
Naunyn-Schmiedeberg's Archives of Pharmacology, 1971H Breithaupt, E Habermann
exaly +3 more sources