Differential coagulotoxicity of metalloprotease isoforms from Bothrops neuwiedi snake venom and consequent variations in antivenom efficacy
Author:
Funder
Australian Research Council Discovery Project
FAPESP
Publisher
Elsevier BV
Subject
Toxicology,General Medicine
Reference53 articles.
1. Structures of N-glycans of bothrops venoms revealed as molecular signatures that contribute to venom phenotype in viperid snakes;Andrade-Silva;Mol. Cell Proteomics,2018
2. Platelet adhesion receptors and (patho)physiological thrombus formation;Andrews;Histol. Histopathol.,2001
3. BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP;Baldo;Toxicon,2008
4. Mechanisms of vascular damage by hemorrhagic snake venom metalloproteinases: tissue distribution and in situ hydrolysis;Baldo;PLoS Negl. Trop. Dis.,2010
5. Purification and functional characterization of bothrojaractivase, a prothrombin-activating metalloproteinase isolated from Bothrops jararaca snake venom;Berger;Toxicon,2008
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