Crystal structure of a phospholipase A2 from Bothrops asper venom: Insights into a new putative "myotoxic cluster".
Sign Up to like & getrecommendations! Published in 2017 at "Biochimie"
DOI: 10.1016/j.biochi.2016.12.015
Abstract: Snake venoms from the Viperidae and Elapidae families often have several phospholipases A2 (PLA2s), which may display different functions despite having a similar structural scaffold. These proteins are considered an important target for the development… read more here.
Keywords: bothrops asper; myotoxic; pla2s; structure ... See more keywords
In Vivo Neutralization of Myotoxin II, a Phospholipase A2 Homologue from Bothrops asper Venom, Using Peptides Discovered via Phage Display Technology
Sign Up to like & getrecommendations! Published in 2022 at "ACS Omega"
DOI: 10.1021/acsomega.2c00280
Abstract: Many snake venom toxins cause local tissue damage in prey and victims, which constitutes an important pathology that is challenging to treat with existing antivenoms. One of the notorious toxins that causes such effects is… read more here.
Keywords: display technology; bothrops asper; homologue; phage display ... See more keywords
Antivenomics and in vivo preclinical efficacy of six Latin American antivenoms towards south-western Colombian Bothrops asper lineage venoms.
Sign Up to like & getrecommendations! Published in 2021 at "PLoS neglected tropical diseases"
DOI: 10.1371/journal.pntd.0009073
Abstract: BACKGROUND Bothrops asper represents the clinically most important snake species in Central America and Northern South America, where it is responsible for an estimated 50-80% of snakebites. Compositional variability among the venom proteomes of B.… read more here.
Keywords: asper lineages; bothrops asper; asper lineage; latin american ... See more keywords
Molecular Architecture of the Antiophidic Protein DM64 and its Binding Specificity to Myotoxin II From Bothrops asper Venom
Sign Up to like & getrecommendations! Published in 2022 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2021.787368
Abstract: DM64 is a toxin-neutralizing serum glycoprotein isolated from Didelphis aurita, an ophiophagous marsupial naturally resistant to snake envenomation. This 64 kDa antitoxin targets myotoxic phospholipases A2, which account for most local tissue damage of viperid… read more here.
Keywords: dm64; asper venom; toxin; bothrops asper ... See more keywords