Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes.
By R. Kini. Toxicon, 2003
684 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology, Pharmacology
View Paper: https://www.semanticscholar.org/paper/32eb872eedf992319276fe12011e0e64ce4fc907
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Genetics
In Molecular Biology
In Pharmacology
Citations in the corpus
- Non-canonical proteolytic activation of human prothrombin by subtilisin from Bacillus subtilis may shift the procoagulant–anticoagulant equilibrium toward thrombosis (2017, background): “Proteolytic conversion of ProT to meizothrombin or T can be also performed by exogenous non-physiological activators, such as serine and metallo-proteases present in snake venom (16) or secreted by bacterial cells (17–21).”
- Venom Composition in Rattlesnakes: Trends and Biological Significance (2008, background): “…venoms are known to vary as a function of numerous intrinsic and extrinsic factors, many components are common to venoms of most species, and a high degree of sequence homology exists among specific components, such as the phospholipases (Kini, 1997) and small myotoxins (Mebs and Ownby, 1990).”