Publications by authors named "Monrudee Srisaisup"
Binary toxin (Bin toxin), BinA and BinB, produced by has been used as a mosquito-control agent due to its high toxicity against the mosquito larvae. The crystal structures of Bin toxin and non-insecticidal but cytotoxic parasporin-2 toxin share some common structural features with those of the aerolysin-like toxin family, thus suggesting a common mechanism of pore formation of these toxins. Here we explored the possible cytotoxicity of Bin proteins (BinA, BinB and BinA + BinB) against Hs68 and HepG2 cell lines.
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- Vip3Aa protein, produced by Bacillus thuringiensis, is highly toxic to important insect pests like Spodoptera exigua and Spodoptera frugiperda, working by binding to specific midgut receptors and inducing cell death through apoptosis.
- The protein is initially synthesized as a protoxin and requires activation by digestive enzymes to become effective, and its cytotoxic mechanism involves internalization into insect cells and disruption of cell division.
- Research using fluorescent labeling of actVip3Aa revealed that the protein does not rely on clathrin-mediated endocytosis or target mitochondria, indicating a unique intracellular pathway leading to cytotoxicity.
Background: The c-Jun N-terminal kinases (JNKs), members of the mitogen-activated protein kinase (MAPK) family, engage in diverse cellular responses to signals produced under normal development and stress conditions. In Drosophila, only one JNK member is present, whereas ten isoforms from three JNK genes (JNK1, 2, and 3) are present in mammalian cells. To date, several mammalian JNK structures have been determined, however, there has been no report of any insect JNK structure.
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