Three toxins, two receptors, one mechanism: Mode of action of Cry1A toxins from Bacillus thuringiensis in Heliothis virescens
Author:
Funder
Max-Planck-Gesellschaft
Publisher
Elsevier BV
Subject
Insect Science,Molecular Biology,Biochemistry
Reference46 articles.
1. Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin;Arenas;J. Biol. Chem.,2010
2. A single amino acid mutation in an ABC transporter causes resistance to Bt toxin Cry1Ab in the silkworm, Bombyx mori;Atsumi;Proc. Natl. Acad. Sci. U. S. A.,2012
3. Parallel evolution of Bacillus thuringiensis toxin resistance in Lepidoptera;Baxter;Genetics,2011
4. Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control;Bravo;Toxicon,2007
5. Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains;Bravo;Biochim. Biophys. Acta (BBA) Biomembr.,2004
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1. Contribution of the transcription factor SfGATAe to Bt Cry toxin resistance in Spodoptera frugiperda through reduction of ABCC2 expression;International Journal of Biological Macromolecules;2024-05
2. New Paralogs of the Heliothis virescens ABCC2 Transporter as Potential Receptors for Bt Cry1A Proteins;Biomolecules;2024-03-26
3. Helicoverpa armigera ATP-binding cassette transporter ABCA2 is a functional receptor of Bacillus thuringiensis Cry2Ab toxin;Pesticide Biochemistry and Physiology;2023-12
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