All Domains of Cry1A Toxins Insert into Insect Brush Border Membranes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference40 articles.
1. Bacillus thuringiensis and Its Pesticidal Crystal Proteins
2. Bacillus thuringiensisCrylA(a) Insecticidal Toxin: Crystal Structure and Channel Formation
3. Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
4. Structure of Cry2Aa Suggests an Unexpected Receptor Binding Epitope
5. Structure of the insecticidal bacterial δ-endotoxin Cry3Bb1 ofBacillus thuringiensis
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1. Channel Formation in Cry Toxins: An Alphafold-2 Perspective;International Journal of Molecular Sciences;2023-11-27
2. ATP Synthase Subunit α from Helicoverpa armigera Acts as a Receptor of Bacillus thuringiensis Cry1Ac and Synergizes Cry1Ac Toxicity;Journal of Agricultural and Food Chemistry;2023-04-10
3. In vivo and in silico comparison analyses of Cry toxin activities toward the sugarcane giant borer;Bulletin of Entomological Research;2023-03-08
4. A major conformational change of N‐terminal helices of Bacillus thuringiensis Cry1Ab insecticidal protein is necessary for membrane insertion and toxicity;The FEBS Journal;2023-01-09
5. The C-Terminal Domain of the Bacillus thuringiensis Cry4Ba Mosquito-Specific Toxin Serves as a Potential Membrane Anchor;Toxins;2019-01-23
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