Protein engineering of Bacillus thuringiensis -endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae-Reference-Cited by-同舟云学术

Protein engineering of Bacillus thuringiensis -endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae

Published:1996-12-10 Issue:25 Volume:93 Page:14338-14343
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Rajamohan F.,Alzate O.,Cotrill J. A.,Curtiss A.,Dean D. H.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference34 articles.

1. Binding of the delta endotoxin from Bacillus thuringiensis to brush-border membrane vesicles of the cabbage butterfly (Pieris brassicae)

2. δ-Endotoxins induce cation channels inSpodoptera frugiperdabrush border membranes in suspension and in planar lipid bilayers

3. Early response of cultured lepidopteran cells to exposure to δ-endotoxin from Bacillus thuringiensis: Involvement of calcium and anionic channels

4. Bacillus thuringiensis delta-endotoxin and larval Manduca sexta midgut brush-border membrane vesicles act synergistically to cause very large increases in the conductance of planar lipid bilayers.

5. V-ATPase-energized epithelia and biological insect control.

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