Bt-R1a Extracellular Cadherin Repeat 12 Mediates Bacillus thuringiensis Cry1Ab Binding and Cytotoxicity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Hydropathic Complementarity Determines Interaction of Epitope 869HITDTNNK876 in Manduca sexta Bt-R1 Receptor with Loop 2 of Domain II ofBacillus thuringiensis Cry1A Toxins
2. Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R1 in Manduca sexta:
3. Safety and Advantages of Bacillus thuringiensis-Protected Plants to Control Insect Pests
4. Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation ofBacillus thuringiensisCry1Ab toxin
5. The receptor for Bacillus thuringiensis CrylA(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N
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