The Heliothis virescens 170kDa aminopeptidase functions as “Receptor A” by mediating specific Bacillus thuringiensis Cry1A δ-endotoxin binding and pore formation
- 1 August 1997
- journal article
- Published by Elsevier in Insect Biochemistry and Molecular Biology
- Vol. 27 (8-9) , 735-743
- https://doi.org/10.1016/s0965-1748(97)00052-0
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- A 106 kDa form of aminopeptidase is a receptor for Bacillus thuringiensis CryIC δ-endotoxin in the brush border membrane of Manduca sextaInsect Biochemistry and Molecular Biology, 1996
- Conversion of Bacillus thuringiensis cryIAc-binding aminopeptidase to a soluble form by endogenous phosphatidylinositol phospholipase CInsect Biochemistry and Molecular Biology, 1996
- Brush border membrane aminopeptidase-n in the midgut of the gypsy moth serves as the receptor for the CryIA(c) δ-endotoxin of Bacillus thuringiensisInsect Biochemistry and Molecular Biology, 1995
- Identification, Isolation, and Cloning of a Bacillus thuringiensis CryIAc Toxin-binding Protein from the Midgut of the Lepidopteran Insect Heliothis virescensPublished by Elsevier ,1995
- Molecular Cloning of an Insect Aminopeptidase N That Serves as a Receptor for Bacillus thuringiensis CryIA(c) ToxinPublished by Elsevier ,1995
- Bacillus thuringiensis CryIA(c) δ-endotoxin binding aminopeptidase in the Manduca sexta midgut has a glycosyl-phosphatidylinositol anchorInsect Biochemistry and Molecular Biology, 1995
- Membrane interactions and surface hydrophobicity of Bacillus thuringiensis δ‐endotoxin CryICFEBS Letters, 1994
- The receptor for Bacillus thuringiensis CrylA(c) delta‐endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase NMolecular Microbiology, 1994
- The crystal δ‐endotoxins of Bacillus thuringiensis: Models for their mechanism of action on the insect gutBioEssays, 1993
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970