Amino acid and divalent ion permeability of the pores formed by the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac in insect midgut brush border membrane vesicles-Reference-Cited by-同舟云学术

Amino acid and divalent ion permeability of the pores formed by the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac in insect midgut brush border membrane vesicles

Published:2002-04 Issue:2 Volume:1561 Page:171-179
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Kirouac Martin,Vachon Vincent,Noël Jean-François,Girard Frédéric,Schwartz Jean-Louis,Laprade Raynald

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference49 articles.

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3. The receptor for Bacillus thuringiensis CryIA(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N;Knight;Mol. Microbiol.,1994

4. A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal CryIA(c) toxin binding and 86Rb+–K+ efflux in vitro;Sangadala;J. Biol. Chem.,1994

5. Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin;Knight;J. Biol. Chem.,1995

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