Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains-Reference-Cited by-同舟云学术

Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains

Published:2004-11 Issue:1 Volume:1667 Page:38-46
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Bravo A.,Gómez I.,Conde J.,Muñoz-Garay C.,Sánchez J.,Miranda R.,Zhuang M.,Gill S.S.,Soberón M.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference48 articles.

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3. Bacillus thuringiensis Cry1A(a) insecticidal toxin: crystal structure and channel formation;Grochulski;J. Mol. Biol.,1995

4. Structure of Cry2Aa suggests an unexpected receptor binding epitope;Morse;Structure,2001

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

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