Two specific membrane-bound aminopeptidase N isoforms from Aedes aegypti larvae serve as functional receptors for the Bacillus thuringiensis Cry4Ba toxin implicating counterpart specificity

Author:

Aroonkesorn Aratee,Pootanakit Kusol,Katzenmeier Gerd,Angsuthanasombat Chanan

Funder

Thailand Research Fund

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference32 articles.

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2. Structural basis of pore formation by mosquito-larvicidal proteins from Bacillus thuringiensis;Angsuthanasombat;Open Toxinol J.,2010

3. Bacillus thuringiensis subsp. israelensis and its dipteran-specific toxins;Ben-Dov;Toxins,2014

4. The Bacillus thuringiensis Cry1Ac toxin-induced permeability change in Manduca sexta midgut brush border membrane vesicles proceeds by more than one mechanism;Carroll;J. Cell. Sci.,1997

5. Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications;Boonserm;J. Mol. Biol.,2005

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