Role of Alkaline Phosphatase fromManduca sextain the Mechanism of Action ofBacillus thuringiensisCry1Ab Toxin

Domain II Loop 3 ofBacillus thuringiensisCry1Ab Toxin Is Involved in a “Ping Pong” Binding Mechanism with Manduca sexta Aminopeptidase-N and Cadherin Receptors

(2009) Sabino Pacheco et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela

(2009) Shuyuan Guo et al.   JOURNAL OF STRUCTURAL BIOLOGY

Dominant Negative Mutants of Bacillus thuringiensis Cry1Ab Toxin Function as Anti-Toxins: Demonstration of the Role of Oligomerization in Toxicity

(2009) Claudia Rodríguez-Almazán et al.   PLoS One

Membrane Insertion of theBacillus thuringiensisCry1Ab Toxin: Single Mutation in Domain II Block Partitioning of the Toxin into the Brush Border Membrane†

(2008) Manoj S. Nair et al.   BIOCHEMISTRY

Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity

(2008) Taek H You et al.   BMC BIOCHEMISTRY

Susceptibility of Manduca sexta to Cry1Ab toxin of Bacillus thuringiensis correlates directly to developmental expression of the cadherin receptor BT-R1

(2008) Natalya Griko et al.   COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY

Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation

(2008) Sabino Pacheco et al.   PEPTIDES