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  1. Bacillus thuringiensis Cry1AbMod toxin counters tolerance associated with low cadherin expression but not that associated with low alkaline phosphatase expression in Manduca sexta
  2. Identification of Bacillus thuringiensis Cry3Aa toxin domain II loop 1 as the binding site of Tenebrio molitor cadherin repeat CR12
  3. Identification and Characterization of Receptors for Insecticidal Toxins from Bacillus thuringiensis
  4. Bacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity
  5. Differential Role of Manduca sexta Aminopeptidase-N and Alkaline Phosphatase in the Mode of Action of Cry1Aa, Cry1Ab, and Cry1Ac Toxins from Bacillus thuringiensis
  6. Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.
  7. A Tenebrio molitor GPI-anchored alkaline phosphatase is involved in binding of Bacillus thuringiensis Cry3Aa to brush border membrane vesicles
  8. Oligomerization of Cry11Aa from Bacillus thuringiensis Has an Important Role in Toxicity against Aedes aegypti
  9. Domains II and III of Bacillus thuringiensis Cry1Ab toxin remain exposed to the solvent after insertion of part of domain I into the membrane.: FIGURE S1.
  10. 125. Cadherin Binding Is Not a Limiting Step for Bacillus thuringiensis subs. israelensis Cry4Ba Toxicity to Aedes aegypti Larvae
  11. Cadherin binding is not a limiting step for Bacillus thuringiensis subsp. israelensis Cry4Ba toxicity to Aedes aegypti larvae
  12. Evolution ofBacillus thuringiensisCry toxins insecticidal activity
  13. Role of GPI-Anchored Membrane Receptors in the Mode of Action of Bacillus thuringiensis Cry Toxins
  14. Domains II and III of Bacillus thuringiensis Cry1Ab Toxin Remain Exposed to the Solvent after Insertion of Part of Domain I into the Membrane
  15. Role of Alkaline Phosphatase from Manduca sexta in the Mechanism of Action of Bacillus thuringiensis Cry1Ab Toxin
  16. Oligomerization of Cry11Aa from Bacillus thuringiensis Has an Important Role in Toxicity against Aedes aegypti
  17. Domain II Loop 3 of Bacillus thuringiensis Cry1Ab Toxin Is Involved in a "Ping Pong" Binding Mechanism with Manduca sexta Aminopeptidase-N and Cadherin Receptors
  18. Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation
  19. Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins
  20. The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta
  21. Bacillus thuringiensis Cry1Ab Mutants Affecting Oligomer Formation Are Non-toxic to Manduca sexta Larvae
  22. Role of receptor interaction in the mode of action of insecticidal Cry and Cyt toxins produced by Bacillus thuringiensis
  23. Specific Epitopes of Domains II and III ofBacillus thuringiensisCry1Ab Toxin Involved in the Sequential Interaction with Cadherin and Aminopeptidase-N Receptors inManduca sexta
  24. Structural Changes of the Cry1Ac Oligomeric Pre-Pore fromBacillus thuringiensisInduced byN-Acetylgalactosamine Facilitates Toxin Membrane Insertion†
  25. Functional display of Bacillus thuringiensis Cry1Ac toxin on T7 phage
  26. Role of Tryptophan Residues in Toxicity of Cry1Ab Toxin from Bacillus thuringiensis
  27. Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains
  28. Tryptophan Spectroscopy Studies and Black Lipid Bilayer Analysis Indicate that the Oligomeric Structure of Cry1Ab Toxin from Bacillus thuringiensis Is the Membrane-Insertion Intermediate †
  29. Molecular Basis for Bacillus thuringiensis Cry1Ab Toxin Specificity:  Two Structural Determinants in the Manduca sexta Bt-R 1 Receptor Interact with Loops α-8 and 2 in Domain II of Cy1Ab Toxin †
  30. Functional studies of helix alpha-5 region from Bacillus thuringiensis Cry1Ab delta-endotoxin
  31. Hydropathic Complementarity Determines Interaction of Epitope 869HITDTNNK876 in Manduca sexta Bt-R1 Receptor with Loop 2 of Domain II of Bacillus thuringiensis Cry1A Toxins
  32. Pore formation activity of Cry1Ab toxin from Bacillus thuringiensis in an improved membrane vesicle preparation from Manduca sexta midgut cell microvilli
  33. Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation ofBacillus thuringiensisCry1Ab toxin
  34. Evidence for intermolecular interaction as a necessary step for pore-formation activity and toxicity of Bacillus thuringiensis Cry1Ab toxin