Mutations at the arginine residues in alpha8 loop of Bacillus thuringiensis delta-endotoxin Cry1Ac affect toxicity and binding to Manduca sexta and Lymantria dispar aminopeptidase N. [electronic resource]
Producer: 20010705Description: 108-12 p. digitalISSN:- 0014-5793
- Amino Acid Substitution
- Aminopeptidases -- metabolism
- Animals
- Bacillus thuringiensis
- Bacillus thuringiensis Toxins
- Bacterial Proteins -- genetics
- Bacterial Toxins
- Binding, Competitive -- drug effects
- Biological Assay
- Cell Membrane -- chemistry
- Digestive System -- chemistry
- Endotoxins -- genetics
- Hemolysin Proteins
- Insect Proteins -- metabolism
- Larva
- Lepidoptera
- Manduca
- Microvilli -- metabolism
- Models, Molecular
- Mutagenesis, Site-Directed
- Pest Control, Biological
- Protein Binding
- Protein Structure, Tertiary -- physiology
- Structure-Activity Relationship
- Surface Plasmon Resonance
No physical items for this record
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
There are no comments on this title.
Log in to your account to post a comment.