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Volumn 497, Issue 2-3, 2001, Pages 108-112
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Mutations at the arginine residues in α8 loop of Bacillus thuringiensis δ-endotoxin Cry1Ac affect toxicity and binding to Manduca sexta and Lymantria dispar aminopeptidase
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Author keywords
Aminopeptidase N; Bacillus thuringiensis; Brush border membrane vesicle; Lymantria dispar; Manduca sexta; Surface plasmon resonance
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Indexed keywords
ALANINE;
AMINOPEPTIDASE;
ARGININE;
BACILLUS THURINGIENSIS TOXIN;
CRY1AC;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
ARTICLE;
BACILLUS THURINGIENSIS;
BINDING AFFINITY;
BRUSH BORDER VESICLE;
GENE STRUCTURE;
GYPSY MOTH;
INSECT;
LC 50;
MANDUCA SEXTA;
MUTATION;
NONHUMAN;
PRIORITY JOURNAL;
RECEPTOR BINDING;
STRAIN DIFFERENCE;
TOXICITY;
AMINO ACID SUBSTITUTION;
AMINOPEPTIDASES;
ANIMALS;
BACILLUS THURINGIENSIS;
BACTERIAL PROTEINS;
BACTERIAL TOXINS;
BINDING, COMPETITIVE;
BIOLOGICAL ASSAY;
CELL MEMBRANE;
DIGESTIVE SYSTEM;
ENDOTOXINS;
HEMOLYSIN PROTEINS;
INSECT PROTEINS;
LARVA;
LEPIDOPTERA;
MANDUCA;
MICROVILLI;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
PEST CONTROL, BIOLOGICAL;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
STRUCTURE-ACTIVITY RELATIONSHIP;
SURFACE PLASMON RESONANCE;
BACILLUS THURINGIENSIS;
HEXAPODA;
LYMANTRIA DISPAR;
MANDUCA SEXTA;
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EID: 0035947103
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(01)02446-2 Document Type: Article |
Times cited : (20)
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References (30)
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