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Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 34, pp. 20793 - 20803
The insecticidal feature of the three-domain Cry delta-endotoxins from Bacillus thuringiensis is generally attributed to their capability to form oligomeric... 
PORE-FORMING DOMAIN | ATOMIC-FORCE MICROSCOPY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | CRY4BA DELTA-ENDOTOXIN | TOXICITY | AEDES-AEGYPTI LARVAE | PROTEINS | OLIGOMERIZATION | BINDING | Pest Control, Biological | Insecticides - chemistry | Bacillus thuringiensis - chemistry | Hemolysin Proteins - genetics | Protein Multimerization | Bacterial Proteins - chemistry | Bacterial Toxins - toxicity | Hemolysin Proteins - chemistry | Sulfonic Acids - chemistry | Bacterial Proteins - toxicity | Endotoxins - chemistry | Micelles | Bacillus thuringiensis - metabolism | Escherichia coli - metabolism | Glucosides - chemistry | Hemolysin Proteins - toxicity | Bacterial Toxins - genetics | Spodoptera - drug effects | Insect Proteins - metabolism | Gene Expression | Spodoptera - cytology | Endotoxins - genetics | Bacterial Proteins - genetics | Insect Proteins - genetics | Receptors, Cell Surface - metabolism | Recombinant Proteins - chemistry | Sf9 Cells - cytology | Aedes - drug effects | Recombinant Proteins - genetics | Bacterial Toxins - chemistry | Molecular Dynamics Simulation | Sf9 Cells - drug effects | Liposomes - chemistry | Animals | Insecticides - metabolism | Escherichia coli - genetics | Recombinant Proteins - toxicity | Protein Conformation | Aedes - cytology | Insecticides - toxicity | Dimyristoylphosphatidylcholine - chemistry | Endotoxins - toxicity | Receptors, Cell Surface - genetics | Index Medicus | three-dimensional reconstructed prepore | Protein Structure and Folding | high-speed atomic force microscopy | conformational transition | micelle-induced trimerization | gel electrophoresis | propeller-like shape | bacillus | protein assembly | bacterial toxin
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 04/2010, Volume 285, Issue 17, pp. 12497 - 12503
Cry toxins produced by Bacillus thuringiensis have been recognized as pore-forming toxins whose primary action is to lyse midgut epithelial cells in their... 
LYMANTRIA-DISPAR | LARVAL MIDGUT | AMINOPEPTIDASE-N-RECEPTOR | CYT TOXINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DOMAIN-II | DELTA-ENDOTOXIN | HELIOTHIS-VIRESCENS | BRUSH-BORDER MEMBRANE | BINDING-PROTEINS | OLIGOMERIC PRE-PORE | Insecticides - chemistry | Bacillus thuringiensis - chemistry | Cadherins - metabolism | Hemolysin Proteins - genetics | Protein Multimerization | Alkaline Phosphatase - metabolism | Bacterial Proteins - chemistry | Manduca - genetics | Mutation, Missense | Hemolysin Proteins - chemistry | Bacillus thuringiensis - genetics | Endotoxins - chemistry | Alkaline Phosphatase - chemistry | Aminopeptidases - chemistry | Cadherins - chemistry | Larva - enzymology | Cadherins - genetics | Aminopeptidases - metabolism | Bacillus thuringiensis - physiology | Insect Proteins - metabolism | Endotoxins - metabolism | Protein Structure, Tertiary | Aminopeptidases - genetics | Alkaline Phosphatase - genetics | Endotoxins - genetics | Larva - metabolism | Bacterial Proteins - genetics | Insect Proteins - genetics | Animals | Insecticides - metabolism | Insect Proteins - chemistry | Protein Binding | Bacterial Proteins - metabolism | Hemolysin Proteins - metabolism | Manduca - enzymology | Index Medicus | Membrane Proteins | Protein Structure and Folding | Receptor Structure-Function | Bacterial Toxins | Receptor | Bacillus thuringiensis | Cry1Ab Toxin | Alkaline Phosphatase | Phosphatase | Aminopeptidase | Insect
Journal Article
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2014, Volume 9, Issue 11, pp. e112555 - e112555
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2011, Volume 108, Issue 34, pp. 14037 - 14042
The soil bacterium Bacillus thuringiensis (Bt) is the most successfully used biopesticide in agriculture, and its insecticidal protein genes are the primary... 
Larvae | Midgut | Bacillus thuringiensis | Genes | Proteomics | Cadherins | Toxins | Transgenic insects | Insect genetics | Microvilli | HELICOVERPA-ARMIGERA | HELIOTHIS-VIRESCENS LARVAE | GENE | PLUTELLA-XYLOSTELLA | FIELD | MULTIDISCIPLINARY SCIENCES | INSECT RESISTANCE | DELTA-ENDOTOXIN | LEPIDOPTERA | BINDING | BT CROPS | Gene Expression Regulation, Enzymologic - drug effects | Transcription, Genetic - drug effects | Bacillus thuringiensis - chemistry | Molecular Weight | Genes, Insect - genetics | Insecticide Resistance - genetics | Molecular Sequence Data | Gene Expression Profiling | RNA, Messenger - metabolism | Moths - genetics | Bacterial Proteins - toxicity | Digestive System - drug effects | Larva - drug effects | Protein Binding - drug effects | Hemolysin Proteins - toxicity | Insecticide Resistance - drug effects | Larva - genetics | Insect Proteins - metabolism | Genetic Linkage | Digestive System - metabolism | Electrophoresis, Polyacrylamide Gel | RNA, Messenger - genetics | Insect Proteins - genetics | CD13 Antigens - metabolism | Microvilli - drug effects | Animals | CD13 Antigens - genetics | Microvilli - metabolism | Brassica - parasitology | Moths - enzymology | Endotoxins - toxicity | Moths - drug effects | Evolutionary biology | Aminopeptidases | Physiological aspects | Genetic aspects | Research | Moths | Enzymes | Bacteria | Vegetables | Invertebrates | Index Medicus | Biological Sciences
Journal Article