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Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 2386 - 9
Cry1A insecticidal toxins bind sequentially to different larval gut proteins facilitating oligomerization, membrane insertion and pore formation. Cry1Ac... 
MANDUCA-SEXTA | TRICHOPLUSIA-NI | ALKALINE-PHOSPHATASE | CABBAGE-LOOPER | MULTIDISCIPLINARY SCIENCES | PRE-PORE | INSECT RESISTANCE | HELICOVERPA-ARMIGERA LARVAE | PORE FORMATION | FIELD-EVOLVED RESISTANCE | MODIFIED BT TOXINS | Insecticides - chemistry | Hemolysin Proteins - pharmacology | Microvilli - chemistry | Hemolysin Proteins - genetics | Protein Multimerization | Bacterial Proteins - chemistry | Cell-Derived Microparticles - chemistry | Hemolysin Proteins - chemistry | Cell Membrane - chemistry | Larva - drug effects | Endotoxins - chemistry | Biological Control Agents - chemistry | Protein Engineering | Multidrug Resistance-Associated Proteins - genetics | Cell Membrane - metabolism | Cell-Derived Microparticles - metabolism | Larva - chemistry | Biological Control Agents - metabolism | Insect Proteins - metabolism | Cell Membrane - drug effects | Endotoxins - metabolism | Endotoxins - genetics | Insecticide Resistance | Larva - metabolism | Bacterial Proteins - genetics | Multidrug Resistance-Associated Proteins - chemistry | Insect Proteins - genetics | Microvilli - drug effects | Bacterial Proteins - pharmacology | Manduca - drug effects | Animals | Insecticides - metabolism | Microvilli - metabolism | Insect Proteins - chemistry | Protein Isoforms | Protein Binding | Bacterial Proteins - metabolism | Mutation | Multidrug Resistance-Associated Proteins - metabolism | Endotoxins - pharmacology | Hemolysin Proteins - metabolism | Moths - drug effects | Oligomerization | Cry1Ac toxin | Membrane vesicles | Toxins | Cadherin | ABC transporter | Western blotting
Journal Article
PLoS Biology, ISSN 1544-9173, 2015, Volume 13, Issue 2, p. e1002049
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
Nature Nanotechnology, ISSN 1748-3387, 2013, Volume 8, Issue 4, pp. 288 - 295
Journal Article
Nature Communications, ISSN 2041-1723, 2015, Volume 6, Issue 1, p. 6198
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2009, Volume 284, Issue 21, pp. 14645 - 14656
Anthrolysin O (ALO) is a pore-forming, cholesterol-dependent cytolysin (CDC) secreted by Bacillus anthracis , the etiologic agent for anthrax. Growing evidence... 
LISTERIA-MONOCYTOGENES | TIGHT JUNCTIONS | CELLS | CONFORMATIONAL-CHANGES | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VITRO MODEL | MEMBRANE INSERTION | THETA-TOXIN | PORE-FORMING TOXINS | PERFRINGOLYSIN-O | BIOLOGICAL WEAPON | Solubility - drug effects | Epithelial Cells - metabolism | Membrane Glycoproteins - metabolism | Calcium - metabolism | Bacteriocins - chemistry | Epithelial Cells - drug effects | Humans | Membrane Glycoproteins - chemistry | Protein Multimerization | Bacterial Proteins - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Hemolysin Proteins - chemistry | Occludin | Protein Binding - drug effects | Protein Structure, Quaternary | Membrane Proteins - metabolism | Bacteriocins - metabolism | Epithelial Cells - cytology | Bacillus anthracis - metabolism | Tight Junctions - drug effects | Caco-2 Cells | Protein Structure, Tertiary | Tight Junctions - metabolism | Amino Acid Sequence | Permeability - drug effects | Intracellular Space - drug effects | Protein Structure, Secondary | Perforin - chemistry | Models, Molecular | Bacillus anthracis - cytology | Cholesterol - metabolism | Bacterial Toxins - chemistry | Bacterial Toxins - metabolism | Intracellular Space - metabolism | Ionomycin - pharmacology | Bacterial Proteins - metabolism | Perforin - metabolism | Hemolysin Proteins - metabolism | Intestines - cytology | Life Sciences | Biochemistry, Molecular Biology | HUMAN POPULATIONS | PATHOGENESIS | ELEMENTS | CALCIUM | LIGHT SCATTERING | CRYSTAL STRUCTURE | DIMERIZATION | MATERIALS SCIENCE | BACILLUS | FUNCTIONS | PROTEINS | ULTRACENTRIFUGATION
Journal Article
CELL, ISSN 0092-8674, 10/2003, Volume 115, Issue 1, pp. 25 - 35
The ClyA protein is a pore-forming cytotoxin expressed by Escherichia coli and some other enterobacteria. It confers cytotoxic activity toward mammalian cells,... 
OUTER-MEMBRANE VESICLES | HOST-CELLS | IN-VITRO | HEAT-LABILE ENTEROTOXIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI K-12 | GENERAL SECRETORY PATHWAY | SHEA | PROTEIN SECRETION | HEMOLYSIN-E | CELL BIOLOGY | Oxidation-Reduction | Protein Disulfide-Isomerases - metabolism | Humans | Bacterial Proteins - chemistry | Hemolysin Proteins - chemistry | Bacterial Toxins - chemistry | Cell Membrane - chemistry | Bacterial Toxins - metabolism | Animals | Transport Vesicles - metabolism | Cytotoxins - chemistry | Escherichia coli - metabolism | Cytotoxins - metabolism | Bacterial Proteins - metabolism | Polymers - chemistry | Cell Membrane - metabolism | Membrane Proteins - metabolism | HeLa Cells | Escherichia coli - ultrastructure | Hemolysin Proteins - metabolism | Polymers - metabolism | Salmonella - metabolism | Transport Vesicles - ultrastructure | Bacterial toxins | Physiological aspects | Gram-negative bacteria | Secretion | Biological transport | Bacterial Toxins/chemistry/metabolism | Cytotoxins/chemistry/metabolism | Salmonella/metabolism | Cell Membrane/chemistry/metabolism | Escherichia coli/metabolism/ultrastructure | Bacterial Proteins/chemistry/metabolism | Transport Vesicles/metabolism/ultrastructure | Membrane Proteins/metabolism | Hemolysin Proteins/chemistry/metabolism | Polymers/chemistry/metabolism | Hela Cells | Protein Disulfide-Isomerase/metabolism
Journal Article
Chemical Communications, ISSN 1359-7345, 11/2010, Volume 46, Issue 43, pp. 8195 - 8197
Journal Article