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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2010, Volume 107, Issue 30, pp. 13473 - 13478
Staphylococcus aureus α-hemolysin (Hla), a potent cytotoxin, plays an important role in the pathogenesis of staphylococcal diseases, including those caused by... 
Receptors | Epithelial cells | Cell lines | Erythrocytes | Small interfering RNA | Cytotoxicity | Toxins | Cell membranes | Focal adhesions | Staphylococcus aureus | Cellular receptor | Pore-forming cytotoxin | CELLS | INFECTIONS | TYROSINE PHOSPHORYLATION | PROTECTION | pore-forming cytotoxin | TOXIN | MULTIDISCIPLINARY SCIENCES | P130(CAS) | MURINE MODEL | ERYTHROCYTES | PORE | BINDING | cellular receptor | Amyloid Precursor Protein Secretases - genetics | Epithelial Cells - metabolism | Hemolysin Proteins - pharmacology | Staphylococcus aureus - physiology | Hemolysin Proteins - genetics | Humans | Focal Adhesions | Molecular Sequence Data | Immunoblotting | RNA Interference | Membrane Proteins - metabolism | Staphylococcus aureus - metabolism | Staphylococcus aureus - genetics | Amino Acid Sequence | Cell Line | Cell Survival - drug effects | Rabbits | Membrane Proteins - genetics | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | ADAM10 Protein | Epithelial Cells - pathology | Host-Pathogen Interactions | Integrin beta1 - metabolism | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Bacterial Proteins - pharmacology | Animals | Epithelial Cells - microbiology | Erythrocytes - metabolism | Cell Line, Tumor | Protein Binding | Bacterial Proteins - metabolism | Mutation | ADAM Proteins - genetics | Integrin beta1 - genetics | Hemolysin Proteins - metabolism | Biological Sciences
Journal Article
Journal Article
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, 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
Insect Biochemistry and Molecular Biology, ISSN 0965-1748, 10/2018, Volume 101, pp. 47 - 56
Cry proteins from (Bt) have been used to control insect pests either as formulated sprays or as in Bt-crops. However, field-evolved resistance to Bt proteins... 
HEK293T cells | Cry receptor | Sf21 cells | Mode of action | Heterologous expression | Bacillus thuringiensis - chemistry | Hemolysin Proteins - pharmacology | Hemolysin Proteins - genetics | Humans | Bacterial Proteins - chemistry | Structure-Activity Relationship | Hemolysin Proteins - chemistry | Sf9 Cells | Protein Isoforms - metabolism | Transfection | Bacillus thuringiensis - genetics | Larva - drug effects | Protein Isoforms - chemistry | Endotoxins - chemistry | Bacillus thuringiensis - metabolism | HEK293 Cells | Protein Domains | Multidrug Resistance-Associated Proteins - genetics | Clone Cells | Larva - genetics | Spodoptera - drug effects | Binding Sites | Insect Proteins - metabolism | Endotoxins - metabolism | Recombinant Proteins - metabolism | Cell Survival - drug effects | Gene Expression | Spodoptera - cytology | Endotoxins - genetics | Larva - metabolism | Bacterial Proteins - genetics | Insect Proteins - genetics | Recombinant Proteins - genetics | Plasmids - metabolism | Larva - cytology | Protein Isoforms - pharmacology | Bacterial Proteins - pharmacology | Animals | Spodoptera - metabolism | Plasmids - chemistry | Protein Binding | Bacterial Proteins - metabolism | Mutation | Multidrug Resistance-Associated Proteins - metabolism | Endotoxins - pharmacology | Hemolysin Proteins - metabolism | Protein Isoforms - genetics | Spodoptera - genetics | Proteins | Insect pests | Analysis | Biological control | Protein binding | Index Medicus
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 of Bacteriology, ISSN 0021-9193, 06/2008, Volume 190, Issue 12, pp. 4147 - 4161
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
HUMAN EPITHELIAL-CELLS | YERSINIA-ENTEROCOLITICA | BACTERIAL ADHESINS | BARTONELLA ADHESIN | NEISSERIA-MENINGITIDIS | HEMOLYSIN PRODUCTION | MICROBIOLOGY | MORAXELLA-CATARRHALIS | EXTRACELLULAR-MATRIX | BIOFILM FORMATION | ANTIGEN-43-MEDIATED AUTOAGGREGATION | Epithelial Cells - metabolism | Humans | Biofilms - growth & development | Molecular Sequence Data | Adhesins, Escherichia coli - chemistry | Adhesins, Escherichia coli - genetics | Bacterial Adhesion - physiology | Escherichia coli - metabolism | Female | Escherichia coli - growth & development | Dimerization | Urinary Tract - microbiology | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Adhesins, Escherichia coli - metabolism | Protein Structure, Secondary | Escherichia coli Infections - microbiology | Escherichia coli Proteins - metabolism | Escherichia coli Infections - metabolism | Blotting, Western | Fibronectins - metabolism | Sequence Homology, Amino Acid | Animals | Escherichia coli - genetics | Epithelial Cells - microbiology | Bacterial Adhesion - genetics | Escherichia coli Proteins - genetics | Mice | HeLa Cells | Laminin - metabolism | Escherichia coli Proteins - chemistry | Microscopy, Fluorescence | Usage | Carrier proteins | Escherichia coli | Physiological aspects | Genetic aspects | Research | Gene expression | Biofilms/growth & development | Adhesins, Escherichia coli/chemistry | Life Sciences | Adhesins, Escherichia coli/genetics | Escherichia coli Proteins/genetics | Escherichia coli/growth & development | Laminin/metabolism | Epithelial Cells/metabolism | Adhesins, Escherichia coli/metabolism | Escherichia coli Infections/metabolism | Escherichia coli/genetics | Escherichia coli/metabolism | Bacteriology | Microbiology and Parasitology | Epithelial Cells/microbiology | Escherichia coli Proteins/chemistry | Escherichia coli Proteins/metabolism | Fibronectins/metabolism | Escherichia coli Infections/microbiology | Urinary Tract/microbiology | Bacterial Adhesion/genetics | Bacterial Adhesion/physiology | Molecular Biology of Pathogens
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
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 11/2015, Volume 112, Issue 46, pp. 14337 - 14342
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2018, Volume 13, Issue 7, pp. e0199317 - e0199317
We assessed the effectiveness of a biofortified maize line (4BtxHC) which accumulates high levels of antioxidant carotenoids that also expressed the... 
RESISTANT | PROTEIN | SESAMIA-NONAGRIOIDES LEPIDOPTERA | GLUTATHIONE | PATHWAY | MULTIDISCIPLINARY SCIENCES | SUSCEPTIBILITY | ANTIOXIDANT ENZYMES | CRY1AB | MAIZE | EXPRESSION | Biological Control Agents - toxicity | Endosperm - metabolism | Superoxide Dismutase - genetics | Reactive Oxygen Species - metabolism | Hemolysin Proteins - genetics | Hemolysin Proteins - antagonists & inhibitors | Lepidoptera - growth & development | Plants, Genetically Modified | Biological Assay | Biological Control Agents - metabolism | Zea mays - metabolism | Transgenes | Biological Control Agents - antagonists & inhibitors | Bacterial Proteins - antagonists & inhibitors | Gene Expression | Plant Leaves - parasitology | Catalase - genetics | Insect Proteins - genetics | Zea mays - parasitology | Carotenoids - biosynthesis | Reactive Oxygen Species - antagonists & inhibitors | Plant Leaves - genetics | Plant Leaves - metabolism | Bacillus thuringiensis - chemistry | Lepidoptera - enzymology | Carotenoids - pharmacology | Bacterial Proteins - toxicity | Glutathione Transferase - genetics | Inactivation, Metabolic - drug effects | Bacillus thuringiensis - genetics | Larva - drug effects | Larva - growth & development | Hemolysin Proteins - toxicity | Larva - enzymology | Lepidoptera - drug effects | Insect Proteins - metabolism | Superoxide Dismutase - metabolism | Endotoxins - metabolism | Recombinant Proteins - metabolism | Zea mays - genetics | Endotoxins - genetics | Bacterial Proteins - genetics | Glutathione Transferase - metabolism | Recombinant Proteins - genetics | Catalase - metabolism | Endotoxins - antagonists & inhibitors | Animals | Recombinant Proteins - toxicity | Bacterial Proteins - metabolism | Endotoxins - toxicity | Hemolysin Proteins - metabolism | Genetic aspects | Carotenoids | Research | European corn borer | Enrichment | Oxidative stress | Larvae | Reactive oxygen species | Bt gene | Cry1Ac toxin | Lipid peroxidation | Superoxide dismutase | Maize | Proteins | Antioxidants | Leaves | Enzymatic activity | Catalase | Glutathione transferase | Plant tissues | Endosperm | Glutathione | Enzymes | Nutrition | Crops | Bioassays | Detoxification | Corn | Gene expression | β-Carotene | Artificial diets | Kernels | Insects | Diet | Toxins | Herbivores | Binding sites | Apoptosis | Index Medicus
Journal Article