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Diabetes, ISSN 0012-1797, 11/2011, Volume 60, Issue 11, pp. 2872 - 2882
OBJECTIVE-To evaluate whether healthy or diabetic adult mice can tolerate an extreme loss of pancreatic a-cells and how this sudden massive depletion affects... 
INSULIN | HYPERGLUCAGONEMIA | ENDOCRINE PANCREAS | GLUCOSE-HOMEOSTASIS | ENDOCRINOLOGY & METABOLISM | RECEPTOR GENE | SECRETION | DIFFERENTIATION | HYPERPLASIA | ISLET CELLS | EXPRESSION | Insulin-Secreting Cells - secretion | Apoptosis - drug effects | Cell Count | Glucagon - genetics | Male | Diphtheria Toxin - toxicity | Insulin - blood | Glucagon - blood | Diabetes Mellitus, Experimental - blood | Hypoglycemia - prevention & control | Intercellular Signaling Peptides and Proteins - metabolism | Glucagon-Secreting Cells - drug effects | Insulin-Secreting Cells - metabolism | Hyperglycemia - chemically induced | Glucagon-Secreting Cells - metabolism | Diabetes Mellitus, Experimental - chemically induced | Diabetes Mellitus, Experimental - metabolism | Glucagon-Secreting Cells - secretion | Hyperglycemia - prevention & control | Promoter Regions, Genetic | Signal Transduction | Glucagon-Secreting Cells - pathology | Intercellular Signaling Peptides and Proteins - genetics | Pancreas - drug effects | Pancreas - pathology | Receptors, Glucagon - metabolism | Mice, Transgenic | Pancreas - metabolism | Heparin-binding EGF-like Growth Factor | Insulin - metabolism | Animals | Insulin-Secreting Cells - drug effects | Tamoxifen - pharmacology | Diabetes Mellitus, Experimental - pathology | Glucagon - metabolism | Mice | Streptozocin - toxicity | Insulin-Secreting Cells - pathology | Selective Estrogen Receptor Modulators - pharmacology | Islet Studies
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
Journal Article
PLoS Neglected Tropical Diseases, ISSN 1935-2727, 04/2015, Volume 9, Issue 4, p. e0003455
Emerging B. cereus strains that cause anthrax-like disease have been isolated in Cameroon (CA strain) and Cote d'Ivoire (CI strain). These strains are unusual,... 
SEQUENCE CONSERVATION | STRAINS | GRAM-POSITIVE BACTERIA | PLASMID | GENES | GREAT APES | MICE | PROTECTIVE ANTIGEN | PLCR | PARASITOLOGY | TROPICAL MEDICINE | PXO1 | Virulence Factors - genetics | Bacillus anthracis - pathogenicity | Bacillus cereus - classification | Bacterial Capsules - metabolism | Genomics | Bacillus cereus - metabolism | Antigens, Bacterial - genetics | Anthrax - microbiology | Toxins, Biological | Bacterial Toxins - metabolism | Animals | Bacillus cereus - genetics | Virulence - genetics | Plasmids | Bacterial Capsules - genetics | Bacterial Toxins - genetics | Virulence Factors - metabolism | Mice | Bacillus anthracis - genetics | Antigens, Bacterial - metabolism | Bacillus anthracis - metabolism | Genetic aspects | Bacillus cereus | Virulence (Microbiology) | Properties | Genes | Bacillus cereus/metabolism | Antigens, Bacterial/genetics | Biochemistry, Molecular Biology | Bacterial Capsules/metabolism | Bacillus cereus/classification | Virulence Factors/genetics | Virulence/genetics | Life Sciences | Bacillus cereus/genetics | Bacillus anthracis/metabolism | Bacillus anthracis/pathogenicity | Virulence Factors/metabolism | Bacterial Capsules/genetics | Anthrax/microbiology | Bacterial Toxins/genetics | Bacterial Toxins/metabolism | Molecular biology | Toxins | Genomes | Mutation | Nosocomial infections
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2016, Volume 11, Issue 4, p. e0153401
Botulinum neurotoxin A (BoNT/A) is composed of three domains: a catalytic domain (LC), a translocation domain (H-N) and a receptor-binding domain (H-C). Like... 
INHIBITION | CHANNEL | SPECTROSCOPIC ANALYSIS | TOXIN T-DOMAIN | LIGHT-CHAIN PROTEASE | TETANUS | BEHAVIOR | MULTIDISCIPLINARY SCIENCES | IDENTIFICATION | PROTEINS | DIPHTHERIA-TOXIN | Protein Structure, Tertiary | Molecular Chaperones - metabolism | Protein Structure, Secondary | Protein Transport - physiology | Permeability | Catalytic Domain - physiology | Protein Folding | Endocytosis - physiology | Membranes - metabolism | Cytosol - metabolism | Neurotoxins - metabolism | Botulinum Toxins, Type A - metabolism | Lipid Bilayers - metabolism | Hydrogen-Ion Concentration | Protein Binding - physiology | Physiological aspects | Genetic aspects | Research | Structure | Botulinum toxin | Protein binding | Translocation | Membranes | Stability | Denaturation | Cloning | Acidification | Biochemistry | Diphtheria | pH effects | Cytosol | Lipid bilayers | Proteins | Endocytosis | Botulism | Mutagenesis | Hydrogen ions | Plasmids | Botulinum Toxin Type A | Neurotoxin A | Bacteria | Toxins | Intoxication | Catalysis | Botulinum Toxins, Type A/metabolism | Lipid Bilayers/metabolism | Membranes/metabolism | Biochemistry, Molecular Biology | Protein Binding/physiology | Catalytic Domain/physiology | Protein Transport/physiology | Neurotoxins/metabolism | Life Sciences | Molecular Chaperones/metabolism | Cytosol/metabolism | Endocytosis/physiology
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, p. e47977
In recent years a growing debate is about whether botulinum neurotoxins are retrogradely transported from the site of injection. Immunodetection of cleaved... 
ACTIVATION | ACIDIC PROTEIN GFAP | RAT | TOXIN | MULTIDISCIPLINARY SCIENCES | NEURONS | AXONAL-TRANSPORT | NEUROEXOCYTOSIS | GLIAL-CELLS | EXPRESSION | SNAP-25 | Immunohistochemistry | Analgesics - pharmacology | Sciatic Nerve - injuries | Spinal Cord - drug effects | Spinal Cord - metabolism | Neuralgia - metabolism | Analgesics - metabolism | Male | Acetylcholine - metabolism | Glial Fibrillary Acidic Protein - metabolism | Botulinum Toxins, Type A - pharmacology | Hindlimb - physiopathology | Sciatic Nerve - metabolism | Biological Transport | Neuralgia - prevention & control | Neuromuscular Agents - pharmacology | Peripheral Nerves - metabolism | Schwann Cells - drug effects | Neuromuscular Agents - metabolism | Cells, Cultured | Nuclear Proteins - metabolism | Schwann Cells - metabolism | Nerve Tissue Proteins - metabolism | Microscopy, Confocal | Animals | Hindlimb - drug effects | Cell Proliferation - drug effects | Mice | Synaptosomal-Associated Protein 25 - metabolism | Botulinum Toxins, Type A - metabolism | CD11b Antigen - metabolism | Hindlimb - metabolism | Astrocytes - metabolism | Ganglia, Spinal - metabolism | Care and treatment | Analysis | Pain | Cell proliferation | Spinal cord | Neurosciences | Complement receptor 3 | Neurobiology | SNAP receptors | Biology | Neuropathy | Proteins | Biological effects | Dorsal root ganglia | Analgesics | Botulinum Toxin Type A | Animal tissues | Fibroblasts | Neurotoxin A | Horns | Growth factors | Nerve endings | CD11b antigen | Neurotoxins | Pain perception | Astrocytes | Glial fibrillary acidic protein | Schwann cells | Injection | Retrograde transport | Ganglia | Quality of life | Councils | SNAP-25 protein | Acetylcholine | Toxins | Transport | Immunofluorescence | Sciatic nerve | Combinatorial analysis | Botulinum toxin
Journal Article
Nature, ISSN 0028-0836, 2012, Volume 490, Issue 7418, pp. 107 - 111
Detection of microbial products by host inflammasomes is an important mechanism of innate immune surveillance. Inflammasomes activate the caspase-1 (CASP1)... 
CYTOSOLIC PHOSPHOLIPASE A | FLAGELLIN | III SECRETION APPARATUS | MECHANISM | MICE DEFICIENT | MULTIDISCIPLINARY SCIENCES | NLRC4 INFLAMMASOME | INFECTION | PYROPTOSIS | CASPASE-1 ACTIVATION | IMMUNE RECOGNITION | Inflammation - pathology | Inflammasomes - metabolism | Hematocrit | Salmonella Infections - immunology | Eicosanoids - biosynthesis | Caspase 1 - metabolism | Male | Inflammation - metabolism | Time Factors | Flagellin - metabolism | Bacterial Toxins - genetics | Antigens, Bacterial - chemistry | Neuronal Apoptosis-Inhibitory Protein - deficiency | Macrophages, Peritoneal - immunology | Calcium-Binding Proteins - deficiency | Interleukin-1beta | Bacterial Toxins - chemistry | Apoptosis Regulatory Proteins - metabolism | Cyclooxygenase 1 - deficiency | Body Fluids - metabolism | Caspase 1 - deficiency | Recombinant Fusion Proteins - genetics | Cytosol - metabolism | Death | Mice | Antigens, Bacterial - metabolism | Capillary Permeability | Peritoneal Cavity | Legionella pneumophila | Intestines - metabolism | Antigens, Bacterial - genetics | Recombinant Fusion Proteins - metabolism | Peritoneal Lavage | Apoptosis Regulatory Proteins - deficiency | Flagellin - genetics | Female | Interleukin-18 | Calcium Signaling | Calcium-Binding Proteins - metabolism | Flagellin - immunology | Salmonella typhimurium - immunology | Mice, Inbred C57BL | Inflammation - immunology | Body Temperature | Neuronal Apoptosis-Inhibitory Protein - metabolism | Immunity, Innate - immunology | Bacterial Toxins - metabolism | Animals | Eicosanoids - metabolism | Fluid Shifts | Cellular signal transduction | Research | Properties | Bacterial proteins | Flagella (Microbiology) | Immune system | Proteins | Bone marrow | Pathology | Infections | Biosynthesis | Rodents
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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2011, Volume 108, Issue 36, pp. 14944 - 14949
The bacterial pathogen Helicobacter pylori chronically infects the human gastric mucosa and is the leading risk factor for the development of gastric cancer.... 
Helicobacter pylori | Epithelial cells | DNA damage | DNA | Cell nucleus | Cell lines | Bacteria | Cultured cells | Infections | Mice | Chromosome breaks | DNA damage signaling | Gastric tumorigenesis | Genomic instability | CYTOLETHAL DISTENDING TOXIN | MULTIDISCIPLINARY SCIENCES | RISK | MISMATCH REPAIR | COLONIZATION | GENETIC INSTABILITY | EPITHELIAL-CELLS | chromosome breaks | GASTRIC-CANCER | INFLAMMATION | INFECTION | MICE | genomic instability | gastric tumorigenesis | Phosphorylation | Epithelial Cells - metabolism | Humans | Stomach Neoplasms - metabolism | Helicobacter Infections - complications | Stomach Neoplasms - pathology | Intracellular Signaling Peptides and Proteins - metabolism | Antigens, Bacterial - genetics | DNA Breaks, Double-Stranded | Helicobacter Infections - pathology | DNA-Binding Proteins - metabolism | Tumor Suppressor Proteins - genetics | Trans-Activators - genetics | Cell Cycle Proteins - genetics | Helicobacter Infections - metabolism | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Stomach Neoplasms - genetics | Tumor Suppressor Proteins - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Genomic Islands | Epithelial Cells - pathology | Nuclear Proteins - metabolism | Ataxia Telangiectasia Mutated Proteins | DNA-Binding Proteins - genetics | Chromosomal Proteins, Non-Histone - genetics | Bacterial Adhesion | Stomach Neoplasms - microbiology | Animals | Histones - genetics | Helicobacter pylori - metabolism | Epithelial Cells - microbiology | Chromosome Aberrations | Cell Line, Tumor | Bacterial Proteins - metabolism | Trans-Activators - metabolism | Histones - metabolism | Tumor Suppressor p53-Binding Protein 1 | Antigens, Bacterial - metabolism | Carcinogens | Cocarcinogens | Physiological aspects | Genetic aspects | Research | Health aspects | Cells | Biological Sciences
Journal Article
Nature, ISSN 0028-0836, 08/2012, Volume 488, Issue 7413, pp. 670 - 674
The inflammasome regulates the release of caspase activation-dependent cytokines, including interleukin (IL)-1 beta, IL-18 and high-mobility group box 1... 
PATHWAYS | APOPTOSIS | ACID | PROTEIN-KINASE PKR | MULTIDISCIPLINARY SCIENCES | INFECTION | NLRP3 INFLAMMASOME | ELF2-ALPHA | STRESS | BINDING | SUBSTRATE RECOGNITION | Crystallins - metabolism | Interleukin-6 - analysis | Phosphorylation | Inflammasomes - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein | eIF-2 Kinase - metabolism | Humans | Salmonella Infections - immunology | Male | Salmonella Infections - metabolism | HMGB1 Protein - secretion | Interleukin-1beta - blood | eIF-2 Kinase - deficiency | Adenosine Triphosphate - pharmacology | CARD Signaling Adaptor Proteins - metabolism | Transfection | Interleukin-6 - blood | Rotenone - pharmacology | Female | Membrane Proteins - metabolism | Escherichia coli - physiology | Macrophages, Peritoneal - drug effects | eIF-2 Kinase - genetics | Calcium-Binding Proteins - metabolism | Cell Line | Salmonella typhimurium - physiology | Interleukin-18 - blood | Salmonella typhimurium - immunology | Inflammasomes - agonists | Mice, Inbred C57BL | Peritonitis - metabolism | Cells, Cultured | Escherichia coli - immunology | Antigens, Bacterial - pharmacology | Escherichia coli Infections - metabolism | eIF-2 Kinase - antagonists & inhibitors | Apoptosis Regulatory Proteins - metabolism | Animals | Carrier Proteins - metabolism | Bacterial Toxins - pharmacology | Uric Acid - pharmacology | RNA, Double-Stranded - immunology | RNA, Double-Stranded - pharmacology | Escherichia coli Infections - immunology | Mice | Adaptor Proteins, Signal Transducing - metabolism | Macrophages, Peritoneal - metabolism | HMGB1 Protein - blood | Physiological aspects | Chromosomal proteins | Research | Cytokines | Aluminum | Health aspects | Proteins | E coli | Pathogenesis | Plasmids | Bone marrow | Bacteria | Kinases
Journal Article