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1. Full Text Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin
by Wai, SN and Lindmark, B and Soderblom, T and Takade, A and Westermark, M and Oscarsson, J and Jass, J and Richter-Dahlfors, A and Mizunoe, Y and Uhlin, BE and Medicinska fakulteten and Institutionen för molekylärbiologi (Medicinska fakulteten) and Umeå universitet
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
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2. Full Text Endosome-mitochondria juxtaposition during apoptosis induced by H. pylori VacA
by Calore, F and Genisset, C and Casellato, A and Rossato, M and Codolo, G and Esposti, M.D and Scorrano, L and De Bernard, M
Cell Death and Differentiation, ISSN 1350-9047, 11/2010, Volume 17, Issue 11, pp. 1707 - 1716
The vacuolating cytotoxin (VacA) is an important virulence factor of Helicobacter pylori with pleiotropic effects on mammalian cells, including the ability to... 
VacA | apoptosis | BAX | Helicobacter pylori | mitochondria | CELLS | VACUOLATING CYTOTOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANE CHANNEL FORMATION | GASTRIC EPITHELIAL APOPTOSIS | ANION-SELECTIVE CHANNELS | TOXIN VACA | CELL BIOLOGY | CELLULAR VACUOLATION | CYTOCHROME-C RELEASE | HELICOBACTER-PYLORI | Apoptosis - drug effects | Calcium - metabolism | Cytochromes c - metabolism | Bacterial Proteins - genetics | Cells, Cultured | Helicobacter pylori - pathogenicity | bcl-2-Associated X Protein - metabolism | Endoplasmic Reticulum - metabolism | Mitochondria - metabolism | Genes, bcl-2 | Microscopy, Electron | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Endosomes - metabolism | Apoptosis Regulatory Proteins - metabolism | Animals | Helicobacter pylori - metabolism | Fluorescent Antibody Technique | Bacterial Proteins - metabolism | Virulence Factors - metabolism | Mice | Apoptosis - physiology
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3. Full Text Proteomics of muscle chronological ageing in post-menopausal women
by Gueugneau, M and Coudy, C and Gourbeyre, O and Chambon, C and Combaret, L and Polge, C and Tailandier, D and Attaix, D and Friguet, B and Maier, A.B and Butler-Browne, G and Bechet, D
BMC Genomics, ISSN 1471-2164, 2014, Volume 15, Issue 1, pp. 1165 - 1165
Background: Muscle ageing contributes to both loss of functional autonomy and increased morbidity. Muscle atrophy accelerates after 50 years of age, but the... 
Human | Biomarkers | Sarcopenia | Ageing | Skeletal muscle | Proteomics | VASTUS-LATERALIS MUSCLE | MITOCHONDRIAL-FUNCTION | SARCOPLASMIC-RETICULUM | DIGE ANALYSIS | HUMAN SKELETAL-MUSCLE | HEAT-SHOCK PROTEINS | HANDGRIP STRENGTH | RYANODINE RECEPTOR | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENDOTHELIAL-CELLS | GENETICS & HEREDITY | AAA-ATPASE | Oxidative Stress | Humans | Middle Aged | Transcriptome | Cytoplasm - metabolism | Muscle, Skeletal - metabolism | Blood Proteins - metabolism | Muscle, Skeletal - cytology | Postmenopause - metabolism | Proteolysis | Cytotoxins - metabolism | Cytoskeletal Proteins - metabolism | Female | Muscles - metabolism | Postmenopause - physiology | Sarcopenia - metabolism | Biomarkers - metabolism | Signal Transduction | Sarcomeres - metabolism | Muscles - physiology | Lipid Metabolism | Mitochondria - metabolism | Muscle, Skeletal - physiology | Energy Metabolism | Aged | Aging - metabolism | Muscles - cytology | Aging | Postmenopausal women | Genetic aspects | Muscle proteins | Properties | Muscles | Physiological aspects | Comparative analysis | Annexins | Life Sciences | Cellular Biology
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4. Contributions of the interaction between dietary protein and gut microbiota to intestinal health
by Ma, Ning and Tian, Yanan and Wu, Yi and Ma, Xi
Current Protein and Peptide Science, ISSN 1389-2037, 08/2017, Volume 18, Issue 8, pp. 795 - 808
There is growing recognition that composition and metabolic activity of the gut microbiota can be modulated by the dietary proteins which in turn impact... 
Dietary protein | Metabolites | Amino acid balance | Intestinal microbiota | Gut barrier | Digestibility | LIPID-METABOLISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BARRIER FUNCTION | HYDROGEN-SULFIDE | CELL-GROWTH | WEANED PIGS | BUTYRATE-PRODUCING BACTERIA | metabolites | GROWTH-PERFORMANCE | POSTWEANING DIARRHEA | intestinal microbiota | amino acid balance | SOYBEAN-MEAL | CHAIN FATTY-ACIDS | gut barrier | digestibility | Dietary Proteins - administration & dosage | Proteobacteria - metabolism | Humans | Gastrointestinal Microbiome - physiology | Dietary Carbohydrates - metabolism | Fusobacteria - metabolism | Dietary Proteins - metabolism | Proteolysis | Actinobacteria - metabolism | Firmicutes - metabolism | Verrucomicrobia - growth & development | Dietary Carbohydrates - administration & dosage | Firmicutes - growth & development | Fatty Acids, Volatile - biosynthesis | Ammonia - metabolism | Gastrointestinal Tract - microbiology | Gastrointestinal Tract - drug effects | Fermentation | Amines - metabolism | Fusobacteria - growth & development | Verrucomicrobia - metabolism | Gastrointestinal Microbiome - drug effects | Bacteroidetes - metabolism | Actinobacteria - growth & development | Bacteroidetes - growth & development | Proteobacteria - growth & development | Sulfide | Inflammatory bowel diseases | Amines | Protein turnover | Proteins | Low carbohydrate diet | Carcinogens | Microorganisms | Microbiota | Colon cancer | Intestine | Colon | Digestive tract | Low protein diet | Immune system | Carbohydrates | Protein metabolism | Nutrient deficiency | Secretion | Digestive system | Health | Health risks | Dietary supplements | Amino acid composition | Gastrointestinal tract | Gene expression | Metabolism | Fatty acids | Gases | Cytotoxins | Ammonia | Signaling | Diet | Cancer
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5. Full Text Modification of sphingolipid metabolism by tamoxifen and N-desmethyltamoxifen in acute myelogenous leukemia—Impact on enzyme activity and response to cytotoxics
by Morad, Samy A.F and Tan, Su-Fern and Feith, David J and Kester, Mark and Claxton, David F and Loughran, Thomas P and Barth, Brian M and Fox, Todd E and Cabot, Myles C
BBA - Molecular and Cell Biology of Lipids, ISSN 1388-1981, 07/2015, Volume 1851, Issue 7, pp. 919 - 928
The triphenylethylene antiestrogen, tamoxifen, can be an effective inhibitor of sphingolipid metabolism. This off-target activity makes tamoxifen an... 
Ceramide | Triphenylethylenes | Tamoxifen | Sphingolipid metabolism | Leukemia | TUMOR-CELL LINES | GLUCOSYLCERAMIDE SYNTHASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOSPHINGOLIPID METABOLISM | DRUG-RESISTANCE | CANCER | P-GLYCOPROTEIN | CELL BIOLOGY | ACID CERAMIDASE | INHIBITION | BIOPHYSICS | SHORT-CHAIN CERAMIDE | MULTIDRUG-RESISTANCE | Leukemia, Myeloid, Acute - pathology | Humans | Leukemia, Myeloid, Acute - metabolism | Estrogen Antagonists - pharmacology | Sphingolipids - metabolism | Stilbenes - pharmacology | Enzyme Activation - drug effects | Phosphotransferases (Alcohol Group Acceptor) - metabolism | Cytotoxins - pharmacology | Phosphotransferases (Alcohol Group Acceptor) - drug effects | Lipid Metabolism - drug effects | Tamoxifen - pharmacology | HL-60 Cells | Tamoxifen - analogs & derivatives | Tumor Cells, Cultured | Physiological aspects | Enzymes | Lipids | Sphingosine
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6. Full Text The Neuroprotective Role of Insulin Against MPP+‐Induced Parkinson's Disease in Differentiated SH‐SY5Y Cells
by Ramalingam, Mahesh and Kim, Sung‐Jin
Journal of Cellular Biochemistry, ISSN 0730-2312, 04/2016, Volume 117, Issue 4, pp. 917 - 926
ABSTRACT Parkinson's disease (PD) is a common chronic neurodegenerative disorder associated with aging that primarily caused by the death of dopaminergic... 
INSULIN | GLYCOGEN SYNTHASE KINASE‐3 (GSK‐3) | TYROSINE HYDROXYLASE (TH) | Bcl‐2 | PROTEIN KINASE B (Akt) | SH‐SY5Y | Bcl-2 | SH-SY5Y | GLYCOGEN SYNTHASE KINASE-3 (GSK-3) | NERVOUS-SYSTEM | OXIDATIVE STRESS | TYROSINE-HYDROXYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AKT/BCL-2 SIGNALING PATHWAYS | DEATH | DOPAMINERGIC-NEURONS | CELL BIOLOGY | INHIBITION | GENE-EXPRESSION | NITRIC-OXIDE | BRAIN | Tyrosine 3-Monooxygenase - metabolism | Reactive Oxygen Species - metabolism | Calcium - metabolism | Dopaminergic Neurons - pathology | Humans | Phosphatidylinositol 3-Kinases - metabolism | Cytotoxins - toxicity | Proto-Oncogene Proteins c-akt - genetics | Proto-Oncogene Proteins c-bcl-2 - metabolism | Neuroprotective Agents - pharmacology | Dopaminergic Neurons - metabolism | Mitogen-Activated Protein Kinase 1 - genetics | Dopaminergic Neurons - drug effects | Proto-Oncogene Proteins c-akt - metabolism | Cytotoxins - antagonists & inhibitors | bcl-2-Associated X Protein - genetics | Tretinoin - pharmacology | Insulin - pharmacology | Mitogen-Activated Protein Kinase 3 - genetics | Signal Transduction | 1-Methyl-4-phenylpyridinium - antagonists & inhibitors | Gene Expression Regulation | bcl-2-Associated X Protein - metabolism | Glycogen Synthase Kinase 3 - metabolism | Phosphatidylinositol 3-Kinases - genetics | Tyrosine 3-Monooxygenase - genetics | Glycogen Synthase Kinase 3 - genetics | Mitogen-Activated Protein Kinase 3 - metabolism | Nitric Oxide Synthase Type II - genetics | Cell Differentiation - drug effects | 1-Methyl-4-phenylpyridinium - toxicity | Cell Line, Tumor | Nitric Oxide - metabolism | Proto-Oncogene Proteins c-bcl-2 - genetics | Mitogen-Activated Protein Kinase 1 - metabolism | Nitric Oxide Synthase Type II - metabolism | Insulin | Analysis | Nitric oxide | Index Medicus
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7. Full Text Constitutive activation of Rho proteins by CNF-1 influences tight junction structure and epithelial barrier function
by Hopkins, Ann M and Walsh, Shaun V and Verkade, Paul and Boquet, Patrice and Nusrat, Asma
Journal of Cell Science, ISSN 0021-9533, 02/2003, Volume 116, Issue 4, pp. 725 - 742
The apical-most epithelial intercellular junction, referred to as the tight junction (TJ), regulates paracellular solute flux in diverse physiological and... 
Tight junction | F-actin | Rho GTPases | Epithelium | Paracellular permeability | TOXIN-INDUCED ACTIVATION | GTP-BINDING PROTEIN | CANINE KIDNEY-CELLS | paracellular permeability | ESCHERICHIA-COLI | PHAGOCYTIC BEHAVIOR | CELL BIOLOGY | ACTIN STRESS FIBERS | BACTERIAL TOXINS | epithelium | CYTOTOXIC NECROTIZING FACTOR-1 | FOCAL ADHESION KINASE | tight junction | RAC1 SMALL GTPASES | Immunohistochemistry | Cadherins - metabolism | Cell Adhesion Molecules | Humans | rac GTP-Binding Proteins - metabolism | Actins - drug effects | cdc42 GTP-Binding Protein - metabolism | Caveolins - metabolism | Carrier Proteins - drug effects | Endosomes - metabolism | Caveolin 1 | Cytotoxins - pharmacology | Endosomes - drug effects | Endosomes - ultrastructure | Tight Junctions - drug effects | Tight Junctions - metabolism | Epithelium - drug effects | Epithelium - metabolism | Tight Junctions - ultrastructure | Cell Membrane Permeability - physiology | Cell Membrane Permeability - drug effects | rho GTP-Binding Proteins - metabolism | Adherens Junctions - drug effects | Membrane Proteins - drug effects | Paxillin | cdc42 GTP-Binding Protein - drug effects | Phosphoproteins - drug effects | Epithelial Cells - metabolism | Epithelial Cells - drug effects | Actins - metabolism | Receptors, Cell Surface | Epithelium - ultrastructure | Phosphoproteins - metabolism | Adherens Junctions - metabolism | Occludin | Cytoskeletal Proteins - metabolism | Cytoskeletal Proteins - drug effects | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Tumor Cells, Cultured | Caveolins - drug effects | Epithelial Cells - ultrastructure | Cadherins - drug effects | Microscopy, Electron | Carrier Proteins - metabolism | Escherichia coli Proteins | Zonula Occludens-1 Protein | Microfilament Proteins - drug effects | Bacterial Toxins - pharmacology | Adherens Junctions - ultrastructure | rac GTP-Binding Proteins - drug effects
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8. Full Text Phosphatidylinositol 4,5-Bisphosphate Regulates Adipocyte Actin Dynamics and GLUT4 Vesicle Recycling
by Makoto Kanzaki and Megumi Furukawa and William Raab and Jeffrey E. Pessin
Journal of Biological Chemistry, ISSN 0021-9258, 07/2004, Volume 279, Issue 29, pp. 30622 - 30633
To investigate the potential role of phosphatidylinositol 4, 5-bisphosphate (PI(4,5)P 2 ) in the regulation of actin polymerization and GLUT4 translocation,... 
PLECKSTRIN HOMOLOGY DOMAINS | ISOLATED RAT ADIPOCYTES | 3T3-L1 ADIPOCYTES | RECEPTOR-MEDIATED ENDOCYTOSIS | GLUCOSE-TRANSPORTER GLUT4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLATHRIN-COATED PITS | N-WASP | PLASMA-MEMBRANE | GOLGI-COMPLEX | LIPID KINASE FAMILY | Dynamins - metabolism | 3T3-L1 Cells - metabolism | Actins - metabolism | Endosomes - metabolism | Muscle Proteins | Phosphatidylinositol 4,5-Diphosphate - metabolism | Endocytosis | trans-Golgi Network - metabolism | Thiazolidines | Transfection | Time Factors | Cytotoxins - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Monosaccharide Transport Proteins - metabolism | Fibroblasts - metabolism | Vesicular Transport Proteins | Cortactin | Wiskott-Aldrich Syndrome Protein, Neuronal | Glucose Transporter Type 4 | Gene Expression Regulation | Cholesterol - metabolism | Receptors, Transferrin - metabolism | Clathrin - metabolism | Bacterial Proteins | Nerve Tissue Proteins - metabolism | Bacterial Toxins - metabolism | Bridged Bicyclo Compounds, Heterocyclic - pharmacology | Animals | Carrier Proteins - metabolism | Qa-SNARE Proteins | Adipocytes - metabolism | Protein Binding | Golgi Apparatus - metabolism | Mice | Thiazoles - pharmacology | DNA, Complementary - metabolism | Microscopy, Fluorescence
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9. Full Text Sex-, species-, and tissue-specific metabolism of empagliflozin in male mouse kidney forms an unstable hemiacetal metabolite (M466/2) that degrades to 4-hydroxycrotonaldehyde, a reactive and cytotoxic species
by Taub, Mitchell E and Ludwig-Schwellinger, Eva and Ishiguro, Naoki and Kishimoto, Wataru and Yu, Hongbin and Wagner, Klaus and Tweedie, Donald
Chemical Research in Toxicology, ISSN 0893-228X, 01/2015, Volume 28, Issue 1, pp. 103 - 115
Following oral administration of empagliflozin (1000 mg/kg/day) to male and female CD-1 mice for 2 years, renal tubular injury was identified in male mice.... 
OXIDATIVE STRESS | CHEMISTRY, MEDICINAL | RAT | ANION TRANSPORTING POLYPEPTIDES | CHEMISTRY, MULTIDISCIPLINARY | CROTONALDEHYDE | PHARMACOKINETICS | SGLT2 INHIBITOR EMPAGLIFLOZIN | COTRANSPORTER | TOXICOLOGY | GENDER-DIFFERENCES | EXPRESSION | DRUG-METABOLISM | Microsomes - metabolism | Rats, Wistar | Species Specificity | Hypoglycemic Agents - metabolism | Oocytes - metabolism | Humans | Liver - metabolism | Xenopus laevis | Male | Aldehydes - metabolism | Glucosides - metabolism | Organic Anion Transporters - metabolism | Kidney - metabolism | Animals | HEK293 Cells | Kidney Diseases - chemically induced | Sex Factors | Cytotoxins - metabolism | Female | Mice | Benzhydryl Compounds - metabolism | Kidney Diseases - metabolism | Index Medicus
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10. Full Text Autoproteolytic cleavage mediates cytotoxicity of Clostridium difficile toxin A
by Kreimeyer, Isa and Euler, Friederike and Marckscheffel, Alexander and Tatge, Helma and Pich, Andreas and Olling, Alexandra and Schwarz, Janett and Just, Ingo and Gerhard, Ralf
Naunyn-Schmiedeberg's Archives of Pharmacology, ISSN 0028-1298, 3/2011, Volume 383, Issue 3, pp. 253 - 262
Toxin A and toxin B from Clostridium difficile are the causative agents of the antibiotic-associated pseudomembranous colitis. They are of an A/B structure... 
Neurosciences | Endocytosis | Biomedicine | Rho GTPases | Bacterial toxin | Clostridium difficile | Autoproteolysis | Pharmacology/Toxicology | CELLS | APOPTOSIS | DOMAIN | DEPENDS | INOSITOL HEXAKISPHOSPHATE | DISEASE | PHARMACOLOGY & PHARMACY | GLUCOSYLATION | RHO-GTPASES | PROTEINS | EXPRESSION | Phytic Acid - chemistry | NIH 3T3 Cells | Apoptosis - drug effects | Humans | Bacterial Proteins - chemistry | Caspase 3 - metabolism | Caspase 8 - metabolism | Cysteine Proteases - metabolism | cdc42 GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - metabolism | Dose-Response Relationship, Drug | Glucosyltransferases - metabolism | Cytotoxins - pharmacology | Cytotoxins - metabolism | Cell Membrane - metabolism | Dithiothreitol - chemistry | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Glycosylation | Bacterial Toxins - chemistry | Cell Shape - drug effects | HT29 Cells | Bacterial Proteins - pharmacology | Bacterial Toxins - metabolism | Animals | Amino Acid Substitution - physiology | Bacterial Toxins - pharmacology | Cytotoxins - chemistry | Enterotoxins - metabolism | Bacterial Proteins - metabolism | Cytosol - metabolism | Mice | Enterotoxins - chemistry | Enterotoxins - pharmacology | rac1 GTP-Binding Protein - metabolism | Protein Structure, Tertiary - physiology | Inositol | G proteins
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11. Full Text Endoplasmic reticulum stress contributes to helicobacter pylori VacA-induced apoptosis
by Akazawa, Yuko and Isomoto, Hajime and Matsushima, Kayoko and Kanda, Tsutomu and Minami, Hitomi and Yamaghchi, Naoyuki and Taura, Naota and Shiozawa, Ken and Ohnita, Ken and Takeshima, Fuminao and Nakano, Masayuki and Moss, Joel and Hirayama, Toshiya and Nakao, Kazuhiko
PLoS ONE, ISSN 1932-6203, 12/2013, Volume 8, Issue 12, p. e82322
Vacuolating cytotoxin A (VacA) is one of the important virulence factors produced by H. pylori. VacA induces apoptotic cell death, which is potentiated by... 
UNFOLDED PROTEIN RESPONSE | FATTY LIVER-DISEASE | VACUOLATING CYTOTOXIN | ER STRESS | MULTIDISCIPLINARY SCIENCES | GASTRIC EPITHELIAL-CELLS | DEATH | CYTOCHROME-C RELEASE | UP-REGULATION | TOXIN VACA | MOLECULAR-MECHANISMS | Gastric Mucosa - microbiology | Apoptosis - drug effects | eIF-2 Kinase - metabolism | Humans | Gastric Mucosa - pathology | Helicobacter pylori - drug effects | Gastric Mucosa - metabolism | RNA, Messenger - metabolism | Vacuoles - drug effects | Heat-Shock Proteins - genetics | Ammonium Chloride - pharmacology | Bcl-2-Like Protein 11 | Eukaryotic Initiation Factor-2 - metabolism | Membrane Proteins - metabolism | Phosphorylation - drug effects | Biomarkers - metabolism | Proto-Oncogene Proteins - metabolism | Endoplasmic Reticulum Stress - drug effects | Heat-Shock Proteins - metabolism | RNA, Messenger - genetics | Apoptosis Regulatory Proteins - metabolism | Gene Expression Regulation - drug effects | Helicobacter pylori - metabolism | Signal Transduction - drug effects | Cell Line, Tumor | Vacuoles - metabolism | Bacterial Proteins - metabolism | Transcription Factor CHOP - metabolism | Proteins | Ammonium compounds | Ammonia | Helicobacter pylori | Ammonium paratungstate | Helicobacter infections | Apoptosis | Cytochrome | Ammonium | Phosphorylation | Bax protein | Transcription | Toxicity | Epithelial cells | Mucosa | Virulence | Gastric mucosa | Homology | Infections | Activation | CCAAT/enhancer-binding protein | Kinases | Stomach cancer | Ammonium chloride | Mitochondria | Cell activation | Virulence factors | Chlorides | Hepatology | Gastroenterology | Stresses | Incubation | Mortality | siRNA | Permeability | Gene expression | Stress | Bacteriology | Signaling | Cell death | Endoplasmic reticulum | BIM protein
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12. Full Text The pore-forming toxin listeriolysin o mediates a novel entry pathway of L. monocytogenes into human hepatocytes
by Vadia, Stephen and Arnett, Eusondia and Haghighat, Anne-Cécile and Wilson-Kubalek, Elisabeth M and Tweten, Rodney K and Seveau, Stephanie
PLoS Pathogens, ISSN 1553-7366, 11/2011, Volume 7, Issue 11, p. e1002356
Intracellular pathogens have evolved diverse strategies to invade and survive within host cells. Among the most studied facultative intracellular pathogens,... 
HOST-CELLS | SURFACE PROTEIN | VIRULENCE FACTOR | MICROBIOLOGY | E-CADHERIN | CHOLESTEROL-DEPENDENT CYTOLYSIN | PLASMA-MEMBRANE REPAIR | MAMMALIAN-CELLS | STREPTOCOCCUS-PNEUMONIAE | VIROLOGY | EPITHELIAL-CELLS | PARASITOLOGY | MOLECULAR-MECHANISMS | Dynamins - metabolism | Pore Forming Cytotoxic Proteins - metabolism | Protein-Tyrosine Kinases - metabolism | Heat-Shock Proteins - metabolism | Humans | Actins - metabolism | Clathrin - metabolism | Hep G2 Cells | Host-Pathogen Interactions | Microspheres | Bacterial Toxins - metabolism | Listeria monocytogenes - pathogenicity | Polystyrenes | Cytotoxins - metabolism | Bacterial Proteins - metabolism | Cell Membrane - metabolism | Cell Membrane - microbiology | HeLa Cells | Hepatocytes - microbiology | Listeria monocytogenes - physiology | Hemolysin Proteins - metabolism | Physiological aspects | Listeriosis | Clathrin | Research | Actin | Risk factors | Proteins | Scanning electron microscopy | Automation | Motility | Microbiology | Listeria | Bacteria | Experiments
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13. Full Text Candidalysin is a fungal peptide toxin critical for mucosal infection
by Moyes, David L and Wilson, Duncan and Richardson, Jonathan P and Mogavero, Selene and Tang, Shirley X and Wernecke, Julia and Höfs, Sarah and Gratacap, Remi L and Robbins, Jon and Runglall, Manohursingh and Murciano, Celia and Blagojevic, Mariana and Thavaraj, Selvam and Förster, Toni M and Hebecker, Betty and Kasper, Lydia and Vizcay, Gema and Iancu, Simona I and Kichik, Nessim and Häder, Antje and Kurzai, Oliver and Luo, Ting and Krüger, Thomas and Kniemeyer, Olaf and Cota, Ernesto and Bader, Oliver and Wheeler, Robert T and Gutsmann, Thomas and Hube, Bernhard and Naglik, Julian R
Nature, ISSN 0028-0836, 04/2016, Volume 532, Issue 7597, pp. 64 - 68
Cytolytic proteins and peptide toxins are classical virulence factors of several bacterial pathogens which disrupt epithelial barrier function, damage cells... 
PATHOGENICITY MECHANISMS | BETA-MANNOSYLATION | PROTEIN-KINASE HOMOLOG | OROPHARYNGEAL CANDIDIASIS | EPITHELIAL-CELLS | FILAMENTOUS GROWTH | MULTIDISCIPLINARY SCIENCES | HYPHAL DEVELOPMENT | ALBICANS ENCODES | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTION FACTOR | Virulence - drug effects | Virulence Factors - genetics | Calcium - metabolism | Epithelial Cells - drug effects | Humans | Fungal Proteins - toxicity | Candida albicans - metabolism | Cytotoxins - secretion | Candidiasis - microbiology | Cytotoxins - toxicity | Host-Pathogen Interactions - immunology | Cytotoxins - metabolism | Mycotoxins - metabolism | Mycotoxins - genetics | Candidiasis - pathology | Virulence Factors - toxicity | Candida albicans - pathogenicity | Mycotoxins - secretion | Epithelial Cells - pathology | Fungal Proteins - genetics | Candida albicans - immunology | Mycotoxins - toxicity | Candidiasis - metabolism | Mucous Membrane - pathology | Signal Transduction - drug effects | Cell Membrane Permeability - drug effects | Epithelial Cells - immunology | Fungal Proteins - secretion | Virulence Factors - metabolism | Cytotoxins - genetics | Mucous Membrane - microbiology | Fungal Proteins - metabolism | Candida albicans | Fungi | Physiological aspects | Mucous membrane | Proteins | Yeast | Peptides | Cytokines | Pathogenesis | Toxins | Fungal infections
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