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Respirology, ISSN 1323-7799, 11/2018, Volume 23, Issue S2, pp. 25 - 25
Journal Article
Nature Reviews Microbiology, ISSN 1740-1526, 05/2018, Volume 16, Issue 6, pp. 1 - 391
The image that accompanies this article was wrongly credited to Macmillan Publishers Limited in the online version. The correct credit is iStockphoto. This has... 
Internet | Lipopolysaccharides
Journal Article
NO paradox in asthma, 12/2005
Asthma results from allergen-driven intrapulmonary Th2 response, and is characterized by intermittent airway obstruction, airway hyperreactivity (AHR), and... 
asthma - nitric oxide - lipopolysaccharides
Journal
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2762 - 14
Thrombin-derived C-terminal peptides (TCPs) of about 2 kDa are present in wounds, where they exert anti-endotoxic functions. Employing a combination of nuclear... 
HOST-DEFENSE PEPTIDES | NMR STRUCTURES | MOLECULAR-DYNAMICS | PROTEIN | MULTIDISCIPLINARY SCIENCES | TOLL-LIKE RECEPTOR | OUTER-MEMBRANE-PERMEABILIZATION | FORCE-FIELD | ANTIMICROBIAL PEPTIDES | LIPOPOLYSACCHARIDE LPS | MECHANISTIC-INSIGHTS | Antimicrobial Cationic Peptides - immunology | Humans | Lipopolysaccharides - metabolism | Neutralization Tests | Antimicrobial Cationic Peptides - metabolism | Lipopolysaccharides - immunology | Lipopolysaccharide Receptors - metabolism | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Thrombin - immunology | Lipopolysaccharide Receptors - chemistry | Amino Acid Sequence | Protein Conformation, alpha-Helical | Antimicrobial Cationic Peptides - chemistry | THP-1 Cells | Lipopolysaccharide Receptors - immunology | Leukocyte Elastase - chemistry | Protein Conformation, beta-Strand | Escherichia coli - genetics | Thrombin - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | Lipopolysaccharides - chemistry | Thrombin - metabolism | Leukocyte Elastase - immunology | Nuclear magnetic resonance--NMR | Complex formation | Antiinflammatory agents | Peptides | Thrombin | Mass spectroscopy | Inflammation | Hydrophobicity | Endotoxin shock | CD14 antigen | Molecular chains | Lipopolysaccharides | Magnetic resonance spectroscopy | Sepsis | Elastase | Mass spectrometry | Conformation | Index Medicus | Medical Biotechnology | Medical and Health Sciences | Medicin och hälsovetenskap | Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) | Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci) | Medicinsk bioteknologi
Journal Article
Developmental and Comparative Immunology, ISSN 0145-305X, 11/2018, Volume 88, pp. 94 - 103
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2018, Volume 13, Issue 8, pp. e0202664 - e0202664
Escherichia coli is one of the major pathogens causing mastitis in dairy cattle. Yet, the factors which mediate the ability for E. coli to develop in the... 
SIGNALING PATHWAYS | COMPLEMENT FRAGMENT C5A | MULTIDISCIPLINARY SCIENCES | LIPOPOLYSACCHARIDE | BOVINE MASTITIS | STAPHYLOCOCCUS-AUREUS | POLYACRYLAMIDE GELS | REDUCES SEVERITY | INTRAMAMMARY INFECTIONS | KAPPA-B | INFLAMMATORY CYTOKINES | Epithelial Cells - metabolism | Milk - microbiology | O Antigens - metabolism | Humans | Lipopolysaccharides - metabolism | Recombinant Proteins - biosynthesis | Lipopolysaccharides - immunology | Lipopolysaccharide Receptors - metabolism | Mastitis, Bovine - pathology | Cattle | DNA Transposable Elements - genetics | Escherichia coli - metabolism | HEK293 Cells | Female | Escherichia coli - growth & development | Mastitis, Bovine - immunology | Epithelial Cells - cytology | O Antigens - chemistry | Lipopolysaccharide Receptors - chemistry | Cell Line | Cytokines - metabolism | Recombinant Proteins - chemistry | Toll-Like Receptor 2 - metabolism | Toll-Like Receptor 4 - metabolism | Mastitis, Bovine - microbiology | Animals | Mutagenesis | Escherichia coli - isolation & purification | Milk - metabolism | Lipopolysaccharides - analysis | Lipopolysaccharide Receptors - genetics | Chemokines - metabolism | Antigens | Polysaccharides | Analysis | Dairy cattle | Physiological aspects | Development and progression | Inflammation | Health aspects | Mitogens | Bacterial antigens | Epithelial cells | Escherichia coli | Genetic aspects | Research | Lipopolysaccharides | Lipids | Inflammatory response | Biosynthesis | Infections | CD14 antigen | E coli | Bacteria | Tumor necrosis factor-TNF | Gram-negative bacteria | Mammary gland | Udder | Recombinant | Milk | Mastitis | Bacterial infections | Neutrophils | Mammary glands | Biological activity | Mutants | Hypotheses | Colonization | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 514, Issue 7521, pp. 187 - 192
The murine caspase-11 non-canonical inflammasome responds to various bacterial infections. Caspase-11 activation-induced pyroptosis, in response to cytoplasmic... 
ACTIVATION | GRAM-NEGATIVE BACTERIA | MULTIDISCIPLINARY SCIENCES | CYTOPLASMIC LPS | NLRP3 | LIPID IVA | MECHANISMS | PYROPTOSIS | PROTEINS | TLR4 | LIPOPOLYSACCHARIDE RECOGNITION | Surface Plasmon Resonance | Epithelial Cells - metabolism | Caspases - immunology | Humans | Lipopolysaccharides - metabolism | Substrate Specificity | Caspases, Initiator - genetics | Genetic Complementation Test | Lipopolysaccharides - immunology | Caspases - metabolism | Caspases, Initiator - metabolism | Protein Multimerization - genetics | Cell Death - drug effects | Caspases - chemistry | Epithelial Cells - cytology | Caspases, Initiator - immunology | Lipid A - metabolism | Caspases - genetics | Cells, Cultured | Rhodobacter sphaeroides - chemistry | Mutant Proteins - metabolism | Keratinocytes - cytology | Macrophages - cytology | Enzyme Activation - drug effects | Immunity, Innate | Necrosis - chemically induced | Macrophages - metabolism | Animals | Rhodobacter sphaeroides - immunology | Keratinocytes - metabolism | Caspases, Initiator - chemistry | Mutant Proteins - chemistry | Lipopolysaccharides - pharmacology | Protein Binding | Macrophages - drug effects | Mice | Enzyme Activation - genetics | Inflammation - enzymology | Protein Multimerization - drug effects | Lipids | Septic shock | Immune response | Health aspects | Analysis | Proteins | Salmonella | Bacterial infections | E coli | Bacteria | Cytotoxicity | Mutation | Apoptosis | Index Medicus
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 11/2018, Volume 119, pp. 1027 - 1035
Journal Article
Journal Article
Journal Article
Cell, ISSN 0092-8674, 2007, Volume 130, Issue 5, pp. 906 - 917
TLR4 and MD-2 form a heterodimer that recognizes LPS (lipopolysaccharide) from Gram-negative bacteria. Eritoran is an analog of LPS that antagonizes its... 
PROTEINS | MOLIMMUNO | BACTERIAL LIPOPOLYSACCHARIDE | MD-2 BINDS | CELL ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TOLL-LIKE RECEPTORS | PROTEIN COMPLEXES | LEUCINE-RICH REPEAT | LIPID IVA | CONFERS LIPOPOLYSACCHARIDE RESPONSIVENESS | TLR4 | MONOMERIC ENDOTOXIN | CELL BIOLOGY | Disaccharides - metabolism | Lymphocyte Antigen 96 - metabolism | Humans | Immunoglobulin Variable Region - chemistry | Lipopolysaccharides - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Hagfishes | Lipopolysaccharides - antagonists & inhibitors | Disaccharides - chemistry | Lymphocyte Antigen 96 - genetics | Disaccharides - pharmacology | Sugar Phosphates - pharmacology | Lymphocyte Antigen 96 - chemistry | Cloning, Molecular | Protein Engineering | Molecular Structure | Toll-Like Receptor 4 - antagonists & inhibitors | Binding Sites | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | Fish Proteins - chemistry | Sugar Phosphates - chemistry | Models, Molecular | Toll-Like Receptor 4 - genetics | Toll-Like Receptor 4 - chemistry | Recombinant Fusion Proteins - chemistry | Toll-Like Receptor 4 - metabolism | Animals | Sugar Phosphates - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Conformation | Lipopolysaccharides - chemistry | Mice | Structural Homology, Protein | Mutation | Structure | Crystals | Index Medicus
Journal Article
Journal of Clinical Periodontology, ISSN 0303-6979, 06/2018, Volume 45, Issue S19, pp. 155 - 155
Journal Article
Journal Article
Atherosclerosis, ISSN 0021-9150, 2013, Volume 229, Issue 2, pp. 356 - 362
Journal Article
Nature, ISSN 0028-0836, 04/2011, Volume 472, Issue 7343, pp. 361 - 365
TRIM5 is a RING domain-E3 ubiquitin ligase that restricts infection by human immunodeficiency virus (HIV)-1 and other retroviruses immediately following virus...