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1. Full Text Bifurcation of Toll-Like Receptor 9 Signaling by Adaptor Protein 3
by Miwa Sasai and Melissa M. Linehan and Akiko Iwasaki
Science, ISSN 0036-8075, 9/2010, Volume 329, Issue 5998, pp. 1530 - 1534
Endosomal Toll-like receptors (TLRs) 7 and 9 recognize viral pathogens and induce signals leading to the activation of nuclear factor KB (NF-KB)-dependent... 
T lymphocytes | Molecules | Cytokines | Microscopy | Genes | REPORTS | Toll like receptors | Agonists | Macrophages | Cells | Endosomes | LOCALIZATION | ACTIVATION | DENDRITIC CELLS | TRAF3 | MULTIDISCIPLINARY SCIENCES | TLR9 | TOLL-LIKE-RECEPTOR-9 | INDUCTION | INTERFERON-ALPHA PRODUCTION | I INTERFERON | AP-3 ADAPTER | Recombinant Fusion Proteins - immunology | Dendritic Cells - immunology | Transcriptional Activation | Interferon Type I - immunology | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Toll-Like Receptor 9 - immunology | Cytoplasmic Vesicles - metabolism | Interferon Type I - metabolism | Membrane Transport Proteins - metabolism | Cytokines - genetics | Dendritic Cells - metabolism | Macrophages - immunology | Cytokines - immunology | Oligodeoxyribonucleotides - immunology | Cytokines - metabolism | Signal Transduction | Vesicle-Associated Membrane Protein 3 - metabolism | Mice, Inbred C57BL | Cells, Cultured | TNF Receptor-Associated Factor 3 - metabolism | Adaptor Protein Complex beta Subunits | Interferon Regulatory Factor-7 - metabolism | Adaptor Protein Complex 3 - metabolism | Protein Transport | Animals | Adaptor Protein Complex 3 - genetics | Interferon Type I - genetics | Mice | Toll-Like Receptor 9 - metabolism | Myeloid Differentiation Factor 88 - metabolism | Lysosomal-Associated Membrane Protein 2 - metabolism | Cellular control mechanisms | Physiological aspects | TLR7 | Research | Health aspects | Immune system | Proteins | Signal transduction | Interferon | Cellular biology | Receptors | Compartments | Bifurcations | Activation
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2. Full Text Differential responses of pattern recognition receptors to outer membrane vesicles of three periodontal pathogens
by Cecil, Jessica D and O'Brien-Simpson, Neil M and Lenzo, Jason C and Holden, James A and Chen, Yu-Yen and Singleton, William and Gause, Katelyn T and Yan, Yan and Caruso, Frank and Reynolds, Eric C
PLoS ONE, ISSN 1932-6203, 04/2016, Volume 11, Issue 4, p. e0151967
Highly purified outer membrane vesicles (OMVs) of the periodontal pathogens, Porphyromonas gingivalis, Treponema denticola and Tannerella forsythia were... 
PROTEINASE-ADHESIN COMPLEXES | BACTEROIDES-GINGIVALIS | BACTERIA | TREPONEMA-DENTICOLA | EPITHELIAL-CELLS | SOLUBLE PEPTIDOGLYCAN | PORPHYROMONAS-GINGIVALIS | DNA | MULTIDISCIPLINARY SCIENCES | RELEASE | VIRULENCE | Cell Line | Receptors, Pattern Recognition - isolation & purification | Bacterial Outer Membrane Proteins - immunology | Bacteroides - chemistry | Receptors, Pattern Recognition - immunology | Receptors, Pattern Recognition - chemistry | Bacteroides - immunology | Humans | Treponema denticola - immunology | Bacterial Outer Membrane Proteins - chemistry | Nod2 Signaling Adaptor Protein - immunology | Porphyromonas gingivalis - chemistry | Toll-Like Receptor 4 - immunology | Nod1 Signaling Adaptor Protein - immunology | Bacterial Outer Membrane Proteins - isolation & purification | Treponema denticola - chemistry | Chronic Periodontitis - microbiology | Lipopolysaccharides - analysis | Chronic Periodontitis - immunology | Toll-Like Receptor 2 - immunology | Peptidoglycan - analysis | Porphyromonas gingivalis - immunology | Virulence (Microbiology) | Periodontitis | Analysis | Risk factors | Pattern recognition receptors | Cell culture | Dental schools | Disease | Lipids | Ultracentrifugation | Nanoparticles | Proteins | Signal transduction | Receptors | Vesicles | Ultrafiltration | Rodents | Toll-like receptors | Bacteria | Nod1 protein | Deoxyribonucleic acid--DNA | NOD2 protein | Pathogens | Enzymes | Enumeration | TLR7 protein | Light scattering | Peptidoglycans | Membrane vesicles | Inflammation | Nucleic acids | Pattern recognition | TLR4 protein | Fatty acids | TLR9 protein | Cytometry | Biofilms | Oral hygiene | TLR2 protein | Deoxyribonucleic acid
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3. Full Text Tim-3 negatively regulates IL-12 expression by monocytes in HCV infection
by Zhang, Ying and Ma, Cheng J and Wang, Jia M and Ji, Xiao J and Wu, Xiao Y and Jia, Zhan S and Moorman, Jonathan P and Yao, Zhi Q
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 5, p. e19664
T-cell immunoglobulin and mucin domain-containing protein 3 (Tim-3) is a newly identified negative immunomodulator that is up-regulated on dysfunctional T... 
ACTIVATION | DENDRITIC CELLS | MULTIDISCIPLINARY SCIENCES | ELEVATED FREQUENCIES | HEPATITIS-C-VIRUS | CD4(+) | T-CELL IMMUNOGLOBULIN | GENE FAMILY | CORE PROTEIN | CONTAINING MOLECULE-3 TIM-3 | PD-1 EXPRESSION | Up-Regulation | Phosphorylation | Hepacivirus - immunology | Coculture Techniques | Humans | Middle Aged | Hepatitis C, Chronic - virology | Suppressor of Cytokine Signaling 1 Protein | Male | Monocytes - metabolism | Hepatocytes - metabolism | Complement C1q - metabolism | Antigens, CD - metabolism | Lipopolysaccharide Receptors - metabolism | STAT1 Transcription Factor - metabolism | Mitochondrial Proteins - metabolism | Viral Core Proteins - metabolism | Adult | Membrane Proteins - metabolism | Interleukin-12 Subunit p40 - biosynthesis | Interleukin-12 Subunit p40 - metabolism | Signal Transduction | Macrophage Activation - immunology | Down-Regulation | Gene Silencing | Suppressor of Cytokine Signaling Proteins - genetics | Hepatitis A Virus Cellular Receptor 2 | Apoptosis Regulatory Proteins - metabolism | Macrophages - metabolism | Carrier Proteins - metabolism | Hepatitis C, Chronic - immunology | Hepatocytes - virology | Protein Binding | Programmed Cell Death 1 Receptor | Infection | Medical research | Cytokines | Immunotherapy | Medicine, Experimental | T cells | Hepatitis C virus | Gene expression | Health aspects | Mitogens | Health care | Multiple sclerosis | PD-1 protein | Veterans | Crosstalk | Lymphocytes T | Arthritis | Infections | Macrophages | CD14 antigen | Lipopolysaccharides | Proteins | Hepatitis | Lymphocytes | Toll-like receptors | Inhibition | Stat1 protein | Immune system | Antigens | Immunoglobulins | Immune response | TLR7 protein | Internal medicine | Immunoregulation | Secretion | Melanoma | Blocking | Interleukin 12 | T cell receptors | Inflammation | TLR4 protein | Medicine | Complement component C1q | Signaling | Monocytes | Hospitals | Infectious diseases | Mucin | Core protein | Hepatocytes | Ligands | Human behavior | Viral infections
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4. Full Text UNC93B1 mediates differential trafficking of endosomal TLRs
by Lee, Bettina L and Moon, Joanne E and Shu, Jeffrey H and Yuan, Lin and Newman, Zachary R and Schekman, Randy and Barton, Gregory M
eLife, ISSN 2050-084X, 02/2013, Volume 2013, Issue 2, p. e00291
UNC93B1, a multipass transmembrane protein required for TLR3, TLR7, TLR9, TLR11, TLR12, and TLR13 function, controls trafficking of TLRs from the endoplasmic... 
NUCLEIC-ACID RECOGNITION | COMPLEX | DENDRITIC CELLS | IMMUNE-RESPONSES | BIOLOGY | TOLL-LIKE RECEPTORS | AP-4 | AMYLOID PRECURSOR PROTEIN | MEMBRANE-PROTEINS | SORTING SIGNALS | CLATHRIN | Humans | Mice, Inbred C57BL | COP-Coated Vesicles - metabolism | Cercopithecus aethiops | Endoplasmic Reticulum - metabolism | Mice, Transgenic | Endosomes - metabolism | Protein Transport | Adaptor Protein Complex 2 - metabolism | Animals | Transfection | RNA Interference | Membrane Transport Proteins - genetics | Toll-Like Receptors - genetics | HEK293 Cells | Golgi Apparatus - metabolism | Membrane Transport Proteins - metabolism | Mutation | Toll-Like Receptors - metabolism | COS Cells | TLR7 protein | Yeast | Biology | TLR3 protein | TLR9 protein | Golgi apparatus | Recruitment | Proteins | Toll-like receptors | Ligands | Localization | Autoimmune diseases | Endoplasmic reticulum | Deoxyribonucleic acid--DNA
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5. Full Text Various human epithelial cells express functional Toll-like receptors, NOD1 and NOD2 to produce anti-microbial peptides, but not proinflammatory cytokines
by Uehara, Akiko and Fujimoto, Yukari and Fukase, Koichi and Takada, Haruhiko
Molecular Immunology, ISSN 0161-5890, 2007, Volume 44, Issue 12, pp. 3100 - 3111
Epithelial cells may form the first barrier of defense against bacteria in human tissues. We recently revealed that oral epithelial cells generated... 
NODs | Epithelial cells | β-Defensin 2 | TLRs | beta-defensin 2 | PEPTIDOGLYCAN RECOGNITION PROTEINS | BETA-DEFENSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | epithelial cells | HUMAN GINGIVAL | LIPOPOLYSACCHARIDES | IMMUNOLOGY | BACTERIAL PEPTIDOGLYCAN | IDENTIFICATION | LIPOTEICHOIC ACIDS | ARTHROPOD | HOST RECOGNITION | INNATE IMMUNITY | beta-Defensins - genetics | Epithelial Cells - metabolism | Carrier Proteins - biosynthesis | Humans | Gene Expression Regulation | Nod2 Signaling Adaptor Protein - genetics | Inflammation | Immunity | Bacteria - immunology | Epithelial Cells - immunology | Toll-Like Receptors - genetics | Cytokines - biosynthesis | Nod1 Signaling Adaptor Protein - genetics | Microbiology | Peptides | Tongue | RNA | Lung | Kidney | Lipid A | Mimicry | Interleukin 6 | peptidoglycan recognition proteins | Intestine | Antimicrobial peptides | Toll-like receptors | Nod1 protein | Interleukin 8 | NOD2 protein | TLR7 protein | Cytokines | lipopeptides | Salivary gland | Poly (I:C) | TLR4 protein | Pharynx | TLR3 protein | Esophagus | Defensins | TLR2 protein | Monocyte chemoattractant protein 1
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6. Full Text TRIpartite Motif 21 (TRIM21) differentially regulates the stability of Interferon Regulatory Factor 5 (IRF5) isoforms
by Lazzari, Elisa and Korczeniewska, Justyna and Ní Gabhann, Joan and Smith, Siobhán and Barnes, Betsy J and Jefferies, Caroline A
PLoS ONE, ISSN 1932-6203, 08/2014, Volume 9, Issue 8, p. e103609
IRF5 is a member of the Interferon Regulatory Factor (IRF) family of transcription factors activated downstream of the Toll-Like receptors (TLRs).... 
VARIANTS | CRYSTAL-STRUCTURE | TRANSACTIVATION | UBIQUITIN | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | DEGRADATION | FAMILY PROTEINS | RISK HAPLOTYPE | I INTERFERON | BLOOD-CELLS | Toll-Like Receptor 7 - genetics | Cell Line | Immunoprecipitation | Toll-Like Receptor 7 - metabolism | Humans | Interferon Regulatory Factors - metabolism | Interferon Regulatory Factors - genetics | Ribonucleoproteins - metabolism | Blotting, Western | Microscopy, Confocal | Protein Isoforms - metabolism | Protein Binding | Ribonucleoproteins - genetics | HeLa Cells | Protein Stability | Real-Time Polymerase Chain Reaction | Protein Isoforms - genetics | Ubiquitin | Systemic lupus erythematosus | Biological response modifiers | Proteolysis | Analysis | Haplotypes | Alternative splicing | Health sciences | Transcription factors | Phosphorylation | Disease | Insertion | Biochemistry | Autophagy | Degradation | Proteins | Receptors | Penicillin | Toll-like receptors | Ubiquitin-protein ligase | Immune system | Lupus | Immune response | TLR7 protein | Stability | Cytokines | Splicing | Gene expression | Chronic conditions | Hypotheses | Cellular biology | Isoforms | Interferon | Molecular biology | Autoimmune diseases | Interferon regulatory factor
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7. Full Text Human Keratinocytes Express Functional Toll-Like Receptor 3, 4, 5, and 9
by Lebre, Maria C and van der Aar, Angelic M.G and van Baarsen, Lisa and van Capel, Toni M.M and Schuitemaker, Joost H.N and Kapsenberg, Martien L and de Jong, Esther C
Journal of Investigative Dermatology, ISSN 0022-202X, 02/2007, Volume 127, Issue 2, pp. 331 - 341
Keratinocytes are continuously in contact with external stimuli and have the capacity to produce several soluble mediators. Pathogen-associated molecular... 
TOLL-LIKE-RECEPTORS | DOUBLE-STRANDED-RNA | DENDRITIC CELLS | SKIN-ASSOCIATED CHEMOKINE | MONOCYTE CHEMOATTRACTANT PROTEIN-1 | INNATE IMMUNE-RESPONSE | INFLAMMATORY PROTEIN 3-ALPHA | NECROSIS-FACTOR-ALPHA | FACTOR-KAPPA-B | HUMAN EPIDERMAL-KERATINOCYTES | DERMATOLOGY | Oligonucleotides - genetics | Phosphorylation | Toll-Like Receptor 5 - genetics | Humans | Toll-Like Receptor 9 - genetics | I-kappa B Proteins - metabolism | RNA, Messenger - metabolism | Flagellin - pharmacology | Tissue Distribution | Cell Nucleus - metabolism | Protein Isoforms - metabolism | Biological Transport | Oligonucleotides - pharmacology | Toll-Like Receptor 3 - genetics | Toll-Like Receptors - metabolism | Chemokine CXCL9 | Toll-Like Receptor 5 - metabolism | Poly I-C - pharmacology | Cytokines - metabolism | Cells, Cultured | Toll-Like Receptor 4 - genetics | Toll-Like Receptor 3 - metabolism | Toll-Like Receptor 4 - metabolism | Chemokine CXCL10 | Transcription Factor RelA - metabolism | Keratinocytes - metabolism | Toll-Like Receptors - genetics | Chemokines, CXC - metabolism | Lipopolysaccharides - pharmacology | CpG Islands | Ligands | Chemokines - metabolism | Toll-Like Receptor 9 - metabolism | CD40 antigen | Oligonucleotides | Flagellin | mRNA | intercellular adhesion molecule 1 | Immunity | Lipopolysaccharides | CXC chemokines | CCL20 protein | Toll-like receptors | CpG islands | TLR7 protein | Dermatology | Keratinocytes | Nuclear transport | Stress | TLR3 protein | TLR9 protein | TLR1 protein | External stimuli | CXCL10 protein | Histocompatibility antigen HLA | Interferon | Internet | Monocyte chemoattractant protein 1 | Tumor necrosis factor- alpha
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8. Full Text Hepatitis b virus lacks immune activating capacity, but actively inhibits plasmacytoid dendritic cell function
by Woltman, Anea and Brouw, M.L.O and Biesta, Paula and Shi, Cui and Janssen, Harry
PLoS ONE, ISSN 1932-6203, 02/2011, Volume 6, Issue 1, p. e15324
textabstractChronic hepatitis B virus (HBV) infection is caused by inadequate anti-viral immunity. Activation of plasmacytoid dendritic cells (pDC) leading to... 
NATURAL-KILLER | BIOLOGY | GENE-EXPRESSION | RECEPTOR | C VIRUS | IMMUNOLOGY | NONPARENCHYMAL LIVER-CELLS | HBV | IFN-ALPHA PRODUCTION | VIRAL-INFECTION | I INTERFERON | Cell Communication - immunology | Dendritic Cells - immunology | Humans | Tumor Necrosis Factor-alpha - genetics | Cells, Cultured | Viral Proteins - pharmacology | Monocytes - immunology | Dendritic Cells - virology | Hepatitis B virus - immunology | Immunity | Tumor Necrosis Factor-alpha - biosynthesis | Case-Control Studies | Medical research | Antiviral agents | Dendritic cells | Research | Genetic transcription | Proteins | Infection | Killer cells | Medicine, Experimental | Hepatitis B virus | Comparative analysis | Health aspects | Hepatitis B | TOR protein | Animal models | Phosphorylation | Transcription | Liver | Chronic infection | Viruses | Infections | Activation | Interleukin 6 | Hepatitis | Cell activation | Hepatology | Gastroenterology | Toll-like receptors | IP-10 protein | Natural killer cells | Active control | Deoxyribonucleic acid--DNA | CpG islands | Antigens | TLR7 protein | Hepatitis B surface antigen | Cytokines | Tumor necrosis factor-α | Gene expression | Patients | TLR9 protein | Hepatitis B e antigen | Interferon regulatory factor 7 | Immunosuppression | Monocytes | Lymphocytes B | Influenza | Ligands | Interferon | Viral infections | Deoxyribonucleic acid | DNA
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9. Full Text Structural Reorganization of the Toll-Like Receptor 8 Dimer Induced by Agonistic Ligands
by Hiromi Tanji and Umeharu Ohto and Takuma Shibata and Kensuke Miyake and Toshiyuki Shimizu
Science, ISSN 0036-8075, 3/2013, Volume 339, Issue 6126, pp. 1426 - 1429
Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses. Several synthetic agonists of TLR7-TLR8 display novel... 
Molecules | Receptors | Hydrogen bonds | REPORTS | Atoms | Ligands | Dimers | Dimerization | Chemicals | Monomers | Crystal structure | RESPONSES | CELLS | STRANDED-RNA | ACTIVATION | RECOGNITION | INTERFERING RNA | MULTIDISCIPLINARY SCIENCES | TLR7 | INDUCTION | SUBFAMILY | VIRUSES | Protein Structure, Tertiary | Amino Acid Sequence | Thiazoles - metabolism | Toll-Like Receptor 8 - chemistry | Protein Structure, Secondary | Signal Transduction | Humans | Protein Multimerization | Quinolines - chemistry | Imidazoles - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Mutant Proteins - metabolism | Quinolines - metabolism | Hydrogen Bonding | Mutant Proteins - chemistry | Protein Binding | Protein Conformation | Thiazoles - chemistry | Toll-Like Receptor 8 - metabolism | Imidazoles - metabolism | Toll-Like Receptor 8 - agonists | Toll-like receptors | Physiological aspects | Health aspects | Ligands (Biochemistry) | Pathogens | Signaling | Immunology | Cellular biology
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10. Full Text IFN-γ synergism with poly I:C reduces growth of murine and human cancer cells with simultaneous changes in cell cycle and immune checkpoint proteins
by Guinn, Zachary P and Petro, Thomas M
Cancer Letters, ISSN 0304-3835, 12/2018, Volume 438, pp. 1 - 9
Previously, we reported that IFN-γ and poly I:C, a TLR3 Pattern Recognition Receptor (PRR) agonist, reduces growth of and induces Cleaved-Caspase-3, ISG54 and... 
PRR agonists | B16 melanoma | IFN-γ | Squamous cell carcinoma | Poly I:C | ACTIVATION | COMPONENTS | IPN-gamma | IMIQUIMOD | RESPONSES | ONCOLOGY | SIGNALING PATHWAY | MICE | TLR7 | NF-KAPPA-B | TUMOR-GROWTH | EXPRESSION | Viruses | Kinases | Macrophages | Caspase-3 | Cell surface | Synergism | Proteins | Cell growth | Lymphocytes | Immunotherapy | Cell cycle | Toll-like receptors | Deoxyribonucleic acid--DNA | TLR7 protein | Melanoma | Caspase | Adjuvants | Poly (I:C) | Pattern recognition | TLR4 protein | TLR3 protein | TLR9 protein | Immune checkpoint | TLR2 protein | γ-Interferon | PD-L1 protein | Adapter proteins | Cancer
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11. Full Text Protein kinase IKKβ-catalyzed phosphorylation of IRF5 at Ser462 induces its dimerization and nuclear translocation in myeloid cells
by Marta Lopez-Pelaez and Douglas J. Lamont and Mark Peggie and Natalia Shpiro and Nathanael S. Gray and Philip Cohen
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 49, pp. 17432 - 17437
The siRNA knockdown of IFN Regulatory Factor 5 (IRF5) in the human plasmacytoid dendritic cell line Gen2.2 prevented IFNβ production induced by compound CL097,... 
Phosphorylation | Myeloid cells | Messenger RNA | Dendritic cells | Interferons | Cell nucleus | Genes | Cell lines | Small interfering RNA | Agonists | Interferon β | IRF5 | TLR7 | IKKβ | Plasmacytoid dendritic cell | interferon beta | LOCALIZATION | ACTIVATION | MULTIDISCIPLINARY SCIENCES | plasmacytoid dendritic cell | INDUCTION | TOLL-LIKE-RECEPTOR-7 | INTERFERON REGULATORY FACTOR | VIRAL-INFECTION | PLASMACYTOID DENDRITIC CELLS | IKK beta | GENE | IN-VIVO | INHIBITORS | Cell Line | NF-kappa B p50 Subunit - metabolism | Humans | Protein Multimerization | Interferon Regulatory Factors - metabolism | Inflammation | I-kappa B Proteins - metabolism | Immunity, Innate | Serine - chemistry | Gene Expression Regulation, Enzymologic | Animals | Transfection | Interferon-beta - metabolism | Ligands | Transcription, Genetic | Mice | Active Transport, Cell Nucleus | Mutation | Microscopy, Fluorescence | Biological Sciences | interferon β
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