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1. Full Text TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis
by Chauhan, Santosh and Kumar, Suresh and Jain, Ashish and Ponpuak, Marisa and Mudd, Michal H and Kimura, Tomonori and Choi, Seong Won and Peters, Ryan and Mandell, Michael and Bruun, Jack-Ansgar and Johansen, Terje and Deretic, Vojo
Developmental cell, ISSN 1534-5807, 10/2016, Volume 39, Issue 1, pp. 13 - 27
Life Sciences & Biomedicine | Developmental Biology | Science & Technology | Cell Biology | Phosphorylation | TOR Serine-Threonine Kinases - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Galectin 3 - metabolism | Ubiquitin - metabolism | Homeostasis | Autophagy-Related Protein-1 Homolog - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | DNA-Binding Proteins - metabolism | Multiprotein Complexes - metabolism | Ubiquitination | Lysosomes - metabolism | HEK293 Cells | Mycobacterium tuberculosis - physiology | Lysosomes - pathology | Protein Stability | Cytoprotection | Transcription Factors - metabolism | Animals | Protein Binding | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | RAW 264.7 Cells | Mice | HeLa Cells | Beclin-1 - metabolism | Autophagy-Related Proteins - metabolism | Calcineurin - metabolism | Intracellular Membranes - metabolism | Ubiquitin | Tuberculosis | Ligases | Index Medicus
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2. Full Text Proteomic and transcriptomic experiments reveal an essential role of RNA degradosome complexes in shaping the transcriptome of Mycobacterium tuberculosis
by Plocinski, Przemyslaw and Macios, Maria and Houghton, Joanna and Niemiec, Emilia and Plocinska, Renata and Brzostek, Anna and Slomka, Marcin and Dziadek, Jaroslaw and Young, Douglas and Dziembowski, Andrzej
Nucleic acids research, ISSN 0305-1048, 06/2019, Volume 47, Issue 11, pp. 5892 - 5905
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | RNA Helicases - metabolism | Multienzyme Complexes | Polyribonucleotide Nucleotidyltransferase - metabolism | Ribonuclease III - metabolism | Endoribonucleases - metabolism | Mycobacterium smegmatis - metabolism | Polyribonucleotide Nucleotidyltransferase - genetics | RNA - analysis | Transcriptome | Escherichia coli Proteins - metabolism | Proteome | Thiouridine - chemistry | RNA - chemistry | RNA Stability | Ribonucleases - metabolism | Escherichia coli - genetics | Proteomics | DEAD-box RNA Helicases - metabolism | Mycobacterium tuberculosis - metabolism | RNA, Bacterial - metabolism | Index Medicus | RNA and RNA-protein complexes | Basic Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | RNA Helicases/metabolism | RNA, Bacterial/metabolism | Immunologi inom det medicinska området | Escherichia coli/genetics | DEAD-box RNA Helicases/metabolism | Mycobacterium tuberculosis/metabolism | Ribonuclease III/metabolism | Mycobacterium smegmatis/metabolism | Polyribonucleotide Nucleotidyltransferase/genetics | Endoribonucleases/metabolism | Medicinska och farmaceutiska grundvetenskaper | Escherichia coli Proteins/metabolism | Thiouridine/chemistry | RNA/analysis | Immunology in the medical area | Ribonucleases/metabolism
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3. Full Text The CATERPILLER protein Monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor α-, and Mycobacterium tuberculosis-induced pro-inflammatory signals
by Williams, Kristi L and Lich, John D and Duncan, Joseph A and Reed, William and Rallabhandi, Prasad and Moore, Christopher and Kurtz, Sherry and McNeil Coffield, V and Accavitti-Loper, Mary A and Su, Lishan and Vogel, Stefanie N and Braunstein, Miriam and Ting, Jenny P.-Y
The Journal of biological chemistry, ISSN 0021-9258, 12/2005, Volume 280, Issue 48, pp. 39914 - 39924
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Protein Kinases - metabolism | Tumor Necrosis Factor-alpha - metabolism | Phosphorylation | Immunoprecipitation | Luciferases - metabolism | Humans | Transcriptional Activation | Interleukin-1 Receptor-Associated Kinases | Monocytes - metabolism | NF-kappa B - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Transfection | Retroviridae - genetics | Antigens, Differentiation - metabolism | Toll-Like Receptors - metabolism | Caspases - chemistry | Mycobacterium tuberculosis - metabolism | Genes, Reporter | RNA - metabolism | Protein Structure, Tertiary | Cell Line | Promoter Regions, Genetic | Cytokines - metabolism | Enzyme-Linked Immunosorbent Assay | Signal Transduction | Nuclear Pore Complex Proteins - metabolism | TNF Receptor-Associated Factor 2 - metabolism | Inflammation | Cytoskeletal Proteins - chemistry | Myeloid Differentiation Factor 88 | Reverse Transcriptase Polymerase Chain Reaction | Plasmids - metabolism | Pyrin | Amino Acid Motifs | Transcription Factor RelA - metabolism | TNF Receptor-Associated Factor 6 - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Intracellular Signaling Peptides and Proteins - physiology | RNA-Binding Proteins - metabolism | Receptors, Immunologic - metabolism | RNA, Small Interfering - metabolism | Index Medicus
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4. Full Text Caseation of human tuberculosis granulomas correlates with elevated host lipid metabolism
by Kim, Mi‐Jeong and Wainwright, Helen C and Locketz, Michael and Bekker, Linda‐Gail and Walther, Gabriele B and Dittrich, Corneli and Visser, Annalie and Wang, Wei and Hsu, Fong‐Fu and Wiehart, Ursula and Tsenova, Liana and Kaplan, Gilla and Russell, David G
EMBO molecular medicine, ISSN 1757-4676, 07/2010, Volume 2, Issue 7, pp. 258 - 274
Mycobacterium | foamy macrophage | granuloma | tuberculosis | Granuloma | Tuberculosis | Foamy macrophage | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Cholesterol Esters - metabolism | Granuloma - metabolism | Lung Diseases - metabolism | Lung Diseases - microbiology | Humans | Tuberculosis - complications | Gene Regulatory Networks | Antigens, CD - metabolism | Coenzyme A Ligases - metabolism | Necrosis | Saposins - metabolism | Peptides - metabolism | Caseins | Tuberculosis - metabolism | Granuloma - microbiology | Granuloma - genetics | Lactosylceramides - metabolism | Lipid Metabolism | Cord Factors - toxicity | Cholesterol - metabolism | Triglycerides - metabolism | Membrane Proteins | Lung Diseases - genetics | Macrophages - metabolism | Animals | Tuberculosis - genetics | Mice | Perilipin-2 | Bacilli | Biochemical analysis | Disease | Trehalose | Cell walls | Esters | Lipids | Infections | Genomes | Gene expression | Metabolism | Macrophages | Cholesterol | Pathology | Disease transmission | Software | Lipid metabolism | Polyclonal antibodies | Index Medicus
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5. Full Text Mycobacteria target DC-SIGN to suppress dendritic cell function
by Geijtenbeek, Teunis B. H and van Vliet, Sana J and Koppel, Estella A and Sanchez-Hernandez, Marta and Vandenbroucke-Grauls, Christine M. J. E and Appelmelk, Ben and van Kooyk, Yvette
The Journal of experimental medicine, ISSN 0022-1007, 2003, Volume 197, Issue 1, pp. 7 - 17
Toll-like receptors | ManLAM | Immunosuppression | Mycobacterium tuberculosis | DC-SIGN | Immunology | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Cell Adhesion Molecules - chemistry | Membrane Glycoproteins - metabolism | Dendritic Cells - immunology | Humans | Lipopolysaccharides - metabolism | Lectins, C-Type - chemistry | Lectins, C-Type - metabolism | Toll-Like Receptors | Endocytosis | Lysosomes - metabolism | Cell Division | Interleukin-10 - metabolism | Receptors, Cell Surface - chemistry | Binding Sites | Mycobacterium tuberculosis - metabolism | Dendritic Cells - metabolism | Drosophila Proteins | Signal Transduction | Cells, Cultured | Immune Tolerance | Receptors, Cell Surface - metabolism | Glycolipids - metabolism | Cell Adhesion Molecules - metabolism | Bacterial Adhesion | Dendritic Cells - microbiology | Protein Binding | Index Medicus | immunosuppression
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6. Full Text AhR sensing of bacterial pigments regulates antibacterial defence
by Moura-Alves, Pedro and Faé, Kellen and Houthuys, Erica and Dorhoi, Anca and Kreuchwig, Annika and Furkert, Jens and Barison, Nicola and Diehl, Anne and Munder, Antje and Constant, Patricia and Skrahina, Tatsiana and Guhlich-Bornhof, Ute and Klemm, Marion and Koehler, Anne-Britta and Bandermann, Silke and Goosmann, Christian and Mollenkopf, Hans-Joachim and Hurwitz, Robert and Brinkmann, Volker and Fillatreau, Simon and Daffe, Mamadou and Tümmler, Burkhard and Kolbe, Michael and Oschkinat, Hartmut and Krause, Gerd and Kaufmann, Stefan H. E
Nature (London), ISSN 0028-0836, 08/2014, Volume 512, Issue 7515, pp. 387 - 392
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Pseudomonas aeruginosa - immunology | Humans | Mycobacterium tuberculosis - immunology | Pyocyanine - metabolism | Pigments, Biological - metabolism | Receptors, Pattern Recognition - metabolism | Pseudomonas Infections - metabolism | Basic Helix-Loop-Helix Transcription Factors - metabolism | Pseudomonas aeruginosa - metabolism | Receptors, Aryl Hydrocarbon - metabolism | Mycobacterium tuberculosis - metabolism | Cytokines - immunology | Cytokines - metabolism | Bone Marrow Cells - cytology | Anti-Bacterial Agents - metabolism | Virulence Factors - chemistry | Macrophage Activation | Feedback, Physiological | Animals | Phenazines - metabolism | Ligands | Virulence Factors - metabolism | Mice | Mycobacterium tuberculosis - growth & development | Pigments, Biological - chemistry | Pigments | Antimicrobial agents | Bacterial infections | Polycyclic aromatic hydrocarbons | Cell cycle | Index Medicus
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7. Full Text M. tuberculosis-Initiated Human Mannose Receptor Signaling Regulates Macrophage Recognition and Vesicle Trafficking by FcRγ-Chain, Grb2, and SHP-1
by Rajaram, Murugesan V.S and Arnett, Eusondia and Azad, Abul K and Guirado, Evelyn and Ni, Bin and Gerberick, Abigail D and He, Li-Zhen and Keler, Tibor and Thomas, Lawrence J and Lafuse, William P and Schlesinger, Larry S
Cell reports (Cambridge), ISSN 2211-1247, 10/2017, Volume 21, Issue 1, pp. 126 - 140
Mycobacterium | human macrophage | tuberculosis | phagosome | lysosome | mannose receptor | C-type lectin | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Mannose-Binding Lectins - metabolism | Phagosomes - microbiology | Phosphorylation | Humans | Transport Vesicles - microbiology | rac GTP-Binding Proteins - metabolism | cdc42 GTP-Binding Protein - metabolism | Phagocytosis - genetics | Lectins, C-Type - genetics | Receptors, IgG - metabolism | Lectins, C-Type - metabolism | Receptors, IgG - genetics | Lysosomes - metabolism | rac GTP-Binding Proteins - genetics | GRB2 Adaptor Protein - genetics | Mycobacterium tuberculosis - metabolism | Macrophages - microbiology | p21-Activated Kinases - genetics | Membrane Fusion | Signal Transduction | Phagosomes - metabolism | Gene Expression Regulation | Receptors, Cell Surface - metabolism | p21-Activated Kinases - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - genetics | Host-Pathogen Interactions | Macrophages - metabolism | Tyrosine - metabolism | Lysosomes - microbiology | Mannose-Binding Lectins - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism | Transport Vesicles - metabolism | cdc42 GTP-Binding Protein - genetics | Protein Binding | Primary Cell Culture | GRB2 Adaptor Protein - metabolism | Mycobacterium tuberculosis - growth & development | Receptors, Cell Surface - genetics | Index Medicus
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8. Full Text Pyrazinamide Inhibits Trans-Translation in Mycobacterium tuberculosis
by Wanliang Shi and Xuelian Zhang and Xin Jiang and Haiming Yuan and Jong Seok Lee and Clifton E. Barry and Honghai Wang and Wenhong Zhang and Ying Zhang
Science (American Association for the Advancement of Science), ISSN 0036-8075, 9/2011, Volume 333, Issue 6049, pp. 1630 - 1632
Proteins | Tuberculosis | Mycobacterium tuberculosis | REPORTS | Ribosomes | Power of attorney | Amino acids | Bacteria | Geometric lines | Codons | Genetic mutation | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Biological and medical sciences | Medical sciences | General pharmacology | Pharmacology. Drug treatments | Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions | Ribosomal Proteins - chemistry | Bacterial Proteins - chemistry | Drug Resistance, Bacterial | Molecular Sequence Data | Ribosomes - metabolism | RNA, Messenger - metabolism | Mycobacterium tuberculosis - drug effects | Prodrugs - metabolism | Ribosomal Proteins - metabolism | Pyrazinamide - pharmacology | Mycobacterium tuberculosis - metabolism | RNA, Bacterial - metabolism | Pyrazinamide - metabolism | Amidohydrolases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Pyrazinamide - analogs & derivatives | RNA, Transfer - metabolism | Ribosomal Proteins - genetics | Amidohydrolases - genetics | Antitubercular Agents - pharmacology | Bacterial Proteins - genetics | Mutant Proteins - metabolism | Protein Binding | Bacterial Proteins - metabolism | Protein Biosynthesis - drug effects | Mutation | Antitubercular Agents - metabolism | Prodrugs - pharmacology | Mycobacterium tuberculosis - genetics | Physiological aspects | Development and progression | Genetic aspects | Research | Pyrazinamide | Health aspects | Genetic translation | Enzymes | Chemotherapy | Inhibitor drugs | Index Medicus
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