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1. Full Text CGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING
by Ablasser, Andrea and Goldeck, Marion and Cavlar, Taner and Deimling, Tobias and Witte, Gregor and Röhl, Ingo and Hopfner, Karl-Peter and Ludwig, Janos and Hornung, Veit
Nature (London), ISSN 0028-0836, 2013, Volume 498, Issue 7454, pp. 380 - 384
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Cell Line | Biocatalysis | Magnetic Resonance Spectroscopy | Humans | Adenosine Monophosphate - chemistry | Models, Molecular | Animals | Cyclization | Oligoribonucleotides - metabolism | Cyclic GMP - chemistry | HEK293 Cells | Nucleotidyltransferases - genetics | Second Messenger Systems - physiology | Membrane Proteins - metabolism | Mice | Molecular Structure | Nucleotidyltransferases - metabolism | Oligoribonucleotides - chemistry | Oligoribonucleotides - biosynthesis | Enzymes | Autoimmune diseases | Chromatography | Crystal structure | Index Medicus
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2. Full Text Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5 '-diphosphates
by Goubau, Delphine and Schlee, Martin and Deddouche, Safia and Pruijssers, Andrea J and Zillinger, Thomas and Goldeck, Marion and Schuberth, Christine and Van der Veen, Annemarthe G and Fujimura, Tsutomu and Rehwinkel, Jan and Iskarpatyoti, Jason A and Barchet, Winfried and Ludwig, Janos and Dermody, Terence S and Hartmann, Gunther and Reis e Sousa, Caetano
Nature (London), ISSN 0028-0836, 10/2014, Volume 514, Issue 7522, pp. 372 - 375
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | DEAD Box Protein 58 | Reoviridae - genetics | Diphosphates - metabolism | Genome, Viral - genetics | Male | Immunity, Innate | Animals | RNA, Viral - chemistry | RNA, Viral - genetics | Base Pairing | Reoviridae - physiology | Base Sequence | Reoviridae - immunology | Female | Mice | RNA, Viral - metabolism | DEAD-box RNA Helicases - metabolism | Antiviral agents | Synthesis | RNA | Analysis | Research | Health aspects | Pyrophosphates | Phosphates | Immunology | Viruses | Infections | Genomes | Phosphatase | Transfer RNA | Index Medicus
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3. Full Text Cytosolic RNA:DNA hybrids activate the cGAS–STING axis
by Mankan, Arun K and Schmidt, Tobias and Chauhan, Dhruv and Goldeck, Marion and Höning, Klara and Gaidt, Moritz and Kubarenko, Andrew V and Andreeva, Liudmila and Hopfner, Karl‐Peter and Hornung, Veit
The EMBO journal, ISSN 0261-4189, 12/2014, Volume 33, Issue 24, pp. 2937 - 2946
cGAS | STING | RNA:DNA hybrids | innate immunity | pattern recognition receptor | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Nucleotides, Cyclic - metabolism | Cell Line | Nucleic Acid Hybridization | Humans | Viruses - immunology | Monocytes - immunology | DNA - metabolism | RNA - genetics | DNA - genetics | Interferon Type I - metabolism | Protein Binding | Membrane Proteins - metabolism | Nucleotidyltransferases - metabolism | Bites and Stings | RNA - metabolism | Hybridization | Cellular biology | Gene expression | Ribonucleic acid--RNA | Deoxyribonucleic acid--DNA | Immune system | Index Medicus
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4. Full Text Sequence-specific activation of the DNA sensor cGAS by Y-form DNA structures as found in primary HIV-1 cDNA
by Herzner, Anna-Maria and Hagmann, Cristina Amparo and Goldeck, Marion and Wolter, Steven and Kübler, Kirsten and Wittmann, Sabine and Gramberg, Thomas and Andreeva, Liudmila and Hopfner, Karl-Peter and Mertens, Christina and Zillinger, Thomas and Jin, Tengchuan and Xiao, Tsan Sam and Bartok, Eva and Coch, Christoph and Ackermann, Damian and Hornung, Veit and Ludwig, Janos and Barchet, Winfried and Hartmann, Gunther and Schlee, Martin
Nature immunology, ISSN 1529-2908, 09/2015, Volume 16, Issue 10, pp. 1025 - 1033
Life Sciences & Biomedicine | Immunology | Science & Technology | Cell Line | Immunization | Humans | Cells, Cultured | DNA, Complementary - genetics | HIV-1 - genetics | Interferon-alpha - immunology | DNA, Viral - chemistry | DNA, Viral - immunology | HIV-1 - immunology | Animals | HEK293 Cells | Nucleotidyltransferases - genetics | DNA, Complementary - immunology | Mice | DNA, Complementary - chemistry | DNA, Viral - genetics | Genetic aspects | Immune response | Diagnosis | Molecular structure | Observations | HIV infection | Index Medicus
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5. Full Text A Conserved Histidine in the RNA Sensor RIG-I Controls Immune Tolerance to N1-2'O-Methylated Self RNA
by Schuberth-Wagner, Christine and Ludwig, Janos and Bruder, Ann Kristin and Herzner, Anna-Maria and Zillinger, Thomas and Goldeck, Marion and Schmidt, Tobias and Schmid-Burgk, Jonathan L and Kerber, Romy and Wolter, Steven and Stümpel, Jan-Philip and Roth, Andreas and Bartok, Eva and Drosten, Christian and Coch, Christoph and Hornung, Veit and Barchet, Winfried and Kümmerer, Beate M and Hartmann, Gunther and Schlee, Martin
Immunity (Cambridge, Mass.), ISSN 1074-7613, 07/2015, Volume 43, Issue 1, pp. 41 - 51
Virus | 2'O-methyl | MTr1 | Cap | Immune recognition of RNA | RIG-I | Innate immune tolerance mechanism | 5'-triphosphate RNA | MRNA | Protein Structure, Tertiary | Amino Acid Sequence | DEAD Box Protein 58 | Yellow fever virus - enzymology | RNA - immunology | Humans | Cells, Cultured | Methyltransferases - genetics | Histidine - genetics | RNA - chemistry | Enzyme Activation - immunology | RNA - genetics | DEAD-box RNA Helicases - genetics | Animals | RNA Processing, Post-Transcriptional - genetics | Immune Tolerance - genetics | RNA, Viral - immunology | Mice | Enzyme Activation - genetics | Methylation | Yellow fever virus - genetics | Proteins | Viruses | Ligands | RNA polymerase | Fever | Tropical diseases | Index Medicus
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6. Full Text Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I
by Hartmann, Gunther and Wang, Yanli and Goldeck, Marion and Patel, Dinshaw J and Li, Haitao and Tuschl, Thomas and Sheng, Gang and Ludwig, Janos and Schuberth, Christine and Juranek, Stefan and Micura, Ronald and Schlee, Martin
Nature structural & molecular biology, ISSN 1545-9993, 07/2010, Volume 17, Issue 7, pp. 781 - 787
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Protein Structure, Tertiary | Amino Acid Sequence | DEAD Box Protein 58 | RNA Helicases - metabolism | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | RNA Helicases - chemistry | Immunity, Innate | Interferon-Induced Helicase, IFIH1 | DEAD-box RNA Helicases - genetics | Point Mutation | Sequence Alignment | DEAD-box RNA Helicases - immunology | Protein Binding | Protein Conformation | RNA, Double-Stranded - metabolism | DEAD-box RNA Helicases - metabolism | Nucleic Acid Conformation | Binding Sites | DEAD-box RNA Helicases - chemistry | RNA, Double-Stranded - chemistry | Physiological aspects | Cell receptors | Genetic aspects | Immune response | Research | RNA | Proteins | Viruses | Molecular biology | Ribonucleic acid--RNA | Crystal structure | Immune system | Index Medicus
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7. Full Text Antiviral immunity via RIG-I-mediated recognition of RNA bearing 59-diphosphates
by Goubau, Delphine and Schlee, Martin and Deddouche, Safia and Pruijssers, Andrea J and Zillinger, Thomas and Goldeck, Marion and Schuberth, Christine and Van Der Veen, Annemarthe G and Fujimura, Tsutomu and Rehwinkel, Jan and Iskarpatyoti, Jason A and Barchet, Winfried and Ludwig, Janos and Dermody, Terence S and Hartmann, Gunther and Reis E Sousa, Caetano
Nature (London), ISSN 0028-0836, 08/2014, Volume 514, Issue 7522, pp. 372 - 375
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8. Full Text Direct RIG‐I activation in human NK cells induces TRAIL‐dependent cytotoxicity toward autologous melanoma cells
by Daßler‐Plenker, Juliane and Paschen, Annette and Putschli, Bastian and Rattay, Stephanie and Schmitz, Saskia and Goldeck, Marion and Bartok, Eva and Hartmann, Gunther and Coch, Christoph
International journal of cancer, ISSN 0020-7136, 04/2019, Volume 144, Issue 7, pp. 1645 - 1656
RIG‐I | melanoma | TRAIL | innate immunity | natural killer (NK) cells | RIG-I | Life Sciences & Biomedicine | Oncology | Science & Technology | Killer cells | Histocompatibility antigens | Melanoma | HLA histocompatibility antigens | Interferon | Biological response modifiers | Tretinoin | Toxicity | Tumor cells | Cytotoxicity | Ribonucleic acid--RNA | Immunity | White blood cells | Receptors | Cell activation | Transfection | Tumor necrosis factor | Immunotherapy | Ligands | Histocompatibility antigen HLA | TRAIL protein | Natural killer cells | Retinoic acid | Apoptosis | Tumors | Index Medicus
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9. Full Text ATP hydrolysis by the viral RNA sensor RIG-I prevents unintentional recognition of self-RNA
by Lässig, Charlotte and Matheisl, Sarah and Sparrer, Konstantin M. J and Mann, Carina C. de Oliveira and Moldt, Manuela and Patel, Jenish R and Goldeck, Marion and Hartmann, Gunther and García-Sastre, Adolfo and Hornung, Veit and Conzelmann, Karl-Klaus and Beckmann, Roland and Hopfner, Karl-Peter
eLife, ISSN 2050-084X, 11/2015, Volume 4, Issue 2015
Biology | Life Sciences & Biomedicine - Other Topics | Life Sciences & Biomedicine | Science & Technology | Hydrolysis | Cell Line | DEAD Box Protein 58 | Adenosine Triphosphate - metabolism | Humans | Substrate Specificity | RNA, Viral - metabolism | DEAD-box RNA Helicases - metabolism | RNA | Genetic aspects | Health aspects | Adenosine triphosphate | Immune system | Tretinoin | Pathogens | RNA viruses | Double-stranded RNA | Glycerol | Polymerization | Viruses | Translocase | Self | Electron microscopy | Ribonucleic acid--RNA | Medicine | Proteins | Measles | Influenza | Ligands | Interferon | Mutation | Adenosine triphosphatase | Index Medicus
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10. Full Text Correction: ATP hydrolysis by the viral RNA sensor RIG-I prevents unintentional recognition of self-RNA
by Lässig, Charlotte and Matheisl, Sarah and Sparrer, Konstantin Mj and de Oliveira Mann, Carina C and Moldt, Manuela and Patel, Jenish R and Goldeck, Marion and Hartmann, Gunther and García-Sastre, Adolfo and Hornung, Veit and Conzelmann, Karl-Klaus and Beckmann, Roland and Hopfner, Karl-Peter
eLife, ISSN 2050-084X, 03/2016, Volume 5
Ribonucleic acid--RNA
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11. Full Text Paraoxonase 2 is down-regulated by the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxododecanoyl)-L-homoserine lactone and attenuates oxidative stress induced by pyocyanin
by Horke, Sven and Witte, Ines and Altenhöfer, Sebastian and Wilgenbus, Petra and Goldeck, Marion and Förstermann, Ulrich and Xiao, Junhui and Kramer, Gerald L and Haines, Donovan C and Chowdhary, Puneet K and Haley, Robert W and Teiber, John F
Biochemical journal, ISSN 0264-6021, 02/2010, Volume 426, Issue 1, pp. 73 - 83
Paraoxonase (PON) | Pseudomonas aeruginosa | Quorum-sensing | Lactonase | Pyocyanin (PCN) | Virulence | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology
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