Nucleic Acid Immunity

A Toll-like receptor recognizes bacterial DNA

Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491 · cited 3×

Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3

Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129

CRISPR Provides Acquired Resistance Against Viruses in Prokaryotes

Barrangou, R., Fremaux, C., Deveau, H., Richards, M., Boyaval, P., Moineau, S., Romero, D. A., & Horvath, P. (2007) · Science · doi:10.1126/science.1138140 · Cited by 5,947

The nuclear RNase III Drosha initiates microRNA processing

Lee, Y., Ahn, C., Han, J., Choi, H., Kim, J., Yim, J., Lee, J., Provost, P., Rådmark, O., Kim, S., et al. (2003) · Nature · doi:10.1038/nature01957 · Cited by 5,299

Role for a bidentate ribonuclease in the initiation step of RNA interference

Bernstein, E., Caudy, A. A., Hammond, S. M., & Hannon, G. J. (2001) · Nature · doi:10.1038/35053110 · Cited by 5,018

Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8

Heil, F., Hemmi, H., Hochrein, H., Ampenberger, F., Kirschning, C., Akira, S., Lipford, G., Wagner, H., & Bauer, S. (2004) · Science · doi:10.1126/science.1093620 · Cited by 3,947

CpG motifs in bacterial DNA trigger direct B-cell activation

Krieg, A. M., Yi, A.-K., Matson, S., Waldschmidt, T. J., Bishop, G. A., Teasdale, R., Koretzky, G. A., & Klinman, D. M. (1995) · Nature · doi:10.1038/374546a0 · Cited by 3,508

Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA

Diebold, S. S., Kaisho, T., Hemmi, H., Akira, S., & Reis e Sousa, C. (2004) · Science · doi:10.1126/science.1093616 · Cited by 3,444

RNA interference is mediated by 21- and 22-nucleotide RNAsPreprint

Elbashir, S. M., Lendeckel, W., & Tuschl, T. (2001) · Genes & Development · doi:10.1101/gad.862301 · Cited by 3,354

Suppression of RNA Recognition by Toll-like Receptors: The Impact of Nucleoside Modification and the Evolutionary Origin of RNA

Karikó, K., Buckstein, M., Ni, H., & Weissman, D. (2005) · Immunity · doi:10.1016/j.immuni.2005.06.008 · Cited by 2,728

Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA

Wu, J., Sun, L., Chen, X., Du, F., Shi, H., Chen, C., & Chen, Z. J. (2012) · Science · doi:10.1126/science.1229963 · Cited by 2,628

AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC

Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627

5'-Triphosphate RNA Is the Ligand for RIG-I

Hornung, V., Ellegast, J., Kim, S., Brzózka, K., Jung, A., Kato, H., Poeck, H., Akira, S., Conzelmann, K.-K., Schlee, M., et al. (2006) · Science · doi:10.1126/science.1132505 · Cited by 2,474

A diverse range of gene products are effectors of the type I interferon antiviral response

Schoggins, J. W., Wilson, S. J., Panis, M., Murphy, M. Y., Jones, C. T., Bieniasz, P. D., & Rice, C. M. (2011) · Nature · doi:10.1038/nature09907 · Cited by 2,412

RIG-I-mediated antiviral responses to single-stranded RNA bearing 5’-phosphates

Pichlmair, A., Schulz, O., Tan, C. P., Näslund, T. I., Liljeström, P., Weber, F., & Reis e Sousa, C. (2006) · Science · doi:10.1126/science.1132998 · Cited by 2,210

Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs

Meister, G., Landthaler, M., Patkaniowska, A., Dorsett, Y., Teng, G., & Tuschl, T. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.07.007 · Cited by 2,052

Quantitative Expression of Toll-Like Receptor 1–10 mRNA in Cellular Subsets of Human Peripheral Blood Mononuclear Cells and Sensitivity to CpG Oligodeoxynucleotides

Hornung, V., Rothenfußer, S., Britsch, S., Krug, A., Jahrsdörfer, B., Giese, T., Endres, S., & Hartmann, G. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.9.4531 · Cited by 1,970

AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA

Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831

CGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING.

Ablasser, A., Goldeck, M., Cavlar, T., Deimling, T., Witte, G., Röhl, I., Hopfner, K.-P., Ludwig, J., & Hornung, V. (2013) · Nature · doi:10.1038/nature12306 · Cited by 1,695

Shared and Unique Functions of the DExD/H-Box Helicases RIG-I, MDA5, and LGP2 in Antiviral Innate Immunity

Yoneyama, M., Kikuchi, M., Matsumoto, K., Imaizumi, T., Miyagishi, M., Taira, K., Foy, E. M., Loo, Y., Gale, M., Akira, S., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2851 · Cited by 1,691

Dicer is essential for mouse development

Bernstein, E., Kim, S. Y., Carmell, M. A., Murchison, E. P., Alcorn, H., Li, M. Z., Mills, A. A., Elledge, S. J., Anderson, K. V., & Hannon, G. J. (2003) · Nature Genetics · doi:10.1038/ng1253 · Cited by 1,627

SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx

Laguette, N., Sobhian, B., Casartelli, N., Ringeard, M., Chable-Bessia, C., Ségéral, E., Yatim, A., Emiliani, S., Schwartz, O., & Benkirane, M. (2011) · Nature · doi:10.1038/nature10117 · Cited by 1,511

Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis

Hakkim, A., Fürnrohr, B. G., Amann, K., Laube, B., Abed, U. A., Brinkmann, V., i, M. H., Voll, R. E., & Zychlinsky, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909927107 · Cited by 1,502

Cell Type-Specific Involvement of RIG-I in Antiviral Response

Kato, H., Sato, S., Yoneyama, M., Yamamoto, M., Uematsu, S., Matsui, K., Tsujimura, T., Takeda, K., Fujita, T., Takeuchi, O., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.04.010 · Cited by 1,368

TLR9 signals after translocating from the ER to CpG DNA in the lysosome

Latz, E., Schoenemeyer, A., Visintin, A., Fitzgerald, K. A., Monks, B. G., Knetter, C. F., Lien, E., Nilsen, N. J., Espevik, T., & Golenbock, D. T. (2004) · Nature Immunology · doi:10.1038/ni1028 · Cited by 1,355

Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes

Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schröder, G. F., Fitzgerald, K. A., Wu, H., & Egelman, E. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.008 · Cited by 1,353

Trex1 prevents cell-intrinsic initiation of autoimmunity

Stetson, D. B., Ko, J. S., Heidmann, T., & Medzhitov, R. (2008) · Cell · doi:10.1016/j.cell.2008.06.032 · Cited by 1,280

siRNAs can function as miRNAsPreprint

Doench, J. G., Petersen, C. P., & Sharp, P. A. (2003) · Genes & Development · doi:10.1101/gad.1064703 · Cited by 1,278

Sequence-specific potent induction of IFN-α by short interfering RNA in plasmacytoid dendritic cells through TLR7

Hornung, V., Guenthner‐Biller, M., Bourquin, C., Ablasser, A., Schlee, M., Uematsu, S., Noronha, A. M., Manoharan, M., Akira, S., de Fougerolles, A., et al. (2005) · Nature Medicine · doi:10.1038/nm1191 · Cited by 1,261

Sequence-dependent stimulation of the mammalian innate immune response by synthetic siRNA

Judge, A. D., Sood, V., Shaw, J. R., Fang, D., McClintock, K., & MacLachlan, I. (2005) · Nature Biotechnology · doi:10.1038/nbt1081 · Cited by 1,260

Mitochondrial DNA that escapes from autophagy causes inflammation and heart failure

Oka, T., Hikoso, S., Yamaguchi, O., Taneike, M., Takeda, T., Tamai, T., Oyabu, J., Murakawa, T., Nakayama, H., Nishida, K., et al. (2012) · Nature · doi:10.1038/nature10992 · Cited by 1,201

Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein

Hrecka, K., Hao, C., Gierszewska, M., Swanson, S. K., Kesik-Brodacka, M., Srivastava, S., Florens, L., Washburn, M. P., & Skowronski, J. (2011) · Nature · doi:10.1038/nature10195 · Cited by 1,200 · cited 4×

Identification of microRNAs of the herpesvirus family

Pfeffer, S., Sewer, A., Lagos‐Quintana, M., Sheridan, R., Sander, C., Grässer, F. A., van Dyk, L. F., Ho, C. K., Shuman, S., Chien, M., et al. (2005) · Nature Methods · doi:10.1038/nmeth746 · Cited by 1,178

Cyclic [G(2′,5′)pA(3′,5′)p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase.

Gao, P., Ascano, M., Wu, Y., Barchet, W., Gaffney, B. L., Zillinger, T., Serganov, A. A., Liu, Y., Jones, R. A., Hartmann, G., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.046 · Cited by 1,101

A-to-I editing of coding and non-coding RNAs by ADARs

Nishikura, K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.4 · Cited by 1,041

The cGAS-cGAMP-STING Pathway of Cytosolic DNA Sensing and Signaling

Cai, X., Chiu, Y., & Chen, Z. J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.040 · Cited by 1,017

RNA editing by ADAR1 prevents MDA5 sensing of endogenous dsRNA as nonself

Liddicoat, B., Piskol, R., Chalk, A. M., Ramaswami, G., Higuchi, M., Hartner, J. C., Li, J. B., Seeburg, P. H., & Walkley, C. R. (2015) · Science · doi:10.1126/science.aac7049 · Cited by 977

Mutations in ADAR1 cause Aicardi-Goutières syndrome associated with a type I interferon signature

Rice, G. I., Kasher, P. R., Forte, G. M. A., Mannion, N. M., Greenwood, S. M., Szynkiewicz, M., Dickerson, J. E., Bhaskar, S. S., Zampini, M., Briggs, T. A., et al. (2012) · Nature Genetics · doi:10.1038/ng.2414 · Cited by 923

CRISPR interference: RNA-directed adaptive immunity in bacteria and archaea

Marraffini, L. A., & Sontheimer, E. J. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2749 · Cited by 919

2′-O methylation of the viral mRNA cap evades host restriction by IFIT family members

Daffis, S., Szretter, K. J., Schriewer, J. M., Li, J., Youn, S., Errett, J. S., Lin, T., Schneller, S. W., Züst, R., Dong, H., et al. (2010) · Nature · doi:10.1038/nature09489 · Cited by 910

Mutations in the gene encoding the 3′-5′ DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locus

Crow, Y. J., Hayward, B. E., Parmar, R., Robins, P., Leitch, A., Ali, M., Black, D. N., van Bokhoven, H., Brunner, H. G., Hamel, B. C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1845 · Cited by 906

A Cellular MicroRNA Mediates Antiviral Defense in Human Cells

Lecellier, C., Dunoyer, P., Arar, K., Lehmann‐Che, J., Eyquem, S., Himber, C., Saı̈b, A., & Voinnet, O. (2005) · Science · doi:10.1126/science.1108784 · Cited by 904

RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III–transcribed RNA intermediate

Ablasser, A., Bauernfeind, F. G., Hartmann, G., Latz, E., Fitzgerald, K. A., & Hornung, V. (2009) · Nature Immunology · doi:10.1038/ni.1779 · Cited by 892

HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase

Goldstone, D. C., Ennis-Adeniran, V., Hedden, J. J., Groom, H. C. T., Rice, G., Christodoulou, E., Walker, P. A., Kelly, G. P., Haire, L. F., Yap, M. W., et al. (2011) · Nature · doi:10.1038/nature10623 · Cited by 871

SAMHD1 restricts the replication of human immunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates

Lahouassa, H., Daddacha, W., Hofmann, H., Ayinde, D., Logue, E. C., Dragin, L., Bloch, N., Maudet, C., Bertrand, M., Gramberg, T., et al. (2012) · Nature Immunology · doi:10.1038/ni.2236 · Cited by 852

Ribonuclease H: the enzymes in eukaryotes

Cerritelli, S. M., & Crouch, R. J. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06908.x · Cited by 845

HIN-200 Proteins Regulate Caspase Activation in Response to Foreign Cytoplasmic DNA

Roberts, T. L., Idris, A., Dunn, J. A., Kelly, G., Burnton, C. M., Hodgson, S., Hardy, L., Garceau, V., Sweet, M. J., Ross, I. L., et al. (2009) · Science · doi:10.1126/science.1169841 · Cited by 830

Impact of Protein Kinase PKR in Cell Biology: from Antiviral to Antiproliferative Action

García, M. A., Gil, J., Ventoso, I., Guerra, S., Domingo, E., Rivas, C., & Esteban, M. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00027-06 · Cited by 818

Recognition of 5′ Triphosphate by RIG-I Helicase Requires Short Blunt Double-Stranded RNA as Contained in Panhandle of Negative-Strand Virus

Schlee, M., Roth, A. H. F. J., Hornung, V., Hagmann, C. A., Wimmenauer, V., Barchet, W., Coch, C., Janke, M., Mihailovic, A., Wardle, G. S., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.05.008 · Cited by 814

Features of systemic lupus erythematosus in Dnase1-deficient mice

Napirei, M., Karsunky, H., Zevnik, B., Stephan, H., Mannherz, H. G., & Möröy, T. (2000) · Nature Genetics · doi:10.1038/76032 · Cited by 789

Self-RNA–antimicrobial peptide complexes activate human dendritic cells through TLR7 and TLR8

Ganguly, D., Chamilos, G., Lande, R., Gregorio, J. D., Meller, S., Facchinetti, V., Homey, B., Barrat, F. J., Żal, T., & Gilliet, M. F. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20090480 · Cited by 777

Novel role of PKR in inflammasome activation and HMGB1 release

Lü, B., Nakamura, T., Inouye, K., Li, J., Tang, Y., Lundbäck, P., Valdés‐Ferrer, S. I., Olofsson, P. S., Kalb, T. H., Roth, J., et al. (2012) · Nature · doi:10.1038/nature11290 · Cited by 772

The Functions of MicroRNAs: mRNA Decay and Translational Repression

Iwakawa, H., & Tomari, Y. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.011 · Cited by 764

Unravelling the structural and mechanistic basis of CRISPR–Cas systems

John van der, O. O. S. T., Westra, E. R., Jackson, R. N., & Wiedenheft, B. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3279 · Cited by 740

Structural Basis of Toll-Like Receptor 3 Signaling with Double-Stranded RNA

Liu, L., Botos, I., Wang, Y., Leonard, J. N., Shiloach, J., Segal, D. M., & Davies, D. R. (2008) · Science · doi:10.1126/science.1155406 · Cited by 733

An unwinding activity that covalently modifies its double-stranded RNA substrate

Bass, B., & Weintraub, H. (1988) · Cell · doi:10.1016/0092-8674(88)90253-x · Cited by 730

Mutations in the gene encoding the 3′-5′ DNA exonuclease TREX1 are associated with systemic lupus erythematosus

Lee-Kirsch, M. A., Gong, M., Chowdhury, D., Senenko, L., Engel, K., Lee, Y.-A., de Silva, U., Bailey, S. L., Witte, T., Vyse, T. J., et al. (2007) · Nature Genetics · doi:10.1038/ng2091 · Cited by 730

RNA Interference Directs Innate Immunity Against Viruses in Adult Drosophila

Wang, X.-H., Aliyari, R., Li, W.-X., Li, H.-W., Kim, K., Carthew, R. W., Atkinson, P. W., & Ding, S. (2006) · Science · doi:10.1126/science.1125694 · Cited by 726

Structural Basis for the Activation of Innate Immune Pattern-Recognition Receptor RIG-I by Viral RNA

Kowalinski, E., Lunardi, T., McCarthy, A. A., Louber, J., Brunel, J., Grigorov, B., Gerlier, D., & Cusack, S. (2011) · Cell · doi:10.1016/j.cell.2011.09.039 · Cited by 707

Viral Encounters with 2′,5′-Oligoadenylate Synthetase and RNase L during the Interferon Antiviral Response

Silverman, R. H. (2007) · Journal of Virology · doi:10.1128/jvi.01471-07 · Cited by 689

Mutations involved in Aicardi-Goutières syndrome implicate SAMHD1 as regulator of the innate immune response

Rice, G., Bond, J., Asipu, A., Brunette, R. L., Manfield, I. W., Carr, I., Fuller, J. C., Jackson, R. M., Lamb, T., Briggs, T. A., et al. (2009) · Nature Genetics · doi:10.1038/ng.373 · Cited by 686

Activation of cyclic GMP-AMP synthase by self-DNA causes autoimmune diseases

Gao, D., Li, T., Li, X.-D., Chen, X., Li, Q., Wight‐Carter, M., & Chen, Z. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516465112 · Cited by 685

Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP

Ablasser, A., Schmid-Burgk, J. L., Hemmerling, I., Horvath, G. L., Schmidt, T., Latz, E., & Hornung, V. (2013) · Nature · doi:10.1038/nature12640 · Cited by 682

The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor

Ewald, S. E., Lee, B. L., Lau, L., Wickliffe, K. E., Shi, G., Chapman, H. A., & Barton, G. M. (2008) · Nature · doi:10.1038/nature07405 · Cited by 651

The RNA Helicase Lgp2 Inhibits TLR-Independent Sensing of Viral Replication by Retinoic Acid-Inducible Gene-I

Rothenfußer, S., Goutagny, N., DiPerna, G., Gong, M., Monks, B. G., Schoenemeyer, A., Yamamoto, M., Akira, S., & Fitzgerald, K. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5260 · Cited by 645

Diverse Functions of Restriction-Modification Systems in Addition to Cellular Defense

Vasu, K., & Nagaraja, V. (2013) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00044-12 · Cited by 639

SAMHD1 restricts HIV-1 infection in resting CD4+ T cells

Baldauf, H., Pan, X., Erikson, E., Schmidt, S., Daddacha, W. B., Burggraf, M., Schenková, K., Ambiel, I., Wabnitz, G. H., Gramberg, T., et al. (2012) · Nature Medicine · doi:10.1038/nm.2964 · Cited by 636

CpG DNA: A potent signal for growth, activation, and maturation of human dendritic cells

Hartmann, G., Weiner, G. J., & KRIEG, A. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9305 · Cited by 623

Structure-Function Analysis of STING Activation by c[G(2′,5′)pA(3′,5′)p] and Targeting by Antiviral DMXAA

Gao, P., Ascano, M., Zillinger, T., Wang, W., Dai, P., Serganov, A. A., Gaffney, B. L., Shuman, S., Jones, R. A., Deng, L., et al. (2013) · Cell · doi:10.1016/j.cell.2013.07.023 · Cited by 612

Structures of the HIN Domain:DNA Complexes Reveal Ligand Binding and Activation Mechanisms of the AIM2 Inflammasome and IFI16 Receptor

Jin, T., Perry, A., Jiang, J., Smith, P. T., Curry, J. A., Unterholzner, L., Jiang, Z., Horvath, G. L., Rathinam, V. A. K., Johnstone, R. W., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.014 · Cited by 610

Mechanism and Function of a Newly Identified CpG DNA Motif in Human Primary B Cells

Hartmann, G., & Krieg, A. M. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.2.944 · Cited by 605

The Double-Stranded RNA-Dependent Protein Kinase PKR: Structure and Function

Clemens, M. J., & Elia, A. (1997) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1997.17.503 · Cited by 605

Mutation of DNASE1 in people with systemic lupus erythematosus

Yasutomo, K., Horiuchi, T., Kagami, S., Tsukamoto, H., Hashimura, C., Urushihara, M., & Kuroda, Y. (2001) · Nature Genetics · doi:10.1038/91070 · Cited by 598

Delineation of a CpG Phosphorothioate Oligodeoxynucleotide for Activating Primate Immune Responses In Vitro and In Vivo

Hartmann, G., Weeratna, R. D., Ballas, Z. K., Payette, P., Blackwell, S. E., Suparto, I. H., Rasmussen, W. L., Waldschmidt, M., Sajuthi, D., Purcell, R. H., et al. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.3.1617 · Cited by 587

RIG-I detects viral genomic RNA during negative-strand RNA virus infection

Rehwinkel, J., Tan, C. P., Goubau, D., Schulz, O., Pichlmair, A., Bier, K., Robb, N., Vreede, F., Barclay, W., Fodor, E., et al. (2010) · Cell · doi:10.1016/j.cell.2010.01.020 · Cited by 585

Trex1 Exonuclease Degrades ssDNA to Prevent Chronic Checkpoint Activation and Autoimmune Disease

Yang, Y., Lindahl, T. L., & Barnes, D. E. (2007) · Cell · doi:10.1016/j.cell.2007.10.017 · Cited by 574

Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

Kumar, A., Haque, J., Lacoste, J., Hiscott, J. B., & Williams, B. R. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6288 · Cited by 568

Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates

Goubau, D., Schlee, M., Deddouche, S., Pruijssers, A. J., Zillinger, T., Goldeck, M., Schuberth, C., Van der Veen, A. G., Fujimura, T., Rehwinkel, J., et al. (2014) · Nature · doi:10.1038/nature13590 · Cited by 557

APOBECs and virus restriction

Harris, R. S., & Dudley, J. P. (2015) · Virology · doi:10.1016/j.virol.2015.03.012 · Cited by 551

Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production

Poeck, H., Bscheider, M., Groß, O., Finger, K., Roth, S., Rebsamen, M., Hannesschläger, N., Schlee, M., Rothenfußer, S., Barchet, W., et al. (2009) · Nature Immunology · doi:10.1038/ni.1824 · Cited by 534

STING manifests self DNA-dependent inflammatory disease

Ahn, J., Gutman, D. M., Saijo, S., & Barber, G. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215006109 · Cited by 523

Immune stimulation mediated by autoantigen binding sites within small nuclear RNAs involves Toll-like receptors 7 and 8

Vollmer, J., Tluk, S., Schmitz, C., Hamm, S., Jurk, M., Forsbach, A., Akira, S., Kelly, K. M., Reeves, W. H., Bauer, S., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051696 · Cited by 515

Autoimmunity Initiates in Nonhematopoietic Cells and Progresses via Lymphocytes in an Interferon-Dependent Autoimmune Disease

Gall, A., Treuting, P., Elkon, K. B., Loo, Y.-M., Gale, M., Barber, G. N., & Stetson, D. B. (2012) · Immunity · doi:10.1016/j.immuni.2011.11.018 · Cited by 510

IFIT1 is an antiviral protein that recognizes 5′-triphosphate RNA

Pichlmair, A., Lassnig, C., Eberle, C.-A., Górna, M. W., Baumann, C., Burkard, T. R., Bürckstümmer, T., Stefanovic, A., Krieger, S., Bennett, K. L., et al. (2011) · Nature Immunology · doi:10.1038/ni.2048 · Cited by 506

BREX is a novel phage resistance system widespread in microbial genomes

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