Double-Stranded RNA Sensors and Modulators in Innate Immunity

The HCV Life Cycle: In vitro Tissue Culture Systems and Therapeutic Targets

Gerold, G., & Pietschmann, T. (2014) · Digestive Diseases · doi:10.1159/000360830 · Cited by 4,854 · see citing works

Principles of Nucleic Acid Structure

Neidle, S., & Sanderson, M. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-369507-9.x5001-8 · Cited by 4,519 · see citing works

Biogenesis of small RNAs in animals

Kim, V. N., Han, J., & Siomi, M. C. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2632 · Cited by 3,197 · see citing works

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 2,439 · see citing works

Inhibiting DNA Methylation Causes an Interferon Response in Cancer via dsRNA Including Endogenous Retroviruses

Chiappinelli, K. B., Strissel, P. L., Desrichard, A., Li, H., Henke, C., Akman, B., Hein, A., Rote, N. S., Cope, L. M., Snyder, A., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.011 · Cited by 2,022 · see citing works

DNA-Demethylating Agents Target Colorectal Cancer Cells by Inducing Viral Mimicry by Endogenous Transcripts

Roulois, D., Loo Yau, H., Singhania, R., Wang, Y., Danesh, A., Shen, S. Y., Han, H., Liang, G., Jones, P. A., Pugh, T. J., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.056 · Cited by 1,527 · see citing works

Identification of host proteins required for HIV infection through a functional genomic screen

Brass, A. L., Dykxhoorn, D. M., Benita, Y., Yan, N., Engelman, A., Xavier, R. J., Lieberman, J., & Elledge, S. J. (2008) · Science · doi:10.1126/science.1152725 · Cited by 1,449 · see citing works

Structure and Mechanism of Helicases and Nucleic Acid Translocases

Singleton, M. R., Dillingham, M. S., & Wigley, D. B. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052305.115300 · Cited by 1,279 · see citing works

MAVS Forms Functional Prion-like Aggregates to Activate and Propagate Antiviral Innate Immune Response

Hou, F., Sun, L., Zheng, H., Skaug, B. A., Jiang, Q., & Chen, Z. J. (2011) · Cell · doi:10.1016/j.cell.2011.06.041 · Cited by 1,274 · see citing works

Sequence-specific recognition of double helical nucleic acids by proteins.

Seeman, N. C., Rosenberg, J. M., & Rich, A. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.3.804 · Cited by 1,125 · see citing works

Molecular Mechanisms of RNA Interference

Wilson, R. C., & Doudna, J. A. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130404 · Cited by 1,081 · see citing works

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 1,024 · see citing works

Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2

Higuchi, M., Maas, S., Single, F. N., Hartner, J., Rozov, A., Burnashev, N., Feldmeyer, D., Sprengel, R., & Seeburg, P. H. (2000) · Nature · doi:10.1038/35017558 · Cited by 967 · see citing works

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 963 · see citing works

Hhal methyltransferase flips its target base out of the DNA helix

Klimašauskas, S., Kumar, S., Roberts, R. J., & Cheng, X. (1994) · Cell · doi:10.1016/0092-8674(94)90342-5 · Cited by 945 · see citing works

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 · see citing works

Origins of Specificity in Protein-DNA Recognition

Rohs, R., Jin, X., West, S. M., Joshi, R., Honig, B. H., & Mann, R. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-091030 · Cited by 902 · see citing works

RNA-based antiviral immunity

Ding, S. (2010) · Nature reviews. Immunology · doi:10.1038/nri2824 · Cited by 863 · see citing works

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 792 · see citing works

Modulation of microRNA processing and expression through RNA editing by ADAR deaminases

Yang, W., Chendrimada, T. P., Wang, Q., Higuchi, M., Seeburg, P. H., Shiekhattar, R., & Nishikura, K. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1041 · Cited by 787 · see citing works

Redirection of Silencing Targets by Adenosine-to-Inosine Editing of miRNAs

Kawahara, Y., Zinshteyn, B., Sethupathy, P., Iizasa, H., Hatzigeorgiou, A. G., & Nishikura, K. (2007) · Science · doi:10.1126/science.1138050 · Cited by 785 · see citing works

Exosome Transfer from Stromal to Breast Cancer Cells Regulates Therapy Resistance Pathways

Boelens, M., Wu, T. J., Nabet, B., Xu, B.-H., Qiu, Y., Yoon, T., Azzam, D. J., Victor, C. T.-S., Wiemann, B., Ishwaran, H., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.051 · Cited by 768 · see citing works

The role of PACT in the RNA silencing pathway

Lee, Y., Hur, I., Park, S. Y., Kim, Y. K., Suh, M. R., & Kim, V. N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600942 · Cited by 698 · see citing works

LGP2 is a positive regulator of RIG-I– and MDA5-mediated antiviral responses

Satoh, T., Kato, H., Kumagai, Y., Yoneyama, M., Sato, S., Matsushita, K., Tsujimura, T., Fujita, T., Akira, S., & Takeuchi, O. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912986107 · Cited by 697 · see citing works

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 689 · see citing works

The RNA-Editing Enzyme ADAR1 Controls Innate Immune Responses to RNA

Mannion, N., Greenwood, S. M., Young, R., Cox, S. L., Brindle, J., Read, D. F., Nellåker, C., Vesely, C., Ponting, C. P., McLaughlin, P. J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.041 · Cited by 644 · see citing works

Small self-RNA generated by RNase L amplifies antiviral innate immunity

Malathi, K., Dong, B., Gale, M., & Silverman, R. H. (2007) · Nature · doi:10.1038/nature06042 · Cited by 636 · see citing works

Mitochondrial double-stranded RNA triggers antiviral signalling in humans

Dhir, A., Dhir, S., Borowski, L. S., Jimenez, L., Teitell, M., Rötig, A., Crow, Y. J., Rice, G. I., Duffy, D., Tamby, C., et al. (2018) · Nature · doi:10.1038/s41586-018-0363-0 · Cited by 631 · see citing works

Dynamic landscape and regulation of RNA editing in mammals

Tan, M. H., Li, Q., Shanmugam, R., Piskol, R., Kohler, J. N., Young, A. N., Liu, K. I., Zhang, R., Ramaswami, G., Ariyoshi, K., et al. (2017) · Nature · doi:10.1038/nature24041 · Cited by 610 · see citing works

DICER1 deficit induces Alu RNA toxicity in age-related macular degeneration

Kaneko, H., Dridi, S., Tarallo, V., Gelfand, B. D., Fowler, B. J., Cho, W. G., Kleinman, M. E., Ponicsan, S. L., Hauswirth, W. W., Chiodo, V. A., et al. (2011) · Nature · doi:10.1038/nature09830 · Cited by 601 · see citing works

DHX9 suppresses RNA processing defects originating from the Alu invasion of the human genome

Aktaş, T., Ilik, İ., Maticzka, D., Bhardwaj, V., Rodrigues, C. P., Mittler, G., Manke, T., Backofen, R., & Akhtar, A. (2017) · Nature · doi:10.1038/nature21715 · Cited by 594 · see citing works

Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling

Rice, G., Duany, Y. D. T., Jenkinson, E. M., Forte, G. M. A., Anderson, B., Ariaudo, G., Bader‐Meunier, B., Baildam, E. M., Battini, R., Beresford, M. W., et al. (2014) · Nature Genetics · doi:10.1038/ng.2933 · Cited by 593 · see citing works

DICER1 loss and Alu RNA induce age-related macular degeneration via the NLRP3 inflammasome and MyD88

Tarallo, V., Hirano, Y., Gelfand, B. D., Dridi, S., Kerur, N., Kim, Y., Cho, W. G., Kaneko, H., Fowler, B. J., Bogdanovich, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.036 · Cited by 592 · see citing works

Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown

Chung, H., Calis, J. J. A., Wu, X., Sun, T., Yu, Y., Sarbanes, S. L., Dao Thi, V. L., Shilvock, A. R., Hoffmann, H.-H., Rosenberg, B. R., et al. (2018) · Cell · doi:10.1016/j.cell.2017.12.038 · Cited by 538 · see citing works

A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains

Chen, C., Cho, D. C., Wang, Q., Lai, F., Carter, K. C., & Nishikura, K. (2000) · RNA · doi:10.1017/s1355838200000170 · Cited by 525 · see citing works

Isoforms of RNA-Editing Enzyme ADAR1 Independently Control Nucleic Acid Sensor MDA5-Driven Autoimmunity and Multi-organ Development

Pestal, K., Funk, C. C., Snyder, J. M., Price, N. D., Treuting, P. M., & Stetson, D. B. (2015) · Immunity · doi:10.1016/j.immuni.2015.11.001 · Cited by 516 · see citing works

Liver Disintegration in the Mouse Embryo Caused by Deficiency in the RNA-editing Enzyme ADAR1

Hartner, J. C., Schmittwolf, C., Kispert, A., Müller, A. M., Higuchi, M., & Seeburg, P. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311347200 · Cited by 508 · see citing works

ADAR1 is essential for the maintenance of hematopoiesis and suppression of interferon signaling

Hartner, J. C., Walkley, C. R., Lü, J., & Orkin, S. H. (2008) · Nature Immunology · doi:10.1038/ni.1680 · Cited by 493 · see citing works

PACT, a protein activator of the interferon‐induced protein kinase, PKR

Patel, R. C., & Sen, G. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4379 · Cited by 457 · see citing works

Exosome RNA Unshielding Couples Stromal Activation to Pattern Recognition Receptor Signaling in Cancer

Nabet, B. Y., Qiu, Y., Shabason, J. E., Wu, T. J., Yoon, T., Kim, B. C., Benci, J. L., DeMichele, A. M., Tchou, J. C., Marcotrigiano, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.06.031 · Cited by 453 · see citing works

Breaching Self-Tolerance to Alu Duplex RNA Underlies MDA5-Mediated Inflammation

Ahmad, S., Mu, X., Yang, F., Greenwald, E., Park, J. W., Jacob, E., Zhang, C.-Z., & Hur, S. (2018) · Cell · doi:10.1016/j.cell.2017.12.016 · Cited by 449 · see citing works

Structural basis of RNA recognition and activation by innate immune receptor RIG-I

Jiang, F., Ramanathan, A., Miller, M. T., Tang, G., Gale, M., Patel, S. S., & Marcotrigiano, J. (2011) · Nature · doi:10.1038/nature10537 · Cited by 429 · see citing works

The RNA Sensor RIG-I Dually Functions as an Innate Sensor and Direct Antiviral Factor for Hepatitis B Virus

Sato, S., Li, K., Kameyama, T., Hayashi, T., Ishida, Y., Murakami, S., Watanabe, T., Iijima, S., Sakurai, Y., Watashi, K., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.12.016 · Cited by 415 · see citing works

Antiviral RNA Interference in Mammalian Cells

Maillard, P. V., Ciaudo, C., Marchais, A., Li, Y., Jay, F., Ding, S., & Voinnet, O. (2013) · Science · doi:10.1126/science.1241930 · Cited by 409 · see citing works

Ubiquitin-Induced Oligomerization of the RNA Sensors RIG-I and MDA5 Activates Antiviral Innate Immune Response

Jiang, X., Kinch, L. N., Brautigam, C. A., Chen, X., Du, F., Grishin, N. V., & Chen, Z. J. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.022 · Cited by 407 · see citing works

Loss of DExD/H Box RNA Helicase LGP2 Manifests Disparate Antiviral Responses

Venkataraman, T., Valdes, M., Elsby, R., Kakuta, S., Cáceres, G., Saijo, S., Iwakura, Y., & Barber, G. N. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.10.6444 · Cited by 400 · see citing works

Structure of the Human cGAS–DNA Complex Reveals Enhanced Control of Immune Surveillance

Zhou, W., Whiteley, A. T., Mann, C. C. D. O., Morehouse, B. R., Nowak, R. P., Fischer, E. S., Gray, N. S., Mekalanos, J. J., & Kranzusch, P. J. (2018) · Cell · doi:10.1016/j.cell.2018.06.026 · Cited by 380 · see citing works

DDX1, DDX21, and DHX36 Helicases Form a Complex with the Adaptor Molecule TRIF to Sense dsRNA in Dendritic Cells

Zhang, Z., Kim, T., Bao, M., Facchinetti, V., Jung, S. Y., Ghaffari, A. A., Qin, J., Cheng, G., & Liu, Y. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.027 · Cited by 376 · see citing works

Cytosolic Viral Sensor RIG-I Is a 5'-Triphosphate–Dependent Translocase on Double-Stranded RNA

Myong, S., Cui, S., Cornish, P. V., Kirchhofer, A., Gack, M. U., Jung, J. U., Hopfner, K., & Ha, T. (2009) · Science · doi:10.1126/science.1168352 · Cited by 368 · see citing works

Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition

Dey, M., Cao, C., Dar, A. C., Tamura, T., Ozato, K., Sicheri, F., & Dever, T. E. (2005) · Cell · doi:10.1016/j.cell.2005.06.041 · Cited by 366 · see citing works

Nlrp9b inflammasome restricts rotavirus infection in intestinal epithelial cells

Zhu, S., Ding, S., Wang, P., Wei, Z., Pan, W. Q., Palm, N. W., Yang, Y., Yu, H., Li, H., Wang, G., et al. (2017) · Nature · doi:10.1038/nature22967 · Cited by 366 · see citing works

RNA Interference Functions as an Antiviral Immunity Mechanism in Mammals

Li, Y., Lü, J., Han, Y., Fan, X., & Ding, S. (2013) · Science · doi:10.1126/science.1241911 · Cited by 365 · see citing works

NF-κB Activation by Double-Stranded-RNA-Activated Protein Kinase (PKR) Is Mediated through NF-κB-Inducing Kinase and IκB Kinase

Zamanian-Daryoush, M., Mogensen, T. H., DiDonato, J. A., & Williams, B. R. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1278-1290.2000 · Cited by 362 · see citing works

ADAR1 Forms a Complex with Dicer to Promote MicroRNA Processing and RNA-Induced Gene Silencing

Ota, H., Sakurai, M., Gupta, R., Valente, L., Wulff, B., Ariyoshi, K., Iizasa, H., Davuluri, R. V., & Nishikura, K. (2013) · Cell · doi:10.1016/j.cell.2013.03.024 · Cited by 357 · see citing works

Critical Role of an Antiviral Stress Granule Containing RIG-I and PKR in Viral Detection and Innate Immunity

Onomoto, K., Jogi, M., Yoo, J., Narita, R., Morimoto, S., Takemura, A., Sambhara, S. R., Kawaguchi, A., Osari, S., Nagata, K., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043031 · Cited by 351 · see citing works

OAS proteins and cGAS: unifying concepts in sensing and responding to cytosolic nucleic acids

Hornung, V., Hartmann, R., Ablasser, A., & Hopfner, K. (2014) · Nature reviews. Immunology · doi:10.1038/nri3719 · Cited by 341 · see citing works

RIG‐I‐like receptors: cytoplasmic sensors for non‐self RNA

Kato, H., Takahasi, K., & Fujita, T. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01052.x · Cited by 340 · see citing works

Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I

Peisley, A., Wu, B., Xu, H., Chen, Z. J., & Hur, S. (2014) · Nature · doi:10.1038/nature13140 · Cited by 315 · see citing works

Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition

Peisley, A., Lin, C., Wu, B., Orme-Johnson, M., Liu, M., Walz, T., & Hur, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113651108 · Cited by 312 · see citing works

Structure of the double‐stranded RNA‐binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA‐mediated activation

Nanduri, S., Carpick, B. W., Yang, Y., Williams, B. R. G., & Qin, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.18.5458 · Cited by 312 · see citing works

The Oligoadenylate Synthetase Family: An Ancient Protein Family with Multiple Antiviral Activities

Kristiansen, H., Gad, H. H., Eskildsen-Larsen, S., Desprès, P., & Hartmann, R. (2010) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2010.0107 · Cited by 310 · see citing works

Nlrp6 regulates intestinal antiviral innate immunity

Wang, P., Zhu, S., Yang, L., Cui, S., Pan, W., Jackson, R., Zheng, Y., Rongvaux, A., Sun, Q., Yang, G., et al. (2015) · Science · doi:10.1126/science.aab3145 · Cited by 304 · see citing works

Adenosine-to-inosine RNA editing and human disease

Slotkin, W., & Nishikura, K. (2013) · Genome Medicine · doi:10.1186/gm508 · Cited by 298 · see citing works

DDX60, a DEXD/H Box Helicase, Is a Novel Antiviral Factor Promoting RIG-I-Like Receptor-Mediated Signaling

Miyashita, M., Oshiumi, H., Matsumoto, M., & Seya, T. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01368-10 · Cited by 296 · see citing works

Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses

Li, Y., Banerjee, S., Wang, Y., Goldstein, S. A., Dong, B., Gaughan, C., Silverman, R. H., & Weiss, S. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519657113 · Cited by 285 · see citing works

Dicer-TRBP Complex Formation Ensures Accurate Mammalian MicroRNA Biogenesis

Wilson, R. C., Tambe, A., Kidwell, M. A., Noland, C. L., Schneider, C. P., & Doudna, J. A. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.030 · Cited by 280 · see citing works

hiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1

Sugimoto, Y., Vigilante, A., Darbo, É., Zirra, A., Militti, C., D’Ambrogio, A., Luscombe, N. M., & Ule, J. (2015) · Nature · doi:10.1038/nature14280 · Cited by 270 · see citing works

Antiviral Activity of Human OASL Protein Is Mediated by Enhancing Signaling of the RIG-I RNA Sensor

Zhu, J., Zhang, Y., Ghosh, A., Cuevas, R. A., Forero, A., Dhar, J., Ibsen, M. S., Schmid-Burgk, J. L., Schmidt, T., Ganapathiraju, M. K., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.05.007 · Cited by 269 · see citing works

Autoimmune Disorders Associated with Gain of Function of the Intracellular Sensor MDA5

Funabiki, M., Kato, H., Miyachi, Y., Toki, H., Motegi, H., Inoue, M., Minowa, O., Yoshida, A., Deguchi, K., Satō, H., et al. (2014) · Immunity · doi:10.1016/j.immuni.2013.12.014 · Cited by 262 · see citing works

The Innate Immune Sensor LGP2 Activates Antiviral Signaling by Regulating MDA5-RNA Interaction and Filament Assembly

Bruns, A. M., Leser, G. P., Lamb, R. A., & Horvath, C. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.07.003 · Cited by 262 · see citing works

Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity

Chiang, J. J., Sparrer, K. M. J., van Gent, M., Lässig, C., Huang, T., Osterrieder, N., Hopfner, K., & Gack, M. U. (2017) · Nature Immunology · doi:10.1038/s41590-017-0005-y · Cited by 260 · see citing works

RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence

Masliah, G., Barraud, P., & Allain, F. H. ‐. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1119-x · Cited by 259 · see citing works

MDA5 Detects the Double-Stranded RNA Replicative Form in Picornavirus-Infected Cells

Feng, Q., Hato, S. V., Langereis, M. A., Zoll, J., Virgen‐Slane, R., Peisley, A., Hur, S., Semler, B. L., van Rij, R. P., & van Kuppeveld, F. J. M. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.10.005 · Cited by 254 · see citing works

PKR Senses Nuclear and Mitochondrial Signals by Interacting with Endogenous Double-Stranded RNAs

Kim, Y., Park, J., Kim, S., Kim, M. A., Kang, M., Kwak, C. S., Kang, M., Kim, B., Rhee, H., & Kim, V. N. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.029 · Cited by 250 · see citing works

Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I

Wu, B., Peisley, A., Tetrault, D. G., Li, Z., Egelman, E. H., Magor, K. E., Walz, T., Penczek, P. A., & Hur, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.06.010 · Cited by 246 · see citing works

How RIG-I like receptors activate MAVS

Wu, B., & Hur, S. (2015) · Current Opinion in Virology · doi:10.1016/j.coviro.2015.04.004 · Cited by 242 · see citing works

The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove

Štefl, R., Oberstrass, F. C., Hood, J. L., Jourdan, M., Zimmermann, M., Skříšovská, L., Maris, C., Peng, L., Hofr, C., Emeson, R. B., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.026 · Cited by 240 · see citing works

Human TRBP and PACT Directly Interact with Each Other and Associate with Dicer to Facilitate the Production of Small Interfering RNA

Kok, K., Ng, M.-H. J., Ching, Y.-P., & Jin, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611768200 · Cited by 239 · see citing works

Structure of Human DROSHA

Kwon, S. C., Nguyen, T. A., Choi, Y.-G., Jo, M. H., Hohng, S., Kim, V. N., & Woo, J. (2015) · Cell · doi:10.1016/j.cell.2015.12.019 · Cited by 238 · see citing works

RIG-I Forms Signaling-Competent Filaments in an ATP-Dependent, Ubiquitin-Independent Manner

Peisley, A., Wu, B., Yao, H., Walz, T., & Hur, S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.024 · Cited by 236 · see citing works

Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity

Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., & Beal, P. A. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3203 · Cited by 232 · see citing works

Rewriting the transcriptome: adenosine-to-inosine RNA editing by ADARs

Walkley, C. R., & Li, J. B. (2017) · Genome biology · doi:10.1186/s13059-017-1347-3 · Cited by 228 · see citing works

Minor-Groove Recognition of Double-Stranded RNA by the Double-Stranded RNA-Binding Domain from the RNA-Activated Protein Kinase PKR

Bevilacqua, P. C., & Cech, T. R. (1996) · Biochemistry · doi:10.1021/bi9607259 · Cited by 227 · see citing works

5’-triphosphate-dependent activation of PKR by RNAs with short stem-loops

Nallagatla, S. R., Hwang, J., Toroney, R., Zheng, X., Cameron, C. E., & Bevilacqua, P. C. (2007) · Science · doi:10.1126/science.1147347 · Cited by 222 · see citing works

TAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKR.

Park, H., Davies, M. V., Langland, J. O., Chang, H. W., Nam, Y. S., Tartaglia, J., Paoletti, E., Jacobs, B. L., Kaufman, R. J., & Venkatesan, S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4713 · Cited by 219 · see citing works

DEAD-box helicases as integrators of RNA, nucleotide and protein binding

Putnam, A. A., & Jankowsky, E. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.02.002 · Cited by 218 · see citing works

An origin of the immunogenicity of in vitro transcribed RNA

Mu, X., Greenwald, E., Ahmad, S., & Hur, S. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky177 · Cited by 218 · see citing works

RNA editing enzyme adenosine deaminase is a restriction factor for controlling measles virus replication that also is required for embryogenesis

Ward, S. V., George, C. X., Welch, M. J., Liou, L., Hahm, B., Lewicki, H. A., de la Torre, J. C., Samuel, C. E., & Oldstone, M. B. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017241108 · Cited by 216 · see citing works

Mutations in DDX58, which Encodes RIG-I, Cause Atypical Singleton-Merten Syndrome

Jang, M., Kim, E. K., Now, H., Nguyen, N., Kim, W.-J., Yoo, J.-Y., Lee, J., Jeong, Y.-M., Kim, C., Kim, O.-H., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.11.019 · Cited by 216 · see citing works

Cryo-EM Structure of Human Dicer and Its Complexes with a Pre-miRNA Substrate

Liu, Z., Wang, J., Cheng, H., Ke, X., Sun, L., Zhang, Q. C., & Wang, H. (2018) · Cell · doi:10.1016/j.cell.2018.03.080 · Cited by 212 · see citing works

Differential roles of human Dicer-binding proteins TRBP and PACT in small RNA processing

Lee, H., Zhou, K., Smith, A. M., Noland, C. L., & Doudna, J. A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt361 · Cited by 210 · see citing works

Dicer Partner Proteins Tune the Length of Mature miRNAs in Flies and Mammals

Fukunaga, R., Han, B., Hung, J., Xu, J. L., Weng, Z., & Zamore, P. D. (2012) · Cell · doi:10.1016/j.cell.2012.09.027 · Cited by 206 · see citing works

MDA5 cooperatively forms dimers and ATP‐sensitive filaments upon binding double‐stranded RNA

Berke, I. C., & Modis, Y. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.19 · Cited by 205 · see citing works

The DHX33 RNA Helicase Senses Cytosolic RNA and Activates the NLRP3 Inflammasome

Mitoma, H., Hanabuchi, S., Kim, T. I., Bao, M., Zhang, Z., Sugimoto, N., & Liu, Y. (2013) · Immunity · doi:10.1016/j.immuni.2013.07.001 · Cited by 204 · see citing works

Structure and Function of the Protein Kinase R

Sadler, A. J., & Williams, B. R. G. (2007) · Springer eBooks · doi:10.1007/978-3-540-71329-6_13 · Cited by 203 · see citing works

Aicardi-Goutières Syndrome Is Caused by IFIH1 Mutations

Oda, H., Nakagawa, K., Abe, J., Awaya, T., Funabiki, M., Hijikata, A., Nishikomori, R., Funatsuka, M., Ohshima, Y., Sugawara, Y., et al. (2014) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.06.007 · Cited by 203 · see citing works

The human 2′-5′oligoadenylate synthetase family: Unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation

Hovanessian, A. G., & Justesen, J. (2007) · Biochimie · doi:10.1016/j.biochi.2007.02.003 · Cited by 202 · see citing works

The SKIV2L RNA exosome limits activation of the RIG-I-like receptors

Eckard, S. C., Rice, G., Fabre, A., Badens, C., Gray, E. E., Hartley, J., Crow, Y. J., & Stetson, D. B. (2014) · Nature Immunology · doi:10.1038/ni.2948 · Cited by 199 · see citing works

The biology of DHX9 and its potential as a therapeutic target

Lee, T., & Pelletier, J. (2016) · Oncotarget · doi:10.18632/oncotarget.8446 · Cited by 190 · see citing works

Reciprocal Inhibition between Intracellular Antiviral Signaling and the RNAi Machinery in Mammalian Cells

Seo, G. J., Kincaid, R. P., Phanaksri, T., Burke, J. M., Pare, J. M., Cox, J. E., Hsiang, T.-Y., Krug, R. M., & Sullivan, C. S. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.09.002 · Cited by 189 · see citing works

A dynamically tuned double‐stranded RNA binding mechanism for the activation of antiviral kinase PKR

Nanduri, S., Rahman, F., Williams, B. R. G., & Qin, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5567 · Cited by 188 · see citing works

Host- and Strain-Specific Regulation of Influenza Virus Polymerase Activity by Interacting Cellular Proteins

Bortz, E., Westera, L., Maamary, J., Steel, J., Albrecht, R. A., Manicassamy, B., Chase, G. P., Martínez‐Sobrido, L., Schwemmle, M., & García‐Sastre, A. (2011) · mBio · doi:10.1128/mbio.00151-11 · Cited by 187 · see citing works

A Pathogenic Mechanism in Huntington's Disease Involves Small CAG-Repeated RNAs with Neurotoxic Activity

Báñez-Coronel, M., Porta, S., Kagerbauer, B., Mateu-Huertas, E., Pantano, L., Ferrer, I., Guzmán, M., Estivill, X., & Martı́, E. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002481 · Cited by 185 · see citing works

DHX9 Pairs with IPS-1 To Sense Double-Stranded RNA in Myeloid Dendritic Cells

Zhang, Z., Yuan, B., Lu, N., Facchinetti, V., & Liu, Y. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101307 · Cited by 184 · see citing works

Cancer therapies activate RIG-I-like receptor pathway through endogenous non-coding RNAs

Rañoa, D. R. E., Parekh, A. D., Pitroda, S. P., Huang, X., Darga, T. E., Wong, A., Huang, L., Andrade, J., Staley, J. P., Satoh, T., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8420 · Cited by 184 · see citing works

Crystal Structure of the 2′-Specific and Double-Stranded RNA-Activated Interferon-Induced Antiviral Protein 2′-5′-Oligoadenylate Synthetase

Hartmann, R., Justesen, J., Sarkar, S. N., Sen, G. C., & Yee, V. C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00433-7 · Cited by 182 · see citing works

Adenosine Deaminase That Acts on RNA 3 (ADAR3) Binding to Glutamate Receptor Subunit B Pre-mRNA Inhibits RNA Editing in Glioblastoma

Oakes, E. K., Anderson, A., Cohen‐Gadol, A., & Hundley, H. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.779868 · Cited by 181 · see citing works

Structure of Human RNase L Reveals the Basis for Regulated RNA Decay in the IFN Response

Han, Y., Donovan, J., Rath, S. P., Whitney, G., Chitrakar, A., & Korennykh, A. V. (2014) · Science · doi:10.1126/science.1249845 · Cited by 180 · see citing works

Mutual Antagonism between the Ebola Virus VP35 Protein and the RIG-I Activator PACT Determines Infection Outcome

Luthra, P., Ramanan, P., Mire, C. E., Weisend, C. M., Tsuda, Y., Yen, B. C., Liu, G., Leung, D. W., Geisbert, T. W., Ebihara, H., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.010 · Cited by 179 · see citing works

The Double-Stranded RNA-Binding Protein PACT Functions as a Cellular Activator of RIG-I to Facilitate Innate Antiviral Response

Kok, K., Lui, P., Ng, M.-H. J., Siu, K., Au, S. W. N., & Jin, D. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.03.007 · Cited by 176 · see citing works

ADAR editing in double-stranded UTRs and other noncoding RNA sequences

Hundley, H. A., & Bass, B. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.02.008 · Cited by 175 · see citing works

DDX60 Is Involved in RIG-I-Dependent and Independent Antiviral Responses, and Its Function Is Attenuated by Virus-Induced EGFR Activation

Oshiumi, H., Miyashita, M., Okamoto, M., Morioka, Y., Okabe, M., Matsumoto, M., & Seya, T. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.047 · Cited by 172 · see citing works

Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments

Peisley, A., Jo, M. H., Lin, C., Wu, B., Orme-Johnson, M., Walz, T., Hohng, S., & Hur, S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208618109 · Cited by 170 · see citing works

Protein Kinase R Contributes to Immunity against Specific Viruses by Regulating Interferon mRNA Integrity

Schulz, O., Pichlmair, A., Rehwinkel, J., Rogers, N. C., Scheuner, D. L., Kato, H., Takeuchi, O., Akira, S., Kaufman, R. J., & Sousa, C. R. E. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.04.007 · Cited by 170 · see citing works

The RIG-I-like Receptor LGP2 Recognizes the Termini of Double-stranded RNA

Li, X., Ranjith-Kumar, C. T., Brooks, M. T., Dharmaiah, S., Herr, A. B., Kao, C. C., & Li, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900818200 · Cited by 167 · see citing works

Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1

Donovan, J., Dufner, M., & Korennykh, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218528110 · Cited by 163 · see citing works

A Left-Handed RNA Double Helix Bound by the Zα Domain of the RNA-Editing Enzyme ADAR1

Plácido, D., Brown, B. A., Lowenhaupt, K., Rich, A., & Athanasiadis, A. (2007) · Structure · doi:10.1016/j.str.2007.03.001 · Cited by 157 · see citing works

Structural Foundations of RNA Silencing by Argonaute

Sheu‐Gruttadauria, J., & MacRae, I. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.018 · Cited by 157 · see citing works

Ribonuclease L mediates the cell-lethal phenotype of double-stranded RNA editing enzyme ADAR1 deficiency in a human cell line

Li, Y., Banerjee, S., Goldstein, S. A., Dong, B., Gaughan, C., Rath, S. P., Donovan, J., Korennykh, A. V., Silverman, R. H., & Weiss, S. R. (2017) · eLife · doi:10.7554/elife.25687 · Cited by 156 · see citing works

Induction and suppression of antiviral RNA interference by influenza A virus in mammalian cells

Li, Y., Basavappa, M. G., Lü, J., Dong, S., Cronkite, D. A., Prior, J. T., Reinecker, H., Hertzog, P. J., Han, Y., Li, W.-X., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.250 · Cited by 155 · see citing works

Multiple sensors ensure guide strand selection in human RNAi pathways

Noland, C. L., & Doudna, J. A. (2013) · RNA · doi:10.1261/rna.037424.112 · Cited by 144 · see citing works

Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5

Uchikawa, E., Lethier, M., Malet, H., Brunel, J., Gerlier, D., & Cusack, S. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.021 · Cited by 143 · see citing works

Protein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon response

Pfaller, C. K., Li, Z., George, C. X., & Samuel, C. E. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2011.08.009 · Cited by 140 · see citing works

OASL1 inhibits translation of the type I interferon–regulating transcription factor IRF7

Lee, M. S., Kim, B., Oh, G. T., & Kim, Y.-J. (2013) · Nature Immunology · doi:10.1038/ni.2535 · Cited by 139 · see citing works

A Phosphate-Binding Pocket within the Platform-PAZ-Connector Helix Cassette of Human Dicer

Tian, Y., Simanshu, D. K., Ma, J., Park, J., Heo, I., Kim, V. N., & Patel, D. J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.01.003 · Cited by 139 · see citing works

Influenza Virus Adaptation PB2-627K Modulates Nucleocapsid Inhibition by the Pathogen Sensor RIG-I

Weber, M., Sediri, H., Felgenhauer, U., Binzen, I., Bänfer, S., Jacob, R., Brunotte, L., García‐Sastre, A., Schmid-Burgk, J. L., Schmidt, T., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.01.005 · Cited by 137 · see citing works

RNase L releases a small RNA from HCV RNA that refolds into a potent PAMP

Malathi, K., Saito, T., Crochet, N., Barton, D. J., Gale, M., & Silverman, R. H. (2010) · RNA · doi:10.1261/rna.2244210 · Cited by 136 · see citing works

The RIG‐I‐like receptor LGP2 inhibits Dicer‐dependent processing of long double‐stranded RNA and blocks RNA interference in mammalian cells

van der Veen, A. G., Maillard, P. V., Schmidt, J. M., Lee, S. A., Deddouche, S., Borg, A., Kjær, S., Snijders, A. P., & Sousa, C. R. E. (2018) · The EMBO Journal · doi:10.15252/embj.201797479 · Cited by 135 · see citing works

STAU1 binding 3′ UTR IRAlus complements nuclear retention to protect cells from PKR-mediated translational shutdownPreprint

Elbarbary, R. A., Li, W., Tian, B., & Maquat, L. E. (2013) · Genes & Development · doi:10.1101/gad.220962.113 · Cited by 134 · see citing works

ATPase‐driven oligomerization of RIG‐I on RNA allows optimal activation of type‐I interferon

Patel, J. R., Jain, A., Chou, Y., Baum, A., Ha, T., & García‐Sastre, A. (2013) · EMBO Reports · doi:10.1038/embor.2013.102 · Cited by 134 · see citing works

PKR is activated by cellular dsRNAs during mitosis and acts as a mitotic regulatorPreprint

Kim, Y., Lee, J. H., Park, J., Cho, J., Yi, H., & Kim, V. N. (2014) · Genes & Development · doi:10.1101/gad.242644.114 · Cited by 133 · see citing works

HIV-1 blocks the signaling adaptor MAVS to evade antiviral host defense after sensing of abortive HIV-1 RNA by the host helicase DDX3

Gringhuis, S. I., Hertoghs, N., Kaptein, T. M., Willems, E., Sarrami‐Forooshani, R., Sprokholt, J. K., van Teijlingen, N. H., Kootstra, N. A., Booiman, T., van Dort, K. A., et al. (2016) · Nature Immunology · doi:10.1038/ni.3647 · Cited by 133 · see citing works

TRBP Control of PACT-Induced Phosphorylation of Protein Kinase R Is Reversed by Stress

Daher, A., Laraki, G., Singh, M., Melendez-Peña, C. E., Bannwarth, S., Peters, A. H. F. M., MEURS, E. F., Braun, R. E., Patel, R. C., & Gatignol, A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01030-08 · Cited by 131 · see citing works

Staufen1 senses overall transcript secondary structure to regulate translation

Ricci, E. P., Küçükural, A., Cenik, C., Mercier, B. C., Singh, G., Heyer, E. E., Ashar-Patel, A., Peng, L., & Moore, M. J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2739 · Cited by 130 · see citing works

Brief Report: IFIH1 Mutation Causes Systemic Lupus Erythematosus With Selective IgA Deficiency

Eyck, L. V., Somer, L. D., Pombal, D., Bornschein, S., Frans, G., Humblet‐Baron, S., Moens, L., de Zegher, F., Bossuyt, X., Wouters, C. H., et al. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39110 · Cited by 129 · see citing works

The TIA1 RNA-Binding Protein Family Regulates EIF2AK2-Mediated Stress Response and Cell Cycle Progression

Meyer, C., Garzia, A., Mazzola, M. C., Gerstberger, S. C., Molina, H., & Tuschl, T. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.011 · Cited by 129 · see citing works

Stem-Loop Recognition by DDX17 Facilitates miRNA Processing and Antiviral Defense

Moy, R. H., Cole, B. S., Yasunaga, A., Gold, B., Shankarling, G. S., Varble, A., Molleston, J. M., tenOever, B. R., Lynch, K. W., & Cherry, S. R. (2014) · Cell · doi:10.1016/j.cell.2014.06.023 · Cited by 125 · see citing works

Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions

Laraki, G., Clerzius, G., Daher, A., Melendez-Peña, C. E., Daniels, S. M., & Gatignol, A. (2008) · RNA Biology · doi:10.4161/rna.5.2.6069 · Cited by 118 · see citing works

p59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human gene related to the 2'-5' oligoadenylate synthetase family

Hartmann, R. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.18.4121 · Cited by 116 · see citing works

Dicer uses distinct modules for recognizing dsRNA termini

Sinha, N. K., Iwasa, J., Shen, P. S., & Bass, B. (2017) · Science · doi:10.1126/science.aaq0921 · Cited by 115 · see citing works

Potential role for snoRNAs in PKR activation during metabolic stress

Youssef, O. A., Safran, S. A., Nakamura, T., Nix, D. A., Hotamışlıgil, G. S., & Bass, B. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424044112 · Cited by 113 · see citing works

PKR Transduces MDA5-Dependent Signals for Type I IFN Induction

Pham, A. M., Maria, F. G. S., Lahiri, T., Friedman, E., Marié, I. J., & Levy, D. E. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005489 · Cited by 111 · see citing works

Structure of Dicer and Mechanistic Implications for RNAiPreprint

MacRae, I. J., Li, F., Zhou, K., Cande, W. Z., & Doudna, J. A. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.042 · Cited by 109 · see citing works

Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR

Dar, A., Dever, T., & Sicheri, F. (2005) · Cell · doi:10.1016/j.cell.2005.06.044 · Cited by 107 · see citing works

MDA5 Localizes to Stress Granules, but This Localization Is Not Required for the Induction of Type I Interferon

Langereis, M. A., Feng, Q., & van Kuppeveld, F. J. M. (2013) · Journal of Virology · doi:10.1128/jvi.03213-12 · Cited by 107 · see citing works

Swiss army knives: non-canonical functions of nuclear Drosha and Dicer

Burger, K., & Gullerová, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3994 · Cited by 99 · see citing works

Visualisation of direct interaction of MDA5 and the dsRNA replicative intermediate form of positive strand RNA viruses

Triantafilou, K., Vakakis, E., Kar, S., Richer, E., Evans, G. L., & Triantafilou, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.103887 · Cited by 99 · see citing works

LGP2 Plays a Critical Role in Sensitizing mda-5 to Activation by Double-Stranded RNA

Childs, K., Randall, R. E., & Goodbourn, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064202 · Cited by 96 · see citing works

ATP Hydrolysis Enhances RNA Recognition and Antiviral Signal Transduction by the Innate Immune Sensor, Laboratory of Genetics and Physiology 2 (LGP2)

Bruns, A. M., Pollpeter, D., Hadizadeh, N., Myong, S., Marko, J. F., & Horvath, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424416 · Cited by 95 · see citing works

Protein Kinase PKR Amplification of Interferon β Induction Occurs through Initiation Factor eIF-2α-mediated Translational Control

McAllister, C. S., Taghavi, N., & Samuel, C. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390039 · Cited by 90 · see citing works

The 2′-5′-Oligoadenylate Synthetase 3 Enzyme Potently Synthesizes the 2′-5′-Oligoadenylates Required for RNase L Activation

Ibsen, M. S., Gad, H. H., Thavachelvam, K., Boesen, T. P., Desprès, P., & Hartmann, R. (2014) · Journal of Virology · doi:10.1128/jvi.01763-14 · Cited by 88 · see citing works

The Nature of the Catalytic Domain of 2′-5′-Oligoadenylate Synthetases

Sarkar, S. N., Ghosh, A., Wang, H.-W., Sung, S., & Sen, G. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25535 · Cited by 87 · see citing works

Activation of 2′-5′ Oligoadenylate Synthetase by Single-stranded and Double-stranded RNA Aptamers

Hartmann, R., Nørby, P. L., Martensen, P. M., Jørgensen, P., James, M. C., Jacobsen, C. B., Moestrup, S. K., Clemens, M. J., & Justesen, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3236 · Cited by 87 · see citing works

Unusual cutaneous features associated with a heterozygous gain-of-function mutation inIFIH1: overlap between Aicardi-Goutières and Singleton-Merten syndromes

Bursztejn, A. ‐., Briggs, T. A., Duany, Y. D. T., Anderson, B., O’Sullivan, J., Williams, S. G., Bodemer, C., Fraitag, S., Gebhard, F. T., Leheup, B., et al. (2015) · British Journal of Dermatology · doi:10.1111/bjd.14073 · Cited by 86 · see citing works

Structural mechanism of sensing long dsRNA via a noncatalytic domain in human oligoadenylate synthetase 3

Donovan, J., Whitney, G., Rath, S. P., & Korennykh, A. V. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419409112 · Cited by 85 · see citing works

RIG-I Uses an ATPase-Powered Translocation-Throttling Mechanism for Kinetic Proofreading of RNAs and Oligomerization

Devarkar, S. C., Schweibenz, B., Wang, C., Marcotrigiano, J., & Patel, S. S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.021 · Cited by 84 · see citing works

Leader-Containing Uncapped Viral Transcript Activates RIG-I in Antiviral Stress Granules

Oh, S.-W., Onomoto, K., Wakimoto, M., Onoguchi, K., Ishidate, F., Fujiwara, T. K., Yoneyama, M., Kato, H., & Fujita, T. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005444 · Cited by 83 · see citing works

ATP-Dependent Effector-like Functions of RIG-I-like Receptors

Yao, H., Dittmann, M., Peisley, A., Hoffmann, H.-H., Gilmore, R. H., Schmidt, T., Schmid-Burgk, J. L., Hornung, V., Rice, C. M., & Hur, S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.03.014 · Cited by 78 · see citing works

Visualizing the Determinants of Viral RNA Recognition by Innate Immune Sensor RIG-I

Luo, D., Kohlway, A. S., Vela, A., & Pyle, A. M. (2012) · Structure · doi:10.1016/j.str.2012.08.029 · Cited by 78 · see citing works

RNA Dimerization Promotes PKR Dimerization and Activation

Heinicke, L. A., Wong, C. J., Lary, J. W., Nallagatla, S. R., Diegelman‐Parente, A., Zheng, X., Cole, J. L., & Bevilacqua, P. C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.005 · Cited by 78 · see citing works

Duplex RNA activated ATPases (DRAs)

Luo, D., Kohlway, A. S., & Pyle, A. M. (2012) · RNA Biology · doi:10.4161/rna.22706 · Cited by 77 · see citing works

In Vivo RNAi Screening Identifies MDA5 as a Significant Contributor to the Cellular Defense against Influenza A Virus

Benitez, A. A., Panis, M., Xue, J., Varble, A., Shim, J. V., Frick, A. L., López, C. B., Sachs, D. M., & tenOever, B. R. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.032 · Cited by 76 · see citing works

Structural and functional analysis reveals that human OASL binds dsRNA to enhance RIG-I signaling

Ibsen, M. S., Gad, H. H., Andersen, L. L., Hornung, V., Julkunen, I., Sarkar, S. N., & Hartmann, R. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv389 · Cited by 76 · see citing works

Protein synthesis inhibition and GADD34 control IFN‐β heterogeneous expression in response to dsRNA

Dalet, A., Argüello, R. J., Combes, A. J., Spinelli, L., Jaeger, S., Fallet, M., Manh, T. V., Mendes, A. V., Perego, J., Reverendo, M., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695000 · Cited by 74 · see citing works

The PKR activator, PACT, becomes a PKR inhibitor during HIV-1 replication

Clerzius, G., Shaw, E., Daher, A., Burugu, S., Gélinas, J., Ear, T., Sinck, L., Routy, J., Mouland, A. J., Patel, R. C., et al. (2013) · Retrovirology · doi:10.1186/1742-4690-10-96 · Cited by 73 · see citing works

The hierarchical structural architecture of inflammasomes, supramolecular inflammatory machines

Hauenstein, A. V., Zhang, L., & Wu, H. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.03.014 · Cited by 72 · see citing works

The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain

Marques, J. T., Anwar, J., Eskildsen-Larsen, S., Rebouillat, D., Paludan, S. R., Sen, G. C., Williams, B. R. G., & Hartmann, R. (2008) · Journal of General Virology · doi:10.1099/vir.0.2008/003558-0 · Cited by 70 · see citing works

An RNA Editor, Adenosine Deaminase Acting on Double-Stranded RNA (ADAR1)

George, C. X., John, L., & Samuel, C. E. (2014) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2014.0001 · Cited by 69 · see citing works

Discriminating Self and Non-Self by RNA: Roles for RNA Structure, Misfolding, and Modification in Regulating the Innate Immune Sensor PKR

Hull, C. M., & Bevilacqua, P. C. (2016) · Accounts of Chemical Research · doi:10.1021/acs.accounts.6b00151 · Cited by 69 · see citing works

RNase III nucleases from diverse kingdoms serve as antiviral effectors

Aguado, L. C., Schmid, S., May, J. P., Sabin, L. R., Panis, M., Blanco-Melo, D., Shim, J. V., Sachs, D. M., Cherry, S. R., Simon, A. E., et al. (2017) · Nature · doi:10.1038/nature22990 · Cited by 67 · see citing works

Mechanism of Interaction of the Double-Stranded RNA (dsRNA) Binding Domain of Protein Kinase R with Short dsRNA Sequences

Ucci, J. W., Kobayashi, Y., Choi, G., Alexandrescu, A. T., & Cole, J. L. (2006) · Biochemistry · doi:10.1021/bi061531o · Cited by 66 · see citing works

Stress-Induced Phosphorylation of PACT Reduces Its Interaction with TRBP and Leads to PKR Activation

Singh, M., Castillo‐Azofeifa, D., Patel, C. V., & Patel, R. C. (2011) · Biochemistry · doi:10.1021/bi200104h · Cited by 65 · see citing works

Activation of the IκBα kinase (IKK) complex by double-stranded RNA-binding defective and catalytic inactive mutants of the interferon-inducible protein kinase PKR

Ishii, T. M., Kwon, H., Hiscott, J. B., Mosialos, G., & Koromilas, A. E. (2001) · Oncogene · doi:10.1038/sj.onc.1204267 · Cited by 65 · see citing works

Activation of Protein Kinase PKR Requires Dimerization-induced cis-Phosphorylation within the Activation Loop

Dey, M., Mann, B. R., Anshu, A., & Mannan, M. A.-U. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.527796 · Cited by 64 · see citing works

Establishing the role of ATP for the function of the RIG-I innate immune sensor

Rawling, D., Fitzgerald, M. E., & Pyle, A. M. (2015) · eLife · doi:10.7554/elife.09391 · Cited by 63 · see citing works

‘Black sheep’ that don’t leave the double-stranded RNA-binding domain fold

Gleghorn, M. L., & Maquat, L. E. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.05.003 · Cited by 63 · see citing works

The interaction between the helicase DHX33 and IPS-1 as a novel pathway to sense double-stranded RNA and RNA viruses in myeloid dendritic cells

Liu, Y., Lu, N., Yuan, B., Weng, L., Wang, F., Liu, Y.-J., & Zhang, Z. (2013) · Cellular and Molecular Immunology · doi:10.1038/cmi.2013.40 · Cited by 61 · see citing works

How do ADARs bind RNA? New protein‐RNA structures illuminate substrate recognition by the RNA editing ADARs

Thomas, J. M., & Beal, P. A. (2017) · BioEssays · doi:10.1002/bies.201600187 · Cited by 61 · see citing works

DDX58 and Classic Singleton-Merten Syndrome

Ferreira, C. R., Crow, Y. J., Gahl, W. A., Gardner, P. J., Goldbach‐Mansky, R. T., Hur, S., de Jesus, A. A., Nehrebecky, M. E., Park, J. W., & Briggs, T. A. (2018) · Journal of Clinical Immunology · doi:10.1007/s10875-018-0572-1 · Cited by 61 · see citing works

Altered Activation of Protein Kinase PKR and Enhanced Apoptosis in Dystonia Cells Carrying a Mutation in PKR Activator Protein PACT

Vaughn, L. S., Bragg, D. C., Sharma, N., Camargos, S., Cardoso, F., & Patel, R. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.669408 · Cited by 60 · see citing works

Emerging roles of DROSHA beyond primary microRNA processing

Lee, D., & Shin, C. (2017) · RNA Biology · doi:10.1080/15476286.2017.1405210 · Cited by 60 · see citing works

Helicase proteins DHX29 and RIG-I cosense cytosolic nucleic acids in the human airway system

Sugimoto, N., Mitoma, H., Kim, T. I., Hanabuchi, S., & Liu, Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400139111 · Cited by 59 · see citing works

Detection of double-stranded RNA-protein interactions by methylene blue-mediated photo-crosslinking.

Liu, Z. R., Wilkie, A. M., Clemens, M. J., & Smith, C. W. J. (1996) · PubMed Central · Cited by 59 · see citing works

The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/MDA5 activation

Ding, Z., Fang, L., Yuan, S., Zhao, L., Wang, X., Long, S., Wang, M., Wang, D., Foda, M. F., & Xiao, S. (2017) · Oncotarget · doi:10.18632/oncotarget.17912 · Cited by 58 · see citing works

Molecular Framework for the Activation of RNA-dependent Protein Kinase

McKenna, S. A., Lindhout, D. A., Kim, I., Liu, C. W., Gelev, V., Wagner, G., & Puglisi, J. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700301200 · Cited by 57 · see citing works

Filament assemblies in foreign nucleic acid sensors

Sohn, J., & Hur, S. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.01.011 · Cited by 54 · see citing works

Increased interaction between PACT molecules in response to stress signals is required for PKR activation

Singh, M., & Patel, R. C. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24152 · Cited by 53 · see citing works

Specific Recognition of HIV TAR RNA by the dsRNA Binding Domains (dsRBD1–dsRBD2) of PKR

Kim, I., Liu, C. W., & Puglisi, J. D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.099 · Cited by 53 · see citing works

DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-ordinate assembly of signalling complexes downstream from MAVS

Gu, L., Fullam, A., McCormack, N., Höhn, Y., & Schröder, M. (2016) · Biochemical Journal · doi:10.1042/bcj20160956 · Cited by 53 · see citing works

PACT- and RIG-I-Dependent Activation of Type I Interferon Production by a Defective Interfering RNA Derived from Measles Virus Vaccine

Ho, T., Kew, C., Lui, P., Chan, C., Satoh, T., Akira, S., Jin, D., & Kok, K. (2015) · Journal of Virology · doi:10.1128/jvi.02161-15 · Cited by 52 · see citing works

PACT Facilitates RNA-Induced Activation of MDA5 by Promoting MDA5 Oligomerization

Lui, P., Wong, L.-Y. R., Ho, T., Au, S. W. N., Chan, C., Kok, K., & Jin, D. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601493 · Cited by 52 · see citing works

Analysis of High-Affinity Binding of Protein Kinase R to Double-Stranded RNA

Husain, B., Mukerji, I., & Cole, J. L. (2012) · Biochemistry · doi:10.1021/bi301226h · Cited by 51 · see citing works

LGP2 virus sensor regulates gene expression network mediated by TRBP-bound microRNAs

Takahashi, T., Nakano, Y., Onomoto, K., Murakami, F., Komori, C., Suzuki, Y., Yoneyama, M., & Ui‐Tei, K. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky575 · Cited by 51 · see citing works

Dissecting the roles of TRBP and PACT in double‐stranded RNA recognition and processing of noncoding RNAs

Heyam, A., Lagos, D., & Plevin, M. J. (2015) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1272 · Cited by 49 · see citing works

RNA sensor LGP2 inhibits TRAF ubiquitin ligase to negatively regulate innate immune signaling

Parisien, J.-P., Lenoir, J. J., Mandhana, R., Rodriguez, K. R., Qian, K., Bruns, A. M., & Horvath, C. M. (2018) · EMBO Reports · doi:10.15252/embr.201745176 · Cited by 49 · see citing works

Stress-induced TRBP phosphorylation enhances its interaction with PKR to regulate cellular survival

Chukwurah, E., & Patel, R. C. (2018) · Scientific Reports · doi:10.1038/s41598-018-19360-8 · Cited by 46 · see citing works

DHX29 functions as an RNA co-sensor for MDA5-mediated EMCV-specific antiviral immunity

Zhu, Q., Tan, P., Li, Y., Lin, M., Li, C., Mao, J., Cui, J., Zhao, W., Wang, H. Y., & Wang, R. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006886 · Cited by 46 · see citing works

RNase L downmodulation of the RNA-binding protein, HuR, and cellular growth

Al‐Ahmadi, W., Al‐Haj, L., Al-Mohanna, F. A., Silverman, R. H., & Khabar, K. S. A. (2009) · Oncogene · doi:10.1038/onc.2009.16 · Cited by 44 · see citing works

ADAR1 is a novel multi targeted anti-HIV-1 cellular protein

Biswas, N., Wang, T., Ding, M., Tumne, A., Chen, Y., Wang, Q., & Gupta, P. (2011) · Virology · doi:10.1016/j.virol.2011.10.024 · Cited by 39 · see citing works

Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19

Blanco-Melo, D., Nilsson-Payant, B. E., Liu, W.-C., Uhl, S., Hoagland, D., Møller, R., Jordan, T. X., Oishi, K., Panis, M., Sachs, D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.026 · Cited by 4,222 · see citing works

Mitochondrial control of inflammation

Marchi, S., Guilbaud, E., Tait, S. W. G., Yamazaki, T., & Galluzzi, L. (2023) · Nature Reviews Immunology · doi:10.1038/s41577-022-00760-x · Cited by 1,027 · see citing works

Lipid nanoparticles enhance the efficacy of mRNA and protein subunit vaccines by inducing robust T follicular helper cell and humoral responses

Alameh, M.-G., Tombácz, I., Bettini, E., Lederer, K., Ndeupen, S., Sittplangkoon, C., Wilmore, J. R., Gaudette, B. T., Soliman, O. Y., Pine, M., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.11.001 · Cited by 775 · see citing works

Immune response, inflammation, and the clinical spectrum of COVID-19

García, L. F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01441 · Cited by 739 · see citing works

Untitled work

Lee (2019) · doi:10.1038/s12276-019-0299-y · Cited by 635 · see citing works

Algorithm for optimized mRNA design improves stability and immunogenicity

Zhang, H., Zhang, L., Lin, A., Xu, C., Li, Z., Liu, K., Liu, B., Ma, X., Zhao, F., Jiang, H., et al. (2023) · Nature · doi:10.1038/s41586-023-06127-z · Cited by 498 · see citing works

Cellular origins of dsRNA, their recognition and consequences

Chen, Y. G., & Hur, S. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00430-1 · Cited by 430 · see citing works

Toll-Like Receptors (TLRs), NOD-Like Receptors (NLRs), and RIG-I-Like Receptors (RLRs) in Innate Immunity. TLRs, NLRs, and RLRs Ligands as Immunotherapeutic Agents for Hematopoietic Diseases

Wicherska‐Pawłowska, K., Wróbel, T., & Rybka, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413397 · Cited by 412 · see citing works

Impact of mRNA chemistry and manufacturing process on innate immune activation

Nelson, J., Sorensen, E. W., Mintri, S., Rabideau, A. E., Zheng, W., Besin, G., Khatwani, N., Su, S. V., Miracco, E. J., Issa, W. J., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz6893 · Cited by 354 · see citing works

Regulation of cGAS- and RLR-mediated immunity to nucleic acids

Ablasser, A., & Hur, S. (2019) · Nature Immunology · doi:10.1038/s41590-019-0556-1 · Cited by 333 · see citing works

COVID-19 vaccine: A recent update in pipeline vaccines, their design and development strategies

Rawat, K., Kumari, P., & Saha, L. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173751 · Cited by 276 · see citing works

Overcoming Barriers for siRNA Therapeutics: From Bench to Bedside

Sajid, M. I., Moazzam, M., Kato, S., Cho, K. Y., & Tiwari, R. K. (2020) · Pharmaceuticals · doi:10.3390/ph13100294 · Cited by 259 · see citing works

ADAR1 prevents autoinflammation by suppressing spontaneous ZBP1 activation

de Reuver, R., Verdonck, S., Dierick, E., Nemegeer, J., Hessmann, E., Ahmad, S., Jans, M., Blancke, G., Nieuwerburgh, F. V., Botzki, A., et al. (2022) · Nature · doi:10.1038/s41586-022-04974-w · Cited by 246 · see citing works

SARS-CoV-2 induces double-stranded RNA-mediated innate immune responses in respiratory epithelial-derived cells and cardiomyocytes

Li, Y., Renner, D. M., Comar, C. E., Whelan, J. N., Reyes, H. M., Cardenas‐Diaz, F. L., Truitt, R., Tan, L. H., Dong, B., Alysandratos, K., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022643118 · Cited by 246 · see citing works

Theoretical basis for stabilizing messenger RNA through secondary structure design

Wayment-Steele, H. K., Kim, D. S., Choe, C. A., Nicol, J. J., Wellington-Oguri, R., Watkins, A. M., Parra Sperberg, R. A., Huang, P.-S., Participants, E., & Das, R. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab764 · Cited by 197 · see citing works

The immunostimulatory RNA RN7SL1 enables CAR-T cells to enhance autonomous and endogenous immune function

Johnson, L. R., Lee, D. Y., Eacret, J. S., Ye, D., June, C. H., & Minn, A. J. (2021) · Cell · doi:10.1016/j.cell.2021.08.004 · Cited by 189 · see citing works

Factors leading to high morbidity and mortality of COVID ‐19 in patients with type 2 diabetes

Rajpal, A., Rahimi, L., & Ismail‐Beigi, F. (2020) · Journal of Diabetes · doi:10.1111/1753-0407.13085 · Cited by 165 · see citing works

Cytokine Storm: The Primary Determinant for the Pathophysiological Evolution of COVID-19 Deterioration

Chen, R., Lan, Z., Ye, J., Pang, L., Liu, Y., Wu, W., Qin, X., Guo, Y., & Zhang, P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.589095 · Cited by 162 · see citing works

All About the RNA: Interferon-Stimulated Genes That Interfere With Viral RNA Processes

Yang, E. C., & Li, M. M. H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.605024 · Cited by 159 · see citing works

Cellular RNA surveillance in health and disease

Wolin, S. L., & Maquat, L. E. (2019) · Science · doi:10.1126/science.aax2957 · Cited by 157 · see citing works

Immunogenicity of In Vitro -Transcribed RNA

Mu, X. N., & Hur, S. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00521 · Cited by 138 · see citing works

RNA‐based medicine: from molecular mechanisms to therapy

Sparmann, A., & Vogel, J. (2023) · The EMBO Journal · doi:10.15252/embj.2023114760 · Cited by 141 · see citing works

Modular, programmable RNA sensing using ADAR editing in living cells

Kaseniit, K. E., Katz, N., Kolber, N. S., Call, C. C., Wengier, D. L., Cody, W. B., Sattely, E. S., & Gao, X. J. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01493-x · Cited by 128 · see citing works

MyD88 and beyond: a perspective on MyD88-targeted therapeutic approach for modulation of host immunity

Saikh, K. U. (2021) · Immunologic Research · doi:10.1007/s12026-021-09188-2 · Cited by 127 · see citing works

A proposed role for the SARS‐CoV‐2 nucleocapsid protein in the formation and regulation of biomolecular condensates

Cascarina, S. M., & Ross, E. D. (2020) · The FASEB Journal · doi:10.1096/fj.202001351 · Cited by 120 · see citing works

RNA regulation of the antiviral protein 2′‐5′‐oligoadenylate synthetase

Schwartz, S. L., & Conn, G. L. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1534 · Cited by 119 · see citing works

cGLRs are a diverse family of pattern recognition receptors in innate immunity

(2023) · doi:10.1016/j.cell.2023.05.038 · Cited by 117 · see citing works

Neurological Complications Associated with the Blood-Brain Barrier Damage Induced by the Inflammatory Response During SARS-CoV-2 Infection

Alquisiras-Burgos, I., Peralta-Arrieta, I., Alonso-Palomares, L. A., Zacapala-Gómez, A. E., Salmerón-Bárcenas, E. G., & Aguilera, P. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02134-7 · Cited by 115 · see citing works

Cancer metastasis as a non-healing wound

Deyell, M., Garris, C., & Laughney, A. M. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01309-w · Cited by 112 · see citing works

RIG-I-Like Receptor-Mediated Recognition of Viral Genomic RNA of Severe Acute Respiratory Syndrome Coronavirus-2 and Viral Escape From the Host Innate Immune Responses

Kouwaki, T., Nishimura, T., Wang, G., & Oshiumi, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.700926 · Cited by 112 · see citing works

Programmable eukaryotic protein synthesis with RNA sensors by harnessing ADAR

Jiang, K., Koob, J. G., Chen, X. D., Krajeski, R. N., Zhang, Y., Volf, V., Zhou, W., Sgrizzi, S. R., Villiger, L., Gootenberg, J. S., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01534-5 · Cited by 115 · see citing works

Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a noncanonical sensor for RNA virus in dendritic cells

Xing, J., Zhang, A., Du, Y., Fang, M., Minze, L. J., Liu, Y., Li, X. C., & Zhang, Z. (2021) · Nature Communications · doi:10.1038/s41467-021-23003-4 · Cited by 108 · see citing works

Silencing of LINE-1 Retrotransposons is a Selective Dependency of Myeloid Leukemia

Gu, Z., Liu, Y., Zhang, Y., Cao, H., Lyu, J., Wang, X., Wylie, A., Newkirk, S. J., Jones, A. E., Lee, M., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00829-8 · Cited by 98 · see citing works

ADAR1: from basic mechanisms to inhibitors

Rehwinkel, J., & Mehdipour, P. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.06.006 · Cited by 97 · see citing works

The endoplasmic reticulum unfolded protein response – homeostasis, cell death and evolution in virus infections

Prasad, V. R., & Greber, U. F. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab016 · Cited by 93 · see citing works

Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases

Kato, K., Ahmad, S., Zhu, Z., Young, J. M., Mu, X. N., Park, S., Malik, H. S., & Hur, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.047 · Cited by 90 · see citing works

Adenosine Deaminases Acting on RNA (ADARs) and Viral Infections

Pfaller, C. K., George, C. X., & Samuel, C. E. (2021) · Annual Review of Virology · doi:10.1146/annurev-virology-091919-065320 · Cited by 89 · see citing works

The competitive landscape of the dsRNA world

Cottrell, K. A., Andrews, R. J., & Bass, B. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.11.033 · Cited by 87 · see citing works

Flavonoids as Promising Antiviral Agents against SARS-CoV-2 Infection: A Mechanistic Review

Tabari, M. A. K., Iranpanah, A., Bahramsoltani, R., & Rahimi, R. (2021) · Molecules · doi:10.3390/molecules26133900 · Cited by 83 · see citing works

Endogenous Double-Stranded RNA

Sadeq, S., Al-Hashimi, S., Cusack, C. M., & Werner, A. (2021) · Non-Coding RNA · doi:10.3390/ncrna7010015 · Cited by 81 · see citing works

The emerging roles of NOD-like receptors in antiviral innate immune signaling pathways

Zheng, C. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.127 · Cited by 79 · see citing works

Multifaceted roles of mitochondria in wound healing and chronic wound pathogenesis

Hunt, M., Torres, M., Bachar-Wikström, E., & Wikstrom, J. D. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1252318 · Cited by 72 · see citing works

Innate immune responses to RNA: sensing and signaling

Luan, X., Wang, L., Song, G., & Zhou, W. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1287940 · Cited by 79 · see citing works

Pathogenic tau–induced transposable element–derived dsRNA drives neuroinflammation

Ochoa, E., Ramirez, P., Gonzalez, E., De Mange, J., Ray, W. J., Bieniek, K. F., & Frost, B. (2023) · Science Advances · doi:10.1126/sciadv.abq5423 · Cited by 73 · see citing works

Targeted Restriction of Viral Gene Expression and Replication by the ZAP Antiviral System

Ficarelli, M., Neil, S. J. D., & Swanson, C. M. (2021) · Annual Review of Virology · doi:10.1146/annurev-virology-091919-104213 · Cited by 71 · see citing works

SUMOylation in Viral Replication and Antiviral Defense

Fan, Y., Li, X., Zhang, L., Zong, Z., Wang, F., Huang, J., Zeng, L., Zhang, C., Yan, H., Zhang, L., et al. (2022) · Advanced Science · doi:10.1002/advs.202104126 · Cited by 72 · see citing works

Delivery of therapeutic oligonucleotides in nanoscale

Wu, L., Zhou, W., Lin, L., Chen, A., Feng, J. C., Qu, X., Zhang, H., & Yue, J. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.05.038 · Cited by 70 · see citing works

Conservation and similarity of bacterial and eukaryotic innate immunity

Ledvina, H. E., & Whiteley, A. T. (2024) · Nature Reviews Microbiology · doi:10.1038/s41579-024-01017-1 · Cited by 70 · see citing works

SARS-CoV-2 Infection of Airway Epithelial Cells

Ryu, G., & Shin, H. (2021) · Immune Network · doi:10.4110/in.2021.21.e3 · Cited by 68 · see citing works

Novel insights into double-stranded RNA-mediated immunopathology

de Reuver, R., & Maelfait, J. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00940-3 · Cited by 66 · see citing works

TRIM18 is a critical regulator of viral myocarditis and organ inflammation

Fang, M., Zhang, A., Du, Y., Lu, W., Wang, J., Minze, L. J., Cox, T. C., Li, X. C., Xing, J., & Zhang, Z. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00840-z · Cited by 64 · see citing works

DExD/H-box helicases: multifunctional regulators in antiviral innate immunity

Su, C., Tang, Y.-D., & Zheng, C. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04072-6 · Cited by 62 · see citing works

Dicer structure and function: conserved and evolving features

Zapletal, D., Kubíček, K., Svoboda, P., & Štefl, R. (2023) · EMBO Reports · doi:10.15252/embr.202357215 · Cited by 62 · see citing works

Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development

Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · BMC Genomics · doi:10.1186/s12864-021-07380-0 · Cited by 61 · see citing works

Reactivation of Endogenous Retroelements in Cancer Development and Therapy

Ishak, C. A., & Carvalho, D. D. D. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030419-033525 · Cited by 58 · see citing works

Targeting DDX3X Triggers Antitumor Immunity via a dsRNA-Mediated Tumor-Intrinsic Type I Interferon Response

Choi, H., Kwon, J., Cho, M. S., Sun, Y., Zheng, X., Wang, J., Bouker, K. B., Casey, J. L., Atkins, M. B., Toretsky, J. A., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3790 · Cited by 58 · see citing works

Impact of ADAR-induced editing of minor viral RNA populations on replication and transmission of SARS-CoV-2

Ringlander, J., Fingal, J., Kann, H., Prakash, K., Rydell, G. E., Andersson, M., Martner, A., Lindh, M., Horal, P., Hellstrand, K., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112663119 · Cited by 57 · see citing works

Deep learning models for predicting RNA degradation via dual crowdsourcing

Wayment-Steele, H. K., Kladwang, W., Watkins, A. M., Kim, D. S., Tunguz, B., Reade, W., Demkin, M., Romano, J., Wellington-Oguri, R., Nicol, J. J., et al. (2022) · Nature Machine Intelligence · doi:10.1038/s42256-022-00571-8 · Cited by 56 · see citing works

Formation and Function of Liquid-Like Viral Factories in Negative-Sense Single-Stranded RNA Virus Infections

Su, J. M., Wilson, M. Z., Samuel, C. E., & Ma, D. (2021) · Viruses · doi:10.3390/v13010126 · Cited by 53 · see citing works

To protect and modify double-stranded RNA – the critical roles of ADARs in development, immunity and oncogenesis

Erdmann, E. A., Mahapatra, A., Mukherjee, P., Yang, B., & Hundley, H. A. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1856768 · Cited by 52 · see citing works

MERS-CoV endoribonuclease and accessory proteins jointly evade host innate immunity during infection of lung and nasal epithelial cells

Comar, C. E., Otter, C. J., Pfannenstiel, J. J., Doerger, E., Renner, D. M., Tan, L. H., Perlman, S. M., Cohen, N. A., Fehr, A. R., & Weiss, S. R. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2123208119 · Cited by 52 · see citing works

Investigating the Potential Roles of SINEs in the Human Genome

Zhang, X.-O., Pratt, H., & Weng, Z. (2021) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-111620-100736 · Cited by 51 · see citing works

TERT activates endogenous retroviruses to promote an immunosuppressive tumour microenvironment

Mao, J., Zhang, Q., Wang, Y., Yang, Z., Xu, L., Ma, X., Guan, D., Zhou, J., Liu, J., Wu, X., et al. (2022) · EMBO Reports · doi:10.15252/embr.202152984 · Cited by 50 · see citing works

H3K9 methylation drives resistance to androgen receptor–antagonist therapy in prostate cancer

Baratchian, M., Tiwari, R., Khalighi, S., Chakravarthy, A., Yuan, W., Berk, M. P., Li, J., Guerinot, A., Bono, J. S. D., Makarov, V., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114324119 · Cited by 51 · see citing works

Targeting organ-specific mitochondrial dysfunction to improve biological aging

Madreiter‐Sokolowski, C. T., Hiden, U., Krstić, J., Panzitt, K., Wagner, M., Enzinger, C., Khalil, M., Abdellatif, M., Malle, E., Madl, T., et al. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108710 · Cited by 54 · see citing works

Recent Advances and Contradictions in the Study of the Individual Roles of Ubiquitin Ligases That Regulate RIG-I-Like Receptor-Mediated Antiviral Innate Immune Responses

Oshiumi, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01296 · Cited by 51 · see citing works

Why Severe COVID-19 Patients Are at Greater Risk of Developing Depression: A Molecular Perspective

Bouças, A. P., Rheinheimer, J., & Lagopoulos, J. (2020) · The Neuroscientist · doi:10.1177/1073858420967892 · Cited by 51 · see citing works

Long Noncoding RNAs as Emerging Regulators of COVID-19

Yang, Q., Fang, L., Wang, Y., Min De, Z. E. N. G., & Luo, M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.700184 · Cited by 50 · see citing works

Comorbidities and clinical complications associated with SARS-CoV-2 infection: an overview

Gupta, A., Marzook, H., & Ahmad, F. (2022) · Clinical and Experimental Medicine · doi:10.1007/s10238-022-00821-4 · Cited by 49 · see citing works

Noncanonical immune response to the inhibition of DNA methylation by Staufen1 via stabilization of endogenous retrovirus RNAs

Ku, Y., Park, J., Cho, R., Lee, Y.-K., Park, H.-M., Kim, M. A., Hur, K., Byun, S. Y., Liu, J., Lee, Y.-S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016289118 · Cited by 49 · see citing works

Flipped over U: structural basis for dsRNA cleavage by the SARS-CoV-2 endoribonuclease

Frazier, M. N., Wilson, I. M., Krahn, J. M., Butay, K. J., Dillard, L. B., Borgnia, M. J., & Stanley, R. E. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac589 · Cited by 48 · see citing works

Chemotherapy‐Induced Senescence Reprogramming Promotes Nasopharyngeal Carcinoma Metastasis by circRNA‐Mediated PKR Activation

Li, Q., Zhao, Y., Xu, C., Liang, Y., Zhao, Y., He, Q., Li, J., Chen, K., Qiao, H., Liu, N., et al. (2023) · Advanced Science · doi:10.1002/advs.202205668 · Cited by 48 · see citing works

Inverted Alu repeats: friends or foes in the human transcriptome

Lee, K., Ku, J., Ku, D., & Kim, Y. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01177-3 · Cited by 48 · see citing works

A review: Antibody-dependent enhancement in COVID-19: The not so friendly side of antibodies

Sánchez‐Zuno, G. A., Matuz-Flores, M. G., González-Estévez, G., Nicoletti, F., Turrubiates‐Hernández, F. J., Mangano, K., & Muñóz-Valle, J. F. (2021) · International Journal of Immunopathology and Pharmacology · doi:10.1177/20587384211050199 · Cited by 48 · see citing works

Functional food: complementary to fight against COVID-19

Farzana, M., Shahriar, S., Jeba, F. R., Tabassum, T., Araf, Y., Ullah, M. A., Tasnim, J., Chakraborty, A., Naima, T. A., Marma, K. K. S., et al. (2022) · Beni-Suef University Journal of Basic and Applied Sciences · doi:10.1186/s43088-022-00217-z · Cited by 45 · see citing works

Nucleic acid-mediated PAMP-triggered immunity in plants

Amari, K., & Niehl, A. (2020) · Current Opinion in Virology · doi:10.1016/j.coviro.2020.04.003 · Cited by 45 · see citing works

Molecular mechanisms of nonself nucleic acid recognition by the innate immune system

Mann, C. C. D. O., & Hornung, V. (2021) · European Journal of Immunology · doi:10.1002/eji.202049116 · Cited by 43 · see citing works

Molecular Mechanisms of Resistance to Immune Checkpoint Inhibitors in Melanoma Treatment: An Update

Vukadin, S., Khaznadar, F., Kizivat, T., Včev, A., & Smolić, M. (2021) · Biomedicines · doi:10.3390/biomedicines9070835 · Cited by 46 · see citing works

RNA editing enzymes: structure, biological functions and applications

Zhang, D., Zhu, L., Gao, Y., Wang, Y., & Li, P. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01216-6 · Cited by 43 · see citing works

In search of critical dsRNA targets of ADAR1

Levanon, E. Y., Cohen‐Fultheim, R., & Eisenberg, E. (2023) · Trends in Genetics · doi:10.1016/j.tig.2023.12.002 · Cited by 42 · see citing works

The nuclear and cytoplasmic activities of RNA polymerase III, and an evolving transcriptome for surveillance

Kessler, A. C., & Maraia, R. J. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1145 · Cited by 39 · see citing works

An engineered T7 RNA polymerase for efficient co-transcriptional capping with reduced dsRNA byproducts in mRNA synthesis

Miller, M. G., Alvizo, O., Baskerville, S., Chintala, A., Chng, C., Dassie, J. P., Dorigatti, J. D., Huisman, G. W., Jenne, S., Kadam, S., et al. (2024) · Faraday Discussions · doi:10.1039/d4fd00023d · Cited by 40 · see citing works

Reactivation of senescence-associated endogenous retroviruses by ATF3 drives interferon signaling in aging

Mao, J., Zhang, Q., Zhuang, Y., Zhang, Y., Li, L., Pan, J., Xu, L., Ding, Y., Wang, M., & Cong, Y. (2024) · Nature Aging · doi:10.1038/s43587-024-00745-6 · Cited by 38 · see citing works

Gene delivery for immunoengineering

Neshat, S. Y., Tzeng, S. Y., & Green, J. J. (2020) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2020.05.008 · Cited by 42 · see citing works

Structural Insights into RNA Dimerization: Motifs, Interfaces and Functions

Bou‐Nader, C., & Zhang, J. (2020) · Molecules · doi:10.3390/molecules25122881 · Cited by 41 · see citing works

In silico analysis of altered expression of long non-coding RNA in SARS-CoV-2 infected cells and their possible regulation by STAT1, STAT3 and interferon regulatory factors

Laha, S., Saha, C., Dutta, S., Basu, M., Chatterjee, R., Ghosh, S. K., & Bhattacharyya, N. P. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e06395 · Cited by 39 · see citing works

RNA Crossing Membranes: Systems and Mechanisms Contextualizing Extracellular RNA and Cell Surface GlycoRNAs

Chai, P., Lebedenko, C. G., & Flynn, R. A. (2023) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-101722-101224 · Cited by 40 · see citing works

Human OAS1 activation is highly dependent on both RNA sequence and context of activating RNA motifs

Schwartz, S. L., Park, E. N., Vachon, V. K., Danzy, S., Lowen, A. C., & Conn, G. L. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa513 · Cited by 38 · see citing works

Cytoplasmic RNA sensors and their interplay with RNA-binding partners in innate antiviral response: theme and variations

Chan, C., & Jin, D. (2022) · RNA · doi:10.1261/rna.079016.121 · Cited by 36 · see citing works

Evidence of Aberrant Immune Response by Endogenous Double‐Stranded RNAs: Attack from Within

Kim, S., Ku, Y., Ku, J., & Kim, Y. (2019) · BioEssays · doi:10.1002/bies.201900023 · Cited by 37 · see citing works

hnRNPM protects against the dsRNA-mediated interferon response by repressing LINE-associated cryptic splicing

Zheng, R., Dunlap, M., Bobkov, G. O. M., Gonzalez‐Figueroa, C., Patel, K. J., Lyu, J., Harvey, S. E., Chan, T. W., Quinones-Valdez, G., Choudhury, M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.05.004 · Cited by 41 · see citing works

Harnessing anti-inflammatory pathways and macrophage nano delivery to treat inflammatory and fibrotic disorders

Zaid, A. K. M. A., & Ariel, A. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115204 · Cited by 35 · see citing works

Filament-like Assemblies of Intracellular Nucleic Acid Sensors: Commonalities and Differences

Cadena, C., & Hur, S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.023 · Cited by 34 · see citing works

Innate Immune Response in SARS-CoV-2 Infection

Schiuma, G., Beltrami, S., Bortolotti, D., Rizzo, S., & Rizzo, R. (2022) · Microorganisms · doi:10.3390/microorganisms10030501 · Cited by 34 · see citing works

PRC2-Inactivating Mutations in Cancer Enhance Cytotoxic Response to DNMT1-Targeted Therapy via Enhanced Viral Mimicry

Patel, A. J., Warda, S., Mååg, J. L. V., Misra, R., Miranda-Román, M. A., Pachai, M. R., Lee, C. J., Li, D., Wang, N., Bayshtok, G., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1671 · Cited by 34 · see citing works

Flaviviridae Nonstructural Proteins: The Role in Molecular Mechanisms of Triggering Inflammation

Latanova, A. A., Starodubova, E. S., & Карпов, В. Л. (2022) · Viruses · doi:10.3390/v14081808 · Cited by 35 · see citing works

SARS‐CoV‐2 biology and variants: anticipation of viral evolution and what needs to be done

Luo, R., Delaunay-Moisan, A., Timmis, K., & Danchin, A. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15487 · Cited by 37 · see citing works

Mitochondrial Contribution to Inflammation in Diabetic Kidney Disease

Mitrofanova, A. V., Fontanella, A. M., Burke, G. W., Merscher, S., & Fornoni, A. (2022) · Cells · doi:10.3390/cells11223635 · Cited by 35 · see citing works

Regulation and function of transposable elements in cancer genomes

Lee, M., Ahmad, S. F., & Xu, J. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05195-2 · Cited by 32 · see citing works

Interferon signaling in the nasal epithelium distinguishes among lethal and common cold coronaviruses and mediates viral clearance

Otter, C. J., Renner, D. M., Fausto, A., Tan, L., Cohen, N. A., & Weiss, S. R. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2402540121 · Cited by 31 · see citing works

Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms

Jeon, J., & Kim, Y. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0067 · Cited by 1 · see citing works

Sensores de ARN de cadena doble en la inmunidad innata

García Japón, B. (2021) · idUS (Universidad de Sevilla)

Sensing of double-stranded RNA in human cells: molecular mechanisms and cellular consequences

Cieslicka, J., Pianka, K., Drążkowska, K., & Sikorski, P. J. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250259 · Cited by 2 · see citing works

Multi-level regulation of cellular recognition of viral dsRNA

Peisley, A., & Hur, S. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1149-4 · Cited by 47 · see citing works

dsRNA Sensing During Viral Infection: Lessons from Plants, Worms, Insects, and Mammals

de Faria, I. J. S., Olmo, R. P., Silva, E. G., & Marques, J. T. (2013) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2013.0026 · Cited by 25 · see citing works