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Human NLRP1 is a sensor for double-stranded RNA
Abstract
A dsRNA detector in the immune toolkit: Nod-like receptor (NLR) proteins recognize pathogen-associated molecular patterns within cells, which triggers the formation of signaling complexes called inflammasomes. These complexes then initiate pyroptosis, a highly inflammatory form of cell death. Recent work has shown that a rhinovirus protease can activate the human NLRP1 inflammasome, but it was unclear whether this is the only pathogen-derived trigger for NLRP1. Bauernfried et al. report that long, double-stranded RNA (dsRNA) generated in the course of Semliki Forest virus infection binds and activates NLRP1 in epithelial cells. dsRNA binding triggered NLRP1 to acquire adenosine triphosphatase (ATPase) activity, a common feature of activated NLR proteins. Thus, in addition to its ability to recognize viral protease activity, human NLRP1 can act as a genuine sensor of virus-associated nucleic acids. Science , this issue p. eabd0811
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“Through recognition of TLR3 in endosomes or retinoic acid-inducible gene I, melanoma differentiation-associated protein 5, and inflammasomes in the cytoplasm,96, 97, 98, 99 depending on the amount, dsRNAs might overactivate innate immunity and lead to adverse events.”
From COVID-19 mRNA vaccines: Platforms and current developments (2022) · cites this paper as [99]
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Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Cyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway
Sun, L., Wu, J., Du, F., Chen, X., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1232458 · Cited by 4,996
Inflammasomes: mechanism of assembly, regulation and signalling
Broz, P., & Dixit, V. M. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.58 · Cited by 3,500
A Completely Reimplemented MPI Bioinformatics Toolkit with a New HHpred Server at its Core
Zimmermann, L., Stephens, A., Nam, S.-Z., Rau, D., Kübler, J., Lozajic, M., Gabler, F., Söding, J., Lupas, A. N., & Alva, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.12.007 · Cited by 2,522
The gasdermins, a protein family executing cell death and inflammation
Broz, P., Pelegrín, P., & Shao, F. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-019-0228-2 · Cited by 1,641
Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
Kanneganti, T., Özören, N., Body–Malapel, M., Amer, A. O., Park, J., Franchi, L., Whitfield, J. R., Barchet, W., Colonna, M., Vandenabeele, P., et al. (2006) · Nature · doi:10.1038/nature04517 · Cited by 1,149
Dickson, M. A., Hahn, W. C., Ino, Y., Ronfard, V., Wu, J. Y., Weinberg, R. A., Louis, D. N., Li, F. P., & Rheinwald, J. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1436-1447.2000 · Cited by 1,104
MCC950 directly targets the NLRP3 ATP-hydrolysis motif for inflammasome inhibition
Coll, R. C., Hill, J. R., Day, C. J., Zamoshnikova, A., Boucher, D., Massey, N. L., Chitty, J. L., Fraser, J. A., Jennings, M. P., Robertson, A. A. B., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0277-7 · Cited by 1,041
Structural mechanism of cytosolic DNA sensing by cGAS
Çivril, F., Deimling, T., Mann, C. C. D. O., Ablasser, A., Moldt, M., Witte, G., Hornung, V., & Hopfner, K. (2013) · Nature · doi:10.1038/nature12305 · Cited by 916
Self-citationSchlee, 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
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Bertheloot, D., Latz, E., & Franklin, B. S. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-00630-3 · Cited by 2,297
Lamers, M. M., & Haagmans, B. L. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00713-0 · Cited by 1,066
Role of pyroptosis in inflammation and cancer
Xiang, W. D., Xie, F., Zhou, X., Wu, Y., Yan, H., Liu, T., Huang, J. S., Wang, F., Zhou, F., & Zhang, L. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00905-x · Cited by 728
FcγR-mediated SARS-CoV-2 infection of monocytes activates inflammation
Junqueira, C., Crespo, Â. C., Ranjbar, S., de Lacerda, L., Lewandrowski, M., Ingber, J., Parry, B. A., Ravid, S., Clark, S. A., Schrimpf, M. R., et al. (2022) · Nature · doi:10.1038/s41586-022-04702-4 · Cited by 699
A 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases
Barnett, K. C., Li, S., Liang, K., & Ting, J. P.-Y. (2023) · Cell · doi:10.1016/j.cell.2023.04.025 · Cited by 458
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 457
COVID-19 mRNA vaccines: Platforms and current developments
Szabó, G. T., Mahiny, A. J., & Vlatkovic, I. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.02.016 · Cited by 308
Prokaryotic innate immunity through pattern recognition of conserved viral proteins
Gao, L. A., Wilkinson, M. E., Strecker, J., Makarova, K. S., Macrae, R. K., Koonin, E. V., & Zhang, F. (2022) · Science · doi:10.1126/science.abm4096 · Cited by 235
The NLR gene family: from discovery to present day
Chou, W.-C., Jha, S., Linhoff, M. W., & Ting, J. P. ‐. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00849-x · Cited by 232
Mechanistic insights from inflammasome structures
Fu, J., Schroder, K., & Wu, H. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-00995-w · Cited by 223
The NLR family of innate immune and cell death sensors
Sundaram, B., Tweedell, R. E., Kumar, S. P., & Kanneganti, T. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.012 · Cited by 224
Advances in mechanism and regulation of PANoptosis: Prospects in disease treatment
Zhu, P., Ke, Z.-R., Chen, J.-X., Li, S., Ma, T., & Fan, X.-L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1120034 · Cited by 200
Integrated NLRP3, AIM2, NLRC4, Pyrin inflammasome activation and assembly drive PANoptosis
Oh, S., Lee, J., Oh, J.-E., Yu, G., Ryu, H., Kim, D., & Lee, S. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01107-9 · Cited by 192
Cell biology of inflammasome activation
Pandey, A., Shen, C. X., Feng, S., & Man, S. M. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.06.010 · Cited by 183
ZAKα-driven ribotoxic stress response activates the human NLRP1 inflammasome
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Self-citationDiverse viral proteases activate the NLRP1 inflammasome
Tsu, B. V., Beierschmitt, C., Ryan, A. P., Agarwal, R., Mitchell, P. S., & Daugherty, M. D. (2021) · eLife · doi:10.7554/elife.60609 · Cited by 180
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Inflammasome components as new therapeutic targets in inflammatory disease
Coll, R. C., & Schroder, K. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01075-9 · Cited by 175
CARD8 is an inflammasome sensor for HIV-1 protease activity
Wang, Q., Gao, H., Clark, K. M., Mugisha, C. S., Davis, K., Tang, J. P., Harlan, G. H., DeSelm, C. J., Presti, R. M., Kutluay, S. B., et al. (2021) · Science · doi:10.1126/science.abe1707 · Cited by 162
The role of NOD-like receptors in innate immunity
Almeida-da-Silva, C. L. C., Savio, L. E. B., Coutinho‐Silva, R., & Ojcius, D. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1122586 · Cited by 170
Organellar homeostasis and innate immune sensing
Harapas, C. R., Idiiatullina, E., Al‐Azab, M., Hrovat-Schaale, K., Reygaerts, T., Steiner, A., Laohamonthonkul, P., Davidson, S., Yu, C., Booty, L. M., et al. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00682-8 · Cited by 152
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Planès, R., Pinilla, M., Santoni, K., Hessel, A., Passemar, C., Lay, K., Paillette, P., Valadão, A. L. C., Robinson, K. S., Bastard, P., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.033 · Cited by 160
Triggers for the onset and recurrence of psoriasis: a review and update
Liu, S., He, M. L., Jiang, J. W., Duan, X., Chai, B., Zhang, J., Tao, Q., & Chen, H. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01381-0 · Cited by 158
The immunostimulatory nature of mRNA lipid nanoparticles
Sharma, P., Hoorn, D., Aitha, A., Breier, D., & Peer, D. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.115175 · Cited by 132
The gasdermin family: emerging therapeutic targets in diseases
Zhu, C., Xu, S., Jiang, R., Yu, Y., Bian, J., & Zou, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01801-8 · Cited by 149
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Jenster, L., Lange, K.-E., Normann, S., Hemdt, A. V., Wuerth, J. D., Schiffelers, L. D. J., Tesfamariam, Y. M., Gohr, F. N., Klein, L., Kaltheuner, I. H., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220837 · Cited by 114
NLRP inflammasomes in health and disease
Xu, Z., Kombe, A. J. K., Deng, S., Zhang, H., Wu, S., Ruan, J., Zhou, Y. Y., & Jin, T. (2024) · Molecular Biomedicine · doi:10.1186/s43556-024-00179-x · Cited by 131
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Sharif, H., Hollingsworth, L. R., Griswold, A. R., Hsiao, J. C., Wang, Q., Bachovchin, D. A., & Wu, H. (2021) · Immunity · doi:10.1016/j.immuni.2021.04.024 · Cited by 97
PANoptosis in Viral Infection: The Missing Puzzle Piece in the Cell Death Field
Nguyen, L. N., & Kanneganti, T. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167249 · Cited by 100
The evolution of regulated cell death pathways in animals and their evasion by pathogens
Tummers, B., & Green, D. R. (2021) · Physiological Reviews · doi:10.1152/physrev.00002.2021 · Cited by 95
Dubey, S. R., Turnbull, C., Pandey, A., Zhao, A., Kurera, M., Al-Zidan, R. N., Shen, C. X., Gautam, M., Mahajan, S., Jadhav, P. S., et al. (2025) · Cellular and Molecular Immunology · doi:10.1038/s41423-025-01354-y · Cited by 101
SARS-CoV-2 and innate immunity: the good, the bad, and the “goldilocks”
Sievers, B. L., Cheng, M. T. K., Csiba, K., Meng, B., & Gupta, R. K. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01104-y · Cited by 91
Viral-mediated activation and inhibition of programmed cell death
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Role of the inflammasome in insulin resistance and type 2 diabetes mellitus
Lu, S., Li, Y., Qian, Z., Zhao, T., Feng, Z., Weng, X., & Yu, L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1052756 · Cited by 91
Paerewijck, O., & Lamkanfi, M. (2022) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2022.101100 · Cited by 86
Pyroptosis and respiratory diseases: A review of current knowledge
Sun, J., & Li, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.920464 · Cited by 82
Viral manipulation of host cell necroptosis and pyroptosis
Verdonck, S., Nemegeer, J., Vandenabeele, P., & Maelfait, J. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.11.011 · Cited by 76
Fantastic voyage: The journey of NLRP3 inflammasome activation
Que, X., Zheng, S., Song, Q., Pei, H., & Zhang, P. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.01.009 · Cited by 91
Involvement of inflammasomes in tumor microenvironment and tumor therapies
Zhang, Z., Li, X., Wang, Y., Wei, Y., & Wei, X. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01407-7 · Cited by 83
Molecular mechanisms of phenotypic variability in monogenic autoinflammatory diseases
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NLRP3 inflammasome as a sensor of micro- and nanoplastics immunotoxicity
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Carrière, J., Dorfleutner, A., & Stehlik, C. (2021) · Immunology · doi:10.1111/imm.13372 · Cited by 78
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Johnson, N. H., Vaccari, J. P. D. R., Bramlett, H. M., Keane, R. W., & Dietrich, W. D. (2022) · Translational research · doi:10.1016/j.trsl.2022.08.014 · Cited by 74
Human NLRP1: From the shadows to center stage
Bauernfried, S., & Hornung, V. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20211405 · Cited by 72
Self-citationdsRNA-induced condensation of antiviral proteins modulates PKR activity
Corbet, G. A., Burke, J. M., Bublitz, G. R., Tay, J. W., & Parker, R. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2204235119 · Cited by 78
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Brinkschulte, R., Fußhöller, D. M., Hoß, F., Rodríguez-Alcázar, J. F., Lauterbach, M., Kolbe, C., Rauen, M., Ince, S., Herrmann, C., Latz, E., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04120-2 · Cited by 69
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de Reuver, R., & Maelfait, J. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00940-3 · Cited by 70
Planès, R., Bert, J.-B., Tairi, S., BenMohamed, L., & Bahraoui, E. (2022) · Viruses · doi:10.3390/v14050999 · Cited by 66
Inflammasome activation: from molecular mechanisms to autoinflammation
Reyna, S. J. L., Caseley, E. A., Topping, J., Rodrigues, F., Jimenez-Macias, J. L., Lawler, S. E., & McDermott, M. (2022) · Clinical & Translational Immunology · doi:10.1002/cti2.1404 · Cited by 67
Activation and regulation mechanisms of NOD-like receptors based on structural biology
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NLRP1- A CINDERELLA STORY: a perspective of recent advances in NLRP1 and the questions they raise
Barry, K. T., Murphy, C., & Mansell, A. S. (2023) · Communications Biology · doi:10.1038/s42003-023-05684-3 · Cited by 63
Structures and functions of the inflammasome engine
Wang, L., Sharif, H., Vora, S. M., Zheng, Y., & Wu, H. (2021) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2021.04.018 · Cited by 61
Understanding the impact of in vitro transcription byproducts and contaminants
Lenk, R., Kleindienst, W., Szabó, G. T., Baiersdörfer, M., Boros, G., Keller, J. M., Mahiny, A. J., & Vlatkovic, I. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1426129 · Cited by 63
DPP9 deficiency: An inflammasomopathy that can be rescued by lowering NLRP1/IL-1 signaling
Harapas, C. R., Robinson, K. S., Lay, K., Wong, J., Traspas, R. M., Nabavizadeh, N., Raas‐Rothschild, A., Boisson, B., Drutman, S. B., Laohamonthonkul, P., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abi4611 · Cited by 57
Role of the NLRP1 inflammasome in skin cancer and inflammatory skin diseases
Calabrese, L., Fiocco, Z., Mellett, M., Aoki, R., Rubegni, P., French, L. E., & Satoh, T. K. (2023) · British Journal of Dermatology · doi:10.1093/bjd/ljad421 · Cited by 56
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Lillo, S., & Saleh, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.839041 · Cited by 58
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(2022) · doi:10.1126/sciimmunol.abm7200 · Cited by 53
The crosstalk between immune cells and tumor pyroptosis: advancing cancer immunotherapy strategies
Hu, M., Deng, F., Song, X., Zhao, H., & Yan, F. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-024-03115-7 · Cited by 57
Hulme, K. D., Noye, E. C., Short, K. R., & Labzin, L. I. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.770066 · Cited by 52
Origins and diversification of animal innate immune responses against viral infections
Iwama, R. E., & Moran, Y. (2023) · Nature Ecology & Evolution · doi:10.1038/s41559-022-01951-4 · Cited by 50
Structural basis for thioredoxin-mediated suppression of NLRP1 inflammasome
Zhang, Z., Shibata, T., Fujimura, A., Kitaura, J., Miyake, K., Ohto, U., & Shimizu, T. (2023) · Nature · doi:10.1038/s41586-023-06532-4 · Cited by 52
Sun, Y., Li, F., Liu, Y., Qiao, D., Yao, X., Liu, G., Li, D., Xiao, C., Wang, T., & Chi, W. (2024) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2024.101263 · Cited by 54
Regulation of antiviral innate immunity by chemical modification of viral RNA
Li, N., & Rana, T. M. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1720 · Cited by 46
Bharadwaj, R., Lusi, C. F., Mashayekh, S., Nagar, A., Subbarao, M., Kane, G. I., Wodzanowski, K. A., Brown, A. R., Okuda, K., Monahan, A., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.04.001 · Cited by 50
Viral proteases activate the CARD8 inflammasome in the human cardiovascular system
Nadkarni, R., Chu, W., Lee, C. Q. E., Mohamud, Y., Yap, L., Toh, G. A., Beh, S., Lim, R., Fan, Y. M., Zhang, Y. L., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20212117 · Cited by 50
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Deng, Z., Lu, L., Li, B., Shi, X., Jin, H., & Hu, W. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1195572 · Cited by 53
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Constant, D. A., Nice, T. J., & Rauch, I. (2021) · Current Opinion in Immunology · doi:10.1016/j.coi.2021.07.014 · Cited by 46
Structural basis of the human NAIP/NLRC4 inflammasome assembly and pathogen sensing
Matico, R., Yu, X., Miller, R., Somani, S., Ricketts, M. D., Kumar, N., Steele, R. A., Medley, Q. G., Berger, S. B., Faustin, B., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01143-z · Cited by 45
Guillemin, A., Kumar, A., Wencker, M., & Ricci, E. P. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.796012 · Cited by 48
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Zou, Z., Zhao, M., Yang, Y., Xie, Y., Li, Z., Zhou, L., Shang, R., & Zhou, P. (2023) · Cellular Oncology · doi:10.1007/s13402-023-00787-9 · Cited by 44
EEF2-inactivating toxins engage the NLRP1 inflammasome and promote epithelial barrier disruption
Pinilla, M., Mazars, R., Vergé, R., Gorse, L., Paradis, M., Suire, B., Santoni, K., Robinson, K. S., Toh, G. A., Prouvensier, L., et al. (2023) · The Journal of Experimental Medicine · doi:10.1084/jem.20230104 · Cited by 49
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Zhou, J. Y., Sarkar, M. K., Okamura, K., Harris, J. E., Gudjonsson, J. E., & Fitzgerald, K. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2213777120 · Cited by 43
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Wang, J., Hua, S., Bao, H., Yuan, J., Zhao, Y., & Chen, S. (2023) · MedComm · doi:10.1002/mco2.374 · Cited by 43
Gong, Y., Yong, D., Liu, G., Xu, J., Ding, J., & Jia, W. W.-G. (2024) · Advanced Science · doi:10.1002/advs.202402936 · Cited by 45
The NLRP1 Inflammasome Induces Pyroptosis in Human Corneal Epithelial Cells
Griswold, A. R., Huang, H., & Bachovchin, D. A. (2022) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.63.3.2 · Cited by 40
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Metadata
- Authors
- Bauernfried, S., Scherr, M. J., Pichlmair, A., Duderstadt, K. E., & Hornung, V.
- Affiliations
- Ludwig-Maximilians-Universität München (DE)
- Max Planck Institute of Biochemistry (DE)
- German Center for Infection Research (DE)
- Corresponding author
- Hornung, Veit
- Venue
- Science
- Published
- 2021-01-29
- Volume
- 371
- Issue
- 6528
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W3109641046
- Cited by
- 304
- References
- 39
- Citations by year
- 2026: 32 · 2025: 36 · 2024: 57 · 2023: 62 · 2022: 76 · 2021: 41
- FWCI
- 14.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- European Research Council (ERC-2014-CoG – 647858 GENESIS, ERC-2018-CoG – 817798 ProDAP, ERC-2018-StG – 804098 REPLISOMEBYPASS)
- Deutsche Forschungsgemeinschaft (TRR 237/A09 (Project-ID 369799452), CRC 1335/P015 (Project-ID 360372040), SPP 1923 (Project-ID 273898015), TRR 179/TP11 (Project-ID 272983813), TRR 237/A07 (Project-ID 369799452))
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- NLRP1, inflammasome, double-stranded RNA, Semliki Forest virus, positive-strand RNA viruses, keratinocytes, leucine-rich repeat domain, NACHT domain, ATPase activity, epithelial barrier function, innate immunity
- MeSH terms
- NLR Proteins, Protein Domains, Adenosine Triphosphatases, Adenosine Triphosphate, Animals, Humans, Hydrolysis, Immunity, Innate, Mice, Transgenic, RNA, Double-Stranded, RNA, Viral, Semliki forest virus, Virus Replication, Keratinocytes, Alphavirus Infections, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Mice, Host-Pathogen Interactions, HEK293 Cells, Inflammasomes
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