Cited by 2,627Inflammasome and immune disordersinterferon and immune responsesImmune Response and Inflammation

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

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

Open access

Hornung, Veit, Ablasser, Andrea, Charrel-Dennis, Marie, Bauernfeind, Franz, Horvath, Gabor, Caffrey, Daniel. R., Latz, Eicke, Fitzgerald, Katherine A.·2009·Nature

DOI 10.1038/nature07725PMC PMC2726264

Open this paper in CoChat — free account

Abstract

The innate immune system senses nucleic acids by germline-encoded pattern recognition receptors. RNA is sensed by Toll-like receptor members TLR3, TLR7 and TLR8, or by the RNA helicases RIG-I (also known as DDX58) and MDA-5 (IFIH1). Little is known about sensors for cytoplasmic DNA that trigger antiviral and/or inflammatory responses. The best characterized of these responses involves activation of the TANK-binding kinase (TBK1)-interferon regulatory factor 3 (IRF3) signalling axis to trigger transcriptional induction of type I interferon genes. A second, less well-defined pathway leads to the activation of an 'inflammasome' that, via caspase-1, controls the catalytic cleavage of the pro-forms of the cytokines IL1beta and IL18 (refs 6, 7). Using mouse and human cells, here we identify the PYHIN (pyrin and HIN domain-containing protein) family member absent in melanoma 2 (AIM2) as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain (but not that of the other PYHIN family members) associates with the adaptor molecule ASC (apoptosis-associated speck-like protein containing a caspase activation and recruitment domain) to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus. Collectively, these observations identify AIM2 as a new receptor for cytoplasmic DNA, which forms an inflammasome with the ligand and ASC to activate caspase-1.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/nature07725

Cites

30 of 30 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

MUSCLE: multiple sequence alignment with high accuracy and high throughput
Edgar, R. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh340 · Cited by 44,662
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Self-citation
DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
Takaoka, A., Wang, Z., Choi, M. K., Yanai, H., Negishi, H., Ban, T., Lu, Y., Miyagishi, M., Kodama, T., Honda, K., et al. (2007) · Nature · doi:10.1038/nature06013 · Cited by 1,704
Intracellular pattern recognition receptors in the host response
Meylan, E., Tschopp, J., & Karin, M. (2006) · Nature · doi:10.1038/nature04946 · Cited by 1,196
Recognition of Cytosolic DNA Activates an IRF3-Dependent Innate Immune Response
Stetson, D. B., & Medzhitov, R. M. (2006) · Immunity · doi:10.1016/j.immuni.2005.12.003 · Cited by 1,003
The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
Muruve, D. A., Pétrilli, V., Zaiss, A. K., White, L. R., Clark, S. A., Ross, P. J., Parks, R. J., & Tschopp, J. (2008) · Nature · doi:10.1038/nature06664 · Cited by 965
A Toll-like receptor–independent antiviral response induced by double-stranded B-form DNA
Ishii, K. J., Coban, C., Kato, H., Takahashi, K., Torii, Y., Takeshita, F., Ludwig, H., Sutter, G., Suzuki, K., Hemmi, H., et al. (2005) · Nature Immunology · doi:10.1038/ni1282 · Cited by 771
Enzymatic Synthesis of Deoxyribonucleic Acid
Richardson, C. C., Schildkraut, C. L., Aposhian, H. V., & Kornberg, A. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51772-5 · Cited by 718
Critical Role for Cryopyrin/Nalp3 in Activation of Caspase-1 in Response to Viral Infection and Double-stranded RNA
Kanneganti, T., Body–Malapel, M., Amer, A. O., Park, J., Whitfield, J. R., Franchi, L., Taraporewala, Z. F., Miller, D. J., Patton, J. T., Inohara, N., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607594200 · Cited by 706
TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines
Ishii, K. J., Kawagoe, T., Koyama, S., Matsui, K., Kumar, H., Kawai, T., Uematsu, S., Takeuchi, O., Takeshita, F., Coban, C., et al. (2008) · Nature · doi:10.1038/nature06537 · Cited by 633

Flagged first, then by citations

Show all 30 references

Sorted by citations

Items 601–700 of 1,004

Innate immune sensing of DNA viruses
Rathinam, V. A. K., & Fitzgerald, K. A. (2011) · Virology · doi:10.1016/j.virol.2011.02.003 · Cited by 102
Self-citation
Poxviruses Evade Cytosolic Sensing through Disruption of an mTORC1-mTORC2 Regulatory Circuit
Meade, N., Furey, C., Li, H., Verma, R., Chai, Q., Rollins, M. G., DiGiuseppe, S., Naghavi, M. H., & Walsh, D. (2018) · Cell · doi:10.1016/j.cell.2018.06.053 · Cited by 107
Targeting innate sensing in the tumor microenvironment to improve immunotherapy
Liu, Z., Han, C., & Fu, Y. (2019) · Cellular and Molecular Immunology · doi:10.1038/s41423-019-0341-y · Cited by 105
Plasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2
Lu, A. Z., Li, Y., Yin, Q., Ruan, J., Yu, X., Egelman, E. H., & Wu, H. (2015) · Cell Discovery · doi:10.1038/celldisc.2015.13 · Cited by 102
Multiple inflammasome complexes are activated in autistic spectrum disorders
Saresella, M., Piancone, F., Marventano, I., Zoppis, M., Hernis, A., Zanette, M., Trabattoni, D., Chiappedi, M. A., Ghezzo, A., Canevini, M. P., et al. (2016) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.03.009 · Cited by 106
Structural basis of RIP2 activation and signaling
Gong, Q., Long, Z., Zhong, F. L., Teo, D. E. T., Jin, Y., Yin, Z., Boo, Z. Z., Zhang, Y., Zhang, J., Yang, R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07447-9 · Cited by 101
The HDAC3 inhibitor RGFP966 ameliorated ischemic brain damage by downregulating the AIM2 inflammasome
Zhang, M. Q., Zhao, Q., Xia, M., Chen, J., Chen, Y., Cao, X., Liu, Y., Yuan, Z., Wang, X., & Xu, Y. (2019) · The FASEB Journal · doi:10.1096/fj.201900394rrr · Cited by 101
dsDNA-induced AIM2 pyroptosis halts aberrant inflammation during rhabdomyolysis-induced acute kidney injury
Baatarjav, C., Komada, T., Karasawa, T., Yamada, N., Sampilvanjil, A., Matsumura, T., & Takahashi, M. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01033-9 · Cited by 102
Tegument protein UL21 of alpha-herpesvirus inhibits the innate immunity by triggering CGAS degradation through TOLLIP-mediated selective autophagy
Ma, Z., Bai, J., Jiang, C., Zhu, H., Liu, D., Pan, M., Wang, X., Pi, J., Jiang, P., & Liu, X. (2022) · Autophagy · doi:10.1080/15548627.2022.2139921 · Cited by 104
Host–Pathogen Interactions During Mycobacterium tuberculosis infections
Stanley, S. A., & Cox, J. S. (2013) · Current topics in microbiology and immunology · doi:10.1007/82_2013_332 · Cited by 106
Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation
Gerlic, M., Faustin, B., Postigo, A. A., Yu, E. C.-W., Proell, M., Gombosuren, N., Krajewska, M., Flynn, R., Croft, M., Way, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215995110 · Cited by 101
Molecular and Structural Basis of DNA Sensors in Antiviral Innate Immunity
Zahid, A., Ismail, H., Li, B., & Jin, T. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.613039 · Cited by 100
Decrease of AIM2 mediated by luteolin contributes to non-small cell lung cancer treatment
Yu, Q., Zhang, M., Ying, Q., Xie, X., Yue, S., Tong, B., Wei, Q., Bai, Z., & Ma, L. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1447-y · Cited by 103
AIM2 controls microglial inflammation to prevent experimental autoimmune encephalomyelitis
Ma, C., Li, S., Hu, Y., Ma, Y., Wu, Y., Wu, C., Liu, X., Wang, B., Hu, G., Zhou, J., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20201796 · Cited by 101
IL-18 Triggered by the Nlrp3 Inflammasome Induces Host Innate Resistance in a Pulmonary Model of Fungal Infection
Ketelut-Carneiro, N., Silva, G. K., Rocha, F. A., Milanezi, C. M., Neto, F. F. C., Zamboni, D. S., & Silva, J. S. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402321 · Cited by 100
Varicella-Zoster Virus Infection Triggers Formation of an Interleukin-1β (IL-1β)-processing Inflammasome Complex
Nour, A. M., Reichelt, M., Ku, C., Ho, M.-Y., Heineman, T. C., & Arvin, A. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.210575 · Cited by 100
TRIM13 Is a Negative Regulator of MDA5-Mediated Type I Interferon Production
Narayan, K., Waggoner, L., Pham, S. T., Hendricks, G. L., Waggoner, S. N., Conlon, J. E., Wang, J. P., Fitzgerald, K. A., & Kang, J. (2014) · Journal of Virology · doi:10.1128/jvi.02593-13 · Cited by 101
Self-citation
A STING to inflammation and autoimmunity
Kumar, V. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.4mir1018-397rr · Cited by 100
AIM2 deficiency in B cells ameliorates systemic lupus erythematosus by regulating Blimp-1–Bcl-6 axis-mediated B-cell differentiation
Yang, M., Long, D., Hu, L., Zhao, Z., Li, Q., Guo, Y., He, Z., Zhao, M., Lu, L., Li, F., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00725-x · Cited by 99
Emerging role of immunogenic cell death in cancer immunotherapy
Arimoto, K., Miyauchi, S., Liu, M., & Zhang, D. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1390263 · Cited by 103
Nucleic Acid Sensors and Type I Interferon Production in Systemic Lupus Erythematosus
Shrivastav, M., & Niewold, T. B. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00319 · Cited by 99
Integrative inflammasome activity in the regulation of intestinal mucosal immune responses
Elinav, E., Henao‐Mejia, J., & Flavell, R. A. (2012) · Mucosal Immunology · doi:10.1038/mi.2012.115 · Cited by 101
Innate Immune Signaling and Its Role in Metabolic and Cardiovascular Diseases
Xu, M. M., Liu, P. P., & Li, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00065.2017 · Cited by 100
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
Mutations of the Listeria monocytogenes PeptidoglycanN-Deacetylase andO-Acetylase Result in Enhanced Lysozyme Sensitivity, Bacteriolysis, and Hyperinduction of Innate Immune Pathways
Rae, C. S., Geissler, A. L., Adamson, P. C., & Portnoy, D. A. (2011) · Infection and Immunity · doi:10.1128/iai.00077-11 · Cited by 98
The Rate of Interleukin-1β Secretion in Different Myeloid Cells Varies with the Extent of Redox Response to Toll-like Receptor Triggering
Carta, S., Tassi, S., Pettinati, I., Delfino, L., Dinarello, C. A., & Rubartelli, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203398 · Cited by 97
AIM2 Drives Joint Inflammation in a Self-DNA Triggered Model of Chronic Polyarthritis
Jakobs, C., Perner, S., & Hornung, V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0131702 · Cited by 103
Self-citation
The NLRP1 Inflammasome in Human Skin and Beyond
Fenini, G., Karakaya, T., Hennig, P., Filippo, M. D., & Beer, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134788 · Cited by 99
Cytosolic dsDNA of mitochondrial origin induces cytotoxicity and neurodegeneration in cellular and zebrafish models of Parkinson’s disease
Matsui, H., Itô, J., Matsui, N., Uechi, T., Onodera, O., & Kakita, A. (2021) · Nature Communications · doi:10.1038/s41467-021-23452-x · Cited by 97
Molecular mechanisms and regulation of inflammasome activation and signaling: sensing of pathogens and damage molecular patterns
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
A 3′UTR SNP in NLRP3 Gene is Associated With Susceptibility to HIV-1 Infection
Pontillo, A., Brandão, L. A. C., Guimarães, R. L., Segat, L., Athanasakis, E., & Crovella, S. (2010) · JAIDS Journal of Acquired Immune Deficiency Syndromes · doi:10.1097/qai.0b013e3181dd17d4 · Cited by 97
Mitochondrial DNA sensing by STING signaling participates in inflammation, cancer and beyond
Liu, S., Feng, M., & Guan, W. (2016) · International Journal of Cancer · doi:10.1002/ijc.30074 · Cited by 99
Immunobiology and structural biology of AIM2 inflammasome
Wang, B., Bhattacharya, M., Roy, S., Tian, Y., & Yin, Q. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100869 · Cited by 96
Battle Royale: Innate Recognition of Poxviruses and Viral Immune Evasion
Yu, H., Bruneau, R. C., Brennan, G., & Rothenburg, S. (2021) · Biomedicines · doi:10.3390/biomedicines9070765 · Cited by 97
Regulation of programmed cell death by Brd4
Hu, J., Pan, D., Guo, L., Chen, K., & Hu, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05505-1 · Cited by 100
Role of pyroptosis in the pathogenesis of various neurological diseases
Oladapo, A., Jackson, T., Menolascino, J., & Periyasamy, P. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.02.001 · Cited by 101
Bacterial RNA: An Underestimated Stimulus for Innate Immune Responses
Eigenbrod, T., & Dalpke, A. H. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500530 · Cited by 96
MITA/STING: A central and multifaceted mediator in innate immune response
Ran, Y., Shu, H., & Wang, Y. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.05.003 · Cited by 96
The RNA- and TRIM25-Binding Domains of Influenza Virus NS1 Protein Are Essential for Suppression of NLRP3 Inflammasome-Mediated Interleukin-1β Secretion
Moriyama, M., Chen, I.-Y., Kawaguchi, A., Koshiba, T., Nagata, K., Takeyama, H., Hasegawa, H., & Ichinohe, T. (2016) · Journal of Virology · doi:10.1128/jvi.00120-16 · Cited by 96
Regulation of inflammasome activity
Guarda, G., & So, A. K.-L. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03283.x · Cited by 99
Inflammasome and Mitophagy Connection in Health and Disease
Yuk, J., Silwal, P., & Jo, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134714 · Cited by 98
Transcriptional Regulation of Inflammasomes
Cornut, M., Bourdonnay, E., & Henry, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218087 · Cited by 98
HUWE1 mediates inflammasome activation and promotes host defense against bacterial infection
Guo, Y., Li, L., Xu, T., Guo, X., Wang, C., Li, Y., Yang, Y., Yang, D., Sun, B., Zhao, X., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138234 · Cited by 96
AIM2-driven inflammasome activation in heart failure
Onódi, Z., Ruppert, M., Kucsera, D., Sayour, A. A., Tóth, V. É., Koncsos, G., Novák, J., Brenner, G. B., Makkos, A., Baranyai, T., et al. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab202 · Cited by 95
Exploration of Pattern Recognition Receptor Agonists as Candidate Adjuvants
Ong, G. H., Lian, B. S. X., Kawasaki, T., & Kawai, T. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.745016 · Cited by 100
Crossed Pathways for Radiation-Induced and Immunotherapy-Related Lung Injury
Zhang, Z., Zhou, J., Verma, V., Liu, X., Wu, M., Yu, J., & Chen, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.774807 · Cited by 97
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
Restoration of absent in melanoma 2 (AIM2) induces G2/M cell cycle arrest and promotes invasion of colorectal cancer cells
Patsos, G., Germann, A., Gebert, J. F., & Dihlmann, S. (2009) · International Journal of Cancer · doi:10.1002/ijc.24905 · Cited by 95
Regulation of NLRP3 and AIM2 inflammasome gene expression levels in gingival fibroblasts by oral biofilms
Bostancı, N., Meier, A., Guggenheim, B., & Belibasakis, G. N. (2011) · Cellular Immunology · doi:10.1016/j.cellimm.2011.04.002 · Cited by 95
Differential Roles for the Interferon-Inducible IFI16 and AIM2 Innate Immune Sensors for Cytosolic DNA in Cellular Senescence of Human Fibroblasts
Duan, X., Ponomareva, L. V., Veeranki, S., Panchanathan, R., Dickerson, E., & Choubey, D. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-10-0565 · Cited by 95
Macrophage CGI-58 Deficiency Activates ROS-Inflammasome Pathway to Promote Insulin Resistance in Mice
Miao, H., Ou, J., Ma, Y., Guo, F., Yang, Z., Wiggins, M., Liu, C., Song, W., Han, X., Wang, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.047 · Cited by 94
Sox2 functions as a sequence-specific DNA sensor in neutrophils to initiate innate immunity against microbial infection
Xia, P., Wang, S., Ye, B., Du, Y., Huang, G., Zhu, P., & Fan, Z. (2015) · Nature Immunology · doi:10.1038/ni.3117 · Cited by 94
AIM2 promotes the development of non-small cell lung cancer by modulating mitochondrial dynamics
Qi, M., Dai, D., Liu, J., Li, Z., Liang, P., Wang, Y., Lu, C., Zhan, Y., An, Z., Song, Y., et al. (2020) · Oncogene · doi:10.1038/s41388-020-1176-9 · Cited by 96
The role of the microbiome and the NLRP3 inflammasome in the gut and lung
Donovan, C., Liu, G., Shen, S., Marshall, J. E., Kim, R., Alemao, C. A., Budden, K. F., Choi, J. P., Kohonen‐Corish, M. R. J., El-Omar, E. M., et al. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr0720-472rr · Cited by 95
Chemical probing reveals insights into the signaling mechanism of inflammasome activation
Gong, Y., Wang, X., Wang, J., Yang, Z., Li, S., Yang, J., Liu, L., Lei, X., & Shao, F. (2010) · Cell Research · doi:10.1038/cr.2010.135 · Cited by 96
Extracellular self-DNA as a damage-associated molecular pattern (DAMP) that triggers self-specific immunity induction in plants
Durán-Flores, D., & Heil, M. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2017.10.010 · Cited by 94
Interactions of the Antiviral Factor Interferon Gamma-Inducible Protein 16 (IFI16) Mediate Immune Signaling and Herpes Simplex Virus-1 Immunosuppression
Diner, B. A., Lum, K. K., Javitt, A., & Cristea, I. M. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047068 · Cited by 93
Inflammasome-mediated innate immunity in Alzheimer’s disease
Venegas, C., & Heneka, M. T. (2019) · The FASEB Journal · doi:10.1096/fj.201900439 · Cited by 93
The expression of NLRP3, NLRP1 and AIM2 in the gingival tissue of periodontitis patients: RT-PCR study and immunohistochemistry
Xue, F., Shu, R., & Xie, Y. (2015) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2015.03.005 · Cited by 93
The Trinity of cGAS, TLR9, and ALRs Guardians of the Cellular Galaxy Against Host-Derived Self-DNA
Kumar, V. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.624597 · Cited by 95
Activation of inflammasomes in adipose tissue of women with gestational diabetes
Lappas, M. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.09.011 · Cited by 96
Strong induction of AIM 2 expression in human epidermis in acute and chronic inflammatory skin conditions
de Koning, H. D., Bergboer, J. G. M., van den Bogaard, E. H. J., van Vlijmen‐Willems, I. M. J. J., Rodijk‐Olthuis, D., Simon, A., Zeeuwen, P. L. J. M., & Schalkwijk, J. (2012) · Experimental Dermatology · doi:10.1111/exd.12037 · Cited by 93
Regulation of inflammasomes by ubiquitination
Bednash, J. S., & Mallampalli, R. K. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.15 · Cited by 95
Mycobacterium tuberculosis and the host cell inflammasome: a complex relationship
Briken, V., Ahlbrand, S. E., & Shah, S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00062 · Cited by 92
Immunomodulatory Effects of Radiotherapy
Kumari, S., Mukherjee, S., Sinha, D., Abdisalaam, S., Krishnan, S., & Asaithamby, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218151 · Cited by 96
Interferon-Inducible Protein 16: Insight into the Interaction with Tumor Suppressor p53
Liao, J. C. C., Lam, R., Brázda, V., Duan, S., Ravichandran, M., Ma, J., Xiao, T., Tempel, W., Zuo, X., Wang, Y., et al. (2011) · Structure · doi:10.1016/j.str.2010.12.015 · Cited by 92
Improvement of DNA vaccination by adjuvants and sophisticated delivery devices: vaccine-platforms for the battle against infectious diseases
Grunwald, T., & Ulbert, S. (2015) · Clinical and Experimental Vaccine Research · doi:10.7774/cevr.2015.4.1.1 · Cited by 93
The functional interactome of PYHIN immune regulators reveals IFIX is a sensor of viral DNA
Diner, B. A., Li, T., Greco, T. M., Crow, M. S., Fuesler, J., Wang, J. P., & Cristea, I. M. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145808 · Cited by 95
The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments
Vajjhala, P. R., Lu, A. Z., Brown, D. L., Pang, S. W., Sagulenko, V., Sester, D. P., Cridland, S. O., Hill, J. M., Schroder, K., Stow, J. L., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.687731 · Cited by 94
A20 (Tnfaip3) Deficiency in Myeloid Cells Protects against Influenza A Virus Infection
Maelfait, J., Roose, K., Bogaert, P., Sze, M., Saelens, X., Pasparakis, M., Carpentier, I., Loo, G., & Beyaert, R. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002570 · Cited by 91
The Recombinant BCG Δ ureC::hly Vaccine Targets the AIM2 Inflammasome to Induce Autophagy and Inflammation
Saiga, H., Nieuwenhuizen, N. E., Gengenbacher, M., Koehler, A., Schuerer, S., Moura‐Alves, P., Wagner, I., Mollenkopf, H., Dorhoi, A., & Kaufmann, S. H. E. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu675 · Cited by 93
Inhibition of AIM2 inflammasome activation by a novel transcript isoform of IFI16
Wang, P., Ye, Z., Deng, J., Siu, K., Gao, W., Chaudhary, V., Cheng, Y., Fung, S., Yuen, K., Ho, T., et al. (2018) · EMBO Reports · doi:10.15252/embr.201845737 · Cited by 94
GLUT1-dependent glycolysis regulates exacerbation of fibrosis via AIM2 inflammasome activation
Cho, S. J., Moon, J., Nikahira, K., Yun, H. S., Harris, R. A., Hong, K. S., Huang, H., Choi, A. M. K., & Stout-Delgado, H. W. (2019) · Thorax · doi:10.1136/thoraxjnl-2019-213571 · Cited by 91
Caspase-1 Promiscuity Is Counterbalanced by Rapid Inactivation of Processed Enzyme
Walsh, J. G., Logue, S. E., Lüthi, A. U., & Martin, S. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225862 · Cited by 91
Sphingosine regulates the NLRP3‐inflammasome and IL‐1β release from macrophages
Luheshi, N., Giles, J. A., López‐Castejón, G., & Brough, D. (2011) · European Journal of Immunology · doi:10.1002/eji.201142079 · Cited by 91
Immune-Complexed Adenovirus Induce AIM2-Mediated Pyroptosis in Human Dendritic Cells
Eichholz, K., Bru, T., Tran, T. T. P., Fernandes, P., Welles, H. C., Mennechet, F. J. D., Manel, N., Alves, P. M., Perreau, M., & Kremer, E. J. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005871 · Cited by 93
Cathelicidin LL‐37: a defense molecule with a potential role in psoriasis pathogenesis
Dombrowski, Y., & Schauber, J. (2012) · Experimental Dermatology · doi:10.1111/j.1600-0625.2012.01459.x · Cited by 90
Glutathione Transferase Omega-1 Regulates NLRP3 Inflammasome Activation Through NEK7 Deglutathionylation
Hughes, M. M., Hooftman, A., Angiari, S., Tummala, P., Zasłona, Z., Runtsch, M. C., McGettrick, A. F., Sutton, C. E., Diskin, C., Rooke, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.072 · Cited by 94
Inflammasomes and Pyroptosis of Liver Cells in Liver Fibrosis
Gan, C., Cai, Q., Tang, C., & Gao, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.896473 · Cited by 94
Critical role for the AIM 2 inflammasome during acute CNS bacterial infection
Hanamsagar, R., Aldrich, A. L., & Kielian, T. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12669 · Cited by 90
Innate Immune Recognition of Yersinia pseudotuberculosis Type III Secretion
Auerbuch, V., Golenbock, D. T., & Isberg, R. R. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000686 · Cited by 91
Non-Inflammasome Forming NLRs in Inflammation and Tumorigenesis
Allen, I. C. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00169 · Cited by 94
The protein kinase PKR is critical for LPS‐induced iNOS production but dispensable for inflammasome activation in macrophages
He, Y., Franchi, L., & Núñez, G. (2013) · European Journal of Immunology · doi:10.1002/eji.201243187 · Cited by 91
Down-regulation of NLRP3 inflammasome in gingival fibroblasts by subgingival biofilms: Involvement of Porphyromonas gingivalis
Belibasakis, G. N., Guggenheim, B., & Bostancı, N. (2012) · Innate Immunity · doi:10.1177/1753425912444767 · Cited by 89
BOT-4-one attenuates NLRP3 inflammasome activation: NLRP3 alkylation leading to the regulation of its ATPase activity and ubiquitination
Shim, D.-W., Shin, W.-Y., Yu, S., Kim, B.-H., Ye, S.-K., Koppula, S., Won, H., Kang, T., & Lee, K.-H. (2017) · Scientific Reports · doi:10.1038/s41598-017-15314-8 · Cited by 91
The Regulation and Modification of GSDMD Signaling in Diseases
Li, Z., Ji, S., Jiang, M., Xu, Y., & Zhang, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.893912 · Cited by 95
Cryo-EM structure of ASC-CARD filament
Li, Y., Fu, T., & Lu, A. Z. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6n1h/pdb · Cited by 89
Cytosolic surveillance and antiviral immunity
Rathinam, V. A. K., & Fitzgerald, K. A. (2011) · Current Opinion in Virology · doi:10.1016/j.coviro.2011.11.004 · Cited by 89
Self-citation
Dextran sodium sulfate potentiates NLRP3 inflammasome activation by modulating the KCa3.1 potassium channel in a mouse model of colitis
Zeng, B., Huang, Y., Chen, S., Xu, R., Xu, L., Qiu, J.-H., Shi, F., Liu, S., Zha, Q., Ouyang, D., et al. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00891-0 · Cited by 89
The inflammasome: in memory of Dr. Jurg Tschopp
Dagenais, M., Skeldon, A. M., & Saleh, M. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.159 · Cited by 92
Pyrin Critical to Macrophage IL-1β Response to Francisella Challenge
Gavrilin, M. A., Mitra, S., Seshadri, S., Nateri, J., Berhe, F., Hall, M. W., & Wewers, M. D. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803073 · Cited by 88
Molecular Mechanism for p202-Mediated Specific Inhibition of AIM2 Inflammasome Activation
Yin, Q., Sester, D. P., Tian, Y., Hsiao, Y., Lu, A. Z., Cridland, J. A., Sagulenko, V., Thygesen, S. J., Choubey, D., Hornung, V., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.024 · Cited by 87
Self-citation
Clinical reviews in allergy and immunology
Leung, D. Y. M., Ledford, D. K., Wechsler, M. E., Fulkerson, P. C., Bochner, B. S., Gauvreau, G. M., Gleich, G. J., Henkel, T., Kolbeck, R., Mathur, S. K., et al. (2012) · Cited by 87
Effect and Regulation of the NLRP3 Inflammasome During Renal Fibrosis
Zhang, H., & Wang, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00379 · Cited by 87
Inflammasomes in Common Immune-Related Skin Diseases
Tang, L., & Zhou, F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00882 · Cited by 89
Activation and Function of NLRP3 Inflammasome in Bone and Joint-Related Diseases
Murakami, T., Nakaminami, Y., Takahata, Y., Hata, K., & Nishimura, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105365 · Cited by 89
Dissection of a type I interferon pathway in controlling bacterial intracellular infection in mice
Lippmann, J., Müller, H. C., Naujoks, J., Tabeling, C., Shin, S., Witzenrath, M., Hellwig, K., Kirschning, C. J., Taylor, G. A., Barchet, W., et al. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01646.x · Cited by 94
Polymorphisms in Inflammasome' Genes and Susceptibility to HIV-1 Infection
Pontillo, A., Oshiro, T. M., Girardelli, M., Kamada, A. J., Crovella, S., & Duarte, A. J. S. (2012) · JAIDS Journal of Acquired Immune Deficiency Syndromes · doi:10.1097/qai.0b013e3182392ebe · Cited by 87
A cGAS-Independent STING/IRF7 Pathway Mediates the Immunogenicity of DNA Vaccines
Suschak, J. J., Wang, S., Fitzgerald, K. A., & Lu, S. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1501836 · Cited by 87
Self-citation
Inflammatory Caspases in Innate Immunity and Inflammation
Yazdi, A. S., Guarda, G., D’Ombrain, M. C., & Drexler, S. K. (2010) · Journal of Innate Immunity · doi:10.1159/000283688 · Cited by 87

Authors: Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A.
Affiliations: University of Massachusetts Chan Medical School (US)
Pfizer (United States) (US)
Corresponding author: Hornung, Veit
Fitzgerald, Katherine A.
ORCID: Hornung, Veit
Ablasser, Andrea
Horvath, Gabor
Latz, Eicke
Fitzgerald, Katherine A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2009-01-21
Volume: 458
Issue: 7237
Pages: 514-518
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature07725
PMC: PMC2726264
OpenAlex: W2042816890
Cited by: 2,627
References: 30
Citations by year: 2026: 108 · 2025: 164 · 2024: 187 · 2023: 152 · 2022: 168 · 2021: 162 · 2020: 158 · 2019: 146 · 2018: 142 · 2017: 137 · 2016: 142 · 2015: 144 · 2014: 147 · 2013: 168 · 2012: 140
FWCI: 66.64
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
MPG.PuRe (Max Planck Society) (submittedVersion)
Funders: National Institute of Allergy and Infectious Diseases (AI065483, R01AI067497, R37AI067497, AI-067497, R01AI065483, R56AI067497)
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: AIM2, cytosolic DNA sensing, inflammasome, caspase-1 activation, ASC, pyrin domain, double-stranded DNA, vaccinia virus, NF-κB activation, innate immunity, autoinflammation, autoimmunity, IL-1β, IL-18
MeSH terms: Animals, Cell Line, Cytoskeletal Proteins, Cytosol, DNA, DNA-Binding Proteins, Enzyme Activation, Humans, Inflammation, Nuclear Proteins, Poly dA-dT, Protein Binding, Vaccinia virus, Cell Death, Caspase 1, Apoptosis Regulatory Proteins, Mice, CARD Signaling Adaptor Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks