AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrity
Open accessAbstract
Significance: Inflammasomes are cellular sensors of harmful situations such as the presence of microbes or alterations in cellular homeostasis. Upon activation, inflammasomes trigger the proteolytic maturation and release of inflammatory cytokines to initiate immune and repair responses. The assembly of inflammasome relies on a diverse repertoire of sensor proteins that can detect specific stimuli. For example, the AIM2 inflammasome is activated by the presence of microbial DNA within the cytosol. In this paper, alterations of the nuclear envelope integrity are found to cause the exposure of nuclear DNA in the cytosol to promote the activation of the AIM2 inflammasome. Nuclear envelope stress can therefore directly engage innate immune sensors to elicit inflammation.
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
Cites
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?
CytoDNA species share similar signaling pathways, most prominently the cGAS-STING pathway, although mtDNA, MN, and other DNA damage-associated DNA fragments are thought to also activate the AIM2 and NLRP3 inflammasome pathway.
“Third, cytoDNA species share similar signaling pathways, most prominently the cGAS-STING pathway, although mtDNA, MN, and other DNA damage-associated DNA fragments are thought to also activate the AIM2 and NLRP3 inflammasome pathway (Di Micco et al., 2016; Motwani and Fitzgerald, 2017; Zhong et al., 2018).”
From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Di Micco et al., 2016
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works
Origin and physiological roles of inflammation
Medzhitov, R. (2008) · Nature · doi:10.1038/nature07201 · Cited by 6,618 · see citing works
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066 · see citing works
Self-citationAndromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,350 · see citing works
Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326 · see citing works
Self-citationImproved vectors and genome-wide libraries for CRISPR screening
Sanjana, N. E., Shalem, O., & Zhang, F. (2014) · Nature Methods · doi:10.1038/nmeth.3047 · Cited by 5,239 · see citing works
Inflammasomes: mechanism of action, role in disease, and therapeutics
Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340 · see citing works
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627 · see citing works
Mechanisms and Functions of Inflammasomes
Lamkanfi, M., & Dixit, V. M. (2014) · Cell · doi:10.1016/j.cell.2014.04.007 · Cited by 2,521 · see citing works
Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167 · see citing works
AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831 · see citing works
Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., & Mann, M. (1996) · Nature · doi:10.1038/379466a0 · Cited by 1,674 · see citing works
Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445 · see citing works
Self-citationInflammatory networks during cellular senescence: causes and consequences.
Freund, A., Orjalo, A. V., Desprez, P.-Y., & Campisi, J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.03.003 · Cited by 1,354 · see citing works
The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
Rathinam, V. A. K., Jiang, Z., Waggoner, S. N., Sharma, S., Cole, L. E., Waggoner, L., Vanaja, S. K., Monks, B. G., Ganesan, S., Latz, E., et al. (2010) · Nature Immunology · doi:10.1038/ni.1864 · Cited by 1,331 · see citing works
Nuclear envelope rupture and repair during cancer cell migration
Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318 · see citing works
Loss of a-Type Lamin Expression Compromises Nuclear Envelope Integrity Leading to Muscular Dystrophy
Sullivan, T. L., Escalante‐Alcalde, D., Bhatt, H., Anver, M. R., BHAT, N. K., Nagashima, K., Stewart, C. L., & Burke, B. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.913 · Cited by 1,197 · see citing works
Goldman, R. D., Shumaker, D. K., Erdos, M. R., Eriksson, M., Goldman, A. E., Gordon, L. B., Gruenbaum, Y., Khuon, S., Mendez, M., Varga, R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402943101 · Cited by 1,103 · see citing works
Bürckstümmer, T., Baumann, C., Blüml, S., Dixit, E., Dürnberger, G., Jahn, H., Planyavsky, M., Bilban, M., Colinge, J., Bennett, K. L., et al. (2009) · Nature Immunology · doi:10.1038/ni.1702 · Cited by 1,091 · see citing works
Nuclear structure in cancer cells
Zink, D., Fischer, A. H., & Nickerson, J. A. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1430 · Cited by 1,070 · see citing works
Fernandes-Alnemri, T., Wu, J., Yu, J.-W., Datta, P., Miller, B., Jankowski, W., Rosenberg, S., Zhang, J., & Alnemri, E. S. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402194 · Cited by 1,026 · see citing works
The cGAS-cGAMP-STING Pathway of Cytosolic DNA Sensing and Signaling
Cai, X., Chiu, Y., & Chen, Z. J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.040 · Cited by 995 · see citing works
Cyclic GMP-AMP Synthase Is an Innate Immune Sensor of HIV and Other Retroviruses
Gao, D., Wu, J., Wu, Y.-T., Du, F., Aroh, C., Yan, N., Sun, L., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1240933 · Cited by 986 · see citing works
ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death
Raab, M., Gentili, M., Belly, H. D., Thiam, H. R., Vargas, P., Jiménez, A. J., Lautenschläger, F., Voituriez, R., Lennon‐Duménil, A., Manel, N., et al. (2016) · Science · doi:10.1126/science.aad7611 · Cited by 946 · see citing works
Pan-viral specificity of IFN-induced genes reveals new roles for cGAS in innate immunity
Schoggins, J. W., MacDuff, D. A., Imanaka, N., Gainey, M. D., Shrestha, B., Eitson, J. L., Mar, K. B., Richardson, R. B., Ratushny, A. V., Litvak, V., et al. (2014) · Nature · doi:10.1038/nature12862 · Cited by 896 · see citing works
Lerner, A. G., Upton, J.-P., Praveen, P. V. K., Ghosh, R., Nakagawa, Y., Igbaria, A., Shen, S., Nguyen, V. Q., Backes, B. J., Heiman, M., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.007 · Cited by 848 · see citing works
HIN-200 Proteins Regulate Caspase Activation in Response to Foreign Cytoplasmic DNA
Roberts, T. L., Idris, A., Dunn, J. A., Kelly, G., Burnton, C. M., Hodgson, S., Hardy, L., Garceau, V., Sweet, M. J., Ross, I. L., et al. (2009) · Science · doi:10.1126/science.1169841 · Cited by 830 · see citing works
Paludan, S. R., & Bowie, A. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.004 · Cited by 764 · see citing works
Shi, H., Wang, Y., Li, X., Zhan, X., Tang, M., Fina, M., Su, L., Pratt, D., Bu, C. H., Hildebrand, S., et al. (2015) · Nature Immunology · doi:10.1038/ni.3333 · Cited by 751 · see citing works
Converging roles of caspases in inflammasome activation, cell death and innate immunity
Man, S. M., & Kanneganti, T. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.7 · Cited by 701 · see citing works
Oslowski, C. M., Hara, T., O’Sullivan-Murphy, B., Kanekura, K., Lu, S., Hara, M., Ishigaki, S., Zhu, L. J., Hayashi, E., Hui, S. T. Y., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.005 · Cited by 678 · see citing works
The pINDUCER lentiviral toolkit for inducible RNA interference in vitro and in vivo
Meerbrey, K. L., Hu, G., Kessler, J. D., Roarty, K. P., Li, M. Z., Fang, J. E., Herschkowitz, J. I., Burrows, A. E., Ciccia, A., Sun, T., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019736108 · Cited by 667 · see citing works
Jin, T., Perry, A., Jiang, J., Smith, P. T., Curry, J. A., Unterholzner, L., Jiang, Z., Horvath, G. L., Rathinam, V. A. K., Johnstone, R. W., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.014 · Cited by 571 · see citing works
Cai, X., Chen, J., Xu, H., Liu, S., Jiang, Q., Halfmann, R., & Chen, Z. J. (2014) · Cell · doi:10.1016/j.cell.2014.01.063 · Cited by 567 · see citing works
IFI16 DNA Sensor Is Required for Death of Lymphoid CD4 T Cells Abortively Infected with HIV
Monroe, K. M., Yang, Z., Johnson, J. R., Geng, X., Doitsh, G., Krogan, N. J., & Greene, W. C. (2014) · Science · doi:10.1126/science.1243640 · Cited by 511 · see citing works
Mechanisms of inflammasome activation: recent advances and novel insights
Vanaja, S. K., Rathinam, V. A. K., & Fitzgerald, K. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.009 · Cited by 499 · see citing works
Schmid-Burgk, J. L., Chauhan, D., Schmidt, T., Ebert, T. S., Reinhardt, J., Endl, E., & Hornung, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.c115.700492 · Cited by 450 · see citing works
Bronner, D. N., Abuaita, B. H., Chen, X., Fitzgerald, K. A., Núñez, G., He, Y. O., Yin, X., & O’Riordan, M. X. (2015) · Immunity · doi:10.1016/j.immuni.2015.08.008 · Cited by 438 · see citing works
Mechanisms of NOD-like Receptor-Associated Inflammasome Activation
Wen, H., Miao, E. A., & Ting, J. P. ‐. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.037 · Cited by 415 · see citing works
ER stress induces NLRP3 inflammasome activation and hepatocyte death
Lebeaupin, C., Proïcs, E., de Bieville, C.-H. D., Rousseau, D., Bonnafous, S., Patouraux, S., Adam, G., Lavallard, V., Rovère, C., Thuc, O. L., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.248 · Cited by 400 · see citing works
Mitochondria: diversity in the regulation of the NLRP3 inflammasome
Gurung, P., Lukens, J. R., & Kanneganti, T.-D. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.11.008 · Cited by 393 · see citing works
Man, S. M., Karki, R., & Kanneganti, T. (2016) · European Journal of Immunology · doi:10.1002/eji.201545839 · Cited by 354 · see citing works
Meunier, É., Wallet, P., Dreier, R. F., Costanzo, S., Anton, L., Rühl, S., Dussurgey, S., Dick, M. S., Kistner, A., Mélanie, R., et al. (2015) · Nature Immunology · doi:10.1038/ni.3119 · Cited by 353 · see citing works
Self-citationCritical Role for the DNA Sensor AIM2 in Stem Cell Proliferation and Cancer
Man, S. M., Zhu, Q., Zhu, L., Liu, Z., Karki, R., Malik, A., Sharma, D., Li, L., Malireddi, R. K. S., Gurung, P., et al. (2015) · Cell · doi:10.1016/j.cell.2015.06.001 · Cited by 331 · see citing works
ER stress activates the NLRP3 inflammasome via an UPR-independent pathway
Menu, P., Mayor, A., Zhou, R., Tardivel, A., Ichijo, H., Mori, K., & Tschopp, J. (2012) · Cell Death and Disease · doi:10.1038/cddis.2011.132 · Cited by 321 · see citing works
Self-citationGills, J. J., LoPiccolo, J., Tsurutani, J., Shoemaker, R. H., Best, C. J. M., Abu-Asab, M. S., Borojerdi, J. P., Warfel, N. A., Gardner, E. R., Danish, M., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-0161 · Cited by 320 · see citing works
Inflammasome-independent role of AIM2 in suppressing colon tumorigenesis via DNA-PK and Akt
Wilson, J. E., Petrucelli, A., Chen, L., Koblansky, A. A., Truax, A. D., Oyama, Y., Rogers, A. B., Brickey, W. J., Wang, Y., Schneider, M., et al. (2015) · Nature Medicine · doi:10.1038/nm.3908 · Cited by 293 · see citing works
Sensing damage by the NLRP3 inflammasome
Leemans, J. C., Cassel, S. L., & Sutterwala, F. S. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01043.x · Cited by 281 · see citing works
Osorio, F. G., Bárcena, C., Soria-Valles, C., Ramsay, A. J., de Carlos, F., Cobo, J., Fueyo, A., Freije, J. M. P., & López-Otín, C. (2012) · Genes & Development · doi:10.1101/gad.197954.112 · Cited by 276 · see citing works
Dynamic Disruptions in Nuclear Envelope Architecture and Integrity Induced by HIV-1 Vpr
de Noronha, C. M. C., Sherman, M. P., Lin, H. W., Cavrois, M., Moir, R. D., Goldman, R. D., & Greene, W. C. (2001) · Science · doi:10.1126/science.1063957 · Cited by 275 · see citing works
Vos, W. H. D., Houben, F., Kamps, M. A. F., Malhas, A. N., Verheyen, F., Cox, J., Manders, E. M. M., Verstraeten, V. L. R. M., Steensel, M. A. M. V., Marcelis, C., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr344 · Cited by 271 · see citing works
Broken nuclei – lamins, nuclear mechanics, and disease
Davidson, P. M., & Lammerding, J. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.11.004 · Cited by 268 · see citing works
Lamins at the crossroads of mechanosignalingPreprint
Osmanagic‐Myers, S., Dechat, T., & Foisner, R. (2015) · Genes & Development · doi:10.1101/gad.255968.114 · Cited by 230 · see citing works
Caron, M., Auclair, M., Sterlingot, H., Kornprobst, M., & Capeau, J. (2003) · AIDS · doi:10.1097/00002030-200311210-00005 · Cited by 176 · see citing works
Antagonism of the STING Pathway via Activation of the AIM2 Inflammasome by Intracellular DNA
Corrales, L. P., Woo, S., Williams, J. B., McWhirter, S. M., Dubensky, T. W., & Gajewski, T. F. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1502538 · Cited by 150 · see citing works
The Posttranslational Processing of Prelamin A and Disease
Davies, B. S. J., Fong, L. G., Yang, S. H., Coffinier, C., & Young, S. G. (2009) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082908-150150 · Cited by 139 · see citing works
Coffinier, C., Hudon, S. E., Farber, E., Chang, S. Y., Hrycyna, C. A., Young, S. G., & Fong, L. G. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704212104 · Cited by 130 · see citing works
Self-citationRapid Inflammasome Activation following Mucosal SIV Infection of Rhesus Monkeys
Barouch, D. H., Ghneim, K., Bosche, W. J., Li, Y., Berkemeier, B., Hull, M. J., Bhattacharyya, S., Cameron, M. J., Liu, J., Smith, K. M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.021 · Cited by 127 · see citing works
Breaching the nuclear envelope in development and disease
Hatch, E. M., & Hetzer, M. W. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201402003 · Cited by 116 · see citing works
Baum, R., Sharma, S., Carpenter, S. B., Li, Q., Busto, P., Fitzgerald, K. A., Marshak‐Rothstein, A., & Gravallese, E. M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1402573 · Cited by 104 · see citing works
Human ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severity
Barrowman, J., Wiley, P. A., Hudon, S. E., Hrycyna, C. A., & Michaelis, S. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds233 · Cited by 104 · see citing works
Self-citationBiochemical Studies of Zmpste24-deficient Mice
Leung, G. K. C., Schmidt, W. K., Bergö, M. O., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102908200 · Cited by 97 · see citing works
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 97 · see citing works
Dreskin, S. C., Thomas, G. W., Dale, S. N., & Heasley, L. E. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.9.5646 · Cited by 95 · see citing works
Exploring the pathophysiology behind the more common genetic and acquired lipodystrophies
Nolis, T. (2013) · Journal of Human Genetics · doi:10.1038/jhg.2013.107 · Cited by 87 · see citing works
Burning Down the House: Cellular Actions during Pyroptosis
LaRock, C. N., & Cookson, B. T. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003793 · Cited by 77 · see citing works
Gantt, S. M., Casper, C., & Ambinder, R. F. (2013) · Current Opinion in Oncology · doi:10.1097/cco.0b013e328363dfee · Cited by 74 · see citing works
Prokocimer, M., Margalit, A., & Gruenbaum, Y. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.02.016 · Cited by 70 · see citing works
Nuclear envelope-related lipodystrophies
Guénantin, A.-C., Briand, N., Bidault, G., Afonso, P., Béréziat, V., Vatier, C., Lascols, O., Caron, M., Capeau, J., & Vigouroux, C. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.12.015 · Cited by 67 · see citing works
NLRP3 and IL ‐1 β in macrophages as critical regulators of metabolic diseases
McGettrick, A. F., & O'Neill, L. A. J. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12169 · Cited by 66 · see citing works
Coffinier, C., Hudon, S. E., Lee, R., Farber, E., Nobumori, C., Miner, J. H., Andres, D., Spielmann, H. P., Hrycyna, C. A., Fong, L. G., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709629200 · Cited by 64 · see citing works
Self-citationCattin, M., Bertrand, A., Schlossarek, S., Bihan, M. L., Jensen, S. S., Neuber, C., Crocini, C., Maron, S., Lainé, J., Mougenot, N., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt172 · Cited by 64 · see citing works
Schneider, D. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00764-x · Cited by 62 · see citing works
Gassart, A. D., Bujisic, B., Zaffalon, L., Decosterd, L. A., Micco, A. D., Frera, G., Tallant, R., & Martinon, F. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514076113 · Cited by 60 · see citing works
Self-citationMorikawa, K., Gouttenoire, J., Hernandez, C., et al. (2013) · Hepatology · doi:10.1002/hep.26671 · Cited by 45 · see citing works
Ford, J., Cornforth, D., Hoggard, P. G., et al. (2004) · Antiviral Therapy · doi:10.1177/135965350400900101 · Cited by 44 · see citing works
Hennessy, M., Clarke, S., Spiers, P., et al. (2004) · Antiviral Therapy · doi:10.1177/135965350400900103 · Cited by 38 · see citing works
Epigenetic regulation of ASC/TMS1 expression: potential role in apoptosis and inflammasome function
Salminen, A., Kauppinen, A., Hiltunen, M., & Kaarniranta, K. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1524-9 · Cited by 35 · see citing works
Chang, S. Y., Hudon, S. E., Yang, S. H., Jung, H.-J., Lee, J. M., Farber, E., Subramanian, T., Andres, D., Spielmann, H. P., Hrycyna, C. A., et al. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m026161 · Cited by 21 · see citing works
Self-citationUsing an EGFPmeter to Evaluate the Lentiviral Vector Production: Tricks and Traps
Bagnis, C., Bailly, P., & Chapel‐Fernandes, S. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-559-6_10 · Cited by 18 · see citing works
Perrin, S., Cremer, J., Zaegel‐Faucher, O., Reynes, J., Dellamonica, P., Micallef, J., Solas, C., Lacarelle, B., Stretti, C., Kaspi, É., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053035 · Cited by 15 · see citing works
Dombrowski, Y., Koglin, S., & Schauber, J. (2012) · Experimental Dermatology · doi:10.1111/j.1600-0625.2012.01466.x · Cited by 8 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The <scp>AIM</scp>2 inflammasome: Sensor of pathogens and cellular perturbations
Lugrin, J., & Martinon, F. (2018) · Immunological Reviews · doi:10.1111/imr.12618 · Cited by 333 · see citing works
Self-citationMitochondria, Oxidative Stress and Innate Immunity
Chen, Y., Zhou, Z., & Min, W. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01487 · Cited by 315 · see citing works
“During Nelfinavir treatment, an HIV aspartyl protease, AIM2 could also be activated upon DNA release from the nucleus with a compromised nuclear envelope integrity (Di Micco et al., 2016).”
BackgroundCytoplasmic DNA: sources, sensing, and role in aging and disease
Miller, K. N., Victorelli, S. G., Salmonowicz, H., Dasgupta, N., Liu, T., Passos, J. F., & Adams, P. D. (2021) · Cell · doi:10.1016/j.cell.2021.09.034 · Cited by 288 · see citing works
Cytosolic DNA Sensing in Organismal Tumor Control
Vanpouille-Box, C., Demaria, S., Formenti, S. C., & Galluzzi, L. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.05.013 · Cited by 250 · see citing works
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 · see citing works
Inflammation: Is It a Healer, Confounder, or a Promoter of Cardiometabolic Risks?
Tate, A. R., & Rao, G. H. R. (2024) · Biomolecules · doi:10.3390/biom14080948 · Cited by 42 · see citing works
González‐Dominguez, A., Montañez, R., Castejón‐Vega, B., Nuñez‐Vasco, J., Lendines‐Cordero, D., Wang, C., Mbalaviele, G., Navarro‐Pando, J. M., Alcocer‐Gómez, E., & Cordero, M. D. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202114012 · Cited by 32 · see citing works
- Authors
- Di Micco, A., Frera, G., Lugrin, J., Jamilloux, Y., Hsu, E.-T., Tardivel, A., De Gassart, A., Zaffalon, L., Bujisic, B., Siegert, S., Quadroni, M., Broz, P., Henry, T., Hrycyna, C. A., & Martinon, F.
- Affiliations
- Department of Biochemistry, University of Lausanne, Epalinges 1066, Switzerland;
- University of Lausanne (CH)
- Inserm (FR)
- Purdue University West Lafayette (US)
- Focal Area Infection Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland;
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2016-07-26
- Volume
- 113
- Issue
- 32
- Pages
- E4671-80
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4987819
- OpenAlex
- W2477702703
- Cited by
- 143
- References
- 82
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 18 · 2023: 11 · 2022: 18 · 2021: 21 · 2020: 15 · 2019: 16 · 2018: 15 · 2017: 15
- FWCI
- 7.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- HAL (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion, other-oa)
- Funders
- EC | European Research Council (281996)
- 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 inflammasome, nelfinavir, nuclear envelope integrity, cytosolic DNA sensing, IL-1β, IL-1 signaling, HIV protease inhibitors, inflammasome activation
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, DNA, Mice, Inbred C57BL, Nuclear Envelope, Receptors, Interleukin-1, Nelfinavir, Caspase 1, Mice, CARD Signaling Adaptor Proteins, Interleukin-1beta, Inflammasomes
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