The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
IRGB10 Liberates Bacterial Ligands for Sensing by the AIM2 and Caspase-11-NLRP3 Inflammasomes
Open accessAbstract
The inflammasome is an intracellular signaling complex, which on recognition of pathogens and physiological aberration, drives activation of caspase-1, pyroptosis, and the release of the pro-inflammatory cytokines IL-1β and IL-18. Bacterial ligands must secure entry into the cytoplasm to activate inflammasomes; however, the mechanisms by which concealed ligands are liberated in the cytoplasm have remained unclear. Here, we showed that the interferon-inducible protein IRGB10 is essential for activation of the DNA-sensing AIM2 inflammasome by Francisella novicida and contributed to the activation of the LPS-sensing caspase-11 and NLRP3 inflammasome by Gram-negative bacteria. IRGB10 directly targeted cytoplasmic bacteria through a mechanism requiring guanylate-binding proteins. Localization of IRGB10 to the bacterial cell membrane compromised bacterial structural integrity and mediated cytosolic release of ligands for recognition by inflammasome sensors. Overall, our results reveal IRGB10 as part of a conserved signaling hub at the interface between cell-autonomous immunity and innate immune sensing pathways.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“(3) the expression of guanylate-binding proteins and an IFN-inducible GTPase commonly known as IRGB10 (official name Gm12250), which increase cytosolic LPS levels by mediating the lysis of vacuoles containing Gram-negative bacteria [646–648].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [648]
Citations
Cites
Krogh, A., Larsson, B., von Heijne, G., & Sonnhammer, E. L. L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4315 · Cited by 12,654
WebLogo: A Sequence Logo Generator: Figure 1Preprint
Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,418
Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659
Phylogeny.fr: robust phylogenetic analysis for the non-specialist
Dereeper, A., Guignon, V., Blanc, G., Audic, S., Buffet, S., Chevenet, F., Dufayard, J.-F., Guindon, S., Lefort, V., Lescot, M., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn180 · Cited by 4,700
Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686
Wang, H., Yang, H., Shivalila, C. S., Dawlaty, M. M., Cheng, A. W., Zhang, F., & Jaenisch, R. (2013) · Cell · doi:10.1016/j.cell.2013.04.025 · Cited by 3,495
Activation and regulation of the inflammasomes
Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884
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
Mechanisms and Functions of Inflammasomes
Lamkanfi, M., & Dixit, V. M. (2014) · Cell · doi:10.1016/j.cell.2014.04.007 · Cited by 2,579
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 311
Lin, J., Wang, J., Fang, J., Li, M., Xu, S., Little, P. J., Zhang, D., & Liu, Z. (2024) · British Journal of Pharmacology · doi:10.1111/bph.16355 · Cited by 20
Impaired interferon-γ signaling promotes the development of silicosis
Peng, Z., Duan, M., Tang, Y., Wu, J., Zhao, K., Zhong, Y., He, Z., Meng, J., Chen, F., Xiao, X., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104647 · Cited by 17
Activation of the Innate Immune Receptors: Guardians of the Micro Galaxy
Nardo, D. D. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-5987-2_1 · Cited by 16
Symptomatology and microbiology of the gastrointestinal tract in post‐COVID conditions
Masir, M. N., & Shirvaliloo, M. (2022) · JGH Open · doi:10.1002/jgh3.12811 · Cited by 19
A potent NLRP3 inhibitor effective against both MCC950-sensitive and -resistant inflammation
Kim, W., Kim, S., Woo, H., Jojare, R. A., Mall, R., Nicotra, A., Py, B. F., Ngo, C., Man, S. M., Patel, C., et al. (2025) · Cell chemical biology · doi:10.1016/j.chembiol.2025.08.006 · Cited by 19
Self-citationTian, X., Liu, C., & Wang, Z. (2021) · International Endodontic Journal · doi:10.1111/iej.13636 · Cited by 16
Impairing Gasdermin D-mediated pyroptosis is protective against retinal degeneration
Sekar, R., Wooff, Y., Cioanca, A. V., Kurera, M., Ngo, C., Man, S. M., & Natoli, R. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02927-2 · Cited by 16
Self-citationOrganelle stress in NLRP3 inflammasome: a central mediator of neurodegenerative diseases
Jia, H., Ma, L., Liu, J., Gao, M., Liang, X., Zhang, F., Gao, Y., Liu, M., Jiang, W., Wei, M., et al. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00922-0 · Cited by 18
Parashar, K., Kopping, E. J., Frank, D. M., Sampath, V., Thanassi, D. G., & Carpino, N. (2017) · Infection and Immunity · doi:10.1128/iai.00406-17 · Cited by 14
Lupfer, C. R., Rippee‐Brooks, M. D., & Anand, P. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.10.001 · Cited by 17
Currey, N., Jahan, Z., Caldon, C. E., Tran, P. N., Benthani, F. A., Lacavalerie, P. D., Roden, D. L., Gloss, B., Campos, C., Bean, E. G., et al. (2019) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2019.01.009 · Cited by 13
Preventing NLRP3 inflammasome activation: Therapeutic atrategy and challenges in atopic dermatitis
Sun, Y., Zhou, Y., Peng, T., Huang, Y., Lü, H., Ying, X., Kang, M., Jiang, H., Wang, J., Zheng, J., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113696 · Cited by 14
Tana, F. L., Guimarães, E. S., Cerqueira, D. M., Campos, P. C., Gomes, M. T. R., Marinho, F. V., & Oliveira, S. C. (2021) · Cellular Microbiology · doi:10.1111/cmi.13375 · Cited by 13
Cell-autonomousToxoplasmakilling program requires Irgm2 but not its microbe vacuolar localization
Pradipta, A., Sasai, M., Motani, K., Su, J., Lee, Y., Kosako, H., & Yamamoto, M. (2021) · Life Science Alliance · doi:10.26508/lsa.202000960 · Cited by 13
Self-citationMechanism of Microbiota-Gut-Brain in Perimenopausal Depression: An Inflammatory Perspective
Yu, X., Zuo, Y., Yang, Y., Cheng, W., Shi, M., Cheng, L., Shao, Q., Xu, Y., & Chen, L. (2025) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2025.10011 · Cited by 12
The noncanonical inflammasome in health and disease
Cahoon, J. G., Yang, D., & Wang, P. (2022) · Infectious Medicine · doi:10.1016/j.imj.2022.09.001 · Cited by 12
Strategies of bacterial detection by inflammasomes
Jastrab, J. B., & Kagan, J. C. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.03.009 · Cited by 14
Liu, Q., Tan, Y., Zhang, Z., Tang, W., Han, L., Peng, K., Liu, M., & Tian, G. (2025) · Inflammation Research · doi:10.1007/s00011-024-01984-4 · Cited by 12
Marques-da-Silva, C., Schmidt-Silva, C., Bowers, C., Charles-Chess, N. A. E., Samuel, C., Shiau, J. C., Park, E., Yuan, Z., Kim, B.-H., Kyle, D. E., et al. (2025) · Cell Host & Microbe · doi:10.1016/j.chom.2025.03.008 · Cited by 12
Autophagy and Bacterial infections
Cadwell, K., Abraham, C., Bel, S., Chauhan, S., Coers, J., Colombo, M. I., Davis, J. R., Hofius, D., Nguyen, H. T. T., Ogawa, M., et al. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2542904 · Cited by 12
New concepts in Chlamydia induced inflammasome responses
Webster, S. J., & GOODALL, J. C. (2017) · Microbes and Infection · doi:10.1016/j.micinf.2017.11.011 · Cited by 11
Alqahtani, M., Ma, Z., Miller, J., Yu, J., Malik, M., & Bakshi, C. S. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1188112 · Cited by 10
Activation of inflammasomes and mechanisms for intracellular recognition of Listeria monocytogenes
Matsuda, Y., Yamauchi, H., & Hara, H. (2023) · Microbiology and Immunology · doi:10.1111/1348-0421.13091 · Cited by 11
Gao, Y., Yue, J., Ha, F., Wang, Y., Wang, R., Yang, X., Zhang, J., Liu, X., Zhang, Y., Han, T., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.97059 · Cited by 10
Valeva, S., Degabriel, M., Michal, F., Gay, G., Rohde, J. R., Randow, F., Lagrange, B., & Henry, T. (2023) · Pathogens and Disease · doi:10.1093/femspd/ftad005 · Cited by 10
Sepsis take-out: Inhibiting bacterial deliveries
Christgen, S. L., & Kanneganti, T. (2021) · Immunity · doi:10.1016/j.immuni.2021.02.010 · Cited by 9
Self-citationActivation and manipulation of inflammasomes and pyroptosis during bacterial infections
Bernard, E. M., & Brož, P. (2022) · Biochemical Journal · doi:10.1042/bcj20220051 · Cited by 10
Wei, Y., Li, W., Yang, S., Zhong, P., Bi, Y., & Tang, Y. (2022) · Bioengineered · doi:10.1080/21655979.2022.2073126 · Cited by 9
RetractedZou, Y., Wang, X., Xu, J., Wang, S., Li, S., Zhu, Y., & Wang, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113279 · Cited by 9
Collab or Cancel? Bacterial Influencers of Inflammasome Signaling
Herrmann, B. I., Grayczyk, J. P., & Brodsky, I. E. (2023) · Annual Review of Microbiology · doi:10.1146/annurev-micro-032521-024017 · Cited by 9
Huang, M., Zhan, C., Yang, B., Lu, Y., Yang, X., & Hou, J. L. (2023) · International Endodontic Journal · doi:10.1111/iej.14006 · Cited by 8
NLRP3 Inflammasome Activation Is Involved in Geniposide‐Induced Hepatotoxicity
Liu, Y., Liu, B., Shi, M., Ye, T., & Li, H. (2025) · Mediators of Inflammation · doi:10.1155/mi/4112856 · Cited by 8
Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
Ha, H. J., Chun, H. L., Lee, S. Y., Jeong, J., Kim, Y., & Park, H. H. (2021) · Communications Biology · doi:10.1038/s42003-020-01640-7 · Cited by 8
Kurmi, S., Doshi, G., & Parab, S. B. (2025) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273377780250505115039 · Cited by 7
Innate Immune Responses and Pulmonary Diseases
Liu, T., Liu, S., & Zhou, X. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-68748-9_4 · Cited by 8
Novel Insights into the Interaction between Enteropathogenic Bacteria, Pyroptosis and IBD
Bao, Z., Deng, Y., Qian, Z., & Zhuang, Y. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2907254 · Cited by 9
Christgen, S. L., Place, D. E., Zheng, M., Briard, B., Yamamoto, M., & Kanneganti, T. (2021) · European Journal of Immunology · doi:10.1002/eji.202149305 · Cited by 7
Self-citationBrown, H. M., Biering, S. B., Zhu, A. C., Choi, J., & Hwang, S. (2018) · BioEssays · doi:10.1002/bies.201700231 · Cited by 7
Role of non-canonical pyroptosis in sepsis and other inflammatory diseases.
Liang, H., Huang, Y., & Gao, Q. F. (2021) · PubMed Central · doi:10.11817/j.issn.1672-7347.2021.210174 · Cited by 8
Cui, W., Wang, T., & Feng, J. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1708319 · Cited by 6
Kim, J. K., Sapkota, A., Roh, T., & Jo, E. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108756 · Cited by 7
Roy, S., Wang, B., Roy, K., Tian, Y., Bhattacharya, M., Williams, S., & Yin, Q. (2025) · Communications Biology · doi:10.1038/s42003-025-07727-3 · Cited by 6
Cheng, Y., Chu, J., Limjunyawong, N., Chen, J., Ye, Y., Chen, K. H., Koylass, N., Sun, S., Dong, X., & Qiu, Z. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20250312 · Cited by 6
Parashar, K., & Carpino, N. (2020) · Immunity Inflammation and Disease · doi:10.1002/iid3.336 · Cited by 6
Francisella novicida Mutant XWK4 Triggers Robust Inflammasome Activation Favoring Infection
Guo, Y., Mao, R., Xie, Q., Cheng, X., Xu, T., Wang, X., Du, Y., & Qi, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.743335 · Cited by 6
Detection of Gasdermin Activation and Lytic Cell Death During Pyroptosis and Apoptosis
Demarco, B., Ramos, S., & Brož, P. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2449-4_14 · Cited by 6
Tessema, M. B., Tuipulotu, D. E., Oates, C. V. L., Brööks, A. G., Man, S. M., Londrigan, S. L., & Reading, P. C. (2023) · Immunology and Cell Biology · doi:10.1111/imcb.12627 · Cited by 6
Self-citationMeng, J., Wang, Q., Wang, H., Shen, X., Qin, T., Zhao, W. H., Li, H., & Yuan, Z. (2025) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(25)60970-8 · Cited by 5
Cellular signaling, molecular activation, and regulation of the AIM2 inflammasome
Lozano‐Ruiz, B., Tzoumpa, A., Picó, J., Huang, Y., & González-Navajas, J. M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91802-2.00027-x · Cited by 5
Guanylate-binding protein 5: a promising biomarker and therapeutic target
Lu, J., & Wang, W. (2025) · Infection and Immunity · doi:10.1128/iai.00026-25 · Cited by 6
Chan, F. H. M., Yeap, H. W., Liu, Z., Rosli, S. N., Low, K. E., Bonne, I., Wu, Y., Chong, S. Z., & Chen, K. W. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115216 · Cited by 3
The dual roles of human PYHIN family proteins in cancer: mechanisms and therapeutic implications
Zeng, S., Zhou, Z., Li, Y., Wu, D., Xiao, Q., & Peng, H. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1576674 · Cited by 3
Identification of specific molecular markers in severe heatstroke using transcriptomics techniques
Duan, Z., Wang, M., Zhou, Y.-C., Lu, J., Ma, Y., Xu, Y.-Z., Deng, J., Liu, H., & Chen, J. (2025) · International Journal of Legal Medicine · doi:10.1007/s00414-025-03634-8 · Cited by 3
Structural insights into GM4951 as a lipid droplet GTPase regulating hepatic lipid metabolism
Raj, R., Jiang, Y., Jha, R. K., Moresco, E. M. Y., Joshi, H., Zhang, Z., & Beutler, B. (2025) · Nature Communications · doi:10.1038/s41467-025-66253-2 · Cited by 3
Woo, H., Jang, Y., Kim, S., Kim, W., Zhang, F., Mall, R., Patel, C., Kurera, M., Ngo, C., Jiang, S., et al. (2026) · EMBO Molecular Medicine · doi:10.1038/s44321-026-00425-5 · Cited by 5
Self-citationInflammasome-Mediated Mechanisms Of Systemic Inflammation In COVID-19 And Asthma
Виткина, Т. И., Lobova, T. G., Bogomaz, T., & Korableva, E. V. (2024) · Russian Open Medical Journal · doi:10.15275/rusomj.2024.0201 · Cited by 3
Liu, S., & Zhang, J. (2025) · Journal of Cell Communication and Signaling · doi:10.1002/ccs3.70035 · Cited by 2
IRGB10 Exposes Bacteria’s Intimate Secrets
Hoß, F., Budden, C. F., & Latz, E. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.09.026 · Cited by 3
LncRNA29RIK in macrophages promotes LPS-mediated sensitivity to obesity
Wang, R., Gao, Y., Wang, Y., Zhang, Y., & Yang, R. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1574507 · Cited by 2
Cytosolic receptors and signaling in antifungal immunity
Khau, S., Désoubeaux, G., Si‐Tahar, M., Biquand, É., & Briard, B. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00627-6 · Cited by 3
Bai, L., Feng, C., Xu, X. L., Ge, W., Yang, Y., Liu, X., Li, Z., Qin, Z., Li, S., & Li, J. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115865 · Cited by 2
Cheng, Y., Mello-Vieira, J., Covarrubias‐Pinto, A., González, A., Kuncha, S. K., Kew, C., Zhang, K., Afzal, M. A., Diab, N., Borchert, S., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2669978 · Cited by 2
Upadhyay, S., Nagampalli, R., Resende, S., & Kanneganti, T. (2026) · Cell Research · doi:10.1038/s41422-026-01287-9 · Cited by 2
Self-citationWar on Viruses: LC3 Recruits GTPases
Kuriakose, T., & Kanneganti, T. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.06.019 · Cited by 2
Self-citationVirulence of Pathogens and the Counteracting Responses of the Host
Land, W. G. (2023) · Springer eBooks · doi:10.1007/978-3-031-21776-0_3 · Cited by 4
Structural basis of IRGB10 oligomerization by GTP hydrolysis
Ha, H. J., Kim, J. H., Lee, G. H., Kim, S., & Park, H. H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1254415 · Cited by 2
Yang, L., Li, Y., Xie, Q., Xu, T., & Qi, X. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01887-1 · Cited by 2
Zhang, X., Cao, Y., Zhao, Z., Tang, L., Zhang, B., Liao, C., Li, G., & Cai, W. (2025) · The Journal of Immunology · doi:10.1093/jimmun/vkaf140 · Cited by 2
Bass, A. R., & Shin, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.27.120477 · Cited by 2
Stress granule component TIA-1 is a negative regulator of the non-canonical NLRP3 inflammasomePreprint
Lamichhane, P. P., Aditi, A., Neil, B. H., Kilgore, P. B., Torres, A. G., Chopra, A. K., & Samir, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.12.634801 · Cited by 2
Lv, Y., Fan, Y., Gao, Q., Chen, Q., Hu, Y., Wang, L., Shi, H., Chen, E., Xu, Q., Cai, Y., et al. (2025) · eLife · doi:10.7554/elife.107339 · Cited by 2
A review of PANoptosis mechanism: current knowledge on pyroptosis, apoptosis and necroptosis in fish
Jin, G., Lv, A., Hu, X., Liu, X., & Chen, Y. (2025) · Reviews in Fish Biology and Fisheries · doi:10.1007/s11160-025-09960-9 · Cited by 1
Lv, Y., Fan, Y., Gao, Q., Chen, Q., Hu, Y., Wang, L., Shi, H., Chen, E., Xu, Q., Cai, Y., et al. (2026) · eLife · doi:10.7554/elife.107339.3 · Cited by 1
Inflammasome Activation Differences Underpin Different Mycobacterium tuberculosis Infection Outcomes
Kumar, R., Kolloli, A., Bhargavi, G., Husain, S., Chang, T. L.-Y., Ghanny, S., Soteropoulos, P., & Subbian, S. (2025) · MedComm · doi:10.1002/mco2.70486 · Cited by 1
Stress granule component protein TIA1 is a negative regulator of the noncanonical NLRP3 inflammasome
Lamichhane, P. P., Aditi, Neil, B. H., Kilgore, P. B., Torres, A. G., Chopra, A. K., & Samir, P. (2025) · ImmunoHorizons · doi:10.1093/immhor/vlaf050 · Cited by 3
IFN-α and IFN-β inhibit NLRP1-driven PANoptosis
Sharma, B. R., Mummareddy, H., Chadchan, S. B., Sarkar, R., Farran, C. A. E., & Kanneganti, T. (2026) · EMBO Reports · doi:10.1038/s44319-026-00888-0 · Cited by 1
Self-citationThe NLRP3 inflammasome at the crossroads of innate immune signaling and cell death
Xiao, N., Lu, Z., Cooper, D. K., & Chen, J. (2026) · Cellular and Molecular Immunology · doi:10.1038/s41423-026-01463-2 · Cited by 2
Inflammasome effector functions: a Tale of Fire and Ice
Jha, S., & Ting, J. P. ‐. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91802-2.00031-1 · Cited by 1
A Continuous IC Glaciochemical Record of the last Glacial Period from the NGRIP Ice Core
Siggaard‐Andersen, M., Hansson, M., Fischer, H., Bigler, M., Roethlisberger, R., Goto‐Azuma, K., Steffensen, J. P., Ruth, U., Andersen, K. K., Clausen, H. B., et al. (2005) · AGUFM · Cited by 1
Triantafilou, K. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734357156.793560837 · Cited by 1
Dual role of Toxoplasma gondii ROP5 and ROP18 for NLRP3 inhibitionPreprint
Murillo-Léon, M., Bastidas-Quintero, A. M., Singh, S., Mueller, X., Gorka, O., Saller, B. S., Arenas, A. F., Campos, C., Gómez‐Marín, J. E., Groß, O., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.17.558105 · Cited by 1
Type-I IFNs induce GBPs and lysosomal defense in hepatocytes to control malariaPreprint
Marques-da-Silva, C., Schmidt-Silva, C., Bowers, C., Charles-Chess, N. A. E., Shiau, J. C., Park, E., Yuan, Z., Kim, B.-H., Kyle, D. E., Harty, J. T., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.22.619707 · Cited by 1
Autophagy Regulates Inflammatory Responses in Antigen-Presenting Cells
Harris, J., Lang, T., & Sukkar, M. B. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00015-9
Immune control of Legionella pneumophila lung infection
Yang, C. (2018) · Minerva Access (University of Melbourne)
The impact of sex and species of cells in herpes simplex virus infection
Tseng, Y. (2019) · ANU Open Research (Australian National University) · doi:10.25911/5d77831416351
Novel therapeutic targets in uveitis
Tempest-Roe, S. (2017) · Spiral (Imperial College London) · doi:10.25560/75500
Yang, X., Cheng, X., Tang, Y., Qiu, X., Liu, Y., Kang, H., Chen, F., Xiao, X., Mackman, N., Billiar, T. R., et al. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3385688
Role of Inflammatory Cytokine Signaling in Control of Bacterial Infection
Saxena, P. (2020) · uO Research (University of Ottawa) · doi:10.20381/ruor-25300
Elizagaray, M. L. (2022) · El Servicio de Difusión de la Creación Intelectual (National University of La Plata) · doi:10.35537/10915/134431
Cell-Autonomous Defenses Against Intracellular Bacteria and Protozoa
Brož, P. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00044-4
Weiss, J. P. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732498116.793545009
McDermott, M., & Caseley, E. A. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736591724.793575100
Fitzgerald, K., & Ketelut-Carneiro, N. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736591724.793566817
Mecsas, J. C. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727304248.793562320
Cellular signaling, molecular activation, and regulation of the noncanonical inflammasome
Dorfleutner, A., & Stehlik, C. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91802-2.00028-1
The Role of the AIM2 Gene in Obesity-Related Glucose and Lipid Metabolic Disorders: A Recent Update
Zhang, Y., Xuan, X., Ye, D., Liu, D., Song, Y., Gao, F., & Lu, S. (2024) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s488978
Prevalence Around Inflammatory Caspases in Urinary Tract Infections, Review
Nisha, N., Sharma, D. C., Sharma, R. D., & Tomar, J. (2024) · Biosciences Biotechnology Research Asia · doi:10.13005/bbra/3308
Wang, S., & Jie, B. (2025) · Clinical Oral Investigations · doi:10.1007/s00784-025-06369-3
Liu, T., Zhao, H., Wang, X., Xu, Q., Li, Y., Wu, Q., Wei, Y., Xin, J., & Pan, Q. (2025) · Communications Biology · doi:10.1038/s42003-025-08950-8
Metadata
- Authors
- Man, S. M., Karki, R., Sasai, M., Place, D. E., Kesavardhana, S., Temirov, J., Frase, S., Zhu, Q., Malireddi, R. K. S., Kuriakose, T., Peters, J. L., Neale, G., Brown, S. A., Yamamoto, M., & Kanneganti, T.-D.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Immunology Frontier Research Center, The University of Osaka (JP)
- Corresponding author
- Kanneganti, Thirumala-Devi
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2016-10
- Volume
- 167
- Issue
- 2
- Pages
- 382-396.e17
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5074697
- OpenAlex
- W2524431814
- Cited by
- 312
- References
- 57
- Citations by year
- 2026: 12 · 2025: 35 · 2024: 18 · 2023: 28 · 2022: 32 · 2021: 30 · 2020: 49 · 2019: 37 · 2018: 31 · 2017: 37 · 2016: 2
- FWCI
- 18.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Seoul National University Open Repository (Seoul National University) (submittedVersion)
- Funders
- National Cancer Institute (R01CA163507, P30CA021765)
- National Institute of Allergy and Infectious Diseases (R01AI101935, R37AI101935, R01AI124346)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR056296)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- AIM2 inflammasome, caspase-11, NLRP3 inflammasome, Francisella novicida, Gram-negative bacteria, guanylate-binding proteins, plasma membrane targeting, DNA sensing, pyroptosis, IL-1β, IL-18, cell-autonomous immunity, innate immune recognition
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, B-Lymphocytes, Cytosol, DNA-Binding Proteins, Francisella, Immunity, Cellular, Immunity, Innate, Ligands, Mice, Mutant Strains, T-Lymphocytes, Gram-Negative Bacterial Infections, Caspases, GTP Phosphohydrolases, Myeloid Cells, Mice, Caspases, Initiator, Host-Pathogen Interactions, 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