{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T22:58:03Z","timestamp":1785452283802,"version":"3.56.0"},"reference-count":188,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:00:00Z","timestamp":1785369600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:00:00Z","timestamp":1785369600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100011033","name":"Ministry of Economy and Competitiveness | Agencia Estatal de Investigaci\u00f3n","doi-asserted-by":"publisher","award":["PID2022-138717NA-I00"],"award-info":[{"award-number":["PID2022-138717NA-I00"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011033","name":"Ministry of Economy and Competitiveness | Agencia Estatal de Investigaci\u00f3n","doi-asserted-by":"publisher","award":["CNS2022-135459"],"award-info":[{"award-number":["CNS2022-135459"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011033","name":"Ministry of Economy and Competitiveness | Agencia Estatal de Investigaci\u00f3n","doi-asserted-by":"publisher","award":["RYC2022-036466-I"],"award-info":[{"award-number":["RYC2022-036466-I"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"publisher"}]},{"name":"NA"},{"DOI":"10.13039\/100012818","name":"Comunidad de Madrid","doi-asserted-by":"publisher","award":["PIPF-2024\/BIO-34773"],"award-info":[{"award-number":["PIPF-2024\/BIO-34773"]}],"id":[{"id":"10.13039\/100012818","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000266","name":"RCUK | Engineering and Physical Sciences Research Council","doi-asserted-by":"publisher","award":["EP\/X02377X\/2"],"award-info":[{"award-number":["EP\/X02377X\/2"]}],"id":[{"id":"10.13039\/501100000266","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["220863"],"award-info":[{"award-number":["220863"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["31142"],"award-info":[{"award-number":["31142"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Microbiol"],"DOI":"10.1038\/s41564-026-02428-x","type":"journal-article","created":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T09:08:31Z","timestamp":1785402511000},"page":"2098-2111","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Cell-autonomous immunity as an integrated immune network against bacterial and viral pathogens"],"prefix":"10.1038","volume":"11","author":[{"given":"Lorena","family":"Mart\u00edn-Gonz\u00e1lez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruno","family":"Ramos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7555-0256","authenticated-orcid":false,"given":"Yizhou","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teresa","family":"Thurston","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7707-0264","authenticated-orcid":false,"given":"Greg","family":"Towers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0044-7588","authenticated-orcid":false,"given":"Dami\u00e1n","family":"Lobato-M\u00e1rquez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,30]]},"reference":[{"key":"2428_CR1","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1126\/science.1233028","volume":"340","author":"F Randow","year":"2013","unstructured":"Randow, F., MacMicking, J. D. & James, L. C. Cellular self-defense: how cell-autonomous immunity protects against pathogens. Science 340, 701\u2013706 (2013).","journal-title":"Science"},{"key":"2428_CR2","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1126\/science.1209791","volume":"334","author":"S Vaishnava","year":"2011","unstructured":"Vaishnava, S. et al. The antibacterial lectin RegIII\u03b3 promotes the spatial segregation of microbiota and host in the intestine. Science 334, 255\u2013258 (2011).","journal-title":"Science"},{"key":"2428_CR3","doi-asserted-by":"publisher","first-page":"216","DOI":"10.1038\/s41392-025-02264-1","volume":"10","author":"R Chen","year":"2025","unstructured":"Chen, R. et al. Pattern recognition receptors: function, regulation and therapeutic potential. Signal Transduct. Target. Ther. 10, 216 (2025).","journal-title":"Signal Transduct. Target. Ther."},{"key":"2428_CR4","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1016\/j.cell.2010.01.022","volume":"140","author":"O Takeuchi","year":"2010","unstructured":"Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805\u2013820 (2010).","journal-title":"Cell"},{"key":"2428_CR5","doi-asserted-by":"publisher","first-page":"3261","DOI":"10.1016\/j.cell.2023.05.038","volume":"186","author":"Y Li","year":"2023","unstructured":"Li, Y. et al. cGLRs are a diverse family of pattern recognition receptors in innate immunity. Cell 186, 3261\u20133276 (2023).","journal-title":"Cell"},{"key":"2428_CR6","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1038\/nri3210","volume":"12","author":"JD MacMicking","year":"2012","unstructured":"MacMicking, J. D. Interferon-inducible effector mechanisms in cell-autonomous immunity. Nat. Rev. Immunol. 12, 367\u2013382 (2012).","journal-title":"Nat. Rev. Immunol."},{"key":"2428_CR7","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1038\/nri3398","volume":"13","author":"LM Stuart","year":"2013","unstructured":"Stuart, L. M., Paquette, N. & Boyer, L. Effector-triggered versus pattern-triggered immunity: how animals sense pathogens. Nat. Rev. Immunol. 13, 199\u2013206 (2013).","journal-title":"Nat. Rev. Immunol."},{"key":"2428_CR8","doi-asserted-by":"publisher","unstructured":"Minkoff, J. M. & tenOever, B. Innate immune evasion strategies of SARS-CoV-2. Nat. Rev. Microbiol. https:\/\/doi.org\/10.1038\/s41579-022-00839-1 (2023).","DOI":"10.1038\/s41579-022-00839-1"},{"key":"2428_CR9","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20210583","volume":"218","author":"NR Cheemarla","year":"2021","unstructured":"Cheemarla, N. R. et al. Dynamic innate immune response determines susceptibility to SARS-CoV-2 infection and early replication kinetics. J. Exp. Med. 218, e20210583 (2021).","journal-title":"J. Exp. Med."},{"key":"2428_CR10","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1038\/s41587-021-01037-9","volume":"40","author":"J Loske","year":"2022","unstructured":"Loske, J. et al. Pre-activated antiviral innate immunity in the upper airways controls early SARS-CoV-2 infection in children. Nat. Biotechnol. 40, 319\u2013324 (2022).","journal-title":"Nat. Biotechnol."},{"key":"2428_CR11","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.01257-21","volume":"95","author":"BE Nilsson-Payant","year":"2021","unstructured":"Nilsson-Payant, B. E. et al. The NF-\u03baB transcriptional footprint is essential for SARS-CoV-2 replication. J. Virol. 95, e01257-21 (2021).","journal-title":"J. Virol."},{"key":"2428_CR12","doi-asserted-by":"publisher","first-page":"jcs260682","DOI":"10.1242\/jcs.260682","volume":"136","author":"J Zhu","year":"2023","unstructured":"Zhu, J., Chiang, C. & Gack, M. U. Viral evasion of the interferon response at a glance. J. Cell Sci. 136, jcs260682 (2023).","journal-title":"J. Cell Sci."},{"key":"2428_CR13","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1016\/j.mib.2016.05.015","volume":"32","author":"DC Beachboard","year":"2016","unstructured":"Beachboard, D. C. & Horner, S. M. Innate immune evasion strategies of DNA and RNA viruses. Curr. Opin. Microbiol. 32, 113\u2013119 (2016).","journal-title":"Curr. Opin. Microbiol."},{"key":"2428_CR14","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/j.molcel.2014.03.010","volume":"54","author":"LE Reddick","year":"2014","unstructured":"Reddick, L. E. & Alto, N. M. Bacteria fighting back: how pathogens target and subvert the host innate immune system. Mol. Cell 54, 321\u2013328 (2014).","journal-title":"Mol. Cell"},{"key":"2428_CR15","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1038\/nri.2016.147","volume":"17","author":"I Jorgensen","year":"2017","unstructured":"Jorgensen, I., Rayamajhi, M. & Miao, E. A. Programmed cell death as a defence against infection. Nat. Rev. Immunol. 17, 151\u2013164 (2017).","journal-title":"Nat. Rev. Immunol."},{"key":"2428_CR16","doi-asserted-by":"publisher","first-page":"2288","DOI":"10.1016\/j.cell.2023.04.025","volume":"186","author":"KC Barnett","year":"2023","unstructured":"Barnett, K. C., Li, S., Liang, K. & Ting, J. P. Y. A 360\u00b0 view of the inflammasome: mechanisms of activation, cell death, and diseases. Cell 186, 2288\u20132312 (2023).","journal-title":"Cell"},{"key":"2428_CR17","doi-asserted-by":"publisher","first-page":"595","DOI":"10.1038\/s41590-023-01451-y","volume":"24","author":"T Pr\u00f3chnicki","year":"2023","unstructured":"Pr\u00f3chnicki, T. et al. Mitochondrial damage activates the NLRP10 inflammasome. Nat. Immunol. 24, 595\u2013603 (2023).","journal-title":"Nat. Immunol."},{"key":"2428_CR18","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1038\/nature22967","volume":"546","author":"S Zhu","year":"2017","unstructured":"Zhu, S. et al. Nlrp9b inflammasome restricts rotavirus infection in intestinal epithelial cells. Nature 546, 667\u2013670 (2017).","journal-title":"Nature"},{"key":"2428_CR19","doi-asserted-by":"publisher","first-page":"660","DOI":"10.1038\/nature15514","volume":"526","author":"J Shi","year":"2015","unstructured":"Shi, J. et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 526, 660\u2013665 (2015).","journal-title":"Nature"},{"key":"2428_CR20","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1038\/nature13683","volume":"514","author":"J Shi","year":"2014","unstructured":"Shi, J. et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature 514, 187\u2013192 (2014).","journal-title":"Nature"},{"key":"2428_CR21","doi-asserted-by":"publisher","first-page":"666","DOI":"10.1038\/nature15541","volume":"526","author":"N Kayagaki","year":"2015","unstructured":"Kayagaki, N. et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526, 666\u2013671 (2015).","journal-title":"Nature"},{"key":"2428_CR22","doi-asserted-by":"publisher","first-page":"956","DOI":"10.1126\/science.aar7607","volume":"362","author":"S R\u00fchl","year":"2018","unstructured":"R\u00fchl, S. et al. ESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation. Science 362, 956\u2013960 (2018).","journal-title":"Science"},{"key":"2428_CR23","doi-asserted-by":"publisher","first-page":"960","DOI":"10.1038\/s41586-022-04825-8","volume":"606","author":"K Nozaki","year":"2022","unstructured":"Nozaki, K. et al. Caspase-7 activates ASM to repair gasdermin and perforin pores. Nature 606, 960\u2013967 (2022).","journal-title":"Nature"},{"key":"2428_CR24","doi-asserted-by":"crossref","unstructured":"Zanoni, I. et al. An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells. Science 352, 1232\u20131236 (2016).","DOI":"10.1126\/science.aaf3036"},{"key":"2428_CR25","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1038\/ni.2215","volume":"13","author":"CS Shi","year":"2012","unstructured":"Shi, C. S. et al. Activation of autophagy by inflammatory signals limits IL-1\u03b2 production by targeting ubiquitinated inflammasomes for destruction. Nat. Immun. 13, 255\u2013263 (2012).","journal-title":"Nat. Immun."},{"key":"2428_CR26","doi-asserted-by":"crossref","unstructured":"Magupalli, V. G. et al. HDAC6 mediates an aggresome-like mechanism for NLRP3 and pyrin inflammasome activation. Science 369, eaas8995 (2020).","DOI":"10.1126\/science.aas8995"},{"key":"2428_CR27","doi-asserted-by":"crossref","unstructured":"O\u2019Keefe, M. E., Dubyak, G. R. & Abbott, D. W. Post-translational control of NLRP3 inflammasome signaling. J. Biol. Chem. 300, 107386 (2024).","DOI":"10.1016\/j.jbc.2024.107386"},{"key":"2428_CR28","doi-asserted-by":"publisher","first-page":"4570","DOI":"10.1016\/j.molcel.2023.11.015","volume":"83","author":"S Zheng","year":"2023","unstructured":"Zheng, S. et al. ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3\u2013NEK7 interaction and inflammasome activation. Mol. Cell 83, 4570\u20134585 (2023).","journal-title":"Mol. Cell"},{"key":"2428_CR29","doi-asserted-by":"crossref","unstructured":"Barry, R. et al. SUMO-mediated regulation of NLRP3 modulates inflammasome activity. Nat. Commun. 9, 3001 (2018).","DOI":"10.1038\/s41467-018-05321-2"},{"key":"2428_CR30","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1038\/s41568-019-0123-y","volume":"19","author":"R Karki","year":"2019","unstructured":"Karki, R. & Kanneganti, T.-D. Diverging inflammasome signals in tumorigenesis and potential targeting. Nat. Rev. Cancer 19, 197\u2013214 (2019).","journal-title":"Nat. Rev. Cancer"},{"key":"2428_CR31","doi-asserted-by":"crossref","unstructured":"Okin, D. & Kagan, J. C. Inflammasomes as regulators of non-infectious disease. Semin. Immunol. 69, 101815 (2023).","DOI":"10.1016\/j.smim.2023.101815"},{"key":"2428_CR32","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1038\/s41586-022-04802-1","volume":"606","author":"E Sefik","year":"2022","unstructured":"Sefik, E. et al. Inflammasome activation in infected macrophages drives COVID-19 pathology. Nature 606, 585\u2013593 (2022).","journal-title":"Nature"},{"key":"2428_CR33","doi-asserted-by":"crossref","unstructured":"Barry, K., Harpur, C., Lam, M., Tate, M. D. & Mansell, A. Aggregated Hendra virus C-protein activates the NLRP3 inflammasome to induce inflammation. J. Inflamm. 20, 38 (2023).","DOI":"10.1186\/s12950-023-00365-8"},{"key":"2428_CR34","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.chom.2009.12.008","volume":"7","author":"T Shimada","year":"2010","unstructured":"Shimada, T. et al. Staphylococcus aureus evades lysozyme-based peptidoglycan digestion that links phagocytosis, inflammasome activation, and IL-1\u03b2 secretion. Cell Host Microbe 7, 38\u201349 (2010).","journal-title":"Cell Host Microbe"},{"key":"2428_CR35","doi-asserted-by":"publisher","first-page":"12419","DOI":"10.1073\/pnas.1019041108","volume":"108","author":"JD Sauer","year":"2011","unstructured":"Sauer, J. D. et al. Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity. Proc. Natl Acad. Sci. USA 108, 12419\u201312424 (2011).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR36","doi-asserted-by":"publisher","first-page":"3756","DOI":"10.1128\/JB.02053-14","volume":"196","author":"TP Burke","year":"2014","unstructured":"Burke, T. P. et al. Listeria monocytogenes is resistant to lysozyme through the regulation, not the acquisition, of cell wall-modifying enzymes. J. Bacteriol. 196, 3756\u20133767 (2014).","journal-title":"J. Bacteriol."},{"key":"2428_CR37","doi-asserted-by":"publisher","first-page":"173","DOI":"10.3390\/v18020173","volume":"18","author":"JD Wuerth","year":"2026","unstructured":"Wuerth, J. D. & Schmidt, F. I. Antiviral inflammasomes and how to find them. Viruses 18, 173 (2026).","journal-title":"Viruses"},{"key":"2428_CR38","doi-asserted-by":"crossref","unstructured":"Jiang, J. et al. Bacterial infection reinforces host metabolic flux from arginine to spermine for NLRP3 inflammasome evasion. Cell Rep. 34, 108832 (2021).","DOI":"10.1016\/j.celrep.2021.108832"},{"key":"2428_CR39","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1084\/jem.20130627","volume":"211","author":"MA Wynosky-Dolfi","year":"2014","unstructured":"Wynosky-Dolfi, M. A. et al. Oxidative metabolism enables Salmonella evasion of the NLRP3 inflammasome. J. Exp. Med. 211, 653\u2013668 (2014).","journal-title":"J. Exp. Med."},{"key":"2428_CR40","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1016\/j.chom.2016.07.018","volume":"20","author":"LK Chung","year":"2016","unstructured":"Chung, L. K. et al. The Yersinia virulence factor YopM hijacks host kinases to inhibit type III effector-triggered activation of the pyrin inflammasome. Cell Host Microbe 20, 296\u2013306 (2016).","journal-title":"Cell Host Microbe"},{"key":"2428_CR41","doi-asserted-by":"crossref","unstructured":"Boal-Carvalho, I. et al. Influenza A viruses limit NLRP3\u2013NEK7-complex formation and pyroptosis in human macrophages. EMBO Rep. 21, e50421 (2020).","DOI":"10.15252\/embr.202050421"},{"key":"2428_CR42","doi-asserted-by":"crossref","unstructured":"Li, J. et al. Zika virus inhibits cell death by inhibiting the expression of NLRP3 and A20. J. Virol. 99, e01980-24 (2025).","DOI":"10.1128\/jvi.01980-24"},{"key":"2428_CR43","doi-asserted-by":"publisher","first-page":"13019","DOI":"10.1128\/JVI.05942-11","volume":"85","author":"N Komune","year":"2011","unstructured":"Komune, N., Ichinohe, T., Ito, M. & Yanagi, Y. Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1\u03b2 secretion. J. Virol. 85, 13019\u201313026 (2011).","journal-title":"J. Virol."},{"key":"2428_CR44","doi-asserted-by":"publisher","first-page":"842","DOI":"10.1128\/JVI.00842-18","volume":"92","author":"T Komatsu","year":"2018","unstructured":"Komatsu, T. et al. Sendai virus V protein inhibits the secretion of interleukin-1\u03b2 by preventing NLRP3 inflammasome. J. Virol. 92, 842\u2013860 (2018).","journal-title":"J. Virol."},{"key":"2428_CR45","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1038\/s41586-021-04020-1","volume":"599","author":"Z Li","year":"2021","unstructured":"Li, Z. et al. Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11. Nature 599, 290\u2013295 (2021).","journal-title":"Nature"},{"key":"2428_CR46","first-page":"03855","volume":"17","author":"K Kim","year":"2025","unstructured":"Kim, K. et al. Differential targeting of human pyroptotic caspase-5 and caspase-4 by Shigella OspC2 and OspC3. mBio 17, 03855\u201325 (2025).","journal-title":"mBio"},{"key":"2428_CR47","doi-asserted-by":"publisher","first-page":"1521","DOI":"10.1016\/j.chom.2021.08.010","volume":"29","author":"G Luchetti","year":"2021","unstructured":"Luchetti, G. et al. Shigella ubiquitin ligase IpaH7.8 targets gasdermin D for degradation to prevent pyroptosis and enable infection. Cell Host Microbe 29, 1521\u20131530 (2021).","journal-title":"Cell Host Microbe"},{"key":"2428_CR48","doi-asserted-by":"publisher","first-page":"1335","DOI":"10.1042\/BCJ20190202","volume":"476","author":"DT Bloomer","year":"2019","unstructured":"Bloomer, D. T. et al. CrmA orthologs from diverse poxviruses potently inhibit caspases-1 and -8, yet cleavage site mutagenesis frequently produces caspase-1-specific variants. Biochem. J. 476, 1335\u20131357 (2019).","journal-title":"Biochem. J."},{"key":"2428_CR49","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.60609","volume":"10","author":"BV Tsu","year":"2021","unstructured":"Tsu, B. V. et al. Diverse viral proteases activate the NLRP1 inflammasome. eLife 10, e60609 (2021).","journal-title":"eLife"},{"key":"2428_CR50","doi-asserted-by":"crossref","unstructured":"Sandstrom, A. et al. Functional degradation: a mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes. Science 364, eaau1330 (2019).","DOI":"10.1126\/science.aau1330"},{"key":"2428_CR51","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1126\/science.aau1208","volume":"364","author":"AJ Chui","year":"2019","unstructured":"Chui, A. J. et al. N-terminal degradation activates the NLRP1B nflammasome. Science 364, 82\u201385 (2019).","journal-title":"Science"},{"key":"2428_CR52","doi-asserted-by":"crossref","unstructured":"Wang, Q. et al. CARD8 is an inflammasome sensor for HIV-1 protease activity. Science 371, eabe1707 (2021).","DOI":"10.1126\/science.abe1707"},{"key":"2428_CR53","doi-asserted-by":"publisher","first-page":"adz1069","DOI":"10.1126\/sciadv.adz1069","volume":"11","author":"IK Hughes","year":"2025","unstructured":"Hughes, I. K., Hood, J. B., Qui\u00f1ones-Molina, A. A., Akiyama, H. & Gummuluru, S. Evasion of CARD8 activation during HIV-1 assembly. Sci. Adv. 11, adz1069 (2025).","journal-title":"Sci. Adv."},{"key":"2428_CR54","doi-asserted-by":"crossref","unstructured":"Kulsuptrakul, J., Turcotte, E. A., Emerman, M. & Mitchell, P. S. A human-specific motif facilitates CARD8 inflammasome activation after HIV-1 infection. eLife 12, e84108 (2023).","DOI":"10.7554\/eLife.84108"},{"key":"2428_CR55","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1016\/j.cell.2024.01.048","volume":"187","author":"Q Wang","year":"2024","unstructured":"Wang, Q. et al. The CARD8 inflammasome dictates HIV\/SIV pathogenesis and disease progression. Cell 187, 1223\u20131237 (2024).","journal-title":"Cell"},{"key":"2428_CR56","doi-asserted-by":"publisher","first-page":"868","DOI":"10.1038\/ni1362","volume":"7","author":"S Uematsu","year":"2006","unstructured":"Uematsu, S. et al. Detection of pathogenic intestinal bacteria by Toll-like receptor 5 on intestinal CD11c+ lamina propria cells. Nat. Immunol. 7, 868\u2013874 (2006).","journal-title":"Nat. Immunol."},{"key":"2428_CR57","doi-asserted-by":"publisher","first-page":"29811","DOI":"10.1073\/pnas.2002747117","volume":"117","author":"AS Akhade","year":"2020","unstructured":"Akhade, A. S. et al. Type 1 interferon-dependent repression of NLRC4 and iPLA2 licenses down-regulation of Salmonella flagellin inside macrophages. Proc. Natl Acad. Sci. USA 117, 29811\u201329822 (2020).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR58","doi-asserted-by":"publisher","first-page":"e1004688","DOI":"10.1371\/journal.ppat.1004688","volume":"11","author":"V Sivaraman","year":"2015","unstructured":"Sivaraman, V. et al. Yersinia pestis activates both IL-1\u03b2 and IL-1 receptor antagonist to modulate lung inflammation during pneumonic plague. PLoS Pathog. 11, e1004688 (2015).","journal-title":"PLoS Pathog."},{"key":"2428_CR59","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2413965122","volume":"122","author":"PA Krakowiak","year":"2025","unstructured":"Krakowiak, P. A. et al. Co-option of mitochondrial nucleic acid-sensing pathways by HSV-1 UL12.5 for reactivation from latent infection. Proc. Natl Acad. Sci. USA 122, e2413965122 (2025).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR60","doi-asserted-by":"publisher","DOI":"10.1038\/s41419-023-06183-3","volume":"14","author":"L Gao","year":"2023","unstructured":"Gao, L. et al. The mechanism of linear ubiquitination in regulating cell death and correlative diseases. Cell Death Dis. 14, 659 (2023).","journal-title":"Cell Death Dis."},{"key":"2428_CR61","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1038\/ncb2006","volume":"12","author":"H Ashida","year":"2010","unstructured":"Ashida, H. et al. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO\/IKK\u03b3 to dampen the host NF-\u03baB-mediated inflammatory response. Nat. Cell Biol. 12, 66\u201373 (2010).","journal-title":"Nat. Cell Biol."},{"key":"2428_CR62","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1038\/nature17657","volume":"533","author":"J Qiu","year":"2016","unstructured":"Qiu, J. et al. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors. Nature 533, 120\u2013124 (2016).","journal-title":"Nature"},{"key":"2428_CR63","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2514645123","volume":"123","author":"S Chung","year":"2026","unstructured":"Chung, S., Hudson, H., Stromberg, K. A. & Sandstrom, A. NLRP1B is an integrated decoy that subverts Shigella flexneri E3 ligase activity to promote effector-triggered immunity. Proc. Natl Acad. Sci. USA 123, e2514645123 (2026).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR64","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20231518","volume":"221","author":"P Parameswaran","year":"2024","unstructured":"Parameswaran, P., Payne, L., Powers, J., Rashighi, M. & Orzalli, M. H. A viral E3 ubiquitin ligase produced by herpes simplex virus 1 inhibits the NLRP1 inflammasome. J. Exp. Med. 221, e20231518 (2024).","journal-title":"J. Exp. Med."},{"key":"2428_CR65","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-77725-4","volume":"10","author":"D Shahnazaryan","year":"2020","unstructured":"Shahnazaryan, D. et al. Herpes simplex virus 1 targets IRF7 via ICP0 to limit type I IFN induction. Sci. Rep. 10, 22216 (2020).","journal-title":"Sci. Rep."},{"key":"2428_CR66","doi-asserted-by":"publisher","first-page":"32208","DOI":"10.1074\/jbc.M704870200","volume":"282","author":"SG Devaraj","year":"2007","unstructured":"Devaraj, S. G. et al. Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus. J. Biol. Chem. 282, 32208\u201332221 (2007).","journal-title":"J. Biol. Chem."},{"key":"2428_CR67","doi-asserted-by":"publisher","first-page":"34667","DOI":"10.1074\/jbc.M114.609644","volume":"289","author":"BA Bailey-Elkin","year":"2014","unstructured":"Bailey-Elkin, B. A. et al. Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression. J. Biol. Chem. 289, 34667\u201334682 (2014).","journal-title":"J. Biol. Chem."},{"key":"2428_CR68","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1038\/s41586-020-2601-5","volume":"587","author":"D Shin","year":"2020","unstructured":"Shin, D. et al. Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature 587, 657\u2013662 (2020).","journal-title":"Nature"},{"key":"2428_CR69","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2024.114135","volume":"43","author":"Y Qin","year":"2024","unstructured":"Qin, Y. et al. ISGylation by HERCs facilitates STING activation. Cell Rep. 43, 114135 (2024).","journal-title":"Cell Rep."},{"key":"2428_CR70","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2420190122","volume":"122","author":"L Sarkar","year":"2025","unstructured":"Sarkar, L. et al. MDA5 ISGylation is crucial for immune signaling to control viral replication and pathogenesis. Proc. Natl Acad. Sci. USA 122, e2420190122 (2025).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR71","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-33671-5","volume":"13","author":"T-C Xiong","year":"2022","unstructured":"Xiong, T.-C. et al. The E3 ubiquitin ligase ARIH1 promotes antiviral immunity and autoimmunity by inducing mono-ISGylation and oligomerization of cGAS. Nat. Commun. 13, 5973 (2022).","journal-title":"Nat. Commun."},{"key":"2428_CR72","doi-asserted-by":"publisher","DOI":"10.1080\/27694127.2025.2542904","volume":"4","author":"K Cadwell","year":"2025","unstructured":"Cadwell, K. et al. Autophagy and bacterial infections. Autophagy Rep. 4, 2542904 (2025).","journal-title":"Autophagy Rep."},{"key":"2428_CR73","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1038\/ncb2979","volume":"16","author":"A Stolz","year":"2014","unstructured":"Stolz, A., Ernst, A. & Dikic, I. Cargo recognition and trafficking in selective autophagy. Nat. Cell Biol. 16, 495\u2013501 (2014).","journal-title":"Nat. Cell Biol."},{"key":"2428_CR74","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1038\/nature21032","volume":"541","author":"J Staring","year":"2017","unstructured":"Staring, J. et al. PLA2G16 represents a switch between entry and clearance of Picornaviridae. Nature 541, 412\u2013416 (2017).","journal-title":"Nature"},{"key":"2428_CR75","doi-asserted-by":"publisher","first-page":"806","DOI":"10.1016\/j.cub.2004.04.033","volume":"14","author":"AJ Perrin","year":"2004","unstructured":"Perrin, A. J., Jiang, X., Birmingham, C. L., So, N. S. Y. & Brumell, J. H. Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system. Curr. Biol. 14, 806\u2013811 (2004).","journal-title":"Curr. Biol."},{"key":"2428_CR76","doi-asserted-by":"publisher","first-page":"5909","DOI":"10.4049\/jimmunol.0900441","volume":"183","author":"YT Zheng","year":"2009","unstructured":"Zheng, Y. T. et al. The adaptor protein p62\/SQSTM1 targets invading bacteria to the autophagy pathway. J. Immunol. 183, 5909\u20135916 (2009).","journal-title":"J. Immunol."},{"key":"2428_CR77","doi-asserted-by":"publisher","first-page":"1215","DOI":"10.1038\/ni.1800","volume":"10","author":"TLM Thurston","year":"2009","unstructured":"Thurston, T. L. M., Ryzhakov, G., Bloor, S., von Muhlinen, N. & Randow, F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10, 1215\u20131221 (2009).","journal-title":"Nat. Immunol."},{"key":"2428_CR78","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1016\/j.molcel.2019.01.035","volume":"74","author":"E Turco","year":"2019","unstructured":"Turco, E. et al. FIP200 claw domain binding to p62 promotes autophagosome formation at ubiquitin condensates. Mol. Cell 74, 330\u2013346 (2019).","journal-title":"Mol. Cell"},{"key":"2428_CR79","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1016\/j.molcel.2019.01.041","volume":"74","author":"BJ Ravenhill","year":"2019","unstructured":"Ravenhill, B. J. et al. The cargo receptor NDP52 initiates selective autophagy by recruiting the ULK complex to cytosol-invading bacteria. Mol. Cell 74, 320\u2013329 (2019).","journal-title":"Mol. Cell"},{"key":"2428_CR80","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/j.chom.2010.01.007","volume":"7","author":"A Orvedahl","year":"2010","unstructured":"Orvedahl, A. et al. Autophagy protects against Sindbis virus infection of the central nervous system. Cell Host Microbe 7, 115\u2013127 (2010).","journal-title":"Cell Host Microbe"},{"key":"2428_CR81","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-25642-z","volume":"12","author":"J Ames","year":"2021","unstructured":"Ames, J. et al. OPTN is a host intrinsic restriction factor against neuroinvasive HSV-1 infection. Nat. Commun. 12, 5401 (2021).","journal-title":"Nat. Commun."},{"key":"2428_CR82","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1016\/j.chom.2016.11.002","volume":"21","author":"LH Franco","year":"2017","unstructured":"Franco, L. H. et al. The ubiquitin ligase Smurf1 functions in selective autophagy of Mycobacterium tuberculosis and anti-tuberculous host defense. Cell Host Microbe 21, 59\u201372 (2017).","journal-title":"Cell Host Microbe"},{"key":"2428_CR83","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1038\/s41586-021-03566-4","volume":"594","author":"EG Otten","year":"2021","unstructured":"Otten, E. G. et al. Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection. Nature 594, 111\u2013116 (2021).","journal-title":"Nature"},{"key":"2428_CR84","doi-asserted-by":"publisher","DOI":"10.1038\/nmicrobiol.2017.66","volume":"2","author":"SJL Van Wijk","year":"2017","unstructured":"Van Wijk, S. J. L. et al. Linear ubiquitination of cytosolic Salmonella Typhimurium activates NF-\u03baB and restricts bacterial proliferation. Nat. Microbiol. 2, 17066 (2017).","journal-title":"Nat. Microbiol."},{"key":"2428_CR85","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1126\/science.282.5396.2085","volume":"282","author":"A Poltorak","year":"1998","unstructured":"Poltorak, A. et al. Defective LPS signaling in C3H\/HeJ and C57BL\/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085\u20132088 (1998).","journal-title":"Science"},{"key":"2428_CR86","doi-asserted-by":"publisher","DOI":"10.1038\/nmicrobiol.2017.63","volume":"2","author":"J Noad","year":"2017","unstructured":"Noad, J. et al. LUBAC-synthesized linear ubiquitin chains restrict cytosol-invading bacteria by activating autophagy and NF-\u03baB. Nat. Microbiol. 2, 17063 (2017).","journal-title":"Nat. Microbiol."},{"key":"2428_CR87","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-26061-w","volume":"12","author":"F Thery","year":"2021","unstructured":"Thery, F. et al. Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity. Nat. Commun. 12, 5772 (2021).","journal-title":"Nat. Commun."},{"key":"2428_CR88","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2315865120","volume":"121","author":"SK Matta","year":"2024","unstructured":"Matta, S. K. et al. Genome-wide and targeted CRISPR screens identify RNF213 as a mediator of interferon gamma-dependent pathogen restriction in human cells. Proc. Natl Acad. Sci. USA 121, e2315865120 (2024).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR89","doi-asserted-by":"publisher","first-page":"1671","DOI":"10.1016\/j.chom.2022.08.008","volume":"30","author":"SC Walsh","year":"2022","unstructured":"Walsh, S. C. et al. The bacterial effector GarD shields Chlamydia trachomatis inclusions from RNF213-mediated ubiquitylation and destruction. Cell Host Microbe 30, 1671\u20131684 (2022).","journal-title":"Cell Host Microbe"},{"key":"2428_CR90","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.01888-22","volume":"13","author":"D Hernandez","year":"2022","unstructured":"Hernandez, D., Walsh, S., Saavedra Sanchez, L., Dickinson, M. S. & Coers, J. Interferon-inducible E3 ligase RNF213 facilitates host-protective linear and K63-linked ubiquitylation of Toxoplasma gondii parasitophorous vacuoles. mBio 13, e0188822 (2022).","journal-title":"mBio"},{"key":"2428_CR91","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1007\/s00335-020-09856-y","volume":"32","author":"D Houzelstein","year":"2021","unstructured":"Houzelstein, D. et al. The ring finger protein 213 gene (Rnf213) contributes to Rift Valley fever resistance in mice. Mamm. Genome 32, 30\u201337 (2021).","journal-title":"Mamm. Genome"},{"key":"2428_CR92","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2218825120","volume":"120","author":"H Tian","year":"2023","unstructured":"Tian, H. et al. RNF213 modulates \u03b3-herpesvirus infection and reactivation via targeting the viral replication and transcription activator. Proc. Natl Acad. Sci. USA 120, e2218825120 (2023).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR93","doi-asserted-by":"publisher","first-page":"4979","DOI":"10.1038\/s44319-024-00280-w","volume":"25","author":"A Crespillo-Casado","year":"2024","unstructured":"Crespillo-Casado, A. et al. Recognition of phylogenetically diverse pathogens through enzymatically amplified recruitment of RNF213. EMBO Rep. 25, 4979\u20135005 (2024).","journal-title":"EMBO Rep."},{"key":"2428_CR94","doi-asserted-by":"publisher","first-page":"913","DOI":"10.1016\/j.chom.2024.04.012","volume":"32","author":"M Szczesna","year":"2024","unstructured":"Szczesna, M. et al. Bacterial esterases reverse lipopolysaccharide ubiquitylation to block host immunity. Cell Host Microbe 32, 913\u2013924 (2024).","journal-title":"Cell Host Microbe"},{"key":"2428_CR95","doi-asserted-by":"publisher","unstructured":"Naydenova, K. et al. Shigella flexneri evades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213. Nat. Struct. Mol. Biol. https:\/\/doi.org\/10.1038\/s41594-025-01530-8 (2025).","DOI":"10.1038\/s41594-025-01530-8"},{"key":"2428_CR96","doi-asserted-by":"publisher","unstructured":"Saavedra-Sanchez, L. et al. The Shigella flexneri effector IpaH1.4 facilitates RNF213 degradation and protects cytosolic bacteria against interferon-induced ubiquitylation. eLife https:\/\/doi.org\/10.7554\/eLife.102714.1 (2025).","DOI":"10.7554\/eLife.102714.1"},{"key":"2428_CR97","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-59444-4","volume":"16","author":"J Ahel","year":"2025","unstructured":"Ahel, J. et al. ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213. Nat. Commun. 16, 4414 (2025).","journal-title":"Nat. Commun."},{"key":"2428_CR98","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1007\/s00018-025-05705-w","volume":"82","author":"MS Ali","year":"2025","unstructured":"Ali, M. S., Tang, Y. S., Lee, H. H. Y., Baker, S. C. & Mok, C. K. P. ISG-15, beyond its functions in the cell: a mini review. Cell. Mol. Life Sci. 82, 289 (2025).","journal-title":"Cell. Mol. Life Sci."},{"key":"2428_CR99","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1038\/s41586-024-08136-y","volume":"637","author":"A Bhardwaj","year":"2025","unstructured":"Bhardwaj, A., Panepinto, M. C., Ueberheide, B. & Neel, B. G. A mechanism for hypoxia-induced inflammatory cell death in cancer. Nature 637, 470\u2013477 (2025).","journal-title":"Nature"},{"key":"2428_CR100","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.bbrc.2020.02.024","volume":"525","author":"M Takeda","year":"2020","unstructured":"Takeda, M. et al. Moyamoya disease patient mutations in the RING domain of RNF213 reduce its ubiquitin ligase activity and enhance NF-\u03baB activation and apoptosis in an AAA+ domain-dependent manner. Biochem. Biophys. Res. Commun. 525, 668\u2013674 (2020).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2428_CR101","doi-asserted-by":"publisher","first-page":"1686880","DOI":"10.3389\/fimmu.2025.1686880","volume":"16","author":"S Padmakumar","year":"2025","unstructured":"Padmakumar, S., Madhavan, A., Nair, B. G. & Kumar, G. B. Pathogen-induced hijacking of host SUMOylation: from molecular mechanisms and prospects for therapeutic modulation. Front. Immunol. 16, 1686880 (2025).","journal-title":"Front. Immunol."},{"key":"2428_CR102","doi-asserted-by":"publisher","first-page":"00654","DOI":"10.1128\/jvi.00654-25","volume":"99","author":"HM Schmidt","year":"2025","unstructured":"Schmidt, H. M. et al. UFMylation promotes orthoflavivirus infectious particle production. J. Virol. 99, 00654\u201325 (2025).","journal-title":"J. Virol."},{"key":"2428_CR103","doi-asserted-by":"publisher","first-page":"2367","DOI":"10.1016\/j.molcel.2023.05.018","volume":"83","author":"SPT Yiu","year":"2023","unstructured":"Yiu, S. P. T. et al. An Epstein\u2013Barr virus protein interaction map reveals NLRP3 inflammasome evasion via MAVS UFMylation. Mol. Cell 83, 2367\u20132386 (2023).","journal-title":"Mol. Cell"},{"key":"2428_CR104","doi-asserted-by":"publisher","unstructured":"L\u00f3pez-Jim\u00e9nez, A. T. et al. Proximity biotinylation at the host\u2013Shigella interface reveals UFMylation as an antibacterial pathway. Preprint at bioRxiv https:\/\/doi.org\/10.1101\/2025.05.29.656827 (2025).","DOI":"10.1101\/2025.05.29.656827"},{"key":"2428_CR105","doi-asserted-by":"publisher","first-page":"1621137","DOI":"10.3389\/fmicb.2025.1621137","volume":"16","author":"Y Xu","year":"2025","unstructured":"Xu, Y. et al. Host SUMOylation in bacterial infections and immune defense mechanisms. Front. Microbiol. 16, 1621137 (2025).","journal-title":"Front. Microbiol."},{"key":"2428_CR106","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1007\/s13365-021-00995-9","volume":"27","author":"F Imbert","year":"2021","unstructured":"Imbert, F. & Langford, D. Viruses, SUMO, and immunity: the interplay between viruses and the host SUMOylation system. J. Neurovirol. 27, 531\u2013541 (2021).","journal-title":"J. Neurovirol."},{"key":"2428_CR107","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-44502-6","volume":"15","author":"J Ren","year":"2024","unstructured":"Ren, J. et al. TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence. Nat. Commun. 15, 244 (2024).","journal-title":"Nat. Commun."},{"key":"2428_CR108","doi-asserted-by":"publisher","first-page":"102373","DOI":"10.1016\/j.coi.2023.102373","volume":"84","author":"Y Rivera-Cuevas","year":"2023","unstructured":"Rivera-Cuevas, Y., Clough, B. & Frickel, E.-M. Human guanylate-binding proteins in intracellular pathogen detection, destruction, and host cell death induction. Curr. Opin. Immunol. 84, 102373 (2023).","journal-title":"Curr. Opin. Immunol."},{"key":"2428_CR109","doi-asserted-by":"publisher","first-page":"5826","DOI":"10.1111\/febs.15662","volume":"288","author":"M Kutsch","year":"2021","unstructured":"Kutsch, M. & Coers, J. Human guanylate binding proteins: nanomachines orchestrating host defense. FEBS J. 288, 5826\u20135849 (2021).","journal-title":"FEBS J."},{"key":"2428_CR110","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1016\/j.chom.2025.03.008","volume":"33","author":"C Marques-da-Silva","year":"2025","unstructured":"Marques-da-Silva, C. et al. Type I interferons induce guanylate-binding proteins and lysosomal defense in hepatocytes to control malaria. Cell Host Microbe 33, 529\u2013544 (2025).","journal-title":"Cell Host Microbe"},{"key":"2428_CR111","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2020104926","volume":"39","author":"M Kutsch","year":"2020","unstructured":"Kutsch, M. et al. Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions. EMBO J. 39, e104926 (2020).","journal-title":"EMBO J."},{"key":"2428_CR112","doi-asserted-by":"crossref","unstructured":"Piro, A. S. et al. Detection of cytosolic Shigella flexneri via a C-terminal triple-arginine motif of GBP1 inhibits actin-based motility. mBio 8, e01979-17 (2017).","DOI":"10.1128\/mBio.01979-17"},{"key":"2428_CR113","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-16889-z","volume":"11","author":"JC Santos","year":"2020","unstructured":"Santos, J. C. et al. Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria. Nat. Commun. 11, 3276 (2020).","journal-title":"Nat. Commun."},{"key":"2428_CR114","doi-asserted-by":"publisher","first-page":"104635","DOI":"10.1016\/j.micpath.2020.104635","volume":"152","author":"H Ning","year":"2021","unstructured":"Ning, H., Wang, S., Li, Y., Sun, G. & He, J. The cell structure damage and embden-meyerhof-parnas pathway inhibition of Listeria monocytogenes induced by glycinin basic peptide. Microb. Pathog. 152, 104635 (2021).","journal-title":"Microb. Pathog."},{"key":"2428_CR115","doi-asserted-by":"publisher","first-page":"542","DOI":"10.1016\/j.immuni.2025.12.017","volume":"59","author":"J Began","year":"2026","unstructured":"Began, J. et al. Caspase-4 binds to LPS membranes with positive curvature for non-canonical inflammasome activation. Immunity 59, 542\u2013558 (2026).","journal-title":"Immunity"},{"key":"2428_CR116","doi-asserted-by":"crossref","unstructured":"Zhu, S. et al. Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection. Science 383, eabm9903 (2024).","DOI":"10.1126\/science.abm9903"},{"key":"2428_CR117","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1016\/j.chom.2017.09.007","volume":"22","author":"MP Wandel","year":"2017","unstructured":"Wandel, M. P. et al. GBPs inhibit motility of Shigella flexneri but are targeted for degradation by the bacterial ubiquitin ligase IpaH9.8. Cell Host Microbe 22, 507\u2013518 (2017).","journal-title":"Cell Host Microbe"},{"key":"2428_CR118","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1038\/nature24467","volume":"551","author":"P Li","year":"2017","unstructured":"Li, P. et al. Ubiquitination and degradation of GBPs by a Shigella effector to suppress host defence. Nature 551, 378\u2013383 (2017).","journal-title":"Nature"},{"key":"2428_CR119","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1038\/nature13157","volume":"509","author":"E Meunier","year":"2014","unstructured":"Meunier, E. et al. Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases. Nature 509, 366\u2013370 (2014).","journal-title":"Nature"},{"key":"2428_CR120","doi-asserted-by":"publisher","DOI":"10.15252\/embj.201798089","volume":"37","author":"JC Santos","year":"2018","unstructured":"Santos, J. C. et al. LPS targets host guanylate-binding proteins to the bacterial outer membrane for non-canonical inflammasome activation. EMBO J. 37, e98089 (2018).","journal-title":"EMBO J."},{"key":"2428_CR121","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.01707-23","volume":"14","author":"AR Bass","year":"2023","unstructured":"Bass, A. R. et al. Human GBP1 facilitates the rupture of the Legionella-containing vacuole and inflammasome activation. mBio 14, e0170723 (2023).","journal-title":"mBio"},{"key":"2428_CR122","doi-asserted-by":"publisher","first-page":"880","DOI":"10.1038\/s41590-020-0697-2","volume":"21","author":"MP Wandel","year":"2020","unstructured":"Wandel, M. P. et al. Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms. Nat. Immunol. 21, 880\u2013891 (2020).","journal-title":"Nat. Immunol."},{"key":"2428_CR123","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1038\/ni.3119","volume":"16","author":"E Meunier","year":"2015","unstructured":"Meunier, E. et al. Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nat. Immunol. 16, 476\u2013484 (2015).","journal-title":"Nat. Immunol."},{"key":"2428_CR124","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1038\/ni.3118","volume":"16","author":"SM Man","year":"2015","unstructured":"Man, S. M. et al. The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection. Nat. Immunol. 16, 467\u2013475 (2015).","journal-title":"Nat. Immunol."},{"key":"2428_CR125","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1016\/j.cell.2016.09.012","volume":"167","author":"SM Man","year":"2016","unstructured":"Man, S. M. et al. IRGB10 liberates bacterial ligands for sensing by the AIM2 and caspase-11\u2013NLRP3 inflammasomes. Cell 167, 382\u2013396 (2016).","journal-title":"Cell"},{"key":"2428_CR126","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.00632-17","volume":"91","author":"Z Zou","year":"2017","unstructured":"Zou, Z. et al. Guanylate-binding protein 1 inhibits nuclear delivery of Kaposi\u2019s sarcoma-associated herpesvirus virions by disrupting formation of actin filament. J. Virol. 91, e00632-17 (2017).","journal-title":"J. Virol."},{"key":"2428_CR127","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/j.chom.2017.06.019","volume":"22","author":"T Kuriakose","year":"2017","unstructured":"Kuriakose, T. & Kanneganti, T.-D. War on viruses: LC3 recruits GTPases. Cell Host Microbe 22, 7\u20139 (2017).","journal-title":"Cell Host Microbe"},{"key":"2428_CR128","doi-asserted-by":"publisher","first-page":"2092","DOI":"10.1016\/j.celrep.2019.04.063","volume":"27","author":"E Braun","year":"2019","unstructured":"Braun, E. et al. Guanylate-binding proteins 2 and 5 exert broad antiviral activity by inhibiting furin-mediated processing of viral envelope proteins. Cell Rep. 27, 2092\u20132104 (2019).","journal-title":"Cell Rep."},{"key":"2428_CR129","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.00823-25","volume":"99","author":"R Farrukee","year":"2025","unstructured":"Farrukee, R. et al. Human guanylate-binding protein (GBP) 1 inhibits replication of severe acute respiratory syndrome coronavirus 2. J. Virol. 99, e0082325 (2025).","journal-title":"J. Virol."},{"key":"2428_CR130","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.02374-24","volume":"15","author":"D Sauter","year":"2024","unstructured":"Sauter, D. & Kirchhoff, F. Antiviral mechanisms of guanylate-binding protein 5: versatile inhibition of multiple viral glycoproteins. mBio 15, e0237424 (2024).","journal-title":"mBio"},{"key":"2428_CR131","doi-asserted-by":"publisher","first-page":"e02086","DOI":"10.1128\/mbio.02086-24","volume":"15","author":"H Veler","year":"2024","unstructured":"Veler, H., Lun, C. M., Waheed, A. A. & Freed, E. O. Guanylate-binding protein 5 antagonizes viral glycoproteins independently of furin processing. mBio 15, e02086\u201324 (2024).","journal-title":"mBio"},{"key":"2428_CR132","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2022269118","volume":"118","author":"W Cui","year":"2021","unstructured":"Cui, W. et al. Structural basis for GTP-induced dimerization and antiviral function of guanylate-binding proteins. Proc. Natl Acad. Sci. USA 118, e2022269118 (2021).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR133","doi-asserted-by":"publisher","first-page":"780","DOI":"10.1007\/s11033-025-10889-2","volume":"52","author":"S Chakraborty","year":"2025","unstructured":"Chakraborty, S., Kasirajan, A., Mariappan, V., Green, S. R. & Pillai, A. K. B. Guanylate binding proteins (GBPs) as novel therapeutic targets against single-stranded RNA viruses. Mol. Biol. Rep. 52, 780 (2025).","journal-title":"Mol. Biol. Rep."},{"key":"2428_CR134","doi-asserted-by":"publisher","first-page":"2673","DOI":"10.4049\/jimmunol.2100325","volume":"207","author":"T Gu","year":"2021","unstructured":"Gu, T., Yu, D., Xu, L., Yao, Y.-L. & Yao, Y.-G. Tupaia GBP1 interacts with STING to initiate autophagy and restrict herpes simplex virus type 1 infection. J. Immunol. 207, 2673\u20132680 (2021).","journal-title":"J. Immunol."},{"key":"2428_CR135","doi-asserted-by":"publisher","first-page":"e1011976","DOI":"10.1371\/journal.ppat.1011976","volume":"20","author":"D Bender","year":"2024","unstructured":"Bender, D. et al. Guanylate-binding protein 1 acts as a pro-viral factor for the life cycle of hepatitis C virus. PLoS Pathog. 20, e1011976 (2024).","journal-title":"PLoS Pathog."},{"key":"2428_CR136","doi-asserted-by":"publisher","first-page":"832057","DOI":"10.3389\/fcimb.2022.832057","volume":"12","author":"S Chhabra","year":"2022","unstructured":"Chhabra, S., Sharma, K. B. & Kalia, M. Human guanylate-binding protein 1 positively regulates Japanese encephalitis virus replication in an interferon gamma primed environment. Front. Cell. Infect. Microbiol. 12, 832057 (2022).","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"2428_CR137","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2218469120","volume":"120","author":"L Goers","year":"2023","unstructured":"Goers, L. et al. Shigella IpaH9.8 limits GBP1-dependent LPS release from intracytosolic bacteria to suppress caspase-4 activation. Proc. Natl Acad. Sci. USA 120, e2218469120 (2023).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR138","doi-asserted-by":"publisher","first-page":"e55920","DOI":"10.1371\/journal.pone.0055920","volume":"8","author":"Z Zhu","year":"2013","unstructured":"Zhu, Z. et al. Nonstructural protein 1 of influenza A virus interacts with human guanylate-binding protein 1 to antagonize antiviral activity. PLoS ONE 8, e55920 (2013).","journal-title":"PLoS ONE"},{"key":"2428_CR139","doi-asserted-by":"crossref","unstructured":"Mesner, D. et al. SARS-CoV-2 evolution influences GBP and IFITM sensitivity. Proc. Natl Acad. Sci. USA 120, e2212577120 (2023).","DOI":"10.1073\/pnas.2212577120"},{"key":"2428_CR140","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1016\/j.immuni.2017.02.011","volume":"46","author":"Y Wang","year":"2017","unstructured":"Wang, Y. et al. Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to regulate responses to DNA virus infection. Immunity 46, 393\u2013404 (2017).","journal-title":"Immunity"},{"key":"2428_CR141","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.67029","volume":"10","author":"TP Burke","year":"2021","unstructured":"Burke, T. P. et al. Interferon receptor-deficient mice are susceptible to eschar-associated rickettsiosis. eLife 10, e67029 (2021).","journal-title":"eLife"},{"key":"2428_CR142","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1038\/s41564-020-0673-5","volume":"5","author":"TP Burke","year":"2020","unstructured":"Burke, T. P. et al. Inflammasome-mediated antagonism of type I interferon enhances Rickettsia pathogenesis. Nat. Microbiol. 5, 688\u2013696 (2020).","journal-title":"Nat. Microbiol."},{"key":"2428_CR143","doi-asserted-by":"publisher","first-page":"2009","DOI":"10.1105\/tpc.108.060194","volume":"20","author":"RAL Van Der Hoorn","year":"2008","unstructured":"Van Der Hoorn, R. A. L. & Kamoun, S. From guard to decoy: a new model for perception of plant pathogen effectors. Plant Cell 20, 2009\u20132017 (2008).","journal-title":"Plant Cell"},{"key":"2428_CR144","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1016\/j.tig.2011.05.006","volume":"27","author":"YS Mao","year":"2011","unstructured":"Mao, Y. S., Zhang, B. & Spector, D. L. Biogenesis and function of nuclear bodies. Trends Genet. 27, 295\u2013306 (2011).","journal-title":"Trends Genet."},{"key":"2428_CR145","doi-asserted-by":"publisher","first-page":"2014","DOI":"10.1242\/jcs.063586","volume":"123","author":"Y Mimura","year":"2010","unstructured":"Mimura, Y., Takahashi, K., Kawata, K., Akazawa, T. & Inoue, N. Two-step colocalization of MORC3 with PML nuclear bodies. J. Cell Sci. 123, 2014\u20132024 (2010).","journal-title":"J. Cell Sci."},{"key":"2428_CR146","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1089\/jir.2010.0111","volume":"31","author":"M-C Geoffroy","year":"2011","unstructured":"Geoffroy, M.-C. & Chelbi-Alix, M. K. Role of promyelocytic leukemia protein in host antiviral defense. J. Interferon Cytokine Res. 31, 145\u2013158 (2011).","journal-title":"J. Interferon Cytokine Res."},{"key":"2428_CR147","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1038\/s41586-021-04054-5","volume":"600","author":"MM Gaidt","year":"2021","unstructured":"Gaidt, M. M. et al. Self-guarding of MORC3 enables virulence factor-triggered immunity. Nature 600, 138\u2013142 (2021).","journal-title":"Nature"},{"key":"2428_CR148","doi-asserted-by":"crossref","unstructured":"Sloan, E., Orr, A. & Everett, R. D. MORC3, a Component of PML nuclear bodies, has a role in restricting herpes simplex virus 1 and human cytomegalovirus. J. Virol. 90, 8621\u20138633 (2016).","DOI":"10.1128\/JVI.00621-16"},{"key":"2428_CR149","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1016\/j.immuni.2016.04.002","volume":"44","author":"A Roers","year":"2016","unstructured":"Roers, A., Hiller, B. & Hornung, V. Recognition of endogenous nucleic acids by the innate immune system. Immunity 44, 739\u2013754 (2016).","journal-title":"Immunity"},{"key":"2428_CR150","doi-asserted-by":"crossref","unstructured":"Fisch, D. et al. PIM1 controls GBP1 activity to limit self-damage and to guard against pathogen infection. Science 382, eadg2253 (2023).","DOI":"10.1126\/science.adg2253"},{"key":"2428_CR151","doi-asserted-by":"publisher","DOI":"10.1126\/science.adw4937","volume":"391","author":"BC Remick","year":"2026","unstructured":"Remick, B. C. et al. Poxvirus attack of antiviral defense pathways unleashes an effector-triggered NF-\u03baB response. Science 391, eadw4937 (2026).","journal-title":"Science"},{"key":"2428_CR152","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1038\/ni.2915","volume":"15","author":"C Odendall","year":"2014","unstructured":"Odendall, C. et al. Diverse intracellular pathogens activate type III interferon expression from peroxisomes. Nat. Immunol. 15, 717\u2013726 (2014).","journal-title":"Nat. Immunol."},{"key":"2428_CR153","doi-asserted-by":"publisher","first-page":"3612","DOI":"10.1073\/pnas.1100126108","volume":"108","author":"F Stavru","year":"2011","unstructured":"Stavru, F., Bouillaud, F., Sartori, A., Ricquier, D. & Cossart, P. Listeria monocytogenes transiently alters mitochondrial dynamics during infection. Proc. Natl Acad. Sci. USA 108, 3612\u20133617 (2011).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR154","doi-asserted-by":"publisher","first-page":"2001147","DOI":"10.1126\/scisignal.2001147","volume":"4","author":"T Koshiba","year":"2011","unstructured":"Koshiba, T., Yasukawa, K., Yanagi, Y. & Kawabata, S. Mitochondrial membrane potential is required for MAVS-mediated antiviral signaling. Sci. Signal. 4, 2001147 (2011).","journal-title":"Sci. Signal."},{"key":"2428_CR155","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1038\/s41564-025-01984-y","volume":"10","author":"S Ghosh","year":"2025","unstructured":"Ghosh, S. et al. Host AAA-ATPase VCP\/p97 lyses ubiquitinated intracellular bacteria as an innate antimicrobial defence. Nat. Microbiol. 10, 1099\u20131114 (2025).","journal-title":"Nat. Microbiol."},{"key":"2428_CR156","doi-asserted-by":"publisher","DOI":"10.1128\/msphere.00511-23","volume":"8","author":"B Clough","year":"2023","unstructured":"Clough, B. et al. p97\/VCP targets Toxoplasma gondii vacuoles for parasite restriction in interferon-stimulated human cells. mSphere 8, e0051123 (2023).","journal-title":"mSphere"},{"key":"2428_CR157","doi-asserted-by":"publisher","first-page":"19733","DOI":"10.1073\/pnas.1210659109","volume":"109","author":"F Hauler","year":"2012","unstructured":"Hauler, F., Mallery, D. L., McEwan, W. A., Bidgood, S. R. & James, L. C. AAA ATPase p97\/VCP is essential for TRIM21-mediated virus neutralization. Proc. Natl Acad. Sci. USA 109, 19733\u201319738 (2012).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2428_CR158","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1038\/s41580-018-0040-z","volume":"19","author":"A Rousseau","year":"2018","unstructured":"Rousseau, A. & Bertolotti, A. Regulation of proteasome assembly and activity in health and disease. Nat. Rev. Mol. Cell Biol. 19, 697\u2013712 (2018).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2428_CR159","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1038\/357375a0","volume":"357","author":"AL Goldberg","year":"1992","unstructured":"Goldberg, A. L. & Rock, K. L. Proteolysis, proteasomes and antigen presentation. Nature 357, 375\u2013379 (1992).","journal-title":"Nature"},{"key":"2428_CR160","doi-asserted-by":"publisher","first-page":"1032","DOI":"10.1038\/s41586-025-08615-w","volume":"639","author":"K Goldberg","year":"2025","unstructured":"Goldberg, K. et al. Cell-autonomous innate immunity by proteasome-derived defence peptides. Nature 639, 1032\u20131041 (2025).","journal-title":"Nature"},{"key":"2428_CR161","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1146\/annurev-immunol-061020-053734","volume":"39","author":"ML Meizlish","year":"2021","unstructured":"Meizlish, M. L., Franklin, R. A., Zhou, X. & Medzhitov, R. Tissue homeostasis and inflammation. Annu. Rev. Immunol. 39, 557\u2013581 (2021).","journal-title":"Annu. Rev. Immunol."},{"key":"2428_CR162","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1038\/nrm1244","volume":"4","author":"AI Tauber","year":"2003","unstructured":"Tauber, A. I. Metchnikoff and the phagocytosis theory. Nat. Rev. Mol. Cell Biol. 4, 897\u2013901 (2003).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2428_CR163","doi-asserted-by":"publisher","unstructured":"Sampaio, N. G. et al. MDA5 guards against infection by surveying cellular RNA homeostasis. Preprint at Research Square https:\/\/doi.org\/10.21203\/rs.3.rs-6466919\/v1 (2025).","DOI":"10.21203\/rs.3.rs-6466919\/v1"},{"key":"2428_CR164","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1038\/s41586-020-2844-1","volume":"588","author":"P Mehdipour","year":"2020","unstructured":"Mehdipour, P. et al. Epigenetic therapy induces transcription of inverted SINEs and ADAR1 dependency. Nature 588, 169\u2013173 (2020).","journal-title":"Nature"},{"key":"2428_CR165","doi-asserted-by":"crossref","unstructured":"Feng, S. et al. Inhibiting EZH2 targets atypical teratoid rhabdoid tumor by triggering viral mimicry via both RNA and DNA sensing pathways. Nat. Commun. 15, 9321 (2024).","DOI":"10.1038\/s41467-024-53515-8"},{"key":"2428_CR166","doi-asserted-by":"publisher","DOI":"10.1126\/sciimmunol.adg2979","volume":"8","author":"TJ Dorrity","year":"2023","unstructured":"Dorrity, T. J. et al. Long 3\u2032 UTRs predispose neurons to inflammation by promoting immunostimulatory double-stranded RNA formation. Sci. Immunol. 8, eadg2979 (2023).","journal-title":"Sci. Immunol."},{"key":"2428_CR167","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.00743-24","volume":"15","author":"C Agbavor","year":"2024","unstructured":"Agbavor, C. et al. The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O during Listeria monocytogenes infection. mBio 15, e00743-24 (2024).","journal-title":"mBio"},{"key":"2428_CR168","doi-asserted-by":"publisher","unstructured":"Jin, S. et al. Oxaloacetate sensing promotes innate immune antiviral defence against influenza virus infection. Nat. Microbiol. https:\/\/doi.org\/10.1038\/s41564-025-02107-3 (2025).","DOI":"10.1038\/s41564-025-02107-3"},{"key":"2428_CR169","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1038\/nature13449","volume":"513","author":"H Xu","year":"2014","unstructured":"Xu, H. et al. Innate immune sensing of bacterial modifications of Rho GTPases by the pyrin inflammasome. Nature 513, 237\u2013241 (2014).","journal-title":"Nature"},{"key":"2428_CR170","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/j.ceb.2020.10.007","volume":"68","author":"BL Woods","year":"2021","unstructured":"Woods, B. L. & Gladfelter, A. S. The state of the septin cytoskeleton from assembly to function. Curr. Opin. Cell Biol. 68, 105\u2013112 (2021).","journal-title":"Curr. Opin. Cell Biol."},{"key":"2428_CR171","doi-asserted-by":"crossref","unstructured":"Angelis, D. & Spiliotis, E. T. Septin mutations in human cancers. Front. Cell Dev. Biol. 4, 122 (2016).","DOI":"10.3389\/fcell.2016.00122"},{"key":"2428_CR172","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1016\/j.chom.2010.10.009","volume":"8","author":"S Mostowy","year":"2010","unstructured":"Mostowy, S. et al. Entrapment of intracytosolic bacteria by septin cage-like structures. Cell Host Microbe 8, 433\u2013444 (2010).","journal-title":"Cell Host Microbe"},{"key":"2428_CR173","doi-asserted-by":"publisher","first-page":"2911","DOI":"10.1083\/jcb.201708091","volume":"217","author":"J Pfanzelter","year":"2018","unstructured":"Pfanzelter, J., Mostowy, S. & Way, M. Septins suppress the release of vaccinia virus from infected cells. J. Cell Biol. 217, 2911\u20132929 (2018).","journal-title":"J. Cell Biol."},{"key":"2428_CR174","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-24721-5","volume":"12","author":"D Lobato-M\u00e1rquez","year":"2021","unstructured":"Lobato-M\u00e1rquez, D. et al. Mechanistic insight into bacterial entrapment by septin cage reconstitution. Nat. Commun. 12, 4511 (2021).","journal-title":"Nat. Commun."},{"key":"2428_CR175","doi-asserted-by":"publisher","first-page":"1418","DOI":"10.1016\/j.celrep.2017.04.063","volume":"19","author":"RG Gaudet","year":"2017","unstructured":"Gaudet, R. G. et al. Innate recognition of intracellular bacterial growth is driven by the TIFA-dependent cytosolic surveillance pathway. Cell Rep. 19, 1418\u20131430 (2017).","journal-title":"Cell Rep."},{"key":"2428_CR176","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.261139","volume":"136","author":"D Lobato-M\u00e1rquez","year":"2023","unstructured":"Lobato-M\u00e1rquez, D. et al. Septins and K63 ubiquitin chains are present in separate bacterial microdomains during autophagy of entrapped Shigella. J. Cell Sci. 136, jcs261139 (2023).","journal-title":"J. Cell Sci."},{"key":"2428_CR177","doi-asserted-by":"publisher","first-page":"ftab023","DOI":"10.1093\/femspd\/ftab023","volume":"79","author":"M Kutsch","year":"2021","unstructured":"Kutsch, M., Gonz\u00e1lez-Prieto, C., Lesser, C. F. & Coers, J. The GBP1 microcapsule interferes with IcsA-dependent septin cage assembly around Shigella flexneri. Pathog. Dis. 79, ftab023 (2021).","journal-title":"Pathog. Dis."},{"key":"2428_CR178","doi-asserted-by":"publisher","first-page":"e28618","DOI":"10.1002\/jmv.28618","volume":"95","author":"AR Lee","year":"2023","unstructured":"Lee, A. R., Kweon, Y. C., Lee, S. M. & Park, C. Y. Human coronavirus 3CL proteases cleave septins and disrupt Hedgehog signaling, causing ciliary dysfunction. J. Med. Virol. 95, e28618 (2023).","journal-title":"J. Med. Virol."},{"key":"2428_CR179","doi-asserted-by":"publisher","first-page":"L603","DOI":"10.1152\/ajplung.00283.2020","volume":"319","author":"LE Kuek","year":"2020","unstructured":"Kuek, L. E. & Lee, R. J. First contact: the role of respiratory cilia in host\u2013pathogen interactions in the airways. Am. J. Physiol. Lung Cell. Mol. Physiol. 319, L603\u2013L619 (2020).","journal-title":"Am. J. Physiol. Lung Cell. Mol. Physiol."},{"key":"2428_CR180","doi-asserted-by":"publisher","first-page":"1029","DOI":"10.15252\/embr.201541832","volume":"17","author":"A Sirianni","year":"2016","unstructured":"Sirianni, A. et al. Mitochondria mediate septin cage assembly to promote autophagy of Shigella. EMBO Rep. 17, 1029\u20131043 (2016).","journal-title":"EMBO Rep."},{"key":"2428_CR181","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-48205-4","volume":"15","author":"W Xian","year":"2024","unstructured":"Xian, W. et al. The Shigella kinase effector OspG modulates host ubiquitin signaling to escape septin-cage entrapment. Nat. Commun. 15, 3890 (2024).","journal-title":"Nat. Commun."},{"key":"2428_CR182","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2023.113528","volume":"42","author":"L Lecordier","year":"2023","unstructured":"Lecordier, L. et al. Apolipoproteins L1 and L3 control mitochondrial membrane dynamics. Cell Rep. 42, 113528 (2023).","journal-title":"Cell Rep."},{"key":"2428_CR183","doi-asserted-by":"crossref","unstructured":"Gaudet, R. G. et al. A human apolipoprotein L with detergent-like activity kills intracellular pathogens. Science 373, eabf8113 (2021).","DOI":"10.1126\/science.abf8113"},{"key":"2428_CR184","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1111\/febs.15444","volume":"288","author":"E Pays","year":"2021","unstructured":"Pays, E. The function of apolipoproteins L (APOLs): relevance for kidney disease, neurotransmission disorders, cancer and viral infection. FEBS J. 288, 360\u2013381 (2021).","journal-title":"FEBS J."},{"key":"2428_CR185","doi-asserted-by":"publisher","first-page":"916","DOI":"10.1038\/s42003-021-02387-5","volume":"4","author":"M Ultsch","year":"2021","unstructured":"Ultsch, M. et al. Structures of the ApoL1 and ApoL2 N-terminal domains reveal a non-classical four-helix bundle motif. Commun. Biol. 4, 916 (2021).","journal-title":"Commun. Biol."},{"key":"2428_CR186","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2021.167277","volume":"434","author":"S Lesage","year":"2022","unstructured":"Lesage, S. et al. Discovery of genes that modulate flavivirus replication in an interferon-dependent manner. J. Mol. Biol. 434, 167277 (2022).","journal-title":"J. Mol. Biol."},{"key":"2428_CR187","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abm6668","volume":"8","author":"P Gao","year":"2022","unstructured":"Gao, P. et al. Apolipoprotein E mediates cell resistance to influenza virus infection. Sci. Adv. 8, eabm6668 (2022).","journal-title":"Sci. Adv."},{"key":"2428_CR188","doi-asserted-by":"publisher","first-page":"13626","DOI":"10.1073\/pnas.1917993117","volume":"117","author":"A Rausell","year":"2020","unstructured":"Rausell, A. et al. Common homozygosity for predicted loss-of-function variants reveals both redundant and advantageous effects of dispensable human genes. Proc. Natl Acad. Sci. USA 117, 13626\u201313636 (2020).","journal-title":"Proc. Natl Acad. Sci. USA"}],"container-title":["Nature Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41564-026-02428-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41564-026-02428-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41564-026-02428-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T22:04:37Z","timestamp":1785449077000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41564-026-02428-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,30]]},"references-count":188,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["2428"],"URL":"https:\/\/doi.org\/10.1038\/s41564-026-02428-x","relation":{},"ISSN":["2058-5276"],"issn-type":[{"value":"2058-5276","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,30]]},"assertion":[{"value":"31 October 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 June 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 July 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Ethics"}}]}}