The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS
Open accessAbstract
Significance: A major component of the cell envelope of Gram-negative bacteria is LPS, also known as endotoxin. LPS produced during bacterial infections triggers inflammation, which can lead to septic shock and death. Our immune system can recognize LPS both outside and inside of cells. The recognition of extracellular and vacuolar LPS by LPS binding proteins is well described, but little is known about the recognition of cytoplasmic LPS. Here, we show that cytoplasmic LPS derived from the intracellular bacterial pathogen Legionella activated a proinflammatory immune response. We further identified host guanylate binding proteins as critical mediators of immunity triggered by cytoplasmic LPS. These findings are likely to advance our understanding of how cells can sense intracellular LPS.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [647]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUES
Folch, J., Lees, M., & Stanley, G. H. S. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64849-5 · Cited by 65,189
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
Noncanonical Inflammasome Activation by Intracellular LPS Independent of TLR4
Kayagaki, N., Wong, M. T., Stowe, I. B., Ramani, S. R., Gonzalez, L. C., Akashi‐Takamura, S., Miyake, K., Zhang, J., Lee, W. P., Muszyński, A., et al. (2013) · Science · doi:10.1126/science.1240248 · Cited by 1,545
Cytoplasmic LPS Activates Caspase-11: Implications in TLR4-Independent Endotoxic Shock
Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K., & Miao, E. A. (2013) · Science · doi:10.1126/science.1240988 · Cited by 1,261
Self-citationHirschfeld, M. J., Ma, Y., Weis, J. H., Vogel, S. N., & Weis, J. J. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.2.618 · Cited by 1,155
LPS, TLR4 and infectious disease diversity
Miller, S., Ernst, R. K., & Bader, M. W. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1068 · Cited by 1,059
Self-citationSensing and reacting to microbes through the inflammasomes
Franchi, L., Muñoz-Planillo, R., & Núñez, G. (2012) · Nature Immunology · doi:10.1038/ni.2231 · Cited by 1,046
Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
Thurston, T. L. M., Wandel, M. P., von Muhlinen, N., Foeglein, Á., & Randow, F. (2012) · Nature · doi:10.1038/nature10744 · Cited by 1,034
TRIF Licenses Caspase-11-Dependent NLRP3 Inflammasome Activation by Gram-Negative Bacteria
Rathinam, V. A. K., Vanaja, S. K., Waggoner, L., Sokolovska, A., Becker, C., Stuart, L. M., Leong, J. M., & Fitzgerald, K. A. (2012) · Cell · doi:10.1016/j.cell.2012.07.007 · Cited by 729
Berger, K. H., & Isberg, R. R. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01092.x · Cited by 646
Cited by
Sorted by citations
Items 201–300 of 357
Miao, N., Kang, Z., Wang, Z., Yu, W., Liu, T., Kong, L.-Z., Zheng, Y., Ding, C., Zhang, Z., Zhong, C., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02516-7 · Cited by 20
Resolvin D1 attenuated liver injury caused by chronic ethanol and acute LPS challenge in mice
Hardesty, J., Warner, J. B., Song, Y., Rouchka, E. C., McClain, C. J., Warner, D. R., & Kirpich, I. (2022) · The FASEB Journal · doi:10.1096/fj.202200778r · Cited by 20
Emerging mechanisms and functions of inflammasome complexes in teleost fish
Chang, M. X. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1065181 · Cited by 21
Zheng, Y., Yang, S., Dai, W., Wang, J., Bi, S., Zhang, X., Zheng, Z., Sun, Y., Wu, S., & Kong, J. (2023) · International Journal of Oncology · doi:10.3892/ijo.2023.5596 · Cited by 20
Host-Intrinsic Interferon Status in Infection and Immunity
Liu, B. C., Sarhan, J., & Poltorak, A. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.06.004 · Cited by 21
Anand, I. S., Choi, W.-Y., & Isberg, R. R. (2020) · Cellular Microbiology · doi:10.1111/cmi.13151 · Cited by 19
A Rapid Caspase-11 Response Induced by IFNγ Priming Is Independent of Guanylate Binding Proteins
Brubaker, S. W., Brewer, S. M., Massis, L. M., Napier, B. A., & Monack, D. M. (2020) · iScience · doi:10.1016/j.isci.2020.101612 · Cited by 20
Position-Specific Secondary Acylation Determines Detection of Lipid A by Murine TLR4 and Caspase-11
Harberts, E. M., Grubaugh, D., Akuma, D., Shin, S., Ernst, R. K., & Brodsky, I. E. (2022) · Infection and Immunity · doi:10.1128/iai.00201-22 · Cited by 23
Self-citationResta, S. C., Guerra, F., Talà, A., Bucci, C., & Alifano, P. (2024) · Cells · doi:10.3390/cells13211758 · Cited by 19
Recognition of Intracellular Bacteria by Inflammasomes
Brož, P. (2020) · John Wiley & Sons, Inc. eBooks · doi:10.1128/9781683670261.ch20 · Cited by 18
Protective Immunity and Immunopathology in Ehrlichiosis
Ismail, N., Sharma, A. K., Soong, L., & Walker, D. H. (2022) · Zoonoses · doi:10.15212/zoonoses-2022-0009 · Cited by 18
Pyroptosis modulation by bacterial effector proteins
Chai, Q., Lei, Z., & Liu, C. H. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101804 · Cited by 18
Crespillo-Casado, A., Pothukuchi, P., Naydenova, K., Yip, M. C. J., Young, J. M., Jérôme Boulanger, A., Dharamdasani, V., Harper, C., Hammoudi, P., Otten, E. G., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00280-w · Cited by 18
Coers, J., & Haldar, A. K. (2015) · Communicative & Integrative Biology · doi:10.1080/19420889.2015.1115163 · Cited by 19
Self-citationActivation of NLRP3 inflammasome in macrophages by mycoplasmal lipoproteins and lipopeptides
Saeki, A., SUGIYAMA, M., Hasebe, A., Suzuki, T., & Shibata, K. (2018) · Molecular Oral Microbiology · doi:10.1111/omi.12225 · Cited by 18
Herkt, C. E., Caffrey, B. E., Surmann, K., Blankenburg, S., Salazar, M. G., Jung, A. L., Herbel, S. M., Hoffmann, K., Schulte, L. N., Chen, W., et al. (2020) · mBio · doi:10.1128/mbio.03155-19 · Cited by 20
Li, M., Sun, G., Zhao, J., Pu, S., Lv, Y., Wang, Y., Li, Y., Zhao, X., Wang, Y., Yang, S., et al. (2024) · Haematologica · doi:10.3324/haematol.2023.284145 · Cited by 17
Tyrkalska, S. D., Candel, S., & Mulero, V. (2020) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2020.103874 · Cited by 18
Sun, Y., Lu, Y., Liu, L., Saaoud, F., Shao, Y., Xu, K., Drummer, C., Cueto, R., Shan, H., Jiang, X., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.177229 · Cited by 16
Schroyen, M., Steibel, J. P., Koltes, J. E., Choi, I., Raney, N. E., Eisley, C. J., Fritz-Waters, E. R., Reecy, J. M., Dekkers, J. C. M., Rowland, R. R. R., et al. (2015) · BMC Genomics · doi:10.1186/s12864-015-1741-8 · Cited by 18
Bai, S., Mu, Z., Huang, Y., & Ji, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-19401-2 · Cited by 15
Torres-Escobar, A., Wilkins, A. A., Juárez-Rodríguez, M. D., Circu, M., Latimer, B., Dragoi, A., & Ivanov, S. (2024) · Nature Communications · doi:10.1038/s41467-024-52184-x · Cited by 14
Human GBP1 Is Involved in the Repair of Damaged Phagosomes/Endolysosomes
Buijze, H., Brinkmann, V., HURWITZ, R. M., Dorhoi, A., Kaufmann, S. H. E., & Pei, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119701 · Cited by 16
Caspase Exploitation by Legionella pneumophila
Krause, K., & Amer, A. O. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00515 · Cited by 15
Mariappan, V., Adikari, S., Lokesh, S., Easow, J. M., & Pillai, A. B. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.11.037 · Cited by 15
WildCARDs: Inflammatory caspases directly detect LPS
Hagar, J. A., Aachoui, Y., & Miao, E. A. (2014) · Cell Research · doi:10.1038/cr.2014.128 · Cited by 15
Self-citationSubversion of Cell-Autonomous Host Defense by Chlamydia Infection
Fischer, A., & Rudel, T. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_13 · Cited by 15
Innate sensing and cell-autonomous resistance pathways in Legionella pneumophila infection
Naujoks, J., Lippmann, J., Suttorp, N., & Opitz, B. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.10.004 · Cited by 16
Mechanisms conferring multi-layered protection against intestinal Salmonella Typhimurium infection
Kroon, S., & Hardt, W. (2025) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf038 · Cited by 14
Caspase-11 drives macrophage hyperinflammation in models of Polg-related mitochondrial disease
VanPortfliet, J. J., Lei, Y., Ramanathan, M., Martinez, C. G., Wong, J. K., Stodola, T. J., Hoffmann, B. R., Pflug, K. M., Sitcheran, R., Kneeland, S. C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59907-8 · Cited by 18
Nawaz, M., Gouife, M., Zhu, S., Yue, X., Huang, K., Ma, R., Jiang, J., Jin, S., Zhu, J., & Xie, J. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.108789 · Cited by 14
Kim, S., & Isberg, R. R. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2303942120 · Cited by 16
Clough, B., Finethy, R., Khan, R. T., Fisch, D., Jordan, S., Patel, H., Coers, J., & Frickel, E.-M. (2019) · Wellcome Open Research · doi:10.12688/wellcomeopenres.15329.1 · Cited by 14
Self-citationGao, J., Hu, X., Xu, C., Guo, M., Li, S., Yang, F., Pan, X., Zhou, F., Jin, Y., Bai, F., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105035 · Cited by 13
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
Geraci, C., Varzandi, A. R., Schiavo, G., Bovo, S., Ribani, A., Utzeri, V. J., Galimberti, G., Buttazzoni, L., Óvilo, C., Gallo, M., et al. (2019) · Livestock Science · doi:10.1016/j.livsci.2019.03.003 · Cited by 13
Legionella pneumophila usurps host cell lipids for vacuole expansion and bacterial growth
Ghosh, S., Bandyopadhyay, S., Smith, D. M., Adak, S., Semenkovich, C. F., Nagy, L., Wolfgang, M. J., & O’Connor, T. J. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011996 · 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
GBP2 acts as a member of the interferon signalling pathway in lupus nephritis
Zhang, Y., Liao, Y., Hang, Q., Sun, D., & Liu, Y. (2022) · BMC Immunology · doi:10.1186/s12865-022-00520-5 · Cited by 12
Caspase-4 binds to LPS membranes with positive curvature for non-canonical inflammasome activation
Began, J., Boegli, A., Anton, L., Biriukov, D., Vairamuthu, J., Santos, J. C., & Brož, P. (2026) · Immunity · doi:10.1016/j.immuni.2025.12.017 · Cited by 13
Che, N., Zhang, Y., Zhang, S., Kong, X., Zhang, Y., Wang, S., Yuan, Z., & Liao, Y. (2024) · International Journal of Medical Sciences · doi:10.7150/ijms.94592 · Cited by 11
Pollock, T., Marrero, V. R. V., Brodsky, I. E., & Shin, S. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1010767 · Cited by 13
Pushing boundaries: mechanisms enabling bacterial pathogens to spread between cells
Raab, J. E., Hamilton, D. J., Harju, T. B., Huynh, T. N. T., & Russo, B. C. (2024) · Infection and Immunity · doi:10.1128/iai.00524-23 · Cited by 11
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
Iske, J., Fatimy, R. E., Nian, Y., Ghouzlani, A., Eskandari, S. K., Biefer, H. R. C., Vasudevan, A., & Elkhal, A. (2024) · eLife · doi:10.7554/elife.88686.3 · Cited by 10
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
Li, F.-J., Starrs, L. M., Mathur, A., Tuipulotu, D. E., Man, S. M., & Burgio, G. (2024) · Communications Biology · doi:10.1038/s42003-024-07204-3 · Cited by 10
Role of Pyroptosis in inflammatory bowel disease
Xiao, Z., Xie, J., Zhao, X., Chen, X., Lu, Y., Xu, Y., Wu, M., An, L., & Li, Q. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114619 · Cited by 10
Maciag, K., Raychowdhury, R., Smith, K., Schneider, A. M., Coers, J., Mumbach, M. R., Schwartz, S., & Hacohen, N. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.3a0218-069rr · Cited by 10
Self-citationInflammasomes primarily restrict cytosolic Salmonella replication within human macrophagesPreprint
Egan, M. S., O'Rourke, E. A., Mageswaran, S. K., Zuo, B., Martynyuk, I., Demissie, T., Hunter, E. N., Bass, A. R., Chang, Y., Brodsky, I. E., et al. (2023) · eLife · doi:10.7554/elife.90107 · Cited by 10
Dual role of pyroptosis in liver diseases: mechanisms, implications, and therapeutic perspectives
Yang, S., Zou, Y., Zhong, C., Zhou, Z., Peng, X., & Tang, C. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1522206 · Cited by 9
Activation and manipulation of inflammasomes and pyroptosis during bacterial infections
Bernard, E. M., & Brož, P. (2022) · Biochemical Journal · doi:10.1042/bcj20220051 · Cited by 10
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
Cell Death, by Any Other Name…
Kandouz, M. (2024) · Cells · doi:10.3390/cells13040325 · Cited by 10
Subversion of GBP-mediated host defense by E3 ligases acquired during Yersinia pestis evolution
Cao, S., Jiao, Y., Jiang, W., Wu, Y., Qin, S., Ren, Y., You, Y., Tan, Y., Guo, X., Chen, H., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32218-y · Cited by 9
Ghosh, S., Roy, S., Baid, N., Das, U. K., Rakshit, S., Sanghavi, P., Hajra, D., Das, S., Menon, S., Sahil, M., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-025-01984-y · Cited by 10
Chhabra, S., Sharma, K. B., & Kalia, M. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.832057 · Cited by 10
Iske, J., Fatimy, R. E., Nian, Y., Ghouzlani, A., Eskandari, S. K., Biefer, H. R. C., Vasudevan, A., & Elkhal, A. (2023) · eLife · doi:10.7554/elife.88686 · Cited by 8
Tupik, J. D., Madanick, J. M., Ivester, H. M., & Allen, I. C. (2022) · Cells · doi:10.3390/cells11101681 · Cited by 9
The role of galectins in the regulation of autophagy and inflammasome in host immunity
Lo, T.-H., Weng, I., Chen, H.-L., & Liu, F. (2024) · Seminars in Immunopathology · doi:10.1007/s00281-024-01018-5 · Cited by 8
GBP1 promotes acute rejection after liver transplantation by inducing Kupffer cells pyroptosis
Duan, H., Chang, Q., Ding, H., Shao, W., Wang, Y., Lu, K., Zhang, L., & Xu, J. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167644 · Cited by 7
Richard, K., Vogel, S. N., & Perkins, D. J. (2016) · Innate Immunity · doi:10.1177/1753425916650027 · Cited by 7
Brown, H. M., Biering, S. B., Zhu, A. C., Choi, J., & Hwang, S. (2018) · BioEssays · doi:10.1002/bies.201700231 · Cited by 7
Caspase-11 Contributes to Oviduct Pathology during Genital Chlamydia Infection in Mice
Allen, J., Gyorke, C. E., Tripathy, M. K., Zhang, Y., Lovett, A., Montgomery, S. A., & Nagarajan, U. M. (2019) · Infection and Immunity · doi:10.1128/iai.00262-19 · 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
STAT1 mediates the pro-inflammatory role of GBP5 in colitis
Li, Y., Wang, W., Zhu, R., Zhu, X., Sun, M., Huang, Y., Chen, W., Gao, S., Jiao, N., Lin, X., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-07843-0 · Cited by 6
Dai, Y., Xiang, H., Guo, F., Wu, Y., Zhao, L., Kong, X., Xu, Y., Shang, D., & Tao, X. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115135 · 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
Cachón-González, M. B., Zhao, C., Franklin, R. J. M., & Cox, T. M. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac299 · Cited by 6
Fitzgerald, K. A., & Rathinam, V. A. K. (2015) · Nature Immunology · doi:10.1038/ni.3144 · Cited by 6
Yao, Q., Chen, S., Qian, W., Yang, C., & Li, J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1724908 · Cited by 5
Endolysosomal damage surveillance enables rapid inflammasome sensing of pathogens
Shivcharan, S., Younis, D. A., Wright, S. S., Wang, C., Behl, B., Shumba, P., Delgado, K. N., Chawla, A. K., Alto, N. M., Panjwani, N., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116002 · Cited by 6
Mascarenhas, D. P. A., & Zamboni, D. S. (2024) · Current Opinion in Microbiology · doi:10.1016/j.mib.2024.102495 · Cited by 5
Role of Canonical and Non-canonical Inflammasomes During Burkholderia Infection
Sahoo, M., Lantier, L., & Re, F. (2016) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-41171-2_10 · Cited by 5
Microglia Caspase11 non‐canonical inflammasome drives fever
Yu, P., Li, Y., Fu, W., Yu, X., Sui, D., Xu, H., & Sun, W. (2024) · Acta Physiologica · doi:10.1111/apha.14187 · Cited by 5
Al‐Quraishy, S., Dkhil, M. A., Abdel‐Baki, A. S., Delić, D., & Wunderlich, F. T. (2018) · Parasitology Research · doi:10.1007/s00436-018-5789-7 · Cited by 5
Mastronardi, C. A., Paz-Filho, G., Zanoni, M., Molano‐González, N., Arcos‐Burgos, M., Licinio, J., & Wong, M. (2015) · NeuroImmunoModulation · doi:10.1159/000368310 · Cited by 5
Molecular evolution and adaptations of Legionella pneumophila from amoebae hosts to macrophages
Shin, C. J., & Kwaik, Y. A. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2026.1787137 · Cited by 4
Zhao, D., Zhuang, J., Wang, L., Wu, L., Xu, W., Zhao, L., Jiang, H. F., Jin, W., & Miao, C. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s486763 · Cited by 6
Molecular mechanism and immunological function of pyroptosis
Dong, N., & Shao, F. (2019) · Scientia Sinica Vitae · doi:10.1360/ssv-2019-0242 · Cited by 4
Cell-Autonomous Immunity: From Cytosolic Sensing to Self-Defense
Han, D., Zhang, B., Wang, Z., & Mi, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094025 · Cited by 5
A comparison of the effects of polystyrene and polycaprolactone nanoplastics on macrophages
Collin‐Faure, V., Boulée, M., Diemer, H., Fenel, D., Moriscot, C., Cianférani, S., Darrouzet, É., Carrière, M., & Rabilloud, T. (2025) · Environmental Science Nano · doi:10.1039/d5en00074b · Cited by 3
Inflammasomes primarily restrict cytosolic Salmonella replication within human macrophages
Egan, M. S., O'Rourke, E. A., Mageswaran, S. K., Zuo, B., Martynyuk, I., Demissie, T., Hunter, E. N., Bass, A. R., Chang, Y., Brodsky, I. E., et al. (2025) · eLife · doi:10.7554/elife.90107.3 · Cited by 4
Tessema, M. B., Feng, S., Tuipulotu, D. E., Farrukee, R., Ngo, C., de Graça, C. G., Yamomoto, M., Utzschneider, D. T., Brööks, A. G., Londrigan, S. L., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06748-8 · 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
Gusso, D., Pinto, F. J., Andrade‐Barros, A. I., Bernardo, J. T. G., DeOcesano-Pereira, C., Lopes‐Ferreira, M., & Lima, C. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1686758 · Cited by 2
Noncanonical inflammasomes: New insights into their roles in inflammation and immunopathology
Yi, Y. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153991 · Cited by 2
GBP1 recruitment to actin-rich pedestals of extracellular Gram-negative bacteria promotes pyroptosis
Bennison, D. J., Chaudhary, I., CHAUDHURİ, D., Wong, J. C. N., Punwatkar, A., Biswas, P. P., Stephenson, M., Zhong, Q., Kallemeijn, W. W., Guenot, M., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00830-z · Cited by 2
Solger, F., Rauch, J., Vormittag, S., Fan, M., Raykov, L., Charki, P., Katic, A., Letourneur, F., Soldati, T., Seibel, J., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013026 · Cited by 2
Evolution of Cell-Autonomous Effector Mechanisms in Macrophages versus Non-Immune Cells
Gaudet, R. G., Bradfield, C. J., & MacMicking, J. D. (2017) · ASM Press eBooks · doi:10.1128/9781555819194.ch34 · Cited by 2
Bass, A. R., & Shin, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.27.120477 · Cited by 2
GBP2 engages Galectin-9 for immunity against Toxoplasma gondiiPreprint
Kravets, E., Poschmann, G., Hänsch, S., Raba, V., Weidtkamp‐Peters, S., Degrandi, D., Stühler, K., & Pfeffer, K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.28.474342 · Cited by 2
Self-citationInflammasomes primarily restrict cytosolic Salmonella replication within human macrophagesPreprint
Egan, M. S., O'Rourke, E. A., Mageswaran, S. K., Zuo, B., Martynyuk, I., Demissie, T., Hunter, E. N., Bass, A. R., Chang, Y., Brodsky, I. E., et al. (2023) · eLife · doi:10.7554/elife.90107.1 · 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
Molecular signaling of inflammatory responses in macrophages
Yi, Y. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822368-0.00005-0 · 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
Bak and Bax are crucial for Gbp2-mediated pyroptosis during Vibrio and Salmonella infections
Luo, Y., & Bae, J. (2025) · The Journal of Microbiology · doi:10.71150/jm.2508004 · 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
Metadata
- Authors
- Pilla, D. M., Hagar, J. A., Haldar, A. K., Mason, A. K., Degrandi, D., Pfeffer, K., Ernst, R. K., Yamamoto, M., Miao, E. A., & Coers, J.
- Affiliations
- Duke University (US)
- University of North Carolina at Chapel Hill (US)
- University of Maryland, Baltimore (US)
- Heinrich Heine University Düsseldorf (DE)
- The University of Osaka (JP)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-04-08
- Volume
- 111
- Issue
- 16
- Pages
- 6046-6051
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4000848
- OpenAlex
- W1984035213
- Cited by
- 357
- References
- 43
- Citations by year
- 2026: 20 · 2025: 28 · 2024: 24 · 2023: 27 · 2022: 32 · 2021: 22 · 2020: 42 · 2019: 32 · 2018: 26 · 2017: 30 · 2016: 31 · 2015: 31 · 2014: 11
- FWCI
- 14.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (12PRE10440003)
- Deutsche Forschungsgemeinschaft (FOR729)
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R21AI099823, R01AI103197, R01AI097518, U54AI057157, R37AI103197)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- guanylate-binding proteins, caspase-11, pyroptosis, non-canonical inflammasome, Legionella pneumophila, cell-autonomous immunity, macrophages, interferon signaling, Escherichia coli LPS, intracellular bacterial infection
- MeSH terms
- NADPH Oxidase 2, Animals, Cytoplasm, Enzyme Activation, Interferon-gamma, Legionnaires' Disease, Lipopolysaccharides, Macrophage Activation, Macrophages, Membrane Glycoproteins, Mice, Inbred C57BL, Mutation, Salmonella typhimurium, Legionella pneumophila, Apoptosis, GTP-Binding Proteins, NADPH Oxidases, Caspases, Mice, Nitric Oxide Synthase Type II, Caspases, Initiator
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