Cited by 357Inflammasome and immune disordersinterferon and immune responsesImmune Response and Inflammation

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 access

Pilla, Danielle M., Hagar, Jon A., Haldar, Arun K., Mason, Ashley K., Degrandi, Daniel, Pfeffer, Klaus, Ernst, Robert K., Yamamoto, Masahiro, Miao, Edward A., Coers, Jörn·2014·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1321700111PMC PMC4000848

Open this paper in CoChat — free account Open PDF

Abstract

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.

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

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

Integrity signals

Registry

Crossref · 10.1073/pnas.1321700111

Cites

43 of 43 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

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

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

Claims other papers make about this one

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

Self-check

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

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

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-citation
Cutting Edge: Repurification of Lipopolysaccharide Eliminates Signaling Through Both Human and Murine Toll-Like Receptor 2
Hirschfeld, 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-citation
Sensing 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
Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila
Berger, K. H., & Isberg, R. R. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01092.x · Cited by 646

Show all 43 references

Sorted by citations

Items 101–200 of 357

Pyroptotic and non‐pyroptotic effector functions of caspase‐11
Khweek, A. A., & Amer, A. O. (2020) · Immunological Reviews · doi:10.1111/imr.12910 · Cited by 71
Noncanonical Pyroptosis Triggered by Macrophage‐Derived Extracellular Vesicles in Chondrocytes Leading to Cartilage Catabolism in Osteoarthritis
Ebata, T., Terkawi, M. A., Kitahara, K., Yokota, S., Shiota, J., Nishida, Y., Matsumae, G., Alhasan, H., Hamasaki, M., Hontani, K., et al. (2023) · Arthritis & Rheumatology · doi:10.1002/art.42505 · Cited by 69
Facile One‐Pot Synthesis of Tellurium Nanorods as Antioxidant and Anticancer Agents
Huang, W., Wu, H., Li, X., & Chen, T. (2016) · Chemistry - An Asian Journal · doi:10.1002/asia.201600757 · Cited by 69
Sensing of invading pathogens by GBPs: At the crossroads between cell-autonomous and innate immunity
Santos, J. C., & Brož, P. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.4mr0118-038r · Cited by 72
Regulation, Activation and Function of Caspase-11 during Health and Disease
Agnew, A., Nulty, C., & Creagh, E. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041506 · Cited by 70
Pyroptosis in defense against intracellular bacteria
Li, L., Dickinson, M. S., Coers, J., & Miao, E. A. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101805 · Cited by 73
Self-citation
The Listeria monocytogenes PASTA Kinase PrkA and Its Substrate YvcK Are Required for Cell Wall Homeostasis, Metabolism, and Virulence
Pensinger, D. A., Boldon, K. M., Chen, G. Y., Vincent, W. J. B., Kyle, S., Xiong, M., Schaenzer, A. J., Forster, E. R., Coers, J., Striker, R., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1006001 · Cited by 63
Self-citation
Sensing the enemy, containing the threat: cell-autonomous immunity toChlamydia trachomatis
Finethy, R., & Coers, J. (2016) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuw027 · Cited by 68
Self-citation
Salmonella enterica Serovar Typhimurium Induces NAIP/NLRC4- and NLRP3/ASC-Independent, Caspase-4-Dependent Inflammasome Activation in Human Intestinal Epithelial Cells
Naseer, N., Zhang, J., Bauer, R., Constant, D. A., Nice, T. J., Brodsky, I. E., Rauch, I., & Shin, S. (2022) · Infection and Immunity · doi:10.1128/iai.00663-21 · Cited by 67
Mechanisms and functions of guanylate-binding proteins and related interferon-inducible GTPases: Roles in intracellular lysis of pathogens
Ngo, C., & Man, S. M. (2017) · Cellular Microbiology · doi:10.1111/cmi.12791 · Cited by 67
Inner sensors of endotoxin – implications for sepsis research and therapy
Skirecki, T., & Cavaillon, J. (2019) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuz004 · Cited by 64
Dysregulated hemolysin liberates bacterial outer membrane vesicles for cytosolic lipopolysaccharide sensing
Chen, S., Yang, D., Wen, Y., Jiang, Z., Zhang, L., Jiang, J., Chen, Y., Hu, T., Wang, Q., Zhang, Y., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007240 · Cited by 67
Cross talk between intracellular pathogens and cell death
Demarco, B., Chen, K. W., & Brož, P. (2020) · Immunological Reviews · doi:10.1111/imr.12892 · Cited by 62
Irgm2 and Gate‐16 cooperatively dampen Gram‐negative bacteria‐induced caspase‐11 response
Eren, E., Planès, R., Bagayoko, S., Bordignon, P., Chaoui, K., Hessel, A., Santoni, K., Pinilla, M., Lagrange, B., Burlet‐Schiltz, O., et al. (2020) · EMBO Reports · doi:10.15252/embr.202050829 · Cited by 62
Self-citation
Role of Pyroptosis, a Pro-inflammatory Programmed Cell Death, in Epilepsy
Atabaki, R., Khaleghzadeh‐Ahangar, H., Esmaeili, N., & Moghaddam, P. M. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01250-3 · Cited by 66
Mechanistic Insights into Gasdermin Pore Formation and Regulation in Pyroptosis
Wang, C., & Ruan, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167297 · Cited by 64
The inflammasome: Learning from bacterial evasion strategies
Shin, S., & Brodsky, I. E. (2015) · Seminars in Immunology · doi:10.1016/j.smim.2015.03.006 · Cited by 59
Inflammasomes as polyvalent cell death platforms
de Vasconcelos, N. M., Opdenbosch, N. V., & Lamkanfi, M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2204-3 · Cited by 65
Non-canonical NLRP3 inflammasome activation and IL-1β signaling are necessary to L. amazonensis control mediated by P2X7 receptor and leukotriene B4
Chaves, M. M., Sinflorio, D. A., Thorstenberg, M. L., Martins, M. D. A., Moreira-Souza, A. C. A., Rangel, T. P., Silva, C. L. M., Bellio, M., Canetti, C. D. A., & Coutinho‐Silva, R. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007887 · Cited by 60
TRIM21 is critical for survival of Toxoplasma gondii infection and localises to GBP-positive parasite vacuoles
Foltz, C., Napolitano, A., Khan, R. T., Clough, B., Hirst, E. M. A., & Frickel, E. (2017) · Scientific Reports · doi:10.1038/s41598-017-05487-7 · Cited by 61
Emerging Insights into Noncanonical Inflammasome Recognition of Microbes
Russo, A. J., Behl, B., Banerjee, I., & Rathinam, V. A. K. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.10.003 · Cited by 57
MyD88-dependent inflammasome activation and autophagy inhibition contributes to Ehrlichia-induced liver injury and toxic shock
Kader, M., Alaoui-El-Azher, M., Vorhauer, J., Kode, B. B., Wells, J. Z., Stolz, D. B., Michalopoulos, G. K., Wells, A. H., Scott, M. J., & Ismail, N. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006644 · Cited by 59
Dynamin‐related Irgm proteins modulate LPS‐induced caspase‐11 activation and septic shock
Finethy, R., Dockterman, J., Kutsch, M., Orench‐Rivera, N., Wallace, G., Piro, A. S., Luoma, S., Haldar, A. K., Hwang, S., Martinez, J., et al. (2020) · EMBO Reports · doi:10.15252/embr.202050830 · Cited by 56
Self-citation
LPS-neutralizing peptides reduce outer membrane vesicle-induced inflammatory responses
Pfalzgraff, A., Correa, W., Heinbockel, L., Schromm, A. B., Lübow, C., Gisch, N., de Tejada, G. M., Brandenburg, K., & Weindl, G. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.05.018 · Cited by 53
IRF5 genetic risk variants drive myeloid-specific IRF5 hyperactivation and presymptomatic SLE
Li, D., Matta, B., Song, S., Nelson, V. L., Diggins, K. E., Simpfendorfer, K. R., Gregersen, P. K., Linsley, P. S., & Barnes, B. J. (2019) · JCI Insight · doi:10.1172/jci.insight.124020 · Cited by 53
Piscirickettsia salmonis Imbalances the Innate Immune Response to Succeed in a Productive Infection in a Salmonid Cell Line Model
Álvarez, C., Gómez, F. A., Mercado, L. A., Ramírez, R., & Marshall, S. H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163943 · Cited by 52
Novel perspectives on non-canonical inflammasome activation
Mortellaro, A., Diamond, C. E., Khameneh, H. J., & Brough, D. (2015) · ImmunoTargets and Therapy · doi:10.2147/itt.s57976 · Cited by 54
Cell-autonomous immunity by IFN-induced GBPs in animals and plants
Huang, S., Meng, Q., Mamińska, A., & MacMicking, J. D. (2019) · Current Opinion in Immunology · doi:10.1016/j.coi.2019.04.017 · Cited by 47
Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses
Stewart, M. K., & Cookson, B. T. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.50 · Cited by 49
IFN-γ extends the immune functions of Guanylate Binding Proteins to inflammasome-independent antibacterial activities during Francisella novicida infection
Wallet, P., Benaoudia, S., Mosnier, A., Lagrange, B., Martin, A., Lindgren, H., Golovliov, I. R., Michal, F., Basso, P., Djebali, S., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006630 · Cited by 55
Self-citation
Viewing Legionella pneumophila Pathogenesis through an Immunological Lens
Liu, X., & Shin, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.028 · Cited by 53
Caspase-11 Non-Canonical Inflammasome: Emerging Activator and Regulator of Infection-Mediated Inflammatory Responses
Yi, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082736 · Cited by 49
Scaling of immune responses against intracellular bacterial infection
Abdullah, Z., & Knolle, P. A. (2014) · The EMBO Journal · doi:10.15252/embj.201489055 · Cited by 49
Interferons: Tug of War Between Bacteria and Their Host
Alphonse, N., Dickenson, R. E., & Odendall, C. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.624094 · Cited by 52
Focus on the Mechanisms and Functions of Pyroptosis, Inflammasomes, and Inflammatory Caspases in Infectious Diseases
Song, H., Yang, B., Li, Y., Qian, A., Kang, Y., & Shan, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2501279 · Cited by 51
High-affinity caspase-4 binding to LPS presented as high molecular mass aggregates or in outer membrane vesicles
Wacker, M. A., Teghanemt, A., Weiss, J. P., & Barker, J. H. (2017) · Innate Immunity · doi:10.1177/1753425917695446 · Cited by 47
Guanylate Binding Proteins Regulate Inflammasome Activation in Response to Hyperinjected Yersinia Translocon Components
Zwack, E. E., Feeley, E. M., Burton, A. R., Hu, B., Yamamoto, M., Kanneganti, T., Bliska, J. B., Coers, J., & Brodsky, I. E. (2017) · Infection and Immunity · doi:10.1128/iai.00778-16 · Cited by 48
Self-citation
IRG1 and Inducible Nitric Oxide Synthase Act Redundantly with Other Interferon-Gamma-Induced Factors To Restrict Intracellular Replication of Legionella pneumophila
Price, J. V., Russo, D., Ji, D. X., Chavez, R. A., DiPeso, L., Lee, A. Y.-F., Coers, J., & Vance, R. E. (2019) · mBio · doi:10.1128/mbio.02629-19 · Cited by 45
Self-citation
Inflammasome activation and evasion by bacterial pathogens
Ta, A., & Vanaja, S. K. (2020) · Current Opinion in Immunology · doi:10.1016/j.coi.2020.11.006 · Cited by 45
Caspase-11 and caspase-1 differentially modulate actin polymerization via RhoA and Slingshot proteins to promote bacterial clearance
Caution, K., Gavrilin, M. A., Tazi, M., Kanneganti, A., Layman, D., Hoque, S., Krause, K., & Amer, A. O. (2015) · Scientific Reports · doi:10.1038/srep18479 · Cited by 45
Caspase-4 disaggregates lipopolysaccharide micelles via LPS-CARD interaction
An, J., Kim, S. H., Hwang, D., Lee, K. E., Kim, J. M., Yang, E. G., Kim, S. Y., & Chung, H. S. (2019) · Scientific Reports · doi:10.1038/s41598-018-36811-4 · Cited by 45
Recognition of Intracellular Bacteria by Inflammasomes
Brož, P. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.bai-0003-2019 · Cited by 41
Shigella IpaH9.8 limits GBP1-dependent LPS release from intracytosolic bacteria to suppress caspase-4 activation
Goers, L., Kim, K., Stedman, T. C., Canning, P. J., Mou, X., Ernst, N. H., Coers, J., & Lesser, C. F. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218469120 · Cited by 39
Self-citation
Type I Interferon Contributes to Noncanonical Inflammasome Activation, Mediates Immunopathology, and Impairs Protective Immunity during Fatal Infection with Lipopolysaccharide-Negative Ehrlichiae
Yang, Q., Stevenson, H. L., Scott, M. J., & Ismail, N. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.10.005 · Cited by 37
hGBP1 Coordinates Chlamydia Restriction and Inflammasome Activation through Sequential GTP Hydrolysis
Xavier, A., Al‐Zeer, M. A., Meyer, T. F., & Daumke, O. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107667 · Cited by 36
The noncanonical inflammasome-induced pyroptosis and septic shock
Wu, J., Cai, J., Tang, Y., & Lü, B. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101844 · Cited by 37
EGFR signaling augments TLR4 cell surface expression and function in macrophages via regulation of Rab5a activation
Tang, J. Y., Zhou, B., Scott, M. J., Chen, L., Lai, D., Fan, E., Li, Y., Wu, Q., Billiar, T. R., Wilson, M. A., et al. (2019) · Protein & Cell · doi:10.1007/s13238-019-00668-8 · Cited by 36
Bacterial secretion systems and regulation of inflammasome activation
Ratner, D., Ørning, P., & Lien, E. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0716-330r · Cited by 41
Defensive‐lipid droplets: Cellular organelles designed for antimicrobial immunity
Safi, R., Sánchez‐Álvarez, M., Bosch, M., Demangel, C., Parton, R. G., & Pol, A. (2023) · Immunological Reviews · doi:10.1111/imr.13199 · Cited by 36
Detecting lipopolysaccharide in the cytosol of mammalian cells: Lessons from MD-2/TLR4
Barker, J. H., & Weiss, J. P. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mir1118-434r · Cited by 34
The Proinflammatory Role of Guanylate-Binding Protein 5 in Inflammatory Bowel Diseases
Li, Y., Lin, X., Gao, S., Wang, W., Cheng, S., Wang, W., Huang, Y., 邹一丰, Zhu, L., Jia, K., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.926915 · Cited by 34
Antimicrobial inflammasomes: unified signalling against diverse bacterial pathogens
Eldridge, M. J. G., & Shenoy, A. R. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.10.008 · Cited by 33
TRIF signaling is required for caspase-11-dependent immune responses and lethality in sepsis
Tang, Y., Zhang, R., Xue, Q., Meng, R., Wang, X., Yang, Y., Xie, L., Xiao, X., Billiar, T. R., & Lü, B. (2018) · Molecular Medicine · doi:10.1186/s10020-018-0065-y · Cited by 32
Interferon-Induced Guanylate-Binding Proteins Promote Cytosolic Lipopolysaccharide Detection by Caspase-11
Meunier, É., & Brož, P. (2014) · DNA and Cell Biology · doi:10.1089/dna.2014.2701 · Cited by 32
Fight or flight
Croker, B. A., Silke, J., & Gerlic, M. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000148 · Cited by 33
Interferon-γ in Salmonella pathogenesis: New tricks for an old dog
Ingram, J. P., Brodsky, I. E., & Balachandran, S. (2016) · Cytokine · doi:10.1016/j.cyto.2016.10.009 · Cited by 32
NLRP11 is a pattern recognition receptor for bacterial lipopolysaccharide in the cytosol of human macrophages
Rojas-López, M., Zajac, A. S., Kharbanda, V., Miller, K. A., Gil-Marqués, M. L., Hachey, A. C., Kharbanda, V., Egger, K. T., & Goldberg, M. B. (2023) · Science Immunology · doi:10.1126/sciimmunol.abo4767 · Cited by 31
Guanylate-binding proteins at the crossroad of noncanonical inflammasome activation during bacterial infections
Gomes, M. T. R., Cerqueira, D. M., Guimarães, E. S., Campos, P. C., & Oliveira, S. C. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.4mr0119-013r · Cited by 32
IRF8 Regulates Gram-Negative Bacteria–Mediated NLRP3 Inflammasome Activation and Cell Death
Karki, R., Lee, E., Sharma, B. R., Banoth, B., & Kanneganti, T. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1901508 · Cited by 31
The non-canonical inflammasome activators Caspase-4 and Caspase-5 are differentially regulated during immunosuppression-associated organ damage
Ghait, M., Duduskar, S. N., Rooney, M. D., Häfner, N., Reng, L., Göhrig, B., Reuken, P. A., Bloos, F., Bauer, M. W., Sponholz, C., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1239474 · Cited by 30
Inflammasome‐mediated pyroptosis in defense against pathogenic bacteria
Oh, C., Spears, T. J., & Aachoui, Y. (2024) · Immunological Reviews · doi:10.1111/imr.13408 · Cited by 31
Identification of a systemic interferon-γ inducible antimicrobial gene signature in leprosy patients undergoing reversal reaction
Teles, R. M. B., Lu, J. N., Tió‐Coma, M., Goulart, I. M. B., Banu, S., Hagge, D. A., Bobosha, K., Ottenhoff, T. H. M., Pellegrini, M. A., Geluk, A., et al. (2019) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0007764 · Cited by 28
The Yersinia Type III Secretion System as a Tool for Studying Cytosolic Innate Immune Surveillance
Schubert, K., Xu, Y., Shao, F., & Auerbuch, V. (2020) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-120221 · Cited by 25
Caspase-11 Non-canonical Inflammasomes in the Lung
Oh, C., Verma, A., & Aachoui, Y. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01895 · Cited by 28
Role of Gate-16 and Gabarap in Prevention of Caspase-11-Dependent Excess Inflammation and Lethal Endotoxic Shock
Sakaguchi, N., Sasai, M., Bando, H., Lee, Y., Pradipta, A., Su, J., & Yamamoto, M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.561948 · Cited by 27
Self-citation
Human macrophages utilize a wide range of pathogen recognition receptors to recognize Legionella pneumophila, including Toll-Like Receptor 4 engaging Legionella lipopolysaccharide and the Toll-like Receptor 3 nucleic-acid sensor
Grigoryeva, L. S., & Cianciotto, N. P. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009781 · Cited by 27
Caspase-11 Noncanonical Inflammasome: A Novel Key Player in Murine Models of Neuroinflammation and Multiple Sclerosis
Yi, Y. (2021) · NeuroImmunoModulation · doi:10.1159/000516064 · Cited by 28
Inflammasome biology taught by Legionella pneumophila
Mascarenhas, D. P. A., & Zamboni, D. S. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.3mr0916-380r · Cited by 30
Diverse pro-inflammatory endotoxin recognition systems of mammalian innate immunity
Weiss, J. P., & Barker, J. H. (2018) · F1000Research · doi:10.12688/f1000research.13977.1 · Cited by 28
Essential Role of mGBP7 for Survival of Toxoplasma gondii Infection
Steffens, N., Beuter-Gunia, C., Kravets, E., Reich, A., Legewie, L., Pfeffer, K., & Degrandi, D. (2020) · mBio · doi:10.1128/mbio.02993-19 · Cited by 26
Self-citation
Vying for the control of inflammasomes: The cytosolic frontier of enteric bacterial pathogen–host interactions
Sanchez‐Garrido, J., Slater, S. L., Clements, A., Shenoy, A. R., & Frankel, G. M. (2020) · Cellular Microbiology · doi:10.1111/cmi.13184 · Cited by 24
The regulation of acute immune responses to the bacterial lung pathogenLegionella pneumophila
Brown, A. S., Yang, C., Hartland, E. L., & van Driel, I. R. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0816-340r · Cited by 25
Sweet host revenge: Galectins and GBPs join forces at broken membranes
Coers, J. (2017) · Cellular Microbiology · doi:10.1111/cmi.12793 · Cited by 27
Self-citation
Interferon inducible GBPs restrict Burkholderia thailandensis motility induced cell-cell fusion
Place, D. E., Briard, B., Samir, P., Karki, R., Bhattacharya, A., Guy, C. S., Peters, J. L., Frase, S., Vogel, P., Neale, G. A. M., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008364 · Cited by 26
Self-citation
TYK2 licenses non-canonical inflammasome activation during endotoxemia
Poelzl, A., Lassnig, C., Tangermann, S., Hromadová, D., Reichart, U., Gawish, R., Mueller, K. M., Moriggl, R., Linkermann, A., Glösmann, M., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00621-x · Cited by 26
An Update on CARD Only Proteins (COPs) and PYD Only Proteins (POPs) as Inflammasome Regulators
Devi, S., Stehlik, C., & Dorfleutner, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186901 · Cited by 24
Identification of a Prognosis-Related Risk Signature for Bladder Cancer to Predict Survival and Immune Landscapes
Wang, L., Wang, Y., Wang, J., Li, L., & Bi, J. (2021) · Journal of Immunology Research · doi:10.1155/2021/3236384 · Cited by 28
Interactions of Autophagy and the Immune System in Health and Diseases
Pant, A., Yao, X., Lavedrine, A., Viret, C., Dockterman, J., Chauhan, S. C., Shi, C.-S., Manjithaya, R. R., Cadwell, K., Kufer, T. A., et al. (2022) · Autophagy Reports · doi:10.1080/27694127.2022.2119743 · Cited by 28
Self-citation
An updated view on the functions of caspases in inflammation and immunity
Songane, M., Khair, M., & Saleh, M. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.01.001 · Cited by 27
Bacterial outer membrane vesicles and their functionalization as vehicles for bioimaging, diagnosis and therapy
Xue, K., Wang, L., & Liu, J. (2022) · Materials Advances · doi:10.1039/d2ma00420h · Cited by 27
Catalytic activity and autoprocessing of murine caspase-11 mediate noncanonical inflammasome assembly in response to cytosolic LPS
Akuma, D., Wodzanowski, K. A., Wertman, R. S., Exconde, P. M., Marrero, V. R. V., Odunze, C. E., Grubaugh, D., Shin, S., Taabazuing, C. Y., & Brodsky, I. E. (2023) · eLife · doi:10.7554/elife.83725 · Cited by 26
Pan-caspase inhibitors induce necroptosis via ROS-mediated activation of mixed lineage kinase domain-like protein and p38 in classically activated macrophages
Koike, A., Hanatani, M., & Fujimori, K. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.04.027 · Cited by 25
Interferon-induced GTPases orchestrate host cell-autonomous defence against bacterial pathogens
Rafeld, H. L., Kolanus, W., van Driel, I. R., & Hartland, E. L. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200900 · Cited by 23
SdhA blocks disruption of the Legionella-containing vacuole by hijacking the OCRL phosphatase
Choi, W. Y., Kim, S., Auraß, P., Huo, W., Creasey, E. A., Edwards, M., Lowe, M., & Isberg, R. R. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109894 · Cited by 24
Lipid A Variants Activate Human TLR4 and the Noncanonical Inflammasome Differently and Require the Core Oligosaccharide for Inflammasome Activation
Alexander-Floyd, J., Bass, A. R., Harberts, E. M., Grubaugh, D., Buxbaum, J. D., Brodsky, I. E., Ernst, R. K., & Shin, S. (2022) · Infection and Immunity · doi:10.1128/iai.00208-22 · Cited by 25
Self-citation
Human GBP1 facilitates the rupture of the Legionella- containing vacuole and inflammasome activation
Bass, A. R., Egan, M. S., Alexander-Floyd, J., Fischer, N. L., Doerner, J., & Shin, S. (2023) · mBio · doi:10.1128/mbio.01707-23 · Cited by 23
Dangerous Liaisons: Caspase-11 and Reactive Oxygen Species Crosstalk in Pathogen Elimination
Roberts, J. S., & Yilmaz, Ö. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161023337 · Cited by 24
New Insights on the Early Interaction Between Typhoid and Non-typhoid Salmonella Serovars and the Host Cells
Schultz, B. M., Melo-González, F., Salazar, G. A., Porto, B. N., Riedel, C. A., Kalergis, A. M., & Bueno, S. M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.647044 · Cited by 24
Guanylate-binding proteins induce apoptosis of leukemia cells by regulating MCL-1 and BAK
Luo, Y., Jin, H., Kim, J. H., & Bae, J. (2021) · Oncogenesis · doi:10.1038/s41389-021-00341-y · Cited by 24
Guanylate-Binding Protein-Dependent Noncanonical Inflammasome Activation Prevents Burkholderia thailandensis-Induced Multinucleated Giant Cell Formation
Dilucca, M., Ramos, S., Shkarina, K., Santos, J. C., & Brož, P. (2021) · mBio · doi:10.1128/mbio.02054-21 · Cited by 24
Legionella pneumophila , a Rosetta stone to understanding bacterial pathogenesis
Romanov, K. A., & O’Connor, T. J. (2024) · Journal of Bacteriology · doi:10.1128/jb.00324-24 · Cited by 22
Cytosolic detection of phagosomal bacteria—Mechanisms underlying PAMP exodus from the phagosome into the cytosol
Ragland, S. A., & Kagan, J. C. (2021) · Molecular Microbiology · doi:10.1111/mmi.14841 · Cited by 22
Francisella Inflammasomes: Integrated Responses to a Cytosolic Stealth Bacterium
Wallet, P., Lagrange, B., & Henry, T. (2016) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-41171-2_12 · Cited by 27
Noncanonical inflammasomes: Antimicrobial defense that does not play by the rules
Crowley, S. M., Vallance, B. A., & Knodler, L. A. (2017) · Cellular Microbiology · doi:10.1111/cmi.12730 · Cited by 24
The Role of Lipids in Legionella-Host Interaction
Kowalczyk, B., Chmiel, E., & Palusińska‐Szysz, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031487 · Cited by 22
Proteomic analysis of P. gingivalis-Lipopolysaccharide induced neuroinflammation in SH-SY5Y and HMC3 cells
Verma, A., Azhar, G., Patyal, P., Zhang, W., Zhang, X., & Wei, J. Y. (2024) · GeroScience · doi:10.1007/s11357-024-01117-z · Cited by 22
Fundamental and emerging insights into innate and adaptive immunity in inflammatory bowel diseases
Monteleone, G., Calisi, C., Salvatori, S., & Marafini, I. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1665530 · Cited by 24
Zebrafish Models to Study Inflammasome-Mediated Regulation of Hematopoiesis
Rodríguez‐Ruiz, L., Lozano‐Gil, J. M., Lachaud, C., Mesa-del-Castillo, P., Cayuela, M. L., García‐Moreno, D., Pérez‐Oliva, A. B., & Mulero, V. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.10.006 · Cited by 20
Regulatory Roles of Flavonoids in Caspase-11 Non-Canonical Inflammasome-Mediated Inflammatory Responses and Diseases
Yi, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210402 · Cited by 21
Evolution of Cell-Autonomous Effector Mechanisms in Macrophages versus Non-Immune Cells
Gaudet, R. G., Bradfield, C. J., & MacMicking, J. D. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0050-2016 · Cited by 23

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: Haldar, Arun K.
Degrandi, Daniel
Pfeffer, Klaus
Ernst, Robert K.
Yamamoto, Masahiro
Miao, Edward A.
Coers, Jörn
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
DOI: 10.1073/pnas.1321700111
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

Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks