Cited by 244Inflammasome and immune disordersImmune Response and InflammationIL-33, ST2, and ILC Pathways

The DOI matches its Crossref record; 153 of the 153 references it cites were found in a registry or an index.

Inflammasome Priming in Sterile Inflammatory Disease

Patel, Meghana N., Carroll, Richard G., Galván-Peña, Silvia, Mills, Evanna L., Olden, Robin, Triantafilou, Martha, Wolf, Amaya I., Bryant, Clare E., Triantafilou, Kathy, Masters, Seth L.·2017·Trends in Molecular Medicine

DOI 10.1016/j.molmed.2016.12.007

Open this paper in CoChat — free account

Abstract

The inflammasome is a cytoplasmic protein complex that processes interleukins (IL)-1β and IL-18, and drives a form of cell death known as pyroptosis. Oligomerization of this complex is actually the second step of activation, and a priming step must occur first. This involves transcriptional upregulation of pro-IL-1β, inflammasome sensor NLRP3, or the non-canonical inflammasome sensor caspase-11. An additional aspect of priming is the post-translational modification of particular inflammasome constituents. Priming is typically accomplished in vitro using a microbial Toll-like receptor (TLR) ligand. However, it is now clear that inflammasomes are activated during the progression of sterile inflammatory diseases such as atherosclerosis, metabolic disease, and neuroinflammatory disorders. Therefore, it is time to consider the endogenous factors and mechanisms that may prime the inflammasome in these conditions.

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 · 10.1016/j.molmed.2016.12.007

Cites

153 of 153 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.

2 retracted

RETRACTED: mTORC1-Induced HK1-Dependent Glycolysis Regulates NLRP3 Inflammasome Activation
Moon, J.-S., Hisata, S., Park, M. A., DeNicola, G. M., Ryter, S. W., Nakahira, K., & Choi, A. M. K. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.046 · Cited by 379
Retracted
UCP2-induced fatty acid synthase promotes NLRP3 inflammasome activation during sepsis
Moon, J.-S., Lee, S., Park, M.-A., Siempos, I. I., Haslip, M., Lee, P. J., Yun, M., Kim, C. K., Howrylak, J., Ryter, S. W., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78253 · Cited by 238
Retracted
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602
The Inflammasomes
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475
Obesity induces a phenotypic switch in adipose tissue macrophage polarization
Lumeng, C. N., Bodzin, J. L., & Saltiel, A. R. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29881 · Cited by 4,664
Succinate is an inflammatory signal that induces IL-1β through HIF-1α
Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176
Self-citation
NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
Duewell, P., Kono, H., Rayner, K. J., Sirois, C. M., Vladimer, G., Bauernfeind, F. G., Abela, G. S., Franchi, L., Nuñez, G., Schnurr, M., et al. (2010) · Nature · doi:10.1038/nature08938 · Cited by 4,026
Inflammasomes: mechanism of action, role in disease, and therapeutics
Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340
Cutting Edge: NF-κB Activating Pattern Recognition and Cytokine Receptors License NLRP3 Inflammasome Activation by Regulating NLRP3 Expression
Bauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,087
Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898
Mechanism and Regulation of NLRP3 Inflammasome Activation
He, Y., Hara, H., & Núñez, G. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.002 · Cited by 2,759
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708
The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance
Vandanmagsar, B., Youm, Y.-H., Ravussin, A., Galgani, J. E., Stadler, K., Mynatt, R. L., Ravussin, E., Stephens, J. M., & Dixit, V. D. (2011) · Nature Medicine · doi:10.1038/nm.2279 · Cited by 2,655
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613
Inflammasome-mediated dysbiosis regulates progression of NAFLD and obesity
Henao-Mejia, J., Elinav, E., Jin, C., Hao, L., Mehal, W. Z., Strowig, T., Thaiss, C. A., Kau, A. L., Eisenbarth, S. C., Jurczak, M. J., et al. (2012) · Nature · doi:10.1038/nature10809 · Cited by 2,435
Inflammatory caspases are innate immune receptors for intracellular LPS
Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F. (2014) · Nature · doi:10.1038/nature13683 · Cited by 2,285
Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282
Self-citation
NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production?
Tschopp, J., & Schroder, K. (2010) · Nature reviews. Immunology · doi:10.1038/nri2725 · Cited by 1,859
Immunometabolism governs dendritic cell and macrophage function
O'Neill, L. A. J., & Pearce, E. J. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20151570 · Cited by 1,779
NALP3 Forms an IL-1β-Processing Inflammasome with Increased Activity in Muckle-Wells Autoinflammatory Disorder
Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., & Tschopp, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00046-9 · Cited by 1,768
Fatty acid–induced NLRP3-ASC inflammasome activation interferes with insulin signaling
Wen, H., Gris, D., Lei, Y., Jha, S., Zhang, L., Huang, M. T.-H., Brickey, W. J., & Ting, J. P.-Y. (2011) · Nature Immunology · doi:10.1038/ni.2022 · Cited by 1,698
The Inflammasome NLRs in Immunity, Inflammation, and Associated Diseases
Davis, B. K., Wen, H., & Ting, J. P.-Y. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101405 · Cited by 1,618
Itaconate Links Inhibition of Succinate Dehydrogenase with Macrophage Metabolic Remodeling and Regulation of Inflammation
Lampropoulou, V., Sergushichev, A., Bambousková, M., Nair, S., Vincent, E. E., Loginicheva, E., Cervantes‐Barragán, L., Ma, X., Huang, S. C., Griss, T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.004 · Cited by 1,583
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
Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
Masters, S. L., Dunne, A., Subramanian, S. L., Hull, R. L., Tannahill, G. M., Sharp, F. A., Becker, C., Franchi, L., Yoshihara, E., Chen, Z., et al. (2010) · Nature Immunology · doi:10.1038/ni.1935 · Cited by 1,330 · cited 7×
“Oxidized LDL is shown to provide both signal 1 and signal 2 to prime and activate NLRP3 inflammasome in mouse models of atherosclerosis [52] and islet amyloid polypeptide (IAPP)-induced inflammasome activation in type 2 diabetes (T2D) ([31]).”
InfluentialSelf-citation
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
Therapeutic targeting of microRNAs: current status and future challenges
Li, Z., & Rana, T. M. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4359 · Cited by 1,052
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
SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene
Yokoyama, C., Wang, X., Briggs, M. R., Admon, A., Wu, J., Hua, X., Goldstein, J. L., & Brown, M. S. (1993) · Cell · doi:10.1016/s0092-8674(05)80095-9 · Cited by 975
Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation
Iyer, S. S., He, Q., Janczy, J. R., Elliott, E. I., Zhong, Z., Olivier, A. K., Sadler, J. J., Knepper-Adrian, V., Han, R., Qiao, L., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.001 · Cited by 968
CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation
Sheedy, F. J., Grebe, A., Rayner, K. J., Kalantari, P., Ramkhelawon, B., Carpenter, S. B., Becker, C. E., Ediriweera, H. N., Mullick, A. E., Golenbock, D. T., et al. (2013) · Nature Immunology · doi:10.1038/ni.2639 · Cited by 935
Caspase-8 regulates TNF-α-induced epithelial necroptosis and terminal ileitis
Günther, C., Martini, E., Wittkopf, N., Amann, K., Weigmann, B., Neumann, H., Waldner, M. J., Hedrick, S. Μ., Tenzer, S., Neurath, M. F., et al. (2011) · Nature · doi:10.1038/nature10400 · Cited by 882
NLRP3 inflammasome and its inhibitors: a review
Shao, B.-Z., Xu, Z.-Q., Han, B.-Z., Su, D.-F., & Liu, C. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00262 · Cited by 836 · cited 1×
“There are many excellent recent reviews highlighting the discovery and novel mechanistic understanding of small-molecule inhibitors for NLRs and caspases, and the preclinical/ clinical impact of targeting the inflammasome products IL-1β and IL-18 in disease [138, 139, 140, 141, 142] .”
Non-transcriptional Priming and Deubiquitination Regulate NLRP3 Inflammasome Activation
Juliana, C. A., Fernandes‐Alnemri, T., Kang, S., Farias, A., Qin, F., & Alnemri, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407130 · Cited by 803
Upregulated NLRP3 Inflammasome Activation in Patients With Type 2 Diabetes
Lee, H., Kim, J.-J., Kim, H. J., Shong, M., Ku, B. J., & Jo, E. (2012) · Diabetes · doi:10.2337/db12-0420 · Cited by 745
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
Interleukin-1β-Induced Insulin Resistance in Adipocytes through Down-Regulation of Insulin Receptor Substrate-1 Expression
Jager, J., Grémeaux, T., Cormont, M., MARCHAND‐BRUSTEL, Y. L., & Tanti, J. (2006) · Endocrinology · doi:10.1210/en.2006-0692 · Cited by 727
Inflammasome is a central player in the induction of obesity and insulin resistance
Stienstra, R., van Diepen, J. A., Tack, C. J., Zaki, M. H., van de Veerdonk, F. L., Perera, D., Neale, G. A., Hooiveld, G. J., Hijmans, A., Vroegrijk, I., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100255108 · Cited by 727
Adipokines Mediate Inflammation and Insulin Resistance
Kwon, H., & Pessin, J. E. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00071 · Cited by 723
Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity
Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718
Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome
Iyer, S. S., Pulskens, W. P., Sadler, J. J., Butter, L. M., Teske, G. J., Ulland, T. K., Eisenbarth, S. C., Florquin, S., Flavell, R. A., Leemans, J. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908698106 · Cited by 691
Loss-of-function mutations in TNFAIP3 leading to A20 haploinsufficiency cause an early-onset autoinflammatory disease
Zhou, Q., Wang, H., Schwartz, D. M., Stoffels, M., Park, Y. H., Zhang, Y., Yang, D., Demirkaya, E., Takeuchi, M., Tsai, W. L., et al. (2015) · Nature Genetics · doi:10.1038/ng.3459 · Cited by 658
Cutting Edge: Reactive Oxygen Species Inhibitors Block Priming, but Not Activation, of the NLRP3 Inflammasome
Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Núñez, G., & Hornung, V. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100613 · Cited by 617
Characterization of a functional NF-kappa B site in the human interleukin 1 beta promoter: evidence for a positive autoregulatory loop.
Hiscott, J., Marois, J., Garoufalis, J., D'Addario, M., Roulston, A., Kwan, I., Pepin, N., Lacoste, J., Nguyen, H., & Bensi, G. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6231 · Cited by 585
Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies
Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055375 · Cited by 585
An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells
Zanoni, I., Tan, Y., Di Gioia, M., Broggi, A., Ruan, J., Shi, J., Donado, C. A., Shao, F., Wu, H., Springstead, J. R., et al. (2016) · Science · doi:10.1126/science.aaf3036 · Cited by 583
Cutting Edge: TNF-α Mediates Sensitization to ATP and Silica via the NLRP3 Inflammasome in the Absence of Microbial Stimulation
Franchi, L., Eigenbrod, T., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900173 · Cited by 574
FADD and Caspase-8 Mediate Priming and Activation of the Canonical and Noncanonical Nlrp3 Inflammasomes
Gurung, P., Anand, P., Malireddi, R. K. S., Walle, L. V., Opdenbosch, N. V., Dillon, C. P., Weinlich, R., Green, D. R., Lamkanfi, M., & Kanneganti, T. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302839 · Cited by 558
SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element.
Hua, X., Yokoyama, C., Wu, J., Briggs, M. R., Brown, M. S., Goldstein, J. L., & Wang, X. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.24.11603 · Cited by 544
Caspase-11 Protects Against Bacteria That Escape the Vacuole
Aachoui, Y., Leaf, I. A., Hagar, J. A., Fontana, M. F., Campos, C. G., Zak, D. E., Tan, M. H., Cotter, P. A., Vance, R. E., Aderem, A. A., et al. (2013) · Science · doi:10.1126/science.1230751 · Cited by 544
NLRP3 inflammasome activity is negatively controlled by miR-223
Bauernfeind, F., Rieger, A., Schildberg, F. A., Knolle, P. A., Schmid-Burgk, J. L., & Hornung, V. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201516 · Cited by 544
Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M. (2012) · Nature · doi:10.1038/nature11419 · Cited by 535
Circulating Oxidized LDL Is a Useful Marker for Identifying Patients With Coronary Artery Disease
Holvoet, P., Mertens, A. C., Verhamme, P. B., Bogaerts, K., Beyens, G., Verhaeghe, R., Collen, D., Muls, E., & de Werf, F. V. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.21.5.844 · Cited by 530
Negative regulation of the NLRP3 inflammasome by A20 protects against arthritis
Walle, L. V., Opdenbosch, N. V., Jacques, P., Fossoul, A., Verheugen, E., Vogel, P., Beyaert, R., Elewaut, D. S., Kanneganti, T., Loo, G., et al. (2014) · Nature · doi:10.1038/nature13322 · Cited by 515
Lipid homeostasis, lipotoxicity and the metabolic syndrome
Unger, R. H., Clark, G. O., Scherer, P. E., & Orci, L. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.10.006 · Cited by 511
The Membrane Attack Complex of Complement
Müller‐Eberhard, H. J. (1986) · Annual Review of Immunology · doi:10.1146/annurev.iy.04.040186.002443 · Cited by 507
Inflammasomes in liver diseases
Szabó, G., & Csák, T. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.03.035 · Cited by 498
NLRP3 inflammasome activation is required for fibrosis development in NAFLD
Wree, A., McGeough, M. D., Peña, C. A., Schlattjan, M., Li, H., Inzaugarat, M. E., Messer, K., Canbay, A., Hoffman, H. M., & Feldstein, A. E. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1170-1 · Cited by 486
Detection and localization of tumor necrosis factor in human atheroma
Barath, P., Fishbein, M. C., Cao, J., Berenson, J. R., Helfant, R. H., & Forrester, J. S. (1990) · The American Journal of Cardiology · doi:10.1016/0002-9149(90)90291-8 · Cited by 448
Endoplasmic Reticulum Stress Activates the Inflammasome via NLRP3- and Caspase-2-Driven Mitochondrial Damage
Bronner, D. N., Abuaita, B. H., Chen, X., Fitzgerald, K. A., Núñez, G., He, Y. O., Yin, X., & O’Riordan, M. X. (2015) · Immunity · doi:10.1016/j.immuni.2015.08.008 · Cited by 447
Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-κB
Frede, S., Stockmann, C., Freitag, P., & Fandrey, J. (2006) · Biochemical Journal · doi:10.1042/bj20051839 · Cited by 436
Effects of ACL Reconstructive Surgery on Temporal Variations of Cytokine Levels in Synovial Fluid
Bigoni, M., Turati, M., Gandolla, M., Sacerdote, P., Piatti, M., Castelnuovo, A., Franchi, S., Gorla, M., Munegato, D., Gaddi, D., et al. (2016) · Mediators of Inflammation · doi:10.1155/2016/8243601 · Cited by 431
ER stress induces NLRP3 inflammasome activation and hepatocyte death
Lebeaupin, C., Proïcs, E., de Bieville, C.-H. D., Rousseau, D., Bonnafous, S., Patouraux, S., Adam, G., Lavallard, V., Rovère, C., Thuc, O. L., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.248 · Cited by 413
The G protein-coupled receptor kinase (GRK) interactome: Role of GRKs in GPCR regulation and signaling
Ribas, C., Penela, P., Murga, C., Salcedo, A., García‐Hoz, C., Jurado-Pueyo, M., Aymerich, I., & Mayor, F. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.019 · Cited by 409
Targeting the NLRP3 inflammasome in chronic inflammatory diseases: current perspectives
Doyle, S., Ozaki, E., & Campbell, M. (2015) · Journal of Inflammation Research · doi:10.2147/jir.s51250 · Cited by 389
Complement membrane attack on nucleated cells: resistance, recovery and non-lethal effects
Morgan, B. P. (1989) · Biochemical Journal · doi:10.1042/bj2640001 · Cited by 383
Gene expression, synthesis, and secretion of interleukin 18 and interleukin 1β are differentially regulated in human blood mononuclear cells and mouse spleen cells
Puren, A. J., Fantuzzi, G., & Dinarello, C. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2256 · Cited by 379
NLRP3 inflammasome activation downstream of cytoplasmic LPS recognition by both caspase‐4 and caspase‐5
Baker, P. J., Boucher, D., Bierschenk, D., Tebartz, C., Whitney, P. G., D’Silva, D. B., Tanzer, M. C., Monteleone, M. M., Robertson, A. A. B., Cooper, M. A., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545655 · Cited by 370
Self-citation
The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation
Triantafilou, K., Hughes, T. R., Triantafilou, M., & Morgan, B. P. (2013) · Journal of Cell Science · doi:10.1242/jcs.124388 · Cited by 361
Self-citation
MicroRNA therapeutics: Discovering novel targets and developing specific therapy
Bansal, P., Christopher, A., Kaur, R., Kaur, G., Kaur, A., & Gupta, V. (2016) · Perspectives in Clinical Research · doi:10.4103/2229-3485.179431 · Cited by 360
Dimethylfumarate inhibits microglial and astrocytic inflammation by suppressing the synthesis of nitric oxide, IL-1β, TNF-α and IL-6 in an in-vitro model of brain inflammation
Wilms, H., Sievers, J., Rickert, U., Rostami‐Yazdi, M., Mrowietz, U., & Lucius, R. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-30 · Cited by 355
Molecular mechanisms involved in inflammasome activation
Bryant, C. E., & Fitzgerald, K. A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.06.002 · Cited by 351
Self-citation
Mutant superoxide dismutase 1-induced IL-1β accelerates ALS pathogenesis
Meissner, F., Molawi, K., & Zychlinsky, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002396107 · Cited by 332
Complement-mediated regulation of the IL-17A axis is a central genetic determinant of the severity of experimental allergic asthma
Lajoie, S., Lewkowich, I. P., Suzuki, Y., Clark, J. R., Sproles, A. A., Dienger, K. M., Budelsky, A., & Wills-Karp, M. A. (2010) · Nature Immunology · doi:10.1038/ni.1926 · Cited by 329
Long-term treatment with interleukin-1β induces insulin resistance in murine and human adipocytes
Lagathu, C., Yvan‐Charvet, L., Bastard, J., Maachi, M., Quignard‐Boulangé, A., Capeau, J., & Caron, M. (2006) · Diabetologia · doi:10.1007/s00125-006-0335-z · Cited by 328
C3a modulates IL-1β secretion in human monocytes by regulating ATP efflux and subsequent NLRP3 inflammasome activation
Asgari, E., Friec, G. L., Yamamoto, H., Perucha, E., Sacks, S. H., Köhl, J., Cook, H. T., & Kemper, C. (2013) · Blood · doi:10.1182/blood-2013-05-502229 · Cited by 321
The Metabolic Syndrome, Circulating Oxidized LDL, and Risk of Myocardial Infarction in Well-Functioning Elderly People in the Health, Aging, and Body Composition Cohort
Holvoet, P., Kritchevsky, S. B., Tracy, R. P., Mertens, A. C., Rubin, S. M., Butler, J., Goodpaster, B. H., & Harris, T. B. (2004) · Diabetes · doi:10.2337/diabetes.53.4.1068 · Cited by 318
IRGB10 Liberates Bacterial Ligands for Sensing by the AIM2 and Caspase-11-NLRP3 Inflammasomes
Man, S. M., Karki, R., Sasai, M., Place, D. E., Kesavardhana, S., Temirov, J., Frase, S., Zhu, Q., Malireddi, R. K. S., Kuriakose, T., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.012 · Cited by 312
Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection
Ichinohe, T., Yamazaki, T., Koshiba, T., & Yanagi, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312571110 · Cited by 291
Cholesterol Crystals Induce Complement-Dependent Inflammasome Activation and Cytokine Release
Samstad, E. O., Niyonzima, N., Nymo, S. H., Aune, M. H., Ryan, L., Bakke, S. S., Lappegård, K. T., Brekke, O., Lambris, J. D., Damås, J. K., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302484 · Cited by 286
LXRs link metabolism to inflammation through Abca1-dependent regulation of membrane composition and TLR signaling
Ito, A., Hong, C., Rong, X., Zhu, X., Tarling, E. J., Hedde, P. N., Gratton, E., Parks, J., & Tontonoz, P. (2015) · eLife · doi:10.7554/elife.08009 · Cited by 281 · cited 1×
“Similarly, while the activation of LXRs reduces cholesterol and negatively regulates IL1Btranscription ([43]), activation of SREBPs not only increases cholesterol synthesis but also increases inflammasome priming, as shown in human umbilical vein endothelial cells (HUVEC) in vitro, and in mouse aortas in vivo([44]).”
S100A8 and S100A9 Induce Cytokine Expression and Regulate the NLRP3 Inflammasome via ROS-Dependent Activation of NF-κB1
Simard, J.-C., Césaro, A., Chapeton-Montes, J. A., Tardif, M. R., Antoine, F., Girard, D., & Tessier, P. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072138 · Cited by 274
TLR4 mutation reduces microglial activation, increases Aβ deposits and exacerbates cognitive deficits in a mouse model of Alzheimer’s disease
Song, M., Jin, J., Lim, J.-E., Kou, J., Pattanayak, A., Rehman, J. A., Kim, H.-D., Tahara, K., Lalonde, R., & Fukuchi, K.-I. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-92 · Cited by 273
Sterol Regulatory Element Binding Protein 2 Activation of NLRP3 Inflammasome in Endothelium Mediates Hemodynamic-Induced Atherosclerosis Susceptibility
Xiao, H., Lu, M., Lin, T. Y., Chen, Z., Chen, G., Wang, W.-C., Marin, T., Shentu, T.-P., Wen, L., Gongol, B., et al. (2013) · Circulation · doi:10.1161/circulationaha.113.002714 · Cited by 257
Basic Calcium Phosphate Crystals Induce Monocyte/Macrophage IL-1β Secretion through the NLRP3 Inflammasome In Vitro
Pazár, B., Ea, H., Narayan, S., Kolly, L., Bagnoud, N., Chobaz, V., Roger, T., Lioté, F., So, A. K.-L., & Busso, N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001284 · Cited by 252
Toll or Interleukin-1 Receptor (TIR) Domain-containing Adaptor Inducing Interferon-β (TRIF)-mediated Caspase-11 Protease Production Integrates Toll-like Receptor 4 (TLR4) Protein- and Nlrp3 Inflammasome-mediated Host Defense against Enteropathogens
Gurung, P., Malireddi, R. K. S., Anand, P., Demon, D., Walle, L. V., Liu, Z., Vogel, P., Lamkanfi, M., & Kanneganti, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401406 · Cited by 245
Cutting Edge: TLR Signaling Licenses IRAK1 for Rapid Activation of the NLRP3 Inflammasome
Fernandes‐Alnemri, T., Kang, S., Anderson, C., Sagara, J., Fitzgerald, K. A., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301681 · Cited by 243
Resident Macrophages Mediate Islet Amyloid Polypeptide–Induced Islet IL-1β Production and β-Cell Dysfunction
Westwell-Roper, C. Y., Ehses, J. A., & Verchere, C. B. (2013) · Diabetes · doi:10.2337/db13-0863 · Cited by 232
Modulatory mechanisms controlling the NLRP3 inflammasome in inflammation: recent developments
Haneklaus, M., O'Neill, L. A. J., & Coll, R. C. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2012.12.004 · Cited by 230
Inflammasome Priming by Lipopolysaccharide Is Dependent upon ERK Signaling and Proteasome Function
Ghonime, M. G., Shamaa, O. R., Das, S., El-Domany, R. A., Fernandes‐Alnemri, T., Alnemri, E. S., Gavrilin, M. A., & Wewers, M. D. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1301974 · Cited by 207
The membrane attack complex as an inflammatory trigger
Morgan, B. P. (2016) · Immunobiology · doi:10.1016/j.imbio.2015.04.006 · Cited by 205
Circulating Levels of Oxidative Stress Markers and Endothelial Adhesion Molecules in Men with Abdominal Obesity
Couillard, C., Ruel, G., Archer, W. R., Pomerleau, S., Bergeron, J., Couture, P., Lamarche, B., & Bergeron, N. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-2438 · Cited by 202
Cutting Edge: The NLRP3 Inflammasome Links Complement-Mediated Inflammation and IL-1β Release
Laudisi, F., Spreafico, R., Evrard, M., Hughes, T. R., Mandriani, B., Kandasamy, M., Morgan, B. P., Sivasankar, B., & Mortellaro, A. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300489 · Cited by 198
Dimethyl Fumarate Inhibits Dendritic Cell Maturation via Nuclear Factor κB (NF-κB) and Extracellular Signal-regulated Kinase 1 and 2 (ERK1/2) and Mitogen Stress-activated Kinase 1 (MSK1) Signaling
Peng, H., Guerau‐de‐Arellano, M., Mehta, V. B., Yang, Y., Huss, D. J., Papenfuss, T. L., Lovett‐Racke, A. E., & Racke, M. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.383380 · Cited by 196
Saturated Fatty Acids Engage an IRE1α-Dependent Pathway to Activate the NLRP3 Inflammasome in Myeloid Cells
Robblee, M. M., Kim, C. C., Abate, J. P., Valdearcos, M., Sandlund, K. L. M., Shenoy, M. K., Volmer, R., Iwawaki, T., & Koliwad, S. K. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.053 · Cited by 193
Reactive oxygen species activated NLRP3 inflammasomes initiate inflammation in hyperosmolarity stressed human corneal epithelial cells and environment-induced dry eye patients
Zheng, Q., Ren, Y., Reinach, P. S., Xiao, B., Lu, H., Zhu, Y., Qu, J., & Chen, W. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.02.013 · Cited by 181
C3a(C3adesArg) induces production and release of interleukin 1 by cultured human monocytes.
Haeffner‐Cavaillon, N., Cavaillon, J., Laude, M., & Kazatchkine, M. D. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.139.3.794 · Cited by 177
Immune Responsive Gene 1 (IRG1) Promotes Endotoxin Tolerance by Increasing A20 Expression in Macrophages through Reactive Oxygen Species
Li, Y., Zhang, P., Wang, C., Han, C., Meng, J., Liu, X., Xu, S., Li, N., Wang, Q., Shi, X., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.454538 · Cited by 177
Deubiquitinases Regulate the Activity of Caspase-1 and Interleukin-1β Secretion via Assembly of the Inflammasome
López‐Castejón, G., Luheshi, N., Compan, V., High, S., Whitehead, R. C., Flitsch, S. L., Kirov, A., Prudovsky, I. A., Swanton, E., & Brough, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422238 · Cited by 175
Dietary saturated fatty acids prime the NLRP 3 inflammasome via TLR 4 in dendritic cells—implications for diet‐induced insulin resistance
Reynolds, C. M., McGillicuddy, F. C., Harford, K. A., Finucane, O. M., Mills, K. H. G., & Roche, H. M. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200058 · Cited by 172
Prime time for PROTACs
Deshaies, R. J. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1887 · Cited by 162
Caspase-11 Gene Expression in Response to Lipopolysaccharide and Interferon-γ Requires Nuclear Factor-κB and Signal Transducer and Activator of Transcription (STAT) 1
Schauvliege, R., Vanrobaeys, J., Schotte, P., & Beyaert, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207852200 · Cited by 162
Pterostilbene and allopurinol reduce fructose-induced podocyte oxidative stress and inflammation via microRNA-377
Wang, W., Ding, X., Gu, T.-T., Song, L., Li, J., Xue, Q., & Kong, L. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.029 · Cited by 155
The relationship between oxidized LDL and other cardiovascular risk factors and subclinical CVD in different ethnic groups: The Multi-Ethnic Study of Atherosclerosis (MESA)
Holvoet, P., Jenny, N. S., Schreiner, P. J., Tracy, R. P., & Jacobs, D. R. (2006) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2006.08.002 · Cited by 149
Complement pathway amplifies caspase-11–dependent cell death and endotoxin-induced sepsis severity
Napier, B. A., Brubaker, S. W., Sweeney, T. E., Monette, P., Rothmeier, G. H., Gertsvolf, N. A., Puschnik, A., Carette, J. E., Khatri, P., & Monack, D. M. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160027 · Cited by 149
Moderate Hypoxia Potentiates Interleukin-1β Production in Activated Human Macrophages
Folco, E. J. E., Sukhova, G. K., Quillard, T., & Libby, P. (2014) · Circulation Research · doi:10.1161/circresaha.115.304437 · Cited by 148
Dimethyl fumarate ameliorates dextran sulfate sodium-induced murine experimental colitis by activating Nrf2 and suppressing NLRP3 inflammasome activation
Liu, X., Zhou, W., Zhang, X., Lü, P., Du, Q., Tao, L., Ding, Y., Wang, Y., & Hu, R. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.05.002 · Cited by 148
Chronic TLR Stimulation Controls NLRP3 Inflammasome Activation through IL-10 Mediated Regulation of NLRP3 Expression and Caspase-8 Activation
Gurung, P., Li, B., Malireddi, R. K. S., Lamkanfi, M., Geiger, T. L., & Kanneganti, T. (2015) · Scientific Reports · doi:10.1038/srep14488 · Cited by 147
CAPS — pathogenesis, presentation and treatment of an autoinflammatory disease
Kuemmerle-Deschner, J. B. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-015-0491-7 · Cited by 144
RAGE: A Multi-Ligand Receptor Unveiling Novel Insights in Health and Disease
Alexiou, P., Chatzopoulou, M., Pegklidou, K., & Demopoulos, V. J. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710791331086 · Cited by 140
Detection of immune danger signals by NALP3
Martinon, F. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0607362 · Cited by 140
Identification of a Locus on Chromosome 1q44 for Familial Cold Urticaria
Hoffman, H. M., Wright, F. A., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2000) · The American Journal of Human Genetics · doi:10.1086/302874 · Cited by 137
Pertussis Toxin-sensitive Activation of Phospholipase C by the C5a and fMet-Leu-Phe Receptors
Jiang, H., Kuang, Y., Wu, Y., Smrcka, A. V., Simon, M. I., & Wu, D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13430 · Cited by 137
Aging-Associated TNF Production Primes Inflammasome Activation and NLRP3-Related Metabolic Disturbances
Bauernfeind, F., Niepmann, S., Knolle, P. A., & Hornung, V. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501336 · Cited by 137
Disease-associated amyloid and misfolded protein aggregates activate the inflammasome
Masters, S. L., & O'Neill, L. A. J. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.01.005 · Cited by 134
Self-citation
The redox state of the alarmin HMGB1 is a pivotal factor in neuroinflammatory and microglial priming: A role for the NLRP3 inflammasome
Frank, M. G., Weber, M. D., Fonken, L. K., Hershman, S. A., Watkins, L. R., & Maier, S. F. (2016) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2015.10.009 · Cited by 133
Bacterial recognition pathways that lead to inflammasome activation
Storek, K. M., & Monack, D. M. (2015) · Immunological Reviews · doi:10.1111/imr.12289 · Cited by 132
Mutant SOD1 linked to familial amyotrophic lateral sclerosis, but not wild-type SOD1, induces ER stress in COS7 cells and transgenic mice
Tobisawa, S., Hozumi, Y., Arawaka, S., Koyama, S., Wada, M., Nagai, M., Aoki, M., Itoyama, Y., Goto, K., & Kato, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00353-x · Cited by 128
Crystal Formation in Inflammation
Franklin, B. S., Mangan, M., & Latz, E. (2016) · Annual Review of Immunology · doi:10.1146/annurev-immunol-041015-055539 · Cited by 125
Mapping of the C5a receptor signal transduction network in human neutrophils.
Buhl, A. M., Avdi, N. J., Worthen, G. S., & Johnson, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9190 · Cited by 123
C5a delays apoptosis of human neutrophils by a phosphatidylinositol 3-kinase-signaling pathway
Perianayagam, M. C., Balakrishnan, V. S., King, A. J., Pereira, B. J. G., & Jaber, B. L. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00139.x · Cited by 121
Gi-Protein-Dependent Inhibition of IL-12 Production Is Mediated by Activation of the Phosphatidylinositol 3-Kinase-Protein 3 Kinase B/Akt Pathway and JNK
la Sala, A., Gadina, M., & Kelsall, B. L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2994 · Cited by 107
MicroRNA-155–deficient dendritic cells cause less severe GVHD through reduced migration and defective inflammasome activation
Chen, S., Smith, B. A. H., Iype, J. M., Prestipino, A., Pfeifer, D., Grundmann, S., Schmitt-Graeff, A. H., Idzko, M., Beck, Y., Prinz, G., et al. (2015) · Blood · doi:10.1182/blood-2014-12-617258 · Cited by 107
Critical Role for Mast Cells in Interleukin-1β-Driven Skin Inflammation Associated with an Activating Mutation in the Nlrp3 Protein
Nakamura, Y., Franchi, L., Kambe, N., Meng, G., Strober, W., & Núñez, G. (2012) · Immunity · doi:10.1016/j.immuni.2012.04.013 · Cited by 107
Suppression of NLRP3 inflammasome by γ-tocotrienol ameliorates type 2 diabetes
Kim, Y., Wang, W., Okla, M., Kang, I., Moreau, R. F., & Chung, S. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m062828 · Cited by 100
Complement C5a activation of phospholipase D in human neutrophils. A major route to the production of phosphatidates and diglycerides.
Mullmann, T. J., Siegel, M. I., Egan, R. W., & Billah, M. M. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.5.1901 · Cited by 99
Reactive Oxygen Species Regulate Caspase-11 Expression and Activation of the Non-canonical NLRP3 Inflammasome during Enteric Pathogen Infection
Lupfer, C. R., Anand, P., Liu, Z., Stokes, K. L., Vogel, P., Lamkanfi, M., & Kanneganti, T. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004410 · Cited by 97
Negative regulation of NLRP3 inflammasome signaling
Chen, S., & Sun, B. (2013) · Protein & Cell · doi:10.1007/s13238-013-2128-8 · Cited by 84
Butyric acid in functional constipation
Pituch, A., Walkowiak, J., & Banaszkiewicz, A. (2013) · Gastroenterology Review · doi:10.5114/pg.2013.38731 · Cited by 80
MicroRNA-133a-1 regulates inflammasome activation through uncoupling protein-2
Bandyopadhyay, S., Lane, T., Rajanbabu, V., Parthasarathy, P. T., Cho, Y., Galam, L., Lockey, R. F., & Kolliputi, N. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.08.056 · Cited by 77
Complement Component C5a Primes Retinal Pigment Epithelial Cells for Inflammasome Activation by Lipofuscin-mediated Photooxidative Damage
Brandstetter, C., Holz, F. G., & Krohne, T. U. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.671180 · Cited by 72
Complement C5a potentiates uric acid crystal‐induced IL‐1β production
An, L., Mehta, P., Xu, L., Turman, S., Reimer, T., Naiman, B. M., Connor, J. R., Sanjuán, M. A. F., Kolbeck, R., & Fung, M. S. C. (2014) · European Journal of Immunology · doi:10.1002/eji.201444560 · Cited by 71
Complement-mediated ‘bystander’ damage initiates host NLRP3 inflammasome activation
Suresh, R., Chandrasekaran, P., Sutterwala, F. S., & Mosser, D. M. (2016) · Journal of Cell Science · doi:10.1242/jcs.179291 · Cited by 68
Sterile signals generate weaker and delayed macrophage NLRP3 inflammasome responses relative to microbial signals
Bezbradica, J. S., Coll, R. C., & Schroder, K. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.11 · Cited by 67
Ceramide triggers an NF-κB-dependent survival pathway through calpain
Demarchi, F., Bertoli, C., Greer, P. A., & Schneider, C. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401592 · Cited by 60
Histone deacetylase 6 negatively regulates NLRP3 inflammasome activation
Hwang, I., Lee, E., Jeon, S., & Yu, J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.10.033 · Cited by 55
Autoinflammatory Skin Disorders: The Inflammasome in Focus
Gurung, P., & Kanneganti, T. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.05.003 · Cited by 55
Differential Activation of Innate Immune Pathways by Distinct Islet Amyloid Polypeptide (IAPP) Aggregates
Westwell-Roper, C. Y., Denroche, H. C., Ehses, J. A., & Verchere, C. B. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.712455 · Cited by 54
Bidirectional Crosstalk between C5a Receptors and the NLRP3 Inflammasome in Macrophages and Monocytes
Haggadone, M. D., Grailer, J. J., Fattahi, F., Zetoune, F. S., & Ward, P. A. (2016) · Mediators of Inflammation · doi:10.1155/2016/1340156 · Cited by 50
Hypoxia primes human normal prostate epithelial cells and cancer cell lines for the NLRP3 and AIM2 inflammasome activation
Panchanathan, R., Liu, H., & Choubey, D. (2016) · Oncotarget · doi:10.18632/oncotarget.8594 · Cited by 46
Posttranscriptional control of NLRP3 inflammasome activation in colonic macrophages
Filardy, A. A., He, J., Bennink, J. R., Yewdell, J. W., & Kelsall, B. L. (2015) · Mucosal Immunology · doi:10.1038/mi.2015.109 · Cited by 45
A Comparative Analysis of Multiple Sclerosis–Relevant Anti-Inflammatory Properties of Ethyl Pyruvate and Dimethyl Fumarate
Miljković, D. M., Blaževski, J., Petković, F., Djedović, N., Momčilović, M. B., Stanisavljević, S., Jevtić, B., Stojković, M. M., & Spasojević, I. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402302 · Cited by 42
Hematopoietic IKBKE limits the chronicity of inflammasome priming and metaflammation
Patel, M. N., Bernard, W. G., Milev, N. B., Cawthorn, W. P., Figg, N. L., Hart, D., Prieur, X., Virtue, S., Hegyi, K., Bonnafous, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414536112 · Cited by 42
Self-citation
Early Upregulation of NLRP3 in the Brain of Neonatal Mice Exposed to Hypoxia-Ischemia: No Early Neuroprotective Effects of NLRP3 Deficiency
Ystgaard, M. B., Sejersted, Y., Løberg, E. M., Lien, E., Yndestad, A., & Saugstad, O. D. (2015) · Neonatology · doi:10.1159/000437247 · Cited by 41
Circulating oxidized LDL is associated with parameters of the metabolic syndrome in postmenopausal women
Lapointe, A., Couillard, C., Piché, M., Weisnagel, S. J., Bergeron, J., Nadeau, A., & Lemieux, S. (2006) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2006.03.036 · Cited by 36
Role of NLRP3 and CARD8 in the regulation of TNF-α induced IL-1β release in vascular smooth muscle cells
TANGI, T. N., Elmabsout, A. A., Bengtsson, T., Sirsjö, A., & Fransén, K. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1026 · Cited by 31
Whole-body insulin sensitivity, low-density lipoprotein (LDL) particle size, and oxidized LDL in overweight, nondiabetic men
Ho, R. C., Davy, K. P., Davy, B. M., & Melby, C. L. (2002) · Metabolism · doi:10.1053/meta.2002.35577 · Cited by 30
Permanent Culture of Macrophages at Physiological Oxygen Attenuates the Antioxidant and Immunomodulatory Properties of Dimethyl Fumarate
Haas, B., Chrusciel, S., Fayad‐Kobeissi, S., Dubois‐Randé, J., Azuaje, F. J., Boczkowski, J., Motterlini, R., & Foresti, R. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24844 · Cited by 26
Cobalt Chloride-induced Hypoxia Ameliorates NLRP3-Mediated Caspase-1 Activation in Mixed Glial Cultures
Kim, E., Won, J.-H., Hwang, I., & Yu, J. (2013) · Immune Network · doi:10.4110/in.2013.13.4.141 · Cited by 22
Target deletion of complement component 9 attenuates antibody-mediated hemolysis and lipopolysaccharide (LPS)-induced acute shock in mice
Fu, X., Ju, J., Lin, Z., Xiao, W., Li, X., Baoxiang, Z., Zhang, T., Ma, X., Li, X., Ma, C., et al. (2016) · Scientific Reports · doi:10.1038/srep30239 · Cited by 22
Suppression of caspase-11 expression by histone deacetylase inhibitors
Heo, H., Yoo, L., Shin, K. S., & Kang, S. J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.009 · Cited by 10
Inflammasome Activation: How Macrophages Watch What They Eat
Vance, R. E. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.011 · Cited by 7

Flagged first, then by citations

Research works printed but not linked: 4

Panchanathan, 2016, Hypoxia primes human normal prostate epithelial cells and cancer cell lines for the NLRP3 and AIM2 inflammasome activation, Oncotarget, 7, 28183, 10.18632/oncotarget.8594 · DOI
Masters, 2010, Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes, Nat. Immunol., 11, 897, 10.1038/ni.1935 · DOI · Paper page
Duewell, 2010, NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals, Nature, 464, 1357, 10.1038/nature08938 · DOI · Paper page
Juliana, 2012, Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation, J. Biol. Chem., 287, 36617, 10.1074/jbc.M112.407130 · DOI

Sorted by citations

Inflammation and its resolution in atherosclerosis: mediators and therapeutic opportunities
Bäck, M., Yurdagul, A., Tabas, I., Öörni, K., & Kovanen, P. T. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0169-2 · Cited by 1,341
Interleukin-1 Beta as a Target for Atherosclerosis Therapy
Libby, P. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2017.09.028 · Cited by 651
Mitochondrial Damage-Associated Molecular Patterns: From Inflammatory Signaling to Human Diseases
Grazioli, S., & Pugin, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00832 · Cited by 429
Small Molecule-Driven NLRP3 Inflammation Inhibition via Interplay between Ubiquitination and Autophagy: Implications for Parkinson Disease
Han, X., Sun, S., Sun, Y., Song, Q., Zhu, J., Song, N., Chen, M., Sun, T., Xia, M., Ding, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1596481 · Cited by 408
Melatonin prevents endothelial cell pyroptosis via regulation of long noncoding RNA MEG3/miR‐223/NLRP3 axis
Zhang, Y., Liu, X., Bai, X., Yuan, L., Li, Z., Fu, J., Li, M., Zhao, T., Yang, H., Xu, R., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12449 · Cited by 395

See all 244

Authors: Patel, M. N., Carroll, R. G., Galván-Peña, S., Mills, E. L., Olden, R., Triantafilou, M., Wolf, A. I., Bryant, C. E., Triantafilou, K., & Masters, S. L.
Affiliations: GlaxoSmithKline (United Kingdom) (GB)
GlaxoSmithKline (United States) (US)
The University of Melbourne (AU)
Corresponding author: Masters, Seth L.
ORCID: Carroll, Richard G.
Galván-Peña, Silvia
Mills, Evanna L.
Triantafilou, Martha
Wolf, Amaya I.
Bryant, Clare E.
Triantafilou, Kathy
Masters, Seth L.
Venue: Trends in Molecular Medicine
Publisher: Elsevier BV
Published: 2017-02
Volume: 23
Issue: 2
Pages: 165-180
ISSN: 1471-4914 (ISSN-L)
DOI: 10.1016/j.molmed.2016.12.007
OpenAlex: W2572287198
Cited by: 241
References: 153
Citations by year: 2026: 12 · 2025: 17 · 2024: 15 · 2023: 24 · 2022: 29 · 2021: 25 · 2020: 37 · 2019: 31 · 2018: 33 · 2017: 17
FWCI: 3.02
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Molecular Medicine (publishedVersion)
PubMed (publishedVersion)
ORCA Online Research @Cardiff (Cardiff University) (acceptedVersion)
ORCA Online Research @Cardiff (Cardiff University) (submittedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Immunology and Microbiology › Immunology › IL-33, ST2, and ILC Pathways
Keywords: inflammasome priming, sterile inflammation, NLRP3 inflammasome, caspase-11, IL-1β processing, IL-18, pyroptosis, post-translational modification, atherosclerosis, metabolic disorders, neuroinflammation, Toll-like receptor ligands
MeSH terms: NLR Family, Pyrin Domain-Containing 3 Protein, Alzheimer Disease, Animals, Humans, Immunity, Innate, Inflammation, Metabolic Diseases, Obesity, Neuroimmunomodulation, Atherosclerosis, Toll-Like Receptors, Interleukin-1beta, Hereditary Autoinflammatory Diseases, Inflammasomes

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Inflammasome Priming in Sterile Inflammatory Disease

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