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Metabolic regulation of NLRP 3
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Summary: A shift in our understanding of macrophage biology has come about as a result of recent discoveries in the area of metabolic reprogramming of macrophages. The NLRP 3 inflammasome drives the activation of caspase‐1, leading to the production of IL ‐1β, IL ‐18, and a type of cell death termed pyroptosis. The NLRP 3 inflammasome has been shown to sense metabolites such as palmitate, uric acid, and cholesterol crystals and is inhibited by ketone bodies produced during metabolic flux. The NLRP 3 inflammasome has also been shown to be regulated by mitochondrial reactive oxygen species and components of glycolysis, such as Hexokinase. Here, we review these findings and discuss their importance for inflammation and furthermore discuss potential therapeutic benefits of targeting NLRP 3.
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“A number of molecules in lipid metabolism pathways have been identified to regulate NLRP3 inflammasome activation [41].”
From HIV-TAT dysregulates microglial lipid metabolism through SREBP2/miR-124 axis: Implication of lipid droplet accumulation microglia in NeuroHIV (2025) · cites this paper as [41]
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3 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
RetractedMoon, J.-S., Nakahira, K., Chung, K.-P., DeNicola, G. M., Koo, M. J., Pabón, M. A., Rooney, K. T., Yoon, J.-H., Ryter, S. W., Stout-Delgado, H., et al. (2016) · Nature Medicine · doi:10.1038/nm.4153 · Cited by 291
RetractedUCP2-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
RetractedMartinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
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
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-citationCaspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases
Coll, R. C., Robertson, A. A. B., Chae, J. J., Higgins, S. C., Muñoz-Planillo, R., Inserra, M. C., Vetter, I., Dungan, L. S., Monks, B. G., Stutz, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3806 · Cited by 2,849
Self-citationThioredoxin-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
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658
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
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
Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291
Self-citationOxidized 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
The ketone metabolite β-hydroxybutyrate blocks NLRP3 inflammasome-mediated inflammatory disease
Youm, Y.-H., Nguyen, K. Y., Grant, R. W., Goldberg, E. L., Bodogai, M., Kim, D., D'Agostino, D., Planavsky, N., Lupfer, C., Kanneganti, T. D., et al. (2015) · Nature Medicine · doi:10.1038/nm.3804 · Cited by 2,172
Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093
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
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
Pyruvate Kinase M2 Is a PHD3-Stimulated Coactivator for Hypoxia-Inducible Factor 1
Luo, W., Hu, H., Chang, R., Zhong, J., Knabel, M., O'Meally, R., Cole, R. N., Pandey, A., & Semenza, G. L. (2011) · Cell · doi:10.1016/j.cell.2011.03.054 · Cited by 1,463
Palsson-McDermott, E. M., Curtis, A. M., Goel, G., Lauterbach, M. A. R., Sheedy, F. J., Gleeson, L. E., van den Bosch, M. W. M., Quinn, S. R., Domingo-Fernandez, R., Johnston, D. G. W., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.005 · Cited by 1,397
Self-citationAnti-inflammatory effect of IL-10 mediated by metabolic reprogramming of macrophages
Ip, W., Hoshi, N., Shouval, D. S., Snapper, S. B., & Medzhitov, R. M. (2017) · Science · doi:10.1126/science.aal3535 · Cited by 1,382
Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes
Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schröder, G. F., Fitzgerald, K. A., Wu, H., & Egelman, E. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.008 · Cited by 1,353
The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
Zhao, Y., Yang, J., Shi, J., Gong, Y., Lu, Q., Xu, H., Liu, L., & Shao, F. (2011) · Nature · doi:10.1038/nature10510 · Cited by 1,310
NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux
He, Y., Zeng, M. Y., Yang, D., Motro, B., & Núñez, G. (2016) · Nature · doi:10.1038/nature16959 · Cited by 1,295
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
Human Monocytes Engage an Alternative Inflammasome Pathway
Gaidt, M. M., Ebert, T. S., Chauhan, D., Schmidt, T., Schmid-Burgk, J. L., Rapino, F. A., Robertson, A. A. B., Cooper, M. A., Graf, T., & Hornung, V. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.012 · Cited by 808
Shi, H., Wang, Y., Li, X., Zhan, X., Tang, M., Fina, M., Su, L., Pratt, D., Bu, C. H., Hildebrand, S., et al. (2015) · Nature Immunology · doi:10.1038/ni.3333 · Cited by 771
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
Canonical Nlrp3 Inflammasome Links Systemic Low-Grade Inflammation to Functional Decline in Aging
Youm, Y.-H., Grant, R. W., McCabe, L. R., Albarado, D. C., Nguyen, K. Y., Ravussin, A., Pistell, P., Newman, S., Carter, R., Laque, A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.09.010 · Cited by 674
Majewski, N., Nogueira, V., Bhaskar, P. T., Coy, P. E., Skeen, J. E., Gottlob, K., Chandel, N. S., Thompson, C. B., Robey, R. B., & Hay, N. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.014 · Cited by 638
The inflammation highway: metabolism accelerates inflammatory traffic in obesity
Johnson, A. R., Justin Milner, J., & Makowski, L. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01151.x · Cited by 603
PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
Xie, M., Yu, Y., Kang, R., Zhu, S., Yang, L., Zeng, L., Sun, X., Yang, M., Billiar, T. R., Wang, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms13280 · Cited by 579
Heid, M. E., Keyel, P. A., Kamga, C., Shiva, S., Watkins, S. C., & Salter, R. D. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301490 · Cited by 570
Hexokinase Is an Innate Immune Receptor for the Detection of Bacterial Peptidoglycan
Wolf, A. J., Reyes, C. N., Liang, W., Becker, C. A., Shimada, K., Wheeler, M. L., Cho, H. C., Popescu, N. I., Coggeshall, K. M., Arditi, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.076 · Cited by 569
Regulation of bile acid synthesis: pathways, nuclear receptors, and mechanisms
Chiang, J. Y. L. (2003) · Journal of Hepatology · doi:10.1016/j.jhep.2003.11.006 · Cited by 559
K + Efflux-Independent NLRP3 Inflammasome Activation by Small Molecules Targeting Mitochondria
Groß, C. J., Mishra, R., Schneider, K. S., Médard, G., Wettmarshausen, J., Dittlein, D., Shi, H., Gorka, O., Koenig, P.-A., Fromm, S., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.08.010 · Cited by 550
Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
Broz, P., Newton, K., Lamkanfi, M., Mariathasan, S., Dixit, V. M., & Monack, D. M. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100257 · Cited by 549
Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
Hahn-Windgassen, A., Nogueira, V., Chen, C.-C., Skeen, J. E., Sonenberg, N., & Hay, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502876200 · Cited by 539
Inflammasome activation leads to Caspase-1–dependent mitochondrial damage and block of mitophagy
Yu, J.-J., Nagasu, H., Murakami, T., Hoang, H., Broderick, L., Hoffman, H., & Horng, T. (2014) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1414859111 · Cited by 449
Inflammaging and Anti-Inflammaging: The Role of Cytokines in Extreme Longevity
Minciullo, P. L., Catalano, A., Mandraffino, G., Casciaro, M., Crucitti, A., Maltese, G., Morabito, N., Lasco, A., Gangemi, S., & Basile, G. (2016) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-015-0377-3 · Cited by 433
Tang, T., Lang, X., Xu, C., Wang, X., Gong, T., Yang, Y., Cui, J., Bai, L., Wang, J., Jiang, W., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00227-x · Cited by 375
β-hydroxybutyrate deactivates neutrophil NLRP3 inflammasome to relieve gout flares
Goldberg, E. L., Asher, J. L., Molony, R. D., Shaw, A. C., Zeiss, C. J., Wang, C., Morozova-Roche, L. A., Herzog, R. I., Iwasaki, A., & Dixit, V. D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.004 · Cited by 370
Pasinelli, P., Houseweart, M. K., Brown, R. H., & Cleveland, D. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240305897 · Cited by 344
Role of IL-1β in type 2 diabetes
Dinarello, C. A., Donath, M. Y., & Mandrup-Poulsen, T. R. (2010) · Current Opinion in Endocrinology Diabetes and Obesity · doi:10.1097/med.0b013e32833bf6dc · Cited by 336
Kelly, B., Tannahill, G. M., Murphy, M. P., & O'Neill, L. A. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662114 · Cited by 334
Self-citationClarke, K., Tchabanenko, K., Pawlosky, R., Carter, E., Todd King, M., Musa-Veloso, K., Ho, M., Roberts, A., Robertson, J., VanItallie, T. B., et al. (2012) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2012.04.008 · Cited by 332
Shao, W., Yeretssian, G., Doiron, K., Hussain, S. N. A., & Saleh, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708182200 · Cited by 322
Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
Meissner, F., Molawi, K., & Zychlinsky, A. (2008) · Nature Immunology · doi:10.1038/ni.1633 · Cited by 308
Park, S., Juliana, C. A., Hong, S., Datta, P., Hwang, I., Fernandes‐Alnemri, T., Yu, J., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301170 · Cited by 275
The interplay between inflammation and metabolism in rheumatoid arthritis
Chimenti, M. S., Triggianese, P., Conigliaro, P., Candi, E., Melino, G., & Perricone, R. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.246 · Cited by 220
Yamanashi, T., Iwata, M., Kamiya, N., Tsunetomi, K., Kajitani, N., Wada, N., Iitsuka, T., Yamauchi, T., Miura, A., Pu, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08055-1 · Cited by 214
Disruption of glycolytic flux is a signal for inflammasome signaling and pyroptotic cell death
Sanman, L. E., Yu, Q., Eisele, N. A., Ng, T. M., van der Linden, W. A., Monack, D. M., Weerapana, E., & Bogyo, M. S. (2016) · eLife · doi:10.7554/elife.13663 · Cited by 198
Reversible Cysteine Oxidation in Hydrogen Peroxide Sensing and Signal Transduction
García‐Santamarina, S., Boronat, S., & Hidalgo, E. (2014) · Biochemistry · doi:10.1021/bi401700f · Cited by 179
Sokołowska, M., Chen, L., Liu, Y., Martínez‐Antón, A., Qi, H., Logun, C., Alsaaty, S., Park, Y. H., Kastner, D. L., Chae, J. J., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401343 · Cited by 177
Bile Acids Control Inflammation and Metabolic Disorder through Inhibition of NLRP3 Inflammasome
Guo, C., Xie, S., Chi, Z., Zhang, J., Liu, Y., Zhang, L., Zheng, M., Zhang, X., Xia, D., Ke, Y., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.10.009 · Cited by 175
Domingo-Fernandéz, R., Coll, R. C., Kearney, J., Breit, S. N., & O'Neill, L. A. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797126 · Cited by 167
Self-citationLee, J. (2013) · Archives of Pharmacal Research · doi:10.1007/s12272-013-0023-8 · Cited by 161
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
Qin, Y., Li, M., Feng, X., Wang, J., Cao, L., Shen, X.-K., Chen, J., Sun, M., Sheng, R., Han, F., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.034 · Cited by 138
Flagellin-induced NLRC4 phosphorylation primes the inflammasome for activation by NAIP5
Matusiak, M., Opdenbosch, N. V., Walle, L. V., Sirard, J., Kanneganti, T., & Lamkanfi, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417945112 · Cited by 134
Feng, H., Gu, J., Gou, F., Huang, W. G., Gao, C., Chen, G., Long, Y., Zhou, X., Yang, M., Liu, S., et al. (2016) · Journal of Diabetes Research · doi:10.1155/2016/6973175 · Cited by 128
Inhibition of caspase-3 activity and activation by protein glutathionylation
Huang, Z., Pinto, J. T., Deng, H., & Richie, J. P. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.02.026 · Cited by 125
Kong, G., Huang, Z., Ji, W., Wang, X., Liu, J., Wu, X., Huang, Z., Li, R., & Zhu, Q. (2017) · Journal of Neurotrauma · doi:10.1089/neu.2017.5192 · Cited by 113
Li, Y., Zheng, J., Liu, J., Yang, J., Liu, Y., Wang, C., Ma, X., Liu, B., Xin, G.-Z., & Liu, L. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00532 · Cited by 110
Innate Immune System Cells in Atherosclerosis
Chávez-Sanchéz, L., Espinosa-Luna, J. E., Chávez-Rueda, A. K., Legorreta-Haquet, M. V., Montoya-Díaz, E., & Blanco-Favela, F. A. (2013) · Archives of Medical Research · doi:10.1016/j.arcmed.2013.11.007 · Cited by 109
Oxidative metabolism enables Salmonella evasion of the NLRP3 inflammasome
Wynosky-Dolfi, M. A., Snyder, A. G., Philip, N. H., Doonan, P. J., Poffenberger, M. C., Avizonis, D. Z., Zwack, E. E., Riblett, A. M., Hu, B., Strowig, T., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20130627 · Cited by 105
The NLRP3 inflammasome contributes to sarcopenia and lower muscle glycolytic potential in old mice
McBride, M. J., Foley, K. P., D’Souza, D. M., Li, Y. E., Lau, T. C., Hawke, T. J., & Schertzer, J. D. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00060.2017 · Cited by 103
Nlrp3 is a key modulator of diet-induced nephropathy and renal cholesterol accumulation
Bakker, P. J., Butter, L. M., Kors, L., Teske, G. J. D., Aten, J., Sutterwala, F. S., Florquin, S., & Leemans, J. C. (2013) · Kidney International · doi:10.1038/ki.2013.503 · Cited by 98
The Induction of Pro–IL-1β by Lipopolysaccharide Requires Endogenous Prostaglandin E2 Production
Zasłona, Z., Pålsson‐McDermott, E. M., Menon, D., Haneklaus, M., Flis, E., Prendeville, H., Corcoran, S. E., Peters-Golden, M. L., & O'Neill, L. A. J. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1602072 · Cited by 94
Self-citationCunha, L. D., Silva, A. L. N., Ribeiro, J. M., Mascarenhas, D. P. A., Quirino, G. F. S., dos Santos, L. L., Flavell, R. A., & Zamboni, D. S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.086 · Cited by 87
Tseng, H. H. L., Vong, C. T., Kwan, Y. W., Lee, S. M., & Hoi, M. P. M. (2016) · Scientific Reports · doi:10.1038/srep35016 · Cited by 85
Nomura, J., So, A. K.-L., Tamura, M., & Busso, N. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402512 · Cited by 79
Lima-Junior, D. S., Mineo, T. W. P., Calich, V. L. G., & Zamboni, D. S. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700258 · Cited by 71
Sulfonylureas as Concomitant Insulin Secretagogues and NLRP3 Inflammasome Inhibitors
Hill, J. R., Coll, R. C., Sue, N., Reid, J. C., Dou, J., Holley, C. L., Pelingon, R., Dickinson, J. B., Biden, T. J., Schroder, K., et al. (2017) · ChemMedChem · doi:10.1002/cmdc.201700270 · Cited by 66
Haneklaus, M., O’Neil, J. D., Clark, A. R., Masters, S. L., & O'Neill, L. A. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.772947 · Cited by 66
Self-citationGuglielmo, A., Sabra, A., Elbery, M., Cerveira, M. M., Ghenov, F., Sunasee, R., & Ckless, K. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.06.028 · Cited by 43
A novel immunomodulatory effect of ugonin U in human neutrophils via stimulation of phospholipase C
Chen, C., Liaw, C., Chen, Y., Chang, W.-Y., Chung, P.-J., & Hwang, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.018 · Cited by 34
Chen, C., Yang, C.-H., Tsai, Y., Liaw, C., Chang, W.-Y., & Hwang, T. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.018 · Cited by 33
Hughes, M. M., Lavrencic, P., Coll, R. C., Ve, T., Ryan, D. G., Williams, N. C., Menon, D., Mansell, A. S., Philip G. Board, Mobli, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701868114 · Cited by 33
Self-citationWang, C., Xu, C., Alippe, Y., Qu, C., Xiao, J., Schipani, E., Civitelli, R., Abu‐Amer, Y., & Mbalaviele, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-05033-5 · Cited by 32
Glutathione and Glutathione Transferase Omega 1 as Key Posttranslational Regulators in Macrophages
Hughes, M. M., McGettrick, A. F., & O'Neill, L. A. J. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0044-2016 · Cited by 29
Self-citationCysteine Oxidation Enhanced by Iron in Tristetraprolin, A Zinc Finger Peptide
Lee, S. J., & Michel, S. L. J. (2010) · Inorganic Chemistry · doi:10.1021/ic9024298 · Cited by 28
Kemper, M. F., Srivastava, S., King, M. T., Clarke, K., Veech, R. L., & Pawlosky, R. J. (2015) · Lipids · doi:10.1007/s11745-015-4085-x · Cited by 26
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The NLRP3 inflammasome: molecular activation and regulation to therapeutics
Swanson, K. V., Deng, M., & Ting, J. P.-Y. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0165-0 · Cited by 4,884
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Metadata
- Authors
- Hughes, M. M., & O'Neill, L. A. J.
- Affiliations
- Trinity College Dublin (IE)
- Corresponding author
- Hughes, Mark M.
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 2017-12-16
- Volume
- 281
- Issue
- 1
- Pages
- 88-98
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- OpenAlex
- W2778840601
- Cited by
- 311
- References
- 86
- Citations by year
- 2026: 12 · 2025: 24 · 2024: 50 · 2023: 48 · 2022: 49 · 2021: 49 · 2020: 47 · 2019: 18 · 2018: 13 · 2017: 1
- FWCI
- 2.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Immunological Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Science Foundation Ireland
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- NLRP3 inflammasome, macrophage metabolic reprogramming, caspase-1 activation, IL-1β, IL-18, pyroptosis, palmitate, uric acid, cholesterol crystals, ketone bodies, mitochondrial reactive oxygen species, hexokinase, glycolysis, inflammation, inflammasome inhibition
- MeSH terms
- Pyroptosis, NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Cholesterol, Hexokinase, Humans, Ketone Bodies, Macrophages, Uric Acid, Reactive Oxygen Species, Palmitic Acid, Caspase 1, Inflammasomes, Cellular Reprogramming
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.
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