The NLRP3 inflammasome: molecular activation and regulation to therapeutics

Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death

Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659 · see citing works

The Inflammasome

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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 · see citing works

Gout-associated uric acid crystals activate the NALP3 inflammasome

Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326 · see citing works

Succinate is an inflammatory signal that induces IL-1β through HIF-1α

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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 · see citing works

Circulating mitochondrial DAMPs cause inflammatory responses to injury

Zhang, Q., Raoof, M., Chen, Y., Sumi, Y., Sursal, T., Junger, W., Brohi, K., Itagaki, K., & Hauser, C. J. (2010) · Nature · doi:10.1038/nature08780 · Cited by 3,812 · see citing works

Caspase-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 · see citing works

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 · see citing works

Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores

Liu, X., Zhang, Z., Ruan, J., Pan, Y., Magupalli, V. G., Wu, H., & Lieberman, J. (2016) · Nature · doi:10.1038/nature18629 · Cited by 3,202 · see citing works

Cryopyrin activates the inflammasome in response to toxins and ATP

Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080 · see citing works

Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization

Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065 · see citing works

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 · see citing works

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 3,006 · see citing works

A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases

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Pore-forming activity and structural autoinhibition of the gasdermin family

Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771 · see citing works

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 · see citing works

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 · see citing works

Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion

He, W.-T., Wan, H., Hu, L., Chen, P., Wang, X., Huang, Z., Yang, Z.-H., Zhong, C.-Q., & Han, J. (2015) · Cell Research · doi:10.1038/cr.2015.139 · Cited by 2,517 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

K+ Efflux Is the Common Trigger of NLRP3 Inflammasome Activation by Bacterial Toxins and Particulate Matter

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 · see citing works

Targeting the NLRP3 inflammasome in inflammatory diseases

Mangan, M. S. J., Olhava, E. J., Roush, W. R., Seidel, H. M., Glick, G. D., & Latz, E. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.97 · Cited by 1,885 · see citing works

Treating inflammation by blocking interleukin-1 in a broad spectrum of diseases

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Fatty acid–induced NLRP3-ASC inflammasome activation interferes with insulin signaling

Wen, H., Gris, D., Lei, Y. L., Jha, S., Zhang, L., Huang, M. T.-H., Brickey, W. J., & Ting, J. P. ‐. (2011) · Nature Immunology · doi:10.1038/ni.2022 · Cited by 1,811 · see citing works

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 · see citing works

The Cytolytic P _2Z Receptor for Extracellular ATP Identified as a P _2X Receptor (P2X ₇ )

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Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle–Wells syndrome

Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2001) · Nature Genetics · doi:10.1038/ng756 · Cited by 1,679 · see citing works

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 · see citing works

Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration

Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445 · see citing works

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 · see citing works

The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses

Rathinam, V. A. K., Jiang, Z., Waggoner, S. N., Sharma, S., Cole, L. E., Waggoner, L., Vanaja, S. K., Monks, B. G., Ganesan, S., Latz, E., et al. (2010) · Nature Immunology · doi:10.1038/ni.1864 · Cited by 1,331 · see citing works

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 · see citing works

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 · see citing works

Toll-like receptor–induced changes in glycolytic metabolism regulate dendritic cell activation

Krawczyk, C. M., Holowka, T., Sun, J., Blagih, J., Amiel, E., DeBerardinis, R. J., Cross, J. R., Jung, E., Thompson, C. B., Jones, R. G., et al. (2010) · Blood · doi:10.1182/blood-2009-10-249540 · Cited by 1,246 · see citing works

New mitochondrial DNA synthesis enables NLRP3 inflammasome activation

Zhong, Z., Liang, S., Sanchez-Lopez, E., He, F., Shalapour, S., Lin, X.-J., Wong, J., Ding, S., Seki, E., Schnabl, B., et al. (2018) · Nature · doi:10.1038/s41586-018-0372-z · Cited by 1,208 · see citing works

The Pore-Forming Protein Gasdermin D Regulates Interleukin-1 Secretion from Living Macrophages

Evavold, C. L., Ruan, J., Tan, Y., Xia, S., Wu, H., & Kagan, J. C. (2018) · Immunity · doi:10.1016/j.immuni.2017.11.013 · Cited by 1,115 · see citing works

NLRP3 inflammasome blockade reduces liver inflammation and fibrosis in experimental NASH in mice

Mridha, A. R., Wree, A., Robertson, A. A. B., Yeh, M. M., Johnson, C. D., Van Rooyen, D. M., Haczeyni, F., Teoh, N. C.-H., Savard, C., Ioannou, G. N., et al. (2017) · Journal of Hepatology · doi:10.1016/j.jhep.2017.01.022 · Cited by 1,110 · see citing works

The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP

Lee, G., Subramanian, N., Kim, A. I., Aksentijevich, I. A., Goldbach‐Mansky, R. T., Sacks, D. B., Germain, R. N., Kastner, D. L., & Chae, J. J. (2012) · Nature · doi:10.1038/nature11588 · Cited by 1,077 · see citing works

Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome

Yan, Y., Jiang, W., Liu, L., Wang, X., Ding, C., Tian, Z., & Zhou, R. (2015) · Cell · doi:10.1016/j.cell.2014.11.047 · Cited by 1,014 · see citing works

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 939 · see citing works

Critical role for calcium mobilization in activation of the NLRP3 inflammasome

Murakami, T., Öckinger, J., Yu, J., Byles, V., McColl, A., Hofer, A. M., & Horng, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117765109 · Cited by 926 · see citing works

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.2016.09.008 · Cited by 838 · see citing works

Oridonin is a covalent NLRP3 inhibitor with strong anti-inflammasome activity

He, H., Jiang, H., Chen, Y., Ye, J., Wang, A., Wang, C., Liu, Q., Liang, G., Deng, X., Jiang, W., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04947-6 · Cited by 827 · see citing works

Differential requirement for the activation of the inflammasome for processing and release of IL-1β in monocytes and macrophages

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ATP Activates a Reactive Oxygen Species-dependent Oxidative Stress Response and Secretion of Proinflammatory Cytokines in Macrophages

Cruz, C. M., Rinna, A., Forman, H. J., Ventura, A. L. M., Persechini, P. M., & Ojcius, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608083200 · Cited by 786 · see citing works

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 780 · see citing works

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 771 · see citing works

Identification of a selective and direct NLRP3 inhibitor to treat inflammatory disorders

Jiang, H., He, H., Chen, Y., Huang, W., Cheng, J., Ye, J., Wang, A., Tao, J., Wang, C., Liu, Q., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20171419 · Cited by 771 · see citing works

Interleukin-1 beta maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity.

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NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component

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 751 · see citing works

Activation of Nrf2-antioxidant signaling attenuates NFκB-inflammatory response and elicits apoptosis

Li, W., Khor, T. O., Xu, C., Shen, G., Jeong, W.-S., Yu, S., & Kong, A.-N. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.07.017 · Cited by 738 · see citing works

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 · see citing works

De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal‐onset multisystem inflammatory disease (NOMID): A new member of the expanding family of pyrin‐associated autoinflammatory diseases

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PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation

Chen, J., & Chen, Z. J. (2018) · Nature · doi:10.1038/s41586-018-0761-3 · Cited by 692 · see citing works

The Adaptor MAVS Promotes NLRP3 Mitochondrial Localization and Inflammasome Activation

Subramanian, N., Natarajan, K., Clatworthy, M. R., Wang, Z., & Germain, R. N. (2013) · Cell · doi:10.1016/j.cell.2013.02.054 · Cited by 675 · see citing works

Mitochondrial calcium and the permeability transition in cell death

Lemasters, J. J., Theruvath, T. P., Zhong, Z., & Nieminen, A. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.06.009 · Cited by 656 · see citing works

Noncanonical inflammasome signaling elicits gasdermin D–dependent neutrophil extracellular traps

Chen, K. W., Monteleone, M. M., Boucher, D., Sollberger, G., Ramnath, D., Condon, N. D., von Pein, J. B., Brož, P., Sweet, M. J., & Schroder, K. (2018) · Science Immunology · doi:10.1126/sciimmunol.aar6676 · Cited by 640 · see citing works

The DNA Inflammasome in Human Myeloid Cells Is Initiated by a STING-Cell Death Program Upstream of NLRP3

Gaidt, M. M., Ebert, T. S., Chauhan, D., Ramshorn, K., Pinci, F., Zuber, S., O’Duill, F., Schmid-Burgk, J. L., Hoss, F., Buhmann, R., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.039 · Cited by 638 · see citing works

Post-Translational Modification Control of Innate Immunity

Liu, J., Qian, C., & Cao, X. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.020 · Cited by 632 · see citing works

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 · see citing works

Anti-inflammatory Compounds Parthenolide and Bay 11-7082 Are Direct Inhibitors of the Inflammasome

Juliana, C. A., Fernandes‐Alnemri, T., Wu, J., Datta, P., Solórzano, L., Yu, J., Meng, R., Quong, A. A., Latz, E., Scott, C. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082305 · Cited by 617 · see citing works

OLT1177, a β-sulfonyl nitrile compound, safe in humans, inhibits the NLRP3 inflammasome and reverses the metabolic cost of inflammation

Marchetti, C., Swartzwelter, B. J., Gamboni, F., Neff, C. P., Richter, K., Azam, T., Carta, S., Tengesdal, I. W., Nemkov, T. G., D’Alessandro, A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716095115 · Cited by 596 · see citing works

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 · see citing works

Identification of Bacterial Muramyl Dipeptide as Activator of the NALP3/Cryopyrin Inflammasome

Martinon, F., Agostini, L., Meylan, E., & Tschopp, J. (2004) · Current Biology · doi:10.1016/j.cub.2004.10.027 · Cited by 579 · see citing works

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 · see citing works

Inhibiting the NLRP3 inflammasome with MCC950 promotes non-phlogistic clearance of amyloid-β and cognitive function in APP/PS1 mice

Dempsey, C., Rubio Araiz, A., Bryson, K. J., Finucane, O., Larkin, C., Mills, E. L., Robertson, A. A. B., Cooper, M. A., O'Neill, L. A. J., & Lynch, M. A. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.12.014 · Cited by 571 · see citing works

Prion-like Polymerization Underlies Signal Transduction in Antiviral Immune Defense and Inflammasome Activation

Cai, X., Chen, J., Xu, H., Liu, S., Jiang, Q., Halfmann, R., & Chen, Z. J. (2014) · Cell · doi:10.1016/j.cell.2014.01.063 · Cited by 567 · see citing works

Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity

Boucher, D., Monteleone, M. M., Coll, R. C., Chen, K. W., Ross, C. M., Teo, J. L., Gomez, G. A., Holley, C. L., Bierschenk, D., Stacey, K. J., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20172222 · Cited by 557 · see citing works

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 554 · see citing works

Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against <i>Salmonella</i>

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 · see citing works

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 · see citing works

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 530 · see citing works

Tranilast directly targets NLRP3 to treat inflammasome‐driven diseases

Huang, Y., Jiang, H., Chen, Y., Wang, X., Yang, Y., Tao, J., Deng, X., Liang, G., Zhang, H., Jiang, W., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708689 · Cited by 521 · see citing works

Neutrophil Extracellular Trap–Associated Protein Activation of the NLRP3 Inflammasome Is Enhanced in Lupus Macrophages

Kahlenberg, J. M., Carmona‐Rivera, C., Smith, C. K., & Kaplan, M. J. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202388 · Cited by 511 · see citing works

Caspase-1 Activation of Lipid Metabolic Pathways in Response to Bacterial Pore-Forming Toxins Promotes Cell Survival

Gurcel, L., Abrami, L., Girardin, S. E., Tschopp, J., & van der Goot, F. G. (2006) · Cell · doi:10.1016/j.cell.2006.07.033 · Cited by 508 · see citing works

Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling

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NLRP3 Phosphorylation Is an Essential Priming Event for Inflammasome Activation

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Cholesterol Homeostatic Regulator SCAP-SREBP2 Integrates NLRP3 Inflammasome Activation and Cholesterol Biosynthetic Signaling in Macrophages

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Interleukin-1β Maturation Triggers Its Relocation to the Plasma Membrane for Gasdermin-D-Dependent and -Independent Secretion

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NLRP3/Cryopyrin Is Necessary for Interleukin-1β (IL-1β) Release in Response to Hyaluronan, an Endogenous Trigger of Inflammation in Response to Injury

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IRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation

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cGAS drives noncanonical-inflammasome activation in age-related macular degeneration

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Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection

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Protein kinase D at the Golgi controls NLRP3 inflammasome activation

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(1,3)-β-Glucans Activate Both Dectin-1 and NLRP3 Inflammasome in Human Macrophages

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3,4-Methylenedioxy-β-nitrostyrene Inhibits NLRP3 Inflammasome Activation by Blocking Assembly of the Inflammasome

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Concerted Activation of the AIM2 and NLRP3 Inflammasomes Orchestrates Host Protection against Aspergillus Infection

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Multiple cathepsins promote pro-IL-1β synthesis and NLRP3-mediated IL-1β activation

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The Mitochondrial Antiviral Protein MAVS Associates with NLRP3 and Regulates Its Inflammasome Activity

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NLRP3 inflammasome inhibition is disrupted in a group of auto-inflammatory disease CAPS mutations

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Nuclear Factor E2-Related Factor-2 Negatively Regulates NLRP3 Inflammasome Activity by Inhibiting Reactive Oxygen Species-Induced NLRP3 Priming

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The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation

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Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non‐apoptotic caspase‐8 is required for inflammasome priming

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Activation of the AMPK-FOXO3 Pathway Reduces Fatty Acid–Induced Increase in Intracellular Reactive Oxygen Species by Upregulating Thioredoxin

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SUMO-mediated regulation of NLRP3 modulates inflammasome activity

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The Inhibitory Innate Immune Sensor NLRP12 Maintains a Threshold against Obesity by Regulating Gut Microbiota Homeostasis

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Caspase-8 as an Effector and Regulator of NLRP3 Inflammasome Signaling

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NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22

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The NLRP3 inflammasome is activated by nanoparticles through ATP, ADP and adenosine

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K+ regulates Ca2+ to drive inflammasome signaling: dynamic visualization of ion flux in live cells

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Glutathione S-Transferase Omega 1-1 Is a Target of Cytokine Release Inhibitory Drugs and May Be Responsible for Their Effect on Interleukin-1औ Posttranslational Processing

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TLR Agonists Stimulate Nlrp3-Dependent IL-1β Production Independently of the Purinergic P2X7 Receptor in Dendritic Cells and In Vivo

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Lipopolysaccharide Primes the NALP3 Inflammasome by Inhibiting Its Ubiquitination and Degradation Mediated by the SCFFBXL2 E3 Ligase

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Dual Engagement of the NLRP3 and AIM2 Inflammasomes by Plasmodium-Derived Hemozoin and DNA during Malaria

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Cutting Edge: Mitochondrial Assembly of the NLRP3 Inflammasome Complex Is Initiated at Priming

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The oxidized phospholipid oxPAPC protects from septic shock by targeting the non-canonical inflammasome in macrophages

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Disruption of glycolytic flux is a signal for inflammasome signaling and pyroptotic cell death

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Chloride regulates dynamic NLRP3-dependent ASC oligomerization and inflammasome priming

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Nuclear Factor E2-related Factor-2 (Nrf2) Is Required for NLRP3 and AIM2 Inflammasome Activation

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Cytosolic Double-Stranded RNA Activates the NLRP3 Inflammasome via MAVS-Induced Membrane Permeabilization and K+ Efflux

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Disruption of Nrf2, a Key Inducer of Antioxidant Defenses, Attenuates ApoE-Mediated Atherosclerosis in Mice

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Cutting Edge: TRAF6 Mediates TLR/IL-1R Signaling–Induced Nontranscriptional Priming of the NLRP3 Inflammasome

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MCC950, the Selective Inhibitor of Nucleotide Oligomerization Domain-Like Receptor Protein-3 Inflammasome, Protects Mice against Traumatic Brain Injury

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A single domain antibody fragment that recognizes the adaptor ASC defines the role of ASC domains in inflammasome assembly

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