The DOI matches its Crossref record; 186 of the 186 references it cites were found in a registry or an index.
Initiation and perpetuation of NLRP 3 inflammasome activation and assembly
Open accessAbstract
Summary: The NLRP 3 ( NOD ‐like receptor family, pyrin domain containing 3) inflammasome is a multiprotein complex that orchestrates innate immune responses to infection and cell stress through activation of caspase‐1 and maturation of inflammatory cytokines pro‐interleukin‐1β (pro‐ IL ‐1β) and pro‐ IL ‐18. Activation of the inflammasome during infection can be protective, but unregulated NLRP 3 inflammasome activation in response to non‐pathogenic endogenous or exogenous stimuli can lead to unintended pathology. NLRP 3 associates with mitochondria and mitochondrial molecules, and activation of the NLRP 3 inflammasome in response to diverse stimuli requires cation flux, mitochondrial Ca 2+ uptake, and mitochondrial reactive oxygen species accumulation. It remains uncertain whether NLRP 3 surveys mitochondrial integrity and senses mitochondrial damage, or whether mitochondria simply serve as a physical platform for inflammasome assembly. The structure of the active, caspase‐1‐processing NLRP 3 inflammasome also requires further clarification, but recent studies describing the prion‐like properties of ASC have advanced the understanding of how inflammasome assembly and caspase‐1 activation occur while raising new questions regarding the propagation and resolution of NLRP 3 inflammasome activation. Here, we review the mechanisms and pathways regulating NLRP 3 inflammasome activation, discuss emerging concepts in NLRP 3 complex organization, and expose the knowledge gaps hindering a comprehensive understanding of NLRP 3 activation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The NLRP3 inflammasome is also unusual in that it responds to a very broad range of signals as the second event that produces inflammasome formation/activation (eg, ATP, K+ efflux, β-amyloid, silica, uric acid crystals, ROS; (Elliott and Sutterwala, 2015).”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Elliott and Sutterwala, 2015
In the citing paper
“The NLRP3 inflammasome responds to a broad range of signals, for example, ATP, K+ efflux, β-amyloid, silica, uric acid crystals, and reactive oxygen species (ROS)(Elliott and Sutterwala, 2015).”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Elliott and Sutterwala, 2015
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Martinon, 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
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
Autophagy and Viruses: Adversaries or Allies?
Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,444
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
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
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
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
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–830 of 830
Zeng, M., Xing, W., Liang, G., Yuan, F., Wang, W., Liu, J., & He, Z. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116305
Yang, G., Hou, Z., Zhao, J., Zhang, A., Shen, Y., Lin, Y., Chen, K., Yu, Y., & Zhang, Y. (2026) · Research Square · doi:10.21203/rs.3.rs-8774215/v1
Wu, Z., Chen, Y., Fu, X., Li, Y., Lu, Y., & Sun, W. (2026) · Natural Product Communications · doi:10.1177/1934578x261425493
Wang, T., Liu, X., Li, J., Ding, Y., Yue, Y., Li, J., Wang, M., Wei, N., & Hao, L. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1762290
Implication de l'inflammasome NLRP3 dans la sécrétion non conventionnelle de la protéine FADD
Mouasni, S. (2018) · theses.fr (ABES) · doi:10.70675/8623f190zbb94z44b7z8b70zd93fa9be484d
Assrawi, E. (2019) · theses.fr (ABES) · doi:10.70675/82f530d5z0154z474cz9746z470b6a42c9e0
Louvrier, C. (2019) · theses.fr (ABES) · doi:10.70675/ee57af23z15cdz4ec8zafebz9f9ac9f08220
Specific inhibition of NLRP3 inflammasome by a Smurf1 inhibitor in vitro and in vivo
Meng, L., Xuan, H., Zhou, P., Xu, W., Bian, W., Lin, Y., & Guan, Y. (2026) · Open Medicine · doi:10.1515/med-2026-1397
Shah, R. B., Li, Y., Person, A., Frigon, L., Đukić, N., Kini, E., Chen, R., Pascal, J. M., Cohen, M. S., Ahel, I., et al. (2026) · Science Advances · doi:10.1126/sciadv.adz9284
Banerjee, S., & Mukhopadhyay, M. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-40471-9.00001-x
From mitochondrial zonation to immune dysregulation: a mechanistic axis in diabetic cardiomyopathy
Chen, J., Fu, L., Zhang, J., Ding, R., Zhang, H., Xu, G., Hu, J., & Yang, P. (2026) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2026.1775592
Tom, V. V., Mallick, S., SASIDHARAN, A., Biswas, T., Bose, B., Somayaji, Y., & Fernandes, R. (2026) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-026-05580-4
Li, F., Wang, Y., Liu, X., Wu, Y., Miao, N., Wang, J., Chen, X., Wu, T., Fu, Q., Zeng, C., et al. (2026) · Molecular Medicine · doi:10.1186/s10020-026-01544-y
Chen, S., Yang, L., Wang, P., Wen, C., Shi, Z., Tan, R., Guan, W., Jiang, G., Zhang, P., Liang, C., et al. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04744-0
Xie, R., Yuan, L., Cai, J., Liu, B., Wu, J., Ren, Z., Qin, Y., Yu, N., Li, J. H., & Zhou, G. (2026) · Neuroscience Letters · doi:10.1016/j.neulet.2026.138680
Molecular switches in cell death: the interplay of apoptosis and pyroptosis in cancer
Liu, Y., & Xie, Y. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-03059-9
Zhang, Y. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06083-5 · Cited by 1
季, 晓. (2026) · Asian Case Reports in Emergency Medicine · doi:10.12677/acrem.2026.143048
Ma, M., Zhang, M., Sun, H., Xie, X., Guo, X., Li, H., & Jin, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1924802
Steckert, A. V., Feltrin, K. D., Rodrigues, L. F. S., de Liz, F. M., Muller, M. M. F., Bortoluzzi, D. P., Mayer, A. B., Ceretta, L. B., Barichello, T., Dal‐Pizzol, F., et al. (2026) · Brain and Behavior · doi:10.1002/brb3.71707
Colestasis intrahepática del embarazo: de la fisiopatología al tratamiento
Rodríguez, M. A. O., & Luján-Ramos, M. A. (2026) · Hepatología · doi:10.59093/27112330.178
Wang, H., Sun, Y., Liu, S., Chen, C., Long, J., Yan, Q., Lin, Y., Li, S., Huang, Y., Liu, F., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158816
Unraveling the mitochondrial–lysosomal crosstalk: a new frontier in sepsis-induced acute lung injury
Deng, Y., Tu, G., Ma, J., Zhang, Z., Shen, Y., Liu, Y., Wu, J., Deng, Z., 钟守维, Zou, K., et al. (2026) · Critical Care Sepsis and Severe Infection · doi:10.1186/s44541-026-00011-9
Dzhemileva, L. U., D'yakonov, V. A., Marshala, S. N., Хуснутдинова, Э. К., Deviatkin, A. A., & Shipulin, G. A. (2026) · Medical Sciences · doi:10.3390/medsci14060612
Ahn, S., Park, S., & Simu, S. Y. (2026) · Medicina · doi:10.3390/medicina62101969
Kurata, M., Takahashi, K., Kaneko, N., Kameda, K., Nakamura, T., Hosokawa, S., Murakami, K., Ogura, H., Ishido, S., Yamaguchi, O., et al. (2026) · The Journal of Immunology · doi:10.1093/jimmun/vkag257
BindingDB Entry 50017788: Synthesis and Pharmacological Evaluation of New
BindingDB (2023) · UC San Diego · doi:10.7270/q2mp57d8
Metadata
- Authors
- Elliott, E. I., & Sutterwala, F. S.
- Affiliations
- University of Iowa (US)
- Corresponding author
- Sutterwala, Fayyaz S.
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 2015-04-16
- Volume
- 265
- Issue
- 1
- Pages
- 35-52
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- PMC
- PMC4400874
- OpenAlex
- W2068633454
- Cited by
- 821
- References
- 186
- Citations by year
- 2026: 39 · 2025: 56 · 2024: 87 · 2023: 93 · 2022: 127 · 2021: 98 · 2020: 87 · 2019: 79 · 2018: 63 · 2017: 43 · 2016: 37 · 2015: 11
- FWCI
- 4.98
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Immunological Reviews (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH (R01 AI087630, T32 GM007337)
- 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
- NLRP3 inflammasome, inflammasome assembly, caspase-1 activation, mitochondrial calcium uptake, mitochondrial reactive oxygen species, innate immunity
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Humans, Immunity, Innate, Mitochondria, Calcium Signaling, Caspase 1, Multiprotein Complexes, 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
