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NameNACHT, LRR and PYD domains-containing protein 3
Synonyms
  • Angiotensin/vasopressin receptor AII/AVP-like
  • C1orf7
  • Caterpiller protein 1.1
  • CIAS1
  • CLR1.1
  • Cold-induced autoinflammatory syndrome 1 protein
  • Cryopyrin
  • NALP3
  • PYPAF1
  • PYRIN-containing APAF1-like protein 1
Gene NameNLRP3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0008987|NACHT, LRR and PYD domains-containing protein 3
MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMID
FNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGL
LEYLSRISICKMKKDYRKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQ
QEREQELLAIGKTKTCESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKMM
LDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIHKIVRKPSRILFL
MDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQH
LLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCT
GLKQQMESGKSLAQTSKTTTAVYVFFLSSLLQPRGGSQEHGLCAHLWGLCSLAADGIWNQ
KILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEK
EGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKI
SQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTR
MDHMVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPSSSHAACSHGL
VNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRC
GLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLT
SACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVNSGLTSVC
CSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWD
LSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALET
LQEEKPELTVVFEPSW
Number of residues1036
Molecular Weight118171.375
Theoretical pINot Available
GO Classification
Functions
  • ATP binding
  • transcription factor binding
  • sequence-specific DNA binding
  • peptidoglycan binding
Processes
  • interleukin-18 production
  • activation of cysteine-type endopeptidase activity involved in apoptotic process
  • negative regulation of interleukin-1 beta secretion
  • negative regulation of acute inflammatory response
  • negative regulation of NF-kappaB import into nucleus
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • negative regulation of NF-kappaB transcription factor activity
  • protein oligomerization
  • defense response
  • NLRP3 inflammasome complex assembly
  • positive regulation of type 2 immune response
  • inflammatory response
  • positive regulation of NF-kappaB transcription factor activity
  • defense response to virus
  • positive regulation of interleukin-1 beta secretion
  • interleukin-1 beta production
  • innate immune response
  • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway
  • apoptotic process
  • positive regulation of transcription from RNA polymerase II promoter
  • positive regulation of T-helper 2 cell cytokine production
  • negative regulation of inflammatory response
  • positive regulation of T-helper 2 cell differentiation
  • cellular response to lipopolysaccharide
  • transcription, DNA-templated
  • detection of biotic stimulus
  • positive regulation of interleukin-4 production
  • signal transduction
  • interleukin-1 secretion
Components
  • extracellular region
  • nucleus
  • endoplasmic reticulum
  • cytosol
  • NLRP3 inflammasome complex
  • cytoplasm
General FunctionTranscription factor binding
Specific FunctionAs the sensor component of the NLRP3 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP3, PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitement of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP3 inflammasome is also required for HMGB1 secretion (PubMed:22801494). The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. Under resting conditions, NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, reactive oxygen species, K(+) efflux, crystals of monosodium urate or cholesterol, beta-amyloid fibers, environmental or industrial particles and nanoparticles, etc. However, it is unclear what constitutes the direct NLRP3 activator. Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth (By similarity). During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF (By similarity).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDQ96P20
UniProtKB Entry NameNLRP3_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0013549|NACHT, LRR and PYD domains-containing protein 3 (NLRP3)
ATGAAGATGGCAAGCACCCGCTGCAAGCTGGCCAGGTACCTGGAGGACCTGGAGGATGTG
GACTTGAAGAAATTTAAGATGCACTTAGAGGACTATCCTCCCCAGAAGGGCTGCATCCCC
CTCCCGAGGGGTCAGACAGAGAAGGCAGACCATGTGGATCTAGCCACGCTAATGATCGAC
TTCAATGGGGAGGAGAAGGCGTGGGCCATGGCCGTGTGGATCTTCGCTGCGATCAACAGG
AGAGACCTTTATGAGAAAGCAAAAAGAGATGAGCCGAAGTGGGGTTCAGATAATGCACGT
GTTTCGAATCCCACTGTGATATGCCAGGAAGACAGCATTGAAGAGGAGTGGATGGGTTTA
CTGGAGTACCTTTCGAGAATCTCTATTTGTAAAATGAAGAAAGATTACCGTAAGAAGTAC
AGAAAGTACGTGAGAAGCAGATTCCAGTGCATTGAAGACAGGAATGCCCGTCTGGGTGAG
AGTGTGAGCCTCAACAAACGCTACACACGACTGCGTCTCATCAAGGAGCACCGGAGCCAG
CAGGAGAGGGAGCAGGAGCTTCTGGCCATCGGCAAGACCAAGACGTGTGAGAGCCCCGTG
AGTCCCATTAAGATGGAGTTGCTGTTTGACCCCGATGATGAGCATTCTGAGCCTGTGCAC
ACCGTGGTGTTCCAGGGGGCGGCAGGGATTGGGAAAACAATCCTGGCCAGGAAGATGATG
TTGGACTGGGCGTCGGGGACACTCTACCAAGACAGGTTTGACTATCTGTTCTATATCCAC
TGTCGGGAGGTGAGCCTTGTGACACAGAGGAGCCTGGGGGACCTGATCATGAGCTGCTGC
CCCGACCCAAACCCACCCATCCACAAGATCGTGAGAAAACCCTCCAGAATCCTCTTCCTC
ATGGACGGCTTCGATGAGCTGCAAGGTGCCTTTGACGAGCACATAGGACCGCTCTGCACT
GACTGGCAGAAGGCCGAGCGGGGAGACATTCTCCTGAGCAGCCTCATCAGAAAGAAGCTG
CTTCCCGAGGCCTCTCTGCTCATCACCACGAGACCTGTGGCCCTGGAGAAACTGCAGCAC
TTGCTGGACCATCCTCGGCATGTGGAGATCCTGGGTTTCTCCGAGGCCAAAAGGAAAGAG
TACTTCTTCAAGTACTTCTCTGATGAGGCCCAAGCCAGGGCAGCCTTCAGTCTGATTCAG
GAGAACGAGGTCCTCTTCACCATGTGCTTCATCCCCCTGGTCTGCTGGATCGTGTGCACT
GGACTGAAACAGCAGATGGAGAGTGGCAAGAGCCTTGCCCAGACATCCAAGACCACCACC
GCGGTGTACGTCTTCTTCCTTTCCAGTTTGCTGCAGCCCCGGGGAGGGAGCCAGGAGCAC
GGCCTCTGCGCCCACCTCTGGGGGCTCTGCTCTTTGGCTGCAGATGGAATCTGGAACCAG
AAAATCCTGTTTGAGGAGTCCGACCTCAGGAATCATGGACTGCAGAAGGCGGATGTGTCT
GCTTTCCTGAGGATGAACCTGTTCCAAAAGGAAGTGGACTGCGAGAAGTTCTACAGCTTC
ATCCACATGACTTTCCAGGAGTTCTTTGCCGCCATGTACTACCTGCTGGAAGAGGAAAAG
GAAGGAAGGACGAACGTTCCAGGGAGTCGTTTGAAGCTTCCCAGCCGAGACGTGACAGTC
CTTCTGGAAAACTATGGCAAATTCGAAAAGGGGTATTTGATTTTTGTTGTACGTTTCCTC
TTTGGCCTGGTAAACCAGGAGAGGACCTCCTACTTGGAGAAGAAATTAAGTTGCAAGATC
TCTCAGCAAATCAGGCTGGAGCTGCTGAAATGGATTGAAGTGAAAGCCAAAGCTAAAAAG
CTGCAGATCCAGCCCAGCCAGCTGGAATTGTTCTACTGTTTGTACGAGATGCAGGAGGAG
GACTTCGTGCAAAGGGCCATGGACTATTTCCCCAAGATTGAGATCAATCTCTCCACCAGA
ATGGACCACATGGTTTCTTCCTTTTGCATTGAGAACTGTCATCGGGTGGAGTCACTGTCC
CTGGGGTTTCTCCATAACATGCCCAAGGAGGAAGAGGAGGAGGAAAAGGAAGGCCGACAC
CTTGATATGGTGCAGTGTGTCCTCCCAAGCTCCTCTCATGCTGCCTGTTCTCATGGATTG
GTGAACAGCCACCTCACTTCCAGTTTTTGCCGGGGCCTCTTTTCAGTTCTGAGCACCAGC
CAGAGTCTAACTGAATTGGACCTCAGTGACAATTCTCTGGGGGACCCAGGGATGAGAGTG
TTGTGTGAAACGCTCCAGCATCCTGGCTGTAACATTCGGAGATTGTGGTTGGGGCGCTGT
GGCCTCTCGCATGAGTGCTGCTTCGACATCTCCTTGGTCCTCAGCAGCAACCAGAAGCTG
GTGGAGCTGGACCTGAGTGACAACGCCCTCGGTGACTTCGGAATCAGACTTCTGTGTGTG
GGACTGAAGCACCTGTTGTGCAATCTGAAGAAGCTCTGGTTGGTCAGCTGCTGCCTCACA
TCAGCATGTTGTCAGGATCTTGCATCAGTATTGAGCACCAGCCATTCCCTGACCAGACTC
TATGTGGGGGAGAATGCCTTGGGAGACTCAGGAGTCGCAATTTTATGTGAAAAAGCCAAG
AATCCACAGTGTAACCTGCAGAAACTGGGGTTGGTGAATTCTGGCCTTACGTCAGTCTGT
TGTTCAGCTTTGTCCTCGGTACTCAGCACTAATCAGAATCTCACGCACCTTTACCTGCGA
GGCAACACTCTCGGAGACAAGGGGATCAAACTACTCTGTGAGGGACTCTTGCACCCCGAC
TGCAAGCTTCAGGTGTTGGAATTAGACAACTGCAACCTCACGTCACACTGCTGCTGGGAT
CTTTCCACACTTCTGACCTCCAGCCAGAGCCTGCGAAAGCTGAGCCTGGGCAACAATGAC
CTGGGCGACCTGGGGGTCATGATGTTCTGTGAAGTGCTGAAACAGCAGAGCTGCCTCCTG
CAGAACCTGGGGTTGTCTGAAATGTATTTCAATTATGAGACAAAAAGTGCGTTAGAAACA
CTTCAAGAAGAAAAGCCTGAGCTGACCGTCGTCTTTGAGCCTTCTTGGTAG
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:16400
Chromosome Location1
LocusNot Available
References
  1. Hoffman HM, Mueller JL, Broide DH, Wanderer AA, Kolodner RD: Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat Genet. 2001 Nov;29(3):301-5. 11687797
  2. Aganna E, Martinon F, Hawkins PN, Ross JB, Swan DC, Booth DR, Lachmann HJ, Bybee A, Gaudet R, Woo P, Feighery C, Cotter FE, Thome M, Hitman GA, Tschopp J, McDermott MF: Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis. Arthritis Rheum. 2002 Sep;46(9):2445-52. 12355493
  3. Manji GA, Wang L, Geddes BJ, Brown M, Merriam S, Al-Garawi A, Mak S, Lora JM, Briskin M, Jurman M, Cao J, DiStefano PS, Bertin J: PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B. J Biol Chem. 2002 Mar 29;277(13):11570-5. Epub 2002 Jan 10. 11786556
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. 16710414
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  7. O'Connor W Jr, Harton JA, Zhu X, Linhoff MW, Ting JP: Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties. J Immunol. 2003 Dec 15;171(12):6329-33. 14662828
  8. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. 11042152
  9. Agostini L, Martinon F, Burns K, McDermott MF, Hawkins PN, Tschopp J: NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity. 2004 Mar;20(3):319-25. 15030775
  10. Papin S, Cuenin S, Agostini L, Martinon F, Werner S, Beer HD, Grutter C, Grutter M, Tschopp J: The SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing. Cell Death Differ. 2007 Aug;14(8):1457-66. Epub 2007 Apr 13. 17431422
  11. Kummer JA, Broekhuizen R, Everett H, Agostini L, Kuijk L, Martinon F, van Bruggen R, Tschopp J: Inflammasome components NALP 1 and 3 show distinct but separate expression profiles in human tissues suggesting a site-specific role in the inflammatory response. J Histochem Cytochem. 2007 May;55(5):443-52. Epub 2006 Dec 12. 17164409
  12. McCall SH, Sahraei M, Young AB, Worley CS, Duncan JA, Ting JP, Marriott I: Osteoblasts express NLRP3, a nucleotide-binding domain and leucine-rich repeat region containing receptor implicated in bacterially induced cell death. J Bone Miner Res. 2008 Jan;23(1):30-40. 17907925
  13. Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES: Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem. 2012 Oct 19;287(43):36617-22. doi: 10.1074/jbc.M112.407130. Epub 2012 Sep 4. 22948162
  14. Lu B, Nakamura T, Inouye K, Li J, Tang Y, Lundback P, Valdes-Ferrer SI, Olofsson PS, Kalb T, Roth J, Zou Y, Erlandsson-Harris H, Yang H, Ting JP, Wang H, Andersson U, Antoine DJ, Chavan SS, Hotamisligil GS, Tracey KJ: Novel role of PKR in inflammasome activation and HMGB1 release. Nature. 2012 Aug 30;488(7413):670-4. doi: 10.1038/nature11290. 22801494
  15. Shenoy AR, Wellington DA, Kumar P, Kassa H, Booth CJ, Cresswell P, MacMicking JD: GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals. Science. 2012 Apr 27;336(6080):481-5. doi: 10.1126/science.1217141. Epub 2012 Mar 29. 22461501
  16. Lo YH, Huang YW, Wu YH, Tsai CS, Lin YC, Mo ST, Kuo WC, Chuang YT, Jiang ST, Shih HM, Lai MZ: Selective inhibition of the NLRP3 inflammasome by targeting to promyelocytic leukemia protein in mouse and human. Blood. 2013 Apr 18;121(16):3185-94. doi: 10.1182/blood-2012-05-432104. Epub 2013 Feb 21. 23430110
  17. Haneklaus M, O'Neill LA, Coll RC: Modulatory mechanisms controlling the NLRP3 inflammasome in inflammation: recent developments. Curr Opin Immunol. 2013 Feb;25(1):40-5. doi: 10.1016/j.coi.2012.12.004. Epub 2013 Jan 7. 23305783
  18. Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR, Schroder GF, Fitzgerald KA, Wu H, Egelman EH: Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell. 2014 Mar 13;156(6):1193-206. doi: 10.1016/j.cell.2014.02.008. 24630722
  19. Baroja-Mazo A, Martin-Sanchez F, Gomez AI, Martinez CM, Amores-Iniesta J, Compan V, Barbera-Cremades M, Yague J, Ruiz-Ortiz E, Anton J, Bujan S, Couillin I, Brough D, Arostegui JI, Pelegrin P: The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response. Nat Immunol. 2014 Aug;15(8):738-48. doi: 10.1038/ni.2919. Epub 2014 Jun 22. 24952504
  20. Lu A, Wu H: Structural mechanisms of inflammasome assembly. FEBS J. 2015 Feb;282(3):435-44. doi: 10.1111/febs.13133. Epub 2014 Nov 21. 25354325
  21. Kimura T, Jain A, Choi SW, Mandell MA, Schroder K, Johansen T, Deretic V: TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity. J Cell Biol. 2015 Sep 14;210(6):973-89. 26347139
  22. Bae JY, Park HH: Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly. J Biol Chem. 2011 Nov 11;286(45):39528-36. doi: 10.1074/jbc.M111.278812. Epub 2011 Aug 31. 21880711
  23. Dode C, Le Du N, Cuisset L, Letourneur F, Berthelot JM, Vaudour G, Meyrier A, Watts RA, Scott DG, Nicholls A, Granel B, Frances C, Garcier F, Edery P, Boulinguez S, Domergues JP, Delpech M, Grateau G: New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: a novel mutation underlies both syndromes. Am J Hum Genet. 2002 Jun;70(6):1498-506. Epub 2002 Apr 25. 11992256
  24. Feldmann J, Prieur AM, Quartier P, Berquin P, Certain S, Cortis E, Teillac-Hamel D, Fischer A, de Saint Basile G: Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am J Hum Genet. 2002 Jul;71(1):198-203. Epub 2002 May 24. 12032915
  25. Aksentijevich I, Nowak M, Mallah M, Chae JJ, Watford WT, Hofmann SR, Stein L, Russo R, Goldsmith D, Dent P, Rosenberg HF, Austin F, Remmers EF, Balow JE Jr, Rosenzweig S, Komarow H, Shoham NG, Wood G, Jones J, Mangra N, Carrero H, Adams BS, Moore TL, Schikler K, Hoffman H, Lovell DJ, Lipnick R, Barron K, O'Shea JJ, Kastner DL, Goldbach-Mansky R: 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. Arthritis Rheum. 2002 Dec;46(12):3340-8. 12483741
  26. Hoffman HM, Gregory SG, Mueller JL, Tresierras M, Broide DH, Wanderer AA, Kolodner RD: Fine structure mapping of CIAS1: identification of an ancestral haplotype and a common FCAS mutation, L353P. Hum Genet. 2003 Feb;112(2):209-16. Epub 2002 Nov 16. 12522564
  27. Frenkel J, van Kempen MJ, Kuis W, van Amstel HK: Variant chronic infantile neurologic, cutaneous, articular syndrome due to a mutation within the leucine-rich repeat domain of CIAS1. Arthritis Rheum. 2004 Aug;50(8):2719-20. 15334500
  28. Arostegui JI, Aldea A, Modesto C, Rua MJ, Arguelles F, Gonzalez-Ensenat MA, Ramos E, Rius J, Plaza S, Vives J, Yague J: Clinical and genetic heterogeneity among Spanish patients with recurrent autoinflammatory syndromes associated with the CIAS1/PYPAF1/NALP3 gene. Arthritis Rheum. 2004 Dec;50(12):4045-50. 15593220
  29. Neven B, Callebaut I, Prieur AM, Feldmann J, Bodemer C, Lepore L, Derfalvi B, Benjaponpitak S, Vesely R, Sauvain MJ, Oertle S, Allen R, Morgan G, Borkhardt A, Hill C, Gardner-Medwin J, Fischer A, de Saint Basile G: Molecular basis of the spectral expression of CIAS1 mutations associated with phagocytic cell-mediated autoinflammatory disorders CINCA/NOMID, MWS, and FCU. Blood. 2004 Apr 1;103(7):2809-15. Epub 2003 Nov 20. 14630794
  30. Stojanov S, Weiss M, Lohse P, Belohradsky BH: A novel CIAS1 mutation and plasma/cerebrospinal fluid cytokine profile in a German patient with neonatal-onset multisystem inflammatory disease responsive to methotrexate therapy. Pediatrics. 2004 Jul;114(1):e124-7. 15231984
  31. Shalev SA, Sprecher E, Indelman M, Hujirat Y, Bergman R, Rottem M: A novel missense mutation in CIAS1 encoding the pyrin-like protein, cryopyrin, causes familial cold autoinflammatory syndrome in a family of Ethiopian origin. Int Arch Allergy Immunol. 2007;143(3):190-3. Epub 2007 Feb 6. 17284928