메뉴 건너뛰기




Volumn 18, Issue 8, 2017, Pages 832-842

The monogenic autoinflammatory diseases define new pathways in human innate immunity and inflammation

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; PATHOGEN ASSOCIATED MOLECULAR PATTERN; PATTERN RECOGNITION RECEPTOR; PROTEIN KINASE C; CYTOKINE; IL1B PROTEIN, HUMAN; INTERFERON;

EID: 85025805288     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.3777     Document Type: Review
Times cited : (300)

References (163)
  • 1
    • 0033515520 scopus 로고    scopus 로고
    • Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes
    • McDermott, M.F. et al. Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 97, 133-144 (1999).
    • (1999) Cell , vol.97 , pp. 133-144
    • McDermott, M.F.1
  • 3
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R. &Janeway, C.A. Jr. Innate immunity: the virtues of a nonclonal system of recognition. Cell 91, 295-298 (1997).
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 4
    • 84901310586 scopus 로고    scopus 로고
    • Mechanisms and functions of inflammasomes
    • Lamkanfi, M. &Dixit, V.M. Mechanisms and functions of inflammasomes. Cell 157, 1013-1022 (2014).
    • (2014) Cell , vol.157 , pp. 1013-1022
    • Lamkanfi, M.1    Dixit, V.M.2
  • 5
    • 84978374487 scopus 로고    scopus 로고
    • Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
    • Liu, X. et al. Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores. Nature 535, 153-158 (2016).
    • (2016) Nature , vol.535 , pp. 153-158
    • Liu, X.1
  • 6
    • 84978419608 scopus 로고    scopus 로고
    • Pore-forming activity and structural autoinhibition of the gasdermin family
    • Ding, J. et al. Pore-forming activity and structural autoinhibition of the gasdermin family. Nature 535, 111-116 (2016).
    • (2016) Nature , vol.535 , pp. 111-116
    • Ding, J.1
  • 7
    • 84942856523 scopus 로고    scopus 로고
    • Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
    • Kayagaki, N. et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526, 666-671 (2015).
    • (2015) Nature , vol.526 , pp. 666-671
    • Kayagaki, N.1
  • 8
    • 84942892037 scopus 로고    scopus 로고
    • Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
    • Shi, J. et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 526, 660-665 (2015).
    • (2015) Nature , vol.526 , pp. 660-665
    • Shi, J.1
  • 9
    • 85007439966 scopus 로고    scopus 로고
    • Pyroptosis: Gasdermin-mediated programmed necrotic cell death
    • Shi, J., Gao, W. &Shao, F. Pyroptosis: gasdermin-mediated programmed necrotic cell death. Trends Biochem. Sci. 42, 245-254 (2017).
    • (2017) Trends Biochem. Sci. , vol.42 , pp. 245-254
    • Shi, J.1    Gao, W.2    Shao, F.3
  • 10
    • 85022210909 scopus 로고    scopus 로고
    • Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a Gasdermin
    • Wang, Y. et al. Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a Gasdermin. Nature http://dx.doi.org/10.1038/nature22393 (2017).
    • (2017) Nature
    • Wang, Y.1
  • 11
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever
    • The International FMF Consortium
    • The International FMF Consortium. Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. Cell 90, 797-807 (1997).
    • (1997) Cell , vol.90 , pp. 797-807
  • 12
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • French FMF Consortium
    • French FMF Consortium. A candidate gene for familial Mediterranean fever. Nat. Genet. 17, 25-31 (1997).
    • (1997) Nat. Genet. , vol.17 , pp. 25-31
  • 13
    • 0037228468 scopus 로고    scopus 로고
    • Clinical and diagnostic value of genetic testing in 216 Israeli children with Familial Mediterranean fever
    • Padeh, S. et al. Clinical and diagnostic value of genetic testing in 216 Israeli children with Familial Mediterranean fever. J. Rheumatol. 30, 185-190 (2003).
    • (2003) J. Rheumatol. , vol.30 , pp. 185-190
    • Padeh, S.1
  • 14
    • 66449096202 scopus 로고    scopus 로고
    • Familial Mediterranean fever with a single MEFV mutation: Where is the second hit
    • Booty, M.G. et al. Familial Mediterranean fever with a single MEFV mutation: where is the second hit? Arthritis Rheum. 60, 1851-1861 (2009).
    • (2009) Arthritis Rheum. , vol.60 , pp. 1851-1861
    • Booty, M.G.1
  • 15
    • 66449090908 scopus 로고    scopus 로고
    • Clinical disease among patients heterozygous for familial Mediterranean fever
    • Marek-Yagel, D. et al. Clinical disease among patients heterozygous for familial Mediterranean fever. Arthritis Rheum. 60, 1862-1866 (2009).
    • (2009) Arthritis Rheum. , vol.60 , pp. 1862-1866
    • Marek-Yagel, D.1
  • 16
    • 33744762729 scopus 로고    scopus 로고
    • Clinical and subclinical inflammation in patients with familial Mediterranean fever and in heterozygous carriers of MEFV mutations
    • Lachmann, H.J. et al. Clinical and subclinical inflammation in patients with familial Mediterranean fever and in heterozygous carriers of MEFV mutations. Rheumatology 45, 746-750 (2006).
    • (2006) Rheumatology , vol.45 , pp. 746-750
    • Lachmann, H.J.1
  • 17
    • 79956299492 scopus 로고    scopus 로고
    • Gain-of-function Pyrin mutations induce NLRP3 protein-independent interleukin-1β activation and severe autoinflammation in mice
    • Chae, J.J. et al. Gain-of-function Pyrin mutations induce NLRP3 protein-independent interleukin-1β activation and severe autoinflammation in mice. Immunity 34, 755-768 (2011).
    • (2011) Immunity , vol.34 , pp. 755-768
    • Chae, J.J.1
  • 18
    • 34548768341 scopus 로고    scopus 로고
    • Pyrin levels in human monocytes and monocyte-derived macrophages regulate IL-1beta processing and release
    • Seshadri, S., Duncan, M.D., Hart, J.M., Gavrilin, M.A. &Wewers, M.D. Pyrin levels in human monocytes and monocyte-derived macrophages regulate IL-1beta processing and release. J. Immunol. 179, 1274-1281 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 1274-1281
    • Seshadri, S.1    Duncan, M.D.2    Hart, J.M.3    Gavrilin, M.A.4    Wewers, M.D.5
  • 19
    • 30844432876 scopus 로고    scopus 로고
    • Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization
    • Yu, J.W. et al. Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization. Cell Death Differ. 13, 236-249 (2006).
    • (2006) Cell Death Differ. , vol.13 , pp. 236-249
    • Yu, J.W.1
  • 20
    • 84907270863 scopus 로고    scopus 로고
    • Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome
    • Xu, H. et al. Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature 513, 237-241 (2014).
    • (2014) Nature , vol.513 , pp. 237-241
    • Xu, H.1
  • 21
    • 84976329660 scopus 로고    scopus 로고
    • Pyrin inflammasome activation and RhoA signaling in the autoinflammatory diseases FMF and HIDS
    • Park, Y.H., Wood, G., Kastner, D.L. &Chae, J.J. Pyrin inflammasome activation and RhoA signaling in the autoinflammatory diseases FMF and HIDS. Nat. Immunol. 17, 914-921 (2016).
    • (2016) Nat. Immunol. , vol.17 , pp. 914-921
    • Park, Y.H.1    Wood, G.2    Kastner, D.L.3    Chae, J.J.4
  • 22
    • 84962744592 scopus 로고    scopus 로고
    • Familial autoinflammation with neutrophilic dermatosis reveals a regulatory mechanism of pyrin activation
    • Masters, S.L. et al. Familial autoinflammation with neutrophilic dermatosis reveals a regulatory mechanism of pyrin activation. Sci. Transl. Med. 8, 332ra45 (2016).
    • (2016) Sci. Transl. Med. , vol.8 , pp. 332ra45
    • Masters, S.L.1
  • 23
    • 84982091531 scopus 로고    scopus 로고
    • Site-specific phosphorylation and microtubule dynamics control Pyrin inflammasome activation
    • Gao, W., Yang, J., Liu, W., Wang, Y. &Shao, F. Site-specific phosphorylation and microtubule dynamics control Pyrin inflammasome activation. Proc. Natl. Acad. Sci. USA 113, E4857-E4866 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. E4857-E4866
    • Gao, W.1    Yang, J.2    Liu, W.3    Wang, Y.4    Shao, F.5
  • 24
    • 85005992585 scopus 로고    scopus 로고
    • Familial Mediterranean fever mutations lift the obligatory requirement for microtubules in Pyrin inflammasome activation
    • Van Gorp, H. et al. Familial Mediterranean fever mutations lift the obligatory requirement for microtubules in Pyrin inflammasome activation. Proc. Natl. Acad. Sci. USA 113, 14384-14389 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 14384-14389
    • Van Gorp, H.1
  • 25
    • 0034642515 scopus 로고    scopus 로고
    • Recognition of Pathogens by Plants
    • Holt, B.F. III., Mackey, D. &Dangl, J.L. Recognition of pathogens by plants. Curr. Biol. 10, R5-R7 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. R5-R7
    • Holt, B.F.1    Mackey, D.2    Dangl, J.L.3
  • 26
    • 77956268009 scopus 로고    scopus 로고
    • Immunology taught by bacteria
    • Vance, R.E. Immunology taught by bacteria. J. Clin. Immunol. 30, 507-511 (2010).
    • (2010) J. Clin. Immunol. , vol.30 , pp. 507-511
    • Vance, R.E.1
  • 27
    • 85007586393 scopus 로고    scopus 로고
    • The Yersinia pestis effector YopM inhibits pyrin inflammasome activation
    • Ratner, D. et al. The Yersinia pestis effector YopM inhibits pyrin inflammasome activation. PLoS Pathog. 12, e1006035 (2016).
    • (2016) PLoS Pathog. , vol.12 , pp. e1006035
    • Ratner, D.1
  • 28
    • 84995580482 scopus 로고    scopus 로고
    • The Yersinia virulence factor YopM hijacks host kinases to inhibit type III effector-triggered activation of the pyrin inflammasome
    • Chung, L.K. et al. The Yersinia virulence factor YopM hijacks host kinases to inhibit type III effector-triggered activation of the pyrin inflammasome. Cell Host Microbe 20, 296-306 (2016).
    • (2016) Cell Host Microbe , vol.20 , pp. 296-306
    • Chung, L.K.1
  • 29
    • 84964664672 scopus 로고    scopus 로고
    • A Burkholderia type VI effector deamidates Rho GTPases to activate the pyrin inflammasome and trigger inflammation
    • Aubert, D.F. et al. A Burkholderia type VI effector deamidates Rho GTPases to activate the pyrin inflammasome and trigger inflammation. Cell Host Microbe 19, 664-674 (2016).
    • (2016) Cell Host Microbe , vol.19 , pp. 664-674
    • Aubert, D.F.1
  • 30
    • 85011575295 scopus 로고    scopus 로고
    • Homeostasis-altering molecular processes as mechanisms of inflammasome activation
    • Liston, A. &Masters, S.L. Homeostasis-altering molecular processes as mechanisms of inflammasome activation. Nat. Rev. Immunol. 17, 208-214 (2017).
    • (2017) Nat. Rev. Immunol. , vol.17 , pp. 208-214
    • Liston, A.1    Masters, S.L.2
  • 31
    • 0033039501 scopus 로고    scopus 로고
    • Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome
    • Drenth, J.P. et al. Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. Nat. Genet. 22, 178-181 (1999).
    • (1999) Nat. Genet. , vol.22 , pp. 178-181
    • Drenth, J.P.1
  • 32
    • 0032987982 scopus 로고    scopus 로고
    • Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome
    • Houten, S.M. et al. Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat. Genet. 22, 175-177 (1999).
    • (1999) Nat. Genet. , vol.22 , pp. 175-177
    • Houten, S.M.1
  • 33
    • 84976313489 scopus 로고    scopus 로고
    • Control of the innate immune response by the mevalonate pathway
    • Akula, M.K. et al. Control of the innate immune response by the mevalonate pathway. Nat. Immunol. 17, 922-929 (2016).
    • (2016) Nat. Immunol. , vol.17 , pp. 922-929
    • Akula, M.K.1
  • 34
    • 84866933028 scopus 로고    scopus 로고
    • Exome sequencing identifies MVK mutations in disseminated superficial actinic porokeratosis
    • Zhang, S.-Q. et al. Exome sequencing identifies MVK mutations in disseminated superficial actinic porokeratosis. Nat. Genet. 44, 1156-1160 (2012).
    • (2012) Nat. Genet. , vol.44 , pp. 1156-1160
    • Zhang, S.-Q.1
  • 35
    • 84954223176 scopus 로고    scopus 로고
    • Identification of three mutations in the MVK gene in six patients associated with disseminated superficial actinic porokeratosis
    • Liu, Y. et al. Identification of three mutations in the MVK gene in six patients associated with disseminated superficial actinic porokeratosis. Clin. Chim. Acta 454, 124-129 (2016).
    • (2016) Clin. Chim. Acta , vol.454 , pp. 124-129
    • Liu, Y.1
  • 36
    • 0035179970 scopus 로고    scopus 로고
    • 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. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 29, 301-305 (2001).
    • (2001) Nat. Genet. , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 37
    • 1642285783 scopus 로고    scopus 로고
    • NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder
    • Agostini, L. et al. NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 20, 319-325 (2004).
    • (2004) Immunity , vol.20 , pp. 319-325
    • Agostini, L.1
  • 38
    • 84940467473 scopus 로고    scopus 로고
    • Phenotypic and genotypic characteristics of cryopyrin-associated periodic syndrome: A series of 136 patients from the Eurofever Registry
    • Levy, R. et al. Phenotypic and genotypic characteristics of cryopyrin-associated periodic syndrome: a series of 136 patients from the Eurofever Registry. Ann. Rheum. Dis. 74, 2043-2049 (2015).
    • (2015) Ann. Rheum. Dis. , vol.74 , pp. 2043-2049
    • Levy, R.1
  • 39
    • 27744440753 scopus 로고    scopus 로고
    • Somatic mosaicism of CIAS1 in a patient with chronic infantile neurologic, cutaneous, articular syndrome
    • Saito, M. et al. Somatic mosaicism of CIAS1 in a patient with chronic infantile neurologic, cutaneous, articular syndrome. Arthritis Rheum. 52, 3579-3585 (2005).
    • (2005) Arthritis Rheum. , vol.52 , pp. 3579-3585
    • Saito, M.1
  • 40
    • 41349094800 scopus 로고    scopus 로고
    • Disease-associated CIAS1 mutations induce monocyte death, revealing low-level mosaicism in mutation-negative cryopyrin-associated periodic syndrome patients
    • Saito, M. et al. Disease-associated CIAS1 mutations induce monocyte death, revealing low-level mosaicism in mutation-negative cryopyrin-associated periodic syndrome patients. Blood 111, 2132-2141 (2008).
    • (2008) Blood , vol.111 , pp. 2132-2141
    • Saito, M.1
  • 41
    • 80155148684 scopus 로고    scopus 로고
    • High incidence of NLRP3 somatic mosaicism in patients with chronic infantile neurologic, cutaneous, articular syndrome: Results of an international multicenter collaborative study
    • Tanaka, N. et al. High incidence of NLRP3 somatic mosaicism in patients with chronic infantile neurologic, cutaneous, articular syndrome: results of an international multicenter collaborative study. Arthritis Rheum. 63, 3625-3632 (2011).
    • (2011) Arthritis Rheum. , vol.63 , pp. 3625-3632
    • Tanaka, N.1
  • 42
    • 84937609176 scopus 로고    scopus 로고
    • Brief report: Cryopyrin-associated periodic syndrome caused by a myeloid-restricted somatic NLRP3 mutation
    • Zhou, Q. et al. Brief report: cryopyrin-associated periodic syndrome caused by a myeloid-restricted somatic NLRP3 mutation. Arthrtis Rheumatol. 67, 2482-2486 (2015).
    • (2015) Arthrtis Rheumatol. , vol.67 , pp. 2482-2486
    • Zhou, Q.1
  • 43
    • 84997712052 scopus 로고    scopus 로고
    • Brief report: Late-onset cryopyrin-associated periodic syndrome due to myeloid-restricted somatic NLRP3 mosaicism
    • Mensa-Vilaro, A. et al. Brief report: late-onset cryopyrin-associated periodic syndrome due to myeloid-restricted somatic NLRP3 mosaicism. Arthritis Rheumatol. 68, 3035-3041 (2016).
    • (2016) Arthritis Rheumatol. , vol.68 , pp. 3035-3041
    • Mensa-Vilaro, A.1
  • 44
    • 84922375101 scopus 로고    scopus 로고
    • Myeloid lineage-restricted somatic mosaicism of NLRP3 mutations in patients with variant Schnitzler syndrome
    • de Koning, H.D. et al. Myeloid lineage-restricted somatic mosaicism of NLRP3 mutations in patients with variant Schnitzler syndrome. J. Allergy Clin. Immunol. 135, 561-564 (2015).
    • (2015) J. Allergy Clin. Immunol. , vol.135 , pp. 561-564
    • De Koning, H.D.1
  • 45
    • 75849132801 scopus 로고    scopus 로고
    • Genetic predisposition (NLRP3 V198M mutation) for IL-1-mediated inflammation in a patient with Schnitzler syndrome
    • Loock, J. et al. Genetic predisposition (NLRP3 V198M mutation) for IL-1-mediated inflammation in a patient with Schnitzler syndrome. J. Allergy Clin. Immunol. 125, 500-502 (2010).
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 500-502
    • Loock, J.1
  • 46
    • 84870508924 scopus 로고    scopus 로고
    • The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP
    • Lee, G.S. et al. The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP. Nature 492, 123-127 (2012).
    • (2012) Nature , vol.492 , pp. 123-127
    • Lee, G.S.1
  • 47
    • 84858677223 scopus 로고    scopus 로고
    • Sensing and reacting to microbes through the inflammasomes
    • Franchi, L., Muñoz-Planillo, R. &Núñez, G. Sensing and reacting to microbes through the inflammasomes. Nat. Immunol. 13, 325-332 (2012).
    • (2012) Nat. Immunol. , vol.13 , pp. 325-332
    • Franchi, L.1    Muñoz-Planillo, R.2    Núñez, G.3
  • 48
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • Hornung, V. et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 9, 847-856 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 847-856
    • Hornung, V.1
  • 49
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A. &Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237-241 (2006).
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Pétrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 50
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • Dostert, C. et al. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320, 674-677 (2008).
    • (2008) Science , vol.320 , pp. 674-677
    • Dostert, C.1
  • 51
    • 34547101484 scopus 로고    scopus 로고
    • Differential requirement of P2X7 receptor and intracellular K+ for caspase-1 activation induced by intracellular and extracellular bacteria
    • Franchi, L., Kanneganti, T.-D., Dubyak, G.R. &Núñez, G. Differential requirement of P2X7 receptor and intracellular K+ for caspase-1 activation induced by intracellular and extracellular bacteria. J. Biol. Chem. 282, 18810-18818 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 18810-18818
    • Franchi, L.1    Kanneganti, T.-D.2    Dubyak, G.R.3    Núñez, G.4
  • 52
    • 77951800951 scopus 로고    scopus 로고
    • NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
    • Duewell, P. et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 464, 1357-1361 (2010).
    • (2010) Nature , vol.464 , pp. 1357-1361
    • Duewell, P.1
  • 53
    • 84883825948 scopus 로고    scopus 로고
    • Mechanisms of disease: Inflammasome activation and the development of type 2 diabetes
    • Grant, R.W. &Dixit, V.D. Mechanisms of disease: inflammasome activation and the development of type 2 diabetes. Front. Immunol. 4, 50 (2013).
    • (2013) Front. Immunol. , vol.4 , pp. 50
    • Grant, R.W.1    Dixit, V.D.2
  • 54
    • 33747162175 scopus 로고    scopus 로고
    • Abnormal disulfide-linked oligomerization results in ER retention and altered signaling by TNFR1 mutants in TNFR1-associated periodic fever syndrome (TRAPS)
    • Lobito, A.A. et al. Abnormal disulfide-linked oligomerization results in ER retention and altered signaling by TNFR1 mutants in TNFR1-associated periodic fever syndrome (TRAPS). Blood 108, 1320-1327 (2006).
    • (2006) Blood , vol.108 , pp. 1320-1327
    • Lobito, A.A.1
  • 55
    • 77953089570 scopus 로고    scopus 로고
    • Concerted action of wild-type and mutant TNF receptors enhances inflammation in TNF receptor 1-associated periodic fever syndrome
    • Simon, A. et al. Concerted action of wild-type and mutant TNF receptors enhances inflammation in TNF receptor 1-associated periodic fever syndrome. Proc. Natl. Acad. Sci. USA 107, 9801-9806 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9801-9806
    • Simon, A.1
  • 56
    • 79952184583 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS)
    • Bulua, A.C. et al. Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS). J. Exp. Med. 208, 519-533 (2011).
    • (2011) J. Exp. Med. , vol.208 , pp. 519-533
    • Bulua, A.C.1
  • 57
    • 28844494900 scopus 로고    scopus 로고
    • The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals
    • Williams, K.L. et al. The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. J. Biol. Chem. 280, 39914-39924 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 39914-39924
    • Williams, K.L.1
  • 58
    • 33846473862 scopus 로고    scopus 로고
    • Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes
    • Lich, J.D. et al. Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes. J. Immunol. 178, 1256-1260 (2007).
    • (2007) J. Immunol. , vol.178 , pp. 1256-1260
    • Lich, J.D.1
  • 59
    • 84861460062 scopus 로고    scopus 로고
    • NLRP12 suppresses colon inflammation and tumorigenesis through the negative regulation of noncanonical NF-κB signaling
    • Allen, I.C. et al. NLRP12 suppresses colon inflammation and tumorigenesis through the negative regulation of noncanonical NF-κB signaling. Immunity 36, 742-754 (2012).
    • (2012) Immunity , vol.36 , pp. 742-754
    • Allen, I.C.1
  • 60
    • 40349113175 scopus 로고    scopus 로고
    • Mutations in NALP12 cause hereditary periodic fever syndromes
    • Jéru, I. et al. Mutations in NALP12 cause hereditary periodic fever syndromes. Proc. Natl. Acad. Sci. USA 105, 1614-1619 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1614-1619
    • Jéru, I.1
  • 61
    • 84988432082 scopus 로고    scopus 로고
    • NLRP12 autoinflammatory disease: A Chinese case series and literature review
    • Shen, M., Tang, L., Shi, X., Zeng, X. &Yao, Q. NLRP12 autoinflammatory disease: a Chinese case series and literature review. Clin. Rheumatol. http://dx.doi.org/10.1007/s10067-016-3410-y (2016).
    • (2016) Clin. Rheumatol.
    • Shen, M.1    Tang, L.2    Shi, X.3    Zeng, X.4    Yao, Q.5
  • 62
    • 79955566751 scopus 로고    scopus 로고
    • Identification and functional consequences of a recurrent NLRP12 missense mutation in periodic fever syndromes
    • Jéru, I. et al. Identification and functional consequences of a recurrent NLRP12 missense mutation in periodic fever syndromes. Arthritis Rheum. 63, 1459-1464 (2011).
    • (2011) Arthritis Rheum. , vol.63 , pp. 1459-1464
    • Jéru, I.1
  • 63
    • 79953702540 scopus 로고    scopus 로고
    • Clinical presentation and pathogenesis of cold-induced autoinflammatory disease in a family with recurrence of an NLRP12 mutation
    • Borghini, S. et al. Clinical presentation and pathogenesis of cold-induced autoinflammatory disease in a family with recurrence of an NLRP12 mutation. Arthritis Rheum. 63, 830-839 (2011).
    • (2011) Arthritis Rheum. , vol.63 , pp. 830-839
    • Borghini, S.1
  • 64
    • 0037091012 scopus 로고    scopus 로고
    • Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder
    • Wise, C.A. et al. Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder. Hum. Mol. Genet. 11, 961-969 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 961-969
    • Wise, C.A.1
  • 65
    • 35348934890 scopus 로고    scopus 로고
    • Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants
    • Yu, J.W. et al. Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants. Mol. Cell 28, 214-227 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 214-227
    • Yu, J.W.1
  • 66
    • 0344823965 scopus 로고    scopus 로고
    • Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway
    • Shoham, N.G. et al. Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway. Proc. Natl. Acad. Sci. USA 100, 13501-13506 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13501-13506
    • Shoham, N.G.1
  • 67
    • 84899659118 scopus 로고    scopus 로고
    • The F-BAR protein PSTPIP1 controls extracellular matrix degradation and filopodia formation in macrophages
    • Starnes, T.W. et al. The F-BAR protein PSTPIP1 controls extracellular matrix degradation and filopodia formation in macrophages. Blood 123, 2703-2714 (2014).
    • (2014) Blood , vol.123 , pp. 2703-2714
    • Starnes, T.W.1
  • 68
    • 84977103263 scopus 로고    scopus 로고
    • Disease activity accounts for long-term efficacy of IL-1 blockers in pyogenic sterile arthritis pyoderma gangrenosum and severe acne syndrome
    • Omenetti, A. et al. Disease activity accounts for long-term efficacy of IL-1 blockers in pyogenic sterile arthritis pyoderma gangrenosum and severe acne syndrome. Rheumatology 55, 1325-1335 (2016).
    • (2016) Rheumatology , vol.55 , pp. 1325-1335
    • Omenetti, A.1
  • 69
    • 22244469461 scopus 로고    scopus 로고
    • Homozygous mutations in LPIN2 are responsible for the syndrome of chronic recurrent multifocal osteomyelitis and congenital dyserythropoietic anaemia (Majeed syndrome)
    • Ferguson, P.J. et al. Homozygous mutations in LPIN2 are responsible for the syndrome of chronic recurrent multifocal osteomyelitis and congenital dyserythropoietic anaemia (Majeed syndrome). J. Med. Genet. 42, 551-557 (2005).
    • (2005) J. Med. Genet. , vol.42 , pp. 551-557
    • Ferguson, P.J.1
  • 71
    • 85012261804 scopus 로고    scopus 로고
    • Lipin-2 regulates NLRP3 inflammasome by affecting P2X7 receptor activation
    • Lordén, G. et al. Lipin-2 regulates NLRP3 inflammasome by affecting P2X7 receptor activation. J. Exp. Med. 214, 511-528 (2017).
    • (2017) J. Exp. Med. , vol.214 , pp. 511-528
    • Lordén, G.1
  • 72
    • 84858630049 scopus 로고    scopus 로고
    • A role for the NLRP3 inflammasome in metabolic diseases: Did Warburg miss inflammation
    • Wen, H., Ting, J.P.Y. &O'Neill, L.A.J. A role for the NLRP3 inflammasome in metabolic diseases: did Warburg miss inflammation? Nat. Immunol. 13, 352-357 (2012).
    • (2012) Nat. Immunol. , vol.13 , pp. 352-357
    • Wen, H.1    Ting, J.P.Y.2    O'Neill, L.A.J.3
  • 73
    • 85017605327 scopus 로고    scopus 로고
    • Mitochondria are the powerhouses of immunity
    • Mills, E.L., Kelly, B. &O'Neill, L.A.J. Mitochondria are the powerhouses of immunity. Nat. Immunol. 18, 488-498 (2017).
    • (2017) Nat. Immunol. , vol.18 , pp. 488-498
    • Mills, E.L.1    Kelly, B.2    O'Neill, L.A.J.3
  • 74
    • 66649121678 scopus 로고    scopus 로고
    • An autoinflammatory disease with deficiency of the interleukin-1-receptor antagonist
    • Aksentijevich, I. et al. An autoinflammatory disease with deficiency of the interleukin-1-receptor antagonist. N. Engl. J. Med. 360, 2426-2437 (2009).
    • (2009) N. Engl. J. Med. , vol.360 , pp. 2426-2437
    • Aksentijevich, I.1
  • 75
    • 66649113371 scopus 로고    scopus 로고
    • An autoinflammatory disease due to homozygous deletion of the IL1RN locus
    • Reddy, S. et al. An autoinflammatory disease due to homozygous deletion of the IL1RN locus. N. Engl. J. Med. 360, 2438-2444 (2009).
    • (2009) N. Engl. J. Med. , vol.360 , pp. 2438-2444
    • Reddy, S.1
  • 76
    • 84860390352 scopus 로고    scopus 로고
    • Interleukin-36-receptor antagonist deficiency and generalized pustular psoriasis
    • Marrakchi, S. et al. Interleukin-36-receptor antagonist deficiency and generalized pustular psoriasis. N. Engl. J. Med. 365, 620-628 (2011).
    • (2011) N. Engl. J. Med. , vol.365 , pp. 620-628
    • Marrakchi, S.1
  • 77
    • 80052744921 scopus 로고    scopus 로고
    • Mutations in IL36RN/IL1F5 are associated with the severe episodic inflammatory skin disease known as generalized pustular psoriasis
    • Onoufriadis, A. et al. Mutations in IL36RN/IL1F5 are associated with the severe episodic inflammatory skin disease known as generalized pustular psoriasis. Am. J. Hum. Genet. 89, 432-437 (2011).
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 432-437
    • Onoufriadis, A.1
  • 78
    • 84892863312 scopus 로고    scopus 로고
    • Biology of IL-36 cytokines and their role in disease
    • Gresnigt, M.S. &van de Veerdonk, F.L. Biology of IL-36 cytokines and their role in disease. Semin. Immunol. 25, 458-465 (2013).
    • (2013) Semin. Immunol. , vol.25 , pp. 458-465
    • Gresnigt, M.S.1    Van De Veerdonk, F.L.2
  • 79
    • 13244277880 scopus 로고    scopus 로고
    • Nod2 mutation in Crohn's disease potentiates NF-kappaB activity and IL-1β processing
    • Maeda, S. et al. Nod2 mutation in Crohn's disease potentiates NF-kappaB activity and IL-1β processing. Science 307, 734-738 (2005).
    • (2005) Science , vol.307 , pp. 734-738
    • Maeda, S.1
  • 80
    • 13244292161 scopus 로고    scopus 로고
    • Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract
    • Kobayashi, K.S. et al. Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 307, 731-734 (2005).
    • (2005) Science , vol.307 , pp. 731-734
    • Kobayashi, K.S.1
  • 81
    • 84964425113 scopus 로고    scopus 로고
    • NOD1 and NOD2 signalling links ER stress with inflammation
    • Keestra-Gounder, A.M. et al. NOD1 and NOD2 signalling links ER stress with inflammation. Nature 532, 394-397 (2016).
    • (2016) Nature , vol.532 , pp. 394-397
    • Keestra-Gounder, A.M.1
  • 83
    • 84992073928 scopus 로고    scopus 로고
    • Nod2: A critical regulator of ileal microbiota and Crohn's disease
    • Sidiq, T., Yoshihama, S., Downs, I. &Kobayashi, K.S. Nod2: a critical regulator of ileal microbiota and Crohn's disease. Front. Immunol. 7, 367 (2016).
    • (2016) Front. Immunol. , vol.7 , pp. 367
    • Sidiq, T.1    Yoshihama, S.2    Downs, I.3    Kobayashi, K.S.4
  • 84
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • Hugot, J.-P. et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature 411, 599-603 (2001).
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.-P.1
  • 85
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • Ogura, Y. et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411, 603-606 (2001).
    • (2001) Nature , vol.411 , pp. 603-606
    • Ogura, Y.1
  • 86
    • 17944372335 scopus 로고    scopus 로고
    • CARD15 mutations in Blau syndrome
    • Miceli-Richard, C. et al. CARD15 mutations in Blau syndrome. Nat. Genet. 29, 19-20 (2001).
    • (2001) Nat. Genet. , vol.29 , pp. 19-20
    • Miceli-Richard, C.1
  • 87
    • 33244472793 scopus 로고    scopus 로고
    • Signalling pathways and molecular interactions of NOD1 and NOD2
    • Strober, W., Murray, P.J., Kitani, A. &Watanabe, T. Signalling pathways and molecular interactions of NOD1 and NOD2. Nat. Rev. Immunol. 6, 9-20 (2006).
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 9-20
    • Strober, W.1    Murray, P.J.2    Kitani, A.3    Watanabe, T.4
  • 88
    • 19944431022 scopus 로고    scopus 로고
    • Early-onset sarcoidosis and CARD15 mutations with constitutive nuclear factor-kappaB activation: Common genetic etiology with Blau syndrome
    • Kanazawa, N. et al. Early-onset sarcoidosis and CARD15 mutations with constitutive nuclear factor-kappaB activation: common genetic etiology with Blau syndrome. Blood 105, 1195-1197 (2005).
    • (2005) Blood , vol.105 , pp. 1195-1197
    • Kanazawa, N.1
  • 89
    • 84974623115 scopus 로고    scopus 로고
    • Crystal structure of NOD2 and its implications in human disease
    • Maekawa, S., Ohto, U., Shibata, T., Miyake, K. &Shimizu, T. Crystal structure of NOD2 and its implications in human disease. Nat. Commun. 7, 11813 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 11813
    • Maekawa, S.1    Ohto, U.2    Shibata, T.3    Miyake, K.4    Shimizu, T.5
  • 90
    • 84962054020 scopus 로고    scopus 로고
    • Brief report: First identification of intrafamilial recurrence of Blau syndrome due to gonosomal NOD2 mosaicism
    • Mensa-Vilaro, A. et al. Brief report: first identification of intrafamilial recurrence of Blau syndrome due to gonosomal NOD2 mosaicism. Arthritis Rheumatol. 68, 1039-1044 (2016).
    • (2016) Arthritis Rheumatol. , vol.68 , pp. 1039-1044
    • Mensa-Vilaro, A.1
  • 91
    • 84860770362 scopus 로고    scopus 로고
    • PSORS2 is due to mutations in CARD14
    • Jordan, C.T. et al. PSORS2 is due to mutations in CARD14. Am. J. Hum. Genet. 90, 784-795 (2012).
    • (2012) Am. J. Hum. Genet. , vol.90 , pp. 784-795
    • Jordan, C.T.1
  • 92
    • 84863980712 scopus 로고    scopus 로고
    • Familial pityriasis rubra pilaris is caused by mutations in CARD14
    • Fuchs-Telem, D. et al. Familial pityriasis rubra pilaris is caused by mutations in CARD14. Am. J. Hum. Genet. 91, 163-170 (2012).
    • (2012) Am. J. Hum. Genet. , vol.91 , pp. 163-170
    • Fuchs-Telem, D.1
  • 93
    • 84860725325 scopus 로고    scopus 로고
    • Rare and common variants in CARD14, encoding an epidermal regulator of NF-kappaB, in psoriasis
    • Jordan, C.T. et al. Rare and common variants in CARD14, encoding an epidermal regulator of NF-kappaB, in psoriasis. Am. J. Hum. Genet. 90, 796-808 (2012).
    • (2012) Am. J. Hum. Genet. , vol.90 , pp. 796-808
    • Jordan, C.T.1
  • 94
    • 85013942396 scopus 로고    scopus 로고
    • CARD14-mediated activation of paracaspase MALT1 in keratinocytes: Implications for psoriasis
    • Van Nuffel, E. et al. CARD14-mediated activation of paracaspase MALT1 in keratinocytes: implications for psoriasis. J. Invest. Dermatol. 137, 569-575 (2017).
    • (2017) J. Invest. Dermatol. , vol.137 , pp. 569-575
    • Van Nuffel, E.1
  • 95
    • 70949087383 scopus 로고    scopus 로고
    • Inflammatory bowel disease and mutations affecting the interleukin-10 receptor
    • Glocker, E.-O. et al. Inflammatory bowel disease and mutations affecting the interleukin-10 receptor. N. Engl. J. Med. 361, 2033-2045 (2009).
    • (2009) N. Engl. J. Med. , vol.361 , pp. 2033-2045
    • Glocker, E.-O.1
  • 96
    • 77958003426 scopus 로고    scopus 로고
    • Infant colitis: It's in the genes
    • Glocker, E.O. et al. Infant colitis: it's in the genes. Lancet 376, 1272 (2010).
    • (2010) Lancet , vol.376 , pp. 1272
    • Glocker, E.O.1
  • 97
    • 84864206050 scopus 로고    scopus 로고
    • Loss of interleukin-10 signaling and infantile inflammatory bowel disease: Implications for diagnosis and therapy
    • Kotlarz, D. et al. Loss of interleukin-10 signaling and infantile inflammatory bowel disease: implications for diagnosis and therapy. Gastroenterology 143, 347-355 (2012).
    • (2012) Gastroenterology , vol.143 , pp. 347-355
    • Kotlarz, D.1
  • 98
    • 84997199517 scopus 로고    scopus 로고
    • Interleukin 1β mediates intestinal inflammation in mice and patients with interleukin 10 receptor deficiency
    • Shouval, D.S. et al. Interleukin 1β mediates intestinal inflammation in mice and patients with interleukin 10 receptor deficiency. Gastroenterology 151, 1100-1104 (2016).
    • (2016) Gastroenterology , vol.151 , pp. 1100-1104
    • Shouval, D.S.1
  • 99
    • 0031970553 scopus 로고    scopus 로고
    • Genetic studies into inherited and sporadic hemolytic uremic syndrome
    • Warwicker, P. et al. Genetic studies into inherited and sporadic hemolytic uremic syndrome. Kidney Int. 53, 836-844 (1998).
    • (1998) Kidney Int. , vol.53 , pp. 836-844
    • Warwicker, P.1
  • 100
    • 77952682366 scopus 로고    scopus 로고
    • Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome
    • Maga, T.K., Nishimura, C.J., Weaver, A.E., Frees, K.L. &Smith, R.J. Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome. Hum. Mutat. 31, E1445-E1460 (2010).
    • (2010) Hum. Mutat. , vol.31 , pp. E1445-E1460
    • Maga, T.K.1    Nishimura, C.J.2    Weaver, A.E.3    Frees, K.L.4    Smith, R.J.5
  • 101
    • 0242570482 scopus 로고    scopus 로고
    • Familial haemolytic uraemic syndrome and an MCP mutation
    • Noris, M. et al. Familial haemolytic uraemic syndrome and an MCP mutation. Lancet 362, 1542-1547 (2003).
    • (2003) Lancet , vol.362 , pp. 1542-1547
    • Noris, M.1
  • 102
    • 67651166873 scopus 로고    scopus 로고
    • Thrombomodulin mutations in atypical hemolytic-uremic syndrome
    • Delvaeye, M. et al. Thrombomodulin mutations in atypical hemolytic-uremic syndrome. N. Engl. J. Med. 361, 345-357 (2009).
    • (2009) N. Engl. J. Med. , vol.361 , pp. 345-357
    • Delvaeye, M.1
  • 103
    • 85012876399 scopus 로고    scopus 로고
    • Complementopathies
    • Baines, A.C. &Brodsky, R.A. Complementopathies. Blood Rev. http://dx.doi.org/10.1016/j.blre.2017.02.003 (2017).
    • (2017) Blood Rev.
    • Baines, A.C.1    Brodsky, R.A.2
  • 104
    • 17244379811 scopus 로고    scopus 로고
    • Complement factor H polymorphism and age-related macular degeneration
    • Edwards, A.O. et al. Complement factor H polymorphism and age-related macular degeneration. Science 308, 421-424 (2005).
    • (2005) Science , vol.308 , pp. 421-424
    • Edwards, A.O.1
  • 105
    • 20244388812 scopus 로고    scopus 로고
    • Complement factor H variant increases the risk of age-related macular degeneration
    • Haines, J.L. et al. Complement factor H variant increases the risk of age-related macular degeneration. Science 308, 419-421 (2005).
    • (2005) Science , vol.308 , pp. 419-421
    • Haines, J.L.1
  • 106
    • 20244380171 scopus 로고    scopus 로고
    • Complement factor H polymorphism in age-related macular degeneration
    • Klein, R.J. et al. Complement factor H polymorphism in age-related macular degeneration. Science 308, 385-389 (2005).
    • (2005) Science , vol.308 , pp. 385-389
    • Klein, R.J.1
  • 107
    • 85013980911 scopus 로고    scopus 로고
    • Complement factor H inhibits CD47-mediated resolution of inflammation
    • Calippe, B. et al. Complement factor H inhibits CD47-mediated resolution of inflammation. Immunity 46, 261-272 (2017).
    • (2017) Immunity , vol.46 , pp. 261-272
    • Calippe, B.1
  • 108
    • 0027310539 scopus 로고
    • Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria
    • Takeda, J. et al. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell 73, 703-711 (1993).
    • (1993) Cell , vol.73 , pp. 703-711
    • Takeda, J.1
  • 109
    • 0028057807 scopus 로고
    • Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene
    • Bessler, M. et al. Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 13, 110-117 (1994).
    • (1994) EMBO J. , vol.13 , pp. 110-117
    • Bessler, M.1
  • 110
    • 84867255789 scopus 로고    scopus 로고
    • A hypermorphic missense mutation in PLCG2, encoding phospholipase Cγ2, causes a dominantly inherited autoinflammatory disease with immunodeficiency
    • Zhou, Q. et al. A hypermorphic missense mutation in PLCG2, encoding phospholipase Cγ2, causes a dominantly inherited autoinflammatory disease with immunodeficiency. Am. J. Hum. Genet. 91, 713-720 (2012).
    • (2012) Am. J. Hum. Genet. , vol.91 , pp. 713-720
    • Zhou, Q.1
  • 111
    • 84922762977 scopus 로고    scopus 로고
    • Connecting two pathways through Ca2+ signaling: NLRP3 inflammasome activation induced by a hypermorphic PLCG2 mutation
    • Chae, J.J. et al. Connecting two pathways through Ca2+ signaling: NLRP3 inflammasome activation induced by a hypermorphic PLCG2 mutation. Arthritis Rheumatol. 67, 563-567 (2015).
    • (2015) Arthritis Rheumatol. , vol.67 , pp. 563-567
    • Chae, J.J.1
  • 112
    • 84863030888 scopus 로고    scopus 로고
    • Cold urticaria, immunodeficiency, and autoimmunity related to PLCG2 deletions
    • Ombrello, M.J. et al. Cold urticaria, immunodeficiency, and autoimmunity related to PLCG2 deletions. N. Engl. J. Med. 366, 330-338 (2012).
    • (2012) N. Engl. J. Med. , vol.366 , pp. 330-338
    • Ombrello, M.J.1
  • 113
    • 84927126118 scopus 로고    scopus 로고
    • An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome
    • Canna, S.W. et al. An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome. Nat. Genet. 46, 1140-1146 (2014).
    • (2014) Nat. Genet. , vol.46 , pp. 1140-1146
    • Canna, S.W.1
  • 114
    • 84922008927 scopus 로고    scopus 로고
    • Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation
    • Romberg, N. et al. Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation. Nat. Genet. 46, 1135-1139 (2014).
    • (2014) Nat. Genet. , vol.46 , pp. 1135-1139
    • Romberg, N.1
  • 115
    • 84921498910 scopus 로고    scopus 로고
    • The NAIP/NLRC4 inflammasomes
    • Vance, R.E. The NAIP/NLRC4 inflammasomes. Curr. Opin. Immunol. 32, 84-89 (2015).
    • (2015) Curr. Opin. Immunol. , vol.32 , pp. 84-89
    • Vance, R.E.1
  • 116
    • 84911922142 scopus 로고    scopus 로고
    • An inherited mutation in NLRC4 causes autoinflammation in human and mice
    • Kitamura, A., Sasaki, Y., Abe, T., Kano, H. &Yasutomo, K. An inherited mutation in NLRC4 causes autoinflammation in human and mice. J. Exp. Med. 211, 2385-2396 (2014).
    • (2014) J. Exp. Med. , vol.211 , pp. 2385-2396
    • Kitamura, A.1    Sasaki, Y.2    Abe, T.3    Kano, H.4    Yasutomo, K.5
  • 117
    • 85010877091 scopus 로고    scopus 로고
    • Identification of a high-frequency somatic NLRC4 mutation as a cause of autoinflammation by pluripotent cell-based phenotype dissection
    • Kawasaki, Y. et al. Identification of a high-frequency somatic NLRC4 mutation as a cause of autoinflammation by pluripotent cell-based phenotype dissection. Arthritis Rheumatol. 69, 447-459 (2017).
    • (2017) Arthritis Rheumatol. , vol.69 , pp. 447-459
    • Kawasaki, Y.1
  • 118
    • 84988622178 scopus 로고    scopus 로고
    • Germline NLRP1 mutations cause skin inflammatory and cancer susceptibility syndromes via inflammasome activation
    • e17
    • Zhong, F.L. et al. Germline NLRP1 mutations cause skin inflammatory and cancer susceptibility syndromes via inflammasome activation. Cell 167, 187-202.e17 (2016).
    • (2016) Cell , vol.167 , pp. 187-202
    • Zhong, F.L.1
  • 119
    • 85006995122 scopus 로고    scopus 로고
    • A new autoinflammatory and autoimmune syndrome associated with NLRP1 mutations: NAIAD (NLRP1-associated autoinflammation with arthritis and dyskeratosis)
    • Grandemange, S. et al. A new autoinflammatory and autoimmune syndrome associated with NLRP1 mutations: NAIAD (NLRP1-associated autoinflammation with arthritis and dyskeratosis). Ann. Rheum. Dis. http://dx.doi.org/10.1136/annrheumdis-2016-210021 (2016).
    • (2016) Ann. Rheum. Dis.
    • Grandemange, S.1
  • 120
    • 33947497237 scopus 로고    scopus 로고
    • NALP1 in vitiligo-associated multiple autoimmune disease
    • Jin, Y. et al. NALP1 in vitiligo-associated multiple autoimmune disease. N. Engl. J. Med. 356, 1216-1225 (2007).
    • (2007) N. Engl. J. Med. , vol.356 , pp. 1216-1225
    • Jin, Y.1
  • 121
    • 78649775528 scopus 로고    scopus 로고
    • PSMB8 encoding the β5i proteasome subunit is mutated in joint contractures, muscle atrophy, microcytic anemia, and panniculitis-induced lipodystrophy syndrome
    • Agarwal, A.K. et al. PSMB8 encoding the β5i proteasome subunit is mutated in joint contractures, muscle atrophy, microcytic anemia, and panniculitis-induced lipodystrophy syndrome. Am. J. Hum. Genet. 87, 866-872 (2010).
    • (2010) Am. J. Hum. Genet. , vol.87 , pp. 866-872
    • Agarwal, A.K.1
  • 122
    • 80053397654 scopus 로고    scopus 로고
    • A mutation in the immunoproteasome subunit PSMB8 causes autoinflammation and lipodystrophy in humans
    • Kitamura, A.K. et al. A mutation in the immunoproteasome subunit PSMB8 causes autoinflammation and lipodystrophy in humans. J. Clin. Invest. 121, 4150-4160 (2011).
    • (2011) J. Clin. Invest. , vol.121 , pp. 4150-4160
    • Kitamura, A.K.1
  • 123
    • 80052565561 scopus 로고    scopus 로고
    • Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome
    • Arima, K. et al. Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome. Proc. Natl. Acad. Sci. USA 108, 14914-14919 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14914-14919
    • Arima, K.1
  • 124
    • 84863232739 scopus 로고    scopus 로고
    • Mutations in proteasome subunit β type 8 cause chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature with evidence of genetic and phenotypic heterogeneity
    • Liu, Y. et al. Mutations in proteasome subunit β type 8 cause chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature with evidence of genetic and phenotypic heterogeneity. Arthritis Rheum. 64, 895-907 (2012).
    • (2012) Arthritis Rheum. , vol.64 , pp. 895-907
    • Liu, Y.1
  • 125
    • 84946780874 scopus 로고    scopus 로고
    • Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type i IFN production
    • Brehm, A. et al. Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type I IFN production. J. Clin. Invest. 125, 4196-4211 (2015).
    • (2015) J. Clin. Invest. , vol.125 , pp. 4196-4211
    • Brehm, A.1
  • 126
    • 84905825645 scopus 로고    scopus 로고
    • Activated STING in a vascular and pulmonary syndrome
    • Liu, Y. et al. Activated STING in a vascular and pulmonary syndrome. N. Engl. J. Med. 371, 507-518 (2014).
    • (2014) N. Engl. J. Med. , vol.371 , pp. 507-518
    • Liu, Y.1
  • 127
    • 84873711885 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type i interferon pathway
    • Sun, L., Wu, J., Du, F., Chen, X. &Chen, Z.J. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339, 786-791 (2013).
    • (2013) Science , vol.339 , pp. 786-791
    • Sun, L.1    Wu, J.2    Du, F.3    Chen, X.4    Chen, Z.J.5
  • 128
    • 84873724533 scopus 로고    scopus 로고
    • Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA
    • Wu, J. et al. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA. Science 339, 826-830 (2013).
    • (2013) Science , vol.339 , pp. 826-830
    • Wu, J.1
  • 129
    • 67649861901 scopus 로고    scopus 로고
    • Mutations involved in Aicardi-Goutières syndrome implicate SAMHD1 as regulator of the innate immune response
    • Rice, G.I. et al. Mutations involved in Aicardi-Goutières syndrome implicate SAMHD1 as regulator of the innate immune response. Nat. Genet. 41, 829-832 (2009).
    • (2009) Nat. Genet. , vol.41 , pp. 829-832
    • Rice, G.I.1
  • 130
    • 84899495767 scopus 로고    scopus 로고
    • Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type i interferon signaling
    • Rice, G.I. et al. Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling. Nat. Genet. 46, 503-509 (2014).
    • (2014) Nat. Genet. , vol.46 , pp. 503-509
    • Rice, G.I.1
  • 131
    • 84868207785 scopus 로고    scopus 로고
    • Mutations in ADAR1 cause Aicardi-Goutières syndrome associated with a type i interferon signature
    • Rice, G.I. et al. Mutations in ADAR1 cause Aicardi-Goutières syndrome associated with a type I interferon signature. Nat. Genet. 44, 1243-1248 (2012).
    • (2012) Nat. Genet. , vol.44 , pp. 1243-1248
    • Rice, G.I.1
  • 132
    • 84887607415 scopus 로고    scopus 로고
    • Assessment of interferon-related biomarkers in Aicardi-Goutières syndrome associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, and ADAR: A case-control study
    • Rice, G.I. et al. Assessment of interferon-related biomarkers in Aicardi-Goutières syndrome associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, and ADAR: a case-control study. Lancet Neurol. 12, 1159-1169 (2013).
    • (2013) Lancet Neurol. , vol.12 , pp. 1159-1169
    • Rice, G.I.1
  • 133
    • 33746522835 scopus 로고    scopus 로고
    • Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutières syndrome and mimic congenital viral brain infection
    • Crow, Y.J. et al. Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutières syndrome and mimic congenital viral brain infection. Nat. Genet. 38, 910-916 (2006).
    • (2006) Nat. Genet. , vol.38 , pp. 910-916
    • Crow, Y.J.1
  • 134
    • 33746581694 scopus 로고    scopus 로고
    • Mutations in the gene encoding the 3′-5′ DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locus
    • Crow, Y.J. et al. Mutations in the gene encoding the 3′-5′ DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locus. Nat. Genet. 38, 917-920 (2006).
    • (2006) Nat. Genet. , vol.38 , pp. 917-920
    • Crow, Y.J.1
  • 135
    • 84949599562 scopus 로고    scopus 로고
    • Loss-of-function mutations in TNFAIP3 leading to A20 haploinsufficiency cause an early-onset autoinflammatory disease
    • Zhou, Q. et al. Loss-of-function mutations in TNFAIP3 leading to A20 haploinsufficiency cause an early-onset autoinflammatory disease. Nat. Genet. 48, 67-73 (2016).
    • (2016) Nat. Genet. , vol.48 , pp. 67-73
    • Zhou, Q.1
  • 136
    • 84905562455 scopus 로고    scopus 로고
    • Negative regulation of the NLRP3 inflammasome by A20 protects against arthritis
    • Vande Walle, L. et al. Negative regulation of the NLRP3 inflammasome by A20 protects against arthritis. Nature 512, 69-73 (2014).
    • (2014) Nature , vol.512 , pp. 69-73
    • Vande Walle, L.1
  • 137
    • 84921305910 scopus 로고    scopus 로고
    • A20 restricts ubiquitination of pro-interleukin-1β protein complexes and suppresses NLRP3 inflammasome activity
    • Duong, B.H. et al. A20 restricts ubiquitination of pro-interleukin-1β protein complexes and suppresses NLRP3 inflammasome activity. Immunity 42, 55-67 (2015).
    • (2015) Immunity , vol.42 , pp. 55-67
    • Duong, B.H.1
  • 138
    • 84957818338 scopus 로고    scopus 로고
    • Recruitment of A20 by the C-terminal domain of NEMO suppresses NF-κB activation and autoinflammatory disease
    • Zilberman-Rudenko, J. et al. Recruitment of A20 by the C-terminal domain of NEMO suppresses NF-κB activation and autoinflammatory disease. Proc. Natl. Acad. Sci. USA 113, 1612-1617 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 1612-1617
    • Zilberman-Rudenko, J.1
  • 139
    • 84985992152 scopus 로고    scopus 로고
    • Biallelic hypomorphic mutations in a linear deubiquitinase define otulipenia, an early-onset autoinflammatory disease
    • Zhou, Q. et al. Biallelic hypomorphic mutations in a linear deubiquitinase define otulipenia, an early-onset autoinflammatory disease. Proc. Natl. Acad. Sci. USA 113, 10127-10132 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 10127-10132
    • Zhou, Q.1
  • 140
    • 84981719187 scopus 로고    scopus 로고
    • The deubiquitinase OTULIN is an essential negative regulator of inflammation and autoimmunity
    • e20
    • Damgaard, R.B. et al. The deubiquitinase OTULIN is an essential negative regulator of inflammation and autoimmunity. Cell 166, 1215-1230.e20 (2016).
    • (2016) Cell , vol.166 , pp. 1215-1230
    • Damgaard, R.B.1
  • 141
    • 84980347632 scopus 로고    scopus 로고
    • Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia
    • Boisson, B. et al. Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia. J. Exp. Med. 212, 939-951 (2015).
    • (2015) J. Exp. Med. , vol.212 , pp. 939-951
    • Boisson, B.1
  • 142
    • 84869429707 scopus 로고    scopus 로고
    • Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency
    • Boisson, B. et al. Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency. Nat. Immunol. 13, 1178-1186 (2012).
    • (2012) Nat. Immunol. , vol.13 , pp. 1178-1186
    • Boisson, B.1
  • 143
    • 84908584244 scopus 로고    scopus 로고
    • Mutations in TRNT1 cause congenital sideroblastic anemia with immunodeficiency, fevers, and developmental delay (SIFD)
    • Chakraborty, P.K. et al. Mutations in TRNT1 cause congenital sideroblastic anemia with immunodeficiency, fevers, and developmental delay (SIFD). Blood 124, 2867-2871 (2014).
    • (2014) Blood , vol.124 , pp. 2867-2871
    • Chakraborty, P.K.1
  • 144
    • 85008471383 scopus 로고    scopus 로고
    • Autoinflammatory periodic fever, immunodeficiency, and thrombocytopenia (PFIT) caused by mutation in actin-regulatory gene WDR1
    • Standing, A.S. et al. Autoinflammatory periodic fever, immunodeficiency, and thrombocytopenia (PFIT) caused by mutation in actin-regulatory gene WDR1. J. Exp. Med. 2041, 59-71 (2017).
    • (2017) J. Exp. Med. , vol.2041 , pp. 59-71
    • Standing, A.S.1
  • 145
    • 84940453310 scopus 로고    scopus 로고
    • Aberrant actin depolymerization triggers the pyrin inflammasome and autoinflammatory disease that is dependent on IL-18, not IL-1β
    • Kim, M.L. et al. Aberrant actin depolymerization triggers the pyrin inflammasome and autoinflammatory disease that is dependent on IL-18, not IL-1β. J. Exp. Med. 212, 927-938 (2015).
    • (2015) J. Exp. Med. , vol.212 , pp. 927-938
    • Kim, M.L.1
  • 146
    • 84895461649 scopus 로고    scopus 로고
    • Early-onset stroke and vasculopathy associated with mutations in ADA2
    • Zhou, Q. et al. Early-onset stroke and vasculopathy associated with mutations in ADA2. N. Engl. J. Med. 370, 911-920 (2014).
    • (2014) N. Engl. J. Med. , vol.370 , pp. 911-920
    • Zhou, Q.1
  • 147
    • 84895465707 scopus 로고    scopus 로고
    • Mutant adenosine deaminase 2 in a polyarteritis nodosa vasculopathy
    • Navon Elkan, P. et al. Mutant adenosine deaminase 2 in a polyarteritis nodosa vasculopathy. N. Engl. J. Med. 370, 921-931 (2014).
    • (2014) N. Engl. J. Med. , vol.370 , pp. 921-931
    • Navon, E.P.1
  • 148
    • 84965060479 scopus 로고    scopus 로고
    • Phenotypic variability in patients with ADA2 deficiency due to identical homozygous R169Q mutations
    • Van Montfrans, J.M. et al. Phenotypic variability in patients with ADA2 deficiency due to identical homozygous R169Q mutations. Rheumatology 55, 902-910 (2016).
    • (2016) Rheumatology , vol.55 , pp. 902-910
    • Van Montfrans, J.M.1
  • 149
    • 84959017087 scopus 로고    scopus 로고
    • Vibratory urticaria associated with a missense variant in ADGRE2
    • Boyden, S.E. et al. Vibratory urticaria associated with a missense variant in ADGRE2. N. Engl. J. Med. 374, 656-663 (2016).
    • (2016) N. Engl. J. Med. , vol.374 , pp. 656-663
    • Boyden, S.E.1
  • 150
    • 33746876396 scopus 로고    scopus 로고
    • Neonatal-onset multisystem inflammatory disease responsive to interleukin-1β inhibition
    • Goldbach-Mansky, R. et al. Neonatal-onset multisystem inflammatory disease responsive to interleukin-1β inhibition. N. Engl. J. Med. 355, 581-592 (2006).
    • (2006) N. Engl. J. Med. , vol.355 , pp. 581-592
    • Goldbach-Mansky, R.1
  • 151
    • 66649102432 scopus 로고    scopus 로고
    • Use of canakinumab in the cryopyrin-associated periodic syndrome
    • Lachmann, H.J. et al. Use of canakinumab in the cryopyrin-associated periodic syndrome. N. Engl. J. Med. 360, 2416-2425 (2009).
    • (2009) N. Engl. J. Med. , vol.360 , pp. 2416-2425
    • Lachmann, H.J.1
  • 152
    • 84942107560 scopus 로고    scopus 로고
    • A 24-month open-label study of canakinumab in neonatal-onset multisystem inflammatory disease
    • Sibley, C.H. et al. A 24-month open-label study of canakinumab in neonatal-onset multisystem inflammatory disease. Ann. Rheum. Dis. 74, 1714-1719 (2015).
    • (2015) Ann. Rheum. Dis. , vol.74 , pp. 1714-1719
    • Sibley, C.H.1
  • 153
    • 49449094892 scopus 로고    scopus 로고
    • A pilot study to evaluate the safety and efficacy of the long-acting interleukin-1 inhibitor rilonacept (interleukin-1 Trap) in patients with familial cold autoinflammatory syndrome
    • Goldbach-Mansky, R. et al. A pilot study to evaluate the safety and efficacy of the long-acting interleukin-1 inhibitor rilonacept (interleukin-1 Trap) in patients with familial cold autoinflammatory syndrome. Arthritis Rheum. 58, 2432-2442 (2008).
    • (2008) Arthritis Rheum. , vol.58 , pp. 2432-2442
    • Goldbach-Mansky, R.1
  • 154
    • 49449094179 scopus 로고    scopus 로고
    • Efficacy and safety of rilonacept (interleukin-1 Trap) in patients with cryopyrin-associated periodic syndromes: Results from two sequential placebo-controlled studies
    • Hoffman, H.M. et al. Efficacy and safety of rilonacept (interleukin-1 Trap) in patients with cryopyrin-associated periodic syndromes: results from two sequential placebo-controlled studies. Arthritis Rheum. 58, 2443-2452 (2008).
    • (2008) Arthritis Rheum. , vol.58 , pp. 2443-2452
    • Hoffman, H.M.1
  • 155
    • 85008220560 scopus 로고    scopus 로고
    • Life-threatening NLRC4-associated hyperinflammation successfully treated with IL-18 inhibition
    • Canna, S.W. et al. Life-threatening NLRC4-associated hyperinflammation successfully treated with IL-18 inhibition. J. Allergy Clin. Immunol. 139, 1698-1701 (2017).
    • (2017) J. Allergy Clin. Immunol. , vol.139 , pp. 1698-1701
    • Canna, S.W.1
  • 156
    • 33745631232 scopus 로고    scopus 로고
    • The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1β production
    • Chae, J.J. et al. The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1β production. Proc. Natl. Acad. Sci. USA 103, 9982-9987 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9982-9987
    • Chae, J.J.1
  • 157
    • 84868313379 scopus 로고    scopus 로고
    • Rilonacept for colchicine-resistant or-intolerant familial Mediterranean fever: A randomized trial
    • Hashkes, P.J. et al. Rilonacept for colchicine-resistant or-intolerant familial Mediterranean fever: a randomized trial. Ann. Intern. Med. 157, 533-541 (2012).
    • (2012) Ann. Intern. Med. , vol.157 , pp. 533-541
    • Hashkes, P.J.1
  • 158
    • 84984621777 scopus 로고    scopus 로고
    • Familial chilblain lupus due to a gain-of-function mutation in STING
    • König, N. et al. Familial chilblain lupus due to a gain-of-function mutation in STING. Ann. Rheum. Dis. 76, 468-472 (2017).
    • (2017) Ann. Rheum. Dis. , vol.76 , pp. 468-472
    • König, N.1
  • 159
    • 84920399194 scopus 로고    scopus 로고
    • Hematopoietic stem cell transplantation rescues the immunologic phenotype and prevents vasculopathy in patients with adenosine deaminase 2 deficiency
    • Van Eyck, L. Jr. et al. Hematopoietic stem cell transplantation rescues the immunologic phenotype and prevents vasculopathy in patients with adenosine deaminase 2 deficiency. J. Allergy Clin. Immunol. 135, 283-287.e5 (2015).
    • (2015) J. Allergy Clin. Immunol. , vol.135 , pp. 283-283e5
    • Van Eyck, L.1
  • 160
    • 34347233869 scopus 로고    scopus 로고
    • Allogeneic bone marrow transplantation in mevalonic aciduria
    • Neven, B. et al. Allogeneic bone marrow transplantation in mevalonic aciduria. N. Engl. J. Med. 356, 2700-2703 (2007).
    • (2007) N. Engl. J. Med. , vol.356 , pp. 2700-2703
    • Neven, B.1
  • 161
    • 84920365254 scopus 로고    scopus 로고
    • Long-term outcome of a successful cord blood stem cell transplant in mevalonate kinase deficiency
    • Giardino, S. et al. Long-term outcome of a successful cord blood stem cell transplant in mevalonate kinase deficiency. Pediatrics 135, e211-e215 (2015).
    • (2015) Pediatrics , vol.135 , pp. e211-e215
    • Giardino, S.1
  • 162
    • 84999850013 scopus 로고    scopus 로고
    • Type i interferon-mediated monogenic autoinflammation: The type i interferonopathies, a conceptual overview
    • Rodero, M.P. &Crow, Y.J. Type I interferon-mediated monogenic autoinflammation: the type I interferonopathies, a conceptual overview. J. Exp. Med. 213, 2527-2538 (2016).
    • (2016) J. Exp. Med. , vol.213 , pp. 2527-2538
    • Rodero, M.P.1    Crow, Y.J.2
  • 163
    • 84943586392 scopus 로고    scopus 로고
    • New monogenic autoinflammatory diseases-A clinical overview
    • Canna, S.W. &Goldbach-Mansky, R. New monogenic autoinflammatory diseases-A clinical overview. Semin. Immunopathol. 37, 387-394 (2015).
    • (2015) Semin. Immunopathol. , vol.37 , pp. 387-394
    • Canna, S.W.1    Goldbach-Mansky, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.