NLRC4: Difference between revisions

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{{Infobox_gene}}
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'''NLR family CARD domain-containing protein 4''' is a [[protein]] that in humans is encoded by the ''NLRC4'' [[gene]].<ref name="pmid11374873">{{cite journal | vauthors = Geddes BJ, Wang L, Huang WJ, Lavellee M, Manji GA, Brown M, Jurman M, Cao J, Morgenstern J, Merriam S, Glucksmann MA, DiStefano PS, Bertin J | title = Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis | journal = Biochemical and Biophysical Research Communications | volume = 284 | issue = 1 | pages = 77–82 | date = Jun 2001 | pmid = 11374873 | pmc = | doi = 10.1006/bbrc.2001.4928 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NLRC4 NLR family, CARD domain containing 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58484| accessdate = }}</ref>
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = NLR family, CARD domain containing 4
| HGNCid = 16412
| Symbol = NLRC4
| AltSymbols =; CARD12; CLAN; CLAN1; CLANA; CLANB; CLANC; CLAND; CLR2.1; IPAF
| OMIM = 606831
| ECnumber = 
| Homologene = 10924
| MGIid = 3036243
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0016045 |text = detection of bacterium}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}} {{GNF_GO|id=GO:0043281 |text = regulation of caspase activity}} {{GNF_GO|id=GO:0050702 |text = interleukin-1 beta secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 58484
    | Hs_Ensembl = ENSG00000091106
    | Hs_RefseqProtein = NP_067032
    | Hs_RefseqmRNA = NM_021209
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 32303029
    | Hs_GenLoc_end = 32344427
    | Hs_Uniprot = Q9NPP4
    | Mm_EntrezGene = 268973
    | Mm_Ensembl = ENSMUSG00000039193
    | Mm_RefseqmRNA = NM_001033367
    | Mm_RefseqProtein = NP_001028539
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 74331824
    | Mm_GenLoc_end = 74353201
    | Mm_Uniprot = 
  }}
}}
'''NLR family, CARD domain containing 4''', also known as '''NLRC4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NLRC4 NLR family, CARD domain containing 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58484| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
The NLRC4 protein is highly conserved across mammalian species. It bears homology to the [[Caenorhabditis elegans|c. elegans]] Ced4 protein. It contains an n-terminal [[CARD domain|CARD]] domain, a central nucleotide binding/[[NACHT domain|NACHT]] domain, and a c-terminal leucine rich repeat ([[Leucine-rich repeat|LRR]]) domain. It belongs to a family of NLR proteins that includes the transcriptional co-activator [[CIITA]] and the canonical inflammasome protein [[NALP3|NLRP3]]. A truncated murine NLRC4 was the first member of this family whose crystal structure was solved.<ref>{{cite journal | vauthors = Hu Z, Yan C, Liu P, Huang Z, Ma R, Zhang C, Wang R, Zhang Y, Martinon F, Miao D, Deng H, Wang J, Chang J, Chai J | title = Crystal structure of NLRC4 reveals its autoinhibition mechanism | journal = Science | volume = 341 | issue = 6142 | pages = 172–5 | date = Jul 2013 | pmid = 23765277 | doi = 10.1126/science.1236381 }}</ref>  
{{PBB_Summary
| section_title =
| summary_text = In C. elegans, Ced4 binds and activates Ced3, an apoptotic initiator caspase, via caspase-associated recruitment domains (CARDs). Human Ced4 homologs include APAF1 (MIM 602233), NOD1 (CARD4; MIM 605980), and NOD2 (CARD15; MIM 605956). These proteins have at least 1 N-terminal CARD domain followed by a centrally located nucleotide-binding domain (NBD or NACHT) and a C-terminal regulatory domain, found only in mammals, that contains either WD40 repeats or leucine-rich repeats (LRRs). CARD12 is a member of the Ced4 family and can induce apoptosis.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NLRC4 NLR family, CARD domain containing 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58484| accessdate = }}</ref>
}}


==References==
== Function ==
{{reflist|2}}
 
==Further reading==
NLRC4 is best associated with triggering formation of the [[inflammasome]]. Unlike NLRP3, certain inflammasome-dependent functions of NLRC4 may be carried out independently of the inflammasome scaffold [[PYCARD|ASC]].  Human Ced4 homologs include [[APAF1]], [[NOD1]] (CARD4), and [[NOD2]] (CARD15). These proteins have at least 1 [[N-terminal]] CARD domain followed by a centrally located  nucleotide-binding domain (NBD or NACHT) and a [[C-terminal]] regulatory domain, found only in mammals, that contains either [[WD40 repeat]]s or [[leucine-rich repeat]]s (LRRs). CARD12 is a member of the Ced4 family and can induce [[apoptosis]].<ref name="entrez" />
{{refbegin | 2}}
 
{{PBB_Further_reading
== Interactions ==
| citations =  
 
*{{cite journal | author=Geddes BJ, Wang L, Huang WJ, ''et al.'' |title=Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis. |journal=Biochem. Biophys. Res. Commun. |volume=284 |issue= 1 |pages= 77-82 |year= 2001 |pmid= 11374873 |doi= 10.1006/bbrc.2001.4928 }}
NLRC4 has been shown to [[Protein-protein interaction|interact]] with NAIP (there is one human NAIP but mice express at least 4 distinct NAIP proteins). The NAIP/NLRC4 interaction may determine the ligand specificity.<ref>{{cite journal | vauthors = Kofoed EM, Vance RE | title = Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity | journal = Nature | volume = 477 | issue = 7366 | pages = 592–5 | date = Sep 2011 | pmid = 21874021 | pmc = 3184209 | doi = 10.1038/nature10394 }}</ref> NLRC4-dependent inflammasome activity activates [[caspase 1|CASP1]].<ref name = pmid15107016>{{cite journal | vauthors = Damiano JS, Oliveira V, Welsh K, Reed JC | title = Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses | journal = The Biochemical Journal | volume = 381 | issue = Pt 1 | pages = 213–9 | date = Jul 2004 | pmid = 15107016 | pmc = 1133779 | doi = 10.1042/BJ20031506 }}</ref> Under certain circumstances, NLRC4 and NLRP3 may occupy the same inflammasome complex.<ref>{{cite journal | vauthors = Man SM, Hopkins LJ, Nugent E, Cox S, Glück IM, Tourlomousis P, Wright JA, Cicuta P, Monie TP, Bryant CE | title = Inflammasome activation causes dual recruitment of NLRC4 and NLRP3 to the same macromolecular complex | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 111 | issue = 20 | pages = 7403–8 | date = May 2014 | pmid = 24803432 | pmc = 4034195 | doi = 10.1073/pnas.1402911111 }}</ref>
*{{cite journal | author=Poyet JL, Srinivasula SM, Tnani M, ''et al.'' |title=Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28309-13 |year= 2001 |pmid= 11390368 |doi= 10.1074/jbc.C100250200 }}
 
*{{cite journal | author=Damiano JS, Stehlik C, Pio F, ''et al.'' |title=CLAN, a novel human CED-4-like gene. |journal=Genomics |volume=75 |issue= 1-3 |pages= 77-83 |year= 2001 |pmid= 11472070 |doi= 10.1006/geno.2001.6579 }}
== Clinical significance ==
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
 
*{{cite journal | author=Fu WN, Bertoni F, Kelsey SM, ''et al.'' |title=Role of DNA methylation in the suppression of Apaf-1 protein in human leukaemia. |journal=Oncogene |volume=22 |issue= 3 |pages= 451-5 |year= 2003 |pmid= 12545166 |doi= 10.1038/sj.onc.1206147 }}
Humans bearing activating mutations in NLRC4 can develop an [[Periodic fever syndrome|autoinflammatory]] syndrome characterized by acute fever, hepatitis, very high serum ferritin, and other features suggestive of [[Macrophage activation syndrome|Macrophage Activation Syndrome (MAS)]]. Some patients also developed a potentially life-threatening enterocolitis that abated during early childhood.<ref name="Canna_2014">{{cite journal | vauthors = Canna SW, de Jesus AA, Gouni S, Brooks SR, Marrero B, Liu Y, DiMattia MA, Zaal KJ, Sanchez GA, Kim H, Chapelle D, Plass N, Huang Y, Villarino AV, Biancotto A, Fleisher TA, Duncan JA, O'Shea JJ, Benseler S, Grom A, Deng Z, Laxer RM, Goldbach-Mansky R | title = An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome | journal = Nature Genetics | volume = 46 | issue = 10 | pages = 1140–6 | date = Oct 2014 | pmid = 25217959 | pmc = 4177369 | doi = 10.1038/ng.3089 }}</ref><ref>{{cite journal | vauthors = Romberg N, Al Moussawi K, Nelson-Williams C, Stiegler AL, Loring E, Choi M, Overton J, Meffre E, Khokha MK, Huttner AJ, West B, Podoltsev NA, Boggon TJ, Kazmierczak BI, Lifton RP | title = Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation | journal = Nature Genetics | volume = 46 | issue = 10 | pages = 1135–9 | date = Oct 2014 | pmid = 25217960 | pmc = 4177367 | doi = 10.1038/ng.3066 }}</ref> In these patients, chronic and extraordinary elevation of serum [[interleukin 18|IL-18]] is found, in distinction from patients with NLRP3 mutations who develop [[Neonatal onset multisystem inflammatory disease|Cryopyrin Associated Periodic Syndromes]].<ref name="Canna_2014" /> A large Japanese family had much milder disease associated with cold-induced urticaria that was caused by a dominantly inherited NLRC4 mutation.<ref>{{cite journal | vauthors = Kitamura A, Sasaki Y, Abe T, Kano H, Yasutomo K | title = An inherited mutation in NLRC4 causes autoinflammation in human and mice | journal = The Journal of Experimental Medicine | volume = 211 | issue = 12 | pages = 2385–96 | date = Nov 2014 | pmid = 25385754 | pmc = 4235634 | doi = 10.1084/jem.20141091 }}</ref>
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
 
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
== References ==
*{{cite journal | author=Agostini L, Martinon F, Burns K, ''et al.'' |title=NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. |journal=Immunity |volume=20 |issue= 3 |pages= 319-25 |year= 2004 |pmid= 15030775 |doi= }}
{{reflist|33em}}
*{{cite journal | author=Damiano JS, Oliveira V, Welsh K, Reed JC |title=Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses. |journal=Biochem. J. |volume=381 |issue= Pt 1 |pages= 213-9 |year= 2004 |pmid= 15107016 |doi= 10.1042/BJ20031506 }}
 
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
== Further reading ==
*{{cite journal  | author=Damiano JS, Newman RM, Reed JC |title=Multiple roles of CLAN (caspase-associated recruitment domain, leucine-rich repeat, and NAIP CIIA HET-E, and TP1-containing protein) in the mammalian innate immune response. |journal=J. Immunol. |volume=173 |issue= 10 |pages= 6338-45 |year= 2004 |pmid= 15528373 |doi= }}
{{refbegin|33em}}
*{{cite journal | author=Sadasivam S, Gupta S, Radha V, ''et al.'' |title=Caspase-1 activator Ipaf is a p53-inducible gene involved in apoptosis. |journal=Oncogene |volume=24 |issue= 4 |pages= 627-36 |year= 2005 |pmid= 15580302 |doi= 10.1038/sj.onc.1208201 }}
* {{cite journal | vauthors = Poyet JL, Srinivasula SM, Tnani M, Razmara M, Fernandes-Alnemri T, Alnemri ES | title = Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 30 | pages = 28309–13 | date = Jul 2001 | pmid = 11390368 | doi = 10.1074/jbc.C100250200 }}
*{{cite journal | author=Lu C, Wang A, Wang L, ''et al.'' |title=Nucleotide binding to CARD12 and its role in CARD12-mediated caspase-1 activation. |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue= 4 |pages= 1114-9 |year= 2005 |pmid= 15882992 |doi= 10.1016/j.bbrc.2005.04.027 }}
* {{cite journal | vauthors = Damiano JS, Stehlik C, Pio F, Godzik A, Reed JC | title = CLAN, a novel human CED-4-like gene | journal = Genomics | volume = 75 | issue = 1-3 | pages = 77–83 | date = Jul 2001 | pmid = 11472070 | doi = 10.1006/geno.2001.6579 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
* {{cite journal | vauthors = Fu WN, Bertoni F, Kelsey SM, McElwaine SM, Cotter FE, Newland AC, Jia L | title = Role of DNA methylation in the suppression of Apaf-1 protein in human leukaemia | journal = Oncogene | volume = 22 | issue = 3 | pages = 451–5 | date = Jan 2003 | pmid = 12545166 | doi = 10.1038/sj.onc.1206147 }}
*{{cite journal  | author=Thalappilly S, Sadasivam S, Radha V, Swarup G |title=Involvement of caspase 1 and its activator Ipaf upstream of mitochondrial events in apoptosis. |journal=FEBS J. |volume=273 |issue= 12 |pages= 2766-78 |year= 2006 |pmid= 16817903 |doi= 10.1111/j.1742-4658.2006.05293.x }}
* {{cite journal | vauthors = Agostini L, Martinon F, Burns K, McDermott MF, Hawkins PN, Tschopp J | title = NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder | journal = Immunity | volume = 20 | issue = 3 | pages = 319–25 | date = Mar 2004 | pmid = 15030775 | doi = 10.1016/S1074-7613(04)00046-9 }}
}}
* {{cite journal | vauthors = Damiano JS, Oliveira V, Welsh K, Reed JC | title = Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses | journal = The Biochemical Journal | volume = 381 | issue = Pt 1 | pages = 213–9 | date = Jul 2004 | pmid = 15107016 | pmc = 1133779 | doi = 10.1042/BJ20031506 }}
* {{cite journal | vauthors = Damiano JS, Newman RM, Reed JC | title = Multiple roles of CLAN (caspase-associated recruitment domain, leucine-rich repeat, and NAIP CIIA HET-E, and TP1-containing protein) in the mammalian innate immune response | journal = Journal of Immunology | volume = 173 | issue = 10 | pages = 6338–45 | date = Nov 2004 | pmid = 15528373 | doi = 10.4049/jimmunol.173.10.6338 }}
* {{cite journal | vauthors = Sadasivam S, Gupta S, Radha V, Batta K, Kundu TK, Swarup G | title = Caspase-1 activator Ipaf is a p53-inducible gene involved in apoptosis | journal = Oncogene | volume = 24 | issue = 4 | pages = 627–36 | date = Jan 2005 | pmid = 15580302 | doi = 10.1038/sj.onc.1208201 }}
* {{cite journal | vauthors = Lu C, Wang A, Wang L, Dorsch M, Ocain TD, Xu Y | title = Nucleotide binding to CARD12 and its role in CARD12-mediated caspase-1 activation | journal = Biochemical and Biophysical Research Communications | volume = 331 | issue = 4 | pages = 1114–9 | date = Jun 2005 | pmid = 15882992 | doi = 10.1016/j.bbrc.2005.04.027 }}
* {{cite journal | vauthors = Thalappilly S, Sadasivam S, Radha V, Swarup G | title = Involvement of caspase 1 and its activator Ipaf upstream of mitochondrial events in apoptosis | journal = The FEBS Journal | volume = 273 | issue = 12 | pages = 2766–78 | date = Jun 2006 | pmid = 16817903 | doi = 10.1111/j.1742-4658.2006.05293.x }}
{{refend}}
{{refend}}
[[Category:LRR proteins]]


{{protein-stub}}
{{NOD-like receptors}}
{{WikiDoc Sources}}
 
[[Category:LRR proteins]]
[[Category:NOD-like receptors]]
 
{{gene-2-stub}}

Revision as of 13:05, 5 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

NLR family CARD domain-containing protein 4 is a protein that in humans is encoded by the NLRC4 gene.[1][2]

Structure

The NLRC4 protein is highly conserved across mammalian species. It bears homology to the c. elegans Ced4 protein. It contains an n-terminal CARD domain, a central nucleotide binding/NACHT domain, and a c-terminal leucine rich repeat (LRR) domain. It belongs to a family of NLR proteins that includes the transcriptional co-activator CIITA and the canonical inflammasome protein NLRP3. A truncated murine NLRC4 was the first member of this family whose crystal structure was solved.[3]

Function

NLRC4 is best associated with triggering formation of the inflammasome. Unlike NLRP3, certain inflammasome-dependent functions of NLRC4 may be carried out independently of the inflammasome scaffold ASC. Human Ced4 homologs include APAF1, NOD1 (CARD4), and NOD2 (CARD15). These proteins have at least 1 N-terminal CARD domain followed by a centrally located nucleotide-binding domain (NBD or NACHT) and a C-terminal regulatory domain, found only in mammals, that contains either WD40 repeats or leucine-rich repeats (LRRs). CARD12 is a member of the Ced4 family and can induce apoptosis.[2]

Interactions

NLRC4 has been shown to interact with NAIP (there is one human NAIP but mice express at least 4 distinct NAIP proteins). The NAIP/NLRC4 interaction may determine the ligand specificity.[4] NLRC4-dependent inflammasome activity activates CASP1.[5] Under certain circumstances, NLRC4 and NLRP3 may occupy the same inflammasome complex.[6]

Clinical significance

Humans bearing activating mutations in NLRC4 can develop an autoinflammatory syndrome characterized by acute fever, hepatitis, very high serum ferritin, and other features suggestive of Macrophage Activation Syndrome (MAS). Some patients also developed a potentially life-threatening enterocolitis that abated during early childhood.[7][8] In these patients, chronic and extraordinary elevation of serum IL-18 is found, in distinction from patients with NLRP3 mutations who develop Cryopyrin Associated Periodic Syndromes.[7] A large Japanese family had much milder disease associated with cold-induced urticaria that was caused by a dominantly inherited NLRC4 mutation.[9]

References

  1. ↑ Geddes BJ, Wang L, Huang WJ, Lavellee M, Manji GA, Brown M, Jurman M, Cao J, Morgenstern J, Merriam S, Glucksmann MA, DiStefano PS, Bertin J (Jun 2001). "Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis". Biochemical and Biophysical Research Communications. 284 (1): 77–82. doi:10.1006/bbrc.2001.4928. PMID 11374873.
  2. ↑ 2.0 2.1 "Entrez Gene: NLRC4 NLR family, CARD domain containing 4".
  3. ↑ Hu Z, Yan C, Liu P, Huang Z, Ma R, Zhang C, Wang R, Zhang Y, Martinon F, Miao D, Deng H, Wang J, Chang J, Chai J (Jul 2013). "Crystal structure of NLRC4 reveals its autoinhibition mechanism". Science. 341 (6142): 172–5. doi:10.1126/science.1236381. PMID 23765277.
  4. ↑ Kofoed EM, Vance RE (Sep 2011). "Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity". Nature. 477 (7366): 592–5. doi:10.1038/nature10394. PMC 3184209. PMID 21874021.
  5. ↑ Damiano JS, Oliveira V, Welsh K, Reed JC (Jul 2004). "Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses". The Biochemical Journal. 381 (Pt 1): 213–9. doi:10.1042/BJ20031506. PMC 1133779. PMID 15107016.
  6. ↑ Man SM, Hopkins LJ, Nugent E, Cox S, Glück IM, Tourlomousis P, Wright JA, Cicuta P, Monie TP, Bryant CE (May 2014). "Inflammasome activation causes dual recruitment of NLRC4 and NLRP3 to the same macromolecular complex". Proceedings of the National Academy of Sciences of the United States of America. 111 (20): 7403–8. doi:10.1073/pnas.1402911111. PMC 4034195. PMID 24803432.
  7. ↑ 7.0 7.1 Canna SW, de Jesus AA, Gouni S, Brooks SR, Marrero B, Liu Y, DiMattia MA, Zaal KJ, Sanchez GA, Kim H, Chapelle D, Plass N, Huang Y, Villarino AV, Biancotto A, Fleisher TA, Duncan JA, O'Shea JJ, Benseler S, Grom A, Deng Z, Laxer RM, Goldbach-Mansky R (Oct 2014). "An activating NLRC4 inflammasome mutation causes autoinflammation with recurrent macrophage activation syndrome". Nature Genetics. 46 (10): 1140–6. doi:10.1038/ng.3089. PMC 4177369. PMID 25217959.
  8. ↑ Romberg N, Al Moussawi K, Nelson-Williams C, Stiegler AL, Loring E, Choi M, Overton J, Meffre E, Khokha MK, Huttner AJ, West B, Podoltsev NA, Boggon TJ, Kazmierczak BI, Lifton RP (Oct 2014). "Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation". Nature Genetics. 46 (10): 1135–9. doi:10.1038/ng.3066. PMC 4177367. PMID 25217960.
  9. ↑ Kitamura A, Sasaki Y, Abe T, Kano H, Yasutomo K (Nov 2014). "An inherited mutation in NLRC4 causes autoinflammation in human and mice". The Journal of Experimental Medicine. 211 (12): 2385–96. doi:10.1084/jem.20141091. PMC 4235634. PMID 25385754.

Further reading

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