NLRP12: Difference between revisions
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*{{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |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 }} | *{{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |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 }} | ||
*{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }} | *{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }} | ||
*{{cite journal |vauthors=Williams KL, Lich JD, Duncan JA, etal |title=The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. |journal=J. Biol. Chem. |volume=280 |issue= 48 |pages= 39914–24 |year= 2006 |pmid= 16203735 |doi= 10.1074/jbc.M502820200 }} | *{{cite journal |vauthors=Williams KL, Lich JD, Duncan JA, etal |title=The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. |journal=J. Biol. Chem. |volume=280 |issue= 48 |pages= 39914–24 |year= 2006 |pmid= 16203735 |doi= 10.1074/jbc.M502820200 |pmc=4422647 }} | ||
*{{cite journal |vauthors=Lich JD, Williams KL, Moore CB, etal |title=Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes. |journal=J. Immunol. |volume=178 |issue= 3 |pages= 1256–60 |year= 2007 |pmid= 17237370 |doi= 10.4049/jimmunol.178.3.1256}} | *{{cite journal |vauthors=Lich JD, Williams KL, Moore CB, etal |title=Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes. |journal=J. Immunol. |volume=178 |issue= 3 |pages= 1256–60 |year= 2007 |pmid= 17237370 |doi= 10.4049/jimmunol.178.3.1256}} | ||
*{{cite journal |vauthors=Arthur JC, Lich JD, Aziz RK, etal |title=Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. |journal=J. Immunol. |volume=179 |issue= 9 |pages= 6291–6 |year= 2007 |pmid= 17947705 |doi= 10.4049/jimmunol.179.9.6291}} | *{{cite journal |vauthors=Arthur JC, Lich JD, Aziz RK, etal |title=Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. |journal=J. Immunol. |volume=179 |issue= 9 |pages= 6291–6 |year= 2007 |pmid= 17947705 |doi= 10.4049/jimmunol.179.9.6291}} | ||
Latest revision as of 17:48, 15 May 2018
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NACHT, LRR and PYD domains-containing protein 12 is a protein that in humans is encoded by the NLRP12 gene.[1][2][3]
NALPs are cytoplasmic proteins that form a subfamily within the larger CATERPILLER protein family. Most short NALPs, such as NALP12, have an N-terminal pyrin (MEFV; MIM 608107) domain (PYD), followed by a NACHT domain, a NACHT-associated domain (NAD), and a C-terminal leucine-rich repeat (LRR) region. The long NALP, NALP1 (MIM 606636), also has a C-terminal extension containing a function to find domain (FIIND) and a caspase recruitment domain (CARD). NALPs are implicated in the activation of proinflammatory caspases (e.g., CASP1; MIM 147678) via their involvement in multiprotein complexes called inflammasomes (Tschopp et al., 2003).[supplied by OMIM][3]
References
- ↑ Tschopp J, Martinon F, Burns K (Feb 2003). "NALPs: a novel protein family involved in inflammation". Nat Rev Mol Cell Biol. 4 (2): 95–104. doi:10.1038/nrm1019. PMID 12563287.
- ↑ Wang L, Manji GA, Grenier JM, Al-Garawi A, Merriam S, Lora JM, Geddes BJ, Briskin M, DiStefano PS, Bertin J (Aug 2002). "PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing". J Biol Chem. 277 (33): 29874–80. doi:10.1074/jbc.M203915200. PMID 12019269.
- ↑ 3.0 3.1 "Entrez Gene: NLRP12 NLR family, pyrin domain containing 12".
Further reading
- Shami PJ, Kanai N, Wang LY, et al. (2001). "Identification and characterization of a novel gene that is upregulated in leukaemia cells by nitric oxide". Br. J. Haematol. 112 (1): 138–47. doi:10.1046/j.1365-2141.2001.02491.x. PMID 11167794.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Williams KL, Taxman DJ, Linhoff MW, et al. (2003). "Cutting edge: Monarch-1: a pyrin/nucleotide-binding domain/leucine-rich repeat protein that controls classical and nonclassical MHC class I genes". J. Immunol. 170 (11): 5354–8. doi:10.4049/jimmunol.170.11.5354. PMID 12759408.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Williams KL, Lich JD, Duncan JA, et al. (2006). "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 (48): 39914–24. doi:10.1074/jbc.M502820200. PMC 4422647. PMID 16203735.
- Lich JD, Williams KL, Moore CB, et al. (2007). "Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes". J. Immunol. 178 (3): 1256–60. doi:10.4049/jimmunol.178.3.1256. PMID 17237370.
- Arthur JC, Lich JD, Aziz RK, et al. (2007). "Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase". J. Immunol. 179 (9): 6291–6. doi:10.4049/jimmunol.179.9.6291. PMID 17947705.
- Chen L, Wilson JE, Koenigsknecht MJ, et al. (2017). "NLRP12 attenuates colon inflammation by maintaining colonic microbial diversity and promoting protective commensal bacterial growth". Nature Immunology. doi:10.1038/ni.3690.
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