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Volumn 13, Issue 6, 2016, Pages 722-728

Regulation of inflammasomes by ubiquitination

Author keywords

Deubiquitinase; E3 ligase; Inflammasome; Innate immunity; Ubiqutin

Indexed keywords

ADAPTOR PROTEIN; APOPTOSIS ASSOCIATED SPECK LIKE PROTEIN CONTAINING A CASPASE ACTIVATION AND RECRUITMENT DOMAIN PROTEIN; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CRYOPYRIN; DEUBIQUITINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 18; INTERLEUKIN 1BETA; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PATHOGEN ASSOCIATED MOLECULAR PATTERN; PATTERN RECOGNITION RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84994620550     PISSN: 16727681     EISSN: None     Source Type: Journal    
DOI: 10.1038/cmi.2016.15     Document Type: Review
Times cited : (72)

References (62)
  • 1
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K, Tschopp J. The inflammasomes. Cell 2010; 140: 821-832.
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 2
    • 84927732725 scopus 로고    scopus 로고
    • Regulation of inflammasome activation
    • Man SM, Kanneganti TD. Regulation of inflammasome activation. Immunol Rev 2015; 265: 6-21.
    • (2015) Immunol Rev , vol.265 , pp. 6-21
    • Man, S.M.1    Kanneganti, T.D.2
  • 3
    • 0037108346 scopus 로고    scopus 로고
    • Cutting edge: CATERPIL-LER: a large family of mammalian genes containing CARD, pyrin, nucleotide-binding, and leucine-rich repeat domains
    • Harton JA, Linhoff MW, Zhang J, Ting JP. Cutting edge: CATERPIL-LER: a large family of mammalian genes containing CARD, pyrin, nucleotide-binding, and leucine-rich repeat domains. J Immunol 2002; 169: 4088-4093.
    • (2002) J Immunol , vol.169 , pp. 4088-4093
    • Harton, J.A.1    Linhoff, M.W.2    Zhang, J.3    Ting, J.P.4
  • 5
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 2002; 10: 417-426.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 8
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T, Yu JW, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009; 458: 509-513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 10
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • Burckstummer T, Baumann C, Blüml S, Dixit E, Dürnberger G, Jahn H et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol 2009; 10: 266-272.
    • (2009) Nat Immunol , vol.10 , pp. 266-272
    • Burckstummer, T.1    Baumann, C.2    Blüml, S.3    Dixit, E.4    Dürnberger, G.5    Jahn, H.6
  • 11
    • 84858796861 scopus 로고    scopus 로고
    • An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages
    • Khare S, Dorfleutner A, Bryan NB, Yun C, Radian AD, de Almeida L et al. An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages. Immunity 2012; 36: 464-476.
    • (2012) Immunity , vol.36 , pp. 464-476
    • Khare, S.1    Dorfleutner, A.2    Bryan, N.B.3    Yun, C.4    Radian, A.D.5    De Almeida, L.6
  • 12
    • 84901310586 scopus 로고    scopus 로고
    • Mechanisms and functions of inflammasomes
    • Lamkanfi M, Dixit VM. Mechanisms and functions of inflammasomes. Cell 2014; 157: 1013-1022.
    • (2014) Cell , vol.157 , pp. 1013-1022
    • Lamkanfi, M.1    Dixit, V.M.2
  • 13
    • 34548031870 scopus 로고    scopus 로고
    • The pyroptosome: A supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
    • Fernandes-Alnemri T, Wu J, Yu JW, Datta P, Miller B, Jankowski W et al. The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ 2007; 14: 1590-1604.
    • (2007) Cell Death Differ , vol.14 , pp. 1590-1604
    • Fernandes-Alnemri, T.1    Wu, J.2    Yu, J.W.3    Datta, P.4    Miller, B.5    Jankowski, W.6
  • 14
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell 2014; 156: 1193-1206.
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1    Magupalli, V.G.2    Ruan, J.3    Yin, Q.4    Atianand, M.K.5    Vos, M.R.6
  • 15
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello CA. Biologic basis for interleukin-1 in disease. Blood 1996; 87: 2095-2147.
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 16
    • 0028898380 scopus 로고
    • Persistent elevation of inflammatory cytokines predicts a poor outcome in ARDS. Plasma IL-1 beta and IL-6 levels are consistent and efficient predictors of outcome over time
    • Meduri GU, Headley S, Kohler G, Stentz F, Tolley E, Umberger R et al. Persistent elevation of inflammatory cytokines predicts a poor outcome in ARDS. Plasma IL-1 beta and IL-6 levels are consistent and efficient predictors of outcome over time. Chest 1995; 107: 1062-1073.
    • (1995) Chest , vol.107 , pp. 1062-1073
    • Meduri, G.U.1    Headley, S.2    Kohler, G.3    Stentz, F.4    Tolley, E.5    Umberger, R.6
  • 17
  • 18
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • Ciechanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 2005; 6: 79-87.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 19
    • 84931031608 scopus 로고    scopus 로고
    • Roles of linear ubiquitinylation, a crucial regulator of NF-kappaB and cell death, in the immune system
    • Sasaki K, Iwai K. Roles of linear ubiquitinylation, a crucial regulator of NF-kappaB and cell death, in the immune system. Immunol Rev 2015; 266: 175-189.
    • (2015) Immunol Rev , vol.266 , pp. 175-189
    • Sasaki, K.1    Iwai, K.2
  • 20
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002; 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 21
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 2009; 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 22
    • 84883512048 scopus 로고    scopus 로고
    • The emerging role of the ubiquitin proteasome in pulmonary biology and disease
    • Weathington NM, Sznajder JI, Mallampalli RK. The emerging role of the ubiquitin proteasome in pulmonary biology and disease. Am J Respir Crit Care Med 2013; 188: 530-537.
    • (2013) Am J Respir Crit Care Med , vol.188 , pp. 530-537
    • Weathington, N.M.1    Sznajder, J.I.2    Mallampalli, R.K.3
  • 23
    • 84876667044 scopus 로고    scopus 로고
    • A combinatorial F box protein directed pathway controls TRAF adaptor stability to regulate inflammation
    • Chen BB, Coon TA, Glasser JR, McVerry BJ, Zhao J, Zhao Y et al. A combinatorial F box protein directed pathway controls TRAF adaptor stability to regulate inflammation. Nat Immunol 2013; 14: 470-479.
    • (2013) Nat Immunol , vol.14 , pp. 470-479
    • Chen, B.B.1    Coon, T.A.2    Glasser, J.R.3    McVerry, B.J.4    Zhao, J.5    Zhao, Y.6
  • 24
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-kappaB: Players, pathways, perspectives
    • Gilmore TD. Introduction to NF-kappaB: players, pathways, perspectives. Oncogene 2006; 25: 6680-6684.
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 25
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IkappaBalpha/NF-kappaB complex
    • Jacobs MD, Harrison SC. Structure of an IkappaBalpha/NF-kappaB complex. Cell 1998; 95: 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 26
    • 0034745011 scopus 로고    scopus 로고
    • Control of IkappaBalpha proteolysis by the ubiquitin-proteasome pathway
    • Tanaka K, Kawakami T, Tateishi K, Yashiroda H, Chiba T. Control of IkappaBalpha proteolysis by the ubiquitin-proteasome pathway. Biochimie 2001; 83: 351-356.
    • (2001) Biochimie , vol.83 , pp. 351-356
    • Tanaka, K.1    Kawakami, T.2    Tateishi, K.3    Yashiroda, H.4    Chiba, T.5
  • 27
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell 2006; 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 28
    • 69549119940 scopus 로고    scopus 로고
    • Molecular mechanisms involved in inflamma-some activation
    • Bryant C, Fitzgerald KA. Molecular mechanisms involved in inflamma-some activation. Trends Cell Biol 2009; 19: 455-464.
    • (2009) Trends Cell Biol , vol.19 , pp. 455-464
    • Bryant, C.1    Fitzgerald, K.A.2
  • 29
    • 84907210913 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase tripartite motif 33 is essential for cytosolic RNA-induced NLRP3 inflammasome activation
    • Weng L, Mitoma H, Trichot C, Bao M, Liu Y, Zhang Z et al. The E3 ubiquitin ligase tripartite motif 33 is essential for cytosolic RNA-induced NLRP3 inflammasome activation. J Immunol 2014; 193: 3676-3682.
    • (2014) J Immunol , vol.193 , pp. 3676-3682
    • Weng, L.1    Mitoma, H.2    Trichot, C.3    Bao, M.4    Liu, Y.5    Zhang, Z.6
  • 30
    • 64049084303 scopus 로고    scopus 로고
    • Differential requirement for the activation of the inflammasome for processing and release of IL-1beta in monocytes and macrophages
    • Netea MG, Nold-Petry CA, Nold MF, Joosten LA, Opitz B, van der Meer JH et al. Differential requirement for the activation of the inflammasome for processing and release of IL-1beta in monocytes and macrophages. Blood 2009; 113: 2324-2335.
    • (2009) Blood , vol.113 , pp. 2324-2335
    • Netea, M.G.1    Nold-Petry, C.A.2    Nold, M.F.3    Joosten, L.A.4    Opitz, B.5    Van Der Meer, J.H.6
  • 31
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression
    • Bauernfeind FG, Horvath G, Stutz A, Alnemri ES, MacDonald K, Speert D et al. Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol 2009; 183: 787-791.
    • (2009) J Immunol , vol.183 , pp. 787-791
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3    Alnemri, E.S.4    MacDonald, K.5    Speert, D.6
  • 32
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem 2012; 287: 36617-36622.
    • (2012) J Biol Chem , vol.287 , pp. 36617-36622
    • Juliana, C.1    Fernandes-Alnemri, T.2    Kang, S.3    Farias, A.4    Qin, F.5    Alnemri, E.S.6
  • 34
    • 84898635026 scopus 로고    scopus 로고
    • Inflammasome priming by lipopolysaccharide is dependent upon ERK signaling and proteasome function
    • Ghonime MG, Shamaa OR, Das S, Eldomany RA, Fernandes-Alnemri T, Alnemri ES et al. Inflammasome priming by lipopolysaccharide is dependent upon ERK signaling and proteasome function. J Immunol 2014; 192: 3881-3888.
    • (2014) J Immunol , vol.192 , pp. 3881-3888
    • Ghonime, M.G.1    Shamaa, O.R.2    Das, S.3    Eldomany, R.A.4    Fernandes-Alnemri, T.5    Alnemri, E.S.6
  • 35
    • 84869088114 scopus 로고    scopus 로고
    • Acute lipopolysaccharide priming boosts inflamma-some activation independently of inflammasome sensor induction
    • Schroder K, Sagulenko V, Zamoshnikova A, Richards AA, Cridland JA, Irvine KM et al. Acute lipopolysaccharide priming boosts inflamma-some activation independently of inflammasome sensor induction. Immunobiology 2012; 217: 1325-1329.
    • (2012) Immunobiology , vol.217 , pp. 1325-1329
    • Schroder, K.1    Sagulenko, V.2    Zamoshnikova, A.3    Richards, A.A.4    Cridland, J.A.5    Irvine, K.M.6
  • 36
    • 84921305910 scopus 로고    scopus 로고
    • A20 restricts ubiquitination of pro-interleukin-1beta protein complexes and suppresses NLRP3 inflammasome activity
    • Duong BH, Onizawa M, Oses-Prieto JA, Advincula R, Burlingame A, Malynn BA et al. A20 restricts ubiquitination of pro-interleukin-1beta protein complexes and suppresses NLRP3 inflammasome activity. Immunity 2015; 42: 55-67.
    • (2015) Immunity , vol.42 , pp. 55-67
    • Duong, B.H.1    Onizawa, M.2    Oses-Prieto, J.A.3    Advincula, R.4    Burlingame, A.5    Malynn, B.A.6
  • 37
    • 46949096956 scopus 로고    scopus 로고
    • MG132 proteasome inhibitor modulates proinflammatory cytokines production and expression of their receptors in U937 cells: Involvement of nuclear factor-kappaB and activator protein-1
    • Ortiz-Lazareno PC, Hernandez-Flores G, Dominguez-Rodriguez JR, Lerma-Diaz JM, Jave-Suarez LF, Aguilar-Lemarroy A et al. MG132 proteasome inhibitor modulates proinflammatory cytokines production and expression of their receptors in U937 cells: involvement of nuclear factor-kappaB and activator protein-1. Immunology 2008; 124: 534-541.
    • (2008) Immunology , vol.124 , pp. 534-541
    • Ortiz-Lazareno, P.C.1    Hernandez-Flores, G.2    Dominguez-Rodriguez, J.R.3    Lerma-Diaz, J.M.4    Jave-Suarez, L.F.5    Aguilar-Lemarroy, A.6
  • 38
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py BF, Kim MS, Vakifahmetoglu-Norberg H, Yuan J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol Cell 2013; 49: 331-338.
    • (2013) Mol Cell , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 39
    • 84873834109 scopus 로고    scopus 로고
    • Deubiquitinases regulate the activity of caspase-1 and interleukin-1beta secretion via assembly of the inflammasome
    • Lopez-Castejon G, Luheshi NM, Compan V, High S, Whitehead RC, Flitsch S et al. Deubiquitinases regulate the activity of caspase-1 and interleukin-1beta secretion via assembly of the inflammasome. J Biol Chem 2013; 288: 2721-2733.
    • (2013) J Biol Chem , vol.288 , pp. 2721-2733
    • Lopez-Castejon, G.1    Luheshi, N.M.2    Compan, V.3    High, S.4    Whitehead, R.C.5    Flitsch, S.6
  • 40
    • 84937468257 scopus 로고    scopus 로고
    • Lipopolysaccharide primes the NALP3 inflammasome by inhibiting its ubiquitination and degradation mediated by the SCFFBXL2 E3 ligase
    • Han S, Lear TB, Jerome JA, Rajbhandari S, Snavely CA, Gulick DL et al. Lipopolysaccharide primes the NALP3 inflammasome by inhibiting its ubiquitination and degradation mediated by the SCFFBXL2 E3 ligase. J Biol Chem 2015; 290: 18124-18133.
    • (2015) J Biol Chem , vol.290 , pp. 18124-18133
    • Han, S.1    Lear, T.B.2    Jerome, J.A.3    Rajbhandari, S.4    Snavely, C.A.5    Gulick, D.L.6
  • 41
    • 84920990887 scopus 로고    scopus 로고
    • Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome
    • Yan Y, Jiang W, Liu L, Wang X, Ding C, Tian Z et al. Dopamine controls systemic inflammation through inhibition of NLRP3 inflammasome. Cell 2015; 160: 62-73.
    • (2015) Cell , vol.160 , pp. 62-73
    • Yan, Y.1    Jiang, W.2    Liu, L.3    Wang, X.4    Ding, C.5    Tian, Z.6
  • 42
    • 84943523865 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli uses NleA to inhibit NLRP3 inflammasome activation
    • Yen H, Sugimoto N, Tobe T. Enteropathogenic Escherichia coli uses NleA to inhibit NLRP3 inflammasome activation. PLoS Pathog 2015; 11: e1005121.
    • (2015) PLoS Pathog , vol.11 , pp. e1005121
    • Yen, H.1    Sugimoto, N.2    Tobe, T.3
  • 43
    • 84949648407 scopus 로고    scopus 로고
    • A20 overexpression alleviates pristine-induced lupus nephritis by inhibiting the NF-kappaB and NLRP3 inflammasome activation in macrophages of mice
    • Li M, Shi X, Qian T, Li J, Tian Z, Ni B et al. A20 overexpression alleviates pristine-induced lupus nephritis by inhibiting the NF-kappaB and NLRP3 inflammasome activation in macrophages of mice. Int J Clin Exp Med 2015; 8: 17430-17440.
    • (2015) Int J Clin Exp Med , vol.8 , pp. 17430-17440
    • Li, M.1    Shi, X.2    Qian, T.3    Li, J.4    Tian, Z.5    Ni, B.6
  • 45
    • 84908424472 scopus 로고    scopus 로고
    • Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages
    • Suzuki S, Mimuro H, Kim M, Ogawa M, Ashida H, Toyotome T et al. Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages. Proc Natl Acad Sci USA 2014; 111: E4254-E4263.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. E4254-E4263
    • Suzuki, S.1    Mimuro, H.2    Kim, M.3    Ogawa, M.4    Ashida, H.5    Toyotome, T.6
  • 46
    • 77950887181 scopus 로고    scopus 로고
    • Interaction with Sug1 enables Ipaf ubiquitination leading to caspase 8 activation and cell death
    • Kumar Y, Radha V, Swarup G. Interaction with Sug1 enables Ipaf ubiquitination leading to caspase 8 activation and cell death. Biochem J 2010; 427: 91-104.
    • (2010) Biochem J , vol.427 , pp. 91-104
    • Kumar, Y.1    Radha, V.2    Swarup, G.3
  • 47
    • 65649124933 scopus 로고    scopus 로고
    • [Involvement of LUBAC-mediated linear polyubiquitination of NEMO in NF-kappaB activation]
    • Tokunaga F, Iwai K. [Involvement of LUBAC-mediated linear polyubiquitination of NEMO in NF-kappaB activation]. Tanpakushitsu Kakusan Koso 2009; 54: 635-642.
    • (2009) Tanpakushitsu Kakusan Koso , vol.54 , pp. 635-642
    • Tokunaga, F.1    Iwai, K.2
  • 48
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex
    • Tokunaga F, Nakagawa T, Nakahara M, Saeki Y, Taniguchi M, Sakata S et al. SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex. Nature 2011; 471: 633-636.
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1    Nakagawa, T.2    Nakahara, M.3    Saeki, Y.4    Taniguchi, M.5    Sakata, S.6
  • 49
    • 84903761551 scopus 로고    scopus 로고
    • The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation
    • Rodgers MA, Bowman JW, Fujita H, Orazio N, Shi M, Liang Q et al. The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation. J Exp Med 2014; 211: 1333-1347.
    • (2014) J Exp Med , vol.211 , pp. 1333-1347
    • Rodgers, M.A.1    Bowman, J.W.2    Fujita, H.3    Orazio, N.4    Shi, M.5    Liang, Q.6
  • 50
    • 84924358739 scopus 로고    scopus 로고
    • Cutting edge: SHARPIN is required for optimal NLRP3 inflammasome activation
    • Gurung P, Lamkanfi M, Kanneganti TD. Cutting edge: SHARPIN is required for optimal NLRP3 inflammasome activation. J Immunol 2015; 194: 2064-2067.
    • (2015) J Immunol , vol.194 , pp. 2064-2067
    • Gurung, P.1    Lamkanfi, M.2    Kanneganti, T.D.3
  • 51
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction
    • Shi CS, Shenderov K, Huang NN, Kabat J, Abu-Asab M, Fitzgerald KA et al. Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol 2012; 13: 255-263.
    • (2012) Nat Immunol , vol.13 , pp. 255-263
    • Shi, C.S.1    Shenderov, K.2    Huang, N.N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6
  • 52
    • 84929119017 scopus 로고    scopus 로고
    • MAVS promotes inflammasome activation by targeting ASC for K63-linked ubiquitina-tion via the E3 ligase TRAF3
    • Guan K, Wei C, Zheng Z, Song T, Wu F, Zhang Y et al. MAVS promotes inflammasome activation by targeting ASC for K63-linked ubiquitina-tion via the E3 ligase TRAF3. J Immunol 2015; 194: 4880-4890.
    • (2015) J Immunol , vol.194 , pp. 4880-4890
    • Guan, K.1    Wei, C.2    Zheng, Z.3    Song, T.4    Wu, F.5    Zhang, Y.6
  • 54
    • 84883368914 scopus 로고    scopus 로고
    • Post-translational control of IL-1beta via the human papilloma-virus type 16 E6 oncoprotein: A novel mechanism of innate immune escape mediated by the E3-ubiquitin ligase E6-AP and p53
    • Niebler M, Qian X, Höfler D, Kogosov V, Kaewprag J, Kaufmann AM et al. Post-translational control of IL-1beta via the human papilloma-virus type 16 E6 oncoprotein: a novel mechanism of innate immune escape mediated by the E3-ubiquitin ligase E6-AP and p53. PLoS Pathog 2013; 9: e1003536.
    • (2013) PLoS Pathog , vol.9 , pp. e1003536
    • Niebler, M.1    Qian, X.2    Höfler, D.3    Kogosov, V.4    Kaewprag, J.5    Kaufmann, A.M.6
  • 55
    • 84936891896 scopus 로고    scopus 로고
    • Inflammasomes: Mechanism of action, role in disease, and therapeutics
    • Guo H, Callaway JB, Ting JP. Inflammasomes: mechanism of action, role in disease, and therapeutics. Nat Med 2015; 21: 677-687.
    • (2015) Nat Med , vol.21 , pp. 677-687
    • Guo, H.1    Callaway, J.B.2    Ting, J.P.3
  • 57
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1beta in type 2 diabetes
    • Masters SL, Dunne A, Subramanian SL, Hull RL, Tannahill GM, Sharp FA et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1beta in type 2 diabetes. Nat Immunol 2010; 11: 897-904.
    • (2010) Nat Immunol , vol.11 , pp. 897-904
    • Masters, S.L.1    Dunne, A.2    Subramanian, S.L.3    Hull, R.L.4    Tannahill, G.M.5    Sharp, F.A.6
  • 58
    • 84911948494 scopus 로고    scopus 로고
    • Nucleoside reverse transcriptase inhibitors possess intrinsic anti-inflammatory activity
    • Fowler BJ, Gelfand BD, Kim Y, Kerur N, Tarallo V, Hirano Y et al. Nucleoside reverse transcriptase inhibitors possess intrinsic anti-inflammatory activity. Science 2014; 346: 1000-1003.
    • (2014) Science , vol.346 , pp. 1000-1003
    • Fowler, B.J.1    Gelfand, B.D.2    Kim, Y.3    Kerur, N.4    Tarallo, V.5    Hirano, Y.6
  • 59
    • 77951240589 scopus 로고    scopus 로고
    • Anti-inflammatory compounds parthenolide and Bay 11-7082 are direct inhibitors of the inflammasome
    • Juliana C, Fernandes-Alnemri T, Wu J, Datta P, Solorzano L, Yu JW et al. Anti-inflammatory compounds parthenolide and Bay 11-7082 are direct inhibitors of the inflammasome. J Biol Chem 2010; 285: 9792-9802.
    • (2010) J Biol Chem , vol.285 , pp. 9792-9802
    • Juliana, C.1    Fernandes-Alnemri, T.2    Wu, J.3    Datta, P.4    Solorzano, L.5    Yu, J.W.6
  • 60
    • 84924356420 scopus 로고    scopus 로고
    • The ketone metabolite beta-hydroxybutyrate blocks NLRP3 inflammasome-mediated inflammatory disease
    • Youm YH, Nguyen KY, Grant RW, Goldberg EL, Bodogai M, Kim D et al. The ketone metabolite beta-hydroxybutyrate blocks NLRP3 inflammasome-mediated inflammatory disease. Nat Med 2015; 21: 263-269.
    • (2015) Nat Med , vol.21 , pp. 263-269
    • Youm, Y.H.1    Nguyen, K.Y.2    Grant, R.W.3    Goldberg, E.L.4    Bodogai, M.5    Kim, D.6
  • 61
    • 79951740151 scopus 로고    scopus 로고
    • Type i interferon inhibits interleukin-1 production and inflammasome activation
    • Guarda G, Braun M, Staehli F, Tardivel A, Mattmann C, Förster I et al. Type I interferon inhibits interleukin-1 production and inflammasome activation. Immunity 2011; 34: 213-223.
    • (2011) Immunity , vol.34 , pp. 213-223
    • Guarda, G.1    Braun, M.2    Staehli, F.3    Tardivel, A.4    Mattmann, C.5    Förster, I.6
  • 62
    • 84924415042 scopus 로고    scopus 로고
    • A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases
    • Coll RC, Robertson AA, Chae JJ, Higgins SC, Muñoz-Planillo R, Inserra MC et al. A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases. Nat Med 2015; 21: 248-255.
    • (2015) Nat Med , vol.21 , pp. 248-255
    • Coll, R.C.1    Robertson, A.A.2    Chae, J.J.3    Higgins, S.C.4    Muñoz-Planillo, R.5    Inserra, M.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.