메뉴 건너뛰기




Volumn 117, Issue 3, 2011, Pages 960-970

Tumor suppressor death-associated protein kinase is required for full IL-1β production

Author keywords

[No Author keywords available]

Indexed keywords

DEATH ASSOCIATED PROTEIN KINASE; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; TUMOR NECROSIS FACTOR ALPHA; URIC ACID;

EID: 78751700420     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-08-303115     Document Type: Article
Times cited : (60)

References (50)
  • 1
    • 77950355734 scopus 로고    scopus 로고
    • Anti-inflammatory agents: Present and future
    • Dinarello CA. Anti-inflammatory agents: present and future. Cell. 2010;140(6):935-950.
    • (2010) Cell. , vol.140 , Issue.6 , pp. 935-950
    • Dinarello, C.A.1
  • 2
    • 58049202273 scopus 로고    scopus 로고
    • Inflammasomes: Guardians of cytosolic sanctity
    • Lamkanfi M, Dixit VM. Inflammasomes: guardians of cytosolic sanctity. Immunol Rev. 2009;227:95-105.
    • (2009) Immunol Rev. , vol.227 , pp. 95-105
    • Lamkanfi, M.1    Dixit, V.M.2
  • 3
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: A caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • Franchi L, Eigenbrod T, Muñoz-Planillo R, Nuñez G. The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nat Immunol. 2009;10(3):241-247.
    • (2009) Nat Immunol. , vol.10 , Issue.3 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Muñoz-Planillo, R.3    Nuñez, G.4
  • 4
    • 69549119940 scopus 로고    scopus 로고
    • Molecular mechanisms involved in inflammasome activation
    • Bryant C, Fitzgerald KA. Molecular mechanisms involved in inflammasome activation. Trends Cell Biol. 2009;19:455-464.
    • (2009) Trends Cell Biol. , vol.19 , pp. 455-464
    • Bryant, C.1    Fitzgerald, K.A.2
  • 5
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K, Tschopp J. The inflammasomes. Cell. 2010;140(6):821-832.
    • (2010) Cell. , vol.140 , Issue.6 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 6
    • 77249118801 scopus 로고    scopus 로고
    • The inflammasomes: Mechanisms of activation and function
    • Latz E. The inflammasomes: mechanisms of activation and function. Curr Opin Immunol. 2010;22(1):28-33.
    • (2010) Curr Opin Immunol. , vol.22 , Issue.1 , pp. 28-33
    • Latz, E.1
  • 9
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NLRP3 inflammasome
    • Martinon F, Petrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NLRP3 inflammasome. Nature. 2006;440(7081):237- 241.
    • (2006) Nature , vol.440 , Issue.7081 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 10
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • Dostert C, Petrilli V, van Bruggen R, Steele C, Mossman BT, Tschopp J. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science. 2008;320(5876):674-677.
    • (2008) Science , vol.320 , Issue.5876 , pp. 674-677
    • Dostert, C.1    Petrilli, V.2    Van Bruggen, R.3    Steele, C.4    Mossman, B.T.5    Tschopp, J.6
  • 11
    • 45749111446 scopus 로고    scopus 로고
    • Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
    • Eisenbarth SC, Colegio OR, O'Connor W, Sutterwala FS, Flavell RA. Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants. Nature. 2008;453(7198):1122-1126.
    • (2008) Nature , vol.453 , Issue.7198 , pp. 1122-1126
    • Eisenbarth, S.C.1    Colegio, O.R.2    O'Connor, W.3    Sutterwala, F.S.4    Flavell, R.A.5
  • 12
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • Hornung V, Bauernfeind F, Halle A, et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol. 2008;9(8):847-856.
    • (2008) Nat Immunol. , vol.9 , Issue.8 , pp. 847-856
    • Hornung, V.1    Bauernfeind, F.2    Halle, A.3
  • 13
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen IC, Scull MA, Moore CB, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity. 2009;30(4):556-565.
    • (2009) Immunity , vol.30 , Issue.4 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3
  • 14
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • Halle A, Hornung V, Petzold GC, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 2008;9(8):857-865.
    • (2008) Nat Immunol. , vol.9 , Issue.8 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3
  • 15
    • 77950363011 scopus 로고    scopus 로고
    • Autoinflammatory disease reloaded: A clinical perspective
    • Kastner DL, Aksentijevich I, Goldbach-Mansky R. Autoinflammatory disease reloaded: a clinical perspective. Cell. 2010;140(6):784-790.
    • (2010) Cell. , vol.140 , Issue.6 , pp. 784-790
    • Kastner, D.L.1    Aksentijevich, I.2    Goldbach-Mansky, R.3
  • 16
    • 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, et al. Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol. 2009;183(2):787-791.
    • (2009) J Immunol. , vol.183 , Issue.2 , pp. 787-791
    • Bauernfeind, F.G.1    Horvath, G.2    Stutz, A.3
  • 17
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • Zhou R, Tardivel A, Thorens B, Choi I, Tschopp J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat Immunol. 2010;11(2):136-140.
    • (2010) Nat Immunol. , vol.11 , Issue.2 , pp. 136-140
    • Zhou, R.1    Tardivel, A.2    Thorens, B.3    Choi, I.4    Tschopp, J.5
  • 18
    • 33847376042 scopus 로고    scopus 로고
    • Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation
    • Faustin B, Lartigue L, Bruey JM, et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell. 25(5):713-724.
    • Mol Cell. , vol.25 , Issue.5 , pp. 713-724
    • Faustin, B.1    Lartigue, L.2    Bruey, J.M.3
  • 19
    • 0036671894 scopus 로고    scopus 로고
    • The Inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • DOI 10.1016/S1097-2765(02)00599-3
    • Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-1beta. Mol Cell. 2002;10(2):417-426. (Pubitemid 35007355)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 20
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function, and beyond
    • Bialik S, Kimchi A. The death-associated protein kinases: structure, function, and beyond. Annu Rev Biochem. 2006;75:189-210.
    • (2006) Annu Rev Biochem. , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 21
    • 73649118820 scopus 로고    scopus 로고
    • Death-associated protein kinase (DAPK) and signal transduction: Regulation in cancer
    • Michie AM, McCaig AM, Nakagawa R, Vukovic M. Death-associated protein kinase (DAPK) and signal transduction: regulation in cancer. FEBS J. 2010;277(1):74-80.
    • (2010) FEBS J. , vol.277 , Issue.1 , pp. 74-80
    • Michie, A.M.1    McCaig, A.M.2    Nakagawa, R.3    Vukovic, M.4
  • 22
    • 0030757685 scopus 로고    scopus 로고
    • DAP-kinase loss of expression in various carcinoma and B-cell lymphoma cell lines: Possible implications for role as tumor suppressor gene
    • Kissil JL, Feinstein E, Cohen O, et al. DAP-kinase loss of expression in various carcinoma and B-cell lymphoma cell lines: possible implications for role as tumor suppressor gene. Oncogene. 1997;15(4):403-407. (Pubitemid 27370989)
    • (1997) Oncogene , vol.15 , Issue.4 , pp. 403-407
    • Kissil, J.L.1    Feinstein, E.2    Cohen, O.3    Jones, P.A.4    Tsai, Y.C.5    Knowles, M.A.6    Eydmann, M.E.7    Kimchi, A.8
  • 23
    • 0033564351 scopus 로고    scopus 로고
    • Hypermethylation of the DAP-kinase CpG island is a common alteration in B-cell malignancies
    • Katzenellenbogen RA, Baylin SB, Herman JG. Hypermethylation of the DAP-kinase CpG island is a common alteration in B-cell malignancies. Blood. 1999;93(12):4347-4353.
    • (1999) Blood , vol.93 , Issue.12 , pp. 4347-4353
    • Katzenellenbogen, R.A.1    Baylin, S.B.2    Herman, J.G.3
  • 24
    • 34249314024 scopus 로고    scopus 로고
    • Downregulation of death-associated protein kinase 1 (DAPK1) in chronic lymphocytic leukemia
    • Raval A, Tanner SM, Byrd JC, et al. Downregulation of death-associated protein kinase 1 (DAPK1) in chronic lymphocytic leukemia. Cell. 2007;129(5):879-890.
    • (2007) Cell. , vol.129 , Issue.5 , pp. 879-890
    • Raval, A.1    Tanner, S.M.2    Byrd, J.C.3
  • 25
    • 74549173438 scopus 로고    scopus 로고
    • DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke
    • Tu W, Xu X, Peng L, et al. DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke. Cell. 2010;140(2):222-234.
    • (2010) Cell. , vol.140 , Issue.2 , pp. 222-234
    • Tu, W.1    Xu, X.2    Peng, L.3
  • 26
    • 13444311622 scopus 로고    scopus 로고
    • Bidirectional signals transduced by DAPK ERK interaction promote the apoptotic effect of DAPK
    • Chen CH, Wang WJ, Kuo JC, et al. Bidirectional signals transduced by DAPK ERK interaction promote the apoptotic effect of DAPK. EMBO J. 2005;24(2):294-304.
    • (2005) EMBO J. , vol.24 , Issue.2 , pp. 294-304
    • Chen, C.H.1    Wang, W.J.2    Kuo, J.C.3
  • 27
    • 26244449244 scopus 로고    scopus 로고
    • The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling
    • DOI 10.1016/j.cub.2005.08.050, PII S0960982205009693
    • Anjum R, Roux PP, Ballif BA, Gygi SP, Blenis J. The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling. Curr Biol. 2005;15(19):1762-1767. (Pubitemid 41415634)
    • (2005) Current Biology , vol.15 , Issue.19 , pp. 1762-1767
    • Anjum, R.1    Roux, P.P.2    Ballif, B.A.3    Gygi, S.P.4    Blenis, J.5
  • 28
    • 34548249520 scopus 로고    scopus 로고
    • The tumor suppressor DAPK is reciprocally regulated by tyrosine kinase Src and phosphatase LAR
    • Wang WJ, Juo JC, Ku W, et al. The tumor suppressor DAPK is reciprocally regulated by tyrosine kinase Src and phosphatase LAR. Mol Cell. 2007;27(5):701-716.
    • (2007) Mol Cell. , vol.27 , Issue.5 , pp. 701-716
    • Wang, W.J.1    Juo, J.C.2    Ku, W.3
  • 29
    • 73649097539 scopus 로고    scopus 로고
    • Death-associated protein kinase (DAPK) and signal transduction: Additional roles beyond cell death
    • Lin Y, Hupp TR, Stevens C. Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death. FEBS J. 2010;277(1):48-57.
    • (2010) FEBS J. , vol.277 , Issue.1 , pp. 48-57
    • Lin, Y.1    Hupp, T.R.2    Stevens, C.3
  • 30
    • 49149091747 scopus 로고    scopus 로고
    • The tumor suppressor death associated protein kinase targets to TCR-stimulated NF-kappaB activation
    • Chuang YT, Fang LW, Lin-Feng MH, Chen RH, Lai MZ. The tumor suppressor death associated protein kinase targets to TCR-stimulated NF-kappaB activation. J Immunol. 2008;180(5):3238-3249.
    • (2008) J Immunol. , vol.180 , Issue.5 , pp. 3238-3249
    • Chuang, Y.T.1    Fang, L.W.2    Lin-Feng, M.H.3    Chen, R.H.4    Lai, M.Z.5
  • 31
    • 55049140658 scopus 로고    scopus 로고
    • DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression
    • Mukhopadhyay R, Ray PS, Arif A, Brady AK, Kinter M, Fox PL. DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression. Mol Cell. 2008;32(3):371-382.
    • (2008) Mol Cell. , vol.32 , Issue.3 , pp. 371-382
    • Mukhopadhyay, R.1    Ray, P.S.2    Arif, A.3    Brady, A.K.4    Kinter, M.5    Fox, P.L.6
  • 32
    • 34548434775 scopus 로고    scopus 로고
    • Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages
    • Suzuki T, Franchi L, Toma C, et al. Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages. PLoS Pathog. 2007;3(8):e111.
    • (2007) PLoS Pathog. , vol.3 , Issue.8
    • Suzuki, T.1    Franchi, L.2    Toma, C.3
  • 33
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • Saitoh T, Fujita N, Jang MH, et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature. 2008;456(7219):264-268.
    • (2008) Nature , vol.456 , Issue.7219 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3
  • 34
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • DOI 10.1083/jcb.200109094
    • Inbal B, Bialik S, Sabanay I, Shani G, Kimchi A. DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J Cell Biol. 2002;157(3):455-468. (Pubitemid 34839809)
    • (2002) Journal of Cell Biology , vol.157 , Issue.3 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 35
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • Zalckvar E, Berissi H, Mizrachy L, et al. DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep. 2009;10(3):285-292.
    • (2009) EMBO Rep. , vol.10 , Issue.3 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3
  • 36
    • 33751252292 scopus 로고    scopus 로고
    • Direct observation of individual endogenous protein complexes in situ by proximity ligation
    • Söderberg O, Gullberg M, Jarvius M, et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat Methods. 2006;3(12):995-1000.
    • (2006) Nat Methods , vol.3 , Issue.12 , pp. 995-1000
    • Söderberg, O.1    Gullberg, M.2    Jarvius, M.3
  • 37
    • 56349138968 scopus 로고    scopus 로고
    • DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase activation and autophagic cell death
    • Gozuacik D, Bialik S, Raveh T, et al. DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase activation and autophagic cell death. Cell Death Differ. 2008;15(12):1875-1886.
    • (2008) Cell Death Differ. , vol.15 , Issue.12 , pp. 1875-1886
    • Gozuacik, D.1    Bialik, S.2    Raveh, T.3
  • 38
    • 7944232105 scopus 로고    scopus 로고
    • Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome
    • Martinon F, Agostini L, Meylan E, Tschopp J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr Biol. 2004;14(21):1929-1934.
    • (2004) Curr Biol. , vol.14 , Issue.21 , pp. 1929-1934
    • Martinon, F.1    Agostini, L.2    Meylan, E.3    Tschopp, J.4
  • 39
    • 33750991341 scopus 로고    scopus 로고
    • Death-associated protein kinase phosphorylates mammalian ribosomal protein S6 and reduces protein synthesis
    • DOI 10.1021/bi060413y
    • Schumacher AM, Velentza AV, Watterson DM, Dresios J. Death-associated protein kinase phosphorylates mammalian ribosomal protein S6 and reduces protein synthesis. Biochemistry. 2006;45(45):13614-13621. (Pubitemid 44748507)
    • (2006) Biochemistry , vol.45 , Issue.45 , pp. 13614-13621
    • Schumacher, A.M.1    Velentza, A.V.2    Watterson, D.M.3    Dresios, J.4
  • 40
    • 34347242470 scopus 로고    scopus 로고
    • RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation
    • Roux PP, Shahbazian D, Vu H, et al. RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation. J Biol Chem. 2007;282(19):14056-14064.
    • (2007) J Biol Chem. , vol.282 , Issue.19 , pp. 14056-14064
    • Roux, P.P.1    Shahbazian, D.2    Vu, H.3
  • 41
    • 46749156737 scopus 로고    scopus 로고
    • A high throughput proteomics screen identifies novel substrates of death-associated protein kinase
    • Bialik S, Berissi H, Kimchi A. A high throughput proteomics screen identifies novel substrates of death-associated protein kinase. Mol Cell Proteomics. 2008;7(6):1089-1098.
    • (2008) Mol Cell Proteomics , vol.7 , Issue.6 , pp. 1089-1098
    • Bialik, S.1    Berissi, H.2    Kimchi, A.3
  • 42
    • 33749576792 scopus 로고    scopus 로고
    • Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages
    • Fink SL, Cookson BT. Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages. Cell Microbiol. 2006;8(11):1812-1825.
    • (2006) Cell Microbiol. , vol.8 , Issue.11 , pp. 1812-1825
    • Fink, S.L.1    Cookson, B.T.2
  • 43
  • 45
    • 14844337826 scopus 로고    scopus 로고
    • dapk1, encoding an activator of a p19ARF-p53-mediated apoptotic checkpoint, is a transcription target of p53
    • Martoriati A, Doumont G, Alcalay M, Bellefroid E, Pelicci PG, Marine JC. dapk1, encoding an activator of a p19ARF-p53-mediated apoptotic checkpoint, is a transcription target of p53. Oncogene. 2005;24(8):1461-1466.
    • (2005) Oncogene , vol.24 , Issue.8 , pp. 1461-1466
    • Martoriati, A.1    Doumont, G.2    Alcalay, M.3    Bellefroid, E.4    Pelicci, P.G.5    Marine, J.C.6
  • 46
    • 34247636044 scopus 로고    scopus 로고
    • The MDM2 ubiquitination signal in the DNA-binding domain of p53 forms a docking site for calcium calmodulin kinase superfamily members
    • Craig AL, Chrystal JA, Fraser JA, et al. The MDM2 ubiquitination signal in the DNA-binding domain of p53 forms a docking site for calcium calmodulin kinase superfamily members. Mol Cell Biol. 2007;27(9):3542-3555.
    • (2007) Mol Cell Biol. , vol.27 , Issue.9 , pp. 3542-3555
    • Craig, A.L.1    Chrystal, J.A.2    Fraser, J.A.3
  • 47
    • 29644433255 scopus 로고    scopus 로고
    • Death-associated protein kinase is activated by dephosphorylation in response to cerebral ischemia
    • Shamloo M, Soriano L, Wieloch T, Nikolich K, Urfer R, Oksenberg D. Death-associated protein kinase is activated by dephosphorylation in response to cerebral ischemia. J Biol Chem. 2005;280(51):42290-42299.
    • (2005) J Biol Chem. , vol.280 , Issue.51 , pp. 42290-42299
    • Shamloo, M.1    Soriano, L.2    Wieloch, T.3    Nikolich, K.4    Urfer, R.5    Oksenberg, D.6
  • 48
    • 27144458235 scopus 로고    scopus 로고
    • Death-associated protein kinase as a sensor of mitochondrial membrane potential: Role of lysosome in mitochondrial toxin-induced cell death
    • Shang T, Joseph J, Hillard CJ, Kalyanaraman B. Death-associated protein kinase as a sensor of mitochondrial membrane potential: role of lysosome in mitochondrial toxin-induced cell death. J Biol Chem. 2005;280(41):34644-34653.
    • (2005) J Biol Chem. , vol.280 , Issue.41 , pp. 34644-34653
    • Shang, T.1    Joseph, J.2    Hillard, C.J.3    Kalyanaraman, B.4
  • 49
    • 34247265509 scopus 로고    scopus 로고
    • A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses
    • Mayor A, Martinon F, De Smedt T, Pétrilli V, Tschopp J. A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol. 2007;8(5):497-503.
    • (2007) Nat Immunol. , vol.8 , Issue.5 , pp. 497-503
    • Mayor, A.1    Martinon, F.2    De Smedt, T.3    Pétrilli, V.4    Tschopp, J.5
  • 50
    • 77949773101 scopus 로고    scopus 로고
    • Differential innate immune signalling via Ca2+ sensor protein kinases
    • Boudsocq M, Willmann MR, McCormack M, et al. Differential innate immune signalling via Ca2+ sensor protein kinases. Nature. 2010;464(7287):418-422.
    • (2010) Nature , vol.464 , Issue.7287 , pp. 418-422
    • Boudsocq, M.1    Willmann, M.R.2    McCormack, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.