메뉴 건너뛰기




Volumn 33, Issue 21, 2013, Pages 4152-4165

Cross talk between the Akt and p38α pathways in macrophages downstream of toll-like receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPOLYSACCHARIDE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 14; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38 INHIBITOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PROTEIN KINASE B; SERINE; THREONINE; TOLL LIKE RECEPTOR;

EID: 84886876102     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01691-12     Document Type: Article
Times cited : (62)

References (76)
  • 1
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning BD, Cantley LC. 2007. AKT/PKB signaling: navigating downstream. Cell 129:1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 2
    • 0032929762 scopus 로고    scopus 로고
    • Signalling through phosphoinositide 3-kinases: the lipids take centre stage
    • Leevers SJ, Vanhaesebroeck B, Waterfield MD. 1999. Signalling through phosphoinositide 3-kinases: the lipids take centre stage. Curr. Opin. Cell Biol. 11:219-225.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 219-225
    • Leevers, S.J.1    Vanhaesebroeck, B.2    Waterfield, M.D.3
  • 3
    • 54949109808 scopus 로고    scopus 로고
    • PI3K/Akt: getting it right matters
    • Franke TF. 2008. PI3K/Akt: getting it right matters. Oncogene 27:6473-6488.
    • (2008) Oncogene , vol.27 , pp. 6473-6488
    • Franke, T.F.1
  • 4
    • 84857875585 scopus 로고    scopus 로고
    • PI3K signalling in B- and T-lymphocytes: new developments and therapeutic advances
    • So L, Fruman DA. 2012. PI3K signalling in B- and T-lymphocytes: new developments and therapeutic advances. Biochem. J. 442:465-481.
    • (2012) Biochem. J. , vol.442 , pp. 465-481
    • So, L.1    Fruman, D.A.2
  • 5
    • 34548649547 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase in innate immunity
    • Hazeki K, Nigorikawa K, Hazeki O. 2007. Role of phosphoinositide 3-kinase in innate immunity. Biol. Pharm. Bull. 30:1617-1623.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 1617-1623
    • Hazeki, K.1    Nigorikawa, K.2    Hazeki, O.3
  • 7
    • 0037629646 scopus 로고    scopus 로고
    • PI3K and negative regulation of TLR signaling
    • Fukao T, Koyasu S. 2003. PI3K and negative regulation of TLR signaling. Trends Immunol. 24:358-363.
    • (2003) Trends Immunol , vol.24 , pp. 358-363
    • Fukao, T.1    Koyasu, S.2
  • 9
    • 33644506745 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced production of interleukin-10 is promoted by the serine/threonine kinase Akt
    • Pengal RA, Ganesan LP, Wei G, Fang H, Ostrowski MC, Tridandapani S. 2006. Lipopolysaccharide-induced production of interleukin-10 is promoted by the serine/threonine kinase Akt. Mol. Immunol. 43:1557-1564.
    • (2006) Mol. Immunol. , vol.43 , pp. 1557-1564
    • Pengal, R.A.1    Ganesan, L.P.2    Wei, G.3    Fang, H.4    Ostrowski, M.C.5    Tridandapani, S.6
  • 10
    • 0037374815 scopus 로고    scopus 로고
    • The role of PI3K in immune cells
    • Koyasu S. 2003. The role of PI3K in immune cells. Nat. Immunol. 4:313-319.
    • (2003) Nat. Immunol. , vol.4 , pp. 313-319
    • Koyasu, S.1
  • 13
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward J. 1998. Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol. 10:262-267.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 262-267
    • Downward, J.1
  • 14
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation
    • Chan TO, Rittenhouse SE, Tsichlis PN. 1999. AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation. Annu. Rev. Biochem. 68:965-1014.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 15
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • Williams MR, Arthur JS, Balendran A, van der Kaay J, Poli V, Cohen P, Alessi DR. 2000. The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10:439-448.
    • (2000) Curr. Biol. , vol.10 , pp. 439-448
    • Williams, M.R.1    Arthur, J.S.2    Balendran, A.3    van der Kaay, J.4    Poli, V.5    Cohen, P.6    Alessi, D.R.7
  • 19
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad S, Attwell S, Gray V, Mawji N, Deng JT, Leung D, Yan J, Sanghera J, Walsh MP, Dedhar S. 2001. Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J. Biol. Chem. 276:27462-27469.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27462-27469
    • Persad, S.1    Attwell, S.2    Gray, V.3    Mawji, N.4    Deng, J.T.5    Leung, D.6    Yan, J.7    Sanghera, J.8    Walsh, M.P.9    Dedhar, S.10
  • 20
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • Feng J, Park J, Cron P, Hess D, Hemmings BA. 2004. Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 279:41189-41196.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 21
    • 2442562698 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt activity and Ser473 phosphorylation by protein kinase Calpha in endothelial cells
    • Partovian C, Simons M. 2004. Regulation of protein kinase B/Akt activity and Ser473 phosphorylation by protein kinase Calpha in endothelial cells. Cell. Signal. 16:951-957.
    • (2004) Cell. Signal. , vol.16 , pp. 951-957
    • Partovian, C.1    Simons, M.2
  • 23
    • 23044467856 scopus 로고    scopus 로고
    • PDK2: the missing piece in the receptor tyrosine kinase signaling pathway puzzle
    • doi:10.1152/ajpendo.00011.2005
    • Dong LQ, Liu F. 2005. PDK2: the missing piece in the receptor tyrosine kinase signaling pathway puzzle. Am. J. Physiol. Endocrinol. Metab. 289: E187-E196. doi:10.1152/ajpendo.00011.2005.
    • (2005) Am. J. Physiol. Endocrinol. Metab , vol.289
    • Dong, L.Q.1    Liu, F.2
  • 24
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. 2005. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307:1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 25
    • 28844434558 scopus 로고    scopus 로고
    • mTOR. RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes
    • Hresko RC, Mueckler M. 2005. mTOR. RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes. J. Biol. Chem. 280:40406-40416.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40406-40416
    • Hresko, R.C.1    Mueckler, M.2
  • 27
    • 33748950810 scopus 로고    scopus 로고
    • Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability
    • Shiota C, Woo JT, Lindner J, Shelton KD, Magnuson MA. 2006. Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability. Dev. Cell 11:583-589.
    • (2006) Dev. Cell , vol.11 , pp. 583-589
    • Shiota, C.1    Woo, J.T.2    Lindner, J.3    Shelton, K.D.4    Magnuson, M.A.5
  • 28
    • 37549000623 scopus 로고    scopus 로고
    • Muscle-specific deletion of rictor impairs insulin-stimulated glucose transport and enhances basal glycogen synthase activity
    • Kumar A, Harris TE, Keller SR, Choi KM, Magnuson MA, Lawrence JC, Jr. 2008. Muscle-specific deletion of rictor impairs insulin-stimulated glucose transport and enhances basal glycogen synthase activity. Mol. Cell. Biol. 28:61-70.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 61-70
    • Kumar, A.1    Harris, T.E.2    Keller, S.R.3    Choi, K.M.4    Magnuson, M.A.5    Lawrence Jr., J.C.6
  • 29
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases-MKs-two's company, three's a crowd
    • Gaestel M. 2006. MAPKAP kinases-MKs-two's company, three's a crowd. Nat. Rev. Mol. Cell Biol. 7:120-130.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 120-130
    • Gaestel, M.1
  • 30
    • 0032533546 scopus 로고    scopus 로고
    • The activation of protein kinase B by H2O2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2
    • Shaw M, Cohen P, Alessi DR. 1998. The activation of protein kinase B by H2O2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2. Biochem. J. 336(Part 1):241-246.
    • (1998) Biochem. J. , vol.336 , Issue.PART 1 , pp. 241-246
    • Shaw, M.1    Cohen, P.2    Alessi, D.R.3
  • 31
    • 0035793574 scopus 로고    scopus 로고
    • p38 kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • Rane MJ, Coxon PY, Powell DW, Webster R, Klein JB, Pierce W, Ping P, McLeish KR. 2001. p38 kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J. Biol. Chem. 276:3517-3523.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3517-3523
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3    Webster, R.4    Klein, J.B.5    Pierce, W.6    Ping, P.7    McLeish, K.R.8
  • 34
    • 35548930283 scopus 로고    scopus 로고
    • The MAPKactivated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways
    • Zaru R, Ronkina N, Gaestel M, Arthur JS, Watts C. 2007. The MAPKactivated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways. Nat. Immunol. 8:1227-1235.
    • (2007) Nat. Immunol. , vol.8 , pp. 1227-1235
    • Zaru, R.1    Ronkina, N.2    Gaestel, M.3    Arthur, J.S.4    Watts, C.5
  • 41
    • 0032055131 scopus 로고    scopus 로고
    • Walker KS, Deak M, Paterson A, Hudson K, Cohen P, Alessi DR. 1998. Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha. Biochem. J. 331(Part 1):299-308.
    • (1998) , vol.331 , Issue.PART 1 , pp. 299-308
    • Walker, K.S.1    Deak, M.2    Paterson, A.3    Hudson, K.4    Cohen, P.5    Alessi, D.R.6
  • 42
    • 35048897386 scopus 로고    scopus 로고
    • The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2
    • Batty IH, van der Kaay J, Gray A, Telfer JF, Dixon MJ, Downes CP. 2007. The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2. Biochem. J. 407:255-266.
    • (2007) SHIP2. Biochem. J. , vol.407 , pp. 255-266
    • Batty, I.H.1    van der Kaay, J.2    Gray, A.3    Telfer, J.F.4    Dixon, M.J.5    Downes, C.P.6
  • 44
    • 0037442448 scopus 로고    scopus 로고
    • Nonradioactive methods for the assay of phosphoinositide 3-kinases and phosphoinositide phosphatases and selective detection of signaling lipids in cell and tissue extracts
    • Gray A, Olsson H, Batty IH, Priganica L, Downes CP. 2003. Nonradioactive methods for the assay of phosphoinositide 3-kinases and phosphoinositide phosphatases and selective detection of signaling lipids in cell and tissue extracts. Anal. Biochem. 313:234-245.
    • (2003) Anal. Biochem. , vol.313 , pp. 234-245
    • Gray, A.1    Olsson, H.2    Batty, I.H.3    Priganica, L.4    Downes, C.P.5
  • 45
    • 0031053360 scopus 로고    scopus 로고
    • Akt signaling: linking membrane events to life and death decisions
    • Hemmings BA. 1997. Akt signaling: linking membrane events to life and death decisions. Science 275:628-630.
    • (1997) Science , vol.275 , pp. 628-630
    • Hemmings, B.A.1
  • 52
    • 34250318956 scopus 로고    scopus 로고
    • Heat shock protein 27 functions in inflammatory gene expression and transforming growth factor-beta-activated kinase-1 (TAK1)-mediated signaling
    • Alford KA, Glennie S, Turrell BR, Rawlinson L, Saklatvala J, Dean JL. 2007. Heat shock protein 27 functions in inflammatory gene expression and transforming growth factor-beta-activated kinase-1 (TAK1)-mediated signaling. J. Biol. Chem. 282:6232-6241.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6232-6241
    • Alford, K.A.1    Glennie, S.2    Turrell, B.R.3    Rawlinson, L.4    Saklatvala, J.5    Dean, J.L.6
  • 54
    • 0038558249 scopus 로고    scopus 로고
    • Collaborative induction of inflammatory responses by dectin-1 and Tolllike receptor 2
    • Gantner BN, Simmons RM, Canavera SJ, Akira S, Underhill DM. 2003. Collaborative induction of inflammatory responses by dectin-1 and Tolllike receptor 2. J. Exp. Med. 197:1107-1117.
    • (2003) J. Exp. Med. , vol.197 , pp. 1107-1117
    • Gantner, B.N.1    Simmons, R.M.2    Canavera, S.J.3    Akira, S.4    Underhill, D.M.5
  • 55
    • 84875323963 scopus 로고    scopus 로고
    • Dectin-1 regulates IL-10 production via a MSK1/2 and CREB dependent pathway and promotes the induction of regulatory macrophage markers
    • doi:10.1371/journal.pone.0060086 e60086
    • Elcombe SE, Naqvi S, Van Den Bosch MW, MacKenzie KF, Cianfanelli F, Brown GD, Arthur JS. 2013. Dectin-1 regulates IL-10 production via a MSK1/2 and CREB dependent pathway and promotes the induction of regulatory macrophage markers. PLoS One 8:e60086. doi:10.1371/journal.pone.0060086.
    • (2013) PLoS One , vol.8
    • Elcombe, S.E.1    Naqvi, S.2    Van Den Bosch, M.W.3    MacKenzie, K.F.4    Cianfanelli, F.5    Brown, G.D.6    Arthur, J.S.7
  • 56
    • 42149110310 scopus 로고    scopus 로고
    • Critical roles of the p110 beta subtype of phosphoinositide 3-kinase in lipopolysaccharide-induced Akt activation and negative regulation of nitrite production in RAW 264. 7 cells
    • Tsukamoto K, Hazeki K, Hoshi M, Nigorikawa K, Inoue N, Sasaki T, Hazeki O. 2008. Critical roles of the p110 beta subtype of phosphoinositide 3-kinase in lipopolysaccharide-induced Akt activation and negative regulation of nitrite production in RAW 264.7 cells. J. Immunol. 180: 2054-2061.
    • (2008) J. Immunol. , vol.180 , pp. 2054-2061
    • Tsukamoto, K.1    Hazeki, K.2    Hoshi, M.3    Nigorikawa, K.4    Inoue, N.5    Sasaki, T.6    Hazeki, O.7
  • 58
    • 33846000629 scopus 로고    scopus 로고
    • MAPKactivated protein kinase-2 (MK2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, MK2, Akt, and Hsp27
    • Zheng C, Lin Z, Zhao ZJ, Yang Y, Niu H, Shen X. 2006. MAPKactivated protein kinase-2 (MK2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, MK2, Akt, and Hsp27. J. Biol. Chem. 281:37215-37226.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37215-37226
    • Zheng, C.1    Lin, Z.2    Zhao, Z.J.3    Yang, Y.4    Niu, H.5    Shen, X.6
  • 61
    • 84866887471 scopus 로고    scopus 로고
    • P38alpha negatively regulates T helper type 2 responses by orchestrating multiple TCR-associated signals
    • doi:10.1074/jbc. M112.355594
    • Hu P, Nebreda AR, Liu Y, Carlesso N, Kaplan M, Kapur R. 2012. P38alpha negatively regulates T helper type 2 responses by orchestrating multiple TCR-associated signals. J. Biol. Chem. doi:10.1074/jbc. M112.355594.
    • (2012) J. Biol. Chem
    • Hu, P.1    Nebreda, A.R.2    Liu, Y.3    Carlesso, N.4    Kaplan, M.5    Kapur, R.6
  • 62
    • 0037352702 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages
    • Ojaniemi M, GlumoffV, Harju K, Liljeroos M, Vuori K, Hallman M. 2003. Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages. Eur. J. Immunol. 33:597-605.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 597-605
    • Ojaniemi, M.1    Glumoff, V.2    Harju, K.3    Liljeroos, M.4    Vuori, K.5    Hallman, M.6
  • 65
  • 66
    • 33846122035 scopus 로고    scopus 로고
    • The adaptor molecule MyD88 activates PI-3 kinase signaling in CD4_T cells and enables CpG oligodeoxynucleotide-mediated costimulation
    • Gelman AE, LaRosa DF, Zhang J, Walsh PT, Choi Y, Sunyer JO, Turka LA. 2006. The adaptor molecule MyD88 activates PI-3 kinase signaling in CD4_T cells and enables CpG oligodeoxynucleotide-mediated costimulation. Immunity 25:783-793.
    • (2006) Immunity , vol.25 , pp. 783-793
    • Gelman, A.E.1    LaRosa, D.F.2    Zhang, J.3    Walsh, P.T.4    Choi, Y.5    Sunyer, J.O.6    Turka, L.A.7
  • 67
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan JC, Medzhitov R. 2006. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 125:943-955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 71
    • 1842424697 scopus 로고    scopus 로고
    • The inositol 3-phosphatase PTEN negatively regulates Fc gamma receptor signaling, but supports Toll-like receptor 4 signaling in murine peritoneal macrophages
    • Cao X, Wei G, Fang H, Guo J, Weinstein M, Marsh CB, Ostrowski MC, Tridandapani S. 2004. The inositol 3-phosphatase PTEN negatively regulates Fc gamma receptor signaling, but supports Toll-like receptor 4 signaling in murine peritoneal macrophages. J. Immunol. 172:4851-4857.
    • (2004) J. Immunol. , vol.172 , pp. 4851-4857
    • Cao, X.1    Wei, G.2    Fang, H.3    Guo, J.4    Weinstein, M.5    Marsh, C.B.6    Ostrowski, M.C.7    Tridandapani, S.8
  • 72
    • 0345097326 scopus 로고    scopus 로고
    • SHIP, SHIP2, and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is up-regulated in macrophages and mast cells by lipopolysaccharide
    • Sly LM, Rauh MJ, KalesnikoffJ, Buchse T, Krystal G. 2003. SHIP, SHIP2, and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is up-regulated in macrophages and mast cells by lipopolysaccharide. Exp. Hematol. 31:1170-1181.
    • (2003) Exp. Hematol. , vol.31 , pp. 1170-1181
    • Sly, L.M.1    Rauh, M.J.2    Kalesnikoff, J.3    Buchse, T.4    Krystal, G.5
  • 74
    • 84875498622 scopus 로고    scopus 로고
    • MK2 regulates Ras oncogenesis through stimulating ROS production
    • Kobayashi Y, Qi X, Chen G. 2012. MK2 regulates Ras oncogenesis through stimulating ROS production. Genes Cancer 3:521-530.
    • (2012) Genes Cancer , vol.3 , pp. 521-530
    • Kobayashi, Y.1    Qi, X.2    Chen, G.3
  • 75
    • 79957553362 scopus 로고    scopus 로고
    • Cot/tpl2 activity is required for TLR-induced activation of the Akt p70 S6k pathway in macrophages: implications for NO synthase 2 expression
    • López-Pelaez M, Soria-Castro I, Bosca L, Fernandez M, Alemany S. 2011. Cot/tpl2 activity is required for TLR-induced activation of the Akt p70 S6k pathway in macrophages: implications for NO synthase 2 expression. Eur. J. Immunol. 41:1733-1741.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 1733-1741
    • López-Pelaez, M.1    Soria-Castro, I.2    Bosca, L.3    Fernandez, M.4    Alemany, S.5
  • 76


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.