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Volumn 123, Issue 1, 2013, Pages 164-178

Eukaryotic elongation factor 2 controls TNF-α translation in LPS-induced hepatitis

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR 2; ENDOTOXIN; EUKARYOTIC ELONGATION FACTOR 2; INTERLEUKIN 6; LENTIVIRUS VECTOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 6; MITOGEN ACTIVATED PROTEIN KINASE P38; SHORT HAIRPIN RNA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84873810502     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI65124     Document Type: Article
Times cited : (90)

References (57)
  • 1
    • 50049122380 scopus 로고    scopus 로고
    • The kinase p38 alpha serves cell typespecific inflammatory functions in skin injury and coordinates pro- and anti-inflammatory gene expression
    • Kim C, et al. The kinase p38 alpha serves cell typespecific inflammatory functions in skin injury and coordinates pro- and anti-inflammatory gene expression. Nat Immunol. 2008;9(9): 1019-1027.
    • (2008) Nat Immunol. , vol.9 , Issue.9 , pp. 1019-1027
    • Kim, C.1
  • 2
    • 77954369240 scopus 로고    scopus 로고
    • Acute liver failure: Mechanisms of immune-mediated liver injury
    • Wu Z, Han M, Chen T, Yan W, Ning Q. Acute liver failure: mechanisms of immune-mediated liver injury. Liver Int. 2010;30(6): 782-794.
    • (2010) Liver Int. , vol.30 , Issue.6 , pp. 782-794
    • Wu, Z.1    Han, M.2    Chen, T.3    Yan, W.4    Ning, Q.5
  • 3
    • 53249087835 scopus 로고    scopus 로고
    • The importance of immune dysfunction in determining outcome in acute liver failure
    • Antoniades CG, Berry PA, Wendon JA, Vergani D. The importance of immune dysfunction in determining outcome in acute liver failure. J Hepatol. 2008;49(5): 845-861.
    • (2008) J Hepatol. , vol.49 , Issue.5 , pp. 845-861
    • Antoniades, C.G.1    Berry, P.A.2    Wendon, J.A.3    Vergani, D.4
  • 4
    • 34147126829 scopus 로고    scopus 로고
    • The role of TNF-alpha in chronic inflammatory conditions, intermediary metabolism, and cardiovascular risk
    • Popa C, Netea MG, van Riel PL, van der Meer JW, Stalenhoef AF. The role of TNF-alpha in chronic inflammatory conditions, intermediary metabolism, and cardiovascular risk. J Lipid Res. 2007;48(4): 751-762.
    • (2007) J Lipid Res. , vol.48 , Issue.4 , pp. 751-762
    • Popa, C.1    Netea, M.G.2    Van Riel, P.L.3    Van Der Meer, J.W.4    Stalenhoef, A.F.5
  • 6
    • 38549102077 scopus 로고    scopus 로고
    • TNF-mediated inflammatory disease
    • Bradley Jr. TNF-mediated inflammatory disease. J Pathol. 2008;214(2): 149-160.
    • (2008) J Pathol. , vol.214 , Issue.2 , pp. 149-160
    • Bradley, J.R.1
  • 7
    • 33645799492 scopus 로고    scopus 로고
    • Mechanisms of liver injury. I. TNF-alpha-induced liver injury: Role of IKK, JNK, and ROS pathways
    • Schwabe RF, Brenner DA. Mechanisms of Liver Injury. I. TNF-alpha-induced liver injury: role of IKK, JNK, and ROS pathways. Am J Physiol Gastrointest Liver Physiol. 2006;290:G583-G589.
    • (2006) Am J Physiol Gastrointest Liver Physiol. , vol.290
    • Schwabe, R.F.1    Brenner, D.A.2
  • 8
    • 0027690391 scopus 로고
    • Expression and regulation of tumor necrosis factor in macrophages from cystic fibrosis patients
    • Pfeffer KD, Huecksteadt TP, Hoidal Jr. Expression and regulation of tumor necrosis factor in macrophages from cystic fibrosis patients. Am J Respir Cell Mol Biol. 1993;9(5): 511-519.
    • (1993) Am J Respir Cell Mol Biol. , vol.9 , Issue.5 , pp. 511-519
    • Pfeffer, K.D.1    Huecksteadt, T.P.2    Hoidal, J.R.3
  • 9
    • 0030265356 scopus 로고    scopus 로고
    • Tumour necrosis factors in immune regulation: Everything that's interesting is..new!
    • Pasparakis M, Alexopoulou L, Douni E, Kollias G. Tumour necrosis factors in immune regulation: everything that's interesting is...new! Cytokine Growth Factor Rev. 1996;7(3): 223-229.
    • (1996) Cytokine Growth Factor Rev. , vol.7 , Issue.3 , pp. 223-229
    • Pasparakis, M.1    Alexopoulou, L.2    Douni, E.3    Kollias, G.4
  • 10
    • 0034213138 scopus 로고    scopus 로고
    • P38 MAP kinases: Beyond the stress response
    • Nebreda AR, Porras A. p38 MAP kinases: beyond the stress response. Trends Biochem Sci. 2000; 25(6): 257-260.
    • (2000) Trends Biochem Sci. , vol.25 , Issue.6 , pp. 257-260
    • Nebreda, A.R.1    Porras, A.2
  • 11
    • 27744496768 scopus 로고    scopus 로고
    • The biology of p38 kinase: A central role in inflammation
    • Schieven GL. The biology of p38 kinase: a central role in inflammation. Curr Top Med Chem. 2005;5(10): 921-928.
    • (2005) Curr Top Med Chem. , vol.5 , Issue.10 , pp. 921-928
    • Schieven, G.L.1
  • 12
    • 34547154349 scopus 로고    scopus 로고
    • P38 MAP-kinases pathway regulation, function and role in human diseases
    • Cuenda A, Rousseau S. p38 MAP-kinases pathway regulation, function and role in human diseases. Biochim Biophys Acta. 2007;1773(8): 1358-1375.
    • (2007) Biochim Biophys Acta. , vol.1773 , Issue.8 , pp. 1358-1375
    • Cuenda, A.1    Rousseau, S.2
  • 13
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis JM, Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev. 2001;81(2): 807-869.
    • (2001) Physiol Rev. , vol.81 , Issue.2 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 14
    • 0041660960 scopus 로고    scopus 로고
    • Mechanism of p38 MAP kinase activation in vivo
    • Brancho D, et al. Mechanism of p38 MAP kinase activation in vivo. Genes Dev. 2003;17(16): 1969-1978.
    • (2003) Genes Dev. , vol.17 , Issue.16 , pp. 1969-1978
    • Brancho, D.1
  • 15
    • 74449083698 scopus 로고    scopus 로고
    • Differential activation of p38 MAPK isoforms by MKK6 and MKK3
    • Remy G, et al. Differential activation of p38 MAPK isoforms by MKK6 and MKK3. Cell Signal. 2010;22(4): 660-667.
    • (2010) Cell Signal. , vol.22 , Issue.4 , pp. 660-667
    • Remy, G.1
  • 16
    • 53249111250 scopus 로고    scopus 로고
    • P38 alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure
    • Heinrichsdorff J, Luedde T, Perdiguero E, Nebreda AR, Pasparakis M. p38 alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. EMBO Rep. 2008;9(10): 1048-1054.
    • (2008) EMBO Rep. , vol.9 , Issue.10 , pp. 1048-1054
    • Heinrichsdorff, J.1    Luedde, T.2    Perdiguero, E.3    Nebreda, A.R.4    Pasparakis, M.5
  • 17
    • 34249334506 scopus 로고    scopus 로고
    • P38alpha suppresses normal and cancer cell proliferation by antagonizing the JNK-c-Jun pathway
    • Hui L, et al. p38alpha suppresses normal and cancer cell proliferation by antagonizing the JNK-c-Jun pathway. Nat Genet. 2007;39(6): 741-749.
    • (2007) Nat Genet. , vol.39 , Issue.6 , pp. 741-749
    • Hui, L.1
  • 18
    • 27944461325 scopus 로고    scopus 로고
    • Generation and characterization of p38beta (MAPK11) gene-targeted mice
    • Beardmore VA, et al. Generation and characterization of p38beta (MAPK11) gene-targeted mice. Mol Cell Biol. 2005;25(23): 10454-10464.
    • (2005) Mol Cell Biol. , vol.25 , Issue.23 , pp. 10454-10464
    • Beardmore, V.A.1
  • 19
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identify protein kinase substrates: EEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta
    • Knebel A, Morrice N, Cohen P. A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. EMBO J. 2001;20(16): 4360-4369.
    • (2001) EMBO J. , vol.20 , Issue.16 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 20
    • 80055058063 scopus 로고    scopus 로고
    • Methylation of eukaryotic elongation factor 2 induced by basic fibroblast growth factor via mitogen-activated protein kinase
    • Jung GA, et al. Methylation of eukaryotic elongation factor 2 induced by basic fibroblast growth factor via mitogen-activated protein kinase. Exp Mol Med. 2011;43(10): 550-560.
    • (2011) Exp Mol Med. , vol.43 , Issue.10 , pp. 550-560
    • Jung, G.A.1
  • 21
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne GJ, Proud CG. Regulation of peptide-chain elongation in mammalian cells. Eur J Biochem. 2002;269(22): 5360-5368.
    • (2002) Eur J Biochem. , vol.269 , Issue.22 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 22
    • 0034107580 scopus 로고    scopus 로고
    • Activation of mRNA translation in rat cardiac myocytes by insulin involves multiple rapamycin-sensitive steps
    • Wang L, Wang X, Proud CG. Activation of mRNA translation in rat cardiac myocytes by insulin involves multiple rapamycin-sensitive steps. Am J Physiol Heart Circ Physiol. 2000;278(4):H1056-H1068.
    • (2000) Am J Physiol Heart Circ Physiol , vol.278 , Issue.4
    • Wang, L.1    Wang, X.2    Proud, C.G.3
  • 23
    • 0037109036 scopus 로고    scopus 로고
    • Stressinduced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways
    • Knebel A, Haydon CE, Morrice N, Cohen P. Stressinduced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways. Biochem J. 2002;367(pt 2): 525-532.
    • (2002) Biochem J. , vol.367 , Issue.PART 2 , pp. 525-532
    • Knebel, A.1    Haydon, C.E.2    Morrice, N.3    Cohen, P.4
  • 24
    • 0033965158 scopus 로고    scopus 로고
    • The p38 signal transduction pathway: Activation and function
    • Ono K, Han J. The p38 signal transduction pathway: activation and function. Cell Signal. 2000;12(1): 1-13.
    • (2000) Cell Signal. , vol.12 , Issue.1 , pp. 1-13
    • Ono, K.1    Han, J.2
  • 25
    • 0034816062 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability
    • Mahtani KR, Brook M, Dean JL, Sully G, Saklatvala J, Clark AR. Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. Mol Cell Biol. 2001;21(19): 6461-6469.
    • (2001) Mol Cell Biol. , vol.21 , Issue.19 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 26
    • 77949696703 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase-1 negatively regulates the expression of interleukin- 6, interleukin-8, and cyclooxygenase-2 in A549 human lung epithelial cells
    • Turpeinen T, Nieminen R, Moilanen E, Korhonen R. Mitogen-activated protein kinase phosphatase-1 negatively regulates the expression of interleukin- 6, interleukin-8, and cyclooxygenase-2 in A549 human lung epithelial cells. J Pharmacol Exp Ther. 2010;333(1): 310-318.
    • (2010) J Pharmacol Exp Ther. , vol.333 , Issue.1 , pp. 310-318
    • Turpeinen, T.1    Nieminen, R.2    Moilanen, E.3    Korhonen, R.4
  • 27
    • 79955004429 scopus 로고    scopus 로고
    • Translational control of NKT cell cytokine production by p38 MAPK
    • Nagaleekar VK, et al. Translational control of NKT cell cytokine production by p38 MAPK. J Immunol. 2011;186(7): 4140-4146.
    • (2011) J Immunol. , vol.186 , Issue.7 , pp. 4140-4146
    • Nagaleekar, V.K.1
  • 28
    • 0033145354 scopus 로고    scopus 로고
    • MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis
    • Kotlyarov A, et al. MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. Nat Cell Biol. 1999;1(2): 94-97.
    • (1999) Nat Cell Biol. , vol.1 , Issue.2 , pp. 94-97
    • Kotlyarov, A.1
  • 29
    • 35348983904 scopus 로고    scopus 로고
    • Role of neutrophils in the pathogenesis of acute inflammatory liver injury
    • Ramaiah SK, Jaeschke H. Role of neutrophils in the pathogenesis of acute inflammatory liver injury. Toxicol Pathol. 2007;35(6): 757-766.
    • (2007) Toxicol Pathol. , vol.35 , Issue.6 , pp. 757-766
    • Ramaiah, S.K.1    Jaeschke, H.2
  • 30
    • 84856301921 scopus 로고    scopus 로고
    • TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1(+)CD11b(+) neutrophils
    • Alagbala Ajibade A, et al. TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1(+)CD11b(+) neutrophils. Immunity. 2012;36(1): 43-54.
    • (2012) Immunity. , vol.36 , Issue.1 , pp. 43-54
    • Alagbala Ajibade, A.1
  • 31
    • 79959538608 scopus 로고    scopus 로고
    • Gr-1+ CD11b+ myeloid-derived suppressor cells suppress inflammation and promote insulin sensitivity in obesity
    • Xia S, Sha H, Yang L, Ji Y, Ostrand-Rosenberg S, Qi L. Gr-1+ CD11b+ myeloid-derived suppressor cells suppress inflammation and promote insulin sensitivity in obesity. J Biol Chem. 2011;286(26): 23591-23599.
    • (2011) J Biol Chem. , vol.286 , Issue.26 , pp. 23591-23599
    • Xia, S.1    Sha, H.2    Yang, L.3    Ji, Y.4    Ostrand-Rosenberg, S.5    Qi, L.6
  • 32
    • 35748931783 scopus 로고    scopus 로고
    • The roles of innate immune cells in liver injury and regeneration
    • Dong Z, Wei H, Sun R, Tian Z. The roles of innate immune cells in liver injury and regeneration. Cell Mol Immunol. 2007;4(4): 241-252.
    • (2007) Cell Mol Immunol. , vol.4 , Issue.4 , pp. 241-252
    • Dong, Z.1    Wei, H.2    Sun, R.3    Tian, Z.4
  • 33
    • 21244476768 scopus 로고    scopus 로고
    • BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo
    • Kuma Y, Sabio G, Bain J, Shpiro N, Marquez R, Cuenda A. BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo. J Biol Chem. 2005;280(20): 19472-19479.
    • (2005) J Biol Chem. , vol.280 , Issue.20 , pp. 19472-19479
    • Kuma, Y.1    Sabio, G.2    Bain, J.3    Shpiro, N.4    Marquez, R.5    Cuenda, A.6
  • 34
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A, et al. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 1995;364(2): 229-233.
    • (1995) FEBS Lett. , vol.364 , Issue.2 , pp. 229-233
    • Cuenda, A.1
  • 35
    • 0033177995 scopus 로고    scopus 로고
    • Conditional gene targeting in macrophages and granulocytes using LysMcre mice
    • Clausen BE, Burkhardt C, Reith W, Renkawitz R, Forster I. Conditional gene targeting in macrophages and granulocytes using LysMcre mice. Transgenic Res. 1999;8(4): 265-277.
    • (1999) Transgenic Res. , vol.8 , Issue.4 , pp. 265-277
    • Clausen, B.E.1    Burkhardt, C.2    Reith, W.3    Renkawitz, R.4    Forster, I.5
  • 36
    • 2442637022 scopus 로고    scopus 로고
    • Stress- and mitogen-induced phosphorylation of the synapse-associated protein SAP90/PSD-95 by activation of SAPK3/p38gamma and ERK1/ERK2
    • Sabio G, et al. Stress- and mitogen-induced phosphorylation of the synapse-associated protein SAP90/PSD-95 by activation of SAPK3/p38gamma and ERK1/ERK2. Biochem J. 2004;380(pt 1): 19-30.
    • (2004) Biochem J. , vol.380 , Issue.PART 1 , pp. 19-30
    • Sabio, G.1
  • 37
    • 20244365497 scopus 로고    scopus 로고
    • P38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP
    • Sabio G, et al. p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP. EMBO J. 2005;24(6): 1134-1145.
    • (2005) EMBO J. , vol.24 , Issue.6 , pp. 1134-1145
    • Sabio, G.1
  • 38
    • 79953306828 scopus 로고    scopus 로고
    • Mouse and human neutrophils induce anaphylaxis
    • Jonsson F, et al. Mouse and human neutrophils induce anaphylaxis. J Clin Invest. 2011;121(4): 1484-1496.
    • (2011) J Clin Invest. , vol.121 , Issue.4 , pp. 1484-1496
    • Jonsson, F.1
  • 39
    • 33845899370 scopus 로고    scopus 로고
    • Role of Kupffer cells in the pathogenesis of liver disease
    • Kolios G, Valatas V, Kouroumalis E. Role of Kupffer cells in the pathogenesis of liver disease. World J Gastroenterol. 2006;12(46): 7413-7420.
    • (2006) World J Gastroenterol. , vol.12 , Issue.46 , pp. 7413-7420
    • Kolios, G.1    Valatas, V.2    Kouroumalis, E.3
  • 40
    • 80053184152 scopus 로고    scopus 로고
    • Activation of p38 MAPK in CD4 T cells controls IL-17 production and autoimmune encephalomyelitis
    • Noubade R, et al. Activation of p38 MAPK in CD4 T cells controls IL-17 production and autoimmune encephalomyelitis. Blood. 2011;118(12): 3290-3300.
    • (2011) Blood. , vol.118 , Issue.12 , pp. 3290-3300
    • Noubade, R.1
  • 41
    • 0036863319 scopus 로고    scopus 로고
    • Is MK2 (mitogen-activated Protein Kinase-activated Protein Kinase 2) the key for understanding post-transcriptional regulation of gene expression?
    • Kotlyarov A, Gaestel M. Is MK2 (mitogen-activated protein kinase-activated protein kinase 2) the key for understanding post-transcriptional regulation of gene expression? Biochem Soc Trans. 2002;30(pt 6): 959-963.
    • (2002) Biochem Soc Trans. , vol.30 , Issue.PART 6 , pp. 959-963
    • Kotlyarov, A.1    Gaestel, M.2
  • 42
    • 79954591540 scopus 로고    scopus 로고
    • Bone marrow mesenchymal stem and progenitor cells induce monocyte emigration in response to circulating toll-like receptor ligands
    • Shi C, et al. Bone marrow mesenchymal stem and progenitor cells induce monocyte emigration in response to circulating toll-like receptor ligands. Immunity. 2011;34(4): 590-601.
    • (2011) Immunity. , vol.34 , Issue.4 , pp. 590-601
    • Shi, C.1
  • 43
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • Lee JC, et al. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature. 1994;372(6508): 739-746.
    • (1994) Nature. , vol.372 , Issue.6508 , pp. 739-746
    • Lee, J.C.1
  • 44
    • 44449100233 scopus 로고    scopus 로고
    • Macrophage deletion of p38alpha partially impairs lipopolysaccharide- induced cellular activation
    • Kang YJ, et al. Macrophage deletion of p38alpha partially impairs lipopolysaccharide-induced cellular activation. J Immunol. 2008;180(7): 5075-5082.
    • (2008) J Immunol. , vol.180 , Issue.7 , pp. 5075-5082
    • Kang, Y.J.1
  • 45
    • 27944503331 scopus 로고    scopus 로고
    • MAP kinase p38 inhibitors: Clinical results and an intimate look at their interactions with p38alpha protein
    • Lee MR, Dominguez C. MAP kinase p38 inhibitors: clinical results and an intimate look at their interactions with p38alpha protein. Curr Med Chem. 2005;12(25): 2979-2994.
    • (2005) Curr Med Chem. , vol.12 , Issue.25 , pp. 2979-2994
    • Lee, M.R.1    Dominguez, C.2
  • 46
    • 33644756429 scopus 로고    scopus 로고
    • Oral p38 mitogen-activated protein kinase inhibition with BIRB 796 for active Crohn's disease: A randomized, double-blind, placebo-controlled trial
    • Schreiber S, et al. Oral p38 mitogen-activated protein kinase inhibition with BIRB 796 for active Crohn's disease: a randomized, double-blind, placebo-controlled trial. Clin Gastroenterol Hepatol. 2006;4(3): 325-334.
    • (2006) Clin Gastroenterol Hepatol. , vol.4 , Issue.3 , pp. 325-334
    • Schreiber, S.1
  • 47
    • 0033616588 scopus 로고    scopus 로고
    • Requirement of mitogen-activated protein kinase kinase 3 (MKK3) for tumor necrosis factor-induced cytokine expression
    • Wysk M, Yang DD, Lu HT, Flavell RA, Davis RJ. Requirement of mitogen-activated protein kinase kinase 3 (MKK3) for tumor necrosis factor-induced cytokine expression. Proc Natl Acad Sci U S A. 1999;96(7): 3763-3768.
    • (1999) Proc Natl Acad Sci U S A. , vol.96 , Issue.7 , pp. 3763-3768
    • Wysk, M.1    Yang, D.D.2    Lu, H.T.3    Flavell, R.A.4    Davis, R.J.5
  • 48
    • 0033118982 scopus 로고    scopus 로고
    • Defective IL-12 production in mitogenactivated protein (MAP) kinase kinase 3 (Mkk3)- deficient mice
    • Lu HT, et al. Defective IL-12 production in mitogenactivated protein (MAP) kinase kinase 3 (Mkk3)- deficient mice. EMBO J. 1999;18(7): 1845-1857.
    • (1999) EMBO J. , vol.18 , Issue.7 , pp. 1845-1857
    • Lu, H.T.1
  • 49
    • 0036687249 scopus 로고    scopus 로고
    • Differential involvement of p38 mitogen-activated protein kinase kinases MKK3 and MKK6 in T-cell apoptosis
    • Tanaka N, et al. Differential involvement of p38 mitogen-activated protein kinase kinases MKK3 and MKK6 in T-cell apoptosis. EMBO Rep. 2002;3(8): 785-791.
    • (2002) EMBO Rep. , vol.3 , Issue.8 , pp. 785-791
    • Tanaka, N.1
  • 50
    • 77949489123 scopus 로고    scopus 로고
    • Pharmacological profile of AW-814141, a novel, potent, selective and orally active inhibitor of p38 MAP kinase
    • Chopra P, et al. Pharmacological profile of AW-814141, a novel, potent, selective and orally active inhibitor of p38 MAP kinase. Int Immunopharmacol. 2010;10(4): 467-473.
    • (2010) Int Immunopharmacol. , vol.10 , Issue.4 , pp. 467-473
    • Chopra, P.1
  • 51
    • 80054690072 scopus 로고    scopus 로고
    • Inhibition of p38-MAPK signaling pathway attenuates breast cancer induced bone pain and disease progression in a murine model of cancer-induced bone pain
    • Sukhtankar D, et al. Inhibition of p38-MAPK signaling pathway attenuates breast cancer induced bone pain and disease progression in a murine model of cancer-induced bone pain. Mol Pain. 2011;7:81.
    • (2011) Mol Pain , vol.7 , pp. 81
    • Sukhtankar, D.1
  • 52
    • 79960680264 scopus 로고    scopus 로고
    • NFATc3 regulates the transcription of genes involved in T-cell activation and angiogenesis
    • Urso K, et al. NFATc3 regulates the transcription of genes involved in T-cell activation and angiogenesis. Blood. 2011;118(3): 795-803.
    • (2011) Blood. , vol.118 , Issue.3 , pp. 795-803
    • Urso, K.1
  • 53
    • 1342324679 scopus 로고    scopus 로고
    • Toxoplasma gondii interferes with lipopolysaccharide-induced mitogen-activated protein kinase activation by mechanisms distinct from endotoxin tolerance
    • Kim L, Butcher BA, Denkers EY. Toxoplasma gondii interferes with lipopolysaccharide-induced mitogen-activated protein kinase activation by mechanisms distinct from endotoxin tolerance. J Immunol. 2004;172(5): 3003-3010.
    • (2004) J Immunol. , vol.172 , Issue.5 , pp. 3003-3010
    • Kim, L.1    Butcher, B.A.2    Denkers, E.Y.3
  • 54
    • 33846157438 scopus 로고    scopus 로고
    • Hepatocyte NF-kappaB activation is hepatoprotective during ischemia-reperfusion injury and is augmented by ischemic hypothermia
    • Kuboki S, et al. Hepatocyte NF-kappaB activation is hepatoprotective during ischemia-reperfusion injury and is augmented by ischemic hypothermia. Am J Physiol Gastrointest Liver Physiol. 2007;292(1):G201-G207.
    • (2007) Am J Physiol Gastrointest Liver Physiol , vol.292 , Issue.1
    • Kuboki, S.1
  • 55
    • 38849207589 scopus 로고    scopus 로고
    • Chemotaxis of mouse bone marrow neutrophils and dendritic cells is controlled by adp-ribose, the major product generated by the CD38 enzyme reaction
    • Partida-Sanchez S, et al. Chemotaxis of mouse bone marrow neutrophils and dendritic cells is controlled by adp-ribose, the major product generated by the CD38 enzyme reaction. J Immunol. 2007;179(11): 7827-7839.
    • (2007) J Immunol. , vol.179 , Issue.11 , pp. 7827-7839
    • Partida-Sanchez, S.1
  • 56
    • 77950481334 scopus 로고    scopus 로고
    • Impairment of transforming growth factor beta signaling in caveolin-1-deficient hepatocytes: Role in liver regeneration
    • Mayoral R, Valverde AM, Llorente Izquierdo C, Gonzalez- Rodriguez A, Bosca L, Martin-Sanz P. Impairment of transforming growth factor beta signaling in caveolin-1-deficient hepatocytes: role in liver regeneration. J Biol Chem. 2010;285(6): 3633-3642.
    • (2010) J Biol Chem. , vol.285 , Issue.6 , pp. 3633-3642
    • Mayoral, R.1    Valverde, A.M.2    Llorente Izquierdo, C.3    Gonzalez-Rodriguez, A.4    Bosca, L.5    Martin-Sanz, P.6
  • 57
    • 77958470132 scopus 로고    scopus 로고
    • CD69 limits the severity of cardiomyopathy after autoimmune myocarditis
    • Cruz-Adalia A, et al. CD69 limits the severity of cardiomyopathy after autoimmune myocarditis. Circulation. 2010;122(14): 1396-1404.
    • (2010) Circulation. , vol.122 , Issue.14 , pp. 1396-1404
    • Cruz-Adalia, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.