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Volumn 42, Issue 3, 2012, Pages 189-195

Mitogen-activated protein kinases in inflammation

Author keywords

Inflammation; MAPKS

Indexed keywords


EID: 84922685657     PISSN: 15982467     EISSN: None     Source Type: Journal    
DOI: 10.4167/jbv.2012.42.3.189     Document Type: Review
Times cited : (64)

References (52)
  • 1
    • 47949099098 scopus 로고    scopus 로고
    • Origin and physiological roles of inflammation
    • Medzhitov R. Origin and physiological roles of inflammation. Nature 2008;454:428-35.
    • (2008) Nature , vol.454 , pp. 428-435
    • Medzhitov, R.1
  • 2
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell 2010;140:805-20.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 3
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR domain-containing adaptors in Toll-like receptor signalling
    • O'Neill LA, Bowie AG. The family of five: TIR domain-containing adaptors in Toll-like receptor signalling. Nat Rev Immunol 2007;7:353-64.
    • (2007) Nat Rev Immunol , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 4
    • 33847183077 scopus 로고    scopus 로고
    • Cooperation of Toll-like receptor signals in innate immune defence
    • Trinchieri G, Sher A. Cooperation of Toll-like receptor signals in innate immune defence. Nat Rev Immunol 2007;7:179-90.
    • (2007) Nat Rev Immunol , vol.7 , pp. 179-190
    • Trinchieri, G.1    Sher, A.2
  • 5
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • Miao EA, Leaf IA, Treuting PM, Mao DP, Dors M, Sarkar A, et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol 2010;11:1136-42.
    • (2010) Nat Immunol , vol.11 , pp. 1136-1142
    • Miao, E.A.1    Leaf, I.A.2    Treuting, P.M.3    Mao, D.P.4    Dors, M.5    Sarkar, A.6
  • 6
    • 84922686305 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Yuk JM, Jo EK. Toll-like receptors and innate immunity. J Bacteriol Virol 2011;41:225-35.
    • (2011) J Bacteriol Virol , vol.41 , pp. 225-235
    • Yuk, J.M.1    Jo, E.K.2
  • 7
    • 83755179120 scopus 로고    scopus 로고
    • Pyrin domain (PYD)-containing inflammasome in innate immunity
    • Hong S, Park S, Yu JW. Pyrin domain (PYD)-containing inflammasome in innate immunity. J Bacteriol Virol 2011;41:133-46.
    • (2011) J Bacteriol Virol , vol.41 , pp. 133-146
    • Hong, S.1    Park, S.2    Yu, J.W.3
  • 8
    • 85033333830 scopus 로고    scopus 로고
    • Caspase-11, the main executioner in non-canonical inflammasome
    • Manzoor Z, Koh YS. Caspase-11, the main executioner in non-canonical inflammasome. J Bacteriol Virol 2012; 42:169-71.
    • (2012) J Bacteriol Virol , vol.42 , pp. 169-171
    • Manzoor, Z.1    Koh, Y.S.2
  • 9
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov R. Recognition of microorganisms and activation of the immune response. Nature 2007;449: 819-26.
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 10
    • 44649132540 scopus 로고    scopus 로고
    • Host innate immune receptors and beyond: Making sense of microbial infections
    • Ishii KJ, Koyama S, Nakagawa A, Coban C, Akira S. Host innate immune receptors and beyond: making sense of microbial infections. Cell Host Microbe 2008; 3:352-63.
    • (2008) Cell Host Microbe , vol.3 , pp. 352-363
    • Ishii, K.J.1    Koyama, S.2    Nakagawa, A.3    Coban, C.4    Akira, S.5
  • 11
    • 80052054780 scopus 로고    scopus 로고
    • Nucleic acid recognition and signaling by Toll-like receptor 9: Compartment-dependent regulation
    • Koh YS. Nucleic acid recognition and signaling by Toll-like receptor 9: compartment-dependent regulation. J Bacteriol Virol 2011;41:131-2.
    • (2011) J Bacteriol Virol , vol.41 , pp. 131-132
    • Koh, Y.S.1
  • 12
    • 12444341944 scopus 로고    scopus 로고
    • Toll-like receptors in innate immunity
    • Takeda K, Akira S. Toll-like receptors in innate immunity. Int Immunol 2005;17:1-14.
    • (2005) Int Immunol , vol.17 , pp. 1-14
    • Takeda, K.1    Akira, S.2
  • 14
    • 0036008014 scopus 로고    scopus 로고
    • Small anti-viral compounds activate immune cells via TLR7 MyD88-dependent signaling pathway
    • Hemmi H, Kaisho T, Takeuchi O, Sato S, Sanjo H, Hoshino K, et al. Small anti-viral compounds activate immune cells via TLR7 MyD88-dependent signaling pathway. Nat Immunol 2002;3:196-200.
    • (2002) Nat Immunol , vol.3 , pp. 196-200
    • Hemmi, H.1    Kaisho, T.2    Takeuchi, O.3    Sato, S.4    Sanjo, H.5    Hoshino, K.6
  • 15
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
    • Yamamoto M, Sato S, Hemmi H, Hoshino K, Kaisho T, Sanjo H, et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science 2003;301:640-3.
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Hoshino, K.4    Kaisho, T.5    Sanjo, H.6
  • 16
    • 0346157331 scopus 로고    scopus 로고
    • TIR domain-containing adaptors define the specificity of TLR signaling
    • Yamamoto M, Takeda K, Akira S. TIR domain-containing adaptors define the specificity of TLR signaling. Mol Immunol 2004;40:861-8.
    • (2004) Mol Immunol , vol.40 , pp. 861-868
    • Yamamoto, M.1    Takeda, K.2    Akira, S.3
  • 17
  • 18
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-kappa B by Toll-like receptors
    • Kawai T, Akira S. Signaling to NF-kappa B by Toll-like receptors. Trends Mol Med 2007;13:460-9.
    • (2007) Trends Mol Med , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 19
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai T, Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol 2010;11:373-84.
    • (2010) Nat Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 20
    • 52049095036 scopus 로고    scopus 로고
    • New insights into NF-kappa B regulation and function
    • Sun SC, Ley SC. New insights into NF-kappa B regulation and function. Trends Immunol 2008;29:469-78.
    • (2008) Trends Immunol , vol.29 , pp. 469-478
    • Sun, S.C.1    Ley, S.C.2
  • 21
    • 34548679608 scopus 로고    scopus 로고
    • TLR5 and Ipaf: Dual sensors of bacterial flagellin in the innate immune system
    • Miao EA, Andersen-Nissen E, Warren SE, Aderem A. TLR5 and Ipaf: dual sensors of bacterial flagellin in the innate immune system. Semin Immunopathol 2007; 29:275-88.
    • (2007) Semin Immunopathol , vol.29 , pp. 275-288
    • Miao, E.A.1    Andersen-Nissen, E.2    Warren, S.E.3    Aderem, A.4
  • 23
    • 67749117934 scopus 로고    scopus 로고
    • Signal integration by JNK and p38 MAPK pathways in cancer development
    • Wagner EF, Nebreda AR. Signal integration by JNK and p38 MAPK pathways in cancer development. Nat Rev Cancer 2009;9:537-49.
    • (2009) Nat Rev Cancer , vol.9 , pp. 537-549
    • Wagner, E.F.1    Nebreda, A.R.2
  • 24
    • 79953163484 scopus 로고    scopus 로고
    • MAPK signaling in inflammation-associated cancer development
    • Huang P, Han J, Hui L. MAPK signaling in inflammation-associated cancer development. Protein Cell 2010;1:218-26.
    • (2010) Protein Cell , vol.1 , pp. 218-226
    • Huang, P.1    Han, J.2    Hui, L.3
  • 25
    • 0036909437 scopus 로고    scopus 로고
    • Multi-protein complexes in eukaryotic gene transcription
    • Martinez E. Multi-protein complexes in eukaryotic gene transcription. Plant Mol Biol 2002;50:925-47.
    • (2002) Plant Mol Biol , vol.50 , pp. 925-947
    • Martinez, E.1
  • 27
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions
    • Pearson G, Robinson F, Beers Gibson T, Xu BE, Karandikar M, Berman K, et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr Rev 2001;22:153-83.
    • (2001) Endocr Rev , vol.22 , pp. 153-183
    • Pearson, G.1    Robinson, F.2    Beers Gibson, T.3    Xu, B.E.4    Karandikar, M.5    Berman, K.6
  • 28
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • Roux PP, Blenis J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol Mol Biol Rev 2004; 68:320-44.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 29
    • 0029913457 scopus 로고    scopus 로고
    • Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase
    • Blank JL, Gerwins P, Elliott EM, Sather S, Johnson GL. Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase. J Biol Chem 1996;271:5361-8.
    • (1996) J Biol Chem , vol.271 , pp. 5361-5368
    • Blank, J.L.1    Gerwins, P.2    Elliott, E.M.3    Sather, S.4    Johnson, G.L.5
  • 30
    • 0028904384 scopus 로고
    • A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/ threonine kinase via an SH3 domain
    • Chou MM, Hanafusa H. A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/ threonine kinase via an SH3 domain. J Biol Chem 1995; 270:7359-64.
    • (1995) J Biol Chem , vol.270 , pp. 7359-7364
    • Chou, M.M.1    Hanafusa, H.2
  • 31
    • 33745327045 scopus 로고    scopus 로고
    • Back to the roots: The remarkable RAF oncogene story
    • Zebisch A, Troppmair J. Back to the roots: the remarkable RAF oncogene story. Cell Mol Life Sci 2006;63:1314-30.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1314-1330
    • Zebisch, A.1    Troppmair, J.2
  • 32
    • 0020539047 scopus 로고
    • Identification of transforming gene in two human sarcoma cell lines as a new member of the ras gene family located on chromosome 1
    • Hall A, Marshall CJ, Spurr NK, Weiss RA. Identification of transforming gene in two human sarcoma cell lines as a new member of the ras gene family located on chromosome 1. Nature 1983;303:396-400.
    • (1983) Nature , vol.303 , pp. 396-400
    • Hall, A.1    Marshall, C.J.2    Spurr, N.K.3    Weiss, R.A.4
  • 34
    • 0027935756 scopus 로고
    • Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation
    • Hallberg B, Rayter SI, Downward J. Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation. J Biol Chem 1994;269:3913-6.
    • (1994) J Biol Chem , vol.269 , pp. 3913-3916
    • Hallberg, B.1    Rayter, S.I.2    Downward, J.3
  • 36
    • 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;81:807-69.
    • (2001) Physiol Rev , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 37
    • 34547164540 scopus 로고    scopus 로고
    • The c-Jun kinase/stress-activated pathway: Regulation, function and role in human disease
    • Johnson GL, Nakamura K. The c-Jun kinase/stress-activated pathway: Regulation, function and role in human disease. Biochim Biophys Acta 2007;1773:1341-8.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 1341-1348
    • Johnson, G.L.1    Nakamura, K.2
  • 38
    • 0024997935 scopus 로고
    • pp54 microtubule-associated protein 2 kinase. A novel serine/threonine protein kinase regulated by phosphorylation and stimulated by poly-L-lysine
    • Kyriakis JM, Avruch J. pp54 microtubule-associated protein 2 kinase. A novel serine/threonine protein kinase regulated by phosphorylation and stimulated by poly-L-lysine. J Biol Chem 1990;265:17355-63.
    • (1990) J Biol Chem , vol.265 , pp. 17355-17363
    • Kyriakis, J.M.1    Avruch, J.2
  • 39
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • Yang DD, Kuan CY, Whitmarsh AJ, Rincón M, Zheng TS, Davis RJ, et al. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature 1997;389:865-70.
    • (1997) Nature , vol.389 , pp. 865-870
    • Yang, D.D.1    Kuan, C.Y.2    Whitmarsh, A.J.3    Rincón, M.4    Zheng, T.S.5    Davis, R.J.6
  • 40
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Dérijard B, Hibi M, Wu IH, Barrett T, Su B, Deng T, et al. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994;76:1025-37.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Dérijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6
  • 43
    • 0028303977 scopus 로고
    • Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway
    • Akira S, Nishio Y, Inoue M, Wang XJ, Wei S, Matsusaka T, et al. Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway. Cell 1994;77:63-71.
    • (1994) Cell , vol.77 , pp. 63-71
    • Akira, S.1    Nishio, Y.2    Inoue, M.3    Wang, X.J.4    Wei, S.5    Matsusaka, T.6
  • 44
    • 12344252237 scopus 로고    scopus 로고
    • AP-1 subunits: Quarrel and harmony among siblings
    • Hess J, Angel P, Schorpp-Kistner M. AP-1 subunits: quarrel and harmony among siblings. J Cell Sci 2004; 117:5965-73.
    • (2004) J Cell Sci , vol.117 , pp. 5965-5973
    • Hess, J.1    Angel, P.2    Schorpp-Kistner, M.3
  • 45
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • Shaulian E, Karin M. AP-1 in cell proliferation and survival. Oncogene 2001;20:2390-400.
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 46
    • 0242606442 scopus 로고    scopus 로고
    • A role for AP-1 in apoptosis: The case for and against
    • Ameyar M, Wisniewska M, Weitzman JB. A role for AP-1 in apoptosis: the case for and against. Biochimie 2003;85:747-52.
    • (2003) Biochimie , vol.85 , pp. 747-752
    • Ameyar, M.1    Wisniewska, M.2    Weitzman, J.B.3
  • 47
    • 35848938280 scopus 로고    scopus 로고
    • p38alpha: A suppressor of cell proliferation and tumorigenesis
    • Hui L, Bakiri L, Stepniak E, Wagner EF. p38alpha: a suppressor of cell proliferation and tumorigenesis. Cell Cycle 2007;6:2429-33.
    • (2007) Cell Cycle , vol.6 , pp. 2429-2433
    • Hui, L.1    Bakiri, L.2    Stepniak, E.3    Wagner, E.F.4
  • 48
    • 0034610981 scopus 로고    scopus 로고
    • Deficiency of the stress kinase p38alpha results in embryonic lethality: Characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells
    • Allen M, Svensson L, Roach M, Hambor J, McNeish J, Gabel CA. Deficiency of the stress kinase p38alpha results in embryonic lethality: characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells. J Exp Med 2000;191: 859-70.
    • (2000) J Exp Med , vol.191 , pp. 859-870
    • Allen, M.1    Svensson, L.2    Roach, M.3    Hambor, J.4    McNeish, J.5    Gabel, C.A.6
  • 50
    • 58249087541 scopus 로고    scopus 로고
    • Regulation of PKD by the MAPK p38delta in insulin secretion and glucose homeostasis
    • Sumara G, Formentini I, Collins S, Sumara I, Windak R, Bodenmiller B, et al. Regulation of PKD by the MAPK p38delta in insulin secretion and glucose homeostasis. Cell 2009;136:235-48.
    • (2009) Cell , vol.136 , pp. 235-248
    • Sumara, G.1    Formentini, I.2    Collins, S.3    Sumara, I.4    Windak, R.5    Bodenmiller, B.6
  • 51
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • Lee JC, Laydon JT, McDonnell PC, Gallagher TF, Kumar S, Green D, et al. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 1994;372:739-46.
    • (1994) Nature , vol.372 , pp. 739-746
    • Lee, J.C.1    Laydon, J.T.2    McDonnell, P.C.3    Gallagher, T.F.4    Kumar, S.5    Green, D.6
  • 52
    • 34547212349 scopus 로고    scopus 로고
    • The pathways to tumor suppression via route p38
    • Han J, Sun P. The pathways to tumor suppression via route p38. Trends Biochem Sci 2007;32:364-71.
    • (2007) Trends Biochem Sci , vol.32 , pp. 364-371
    • Han, J.1    Sun, P.2


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