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Volumn 14, Issue 1, 2014, Pages

MAPK-activated protein kinase 2-deficiency causes hyperacute tumor necrosis factor-induced inflammatory shock

Author keywords

Actin cytoskeleton; Cecal ligation and puncture; Endothelial permeability; Inflammatory shock; MK2; Reactive oxygen species; Tumor necrosis factor

Indexed keywords

LIPOPOLYSACCHARIDE; MAP-KINASE-ACTIVATED KINASE 2; PROTEIN SERINE THREONINE KINASE; SIGNAL PEPTIDE; TUMOR NECROSIS FACTOR ALPHA;

EID: 84908420209     PISSN: None     EISSN: 14726793     Source Type: Journal    
DOI: 10.1186/s12899-014-0005-1     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 52049118753 scopus 로고    scopus 로고
    • MK2 and MK3-A pair of isoenzymes?
    • 18508601
    • MK2 and MK3-a pair of isoenzymes? N Ronkina, A Kotlyarov, M Gaestel, Front Biosci 2008 13 5511 5521 10.2741/3095 18508601
    • (2008) Front Biosci , vol.13 , pp. 5511-5521
    • Ronkina, N.1    Kotlyarov, A.2    Gaestel, M.3
  • 2
    • 77955059513 scopus 로고    scopus 로고
    • Mechanisms and functions of p38 MAPK signalling
    • 20626350
    • Mechanisms and functions of p38 MAPK signalling. A Cuadrado, AR Nebreda, Biochem J 2010 429 403 417 10.1042/BJ20100323 20626350
    • (2010) Biochem J , vol.429 , pp. 403-417
    • Cuadrado, A.1    Nebreda, A.R.2
  • 3
    • 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?
    • 12440954
    • Is MK2 (mitogen-activated protein kinase-activated protein kinase 2) the key for understanding post-transcriptional regulation of gene expression? A Kotlyarov, M Gaestel, Biochem Soc Trans 2002 30 Pt 6 959 963 12440954
    • (2002) Biochem Soc Trans , vol.30 , pp. 959-963
    • Kotlyarov, A.1    Gaestel, M.2
  • 4
    • 0032563807 scopus 로고    scopus 로고
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
    • 9768359
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. R Ben-Levy, S Hooper, R Wilson, HF Paterson, CJ Marshall, Curr Biol 1998 8 1049 1057 10.1016/S0960-9822(98)70442-7 9768359
    • (1998) Curr Biol , vol.8 , pp. 1049-1057
    • Ben-Levy, R.1    Hooper, S.2    Wilson, R.3    Paterson, H.F.4    Marshall, C.J.5
  • 5
    • 40949102111 scopus 로고    scopus 로고
    • Post-transcriptional control of cytokine production
    • 18349815
    • Post-transcriptional control of cytokine production. P Anderson, Nat Immunol 2008 9 353 359 10.1038/ni1584 18349815
    • (2008) Nat Immunol , vol.9 , pp. 353-359
    • Anderson, P.1
  • 7
    • 0036479125 scopus 로고    scopus 로고
    • MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels
    • 11741878
    • MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels. A Neininger, D Kontoyiannis, A Kotlyarov, R Winzen, R Eckert, H-D Volk, H Holtmann, G Kollias, M Gaestel, J Biol Chem 2002 277 3065 3068 10.1074/jbc.C100685200 11741878
    • (2002) J Biol Chem , vol.277 , pp. 3065-3068
    • Neininger, A.1    Kontoyiannis, D.2    Kotlyarov, A.3    Winzen, R.4    Eckert, R.5    Volk, H.-D.6    Holtmann, H.7    Kollias, G.8    Gaestel, M.9
  • 8
    • 80051499526 scopus 로고    scopus 로고
    • Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region
    • Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region. W Zhao, M Liu, NJ D'Silva, KL Kirkwood, J Interf Cytokine Res 2011 31 629 637 10.1089/jir.2010.0154
    • (2011) J Interf Cytokine Res , vol.31 , pp. 629-637
    • Zhao, W.1    Liu, M.2    D'Silva, N.J.3    Kirkwood, K.L.4
  • 10
    • 84897012172 scopus 로고    scopus 로고
    • Effect of SB203580 on pathologic change of pancreatic tissue and expression of TNF-α and IL-1β in rats with severe acute pancreatitis
    • 24563432
    • Effect of SB203580 on pathologic change of pancreatic tissue and expression of TNF-α and IL-1β in rats with severe acute pancreatitis. X-Y Wang, Q-Q Tang, J-L Zhang, M-Y Fang, Y-X Li, Eur Rev Med Pharmacol Sci 2014 18 338 343 24563432
    • (2014) Eur Rev Med Pharmacol Sci , vol.18 , pp. 338-343
    • Wang, X.-Y.1    Tang, Q.-Q.2    Zhang, J.-L.3    Fang, M.-Y.4    Li, Y.-X.5
  • 11
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • 9703499
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. E Carballo, WS Lai, PJ Blackshear, Science 1998 281 1001 1005 10.1126/science.281.5379.1001 9703499
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 13
    • 34548241289 scopus 로고    scopus 로고
    • Tristetraprolin regulates TNF TNF-alpha mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways
    • 17606294
    • Tristetraprolin regulates TNF TNF-alpha mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways. KM Deleault, SJ Skinner, SA Brooks, Mol Immunol 2008 45 13 24 10.1016/j.molimm.2007.05.017 17606294
    • (2008) Mol Immunol , vol.45 , pp. 13-24
    • Deleault, K.M.1    Skinner, S.J.2    Brooks, S.A.3
  • 14
    • 33644753147 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element
    • 16508014
    • Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element. E Hitti, T Iakovleva, M Brook, S Deppenmeier, AD Gruber, D Radzioch, AR Clark, PJ Blackshear, A Kotlyarov, M Gaestel, Mol Cell Biol 2006 26 2399 2407 10.1128/MCB.26.6.2399-2407.2006 16508014
    • (2006) Mol Cell Biol , vol.26 , pp. 2399-2407
    • Hitti, E.1    Iakovleva, T.2    Brook, M.3    Deppenmeier, S.4    Gruber, A.D.5    Radzioch, D.6    Clark, A.R.7    Blackshear, P.J.8    Kotlyarov, A.9    Gaestel, M.10
  • 15
    • 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
    • 11533235
    • Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. KR Mahtani, M Brook, JL Dean, G Sully, J Saklatvala, AR Clark, Mol Cell Biol 2001 21 6461 6469 10.1128/MCB.21.9.6461-6469.2001 11533235
    • (2001) Mol Cell Biol , vol.21 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 16
    • 84866951611 scopus 로고    scopus 로고
    • The p38/MK2-driven exchange between tristetraprolin and HuR regulates AU-rich element-dependent translation
    • 23028373
    • The p38/MK2-driven exchange between tristetraprolin and HuR regulates AU-rich element-dependent translation. C Tiedje, N Ronkina, M Tehrani, S Dhamija, K Laass, H Holtmann, A Kotlyarov, M Gaestel, PLoS Genet 2012 8 1002977 10.1371/journal.pgen.1002977 23028373
    • (2012) PLoS Genet , vol.8 , pp. 51002977
    • Tiedje, C.1    Ronkina, N.2    Tehrani, M.3    Dhamija, S.4    Laass, K.5    Holtmann, H.6    Kotlyarov, A.7    Gaestel, M.8
  • 17
    • 33845807361 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK
    • 17030606
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK. N Ronkina, A Kotlyarov, O Dittrich-Breiholz, M Kracht, E Hitti, K Milarski, R Askew, S Marusic, L-L Lin, M Gaestel, J-B Telliez, Mol Cell Biol 2007 27 170 181 10.1128/MCB.01456-06 17030606
    • (2007) Mol Cell Biol , vol.27 , pp. 170-181
    • Ronkina, N.1    Kotlyarov, A.2    Dittrich-Breiholz, O.3    Kracht, M.4    Hitti, E.5    Milarski, K.6    Askew, R.7    Marusic, S.8    Lin, L.-L.9    Gaestel, M.10    Telliez, J.-B.11
  • 18
    • 0027482463 scopus 로고
    • Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27
    • 8226968
    • Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. JN Lavoie, E Hickey, LA Weber, J Landry, J Biol Chem 1993 268 24210 24214 8226968
    • (1993) J Biol Chem , vol.268 , pp. 24210-24214
    • Lavoie, J.N.1    Hickey, E.2    Weber, L.A.3    Landry, J.4
  • 19
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • 16205709
    • Some like it hot: the structure and function of small heat-shock proteins. M Haslbeck, T Franzmann, D Weinfurtner, J Buchner, Nat Struct Mol Biol 2005 12 842 846 10.1038/nsmb993 16205709
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 20
    • 14044250859 scopus 로고    scopus 로고
    • Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels
    • 15706088
    • Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels. A-P Arrigo, S Virot, S Chaufour, W Firdaus, C Kretz-Remy, C Diaz-Latoud, Antioxid Redox Signal 2005 7 414 422 10.1089/ars.2005.7.414 15706088
    • (2005) Antioxid Redox Signal , vol.7 , pp. 414-422
    • Arrigo, A.-P.1    Virot, S.2    Chaufour, S.3    Firdaus, W.4    Kretz-Remy, C.5    Diaz-Latoud, C.6
  • 21
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • Actin cytoskeleton and small heat shock proteins: how do they interact? N Mounier, A-P Arrigo, Cell Stress Chaperon 2002 7 167 176 10.1379/1466-1268(2002)007<0167:ACASHS>2.0.CO;2
    • (2002) Cell Stress Chaperon , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.-P.2
  • 22
    • 41149164199 scopus 로고    scopus 로고
    • Regulation of endothelial junctional permeability
    • 18375586
    • Regulation of endothelial junctional permeability. E Vandenbroucke, D Mehta, R Minshall, AB Malik, Ann N Y Acad Sci 2008 1123 134 145 10.1196/annals.1420.016 18375586
    • (2008) Ann N y Acad Sci , vol.1123 , pp. 134-145
    • Vandenbroucke, E.1    Mehta, D.2    Minshall, R.3    Malik, A.B.4
  • 23
    • 59849121672 scopus 로고    scopus 로고
    • Reprint of the role of cytoskeleton in the regulation of vascular endothelial barrier function [Microvascular Research 76 (2008) 202-207]
    • 19232242
    • Reprint of "The role of cytoskeleton in the regulation of vascular endothelial barrier function" [Microvascular Research 76 (2008) 202-207]. NV Bogatcheva, AD Verin, Microvasc Res 2009 77 64 69 10.1016/S0026-2862(09)00021-1 19232242
    • (2009) Microvasc Res , vol.77 , pp. 64-69
    • Bogatcheva, N.V.1    Verin, A.D.2
  • 24
    • 0026018299 scopus 로고
    • Demonstration of actin filament stress fibers in microvascular endothelial cells in situ
    • 1921751
    • Demonstration of actin filament stress fibers in microvascular endothelial cells in situ. V Nehls, D Drenckhahn, Microvasc Res 1991 42 103 112 10.1016/0026-2862(91)90078-P 1921751
    • (1991) Microvasc Res , vol.42 , pp. 103-112
    • Nehls, V.1    Drenckhahn, D.2
  • 26
    • 77955856027 scopus 로고    scopus 로고
    • Endothelial adherens junctions and the actin cytoskeleton: An infinity net?
    • 20377920
    • Endothelial adherens junctions and the actin cytoskeleton: an "infinity net"? MG Lampugnani, J Biol 2010 9 16 10.1186/jbiol232 20377920
    • (2010) J Biol , vol.9 , pp. 16
    • Lampugnani, M.G.1
  • 27
    • 0032905202 scopus 로고    scopus 로고
    • LPS challenge in D-galactosamine-sensitized mice accounts for caspase-dependent fulminant hepatitis, not for septic shock
    • 10194182
    • LPS challenge in D-galactosamine-sensitized mice accounts for caspase-dependent fulminant hepatitis, not for septic shock. A Mignon, N Rouquet, M Fabre, S Martin, JC Pagès, JF Dhainaut, A Kahn, P Briand, V Joulin, Am J Respir Crit Care Med 1999 159 1308 1315 10.1164/ajrccm.159.4.9712012 10194182
    • (1999) Am J Respir Crit Care Med , vol.159 , pp. 1308-1315
    • Mignon, A.1    Rouquet, N.2    Fabre, M.3    Martin, S.4    Pagès, J.C.5    Dhainaut, J.F.6    Kahn, A.7    Briand, P.8    Joulin, V.9
  • 28
    • 0037386245 scopus 로고    scopus 로고
    • Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2
    • 12652297
    • Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2. A Cauwels, B Janssen, A Waeytens, C Cuvelier, P Brouckaert, Nat Immunol 2003 4 387 393 10.1038/ni914 12652297
    • (2003) Nat Immunol , vol.4 , pp. 387-393
    • Cauwels, A.1    Janssen, B.2    Waeytens, A.3    Cuvelier, C.4    Brouckaert, P.5
  • 29
    • 77956399701 scopus 로고    scopus 로고
    • Reactive oxygen species and small-conductance calcium-dependent potassium channels are key mediators of inflammation-induced hypotension and shock
    • 20496172
    • Reactive oxygen species and small-conductance calcium-dependent potassium channels are key mediators of inflammation-induced hypotension and shock. A Cauwels, E Rogge, B Janssen, P Brouckaert, J Mol Med 2010 88 921 930 10.1007/s00109-010-0633-2 20496172
    • (2010) J Mol Med , vol.88 , pp. 921-930
    • Cauwels, A.1    Rogge, E.2    Janssen, B.3    Brouckaert, P.4
  • 30
    • 58149084932 scopus 로고    scopus 로고
    • Chemistry and antihypertensive effects of tempol and other nitroxides
    • 19112152
    • Chemistry and antihypertensive effects of tempol and other nitroxides. CS Wilcox, A Pearlman, Pharmacol Rev 2008 60 418 469 10.1124/pr.108.000240 19112152
    • (2008) Pharmacol Rev , vol.60 , pp. 418-469
    • Wilcox, C.S.1    Pearlman, A.2
  • 31
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3 T3-ras cells
    • 9405255
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3 T3-ras cells. P Mehlen, E Hickey, LA Weber, AP Arrigo, Biochem Biophys Res Commun 1997 241 187 192 10.1006/bbrc.1997.7635 9405255
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 32
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • 9029143
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. M Ehrnsperger, S Gräber, M Gaestel, J Buchner, EMBO J 1997 16 221 229 10.1093/emboj/16.2.221 9029143
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 33
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
    • 10383393
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. T Rogalla, M Ehrnsperger, X Preville, A Kotlyarov, G Lutsch, C Ducasse, C Paul, M Wieske, AP Arrigo, J Buchner, M Gaestel, J Biol Chem 1999 274 18947 18956 10.1074/jbc.274.27.18947 10383393
    • (1999) J Biol Chem , vol.274 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3    Kotlyarov, A.4    Lutsch, G.5    Ducasse, C.6    Paul, C.7    Wieske, M.8    Arrigo, A.P.9    Buchner, J.10    Gaestel, M.11
  • 34
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • 8051180
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. R Benndorf, K Hayess, S Ryazantsev, M Wieske, J Behlke, G Lutsch, J Biol Chem 1994 269 20780 20784 8051180
    • (1994) J Biol Chem , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 35
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • 9048659
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. J Huot, F Houle, F Marceau, J Landry, Circ Res 1997 80 383 392 10.1161/01.RES.80.3.383 9048659
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 36
    • 0027461977 scopus 로고
    • TNF-alpha induces endothelial cell F-actin depolymerization, new actin synthesis, and barrier dysfunction
    • 8476021
    • TNF-alpha induces endothelial cell F-actin depolymerization, new actin synthesis, and barrier dysfunction. SE Goldblum, X Ding, J Campbell-Washington, Am J Physiol 1993 264 4 Pt 1 894 C905 8476021
    • (1993) Am J Physiol , vol.264 , Issue.4 , pp. 3894-C905
    • Goldblum, S.E.1    Ding, X.2    Campbell-Washington, J.3
  • 37
    • 0029068086 scopus 로고
    • Tumor necrosis factor-alpha induces changes in the phosphorylation, cellular localization, and oligomerization of human hsp27, a stress protein that confers cellular resistance to this cytokine
    • 7673331
    • Tumor necrosis factor-alpha induces changes in the phosphorylation, cellular localization, and oligomerization of human hsp27, a stress protein that confers cellular resistance to this cytokine. P Mehlen, A Mehlen, D Guillet, X Preville, AP Arrigo, J Cell Biochem 1995 58 248 259 10.1002/jcb.240580213 7673331
    • (1995) J Cell Biochem , vol.58 , pp. 248-259
    • Mehlen, P.1    Mehlen, A.2    Guillet, D.3    Preville, X.4    Arrigo, A.P.5
  • 38
    • 0037013159 scopus 로고    scopus 로고
    • Inhibition of p38 MAPK Activation via Induction of MKP-1: Atrial Natriuretic Peptide Reduces TNF-alpha-Induced Actin Polymerization and Endothelial Permeability
    • 11988488
    • Inhibition of p38 MAPK Activation via Induction of MKP-1: Atrial Natriuretic Peptide Reduces TNF-alpha-Induced Actin Polymerization and Endothelial Permeability. AK Kiemer, NC Weber, R Fürst, N Bildner, S Kulhanek-Heinze, AM Vollmar, Circ Res 2002 90 874 881 10.1161/01.RES.0000017068.58856.F3 11988488
    • (2002) Circ Res , vol.90 , pp. 874-881
    • Kiemer, A.K.1    Weber, N.C.2    Fürst, R.3    Bildner, N.4    Kulhanek-Heinze, S.5    Vollmar, A.M.6
  • 39
    • 34548478100 scopus 로고    scopus 로고
    • Roles of Rho/ROCK and MLCK in TNF-alpha-induced changes in endothelial morphology and permeability
    • 17476691
    • Roles of Rho/ROCK and MLCK in TNF-alpha-induced changes in endothelial morphology and permeability. JAG McKenzie, AJ Ridley, J Cell Physiol 2007 213 221 228 10.1002/jcp.21114 17476691
    • (2007) J Cell Physiol , vol.213 , pp. 221-228
    • McKenzie, J.A.G.1    Ridley, A.J.2
  • 40
    • 0036357937 scopus 로고    scopus 로고
    • Molecular mechanisms of thrombin-induced endothelial cell permeability
    • 11841342
    • Molecular mechanisms of thrombin-induced endothelial cell permeability. NV Bogatcheva, JGN Garcia, AD Verin, Biochemistry 2002 67 75 84 11841342
    • (2002) Biochemistry , vol.67 , pp. 75-84
    • Bogatcheva, N.V.1    Garcia, J.G.N.2    Verin, A.D.3
  • 41
    • 34447258367 scopus 로고    scopus 로고
    • MK2 controls the level of negative feedback in the NF-kappaB pathway and is essential for vascular permeability and airway inflammation
    • 17576778
    • MK2 controls the level of negative feedback in the NF-kappaB pathway and is essential for vascular permeability and airway inflammation. MM Gorska, Q Liang, SJ Stafford, N Goplen, N Dharajiya, L Guo, S Sur, M Gaestel, R Alam, J Exp Med 2007 204 1637 1652 17576778
    • (2007) J Exp Med , vol.204 , pp. 1637-1652
    • Gorska, M.M.1    Liang, Q.2    Stafford, S.J.3    Goplen, N.4    Dharajiya, N.5    Guo, L.6    Sur, S.7    Gaestel, M.8    Alam, R.9
  • 42
    • 0026585007 scopus 로고
    • Anti-tumor necrosis factor antibody therapy fails to prevent lethality after cecal ligation and puncture or endotoxemia
    • 1315357
    • Anti-tumor necrosis factor antibody therapy fails to prevent lethality after cecal ligation and puncture or endotoxemia. MK Eskandari, G Bolgos, C Miller, DT Nguyen, LE DeForge, DG Remick, J Immunol 1992 148 2724 2730 1315357
    • (1992) J Immunol , vol.148 , pp. 2724-2730
    • Eskandari, M.K.1    Bolgos, G.2    Miller, C.3    Nguyen, D.T.4    Deforge, L.E.5    Remick, D.G.6
  • 43
    • 84888108831 scopus 로고    scopus 로고
    • What goes up must come down: Molecular basis of MAPKAP kinase 2/3-dependent regulation of the inflammatory response and its inhibition
    • 23832958
    • What goes up must come down: molecular basis of MAPKAP kinase 2/3-dependent regulation of the inflammatory response and its inhibition. M Gaestel, Biol Chem 2013 394 1301 1315 10.1515/hsz-2013-0197 23832958
    • (2013) Biol Chem , vol.394 , pp. 1301-1315
    • Gaestel, M.1
  • 44
    • 11144252660 scopus 로고    scopus 로고
    • MK2-/- gene knockout mouse hearts carry anti-apoptotic signal and are resistant to ischemia reperfusion injury
    • 15623425
    • MK2-/- gene knockout mouse hearts carry anti-apoptotic signal and are resistant to ischemia reperfusion injury. K Shiroto, H Otani, F Yamamoto, C-K Huang, N Maulik, DK Das, J Mol Cell Cardiol 2005 38 93 97 10.1016/j.yjmcc.2004.10.018 15623425
    • (2005) J Mol Cell Cardiol , vol.38 , pp. 93-97
    • Shiroto, K.1    Otani, H.2    Yamamoto, F.3    Huang, C.-K.4    Maulik, N.5    Das, D.K.6
  • 46
    • 61449154547 scopus 로고    scopus 로고
    • Immunodesign of experimental sepsis by cecal ligation and puncture
    • 19131954
    • Immunodesign of experimental sepsis by cecal ligation and puncture. D Rittirsch, MS Huber-Lang, MA Flierl, PA Ward, Nat Protoc 2009 4 31 36 10.1038/nprot.2008.214 19131954
    • (2009) Nat Protoc , vol.4 , pp. 31-36
    • Rittirsch, D.1    Huber-Lang, M.S.2    Flierl, M.A.3    Ward, P.A.4
  • 47
    • 62549105380 scopus 로고    scopus 로고
    • Hexosaminidase assays
    • 18473163
    • Hexosaminidase assays. M Wendeler, K Sandhoff, Glycoconj J 2009 26 945 952 10.1007/s10719-008-9137-5 18473163
    • (2009) Glycoconj J , vol.26 , pp. 945-952
    • Wendeler, M.1    Sandhoff, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.