메뉴 건너뛰기




Volumn 45, Issue 1, 2008, Pages 13-24

Tristetraprolin regulates TNF TNF-α mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways

Author keywords

MAP Kinase; Post transcriptional regulation; Proteasome; TNF ; Tristetraprolin

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; LIPOPOLYSACCHARIDE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEASOME; TRISTETRAPROLIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 34548241289     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2007.05.017     Document Type: Article
Times cited : (114)

References (61)
  • 1
    • 0033768306 scopus 로고    scopus 로고
    • Post-transcriptional regulation of tumour necrosis factor alpha production
    • Anderson P. Post-transcriptional regulation of tumour necrosis factor alpha production. Ann. Rheum. Dis. 59 Suppl. 1 (2000) i3-i5
    • (2000) Ann. Rheum. Dis. , vol.59 , Issue.SUPPL. 1
    • Anderson, P.1
  • 2
    • 0036093679 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha mRNA stability in human peripheral blood cells after lipopolysaccharide stimulation
    • Baseggio L., Charlot C., Bienvenu J., Felman P., and Salles G. Tumor necrosis factor-alpha mRNA stability in human peripheral blood cells after lipopolysaccharide stimulation. Eur. Cytokine Netw. 13 (2002) 92-98
    • (2002) Eur. Cytokine Netw. , vol.13 , pp. 92-98
    • Baseggio, L.1    Charlot, C.2    Bienvenu, J.3    Felman, P.4    Salles, G.5
  • 3
    • 0024405827 scopus 로고
    • The biology of cachectin/TNF-a primary mediator of the host response
    • Beutler B., and Cerami A. The biology of cachectin/TNF-a primary mediator of the host response. Annu. Rev. Immunol. 7 (1989) 625-655
    • (1989) Annu. Rev. Immunol. , vol.7 , pp. 625-655
    • Beutler, B.1    Cerami, A.2
  • 4
    • 0038518201 scopus 로고    scopus 로고
    • Tristetraprolin binds to the COX-2 mRNA 3′ untranslated region in cancer cells
    • Boutaud O., Dixon D.A., Oates J.A., and Sawaoka H. Tristetraprolin binds to the COX-2 mRNA 3′ untranslated region in cancer cells. Adv. Exp. Med. Biol. 525 (2003) 157-160
    • (2003) Adv. Exp. Med. Biol. , vol.525 , pp. 157-160
    • Boutaud, O.1    Dixon, D.A.2    Oates, J.A.3    Sawaoka, H.4
  • 5
    • 0034644837 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade
    • Brook M., Sully G., Clark A.R., and Saklatvala J. Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade. FEBS Lett. 483 (2000) 57-61
    • (2000) FEBS Lett. , vol.483 , pp. 57-61
    • Brook, M.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 6
    • 33644767306 scopus 로고    scopus 로고
    • Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways
    • Brook M., Tchen C.R., Santalucia T., McIlrath J., Arthur J.S., Saklatvala J., and Clark A.R. Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways. Mol. Cell Biol. 26 (2006) 2408-2418
    • (2006) Mol. Cell Biol. , vol.26 , pp. 2408-2418
    • Brook, M.1    Tchen, C.R.2    Santalucia, T.3    McIlrath, J.4    Arthur, J.S.5    Saklatvala, J.6    Clark, A.R.7
  • 7
    • 0036090190 scopus 로고    scopus 로고
    • Analysis of the function, expression, and subcellular distribution of human tristetraprolin
    • Brooks S.A., Connolly J.E., Diegel R.J., Fava R.A., and Rigby W.F. Analysis of the function, expression, and subcellular distribution of human tristetraprolin. Arthritis Rheum. 46 (2002) 1362-1370
    • (2002) Arthritis Rheum. , vol.46 , pp. 1362-1370
    • Brooks, S.A.1    Connolly, J.E.2    Diegel, R.J.3    Fava, R.A.4    Rigby, W.F.5
  • 8
    • 2942623942 scopus 로고    scopus 로고
    • The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway
    • Brooks S.A., Connolly J.E., and Rigby W.F. The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway. J. Immunol. 172 (2004) 7263-7271
    • (2004) J. Immunol. , vol.172 , pp. 7263-7271
    • Brooks, S.A.1    Connolly, J.E.2    Rigby, W.F.3
  • 9
    • 2442656756 scopus 로고    scopus 로고
    • Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein
    • Cao H., Tuttle J.S., and Blackshear P.J. Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein. J. Biol. Chem. 279 (2004) 21489-21499
    • (2004) J. Biol. Chem. , vol.279 , pp. 21489-21499
    • Cao, H.1    Tuttle, J.S.2    Blackshear, P.J.3
  • 10
    • 0030882906 scopus 로고    scopus 로고
    • Bone marrow transplantation reproduces the tristetraprolin-deficiency syndrome in recombination activating gene-2 (-/-) mice, Evidence that monocyte/macrophage progenitors may be responsible for TNFalpha overproduction
    • Carballo E., Gilkeson G.S., and Blackshear P.J. Bone marrow transplantation reproduces the tristetraprolin-deficiency syndrome in recombination activating gene-2 (-/-) mice, Evidence that monocyte/macrophage progenitors may be responsible for TNFalpha overproduction. J. Clin. Invest. 100 (1997) 986-995
    • (1997) J. Clin. Invest. , vol.100 , pp. 986-995
    • Carballo, E.1    Gilkeson, G.S.2    Blackshear, P.J.3
  • 11
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo E., Lai W.S., and Blackshear P.J. Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science 281 (1998) 1001-1005
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 12
    • 0034653560 scopus 로고    scopus 로고
    • Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability
    • Carballo E., Lai W.S., and Blackshear P.J. Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability. Blood 95 (2000) 1891-1899
    • (2000) Blood , vol.95 , pp. 1891-1899
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 13
    • 0028788194 scopus 로고
    • AU-rich elements: characterization and importance in mRNA degradation
    • Chen C.Y., and Shyu A.B. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci. 20 (1995) 465-470
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.B.2
  • 15
    • 0036884621 scopus 로고    scopus 로고
    • Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages
    • Chen P., Li J., Barnes J., Kokkonen G.C., Lee J.C., and Liu Y. Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J. Immunol. 169 (2002) 6408-6416
    • (2002) J. Immunol. , vol.169 , pp. 6408-6416
    • Chen, P.1    Li, J.2    Barnes, J.3    Kokkonen, G.C.4    Lee, J.C.5    Liu, Y.6
  • 16
    • 33745000728 scopus 로고    scopus 로고
    • Differential regulation of ARE-mediated TNFalpha and IL-1beta mRNA stability by lipopolysaccharide in RAW2647 cells
    • Chen Y.L., Huang Y.L., Lin N.Y., Chen H.C., Chiu W.C., and Chang C.J. Differential regulation of ARE-mediated TNFalpha and IL-1beta mRNA stability by lipopolysaccharide in RAW2647 cells. Biochem. Biophys. Res. Commun. 346 (2006) 160-168
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 160-168
    • Chen, Y.L.1    Huang, Y.L.2    Lin, N.Y.3    Chen, H.C.4    Chiu, W.C.5    Chang, C.J.6
  • 17
    • 2342630414 scopus 로고    scopus 로고
    • Implications of proteasome inhibition: an enhanced macrophage phenotype
    • Cuschieri J., Gourlay D., Garcia I., Jelacic S., and Maier R.V. Implications of proteasome inhibition: an enhanced macrophage phenotype. Cell Immunol. 227 (2004) 140-147
    • (2004) Cell Immunol. , vol.227 , pp. 140-147
    • Cuschieri, J.1    Gourlay, D.2    Garcia, I.3    Jelacic, S.4    Maier, R.V.5
  • 18
    • 0034746363 scopus 로고    scopus 로고
    • The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR
    • Dean J.L., Wait R., Mahtani K.R., Sully G., Clark A.R., and Saklatvala J. The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR. Mol. Cell Biol. 21 (2001) 721-730
    • (2001) Mol. Cell Biol. , vol.21 , pp. 721-730
    • Dean, J.L.1    Wait, R.2    Mahtani, K.R.3    Sully, G.4    Clark, A.R.5    Saklatvala, J.6
  • 20
    • 0032526427 scopus 로고    scopus 로고
    • Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs
    • Fan X.C., and Steitz J.A. Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J. 17 (1998) 3448-3460
    • (1998) EMBO J. , vol.17 , pp. 3448-3460
    • Fan, X.C.1    Steitz, J.A.2
  • 21
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • Fenger-Gron M., Fillman C., Norrild B., and Lykke-Andersen J. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell. 20 (2005) 905-915
    • (2005) Mol. Cell. , vol.20 , pp. 905-915
    • Fenger-Gron, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 22
    • 0028535921 scopus 로고
    • Lipopolysaccharide signals activation of tumor necrosis factor biosynthesis through the ras/raf-1/MEK/MAPK pathway
    • Geppert T.D., Whitehurst C.E., Thompson P., and Beutler B. Lipopolysaccharide signals activation of tumor necrosis factor biosynthesis through the ras/raf-1/MEK/MAPK pathway. Mol. Med. 1 (1994) 93-103
    • (1994) Mol. Med. , vol.1 , pp. 93-103
    • Geppert, T.D.1    Whitehurst, C.E.2    Thompson, P.3    Beutler, B.4
  • 23
    • 0025912577 scopus 로고
    • Complex regulation of tumor necrosis factor mRNA turnover in lipopolysaccharide-activated macrophages
    • Han J.H., Beutler B., and Huez G. Complex regulation of tumor necrosis factor mRNA turnover in lipopolysaccharide-activated macrophages. Biochim. Biophys. Acta 1090 (1991) 22-28
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 22-28
    • Han, J.H.1    Beutler, B.2    Huez, G.3
  • 24
    • 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
    • Hitti E., Iakovleva T., Brook M., Deppenmeier S., Gruber A.D., Radzioch D., Clark A.R., Blackshear P.J., Kotlyarov A., and Gaestel M. 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. Mol. Cell Biol. 26 (2006) 2399-2407
    • (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
  • 26
    • 0346505340 scopus 로고    scopus 로고
    • The IKK NF-kappa B system: a treasure trove for drug development
    • Karin M., Yamamoto Y., and Wang Q.M. The IKK NF-kappa B system: a treasure trove for drug development. Nat. Rev. 3 (2004) 17-26
    • (2004) Nat. Rev. , vol.3 , pp. 17-26
    • Karin, M.1    Yamamoto, Y.2    Wang, Q.M.3
  • 27
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha N., and Anderson P. Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 30 (2001) 963-969
    • (2001) Biochem. Soc. Trans. , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 29
    • 0033103805 scopus 로고    scopus 로고
    • Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies
    • Kontoyiannis D., Pasparakis M., Pizarro T.T., Cominelli F., and Kollias G. Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies. Immunity 10 (1999) 387-398
    • (1999) Immunity , vol.10 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3    Cominelli, F.4    Kollias, G.5
  • 34
    • 0037088665 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA: non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs
    • Lai W.S., Kennington E.A., and Blackshear P.J. Interactions of CCCH zinc finger proteins with mRNA: non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs. J. Biol. Chem. 277 (2002) 9606-9613
    • (2002) J. Biol. Chem. , vol.277 , pp. 9606-9613
    • Lai, W.S.1    Kennington, E.A.2    Blackshear, P.J.3
  • 35
    • 33751566645 scopus 로고    scopus 로고
    • DUSP meet immunology: dual specificity MAPK phosphatases in control of the inflammatory response
    • Lang R., Hammer M., and Mages J. DUSP meet immunology: dual specificity MAPK phosphatases in control of the inflammatory response. J. Immunol. 177 (2006) 7497-7504
    • (2006) J. Immunol. , vol.177 , pp. 7497-7504
    • Lang, R.1    Hammer, M.2    Mages, J.3
  • 36
    • 0033574789 scopus 로고    scopus 로고
    • Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
    • Laroia G., Cuesta R., Brewer G., and Schneider R.J. Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284 (1999) 499-502
    • (1999) Science , vol.284 , pp. 499-502
    • Laroia, G.1    Cuesta, R.2    Brewer, G.3    Schneider, R.J.4
  • 37
    • 0037133276 scopus 로고    scopus 로고
    • Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs
    • Laroia G., Sarkar B., and Schneider R.J. Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 1842-1846
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1842-1846
    • Laroia, G.1    Sarkar, B.2    Schneider, R.J.3
  • 38
    • 24144499990 scopus 로고    scopus 로고
    • Involvement of KSRP in the post-transcriptional regulation of human iNOS expression-complex interplay of KSRP with TTP and HuR
    • Linker K., Pautz A., Fechir M., Hubrich T., Greeve J., and Kleinert H. Involvement of KSRP in the post-transcriptional regulation of human iNOS expression-complex interplay of KSRP with TTP and HuR. Nucleic Acids Res. 33 (2005) 4813-4827
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4813-4827
    • Linker, K.1    Pautz, A.2    Fechir, M.3    Hubrich, T.4    Greeve, J.5    Kleinert, H.6
  • 39
    • 13244298460 scopus 로고    scopus 로고
    • Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1
    • Lykke-Andersen J., and Wagner E. Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Genes Dev. 19 (2005) 351-361
    • (2005) Genes Dev. , vol.19 , pp. 351-361
    • Lykke-Andersen, J.1    Wagner, E.2
  • 40
    • 0346734188 scopus 로고    scopus 로고
    • Dexamethasone inhibits IL-12p40 production in Lipopolysaccharide-stimulated human monocytic cells by down-regulating the activity of c-Jun N-terminal kinase, the activation protein-1, and NF-{kappa}B transcription factors
    • Ma W., Gee K., Lim W., Chambers K., Angel J.B., Kozlowski M., and Kumar A. Dexamethasone inhibits IL-12p40 production in Lipopolysaccharide-stimulated human monocytic cells by down-regulating the activity of c-Jun N-terminal kinase, the activation protein-1, and NF-{kappa}B transcription factors. J. Immunol. 172 (2004) 330
    • (2004) J. Immunol. , vol.172 , pp. 330
    • Ma, W.1    Gee, K.2    Lim, W.3    Chambers, K.4    Angel, J.B.5    Kozlowski, M.6    Kumar, A.7
  • 41
    • 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 K.R., Brook M., Dean J.L., Sully G., Saklatvala J., and Clark A.R. 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. 21 (2001) 6461-6469
    • (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
  • 42
    • 0034907223 scopus 로고    scopus 로고
    • Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase
    • Ming X.F., Stoecklin G., Lu M., Looser R., and Moroni C. Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase. Mol. Cell Biol. 21 (2001) 5778-5789
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5778-5789
    • Ming, X.F.1    Stoecklin, G.2    Lu, M.3    Looser, R.4    Moroni, C.5
  • 43
    • 0037080834 scopus 로고    scopus 로고
    • The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements
    • Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G., Lutz C.S., and Wilusz J. The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements. EMBO J. 21 (2002) 165-174
    • (2002) EMBO J. , vol.21 , pp. 165-174
    • Mukherjee, D.1    Gao, M.2    O'Connor, J.P.3    Raijmakers, R.4    Pruijn, G.5    Lutz, C.S.6    Wilusz, J.7
  • 44
    • 10844273239 scopus 로고    scopus 로고
    • Role of c-Jun N-terminal kinase on lipopolysaccharide induced maturation of human monocyte-derived dendritic cells
    • Nakahara T., Uchi H., Urabe K., Chen Q., Furue M., and Moroi Y. Role of c-Jun N-terminal kinase on lipopolysaccharide induced maturation of human monocyte-derived dendritic cells. Int. Immunol. 16 (2004) 1701-1709
    • (2004) Int. Immunol. , vol.16 , pp. 1701-1709
    • Nakahara, T.1    Uchi, H.2    Urabe, K.3    Chen, Q.4    Furue, M.5    Moroi, Y.6
  • 45
    • 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
    • Neininger A., Kontoyiannis D., Kotlyarov A., Winzen R., Eckert R., Volk H.D., Holtmann H., Kollias G., and Gaestel M. MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels. J. Biol. Chem. 277 (2002) 3065-3068
    • (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
  • 46
    • 11844278314 scopus 로고    scopus 로고
    • Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay
    • Ogilvie R.L., Abelson M., Hau H.H., Vlasova I., Blackshear P.J., and Bohjanen P.R. Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay. J. Immunol. 174 (2005) 953-961
    • (2005) J. Immunol. , vol.174 , pp. 953-961
    • Ogilvie, R.L.1    Abelson, M.2    Hau, H.H.3    Vlasova, I.4    Blackshear, P.J.5    Bohjanen, P.R.6
  • 47
    • 0032526417 scopus 로고    scopus 로고
    • RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein
    • Peng S.S., Chen C.Y., Xu N., and Shyu A.B. RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J. 17 (1998) 3461-3470
    • (1998) EMBO J. , vol.17 , pp. 3461-3470
    • Peng, S.S.1    Chen, C.Y.2    Xu, N.3    Shyu, A.B.4
  • 48
    • 1242341962 scopus 로고    scopus 로고
    • Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor alpha, cyclooxygenase 2, and inflammatory arthritis
    • Phillips K., Kedersha N., Shen L., Blackshear P.J., and Anderson P. Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor alpha, cyclooxygenase 2, and inflammatory arthritis. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 2011-2016
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2011-2016
    • Phillips, K.1    Kedersha, N.2    Shen, L.3    Blackshear, P.J.4    Anderson, P.5
  • 50
    • 0042847104 scopus 로고    scopus 로고
    • The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events
    • Qureshi N., Perera P.Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., and Vogel S.N. The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events. J. Immunol. 171 (2003) 1515-1525
    • (2003) J. Immunol. , vol.171 , pp. 1515-1525
    • Qureshi, N.1    Perera, P.Y.2    Shen, J.3    Zhang, G.4    Lenschat, A.5    Splitter, G.6    Morrison, D.C.7    Vogel, S.N.8
  • 51
    • 0031964902 scopus 로고    scopus 로고
    • Relative contribution of transcription and translation to the induction of tumor necrosis factor-alpha by lipopolysaccharide
    • Raabe T., Bukrinsky M., and Currie R.A. Relative contribution of transcription and translation to the induction of tumor necrosis factor-alpha by lipopolysaccharide. J. Biol. Chem. 273 (1998) 974-980
    • (1998) J. Biol. Chem. , vol.273 , pp. 974-980
    • Raabe, T.1    Bukrinsky, M.2    Currie, R.A.3
  • 52
    • 20444414937 scopus 로고    scopus 로고
    • Structure/function analysis of tristetraprolin (TTP): p38 stress-activated protein kinase and lipopolysaccharide stimulation do not alter TTP function
    • Rigby W., Roy K., Collins J., Rigby S., Connolly J., Bloch D., and Brooks S. Structure/function analysis of tristetraprolin (TTP): p38 stress-activated protein kinase and lipopolysaccharide stimulation do not alter TTP function. J. Immunol. 174 (2005) 7883-7893
    • (2005) J. Immunol. , vol.174 , pp. 7883-7893
    • Rigby, W.1    Roy, K.2    Collins, J.3    Rigby, S.4    Connolly, J.5    Bloch, D.6    Brooks, S.7
  • 53
    • 0035794225 scopus 로고    scopus 로고
    • Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factor-alpha (TNF-alpha) mRNA induction. Evidence for selective destabilization of TNF-alpha transcripts
    • Rutault K., Hazzalin C.A., and Mahadevan L.C. Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factor-alpha (TNF-alpha) mRNA induction. Evidence for selective destabilization of TNF-alpha transcripts. J. Biol. Chem. 276 (2001) 6666-6674
    • (2001) J. Biol. Chem. , vol.276 , pp. 6666-6674
    • Rutault, K.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 54
    • 0034073984 scopus 로고    scopus 로고
    • Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway
    • Stoecklin G., Ming X.F., Looser R., and Moroni C. Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway. Mol. Cell Biol. 20 (2000) 3753-3763
    • (2000) Mol. Cell Biol. , vol.20 , pp. 3753-3763
    • Stoecklin, G.1    Ming, X.F.2    Looser, R.3    Moroni, C.4
  • 55
    • 0038641941 scopus 로고    scopus 로고
    • A constitutive decay element promotes tumor necrosis factor alpha mRNA degradation via an AU-rich element-independent pathway
    • Stoecklin G., Lu M., Rattenbacher B., and Moroni C. A constitutive decay element promotes tumor necrosis factor alpha mRNA degradation via an AU-rich element-independent pathway. Mol. Cell Biol. 23 (2003) 3506-3515
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3506-3515
    • Stoecklin, G.1    Lu, M.2    Rattenbacher, B.3    Moroni, C.4
  • 56
    • 1942471656 scopus 로고    scopus 로고
    • MK2-induced tristetraprolin: 14-3-3 complexes prevent stress granule association and ARE-mRNA decay
    • Stoecklin G., Stubbs T., Kedersha N., Wax S., Rigby W.F., Blackwell T.K., and Anderson P. MK2-induced tristetraprolin: 14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 23 (2004) 1313-1324
    • (2004) EMBO J. , vol.23 , pp. 1313-1324
    • Stoecklin, G.1    Stubbs, T.2    Kedersha, N.3    Wax, S.4    Rigby, W.F.5    Blackwell, T.K.6    Anderson, P.7
  • 57
    • 0030881742 scopus 로고    scopus 로고
    • Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK
    • Swantek J.L., Cobb M.H., and Geppert T.D. Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK. Mol. Cell Biol. 17 (1997) 6274-6282
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6274-6282
    • Swantek, J.L.1    Cobb, M.H.2    Geppert, T.D.3
  • 60
    • 0035925538 scopus 로고    scopus 로고
    • Superinduction of TNF-a and IL-6 in macrophages by vomitoxin (deoxynivalenol) modulated by mRNA stabilization
    • Wonga S., Schwartz R.C., and Pestka J.J. Superinduction of TNF-a and IL-6 in macrophages by vomitoxin (deoxynivalenol) modulated by mRNA stabilization. Toxicology 161 (2001) 139-149
    • (2001) Toxicology , vol.161 , pp. 139-149
    • Wonga, S.1    Schwartz, R.C.2    Pestka, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.