메뉴 건너뛰기




Volumn 1829, Issue 6-7, 2013, Pages 666-679

Tristetraprolin (TTP): Interactions with mRNA and proteins, and current thoughts on mechanisms of action

Author keywords

AU rich element; MRNA stability; MRNA translation; Post transcriptional regulation; Tristetraprolin

Indexed keywords

ADENOSINE; BINDING PROTEIN; MESSENGER RNA; TRISTETRAPROLIN; TUMOR NECROSIS FACTOR ALPHA; ZINC FINGER PROTEIN;

EID: 84877793134     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2013.02.003     Document Type: Review
Times cited : (317)

References (199)
  • 1
    • 34047226825 scopus 로고    scopus 로고
    • Aberrant regulation of messenger RNA 3'-untranslated region in human cancer
    • Lopez de Silanes I., Quesada M.P., Esteller M. Aberrant regulation of messenger RNA 3'-untranslated region in human cancer. Cell. Oncol. 2007, 29:1-17.
    • (2007) Cell. Oncol. , vol.29 , pp. 1-17
    • Lopez de Silanes, I.1    Quesada, M.P.2    Esteller, M.3
  • 2
    • 35348828470 scopus 로고    scopus 로고
    • MRNA stability and cancer: an emerging link?
    • Benjamin D., Moroni C. mRNA stability and cancer: an emerging link?. Expert. Opin. Biol. Ther. 2007, 7:1515-1529.
    • (2007) Expert. Opin. Biol. Ther. , vol.7 , pp. 1515-1529
    • Benjamin, D.1    Moroni, C.2
  • 3
    • 84859254923 scopus 로고    scopus 로고
    • Sequence variations affecting AU-rich element function and disease
    • Hitti E., Khabar K.S. Sequence variations affecting AU-rich element function and disease. Front. Biosci. 2012, 17:1846-1860.
    • (2012) Front. Biosci. , vol.17 , pp. 1846-1860
    • Hitti, E.1    Khabar, K.S.2
  • 4
    • 84857464812 scopus 로고    scopus 로고
    • Networks controlling mRNA decay in the immune system
    • Schott J., Stoecklin G. Networks controlling mRNA decay in the immune system. Wiley Interdiscip. Rev. RNA 2010, 1:432-456.
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 432-456
    • Schott, J.1    Stoecklin, G.2
  • 5
  • 7
    • 38549113982 scopus 로고    scopus 로고
    • ARED Organism: expansion of ARED reveals AU-rich element cluster variations between human and mouse
    • Halees A.S., El-Badrawi R., Khabar K.S. ARED Organism: expansion of ARED reveals AU-rich element cluster variations between human and mouse. Nucleic Acids Res. 2008, 36:D137-D140.
    • (2008) Nucleic Acids Res. , vol.36
    • Halees, A.S.1    El-Badrawi, R.2    Khabar, K.S.3
  • 8
    • 73949130070 scopus 로고    scopus 로고
    • Dissecting the expression dynamics of RNA-binding proteins in posttranscriptional regulatory networks
    • Mittal N., Roy N., Babu M.M., Janga S.C. Dissecting the expression dynamics of RNA-binding proteins in posttranscriptional regulatory networks. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:20300-20305.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20300-20305
    • Mittal, N.1    Roy, N.2    Babu, M.M.3    Janga, S.C.4
  • 9
    • 0025051298 scopus 로고
    • Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein
    • Lai W.S., Stumpo D.J., Blackshear P.J. Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein. J. Biol. Chem. 1990, 265:16556-16563.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16556-16563
    • Lai, W.S.1    Stumpo, D.J.2    Blackshear, P.J.3
  • 10
    • 0025001736 scopus 로고
    • A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence
    • DuBois R.N., McLane M.W., Ryder K., Lau L.F., Nathans D. A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence. J. Biol. Chem. 1990, 265:19185-19191.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19185-19191
    • DuBois, R.N.1    McLane, M.W.2    Ryder, K.3    Lau, L.F.4    Nathans, D.5
  • 11
    • 0024580248 scopus 로고
    • Nucleotide sequence of a cDNA encoding TIS11, a message induced in Swiss 3T3 cells by the tumor promoter tetradecanoyl phorbol acetate
    • Varnum B.C., Lim R.W., Sukhatme V.P., Herschman H.R. Nucleotide sequence of a cDNA encoding TIS11, a message induced in Swiss 3T3 cells by the tumor promoter tetradecanoyl phorbol acetate. Oncogene 1989, 4:119-120.
    • (1989) Oncogene , vol.4 , pp. 119-120
    • Varnum, B.C.1    Lim, R.W.2    Sukhatme, V.P.3    Herschman, H.R.4
  • 12
    • 0025868519 scopus 로고
    • A corrected sequence for the predicted protein from the mitogen-inducible TIS11 primary response gene
    • Ma Q., Herschman H.R. A corrected sequence for the predicted protein from the mitogen-inducible TIS11 primary response gene. Oncogene 1991, 6:1277-1278.
    • (1991) Oncogene , vol.6 , pp. 1277-1278
    • Ma, Q.1    Herschman, H.R.2
  • 13
    • 0025915286 scopus 로고
    • The human TTP protein: sequence, alignment with related proteins, and chromosomal localization of the mouse and human genes
    • Taylor G.A. The human TTP protein: sequence, alignment with related proteins, and chromosomal localization of the mouse and human genes. Nucleic Acids Res. 1991, 19:3454.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3454
    • Taylor, G.A.1
  • 14
    • 0027530675 scopus 로고
    • A human putative lymphocyte G0/G1 switch gene homologous to a rodent gene encoding a zinc-binding potential transcription factor
    • Heximer S.P., Forsdyke D.R. A human putative lymphocyte G0/G1 switch gene homologous to a rodent gene encoding a zinc-binding potential transcription factor. DNA Cell Biol. 1993, 12:73-88.
    • (1993) DNA Cell Biol. , vol.12 , pp. 73-88
    • Heximer, S.P.1    Forsdyke, D.R.2
  • 15
    • 0029016832 scopus 로고
    • Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro
    • Taylor G.A., Thompson M.J., Lai W.S., Blackshear P.J. Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro. J. Biol. Chem. 1995, 270:13341-13347.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13341-13347
    • Taylor, G.A.1    Thompson, M.J.2    Lai, W.S.3    Blackshear, P.J.4
  • 16
    • 0030034403 scopus 로고    scopus 로고
    • Mitogens stimulate the rapid nuclear to cytosolic translocation of tristetraprolin, a potential zinc-finger transcription factor
    • Taylor G.A., Thompson M.J., Lai W.S., Blackshear P.J. Mitogens stimulate the rapid nuclear to cytosolic translocation of tristetraprolin, a potential zinc-finger transcription factor. Mol. Endocrinol. (Baltimore, Md.) 1996, 10:140-146.
    • (1996) Mol. Endocrinol. (Baltimore, Md.) , vol.10 , pp. 140-146
    • Taylor, G.A.1    Thompson, M.J.2    Lai, W.S.3    Blackshear, P.J.4
  • 17
    • 0028906856 scopus 로고
    • Zinc inhibits turnover of labile mRNAs in intact cells
    • Taylor G.A., Blackshear P.J. Zinc inhibits turnover of labile mRNAs in intact cells. J. Cell. Physiol. 1995, 162:378-387.
    • (1995) J. Cell. Physiol. , vol.162 , pp. 378-387
    • Taylor, G.A.1    Blackshear, P.J.2
  • 18
    • 0028810250 scopus 로고
    • Promoter analysis of Zfp-36, the mitogen-inducible gene encoding the zinc finger protein tristetraprolin
    • Lai W.S., Thompson M.J., Taylor G.A., Liu Y., Blackshear P.J. Promoter analysis of Zfp-36, the mitogen-inducible gene encoding the zinc finger protein tristetraprolin. J. Biol. Chem. 1995, 270:25266-25272.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25266-25272
    • Lai, W.S.1    Thompson, M.J.2    Taylor, G.A.3    Liu, Y.4    Blackshear, P.J.5
  • 20
    • 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., 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. 1997, 100:986-995.
    • (1997) J. Clin. Invest. , vol.100 , pp. 986-995
    • Carballo, E.1    Gilkeson, G.S.2    Blackshear, P.J.3
  • 21
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo E., Lai W.S., Blackshear P.J. Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science (New York, N.Y.) 1998, 281:1001-1005.
    • (1998) Science (New York, N.Y.) , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 22
    • 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., Kollias G. Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies. Immunity 1999, 10:387-398.
    • (1999) Immunity , vol.10 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3    Cominelli, F.4    Kollias, G.5
  • 23
    • 84861135683 scopus 로고    scopus 로고
    • Myeloid-specific tristetraprolin deficiency in mice results in extreme lipopolysaccharide sensitivity in an otherwise minimal phenotype
    • Qiu L.Q., Stumpo D.J., Blackshear P.J. Myeloid-specific tristetraprolin deficiency in mice results in extreme lipopolysaccharide sensitivity in an otherwise minimal phenotype. J. Immunol. 2012, 188:5150-5159.
    • (2012) J. Immunol. , vol.188 , pp. 5150-5159
    • Qiu, L.Q.1    Stumpo, D.J.2    Blackshear, P.J.3
  • 25
    • 0038504080 scopus 로고    scopus 로고
    • Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates
    • Blackshear P.J., Lai W.S., Kennington E.A., Brewer G., Wilson G.M., Guan X., Zhou P. Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates. J. Biol. Chem. 2003, 278:19947-19955.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19947-19955
    • Blackshear, P.J.1    Lai, W.S.2    Kennington, E.A.3    Brewer, G.4    Wilson, G.M.5    Guan, X.6    Zhou, P.7
  • 27
    • 0034625369 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA
    • Lai W.S., Carballo E., Thorn J.M., Kennington E.A., Blackshear P.J. Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA. J. Biol. Chem. 2000, 275:17827-17837.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17827-17837
    • Lai, W.S.1    Carballo, E.2    Thorn, J.M.3    Kennington, E.A.4    Blackshear, P.J.5
  • 28
    • 3142615474 scopus 로고    scopus 로고
    • RNA sequence elements required for high affinity binding by the zinc finger domain of tristetraprolin: conformational changes coupled to the bipartite nature of Au-rich MRNA-destabilizing motifs
    • Brewer B.Y., Malicka J., Blackshear P.J., Wilson G.M. RNA sequence elements required for high affinity binding by the zinc finger domain of tristetraprolin: conformational changes coupled to the bipartite nature of Au-rich MRNA-destabilizing motifs. J. Biol. Chem. 2004, 279:27870-27877.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27870-27877
    • Brewer, B.Y.1    Malicka, J.2    Blackshear, P.J.3    Wilson, G.M.4
  • 30
    • 8544255551 scopus 로고    scopus 로고
    • The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis
    • Carrick D.M., Lai W.S., Blackshear P.J. The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis. Arthritis Res. Ther. 2004, 6:248-264.
    • (2004) Arthritis Res. Ther. , vol.6 , pp. 248-264
    • Carrick, D.M.1    Lai, W.S.2    Blackshear, P.J.3
  • 31
    • 22544459628 scopus 로고    scopus 로고
    • Zfp36l3, a rodent X chromosome gene encoding a placenta-specific member of the Tristetraprolin family of CCCH tandem zinc finger proteins
    • Blackshear P.J., Phillips R.S., Ghosh S., Ramos S.B., Richfield E.K., Lai W.S. Zfp36l3, a rodent X chromosome gene encoding a placenta-specific member of the Tristetraprolin family of CCCH tandem zinc finger proteins. Biol. Reprod. 2005, 73:297-307.
    • (2005) Biol. Reprod. , vol.73 , pp. 297-307
    • Blackshear, P.J.1    Phillips, R.S.2    Ghosh, S.3    Ramos, S.B.4    Richfield, E.K.5    Lai, W.S.6
  • 32
    • 0033522136 scopus 로고    scopus 로고
    • Identification of four CCCH zinc finger proteins in Xenopus, including a novel vertebrate protein with four zinc fingers and severely restricted expression
    • De J., Lai W.S., Thorn J.M., Goldsworthy S.M., Liu X., Blackwell T.K., Blackshear P.J. Identification of four CCCH zinc finger proteins in Xenopus, including a novel vertebrate protein with four zinc fingers and severely restricted expression. Gene 1999, 228:133-145.
    • (1999) Gene , vol.228 , pp. 133-145
    • De, J.1    Lai, W.S.2    Thorn, J.M.3    Goldsworthy, S.M.4    Liu, X.5    Blackwell, T.K.6    Blackshear, P.J.7
  • 33
    • 42549107372 scopus 로고    scopus 로고
    • A deadenylation negative feedback mechanism governs meiotic metaphase arrest
    • Belloc E., Mendez R. A deadenylation negative feedback mechanism governs meiotic metaphase arrest. Nature 2008, 452:1017-1021.
    • (2008) Nature , vol.452 , pp. 1017-1021
    • Belloc, E.1    Mendez, R.2
  • 34
    • 77955572742 scopus 로고    scopus 로고
    • Structure and function of nematode RNA-binding proteins
    • Kaymak E., Wee L.M., Ryder S.P. Structure and function of nematode RNA-binding proteins. Curr. Opin. Struct. Biol. 2010, 20:305-312.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 305-312
    • Kaymak, E.1    Wee, L.M.2    Ryder, S.P.3
  • 35
    • 0035889121 scopus 로고    scopus 로고
    • Roles of tumor necrosis factor-alpha receptor subtypes in the pathogenesis of the tristetraprolin-deficiency syndrome
    • Carballo E., Blackshear P.J. Roles of tumor necrosis factor-alpha receptor subtypes in the pathogenesis of the tristetraprolin-deficiency syndrome. Blood 2001, 98:2389-2395.
    • (2001) Blood , vol.98 , pp. 2389-2395
    • Carballo, E.1    Blackshear, P.J.2
  • 36
    • 33845431240 scopus 로고    scopus 로고
    • Novel mRNA targets for tristetraprolin (TTP) identified by global analysis of stabilized transcripts in TTP-deficient fibroblasts
    • Lai W.S., Parker J.S., Grissom S.F., Stumpo D.J., Blackshear P.J. Novel mRNA targets for tristetraprolin (TTP) identified by global analysis of stabilized transcripts in TTP-deficient fibroblasts. Mol. Cell. Biol. 2006, 26:9196-9208.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9196-9208
    • Lai, W.S.1    Parker, J.S.2    Grissom, S.F.3    Stumpo, D.J.4    Blackshear, P.J.5
  • 37
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3' untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G., Kamen R. A conserved AU sequence from the 3' untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 1986, 46:659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 38
    • 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., Blackshear P.J. Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability. Blood 2000, 95:1891-1899.
    • (2000) Blood , vol.95 , pp. 1891-1899
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 39
    • 0033049125 scopus 로고    scopus 로고
    • Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA
    • Lai W.S., Carballo E., Strum J.R., Kennington E.A., Phillips R.S., Blackshear P.J. Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA. Mol. Cell. Biol. 1999, 19:4311-4323.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4311-4323
    • Lai, W.S.1    Carballo, E.2    Strum, J.R.3    Kennington, E.A.4    Phillips, R.S.5    Blackshear, P.J.6
  • 40
    • 0038751970 scopus 로고    scopus 로고
    • Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease
    • Lai W.S., Kennington E.A., Blackshear P.J. Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol. Cell. Biol. 2003, 23:3798-3812.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3798-3812
    • Lai, W.S.1    Kennington, E.A.2    Blackshear, P.J.3
  • 41
    • 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., Moroni C. Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway. Mol. Cell. Biol. 2000, 20:3753-3763.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3753-3763
    • Stoecklin, G.1    Ming, X.F.2    Looser, R.3    Moroni, C.4
  • 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., Moroni C. Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase. Mol. Cell. Biol. 2001, 21:5778-5789.
    • (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
    • 0035930565 scopus 로고    scopus 로고
    • HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities
    • Raghavan A., Robison R.L., McNabb J., Miller C.R., Williams D.A., Bohjanen P.R. HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities. J. Biol. Chem. 2001, 276:47958-47965.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47958-47965
    • Raghavan, A.1    Robison, R.L.2    McNabb, J.3    Miller, C.R.4    Williams, D.A.5    Bohjanen, P.R.6
  • 46
    • 55049142198 scopus 로고    scopus 로고
    • TNF-alpha stimulation inhibits siRNA-mediated RNA interference through a mechanism involving poly-(A) tail stabilization
    • Mols J., van den Berg A., Otsuka M., Zheng M., Chen J., Han J. TNF-alpha stimulation inhibits siRNA-mediated RNA interference through a mechanism involving poly-(A) tail stabilization. Biochim. Biophys. Acta 2008, 1779:712-719.
    • (2008) Biochim. Biophys. Acta , vol.1779 , pp. 712-719
    • Mols, J.1    van den Berg, A.2    Otsuka, M.3    Zheng, M.4    Chen, J.5    Han, J.6
  • 47
    • 84855857708 scopus 로고    scopus 로고
    • AU-rich element-mediated mRNA decay can occur independently of the miRNA machinery in mouse embryonic fibroblasts and Drosophila S2-cells
    • Helfer S., Schott J., Stoecklin G., Forstemann K. AU-rich element-mediated mRNA decay can occur independently of the miRNA machinery in mouse embryonic fibroblasts and Drosophila S2-cells. PLoS One 2012, 7:e28907.
    • (2012) PLoS One , vol.7
    • Helfer, S.1    Schott, J.2    Stoecklin, G.3    Forstemann, K.4
  • 48
    • 70350374222 scopus 로고    scopus 로고
    • RNA-destabilizing factor tristetraprolin negatively regulates NF-kappaB signaling
    • Liang J., Lei T., Song Y., Yanes N., Qi Y., Fu M. RNA-destabilizing factor tristetraprolin negatively regulates NF-kappaB signaling. J. Biol. Chem. 2009, 284:29383-29390.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29383-29390
    • Liang, J.1    Lei, T.2    Song, Y.3    Yanes, N.4    Qi, Y.5    Fu, M.6
  • 50
    • 84859106748 scopus 로고    scopus 로고
    • Involvement of tristetraprolin in transcriptional activation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase by insulin
    • Ness G.C., Edelman J.L., Brooks P.A. Involvement of tristetraprolin in transcriptional activation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase by insulin. Biochem. Biophys. Res. Commun. 2012, 420:178-182.
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 178-182
    • Ness, G.C.1    Edelman, J.L.2    Brooks, P.A.3
  • 53
    • 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., 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. 2005, 33:4813-4827.
    • (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
  • 54
    • 37149001939 scopus 로고    scopus 로고
    • Phosphorylation site analysis of the anti-inflammatory and mRNA-destabilizing protein tristetraprolin
    • Cao H., Deterding L.J., Blackshear P.J. Phosphorylation site analysis of the anti-inflammatory and mRNA-destabilizing protein tristetraprolin. Expert Rev. Proteomics 2007, 4:711-726.
    • (2007) Expert Rev. Proteomics , vol.4 , pp. 711-726
    • Cao, H.1    Deterding, L.J.2    Blackshear, P.J.3
  • 55
    • 84856855006 scopus 로고    scopus 로고
    • Cullin 4B is recruited to tristetraprolin-containing messenger ribonucleoproteins and regulates TNF-alpha mRNA polysome loading
    • Pfeiffer J.R., Brooks S.A. Cullin 4B is recruited to tristetraprolin-containing messenger ribonucleoproteins and regulates TNF-alpha mRNA polysome loading. J. Immunol. 2012, 188:1828-1839.
    • (2012) J. Immunol. , vol.188 , pp. 1828-1839
    • Pfeiffer, J.R.1    Brooks, S.A.2
  • 56
    • 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., 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. 2006, 26:2399-2407.
    • (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
  • 57
    • 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
    • Deleault K.M., Skinner S.J., Brooks S.A. Tristetraprolin regulates TNF TNF-alpha mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways. Mol. Immunol. 2008, 45:13-24.
    • (2008) Mol. Immunol. , vol.45 , pp. 13-24
    • Deleault, K.M.1    Skinner, S.J.2    Brooks, S.A.3
  • 58
    • 0037376557 scopus 로고    scopus 로고
    • Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases
    • Cao H., Dzineku F., Blackshear P.J. Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases. Arch. Biochem. Biophys. 2003, 412:106-120.
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 106-120
    • Cao, H.1    Dzineku, F.2    Blackshear, P.J.3
  • 59
    • 0035834741 scopus 로고    scopus 로고
    • Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway
    • Carballo E., Cao H., Lai W.S., Kennington E.A., Campbell D., Blackshear P.J. Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway. J. Biol. Chem. 2001, 276:42580-42587.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42580-42587
    • Carballo, E.1    Cao, H.2    Lai, W.S.3    Kennington, E.A.4    Campbell, D.5    Blackshear, P.J.6
  • 61
    • 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., 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. 2001, 21:6461-6469.
    • (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
  • 62
    • 63849239758 scopus 로고    scopus 로고
    • Post-transcriptional gene regulation by MAP kinases via AU-rich elements
    • Clark A., Dean J., Tudor C., Saklatvala J. Post-transcriptional gene regulation by MAP kinases via AU-rich elements. Front. Biosci. 2009, 14:847-871.
    • (2009) Front. Biosci. , vol.14 , pp. 847-871
    • Clark, A.1    Dean, J.2    Tudor, C.3    Saklatvala, J.4
  • 63
    • 33947495156 scopus 로고    scopus 로고
    • Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA
    • Sun L., Stoecklin G., Van Way S., Hinkovska-Galcheva V., Guo R.F., Anderson P., Shanley T.P. Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA. J. Biol. Chem. 2007, 282:3766-3777.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3766-3777
    • Sun, L.1    Stoecklin, G.2    Van Way, S.3    Hinkovska-Galcheva, V.4    Guo, R.F.5    Anderson, P.6    Shanley, T.P.7
  • 65
    • 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.F., Roy K., Collins J., Rigby S., Connolly J.E., Bloch D.B., Brooks S.A. Structure/function analysis of tristetraprolin (TTP): p38 stress-activated protein kinase and lipopolysaccharide stimulation do not alter TTP function. J. Immunol. 2005, 174:7883-7893.
    • (2005) J. Immunol. , vol.174 , pp. 7883-7893
    • Rigby, W.F.1    Roy, K.2    Collins, J.3    Rigby, S.4    Connolly, J.E.5    Bloch, D.B.6    Brooks, S.A.7
  • 66
    • 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., Anderson P. MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 2004, 23:1313-1324.
    • (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
  • 67
    • 7244252846 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications
    • Cao H. Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications. Biochemistry 2004, 43:13724-13738.
    • (2004) Biochemistry , vol.43 , pp. 13724-13738
    • Cao, H.1
  • 68
    • 78751500752 scopus 로고    scopus 로고
    • CARHSP1 is required for effective tumor necrosis factor alpha mRNA stabilization and localizes to processing bodies and exosomes
    • Pfeiffer J.R., McAvoy B.L., Fecteau R.E., Deleault K.M., Brooks S.A. CARHSP1 is required for effective tumor necrosis factor alpha mRNA stabilization and localizes to processing bodies and exosomes. Mol. Cell. Biol. 2011, 31:277-286.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 277-286
    • Pfeiffer, J.R.1    McAvoy, B.L.2    Fecteau, R.E.3    Deleault, K.M.4    Brooks, S.A.5
  • 69
    • 78751504841 scopus 로고    scopus 로고
    • Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment
    • Clement S.L., Scheckel C., Stoecklin G., Lykke-Andersen J. Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol. Cell. Biol. 2011, 31:256-266.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 256-266
    • Clement, S.L.1    Scheckel, C.2    Stoecklin, G.3    Lykke-Andersen, J.4
  • 70
    • 77956261147 scopus 로고    scopus 로고
    • MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment
    • Marchese F.P., Aubareda A., Tudor C., Saklatvala J., Clark A.R., Dean J.L. MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment. J. Biol. Chem. 2010, 285:27590-27600.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27590-27600
    • Marchese, F.P.1    Aubareda, A.2    Tudor, C.3    Saklatvala, J.4    Clark, A.R.5    Dean, J.L.6
  • 72
    • 42449134926 scopus 로고    scopus 로고
    • The AU-rich element mRNA decay-promoting activity of BRF1 is regulated by mitogen-activated protein kinase-activated protein kinase 2
    • Maitra S., Chou C.F., Luber C.A., Lee K.Y., Mann M., Chen C.Y. The AU-rich element mRNA decay-promoting activity of BRF1 is regulated by mitogen-activated protein kinase-activated protein kinase 2. RNA 2008, 14:950-959.
    • (2008) RNA , vol.14 , pp. 950-959
    • Maitra, S.1    Chou, C.F.2    Luber, C.A.3    Lee, K.Y.4    Mann, M.5    Chen, C.Y.6
  • 73
    • 33749822544 scopus 로고    scopus 로고
    • Tristetraprolin regulates Cyclin D1 and c-Myc mRNA stability in response to rapamycin in an Akt-dependent manner via p38 MAPK signaling
    • Marderosian M., Sharma A., Funk A.P., Vartanian R., Masri J., Jo O.D., Gera J.F. Tristetraprolin regulates Cyclin D1 and c-Myc mRNA stability in response to rapamycin in an Akt-dependent manner via p38 MAPK signaling. Oncogene 2006, 25:6277-6290.
    • (2006) Oncogene , vol.25 , pp. 6277-6290
    • Marderosian, M.1    Sharma, A.2    Funk, A.P.3    Vartanian, R.4    Masri, J.5    Jo, O.D.6    Gera, J.F.7
  • 74
    • 33845436674 scopus 로고    scopus 로고
    • BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites
    • Benjamin D., Schmidlin M., Min L., Gross B., Moroni C. BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites. Mol. Cell. Biol. 2006, 26:9497-9507.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9497-9507
    • Benjamin, D.1    Schmidlin, M.2    Min, L.3    Gross, B.4    Moroni, C.5
  • 75
    • 79951592982 scopus 로고    scopus 로고
    • Implication of the ERK pathway on the post-transcriptional regulation of VEGF mRNA stability
    • Essafi-Benkhadir K., Pouyssegur J., Pages G. Implication of the ERK pathway on the post-transcriptional regulation of VEGF mRNA stability. Methods Mol. Biol. 2010, 661:451-469.
    • (2010) Methods Mol. Biol. , vol.661 , pp. 451-469
    • Essafi-Benkhadir, K.1    Pouyssegur, J.2    Pages, G.3
  • 76
    • 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., 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. 2006, 26:2408-2418.
    • (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
  • 77
    • 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., 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. 2004, 172:7263-7271.
    • (2004) J. Immunol. , vol.172 , pp. 7263-7271
    • Brooks, S.A.1    Connolly, J.E.2    Rigby, W.F.3
  • 78
    • 3543003469 scopus 로고    scopus 로고
    • The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 and by tristetraprolin itself
    • Tchen C.R., Brook M., Saklatvala J., Clark A.R. The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 and by tristetraprolin itself. J. Biol. Chem. 2004, 279:32393-32400.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32393-32400
    • Tchen, C.R.1    Brook, M.2    Saklatvala, J.3    Clark, A.R.4
  • 80
    • 58649117962 scopus 로고    scopus 로고
    • The mammalian nonsense-mediated mRNA decay pathway: to decay or not to decay! Which players make the decision?
    • Silva A.L., Romao L. The mammalian nonsense-mediated mRNA decay pathway: to decay or not to decay! Which players make the decision?. FEBS Lett. 2009, 583:499-505.
    • (2009) FEBS Lett. , vol.583 , pp. 499-505
    • Silva, A.L.1    Romao, L.2
  • 81
    • 56049126683 scopus 로고    scopus 로고
    • NMD: multitasking between mRNA surveillance and modulation of gene expression
    • Neu-Yilik G., Kulozik A.E. NMD: multitasking between mRNA surveillance and modulation of gene expression. Adv. Genet. 2008, 62:185-243.
    • (2008) Adv. Genet. , vol.62 , pp. 185-243
    • Neu-Yilik, G.1    Kulozik, A.E.2
  • 82
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof A., Frischmeyer P.A., Dietz H.C., Parker R. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 2002, 295:2262-2264.
    • (2002) Science , vol.295 , pp. 2262-2264
    • van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 84
    • 78449263431 scopus 로고    scopus 로고
    • No-go decay: a quality control mechanism for RNA in translation
    • Harigaya Y., Parker R. No-go decay: a quality control mechanism for RNA in translation. Wiley Interdiscip. Rev. RNA 2010, 1:132-141.
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 132-141
    • Harigaya, Y.1    Parker, R.2
  • 85
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: the complex lives of eukaryotic mRNAs
    • Moore M.J. From birth to death: the complex lives of eukaryotic mRNAs. Science 2005, 309:1514-1518.
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 88
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker R., Song H. The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol. 2004, 11:121-127.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 91
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R., Sheth U. P bodies and the control of mRNA translation and degradation. Mol. Cell 2007, 25:635-646.
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 92
    • 56849103665 scopus 로고    scopus 로고
    • The control of mRNA decapping and P-body formation
    • Franks T.M., Lykke-Andersen J. The control of mRNA decapping and P-body formation. Mol. Cell 2008, 32:605-615.
    • (2008) Mol. Cell , vol.32 , pp. 605-615
    • Franks, T.M.1    Lykke-Andersen, J.2
  • 93
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: post-transcriptional and epigenetic modulators of gene expression
    • Anderson P., Kedersha N. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 2009, 10:430-436.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 94
    • 34347335707 scopus 로고    scopus 로고
    • P-body formation is a consequence, not the cause, of RNA-mediated gene silencing
    • Eulalio A., Behm-Ansmant I., Schweizer D., Izaurralde E. P-body formation is a consequence, not the cause, of RNA-mediated gene silencing. Mol. Cell. Biol. 2007, 27:3970-3981.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3970-3981
    • Eulalio, A.1    Behm-Ansmant, I.2    Schweizer, D.3    Izaurralde, E.4
  • 95
    • 33947301293 scopus 로고    scopus 로고
    • TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements
    • Franks T.M., Lykke-Andersen J. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 2007, 21:719-735.
    • (2007) Genes Dev. , vol.21 , pp. 719-735
    • Franks, T.M.1    Lykke-Andersen, J.2
  • 96
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • Cougot N., Babajko S., Seraphin B. Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 2004, 165:31-40.
    • (2004) J. Cell Biol. , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Seraphin, B.3
  • 97
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain nontranslating mRNAs
    • Teixeira D., Sheth U., Valencia-Sanchez M.A., Brengues M., Parker R. Processing bodies require RNA for assembly and contain nontranslating mRNAs. RNA 2005, 11:371-382.
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 98
    • 0030027575 scopus 로고    scopus 로고
    • Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities
    • Dember L.M., Kim N.D., Liu K.Q., Anderson P. Individual RNA recognition motifs of TIA-1 and TIAR have different RNA binding specificities. J. Biol. Chem. 1996, 271:2783-2788.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2783-2788
    • Dember, L.M.1    Kim, N.D.2    Liu, K.Q.3    Anderson, P.4
  • 99
    • 0033593448 scopus 로고    scopus 로고
    • Identification of TIAR as a protein binding to the translational regulatory AU-rich element of tumor necrosis factor alpha mRNA
    • Gueydan C., Droogmans L., Chalon P., Huez G., Caput D., Kruys V. Identification of TIAR as a protein binding to the translational regulatory AU-rich element of tumor necrosis factor alpha mRNA. J. Biol. Chem. 1999, 274:2322-2326.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2322-2326
    • Gueydan, C.1    Droogmans, L.2    Chalon, P.3    Huez, G.4    Caput, D.5    Kruys, V.6
  • 104
  • 105
    • 41549107524 scopus 로고    scopus 로고
    • RNA recognition by 3'-to-5' exonucleases: the substrate perspective
    • Ibrahim H., Wilusz J., Wilusz C.J. RNA recognition by 3'-to-5' exonucleases: the substrate perspective. Biochim. Biophys. Acta 2008, 1779:256-265.
    • (2008) Biochim. Biophys. Acta , vol.1779 , pp. 256-265
    • Ibrahim, H.1    Wilusz, J.2    Wilusz, C.J.3
  • 107
    • 33646200678 scopus 로고    scopus 로고
    • ARE-mRNA degradation requires the 5'-3' decay pathway
    • Stoecklin G., Mayo T., Anderson P. ARE-mRNA degradation requires the 5'-3' decay pathway. EMBO Rep. 2006, 7:72-77.
    • (2006) EMBO Rep. , vol.7 , pp. 72-77
    • Stoecklin, G.1    Mayo, T.2    Anderson, P.3
  • 109
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha N., Anderson P. Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 2002, 30:963-969.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 110
    • 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., 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. 2004, 101:2011-2016.
    • (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
  • 111
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan J.R., Parker R. Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 2009, 36:932-941.
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 112
    • 0037101945 scopus 로고    scopus 로고
    • Stressful initiations
    • Anderson P., Kedersha N. Stressful initiations. J. Cell Sci. 2002, 115:3227-3234.
    • (2002) J. Cell Sci. , vol.115 , pp. 3227-3234
    • Anderson, P.1    Kedersha, N.2
  • 113
    • 79960928455 scopus 로고    scopus 로고
    • Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin
    • Sandler H., Kreth J., Timmers H.T., Stoecklin G. Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin. Nucleic Acids Res. 2011, 39:4373-4386.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 4373-4386
    • Sandler, H.1    Kreth, J.2    Timmers, H.T.3    Stoecklin, G.4
  • 114
    • 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., 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. 2005, 19:351-361.
    • (2005) Genes Dev. , vol.19 , pp. 351-361
    • Lykke-Andersen, J.1    Wagner, E.2
  • 115
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N., Hinnebusch A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 116
    • 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, 30:959-963.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 959-963
    • Kotlyarov, A.1    Gaestel, M.2
  • 117
    • 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., 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. 2002, 277:3065-3068.
    • (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
  • 120
    • 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., Lykke-Andersen J. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell 2005, 20:905-915.
    • (2005) Mol. Cell , vol.20 , pp. 905-915
    • Fenger-Gron, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 122
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J., Parker R. General translational repression by activators of mRNA decapping. Cell 2005, 122:875-886.
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 123
    • 0033773044 scopus 로고    scopus 로고
    • MRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E
    • Schwartz D.C., Parker R. mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 2000, 20:7933-7942.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7933-7942
    • Schwartz, D.C.1    Parker, R.2
  • 124
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae
    • Schwartz D.C., Parker R. Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 1999, 19:5247-5256.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5247-5256
    • Schwartz, D.C.1    Parker, R.2
  • 125
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth U., Parker R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 2003, 300:805-808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 126
    • 35648933435 scopus 로고    scopus 로고
    • T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs
    • Yamasaki S., Stoecklin G., Kedersha N., Simarro M., Anderson P. T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs. J. Biol. Chem. 2007, 282:30070-30077.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30070-30077
    • Yamasaki, S.1    Stoecklin, G.2    Kedersha, N.3    Simarro, M.4    Anderson, P.5
  • 128
    • 0038798677 scopus 로고    scopus 로고
    • A novel mechanism of tumor suppression by destabilizing AU-rich growth factor mRNA
    • Stoecklin G., Gross B., Ming X.F., Moroni C. A novel mechanism of tumor suppression by destabilizing AU-rich growth factor mRNA. Oncogene 2003, 22:3554-3561.
    • (2003) Oncogene , vol.22 , pp. 3554-3561
    • Stoecklin, G.1    Gross, B.2    Ming, X.F.3    Moroni, C.4
  • 130
    • 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., Sawaoka H. Tristetraprolin binds to the COX-2 mRNA 3' untranslated region in cancer cells. Adv. Exp. Med. Biol. 2003, 525:157-160.
    • (2003) Adv. Exp. Med. Biol. , vol.525 , pp. 157-160
    • Boutaud, O.1    Dixon, D.A.2    Oates, J.A.3    Sawaoka, H.4
  • 131
    • 0037853195 scopus 로고    scopus 로고
    • Tristetraprolin binds to the 3'-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site
    • Sawaoka H., Dixon D.A., Oates J.A., Boutaud O. Tristetraprolin binds to the 3'-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site. J. Biol. Chem. 2003, 278:13928-13935.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13928-13935
    • Sawaoka, H.1    Dixon, D.A.2    Oates, J.A.3    Boutaud, O.4
  • 132
    • 1242337338 scopus 로고    scopus 로고
    • Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1)
    • Sully G., Dean J.L., Wait R., Rawlinson L., Santalucia T., Saklatvala J., Clark A.R. Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1). Biochem. J. 2004, 377:629-639.
    • (2004) Biochem. J. , vol.377 , pp. 629-639
    • Sully, G.1    Dean, J.L.2    Wait, R.3    Rawlinson, L.4    Santalucia, T.5    Saklatvala, J.6    Clark, A.R.7
  • 133
    • 36049006140 scopus 로고    scopus 로고
    • Modulation of immediate early gene expression by tristetraprolin in the differentiation of 3T3-L1 cells
    • Lin N.Y., Lin C.T., Chang C.J. Modulation of immediate early gene expression by tristetraprolin in the differentiation of 3T3-L1 cells. Biochem. Biophys. Res. Commun. 2008, 365:69-74.
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 69-74
    • Lin, N.Y.1    Lin, C.T.2    Chang, C.J.3
  • 134
    • 65349120262 scopus 로고    scopus 로고
    • The mRNA binding proteins HuR and tristetraprolin regulate cyclooxygenase 2 expression during colon carcinogenesis
    • Young L.E., Sanduja S., Bemis-Standoli K., Pena E.A., Price R.L., Dixon D.A. The mRNA binding proteins HuR and tristetraprolin regulate cyclooxygenase 2 expression during colon carcinogenesis. Gastroenterology 2009, 136:1669-1679.
    • (2009) Gastroenterology , vol.136 , pp. 1669-1679
    • Young, L.E.1    Sanduja, S.2    Bemis-Standoli, K.3    Pena, E.A.4    Price, R.L.5    Dixon, D.A.6
  • 135
    • 77954952745 scopus 로고    scopus 로고
    • The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRNAs involved in breast cancer-related processes
    • Al-Souhibani N., Al-Ahmadi W., Hesketh J.E., Blackshear P.J., Khabar K.S. The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRNAs involved in breast cancer-related processes. Oncogene 2010, 29:4205-4215.
    • (2010) Oncogene , vol.29 , pp. 4205-4215
    • Al-Souhibani, N.1    Al-Ahmadi, W.2    Hesketh, J.E.3    Blackshear, P.J.4    Khabar, K.S.5
  • 137
    • 0345276462 scopus 로고    scopus 로고
    • The Wnt/beta-catenin-->Pitx2 pathway controls the turnover of Pitx2 and other unstable mRNAs
    • Briata P., Ilengo C., Corte G., Moroni C., Rosenfeld M.G., Chen C.Y., Gherzi R. The Wnt/beta-catenin-->Pitx2 pathway controls the turnover of Pitx2 and other unstable mRNAs. Mol. cell 2003, 12:1201-1211.
    • (2003) Mol. cell , vol.12 , pp. 1201-1211
    • Briata, P.1    Ilengo, C.2    Corte, G.3    Moroni, C.4    Rosenfeld, M.G.5    Chen, C.Y.6    Gherzi, R.7
  • 138
    • 0037853206 scopus 로고    scopus 로고
    • Inherent instability of plasminogen activator inhibitor type 2 mRNA is regulated by tristetraprolin
    • Yu H., Stasinopoulos S., Leedman P., Medcalf R.L. Inherent instability of plasminogen activator inhibitor type 2 mRNA is regulated by tristetraprolin. J. Biol. Chem. 2003, 278:13912-13918.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13912-13918
    • Yu, H.1    Stasinopoulos, S.2    Leedman, P.3    Medcalf, R.L.4
  • 139
    • 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., Bohjanen P.R. Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay. J. Immunol. 2005, 174:953-961.
    • (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
  • 140
    • 33745000728 scopus 로고    scopus 로고
    • Differential regulation of ARE-mediated TNFalpha and IL-1beta mRNA stability by lipopolysaccharide in RAW264.7 cells
    • Chen Y.L., Huang Y.L., Lin N.Y., Chen H.C., Chiu W.C., Chang C.J. Differential regulation of ARE-mediated TNFalpha and IL-1beta mRNA stability by lipopolysaccharide in RAW264.7 cells. Biochem. Biophys. Res. Commun. 2006, 346:160-168.
    • (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
  • 141
    • 33845885514 scopus 로고    scopus 로고
    • Down-regulation of tristetraprolin expression results in enhanced IL-12 and MIP-2 production and reduced MIP-3alpha synthesis in activated macrophages
    • Jalonen U., Nieminen R., Vuolteenaho K., Kankaanranta H., Moilanen E. Down-regulation of tristetraprolin expression results in enhanced IL-12 and MIP-2 production and reduced MIP-3alpha synthesis in activated macrophages. Mediators Inflamm. 2006, 2006:40691.
    • (2006) Mediators Inflamm. , vol.2006 , pp. 40691
    • Jalonen, U.1    Nieminen, R.2    Vuolteenaho, K.3    Kankaanranta, H.4    Moilanen, E.5
  • 144
    • 79958852872 scopus 로고    scopus 로고
    • Tristetraprolin regulates interleukin-6, which is correlated with tumor progression in patients with head and neck squamous cell carcinoma
    • Van Tubergen E., Vander Broek R., Lee J., Wolf G., Carey T., Bradford C., Prince M., Kirkwood K.L., D'Silva N.J. Tristetraprolin regulates interleukin-6, which is correlated with tumor progression in patients with head and neck squamous cell carcinoma. Cancer 2011, 117:2677-2689.
    • (2011) Cancer , vol.117 , pp. 2677-2689
    • Van Tubergen, E.1    Vander Broek, R.2    Lee, J.3    Wolf, G.4    Carey, T.5    Bradford, C.6    Prince, M.7    Kirkwood, K.L.8    D'Silva, N.J.9
  • 145
    • 80051499526 scopus 로고    scopus 로고
    • Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region
    • Zhao W., Liu M., D'Silva N.J., Kirkwood K.L. Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region. J. Interferon Cytokine Res. 2011, 31:629-637.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 629-637
    • Zhao, W.1    Liu, M.2    D'Silva, N.J.3    Kirkwood, K.L.4
  • 146
    • 84655167569 scopus 로고    scopus 로고
    • The mRNA-binding protein Zfp36 is upregulated by beta-adrenergic stimulation and represses IL-6 production in 3T3-L1 adipocytes
    • Brahma P.K., Zhang H., Murray B.S., Shu F.J., Sidell N., Seli E., Kallen C.B. The mRNA-binding protein Zfp36 is upregulated by beta-adrenergic stimulation and represses IL-6 production in 3T3-L1 adipocytes. Obesity (Silver Spring) 2012, 20:40-47.
    • (2012) Obesity (Silver Spring) , vol.20 , pp. 40-47
    • Brahma, P.K.1    Zhang, H.2    Murray, B.S.3    Shu, F.J.4    Sidell, N.5    Seli, E.6    Kallen, C.B.7
  • 147
    • 64649103302 scopus 로고    scopus 로고
    • Stimulation of polo-like kinase 3 mRNA decay by tristetraprolin
    • Horner T.J., Lai W.S., Stumpo D.J., Blackshear P.J. Stimulation of polo-like kinase 3 mRNA decay by tristetraprolin. Mol. Cell. Biol. 2009, 29:1999-2010.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1999-2010
    • Horner, T.J.1    Lai, W.S.2    Stumpo, D.J.3    Blackshear, P.J.4
  • 149
  • 150
    • 35848935012 scopus 로고    scopus 로고
    • Tristetraprolin inhibits Ras-dependent tumor vascularization by inducing vascular endothelial growth factor mRNA degradation
    • Essafi-Benkhadir K., Onesto C., Stebe E., Moroni C., Pages G. Tristetraprolin inhibits Ras-dependent tumor vascularization by inducing vascular endothelial growth factor mRNA degradation. Mol. Biol. Cell 2007, 18:4648-4658.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4648-4658
    • Essafi-Benkhadir, K.1    Onesto, C.2    Stebe, E.3    Moroni, C.4    Pages, G.5
  • 151
    • 38849092688 scopus 로고    scopus 로고
    • Tristetraprolin down-regulates interleukin-8 and vascular endothelial growth factor in malignant glioma cells
    • Suswam E., Li Y., Zhang X., Gillespie G.Y., Li X., Shacka J.J., Lu L., Zheng L., King P.H. Tristetraprolin down-regulates interleukin-8 and vascular endothelial growth factor in malignant glioma cells. Cancer Res. 2008, 68:674-682.
    • (2008) Cancer Res. , vol.68 , pp. 674-682
    • Suswam, E.1    Li, Y.2    Zhang, X.3    Gillespie, G.Y.4    Li, X.5    Shacka, J.J.6    Lu, L.7    Zheng, L.8    King, P.H.9
  • 153
    • 34548754592 scopus 로고    scopus 로고
    • Tristetraprolin, a negative regulator of mRNA stability, is increased in old B cells and is involved in the degradation of E47 mRNA
    • Frasca D., Landin A.M., Alvarez J.P., Blackshear P.J., Riley R.L., Blomberg B.B. Tristetraprolin, a negative regulator of mRNA stability, is increased in old B cells and is involved in the degradation of E47 mRNA. J. Immunol. 2007, 179:918-927.
    • (2007) J. Immunol. , vol.179 , pp. 918-927
    • Frasca, D.1    Landin, A.M.2    Alvarez, J.P.3    Blackshear, P.J.4    Riley, R.L.5    Blomberg, B.B.6
  • 154
    • 36849054438 scopus 로고    scopus 로고
    • Functional analysis of KSRP interaction with the AU-rich element of interleukin-8 and identification of inflammatory mRNA targets
    • Winzen R., Thakur B.K., Dittrich-Breiholz O., Shah M., Redich N., Dhamija S., Kracht M., Holtmann H. Functional analysis of KSRP interaction with the AU-rich element of interleukin-8 and identification of inflammatory mRNA targets. Mol. Cell. Biol. 2007, 27:8388-8400.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8388-8400
    • Winzen, R.1    Thakur, B.K.2    Dittrich-Breiholz, O.3    Shah, M.4    Redich, N.5    Dhamija, S.6    Kracht, M.7    Holtmann, H.8
  • 157
    • 80052203045 scopus 로고    scopus 로고
    • Constitutive ERK activity induces downregulation of tristetraprolin, a major protein controlling interleukin8/CXCL8 mRNA stability in melanoma cells
    • Bourcier C., Griseri P., Grepin R., Bertolotto C., Mazure N., Pages G. Constitutive ERK activity induces downregulation of tristetraprolin, a major protein controlling interleukin8/CXCL8 mRNA stability in melanoma cells. Am. J. Physiol. Cell Physiol. 2011, 301:C609-C618.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.301
    • Bourcier, C.1    Griseri, P.2    Grepin, R.3    Bertolotto, C.4    Mazure, N.5    Pages, G.6
  • 158
    • 84858796265 scopus 로고    scopus 로고
    • NADPH oxidase-derived superoxide destabilizes lipopolysaccharide-induced interleukin 8 mRNA via p38, extracellular signal-regulated kinase mitogen-activated protein kinase, and the destabilizing factor tristetraprolin
    • Al Ghouleh I., Magder S. NADPH oxidase-derived superoxide destabilizes lipopolysaccharide-induced interleukin 8 mRNA via p38, extracellular signal-regulated kinase mitogen-activated protein kinase, and the destabilizing factor tristetraprolin. Shock 2012, 37:433-440.
    • (2012) Shock , vol.37 , pp. 433-440
    • Al Ghouleh, I.1    Magder, S.2
  • 159
    • 84856962404 scopus 로고    scopus 로고
    • Isoeugenol destabilizes IL-8 mRNA expression in THP-1 cells through induction of the negative regulator of mRNA stability tristetraprolin
    • Galbiati V., Carne A., Mitjans M., Galli C.L., Marinovich M., Corsini E. Isoeugenol destabilizes IL-8 mRNA expression in THP-1 cells through induction of the negative regulator of mRNA stability tristetraprolin. Arch. Toxicol. 2012, 86:239-248.
    • (2012) Arch. Toxicol. , vol.86 , pp. 239-248
    • Galbiati, V.1    Carne, A.2    Mitjans, M.3    Galli, C.L.4    Marinovich, M.5    Corsini, E.6
  • 162
    • 84865417805 scopus 로고    scopus 로고
    • Cutting edge: IL-10-mediated tristetraprolin induction is part of a feedback loop that controls macrophage STAT3 activation and cytokine production
    • Sep 1
    • Gaba A., Grivennikov S.I., Do M.V., Stumpo D.J., Blackshear P.J., Karin M. Cutting edge: IL-10-mediated tristetraprolin induction is part of a feedback loop that controls macrophage STAT3 activation and cytokine production. J. Immunol. Sep 1 2012, 189(5):2089-2093.
    • (2012) J. Immunol. , vol.189 , Issue.5 , pp. 2089-2093
    • Gaba, A.1    Grivennikov, S.I.2    Do, M.V.3    Stumpo, D.J.4    Blackshear, P.J.5    Karin, M.6
  • 163
    • 41149120601 scopus 로고    scopus 로고
    • Post-transcriptional regulation of CLMP mRNA is controlled by tristetraprolin in response to TNFalpha via c-Jun N-terminal kinase signalling
    • Sze K.L., Lui W.Y., Lee W.M. Post-transcriptional regulation of CLMP mRNA is controlled by tristetraprolin in response to TNFalpha via c-Jun N-terminal kinase signalling. Biochem. J. 2008, 410:575-583.
    • (2008) Biochem. J. , vol.410 , pp. 575-583
    • Sze, K.L.1    Lui, W.Y.2    Lee, W.M.3
  • 165
    • 77955727216 scopus 로고    scopus 로고
    • The mRNA decay factor tristetraprolin (TTP) induces senescence in human papillomavirus-transformed cervical cancer cells by targeting E6-AP ubiquitin ligase
    • Sanduja S., Kaza V., Dixon D.A. The mRNA decay factor tristetraprolin (TTP) induces senescence in human papillomavirus-transformed cervical cancer cells by targeting E6-AP ubiquitin ligase. Aging (Albany NY) 2009, 1:803-817.
    • (2009) Aging (Albany NY) , vol.1 , pp. 803-817
    • Sanduja, S.1    Kaza, V.2    Dixon, D.A.3
  • 170
    • 80052838800 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha mRNA: a new target for destabilization by tristetraprolin in endothelial cells
    • Chamboredon S., Ciais D., Desroches-Castan A., Savi P., Bono F., Feige J.J., Cherradi N. Hypoxia-inducible factor-1alpha mRNA: a new target for destabilization by tristetraprolin in endothelial cells. Mol. Biol. Cell 2011, 22:3366-3378.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3366-3378
    • Chamboredon, S.1    Ciais, D.2    Desroches-Castan, A.3    Savi, P.4    Bono, F.5    Feige, J.J.6    Cherradi, N.7
  • 172
    • 78049253973 scopus 로고    scopus 로고
    • Post-transcriptional regulation of the DUSP6/MKP-3 phosphatase by MEK/ERK signaling and hypoxia
    • Bermudez O., Jouandin P., Rottier J., Bourcier C., Pages G., Gimond C. Post-transcriptional regulation of the DUSP6/MKP-3 phosphatase by MEK/ERK signaling and hypoxia. J. Cell. Physiol. 2011, 226:276-284.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 276-284
    • Bermudez, O.1    Jouandin, P.2    Rottier, J.3    Bourcier, C.4    Pages, G.5    Gimond, C.6
  • 173
    • 81155160856 scopus 로고    scopus 로고
    • Hu antigen R and tristetraprolin: counter-regulators of rat apical sodium-dependent bile acid transporter by way of effects on messenger RNA stability
    • Chen F., Shyu A.B., Shneider B.L. Hu antigen R and tristetraprolin: counter-regulators of rat apical sodium-dependent bile acid transporter by way of effects on messenger RNA stability. Hepatology 2011, 54:1371-1378.
    • (2011) Hepatology , vol.54 , pp. 1371-1378
    • Chen, F.1    Shyu, A.B.2    Shneider, B.L.3
  • 174
    • 80052028863 scopus 로고    scopus 로고
    • TNF-alpha-decreased thrombomodulin expression in monocytes is inhibited by propofol through regulation of tristetraprolin and human antigen R activities
    • Lin F.Y., Tsai Y.T., Lee C.Y., Lin C.Y., Lin Y.W., Li C.Y., Shih C.M., Huang C.Y., Chang N.C., Tsai J.C., Chen T.L., Tsai C.S. TNF-alpha-decreased thrombomodulin expression in monocytes is inhibited by propofol through regulation of tristetraprolin and human antigen R activities. Shock 2011, 36:279-288.
    • (2011) Shock , vol.36 , pp. 279-288
    • Lin, F.Y.1    Tsai, Y.T.2    Lee, C.Y.3    Lin, C.Y.4    Lin, Y.W.5    Li, C.Y.6    Shih, C.M.7    Huang, C.Y.8    Chang, N.C.9    Tsai, J.C.10    Chen, T.L.11    Tsai, C.S.12
  • 175
    • 79958070748 scopus 로고    scopus 로고
    • Posttranscriptional regulation of IL-23 expression by IFN-gamma through tristetraprolin
    • Qian X., Ning H., Zhang J., Hoft D.F., Stumpo D.J., Blackshear P.J., Liu J. Posttranscriptional regulation of IL-23 expression by IFN-gamma through tristetraprolin. J. Immunol. 2011, 186:6454-6464.
    • (2011) J. Immunol. , vol.186 , pp. 6454-6464
    • Qian, X.1    Ning, H.2    Zhang, J.3    Hoft, D.F.4    Stumpo, D.J.5    Blackshear, P.J.6    Liu, J.7
  • 176
    • 84870477645 scopus 로고    scopus 로고
    • Regulation of p21/CIP1/WAF-1 mediated cell-cycle arrest by RNase L and tristetraprolin, and involvement of AU-rich elements
    • Sep
    • Al-Haj L., Blackshear P.J., Khabar K.S. Regulation of p21/CIP1/WAF-1 mediated cell-cycle arrest by RNase L and tristetraprolin, and involvement of AU-rich elements. Nucleic Acids Res. Sep 2012, 40(16):7739-7752.
    • (2012) Nucleic Acids Res. , vol.40 , Issue.16 , pp. 7739-7752
    • Al-Haj, L.1    Blackshear, P.J.2    Khabar, K.S.3
  • 179
    • 84860460482 scopus 로고    scopus 로고
    • Identification of tristetraprolin as a factor that modulates the stability of the TAFI transcript through binding to the 3'-untranslated region
    • Novakovic D., Kuo A.C., Lin J.H., Koschinsky M.L., Boffa M.B. Identification of tristetraprolin as a factor that modulates the stability of the TAFI transcript through binding to the 3'-untranslated region. J. Thromb. Haemost. 2012, 10:887-894.
    • (2012) J. Thromb. Haemost. , vol.10 , pp. 887-894
    • Novakovic, D.1    Kuo, A.C.2    Lin, J.H.3    Koschinsky, M.L.4    Boffa, M.B.5
  • 181
    • 42449101248 scopus 로고    scopus 로고
    • Identification of TTP mRNA targets in human dendritic cells reveals TTP as a critical regulator of dendritic cell maturation
    • Emmons J., Townley-Tilson W.H., Deleault K.M., Skinner S.J., Gross R.H., Whitfield M.L., Brooks S.A. Identification of TTP mRNA targets in human dendritic cells reveals TTP as a critical regulator of dendritic cell maturation. RNA 2008, 14:888-902.
    • (2008) RNA , vol.14 , pp. 888-902
    • Emmons, J.1    Townley-Tilson, W.H.2    Deleault, K.M.3    Skinner, S.J.4    Gross, R.H.5    Whitfield, M.L.6    Brooks, S.A.7
  • 183
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • Lehner B., Sanderson C.M. A protein interaction framework for human mRNA degradation. Genome Res. 2004, 14:1315-1323.
    • (2004) Genome Res. , vol.14 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 184
    • 84864383685 scopus 로고    scopus 로고
    • Tristetraprolin inhibits poly(A)-tail synthesis in nuclear mRNA that contains AU-rich elements by interacting with poly(A)-binding protein nuclear 1
    • Su Y.L., Wang S.C., Chiang P.Y., Lin N.Y., Shen Y.F., Chang G.D., Chang C.J. Tristetraprolin inhibits poly(A)-tail synthesis in nuclear mRNA that contains AU-rich elements by interacting with poly(A)-binding protein nuclear 1. PLoS One 2012, 7:e41313.
    • (2012) PLoS One , vol.7
    • Su, Y.L.1    Wang, S.C.2    Chiang, P.Y.3    Lin, N.Y.4    Shen, Y.F.5    Chang, G.D.6    Chang, C.J.7
  • 185
    • 77949716572 scopus 로고    scopus 로고
    • Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85
    • Kedar V.P., Darby M.K., Williams J.G., Blackshear P.J. Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85. PLoS One 2010, 5:e9588.
    • (2010) PLoS One , vol.5
    • Kedar, V.P.1    Darby, M.K.2    Williams, J.G.3    Blackshear, P.J.4
  • 186
    • 71049187181 scopus 로고    scopus 로고
    • A role for transportin in deposition of TTP to cytoplasmic RNA granules and mRNA decay
    • Chang W.L., Tarn W.Y. A role for transportin in deposition of TTP to cytoplasmic RNA granules and mRNA decay. Nucleic Acids Res. 2009, 37:6600-6612.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6600-6612
    • Chang, W.L.1    Tarn, W.Y.2
  • 187
    • 0842332176 scopus 로고    scopus 로고
    • Direct association of tristetraprolin with the nucleoporin CAN/Nup214
    • Carman J.A., Nadler S.G. Direct association of tristetraprolin with the nucleoporin CAN/Nup214. Biochem. Biophys. Res. Commun. 2004, 315:445-449.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 445-449
    • Carman, J.A.1    Nadler, S.G.2
  • 189
    • 41949103837 scopus 로고    scopus 로고
    • P72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein
    • Chen G., Guo X., Lv F., Xu Y., Gao G. p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:4352-4357.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 4352-4357
    • Chen, G.1    Guo, X.2    Lv, F.3    Xu, Y.4    Gao, G.5
  • 190
    • 84857340173 scopus 로고    scopus 로고
    • Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins
    • Kedar V.P., Zucconi B.E., Wilson G.M., Blackshear P.J. Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins. J. Biol. Chem. 2012, 287:5459-5471.
    • (2012) J. Biol. Chem. , vol.287 , pp. 5459-5471
    • Kedar, V.P.1    Zucconi, B.E.2    Wilson, G.M.3    Blackshear, P.J.4
  • 191
    • 77953050555 scopus 로고    scopus 로고
    • Protein phosphatase 2A (PP2A) is increased in old murine B cells and mediates p38 MAPK/tristetraprolin dephosphorylation and E47 mRNA instability
    • Frasca D., Romero M., Landin A.M., Diaz A., Riley R.L., Blomberg B.B. Protein phosphatase 2A (PP2A) is increased in old murine B cells and mediates p38 MAPK/tristetraprolin dephosphorylation and E47 mRNA instability. Mech. Ageing Dev. 2010, 131:306-314.
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 306-314
    • Frasca, D.1    Romero, M.2    Landin, A.M.3    Diaz, A.4    Riley, R.L.5    Blomberg, B.B.6
  • 192
    • 80055086748 scopus 로고    scopus 로고
    • Novel phosphorylation-dependent ubiquitination of tristetraprolin by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1 (MEKK1) and tumor necrosis factor receptor-associated factor 2 (TRAF2)
    • Schichl Y.M., Resch U., Lemberger C.E., Stichlberger D., de Martin R. Novel phosphorylation-dependent ubiquitination of tristetraprolin by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1 (MEKK1) and tumor necrosis factor receptor-associated factor 2 (TRAF2). J. Biol. Chem. 2011, 286:38466-38477.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38466-38477
    • Schichl, Y.M.1    Resch, U.2    Lemberger, C.E.3    Stichlberger, D.4    de Martin, R.5
  • 194
    • 0037124067 scopus 로고    scopus 로고
    • Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms
    • Johnson B.A., Stehn J.R., Yaffe M.B., Blackwell T.K. Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms. J. Biol. Chem. 2002, 277:18029-18036.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18029-18036
    • Johnson, B.A.1    Stehn, J.R.2    Yaffe, M.B.3    Blackwell, T.K.4
  • 195
    • 84863769150 scopus 로고    scopus 로고
    • Differential expression and functional analysis of the tristetraprolin family during early differentiation of 3T3-L1 preadipocytes
    • Lin N.Y., Lin T.Y., Yang W.H., Wang S.C., Wang K.T., Su Y.L., Jiang Y.W., Chang G.D., Chang C.J. Differential expression and functional analysis of the tristetraprolin family during early differentiation of 3T3-L1 preadipocytes. Int. J. Biol. Sci. 2012, 8:761-777.
    • (2012) Int. J. Biol. Sci. , vol.8 , pp. 761-777
    • Lin, N.Y.1    Lin, T.Y.2    Yang, W.H.3    Wang, S.C.4    Wang, K.T.5    Su, Y.L.6    Jiang, Y.W.7    Chang, G.D.8    Chang, C.J.9
  • 198
    • 0036510607 scopus 로고    scopus 로고
    • HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences
    • Dintilhac A., Bernues J. HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. J. Biol. Chem. 2002, 277:7021-7028.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7021-7028
    • Dintilhac, A.1    Bernues, J.2
  • 199
    • 77956642517 scopus 로고    scopus 로고
    • Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies
    • Ozgur S., Chekulaeva M., Stoecklin G. Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies. Mol. Cell. Biol. 2010, 30:4308-4323.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4308-4323
    • Ozgur, S.1    Chekulaeva, M.2    Stoecklin, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.