메뉴 건너뛰기




Volumn 1823, Issue 10, 2012, Pages 1905-1913

Monocyte chemotactic protein-1-induced protein-1 (MCPIP1) is a novel multifunctional modulator of inflammatory reactions

Author keywords

Deubiquitinase; MRNA stability and decay; NF kappaB signaling cascade; Proinflammatory cytokines; RNase; Ubiquitin binding domains

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 1; LIPOPOLYSACCHARIDE; MESSENGER RNA; MONOCYTE CHEMOTACTIC PROTEIN INDUCED PROTEIN 1; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCLASSIFIED DRUG;

EID: 84864818117     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.06.029     Document Type: Review
Times cited : (84)

References (101)
  • 1
    • 0020000298 scopus 로고
    • The phenomenon of the acute phase response
    • Kushner I. The phenomenon of the acute phase response. Ann. N. Y. Acad. Sci. 1982, 389:39-48.
    • (1982) Ann. N. Y. Acad. Sci. , vol.389 , pp. 39-48
    • Kushner, I.1
  • 2
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., Uematsu S., Takeuchi O. Pathogen recognition and innate immunity. Cell 2006, 124:783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 3
    • 62649139025 scopus 로고    scopus 로고
    • Immunological and inflammatory functions of the interleukin-1 family
    • Dinarello C.A. Immunological and inflammatory functions of the interleukin-1 family. Annu. Rev. Immunol. 2009, 27:519-550.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 519-550
    • Dinarello, C.A.1
  • 4
    • 65949118245 scopus 로고    scopus 로고
    • From the obscure and mysterious acute phase response to toll-like receptors and the cytokine network
    • (16)
    • Koj A. From the obscure and mysterious acute phase response to toll-like receptors and the cytokine network. Curr. Immunol. Rev. 2008, 4:199-214. (16).
    • (2008) Curr. Immunol. Rev. , vol.4 , pp. 199-214
    • Koj, A.1
  • 5
    • 77950345093 scopus 로고    scopus 로고
    • Inflammation 2010: new adventures of an old flame
    • Medzhitov R. Inflammation 2010: new adventures of an old flame. Cell 2010, 140:771-776.
    • (2010) Cell , vol.140 , pp. 771-776
    • Medzhitov, R.1
  • 6
    • 77950355734 scopus 로고    scopus 로고
    • Anti-inflammatory agents: present and future
    • Dinarello C.A. Anti-inflammatory agents: present and future. Cell 2010, 140:935-950.
    • (2010) Cell , vol.140 , pp. 935-950
    • Dinarello, C.A.1
  • 7
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R., Preston-Hurlburt P., Janeway C.A. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997, 388:394-397.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway, C.A.3
  • 9
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O., Akira S. Pattern recognition receptors and inflammation. Cell 2010, 140:805-820.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 11
    • 38049083888 scopus 로고    scopus 로고
    • Primer: inflammasomes and interleukin 1beta in inflammatory disorders
    • Church L.D., Cook G.P., McDermott M.F. Primer: inflammasomes and interleukin 1beta in inflammatory disorders. Nat. Clin. Pract. Rheumatol. 2008, 4:34-42.
    • (2008) Nat. Clin. Pract. Rheumatol. , vol.4 , pp. 34-42
    • Church, L.D.1    Cook, G.P.2    McDermott, M.F.3
  • 13
    • 0029115698 scopus 로고
    • Modified proteins as possible signals in the acute phase response
    • (discussion 118-9)
    • Koj A., Guzdek A. Modified proteins as possible signals in the acute phase response. Ann. N. Y. Acad. Sci. 1995, 762:108-118. (discussion 118-9).
    • (1995) Ann. N. Y. Acad. Sci. , vol.762 , pp. 108-118
    • Koj, A.1    Guzdek, A.2
  • 14
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K., Tschopp J. The inflammasomes. Cell 2010, 140:821-832.
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 15
    • 0031569363 scopus 로고    scopus 로고
    • Hyperosmotic stress as a stimulant for proinflammatory cytokine production
    • Shapiro L., Dinarello C.A. Hyperosmotic stress as a stimulant for proinflammatory cytokine production. Exp. Cell Res. 1997, 231:354-362.
    • (1997) Exp. Cell Res. , vol.231 , pp. 354-362
    • Shapiro, L.1    Dinarello, C.A.2
  • 16
    • 0033570091 scopus 로고    scopus 로고
    • The mitogen-activated protein (MAP) kinase p38 and its upstream activator MAP kinase kinase 6 are involved in the activation of signal transducer and activator of transcription by hyperosmolarity
    • Bode J.G., Gatsios P., Ludwig S., Rapp U.R., Haussinger D., Heinrich P.C., Graeve L. The mitogen-activated protein (MAP) kinase p38 and its upstream activator MAP kinase kinase 6 are involved in the activation of signal transducer and activator of transcription by hyperosmolarity. J. Biol. Chem. 1999, 274:30222-30227.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30222-30227
    • Bode, J.G.1    Gatsios, P.2    Ludwig, S.3    Rapp, U.R.4    Haussinger, D.5    Heinrich, P.C.6    Graeve, L.7
  • 17
    • 0028840908 scopus 로고
    • Hypoxia, a novel inducer of acute phase gene expression in a human hepatoma cell line
    • Wenger R.H., Rolfs A., Marti H.H., Bauer C., Gassmann M. Hypoxia, a novel inducer of acute phase gene expression in a human hepatoma cell line. J. Biol. Chem. 1995, 270:27865-27870.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27865-27870
    • Wenger, R.H.1    Rolfs, A.2    Marti, H.H.3    Bauer, C.4    Gassmann, M.5
  • 18
    • 17544404224 scopus 로고    scopus 로고
    • Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity
    • Bogdan C., Rollinghoff M., Diefenbach A. Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity. Curr. Opin. Immunol. 2000, 12:64-76.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 64-76
    • Bogdan, C.1    Rollinghoff, M.2    Diefenbach, A.3
  • 19
    • 34250835251 scopus 로고    scopus 로고
    • The inflammasome mediates UVB-induced activation and secretion of interleukin-1beta by keratinocytes
    • Feldmeyer L., Keller M., Niklaus G., Hohl D., Werner S., Beer H.D. The inflammasome mediates UVB-induced activation and secretion of interleukin-1beta by keratinocytes. Curr. Biol. 2007, 17:1140-1145.
    • (2007) Curr. Biol. , vol.17 , pp. 1140-1145
    • Feldmeyer, L.1    Keller, M.2    Niklaus, G.3    Hohl, D.4    Werner, S.5    Beer, H.D.6
  • 20
    • 33747191203 scopus 로고    scopus 로고
    • The inflammasome: first line of the immune response to cell stress
    • Ogura Y., Sutterwala F.S., Flavell R.A. The inflammasome: first line of the immune response to cell stress. Cell 2006, 126:659-662.
    • (2006) Cell , vol.126 , pp. 659-662
    • Ogura, Y.1    Sutterwala, F.S.2    Flavell, R.A.3
  • 23
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L., Karin M. Mammalian MAP kinase signalling cascades. Nature 2001, 410:37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 24
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 2001, 81:807-869.
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 25
    • 0038538477 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression by mitogen-activated protein kinase p38
    • Clark A.R., Dean J.L., Saklatvala J. Post-transcriptional regulation of gene expression by mitogen-activated protein kinase p38. FEBS Lett. 2003, 546:37-44.
    • (2003) FEBS Lett. , vol.546 , pp. 37-44
    • Clark, A.R.1    Dean, J.L.2    Saklatvala, J.3
  • 26
    • 34547154349 scopus 로고    scopus 로고
    • P38 MAP-kinases pathway regulation, function and role in human diseases
    • Cuenda A., Rousseau S. p38 MAP-kinases pathway regulation, function and role in human diseases. Biochim. Biophys. Acta 2007, 1773:1358-1375.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1358-1375
    • Cuenda, A.1    Rousseau, S.2
  • 27
    • 77952245032 scopus 로고    scopus 로고
    • A central role for p38 MAPK in the early transcriptional response to stress
    • Whitmarsh A.J. A central role for p38 MAPK in the early transcriptional response to stress. BMC Biol. 2010, 8:47.
    • (2010) BMC Biol. , vol.8 , pp. 47
    • Whitmarsh, A.J.1
  • 28
    • 0033990344 scopus 로고    scopus 로고
    • Cell type-specific role for reactive oxygen species in nuclear factor-kappaB activation by interleukin-1
    • Bonizzi G., Piette J., Merville M.P., Bours V. Cell type-specific role for reactive oxygen species in nuclear factor-kappaB activation by interleukin-1. Biochem. Pharmacol. 2000, 59:7-11.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 7-11
    • Bonizzi, G.1    Piette, J.2    Merville, M.P.3    Bours, V.4
  • 31
    • 72949123583 scopus 로고    scopus 로고
    • Post-transcriptional regulons coordinate the initiation and resolution of inflammation
    • Anderson P. Post-transcriptional regulons coordinate the initiation and resolution of inflammation. Nat. Rev. Immunol. 2010, 10:24-35.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 24-35
    • Anderson, P.1
  • 32
    • 0030589152 scopus 로고    scopus 로고
    • Initiation of acute phase response and synthesis of cytokines
    • Koj A. Initiation of acute phase response and synthesis of cytokines. Biochim. Biophys. Acta 1996, 1317:84-94.
    • (1996) Biochim. Biophys. Acta , vol.1317 , pp. 84-94
    • Koj, A.1
  • 33
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor kappaB signaling
    • Hoffmann A., Baltimore D. Circuitry of nuclear factor kappaB signaling. Immunol. Rev. 2006, 210:171-186.
    • (2006) Immunol. Rev. , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 34
    • 0032491401 scopus 로고    scopus 로고
    • The role of C/EBP isoforms in the control of inflammatory and native immunity functions
    • Poli V. The role of C/EBP isoforms in the control of inflammatory and native immunity functions. J. Biol. Chem. 1998, 273:29279-29282.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29279-29282
    • Poli, V.1
  • 36
    • 78650371990 scopus 로고    scopus 로고
    • MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling
    • Liang J., Saad Y., Lei T., Wang J., Qi D., Yang Q., Kolattukudy P.E., Fu M. MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling. J. Exp. Med. 2010, 207:2959-2973.
    • (2010) J. Exp. Med. , vol.207 , pp. 2959-2973
    • Liang, J.1    Saad, Y.2    Lei, T.3    Wang, J.4    Qi, D.5    Yang, Q.6    Kolattukudy, P.E.7    Fu, M.8
  • 37
    • 65949101799 scopus 로고    scopus 로고
    • STAT activation in the acute phase response
    • Kluwer Academic Publishers, Dordrecht-Boston-London, P.B. Sehgal, D.E. Levy, T. Hirano (Eds.) Signal Transducers and Activators of Transcription (STATs)
    • Baumann H. STAT activation in the acute phase response. Activation and Biology 2003, 465-491. Kluwer Academic Publishers, Dordrecht-Boston-London. P.B. Sehgal, D.E. Levy, T. Hirano (Eds.).
    • (2003) Activation and Biology , pp. 465-491
    • Baumann, H.1
  • 38
    • 0028889335 scopus 로고
    • STAT3 and STAT5B are targets of two different signal pathways activated by hematopoietin receptors and control transcription via separate cytokine response elements
    • Lai C.F., Ripperger J., Morella K.K., Wang Y., Gearing D.P., Horseman N.D., Campos S.P., Fey G.H., Baumann H. STAT3 and STAT5B are targets of two different signal pathways activated by hematopoietin receptors and control transcription via separate cytokine response elements. J. Biol. Chem. 1995, 270:23254-23257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23254-23257
    • Lai, C.F.1    Ripperger, J.2    Morella, K.K.3    Wang, Y.4    Gearing, D.P.5    Horseman, N.D.6    Campos, S.P.7    Fey, G.H.8    Baumann, H.9
  • 39
    • 0028362019 scopus 로고
    • Multiple regulatory elements in the interleukin-6 gene mediate induction by prostaglandins, cyclic AMP, and lipopolysaccharide
    • Dendorfer U., Oettgen P., Libermann T.A. Multiple regulatory elements in the interleukin-6 gene mediate induction by prostaglandins, cyclic AMP, and lipopolysaccharide. Mol. Cell. Biol. 1994, 14:4443-4454.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4443-4454
    • Dendorfer, U.1    Oettgen, P.2    Libermann, T.A.3
  • 41
    • 34447647277 scopus 로고    scopus 로고
    • Ets-1 represents a pivotal transcription factor for viral clearance, inflammation, and demyelination in a mouse model of multiple sclerosis
    • Gerhauser I., Alldinger S., Baumgartner W. Ets-1 represents a pivotal transcription factor for viral clearance, inflammation, and demyelination in a mouse model of multiple sclerosis. J. Neuroimmunol. 2007, 188:86-94.
    • (2007) J. Neuroimmunol. , vol.188 , pp. 86-94
    • Gerhauser, I.1    Alldinger, S.2    Baumgartner, W.3
  • 42
    • 0025047444 scopus 로고
    • On the mechanism for efficient repression of the interleukin-6 promoter by glucocorticoids: enhancer, TATA box, and RNA start site (Inr motif) occlusion
    • Ray A., LaForge K.S., Sehgal P.B. On the mechanism for efficient repression of the interleukin-6 promoter by glucocorticoids: enhancer, TATA box, and RNA start site (Inr motif) occlusion. Mol. Cell. Biol. 1990, 10:5736-5746.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5736-5746
    • Ray, A.1    LaForge, K.S.2    Sehgal, P.B.3
  • 43
    • 0028788194 scopus 로고
    • AU-rich elements: characterization and importance in mRNA degradation
    • Chen C.Y., Shyu A.B. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci. 1995, 20:465-470.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.B.2
  • 45
    • 84882920276 scopus 로고    scopus 로고
    • Regulation of mRNA turnover by cellular stress
    • Elsevier, R.A. Bradshaw, E.A. Dennis (Eds.)
    • Srikantan S., Gorospe M. Regulation of mRNA turnover by cellular stress. Handbook of Cell Signaling 2008, 2247-2255. Elsevier. R.A. Bradshaw, E.A. Dennis (Eds.).
    • (2008) Handbook of Cell Signaling , pp. 2247-2255
    • Srikantan, S.1    Gorospe, M.2
  • 46
    • 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
  • 48
    • 33751257755 scopus 로고    scopus 로고
    • Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAs
    • Lu J.Y., Sadri N., Schneider R.J. Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAs. Genes Dev. 2006, 20:3174-3184.
    • (2006) Genes Dev. , vol.20 , pp. 3174-3184
    • Lu, J.Y.1    Sadri, N.2    Schneider, R.J.3
  • 49
    • 0035933724 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA: tristetraprolin-mediated AU-rich element-dependent mRNA degradation can occur in the absence of a poly(A) tail
    • Lai W.S., Blackshear P.J. Interactions of CCCH zinc finger proteins with mRNA: tristetraprolin-mediated AU-rich element-dependent mRNA degradation can occur in the absence of a poly(A) tail. J. Biol. Chem. 2001, 276:23144-23154.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23144-23154
    • Lai, W.S.1    Blackshear, P.J.2
  • 50
    • 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
  • 51
    • 3142546235 scopus 로고    scopus 로고
    • The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation
    • Dean J.L., Sully G., Clark A.R., Saklatvala J. The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. Cell. Signal. 2004, 16:1113-1121.
    • (2004) Cell. Signal. , vol.16 , pp. 1113-1121
    • Dean, J.L.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 52
    • 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
  • 53
    • 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
  • 54
    • 71949091958 scopus 로고    scopus 로고
    • Interleukin-1-inducible MCPIP protein has structural and functional properties of RNase and participates in degradation of IL-1beta mRNA
    • Mizgalska D., Wegrzyn P., Murzyn K., Kasza A., Koj A., Jura J., Jarzab B., Jura J. Interleukin-1-inducible MCPIP protein has structural and functional properties of RNase and participates in degradation of IL-1beta mRNA. FEBS J. 2009, 276:7386-7399.
    • (2009) FEBS J. , vol.276 , pp. 7386-7399
    • Mizgalska, D.1    Wegrzyn, P.2    Murzyn, K.3    Kasza, A.4    Koj, A.5    Jura, J.6    Jarzab, B.7    Jura, J.8
  • 56
    • 80555127350 scopus 로고    scopus 로고
    • MCPIP1 ribonuclease antagonizes dicer and terminates microRNA biogenesis through precursor microRNA degradation
    • Suzuki H.I., Arase M., Matsuyama H., Choi Y.L., Ueno T., Mano H., Sugimoto K., Miyazono K. MCPIP1 ribonuclease antagonizes dicer and terminates microRNA biogenesis through precursor microRNA degradation. Mol. Cell 2011, 44:424-436.
    • (2011) Mol. Cell , vol.44 , pp. 424-436
    • Suzuki, H.I.1    Arase, M.2    Matsuyama, H.3    Choi, Y.L.4    Ueno, T.5    Mano, H.6    Sugimoto, K.7    Miyazono, K.8
  • 57
    • 0141815718 scopus 로고    scopus 로고
    • The proximal region of the 3'-untranslated region of cyclooxygenase-2 is recognized by a multimeric protein complex containing HuR, TIA-1, TIAR, and the heterogeneous nuclear ribonucleoprotein U
    • Cok S.J., Acton S.J., Morrison A.R. The proximal region of the 3'-untranslated region of cyclooxygenase-2 is recognized by a multimeric protein complex containing HuR, TIA-1, TIAR, and the heterogeneous nuclear ribonucleoprotein U. J. Biol. Chem. 2003, 278:36157-36162.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36157-36162
    • Cok, S.J.1    Acton, S.J.2    Morrison, A.R.3
  • 59
    • 33644768174 scopus 로고    scopus 로고
    • Control of translation and mRNA degradation by miRNAs and siRNAs
    • Valencia-Sanchez M.A., Liu J., Hannon G.J., Parker R. Control of translation and mRNA degradation by miRNAs and siRNAs. Genes Dev. 2006, 20:515-524.
    • (2006) Genes Dev. , vol.20 , pp. 515-524
    • Valencia-Sanchez, M.A.1    Liu, J.2    Hannon, G.J.3    Parker, R.4
  • 60
    • 59649117586 scopus 로고    scopus 로고
    • Examining the influence of microRNAs on translation efficiency and on mRNA deadenylation and decay
    • Wu L., Belasco J.G. Examining the influence of microRNAs on translation efficiency and on mRNA deadenylation and decay. Methods Enzymol. 2008, 449:373-393.
    • (2008) Methods Enzymol. , vol.449 , pp. 373-393
    • Wu, L.1    Belasco, J.G.2
  • 62
    • 77949316183 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor alpha- and interleukin-1beta-induced IKK/NF-kappaB and JNK/AP-1 activation
    • Fan Y., Yu Y., Shi Y., Sun W., Xie M., Ge N., Mao R., Chang A., Xu G., Schneider M.D., Zhang H., Fu S., Qin J., Yang J. Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor alpha- and interleukin-1beta-induced IKK/NF-kappaB and JNK/AP-1 activation. J. Biol. Chem. 2010, 285:5347-5360.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5347-5360
    • Fan, Y.1    Yu, Y.2    Shi, Y.3    Sun, W.4    Xie, M.5    Ge, N.6    Mao, R.7    Chang, A.8    Xu, G.9    Schneider, M.D.10    Zhang, H.11    Fu, S.12    Qin, J.13    Yang, J.14
  • 63
    • 67650744586 scopus 로고    scopus 로고
    • The role of ubiquitin in NF-kappaB regulatory pathways
    • Skaug B., Jiang X., Chen Z.J. The role of ubiquitin in NF-kappaB regulatory pathways. Annu. Rev. Biochem. 2009, 78:769-796.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 769-796
    • Skaug, B.1    Jiang, X.2    Chen, Z.J.3
  • 64
    • 38149085473 scopus 로고    scopus 로고
    • The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1
    • Ordureau A., Smith H., Windheim M., Peggie M., Carrick E., Morrice N., Cohen P. The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1. Biochem. J. 2008, 409:43-52.
    • (2008) Biochem. J. , vol.409 , pp. 43-52
    • Ordureau, A.1    Smith, H.2    Windheim, M.3    Peggie, M.4    Carrick, E.5    Morrice, N.6    Cohen, P.7
  • 65
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: activation, specificity, and regulation
    • Pop C., Salvesen G.S. Human caspases: activation, specificity, and regulation. J. Biol. Chem. 2009, 284:21777-21781.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 66
    • 0032127397 scopus 로고    scopus 로고
    • Termination of acute-phase response: role of some cytokines and anti-inflammatory drugs
    • Koj A. Termination of acute-phase response: role of some cytokines and anti-inflammatory drugs. Gen. Pharmacol. 1998, 31:9-18.
    • (1998) Gen. Pharmacol. , vol.31 , pp. 9-18
    • Koj, A.1
  • 67
    • 33645116785 scopus 로고    scopus 로고
    • NF-kappa B activation as a pathological mechanism of septic shock and inflammation
    • Liu S.F., Malik A.B. NF-kappa B activation as a pathological mechanism of septic shock and inflammation. Am. J. Physiol. Lung Cell. Mol. Physiol. 2006, 290:L622-L645.
    • (2006) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.290
    • Liu, S.F.1    Malik, A.B.2
  • 70
    • 31044443091 scopus 로고    scopus 로고
    • Regulation of pro-inflammatory signalling networks by ubiquitin: identification of novel targets for anti-inflammatory drugs
    • Evans P.C. Regulation of pro-inflammatory signalling networks by ubiquitin: identification of novel targets for anti-inflammatory drugs. Expert Rev. Mol. Med. 2005, 7:1-19.
    • (2005) Expert Rev. Mol. Med. , vol.7 , pp. 1-19
    • Evans, P.C.1
  • 71
    • 27844487939 scopus 로고    scopus 로고
    • The NF-kappaB pathway
    • Moynagh P.N. The NF-kappaB pathway. J. Cell Sci. 2005, 118:4589-4592.
    • (2005) J. Cell Sci. , vol.118 , pp. 4589-4592
    • Moynagh, P.N.1
  • 72
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994, 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 73
    • 0032549815 scopus 로고    scopus 로고
    • Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome
    • Lin L., DeMartino G.N., Greene W.C. Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome. Cell 1998, 92:819-828.
    • (1998) Cell , vol.92 , pp. 819-828
    • Lin, L.1    DeMartino, G.N.2    Greene, W.C.3
  • 74
    • 0036771765 scopus 로고    scopus 로고
    • Two pathways to NF-kappaB
    • Pomerantz J.L., Baltimore D. Two pathways to NF-kappaB. Mol. Cell 2002, 10:693-695.
    • (2002) Mol. Cell , vol.10 , pp. 693-695
    • Pomerantz, J.L.1    Baltimore, D.2
  • 75
    • 33750289164 scopus 로고    scopus 로고
    • Low cell cholesterol levels increase NFkappaB activity through a p38 MAPK-dependent mechanism
    • Calleros L., Lasa M., Toro M.J., Chiloeches A. Low cell cholesterol levels increase NFkappaB activity through a p38 MAPK-dependent mechanism. Cell. Signal. 2006, 18:2292-2301.
    • (2006) Cell. Signal. , vol.18 , pp. 2292-2301
    • Calleros, L.1    Lasa, M.2    Toro, M.J.3    Chiloeches, A.4
  • 76
    • 0032811045 scopus 로고    scopus 로고
    • Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro
    • Taylor J.A., Bren G.D., Pennington K.N., Trushin S.A., Asin S., Paya C.V. Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro. J. Mol. Biol. 1999, 290:839-850.
    • (1999) J. Mol. Biol. , vol.290 , pp. 839-850
    • Taylor, J.A.1    Bren, G.D.2    Pennington, K.N.3    Trushin, S.A.4    Asin, S.5    Paya, C.V.6
  • 77
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E., Rothwarf D.M., Delhase M., Hayakawa M., Karin M. The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 1997, 91:243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 79
    • 82955233198 scopus 로고    scopus 로고
    • Regulation of TNF-induced NF-kappaB activation by different cytoplasmic ubiquitination events
    • Verhelst K., Carpentier I., Beyaert R. Regulation of TNF-induced NF-kappaB activation by different cytoplasmic ubiquitination events. Cytokine Growth Factor Rev. 2011, 22:277-286.
    • (2011) Cytokine Growth Factor Rev. , vol.22 , pp. 277-286
    • Verhelst, K.1    Carpentier, I.2    Beyaert, R.3
  • 80
    • 33745027735 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction
    • Zhou L., Azfer A., Niu J., Graham S., Choudhury M., Adamski F.M., Younce C., Binkley P.F., Kolattukudy P.E. Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction. Circ. Res. 2006, 98:1177-1185.
    • (2006) Circ. Res. , vol.98 , pp. 1177-1185
    • Zhou, L.1    Azfer, A.2    Niu, J.3    Graham, S.4    Choudhury, M.5    Adamski, F.M.6    Younce, C.7    Binkley, P.F.8    Kolattukudy, P.E.9
  • 81
    • 44449117059 scopus 로고    scopus 로고
    • A novel CCCH-zinc finger protein family regulates proinflammatory activation of macrophages
    • Liang J., Wang J., Azfer A., Song W., Tromp G., Kolattukudy P.E., Fu M. A novel CCCH-zinc finger protein family regulates proinflammatory activation of macrophages. J. Biol. Chem. 2008, 283:6337-6346.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6337-6346
    • Liang, J.1    Wang, J.2    Azfer, A.3    Song, W.4    Tromp, G.5    Kolattukudy, P.E.6    Fu, M.7
  • 83
    • 18044391849 scopus 로고    scopus 로고
    • Yin and yang of MCP-1
    • Becker L.C. Yin and yang of MCP-1. Circ. Res. 2005, 96:812-814.
    • (2005) Circ. Res. , vol.96 , pp. 812-814
    • Becker, L.C.1
  • 84
    • 47249139521 scopus 로고    scopus 로고
    • Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a novel transcription factor, MCP-1-induced protein (MCPIP)
    • Niu J., Azfer A., Zhelyabovska O., Fatma S., Kolattukudy P.E. Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a novel transcription factor, MCP-1-induced protein (MCPIP). J. Biol. Chem. 2008, 283:14542-14551.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14542-14551
    • Niu, J.1    Azfer, A.2    Zhelyabovska, O.3    Fatma, S.4    Kolattukudy, P.E.5
  • 86
    • 70349492908 scopus 로고    scopus 로고
    • Regulatory feedback loop between NF-kappaB and MCP-1-induced protein 1 RNase
    • Skalniak L., Mizgalska D., Zarebski A., Wyrzykowska P., Koj A., Jura J. Regulatory feedback loop between NF-kappaB and MCP-1-induced protein 1 RNase. FEBS J. 2009, 276:5892-5905.
    • (2009) FEBS J. , vol.276 , pp. 5892-5905
    • Skalniak, L.1    Mizgalska, D.2    Zarebski, A.3    Wyrzykowska, P.4    Koj, A.5    Jura, J.6
  • 87
    • 76549115938 scopus 로고    scopus 로고
    • MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP
    • Younce C.W., Kolattukudy P.E. MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP. Biochem. J. 2010, 426:43-53.
    • (2010) Biochem. J. , vol.426 , pp. 43-53
    • Younce, C.W.1    Kolattukudy, P.E.2
  • 88
    • 84855371108 scopus 로고    scopus 로고
    • Inflammation, endoplasmic reticulum stress, autophagy, and the monocyte chemoattractant protein-1/CCR2 pathway
    • Kolattukudy P.E., Niu J. Inflammation, endoplasmic reticulum stress, autophagy, and the monocyte chemoattractant protein-1/CCR2 pathway. Circ. Res. 2012, 110:174-189.
    • (2012) Circ. Res. , vol.110 , pp. 174-189
    • Kolattukudy, P.E.1    Niu, J.2
  • 89
    • 70350448421 scopus 로고    scopus 로고
    • MCP-1 (monocyte chemotactic protein-1)-induced protein, a recently identified zinc finger protein, induces adipogenesis in 3T3-L1 pre-adipocytes without peroxisome proliferator-activated receptor gamma
    • Younce C.W., Azfer A., Kolattukudy P.E. MCP-1 (monocyte chemotactic protein-1)-induced protein, a recently identified zinc finger protein, induces adipogenesis in 3T3-L1 pre-adipocytes without peroxisome proliferator-activated receptor gamma. J. Biol. Chem. 2009, 284:27620-27628.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27620-27628
    • Younce, C.W.1    Azfer, A.2    Kolattukudy, P.E.3
  • 90
    • 62349092679 scopus 로고    scopus 로고
    • MCP-1 involvement in glial differentiation of neuroprogenitor cells through APP signaling
    • Vrotsos E.G., Kolattukudy P.E., Sugaya K. MCP-1 involvement in glial differentiation of neuroprogenitor cells through APP signaling. Brain Res. Bull. 2009, 79:97-103.
    • (2009) Brain Res. Bull. , vol.79 , pp. 97-103
    • Vrotsos, E.G.1    Kolattukudy, P.E.2    Sugaya, K.3
  • 91
    • 83455245194 scopus 로고    scopus 로고
    • Osteoclast precursor differentiation by MCPIP via oxidative stress, endoplasmic reticulum stress, and autophagy
    • Wang K., Niu J., Kim H., Kolattukudy P.E. Osteoclast precursor differentiation by MCPIP via oxidative stress, endoplasmic reticulum stress, and autophagy. J. Mol. Cell Biol. 2011, 3:360-368.
    • (2011) J. Mol. Cell Biol. , vol.3 , pp. 360-368
    • Wang, K.1    Niu, J.2    Kim, H.3    Kolattukudy, P.E.4
  • 93
    • 33750979012 scopus 로고    scopus 로고
    • Destabilization of interleukin-6 mRNA requires a putative RNA stem-loop structure, an AU-rich element, and the RNA-binding protein AUF1
    • Paschoud S., Dogar A.M., Kuntz C., Grisoni-Neupert B., Richman L., Kuhn L.C. Destabilization of interleukin-6 mRNA requires a putative RNA stem-loop structure, an AU-rich element, and the RNA-binding protein AUF1. Mol. Cell. Biol. 2006, 26:8228-8241.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8228-8241
    • Paschoud, S.1    Dogar, A.M.2    Kuntz, C.3    Grisoni-Neupert, B.4    Richman, L.5    Kuhn, L.C.6
  • 94
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun S.C. Deubiquitylation and regulation of the immune response. Nat. Rev. Immunol. 2008, 8:501-511.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 96
    • 77954176472 scopus 로고    scopus 로고
    • MCP-induced protein 1 suppresses TNFalpha-induced VCAM-1 expression in human endothelial cells
    • Qi Y., Liang J., She Z.G., Cai Y., Wang J., Lei T., Stallcup W.B., Fu M. MCP-induced protein 1 suppresses TNFalpha-induced VCAM-1 expression in human endothelial cells. FEBS Lett. 2010, 584:3065-3072.
    • (2010) FEBS Lett. , vol.584 , pp. 3065-3072
    • Qi, Y.1    Liang, J.2    She, Z.G.3    Cai, Y.4    Wang, J.5    Lei, T.6    Stallcup, W.B.7    Fu, M.8
  • 97
    • 79959521145 scopus 로고    scopus 로고
    • MCP-1-induced protein attenuates endotoxin-induced myocardial dysfunction by suppressing cardiac NF-kappaB activation via inhibition of IkappaB kinase activation
    • Niu J., Wang K., Graham S., Azfer A., Kolattukudy P.E. MCP-1-induced protein attenuates endotoxin-induced myocardial dysfunction by suppressing cardiac NF-kappaB activation via inhibition of IkappaB kinase activation. J. Mol. Cell. Cardiol. 2011, 51:177-186.
    • (2011) J. Mol. Cell. Cardiol. , vol.51 , pp. 177-186
    • Niu, J.1    Wang, K.2    Graham, S.3    Azfer, A.4    Kolattukudy, P.E.5
  • 98
    • 82355184529 scopus 로고    scopus 로고
    • Monocyte chemotactic protein-induced protein 1 (MCPIP1) suppresses stress granule formation and determines apoptosis under stress
    • Qi D., Huang S., Miao R., She Z.G., Quinn T., Chang Y., Liu J., Fan D., Chen Y.E., Fu M. Monocyte chemotactic protein-induced protein 1 (MCPIP1) suppresses stress granule formation and determines apoptosis under stress. J. Biol. Chem. 2011, 286:41692-41700.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41692-41700
    • Qi, D.1    Huang, S.2    Miao, R.3    She, Z.G.4    Quinn, T.5    Chang, Y.6    Liu, J.7    Fan, D.8    Chen, Y.E.9    Fu, M.10
  • 100
    • 84155173319 scopus 로고    scopus 로고
    • Participation of MCP-induced protein 1 in lipopolysaccharide preconditioning-induced ischemic stroke tolerance by regulating the expression of proinflammatory cytokines
    • Liang J., Wang J., Saad Y., Warble L., Becerra E., Kolattukudy P.E. Participation of MCP-induced protein 1 in lipopolysaccharide preconditioning-induced ischemic stroke tolerance by regulating the expression of proinflammatory cytokines. J. Neuroinflammation 2011, 8:182.
    • (2011) J. Neuroinflammation , vol.8 , pp. 182
    • Liang, J.1    Wang, J.2    Saad, Y.3    Warble, L.4    Becerra, E.5    Kolattukudy, P.E.6
  • 101
    • 84865648833 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling inflammation and synthesis of acute phase proteins
    • InTech, F. Veas (Ed.)
    • Jura J., Koj A. Regulatory mechanisms controlling inflammation and synthesis of acute phase proteins. Acute Phase Proteins-Regulation and Functions of Acute Phase Proteins 2011, 61-84. InTech. F. Veas (Ed.).
    • (2011) Acute Phase Proteins-Regulation and Functions of Acute Phase Proteins , pp. 61-84
    • Jura, J.1    Koj, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.