메뉴 건너뛰기




Volumn 1849, Issue 7, 2015, Pages 861-870

Stress granules, P-bodies and cancer

Author keywords

Apoptosis; Cancer; P body; Post transcriptional regulation; Stress granule; Stress response

Indexed keywords

ANTIINFECTIVE AGENT; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; FLUOROURACIL; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; RNA; SODIUM SELENITE;

EID: 84930823568     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2014.11.009     Document Type: Review
Times cited : (318)

References (172)
  • 1
    • 22444435897 scopus 로고    scopus 로고
    • Process or perish: quality control in mRNA biogenesis
    • Fasken M.B., Corbett A.H. Process or perish: quality control in mRNA biogenesis. Nat. Struct. Mol. Biol. 2005, 12:482-488.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 482-488
    • Fasken, M.B.1    Corbett, A.H.2
  • 6
    • 84875781795 scopus 로고    scopus 로고
    • Post-transcriptional regulatory networks in immunity
    • Ivanov P., Anderson P. Post-transcriptional regulatory networks in immunity. Immunol. Rev. 2013, 253:253-272.
    • (2013) Immunol. Rev. , vol.253 , pp. 253-272
    • Ivanov, P.1    Anderson, P.2
  • 7
    • 84901033525 scopus 로고    scopus 로고
    • Principles and properties of eukaryotic mRNPs
    • Mitchell S.F., Parker R. Principles and properties of eukaryotic mRNPs. Mol. Cell 2014, 54:547-558.
    • (2014) Mol. Cell , vol.54 , pp. 547-558
    • Mitchell, S.F.1    Parker, R.2
  • 9
    • 84920847059 scopus 로고    scopus 로고
    • MRNP granules: assembly, function, and connections with disease
    • Buchan J.R. mRNP granules: assembly, function, and connections with disease. RNA Biol. 2014, 11.
    • (2014) RNA Biol. , vol.11
    • Buchan, J.R.1
  • 10
    • 84876453384 scopus 로고    scopus 로고
    • Regulation of stress granules and P-bodies during RNA virus infection
    • Lloyd R.E. Regulation of stress granules and P-bodies during RNA virus infection. Wiley interdiscip. Rev. RNA 2013, 4:317-331.
    • (2013) Wiley interdiscip. Rev. RNA , vol.4 , pp. 317-331
    • Lloyd, R.E.1
  • 11
    • 84887043259 scopus 로고    scopus 로고
    • Role of stress granules and RNA-binding proteins in neurodegeneration: a mini-review
    • Vanderweyde T., Youmans K., Liu-Yesucevitz L., Wolozin B. Role of stress granules and RNA-binding proteins in neurodegeneration: a mini-review. Gerontology 2013, 59:524-533.
    • (2013) Gerontology , vol.59 , pp. 524-533
    • Vanderweyde, T.1    Youmans, K.2    Liu-Yesucevitz, L.3    Wolozin, B.4
  • 13
    • 84858442444 scopus 로고    scopus 로고
    • Mechanisms of deadenylation-dependent decay
    • Chen C.Y., Shyu A.B. Mechanisms of deadenylation-dependent decay. Wiley Interdiscip. Rev. RNA 2011, 2:167-183.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 167-183
    • Chen, C.Y.1    Shyu, A.B.2
  • 14
    • 41149138114 scopus 로고    scopus 로고
    • Multifunctional deadenylase complexes diversify mRNA control
    • Goldstrohm A.C., Wickens M. Multifunctional deadenylase complexes diversify mRNA control. Nat. Rev. Mol. Cell Biol. 2008, 9:337-344.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 337-344
    • Goldstrohm, A.C.1    Wickens, M.2
  • 15
    • 84877801967 scopus 로고    scopus 로고
    • RNA decay machines: deadenylation by the Ccr4-not and Pan2-Pan3 complexes
    • Wahle E., Winkler G.S. RNA decay machines: deadenylation by the Ccr4-not and Pan2-Pan3 complexes. Biochim. Biophys. Acta 2013, 1829:561-570.
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 561-570
    • Wahle, E.1    Winkler, G.S.2
  • 16
    • 80053910875 scopus 로고    scopus 로고
    • Structural and functional insights into eukaryotic mRNA decapping
    • Ling S.H., Qamra R., Song H. Structural and functional insights into eukaryotic mRNA decapping. Wiley Interdiscip. Rev. RNA 2011, 2:193-208.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 193-208
    • Ling, S.H.1    Qamra, R.2    Song, H.3
  • 17
    • 84858446718 scopus 로고    scopus 로고
    • Regulation of cytoplasmic mRNA decay
    • Schoenberg D.R., Maquat L.E. Regulation of cytoplasmic mRNA decay. Nat. Rev. Genet. 2012, 13:246-259.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 246-259
    • Schoenberg, D.R.1    Maquat, L.E.2
  • 18
    • 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
  • 19
    • 0031030491 scopus 로고    scopus 로고
    • A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates
    • Bashkirov V.I., Scherthan H., Solinger J.A., Buerstedde J.M., Heyer W.D. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J. Cell Biol. 1997, 136:761-773.
    • (1997) J. Cell Biol. , vol.136 , pp. 761-773
    • Bashkirov, V.I.1    Scherthan, H.2    Solinger, J.A.3    Buerstedde, J.M.4    Heyer, W.D.5
  • 20
    • 0036909093 scopus 로고    scopus 로고
    • The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
    • Ingelfinger D., Arndt-Jovin D.J., Luhrmann R., Achsel T. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 2002, 8:1489-1501.
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Luhrmann, R.3    Achsel, T.4
  • 21
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • van Dijk E., Cougot N., Meyer S., Babajko S., Wahle E., Seraphin B. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 2002, 21:6915-6924.
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5    Seraphin, B.6
  • 22
    • 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
  • 23
    • 28344456221 scopus 로고    scopus 로고
    • Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body
    • Yu J.H., Yang W.H., Gulick T., Bloch K.D., Bloch D.B. Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body. RNA 2005, 11:1795-1802.
    • (2005) RNA , vol.11 , pp. 1795-1802
    • Yu, J.H.1    Yang, W.H.2    Gulick, T.3    Bloch, K.D.4    Bloch, D.B.5
  • 24
    • 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
  • 27
    • 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
  • 28
    • 16844365216 scopus 로고    scopus 로고
    • The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules
    • Wilczynska A., Aigueperse C., Kress M., Dautry F., Weil D. The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules. J. Cell Sci. 2005, 118:981-992.
    • (2005) J. Cell Sci. , vol.118 , pp. 981-992
    • Wilczynska, A.1    Aigueperse, C.2    Kress, M.3    Dautry, F.4    Weil, D.5
  • 29
    • 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
  • 30
    • 47549087539 scopus 로고    scopus 로고
    • Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells
    • Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B. Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J. Cell Biol. 2008, 182:89-101.
    • (2008) J. Cell Biol. , vol.182 , pp. 89-101
    • Zheng, D.1    Ezzeddine, N.2    Chen, C.Y.3    Zhu, W.4    He, X.5    Shyu, A.B.6
  • 31
    • 36049016095 scopus 로고    scopus 로고
    • Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation
    • Ezzeddine N., Chang T.C., Zhu W., Yamashita A., Chen C.Y., Zhong Z., Yamashita Y., Zheng D., Shyu A.B. Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation. Mol. Cell. Biol. 2007, 27:7791-7801.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7791-7801
    • Ezzeddine, N.1    Chang, T.C.2    Zhu, W.3    Yamashita, A.4    Chen, C.Y.5    Zhong, Z.6    Yamashita, Y.7    Zheng, D.8    Shyu, A.B.9
  • 32
    • 34547625136 scopus 로고    scopus 로고
    • Inhibition of nonsense-mediated mRNA decay (NMD) by a new chemical molecule reveals the dynamic of NMD factors in P-bodies
    • Durand S., Cougot N., Mahuteau-Betzer F., Nguyen C.H., Grierson D.S., Bertrand E., Tazi J., Lejeune F. Inhibition of nonsense-mediated mRNA decay (NMD) by a new chemical molecule reveals the dynamic of NMD factors in P-bodies. J. Cell Biol. 2007, 178:1145-1160.
    • (2007) J. Cell Biol. , vol.178 , pp. 1145-1160
    • Durand, S.1    Cougot, N.2    Mahuteau-Betzer, F.3    Nguyen, C.H.4    Grierson, D.S.5    Bertrand, E.6    Tazi, J.7    Lejeune, F.8
  • 33
    • 33744977432 scopus 로고    scopus 로고
    • Targeting of aberrant mRNAs to cytoplasmic processing bodies
    • Sheth U., Parker R. Targeting of aberrant mRNAs to cytoplasmic processing bodies. Cell 2006, 125:1095-1109.
    • (2006) Cell , vol.125 , pp. 1095-1109
    • Sheth, U.1    Parker, R.2
  • 34
    • 8844245615 scopus 로고    scopus 로고
    • SMG7 acts as a molecular link between mRNA surveillance and mRNA decay
    • Unterholzner L., Izaurralde E. SMG7 acts as a molecular link between mRNA surveillance and mRNA decay. Mol. Cell 2004, 16:587-596.
    • (2004) Mol. Cell , vol.16 , pp. 587-596
    • Unterholzner, L.1    Izaurralde, E.2
  • 35
    • 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
  • 36
    • 33947324981 scopus 로고    scopus 로고
    • In a tight spot: ARE-mRNAs at processing bodies
    • Stoecklin G., Anderson P. In a tight spot: ARE-mRNAs at processing bodies. Genes Dev. 2007, 21:627-631.
    • (2007) Genes Dev. , vol.21 , pp. 627-631
    • Stoecklin, G.1    Anderson, P.2
  • 37
    • 0141856112 scopus 로고    scopus 로고
    • The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies
    • Eystathioy T., Jakymiw A., Chan E.K., Seraphin B., Cougot N., Fritzler M.J. The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies. RNA 2003, 9:1171-1173.
    • (2003) RNA , vol.9 , pp. 1171-1173
    • Eystathioy, T.1    Jakymiw, A.2    Chan, E.K.3    Seraphin, B.4    Cougot, N.5    Fritzler, M.J.6
  • 38
    • 22144478256 scopus 로고    scopus 로고
    • MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies
    • Liu J., Valencia-Sanchez M.A., Hannon G.J., Parker R. MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Nat. Cell Biol. 2005, 7:719-723.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 719-723
    • Liu, J.1    Valencia-Sanchez, M.A.2    Hannon, G.J.3    Parker, R.4
  • 39
    • 20444427566 scopus 로고    scopus 로고
    • Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies
    • Sen G.L., Blau H.M. Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies. Nat. Cell Biol. 2005, 7:633-636.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 633-636
    • Sen, G.L.1    Blau, H.M.2
  • 40
    • 17844371700 scopus 로고    scopus 로고
    • A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    • Andrei M.A., Ingelfinger D., Heintzmann R., Achsel T., Rivera-Pomar R., Luhrmann R. A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA 2005, 11:717-727.
    • (2005) RNA , vol.11 , pp. 717-727
    • Andrei, M.A.1    Ingelfinger, D.2    Heintzmann, R.3    Achsel, T.4    Rivera-Pomar, R.5    Luhrmann, R.6
  • 42
    • 40449118318 scopus 로고    scopus 로고
    • Identification of PCBP2, a facilitator of IRES-mediated translation, as a novel constituent of stress granules and processing bodies
    • Fujimura K., Kano F., Murata M. Identification of PCBP2, a facilitator of IRES-mediated translation, as a novel constituent of stress granules and processing bodies. RNA 2008, 14:425-431.
    • (2008) RNA , vol.14 , pp. 425-431
    • Fujimura, K.1    Kano, F.2    Murata, M.3
  • 44
    • 33845295461 scopus 로고    scopus 로고
    • Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules
    • Leung A.K., Calabrese J.M., Sharp P.A. Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:18125-18130.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18125-18130
    • Leung, A.K.1    Calabrese, J.M.2    Sharp, P.A.3
  • 45
    • 76349083121 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decapping occurs on polyribosomes in Saccharomyces cerevisiae
    • Hu W., Petzold C., Coller J., Baker K.E. Nonsense-mediated mRNA decapping occurs on polyribosomes in Saccharomyces cerevisiae. Nat. Struct. Mol. Biol. 2010, 17:244-247.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 244-247
    • Hu, W.1    Petzold, C.2    Coller, J.3    Baker, K.E.4
  • 46
    • 70249141564 scopus 로고    scopus 로고
    • Co-translational mRNA decay in Saccharomyces cerevisiae
    • Hu W., Sweet T.J., Chamnongpol S., Baker K.E., Coller J. Co-translational mRNA decay in Saccharomyces cerevisiae. Nature 2009, 461:225-229.
    • (2009) Nature , vol.461 , pp. 225-229
    • Hu, W.1    Sweet, T.J.2    Chamnongpol, S.3    Baker, K.E.4    Coller, J.5
  • 47
    • 84918594125 scopus 로고    scopus 로고
    • Quantifying mRNA targeting to P-bodies in living human cells reveals their dual role in mRNA decay and storage
    • Aizer A., Kalo A., Kafri P., Shraga A., Ben-Yishay R., Jacob A., Kinor N., Shav-Tal Y. Quantifying mRNA targeting to P-bodies in living human cells reveals their dual role in mRNA decay and storage. J. Cell Sci. 2014, 127:4443-4456.
    • (2014) J. Cell Sci. , vol.127 , pp. 4443-4456
    • Aizer, A.1    Kalo, A.2    Kafri, P.3    Shraga, A.4    Ben-Yishay, R.5    Jacob, A.6    Kinor, N.7    Shav-Tal, Y.8
  • 50
    • 84884587610 scopus 로고    scopus 로고
    • Stress granules and cell signaling: more than just a passing phase?
    • Kedersha N., Ivanov P., Anderson P. Stress granules and cell signaling: more than just a passing phase?. Trends Biochem. Sci. 2013, 38:494-506.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 494-506
    • Kedersha, N.1    Ivanov, P.2    Anderson, P.3
  • 51
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha N.L., Gupta M., Li W., Miller I., Anderson P. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J. Cell Biol. 1999, 147:1431-1442.
    • (1999) J. Cell Biol. , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 52
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M., Sonenberg N. Translational control in stress and apoptosis. Nat. Rev. Mol. Cell Biol. 2005, 6:318-327.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 53
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson R.J., Hellen C.U., Pestova T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 2010, 11:113-127.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 55
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • Kedersha N., Chen S., Gilks N., Li W., Miller I.J., Stahl J., Anderson P. Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol. Biol. Cell 2002, 13:195-210.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5    Stahl, J.6    Anderson, P.7
  • 60
    • 33744973775 scopus 로고    scopus 로고
    • Relief of microRNA-mediated translational repression in human cells subjected to stress
    • Bhattacharyya S.N., Habermacher R., Martine U., Closs E.I., Filipowicz W. Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 2006, 125:1111-1124.
    • (2006) Cell , vol.125 , pp. 1111-1124
    • Bhattacharyya, S.N.1    Habermacher, R.2    Martine, U.3    Closs, E.I.4    Filipowicz, W.5
  • 61
    • 33847193509 scopus 로고    scopus 로고
    • Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules
    • Gallois-Montbrun S., Kramer B., Swanson C.M., Byers H., Lynham S., Ward M., Malim M.H. Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules. J. Virol. 2007, 81:2165-2178.
    • (2007) J. Virol. , vol.81 , pp. 2165-2178
    • Gallois-Montbrun, S.1    Kramer, B.2    Swanson, C.M.3    Byers, H.4    Lynham, S.5    Ward, M.6    Malim, M.H.7
  • 62
    • 67749145232 scopus 로고    scopus 로고
    • Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies
    • Pare J.M., Tahbaz N., Lopez-Orozco J., LaPointe P., Lasko P., Hobman T.C. Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies. Mol. Biol. Cell 2009, 20:3273-3284.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3273-3284
    • Pare, J.M.1    Tahbaz, N.2    Lopez-Orozco, J.3    LaPointe, P.4    Lasko, P.5    Hobman, T.C.6
  • 64
    • 34247360454 scopus 로고    scopus 로고
    • Probing the mRNA processing body using protein macroarrays and "autoantigenomics"
    • Yang W.H., Bloch D.B. Probing the mRNA processing body using protein macroarrays and "autoantigenomics". RNA 2007, 13:704-712.
    • (2007) RNA , vol.13 , pp. 704-712
    • Yang, W.H.1    Bloch, D.B.2
  • 65
    • 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
  • 66
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn T., Kedersha N., Hickman T., Tisdale S., Anderson P. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat. Cell Biol. 2008, 10:1224-1231.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5
  • 67
    • 34547860022 scopus 로고    scopus 로고
    • GW body disassembly triggered by siRNAs independently of their silencing activity
    • Serman A., Le Roy F., Aigueperse C., Kress M., Dautry F., Weil D. GW body disassembly triggered by siRNAs independently of their silencing activity. Nucleic Acids Res. 2007, 35:4715-4727.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4715-4727
    • Serman, A.1    Le Roy, F.2    Aigueperse, C.3    Kress, M.4    Dautry, F.5    Weil, D.6
  • 68
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: possible roles in the control of translation and mRNA degradation
    • Decker C.J., Parker R. P-bodies and stress granules: possible roles in the control of translation and mRNA degradation. Cold Spring Harb. Perspect. Biol. 2012, 4:a012286.
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. a012286
    • Decker, C.J.1    Parker, R.2
  • 70
    • 84873537120 scopus 로고    scopus 로고
    • Relationship of GW/P-bodies with stress granules
    • Stoecklin G., Kedersha N. Relationship of GW/P-bodies with stress granules. Adv. Exp. Med. Biol. 2013, 768:197-211.
    • (2013) Adv. Exp. Med. Biol. , vol.768 , pp. 197-211
    • Stoecklin, G.1    Kedersha, N.2
  • 71
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson P., Kedersha N. Stress granules: the Tao of RNA triage. Trends Biochem. Sci. 2008, 33:141-150.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 72
    • 84866782195 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism
    • Baird T.D., Wek R.C. Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism. Adv. Nutr. 2012, 3:307-321.
    • (2012) Adv. Nutr. , vol.3 , pp. 307-321
    • Baird, T.D.1    Wek, R.C.2
  • 74
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek S.A., Zhu S., Wek R.C. The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 1995, 15:4497-4506.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 75
    • 20144378698 scopus 로고    scopus 로고
    • Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure
    • McEwen E., Kedersha N., Song B., Scheuner D., Gilks N., Han A., Chen J.J., Anderson P., Kaufman R.J. Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J. Biol. Chem. 2005, 280:16925-16933.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16925-16933
    • McEwen, E.1    Kedersha, N.2    Song, B.3    Scheuner, D.4    Gilks, N.5    Han, A.6    Chen, J.J.7    Anderson, P.8    Kaufman, R.J.9
  • 76
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 2000, 6:1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 77
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H.P., Zhang Y., Bertolotti A., Zeng H., Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 2000, 5:897-904.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 78
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase
    • Srivastava S.P., Kumar K.U., Kaufman R.J. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 1998, 273:2416-2423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 79
    • 84904732950 scopus 로고    scopus 로고
    • Hypoxia, lipids, and cancer: surviving the harsh tumor microenvironment
    • Ackerman D., Simon M.C. Hypoxia, lipids, and cancer: surviving the harsh tumor microenvironment. Trends Cell Biol. 2014, 24:472-478.
    • (2014) Trends Cell Biol. , vol.24 , pp. 472-478
    • Ackerman, D.1    Simon, M.C.2
  • 82
    • 84889575198 scopus 로고    scopus 로고
    • Modulation of oxidative stress as an anticancer strategy
    • Gorrini C., Harris I.S., Mak T.W. Modulation of oxidative stress as an anticancer strategy. Nat. Rev. Drug Discov. 2013, 12:931-947.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 931-947
    • Gorrini, C.1    Harris, I.S.2    Mak, T.W.3
  • 83
    • 84897504519 scopus 로고    scopus 로고
    • The role of reactive oxygen species and metabolism on cancer cells and their microenvironment
    • Costa A., Scholer-Dahirel A., Mechta-Grigoriou F. The role of reactive oxygen species and metabolism on cancer cells and their microenvironment. Semin. Cancer Biol. 2014, 25:23-32.
    • (2014) Semin. Cancer Biol. , vol.25 , pp. 23-32
    • Costa, A.1    Scholer-Dahirel, A.2    Mechta-Grigoriou, F.3
  • 84
    • 84867169460 scopus 로고    scopus 로고
    • Oxidative modification of proteins: an emerging mechanism of cell signaling
    • Wall S.B., Oh J.Y., Diers A.R., Landar A. Oxidative modification of proteins: an emerging mechanism of cell signaling. Front. Physiol. 2012, 3:369.
    • (2012) Front. Physiol. , vol.3 , pp. 369
    • Wall, S.B.1    Oh, J.Y.2    Diers, A.R.3    Landar, A.4
  • 86
    • 37449030154 scopus 로고    scopus 로고
    • The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response
    • Kwon S., Zhang Y., Matthias P. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev. 2007, 21:3381-3394.
    • (2007) Genes Dev. , vol.21 , pp. 3381-3394
    • Kwon, S.1    Zhang, Y.2    Matthias, P.3
  • 87
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto K., Fukuda H., Imajoh-Ohmi S., Saito H., Takekawa M. Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat. Cell Biol. 2008, 10:1324-1332.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 88
    • 14844360344 scopus 로고    scopus 로고
    • Sequestration of TRAF2 into stress granules interrupts tumor necrosis factor signaling under stress conditions
    • Kim W.J., Back S.H., Kim V., Ryu I., Jang S.K. Sequestration of TRAF2 into stress granules interrupts tumor necrosis factor signaling under stress conditions. Mol. Cell. Biol. 2005, 25:2450-2462.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2450-2462
    • Kim, W.J.1    Back, S.H.2    Kim, V.3    Ryu, I.4    Jang, S.K.5
  • 89
    • 2342611976 scopus 로고    scopus 로고
    • Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors: role of reoxygenation, free radicals, and stress granules
    • Moeller B.J., Cao Y., Li C.Y., Dewhirst M.W. Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors: role of reoxygenation, free radicals, and stress granules. Cancer Cell 2004, 5:429-441.
    • (2004) Cancer Cell , vol.5 , pp. 429-441
    • Moeller, B.J.1    Cao, Y.2    Li, C.Y.3    Dewhirst, M.W.4
  • 91
    • 84870270861 scopus 로고    scopus 로고
    • Selenite targets eIF4E-binding protein-1 to inhibit translation initiation and induce the assembly of non-canonical stress granules
    • Fujimura K., Sasaki A.T., Anderson P. Selenite targets eIF4E-binding protein-1 to inhibit translation initiation and induce the assembly of non-canonical stress granules. Nucleic Acids Res. 2012, 40:8099-8110.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8099-8110
    • Fujimura, K.1    Sasaki, A.T.2    Anderson, P.3
  • 94
    • 77955994655 scopus 로고    scopus 로고
    • Human G3BP1 interacts with beta-F1-ATPase mRNA and inhibits its translation
    • Ortega A.D., Willers I.M., Sala S., Cuezva J.M. Human G3BP1 interacts with beta-F1-ATPase mRNA and inhibits its translation. J. Cell Sci. 2010, 123:2685-2696.
    • (2010) J. Cell Sci. , vol.123 , pp. 2685-2696
    • Ortega, A.D.1    Willers, I.M.2    Sala, S.3    Cuezva, J.M.4
  • 96
    • 77957916346 scopus 로고    scopus 로고
    • G3BP: a promising target for cancer therapy
    • Zhang H., Shao R.G. G3BP: a promising target for cancer therapy. Yao Xue Xue Bao 2010, 45:945-951.
    • (2010) Yao Xue Xue Bao , vol.45 , pp. 945-951
    • Zhang, H.1    Shao, R.G.2
  • 97
    • 84890979013 scopus 로고    scopus 로고
    • USP10 antagonizes c-Myc transcriptional activation through SIRT6 stabilization to suppress tumor formation
    • Lin Z., Yang H., Tan C., Li J., Liu Z., Quan Q., Kong S., Ye J., Gao B., Fang D. USP10 antagonizes c-Myc transcriptional activation through SIRT6 stabilization to suppress tumor formation. Cell Rep. 2013, 5:1639-1649.
    • (2013) Cell Rep. , vol.5 , pp. 1639-1649
    • Lin, Z.1    Yang, H.2    Tan, C.3    Li, J.4    Liu, Z.5    Quan, Q.6    Kong, S.7    Ye, J.8    Gao, B.9    Fang, D.10
  • 98
    • 77951598447 scopus 로고    scopus 로고
    • The chemotherapeutic agent bortezomib induces the formation of stress granules
    • Fournier M.J., Gareau C., Mazroui R. The chemotherapeutic agent bortezomib induces the formation of stress granules. Cancer Cell Int. 2010, 10:12.
    • (2010) Cancer Cell Int. , vol.10 , pp. 12
    • Fournier, M.J.1    Gareau, C.2    Mazroui, R.3
  • 99
    • 34347406608 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system induces stress granule formation
    • Mazroui R., Di Marco S., Kaufman R.J., Gallouzi I.E. Inhibition of the ubiquitin-proteasome system induces stress granule formation. Mol. Biol. Cell 2007, 18:2603-2618.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2603-2618
    • Mazroui, R.1    Di Marco, S.2    Kaufman, R.J.3    Gallouzi, I.E.4
  • 100
    • 33749493493 scopus 로고    scopus 로고
    • Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation
    • Mazroui R., Sukarieh R., Bordeleau M.E., Kaufman R.J., Northcote P., Tanaka J., Gallouzi I., Pelletier J. Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation. Mol. Biol. Cell 2006, 17:4212-4219.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4212-4219
    • Mazroui, R.1    Sukarieh, R.2    Bordeleau, M.E.3    Kaufman, R.J.4    Northcote, P.5    Tanaka, J.6    Gallouzi, I.7    Pelletier, J.8
  • 101
    • 79957547144 scopus 로고    scopus 로고
    • P21(WAF1/CIP1) upregulation through the stress granule-associated protein CUGBP1 confers resistance to bortezomib-mediated apoptosis
    • Gareau C., Fournier M.J., Filion C., Coudert L., Martel D., Labelle Y., Mazroui R. p21(WAF1/CIP1) upregulation through the stress granule-associated protein CUGBP1 confers resistance to bortezomib-mediated apoptosis. PLoS One 2011, 6:e20254.
    • (2011) PLoS One , vol.6 , pp. e20254
    • Gareau, C.1    Fournier, M.J.2    Filion, C.3    Coudert, L.4    Martel, D.5    Labelle, Y.6    Mazroui, R.7
  • 102
    • 84903215050 scopus 로고    scopus 로고
    • 5-Fluorouracil affects assembly of stress granules based on RNA incorporation
    • Kaehler C., Isensee J., Hucho T., Lehrach H., Krobitsch S. 5-Fluorouracil affects assembly of stress granules based on RNA incorporation. Nucleic Acids Res. 2014, 42:6436-6447.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 6436-6447
    • Kaehler, C.1    Isensee, J.2    Hucho, T.3    Lehrach, H.4    Krobitsch, S.5
  • 103
    • 0038387494 scopus 로고    scopus 로고
    • 5-fluorouracil: mechanisms of action and clinical strategies
    • Longley D.B., Harkin D.P., Johnston P.G. 5-fluorouracil: mechanisms of action and clinical strategies. Nat. Rev. Cancer 2003, 3:330-338.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 330-338
    • Longley, D.B.1    Harkin, D.P.2    Johnston, P.G.3
  • 105
    • 80051752025 scopus 로고    scopus 로고
    • MicroRNA 130 family regulates the hypoxia response signal through the P-body protein DDX6
    • Saito K., Kondo E., Matsushita M. MicroRNA 130 family regulates the hypoxia response signal through the P-body protein DDX6. Nucleic Acids Res. 2011, 39:6086-6099.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6086-6099
    • Saito, K.1    Kondo, E.2    Matsushita, M.3
  • 106
    • 37149023303 scopus 로고    scopus 로고
    • Anti-inflammatory lipid mediator 15d-PGJ2 inhibits translation through inactivation of eIF4A
    • Kim W.J., Kim J.H., Jang S.K. Anti-inflammatory lipid mediator 15d-PGJ2 inhibits translation through inactivation of eIF4A. EMBO J. 2007, 26:5020-5032.
    • (2007) EMBO J. , vol.26 , pp. 5020-5032
    • Kim, W.J.1    Kim, J.H.2    Jang, S.K.3
  • 107
    • 69949093640 scopus 로고    scopus 로고
    • 15d-PGJ2 induces apoptosis by reactive oxygen species-mediated inactivation of Akt in leukemia and colorectal cancer cells and shows in vivo antitumor activity
    • Shin S.W., Seo C.Y., Han H., Han J.Y., Jeong J.S., Kwak J.Y., Park J.I. 15d-PGJ2 induces apoptosis by reactive oxygen species-mediated inactivation of Akt in leukemia and colorectal cancer cells and shows in vivo antitumor activity. Clin. Cancer Res. 2009, 15:5414-5425.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 5414-5425
    • Shin, S.W.1    Seo, C.Y.2    Han, H.3    Han, J.Y.4    Jeong, J.S.5    Kwak, J.Y.6    Park, J.I.7
  • 113
    • 33845950751 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A
    • Dang Y., Kedersha N., Low W.K., Romo D., Gorospe M., Kaufman R., Anderson P., Liu J.O. Eukaryotic initiation factor 2alpha-independent pathway of stress granule induction by the natural product pateamine A. J. Biol. Chem. 2006, 281:32870-32878.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32870-32878
    • Dang, Y.1    Kedersha, N.2    Low, W.K.3    Romo, D.4    Gorospe, M.5    Kaufman, R.6    Anderson, P.7    Liu, J.O.8
  • 114
    • 0035025064 scopus 로고    scopus 로고
    • Induction of apoptosis by the marine sponge (Mycale) metabolites, mycalamide A and pateamine
    • Hood K.A., West L.M., Northcote P.T., Berridge M.V., Miller J.H. Induction of apoptosis by the marine sponge (Mycale) metabolites, mycalamide A and pateamine. Apoptosis 2001, 6:207-219.
    • (2001) Apoptosis , vol.6 , pp. 207-219
    • Hood, K.A.1    West, L.M.2    Northcote, P.T.3    Berridge, M.V.4    Miller, J.H.5
  • 116
    • 84875158511 scopus 로고    scopus 로고
    • Synthesis of biotinylated episilvestrol: highly selective targeting of the translation factors eIF4AI/II
    • Chambers J.M., Lindqvist L.M., Webb A., Huang D.C., Savage G.P., Rizzacasa M.A. Synthesis of biotinylated episilvestrol: highly selective targeting of the translation factors eIF4AI/II. Org. Lett. 2013, 15:1406-1409.
    • (2013) Org. Lett. , vol.15 , pp. 1406-1409
    • Chambers, J.M.1    Lindqvist, L.M.2    Webb, A.3    Huang, D.C.4    Savage, G.P.5    Rizzacasa, M.A.6
  • 118
    • 84884645790 scopus 로고    scopus 로고
    • Therapeutic potential of the translation inhibitor silvestrol in hepatocellular cancer
    • Kogure T., Kinghorn A.D., Yan I., Bolon B., Lucas D.M., Grever M.R., Patel T. Therapeutic potential of the translation inhibitor silvestrol in hepatocellular cancer. PLoS One 2013, 8:e76136.
    • (2013) PLoS One , vol.8 , pp. e76136
    • Kogure, T.1    Kinghorn, A.D.2    Yan, I.3    Bolon, B.4    Lucas, D.M.5    Grever, M.R.6    Patel, T.7
  • 119
    • 84904097175 scopus 로고    scopus 로고
    • Single-molecule kinetics of the eukaryotic initiation factor 4AI upon RNA unwinding
    • Sun Y., Atas E., Lindqvist L.M., Sonenberg N., Pelletier J., Meller A. Single-molecule kinetics of the eukaryotic initiation factor 4AI upon RNA unwinding. Structure 2014, 22:941-948.
    • (2014) Structure , vol.22 , pp. 941-948
    • Sun, Y.1    Atas, E.2    Lindqvist, L.M.3    Sonenberg, N.4    Pelletier, J.5    Meller, A.6
  • 122
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante M., Sabatini D.M. mTOR signaling in growth control and disease. Cell 2012, 149:274-293.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 123
    • 84877965001 scopus 로고    scopus 로고
    • Regulation of mTORC1 and its impact on gene expression at a glance
    • Laplante M., Sabatini D.M. Regulation of mTORC1 and its impact on gene expression at a glance. J. Cell Sci. 2013, 126:1713-1719.
    • (2013) J. Cell Sci. , vol.126 , pp. 1713-1719
    • Laplante, M.1    Sabatini, D.M.2
  • 124
    • 79958026380 scopus 로고    scopus 로고
    • The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation
    • Mendoza M.C., Er E.E., Blenis J. The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation. Trends Biochem. Sci. 2011, 36:320-328.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 320-328
    • Mendoza, M.C.1    Er, E.E.2    Blenis, J.3
  • 125
    • 84874040052 scopus 로고    scopus 로고
    • Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling
    • Wippich F., Bodenmiller B., Trajkovska M.G., Wanka S., Aebersold R., Pelkmans L. Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling. Cell 2013, 152:791-805.
    • (2013) Cell , vol.152 , pp. 791-805
    • Wippich, F.1    Bodenmiller, B.2    Trajkovska, M.G.3    Wanka, S.4    Aebersold, R.5    Pelkmans, L.6
  • 126
    • 80052736325 scopus 로고    scopus 로고
    • Redox regulates mammalian target of rapamycin complex 1 (mTORC1) activity by modulating the TSC1/TSC2-Rheb GTPase pathway
    • Yoshida S., Hong S., Suzuki T., Nada S., Mannan A.M., Wang J., Okada M., Guan K.L., Inoki K. Redox regulates mammalian target of rapamycin complex 1 (mTORC1) activity by modulating the TSC1/TSC2-Rheb GTPase pathway. J. Biol. Chem. 2011, 286:32651-32660.
    • (2011) J. Biol. Chem. , vol.286 , pp. 32651-32660
    • Yoshida, S.1    Hong, S.2    Suzuki, T.3    Nada, S.4    Mannan, A.M.5    Wang, J.6    Okada, M.7    Guan, K.L.8    Inoki, K.9
  • 128
    • 80053625750 scopus 로고    scopus 로고
    • Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR
    • Damgaard C.K., Lykke-Andersen J. Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR. Genes Dev. 2011, 25:2057-2068.
    • (2011) Genes Dev. , vol.25 , pp. 2057-2068
    • Damgaard, C.K.1    Lykke-Andersen, J.2
  • 130
    • 33646764191 scopus 로고    scopus 로고
    • The cap-dependent translation apparatus integrates and amplifies cancer pathways
    • Polunovsky V.A., Bitterman P.B. The cap-dependent translation apparatus integrates and amplifies cancer pathways. RNA Biol. 2006, 3:10-17.
    • (2006) RNA Biol. , vol.3 , pp. 10-17
    • Polunovsky, V.A.1    Bitterman, P.B.2
  • 131
    • 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
  • 134
    • 80053537984 scopus 로고    scopus 로고
    • RACK1, A multifaceted scaffolding protein: structure and function
    • Adams D.R., Ron D., Kiely P.A. RACK1, A multifaceted scaffolding protein: structure and function. Cell Commun. Signal. 2011, 9:22.
    • (2011) Cell Commun. Signal. , vol.9 , pp. 22
    • Adams, D.R.1    Ron, D.2    Kiely, P.A.3
  • 135
    • 84890450061 scopus 로고    scopus 로고
    • RACK1 function in cell motility and protein synthesis
    • Gandin V., Senft D., Topisirovic I., Ronai Z.A. RACK1 function in cell motility and protein synthesis. Genes Cancer 2013, 4:369-377.
    • (2013) Genes Cancer , vol.4 , pp. 369-377
    • Gandin, V.1    Senft, D.2    Topisirovic, I.3    Ronai, Z.A.4
  • 136
    • 84930510366 scopus 로고    scopus 로고
    • RACK1, a versatile hub in cancer
    • Li J.J., Xie D. RACK1, a versatile hub in cancer. Oncogene 2014, 10.1038/onc.2014.127.
    • (2014) Oncogene
    • Li, J.J.1    Xie, D.2
  • 137
    • 34249778349 scopus 로고    scopus 로고
    • Comparative expression of tristetraprolin (TTP) family member transcripts in normal human tissues and cancer cell lines
    • Carrick D.M., Blackshear P.J. Comparative expression of tristetraprolin (TTP) family member transcripts in normal human tissues and cancer cell lines. Arch. Biochem. Biophys. 2007, 462:278-285.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 278-285
    • Carrick, D.M.1    Blackshear, P.J.2
  • 138
    • 67449132368 scopus 로고    scopus 로고
    • The mRNA-destabilizing protein tristetraprolin is suppressed in many cancers, altering tumorigenic phenotypes and patient prognosis
    • Brennan S.E., Kuwano Y., Alkharouf N., Blackshear P.J., Gorospe M., Wilson G.M. The mRNA-destabilizing protein tristetraprolin is suppressed in many cancers, altering tumorigenic phenotypes and patient prognosis. Cancer Res. 2009, 69:5168-5176.
    • (2009) Cancer Res. , vol.69 , pp. 5168-5176
    • Brennan, S.E.1    Kuwano, Y.2    Alkharouf, N.3    Blackshear, P.J.4    Gorospe, M.5    Wilson, G.M.6
  • 139
    • 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
  • 140
    • 64049107465 scopus 로고    scopus 로고
    • MiR-29a suppresses tristetraprolin, which is a regulator of epithelial polarity and metastasis
    • Gebeshuber C.A., Zatloukal K., Martinez J. miR-29a suppresses tristetraprolin, which is a regulator of epithelial polarity and metastasis. EMBO Rep. 2009, 10:400-405.
    • (2009) EMBO Rep. , vol.10 , pp. 400-405
    • Gebeshuber, C.A.1    Zatloukal, K.2    Martinez, J.3
  • 145
    • 76549101962 scopus 로고    scopus 로고
    • Eukaryotic cold shock domain proteins: highly versatile regulators of gene expression
    • Mihailovich M., Militti C., Gabaldon T., Gebauer F. Eukaryotic cold shock domain proteins: highly versatile regulators of gene expression. Bioessays 2010, 32:109-118.
    • (2010) Bioessays , vol.32 , pp. 109-118
    • Mihailovich, M.1    Militti, C.2    Gabaldon, T.3    Gebauer, F.4
  • 146
    • 34447530917 scopus 로고    scopus 로고
    • Localization of the developmental timing regulator Lin28 to mRNP complexes, P-bodies and stress granules
    • Balzer E., Moss E.G. Localization of the developmental timing regulator Lin28 to mRNP complexes, P-bodies and stress granules. RNA Biol. 2007, 4:16-25.
    • (2007) RNA Biol. , vol.4 , pp. 16-25
    • Balzer, E.1    Moss, E.G.2
  • 148
    • 84874939831 scopus 로고    scopus 로고
    • LIN28/LIN28B: an emerging oncogenic driver in cancer stem cells
    • Zhou J., Ng S.B., Chng W.J. LIN28/LIN28B: an emerging oncogenic driver in cancer stem cells. Int. J. Biochem. Cell Biol. 2013, 45:973-978.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 973-978
    • Zhou, J.1    Ng, S.B.2    Chng, W.J.3
  • 149
    • 84875933577 scopus 로고    scopus 로고
    • Lin28: primal regulator of growth and metabolism in stem cells
    • Shyh-Chang N., Daley G.Q. Lin28: primal regulator of growth and metabolism in stem cells. Cell Stem Cell 2013, 12:395-406.
    • (2013) Cell Stem Cell , vol.12 , pp. 395-406
    • Shyh-Chang, N.1    Daley, G.Q.2
  • 152
    • 84885441032 scopus 로고    scopus 로고
    • Ribonuclease/angiogenin inhibitor 1 regulates stress-induced subcellular localization of angiogenin to control growth and survival
    • Pizzo E., Sarcinelli C., Sheng J., Fusco S., Formiggini F., Netti P., Yu W., D'Alessio G., Hu G.F. Ribonuclease/angiogenin inhibitor 1 regulates stress-induced subcellular localization of angiogenin to control growth and survival. J. Cell Sci. 2013, 126:4308-4319.
    • (2013) J. Cell Sci. , vol.126 , pp. 4308-4319
    • Pizzo, E.1    Sarcinelli, C.2    Sheng, J.3    Fusco, S.4    Formiggini, F.5    Netti, P.6    Yu, W.7    D'Alessio, G.8    Hu, G.F.9
  • 153
    • 84863350770 scopus 로고    scopus 로고
    • Emerging role of angiogenin in stress response and cell survival under adverse conditions
    • Li S., Hu G.F. Emerging role of angiogenin in stress response and cell survival under adverse conditions. J. Cell. Physiol. 2012, 227:2822-2826.
    • (2012) J. Cell. Physiol. , vol.227 , pp. 2822-2826
    • Li, S.1    Hu, G.F.2
  • 154
    • 78649940361 scopus 로고    scopus 로고
    • Angiogenin-mediated rRNA transcription in cancer and neurodegeneration
    • Li S., Hu G.F. Angiogenin-mediated rRNA transcription in cancer and neurodegeneration. Int. J. Biochem. Mol. Biol. 2010, 1:26-35.
    • (2010) Int. J. Biochem. Mol. Biol. , vol.1 , pp. 26-35
    • Li, S.1    Hu, G.F.2
  • 156
    • 65249129859 scopus 로고    scopus 로고
    • Angiogenin cleaves tRNA and promotes stress-induced translational repression
    • Yamasaki S., Ivanov P., Hu G.F., Anderson P. Angiogenin cleaves tRNA and promotes stress-induced translational repression. J. Cell Biol. 2009, 185:35-42.
    • (2009) J. Cell Biol. , vol.185 , pp. 35-42
    • Yamasaki, S.1    Ivanov, P.2    Hu, G.F.3    Anderson, P.4
  • 157
    • 84910673620 scopus 로고    scopus 로고
    • TRNA fragments in human health and disease
    • Anderson P., Ivanov P. tRNA fragments in human health and disease. FEBS Lett. 2014, 588:4297-4304.
    • (2014) FEBS Lett. , vol.588 , pp. 4297-4304
    • Anderson, P.1    Ivanov, P.2
  • 159
    • 80051713296 scopus 로고    scopus 로고
    • Angiogenin-induced tRNA fragments inhibit translation initiation
    • Ivanov P., Emara M.M., Villen J., Gygi S.P., Anderson P. Angiogenin-induced tRNA fragments inhibit translation initiation. Mol. Cell 2011, 43:613-623.
    • (2011) Mol. Cell , vol.43 , pp. 613-623
    • Ivanov, P.1    Emara, M.M.2    Villen, J.3    Gygi, S.P.4    Anderson, P.5
  • 160
    • 14644392203 scopus 로고    scopus 로고
    • Anti-tumor effect of hematopoietic cells carrying the gene of ribonuclease inhibitor
    • Fu P., Chen J., Tian Y., Watkins T., Cui X., Zhao B. Anti-tumor effect of hematopoietic cells carrying the gene of ribonuclease inhibitor. Cancer Gene Ther. 2005, 12:268-275.
    • (2005) Cancer Gene Ther. , vol.12 , pp. 268-275
    • Fu, P.1    Chen, J.2    Tian, Y.3    Watkins, T.4    Cui, X.5    Zhao, B.6
  • 161
    • 84860289772 scopus 로고    scopus 로고
    • Up-regulating ribonuclease inhibitor inhibited epithelial-to-mesenchymal transition and metastasis in murine melanoma cells
    • Pan X., Xiong D., Yao X., Xin Y., Zhang L., Chen J. Up-regulating ribonuclease inhibitor inhibited epithelial-to-mesenchymal transition and metastasis in murine melanoma cells. Int. J. Biochem. Cell Biol. 2012, 44:998-1008.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 998-1008
    • Pan, X.1    Xiong, D.2    Yao, X.3    Xin, Y.4    Zhang, L.5    Chen, J.6
  • 162
    • 84883243999 scopus 로고    scopus 로고
    • A novel role of ribonuclease inhibitor in regulation of epithelial-to-mesenchymal transition and ILK signaling pathway in bladder cancer cells
    • Yao X., Li D., Xiong D.M., Li L., Jiang R., Chen J.X. A novel role of ribonuclease inhibitor in regulation of epithelial-to-mesenchymal transition and ILK signaling pathway in bladder cancer cells. Cell Tissue Res. 2013, 353:409-423.
    • (2013) Cell Tissue Res. , vol.353 , pp. 409-423
    • Yao, X.1    Li, D.2    Xiong, D.M.3    Li, L.4    Jiang, R.5    Chen, J.X.6
  • 163
    • 77956311711 scopus 로고    scopus 로고
    • EIF5A promotes translation elongation, polysome disassembly and stress granule assembly
    • Li C.H., Ohn T., Ivanov P., Tisdale S., Anderson P. eIF5A promotes translation elongation, polysome disassembly and stress granule assembly. PLoS ONE 2010, 5:e9942.
    • (2010) PLoS ONE , vol.5 , pp. e9942
    • Li, C.H.1    Ohn, T.2    Ivanov, P.3    Tisdale, S.4    Anderson, P.5
  • 165
    • 80053022305 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex
    • Hilliker A., Gao Z., Jankowsky E., Parker R. The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Mol. Cell 2011, 43:962-972.
    • (2011) Mol. Cell , vol.43 , pp. 962-972
    • Hilliker, A.1    Gao, Z.2    Jankowsky, E.3    Parker, R.4
  • 166
    • 84055178425 scopus 로고    scopus 로고
    • Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response
    • Shih J.W., Wang W.T., Tsai T.Y., Kuo C.Y., Li H.K., Wu Lee Y.H. Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response. Biochem. J. 2012, 441:119-129.
    • (2012) Biochem. J. , vol.441 , pp. 119-129
    • Shih, J.W.1    Wang, W.T.2    Tsai, T.Y.3    Kuo, C.Y.4    Li, H.K.5    Wu Lee, Y.H.6
  • 168
    • 84930275031 scopus 로고    scopus 로고
    • DDX3 modulates cell adhesion and motility and cancer cell metastasis via Rac1-mediated signaling pathway
    • Chen H.H., Yu H.I., Cho W.C., Tarn W.Y. DDX3 modulates cell adhesion and motility and cancer cell metastasis via Rac1-mediated signaling pathway. Oncogene 2014, 10.1038/onc.2014.190.
    • (2014) Oncogene
    • Chen, H.H.1    Yu, H.I.2    Cho, W.C.3    Tarn, W.Y.4
  • 169
    • 58449134534 scopus 로고    scopus 로고
    • Small silencing RNAs: an expanding universe
    • Ghildiyal M., Zamore P.D. Small silencing RNAs: an expanding universe. Nat. Rev. Genet. 2009, 10:94-108.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 94-108
    • Ghildiyal, M.1    Zamore, P.D.2
  • 170
    • 84904985459 scopus 로고    scopus 로고
    • Regulation of microRNA biogenesis
    • Ha M., Kim V.N. Regulation of microRNA biogenesis. Nat. Rev. Mol. Cell Biol. 2014, 15:509-524.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 509-524
    • Ha, M.1    Kim, V.N.2
  • 171
    • 84905122848 scopus 로고    scopus 로고
    • MicroRNAs in cancer: biomarkers, functions and therapy
    • Hayes J., Peruzzi P.P., Lawler S. MicroRNAs in cancer: biomarkers, functions and therapy. Trends Mol. Med. 2014, 20:460-469.
    • (2014) Trends Mol. Med. , vol.20 , pp. 460-469
    • Hayes, J.1    Peruzzi, P.P.2    Lawler, S.3
  • 172
    • 84897978086 scopus 로고    scopus 로고
    • MiRNA dysregulation in cancer: towards a mechanistic understanding
    • Palanichamy J.K., Rao D.S. miRNA dysregulation in cancer: towards a mechanistic understanding. Front. Genet. 2014, 5:54.
    • (2014) Front. Genet. , vol.5 , pp. 54
    • Palanichamy, J.K.1    Rao, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.