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Volumn 33, Issue 1, 2014, Pages

P68 RNA helicase as a molecular target for cancer therapy

Author keywords

Molecular target; P68; Rna helicase; Transcriptional co activator

Indexed keywords

ANDROGEN RECEPTOR; BETA CATENIN; ESTROGEN RECEPTOR ALPHA; PROTEIN P53; PROTEIN P68; RNA HELICASE; ANTINEOPLASTIC AGENT; DEAD BOX PROTEIN; ENZYME INHIBITOR;

EID: 84965191065     PISSN: None     EISSN: 17569966     Source Type: Journal    
DOI: 10.1186/s13046-014-0064-y     Document Type: Review
Times cited : (44)

References (96)
  • 1
    • 0028301073 scopus 로고
    • RNA helicases: Modulators of RNA structure
    • Fuller-Pace FV: RNA helicases: modulators of RNA structure. Trends Cell Biol 1994, 4:271-274.
    • (1994) Trends Cell Biol , vol.4 , pp. 271-274
    • Fuller-Pace, F.V.1
  • 2
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid SR, Linder P: D-E-A-D protein family of putative RNA helicases. Mol Microbiol 1992, 6:283-291.
    • (1992) Mol Microbiol , vol.6 , pp. 283-291
    • Schmid, S.R.1    Linder, P.2
  • 3
    • 0019175348 scopus 로고
    • SV40 large T shares an antigenic determinant with a cellular protein of molecular weight 68,000
    • Lane DP, Hoeffler WK: SV40 large T shares an antigenic determinant with a cellular protein of molecular weight 68,000. Nature 1980, 288:167-170.
    • (1980) Nature , Issue.288 , pp. 167-170
    • Lane, D.P.1    Hoeffler, W.K.2
  • 4
    • 0024462171 scopus 로고
    • Nuclear protein p68 is an RNA-dependent ATPase
    • Iggo RD, Lane DP: Nuclear protein p68 is an RNA-dependent ATPase. EMBO J 1989, 8:1827-1831.
    • (1989) EMBO J , vol.8 , pp. 1827-1831
    • Iggo, R.D.1    Lane, D.P.2
  • 5
    • 84875173647 scopus 로고    scopus 로고
    • DEAD box RNA helicase functions in cancer
    • Fuller-Pace FV: DEAD box RNA helicase functions in cancer. RNA Biol 2013, 10:121-132.
    • (2013) RNA Biol , vol.10 , pp. 121-132
    • Fuller-Pace, F.V.1
  • 7
    • 0032814142 scopus 로고    scopus 로고
    • Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha
    • Endoh H, Maruyama K, Masuhiro Y, Kobayashi Y, Goto M, Tai H, Yanagisawa J, Metzger D, Hashimoto S, Kato S: Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha. Mol Cell Biol 1999, 19:5363-5372.
    • (1999) Mol Cell Biol , vol.19 , pp. 5363-5372
    • Endoh, H.1    Maruyama, K.2    Masuhiro, Y.3    Kobayashi, Y.4    Goto, M.5    Tai, H.6    Yanagisawa, J.7    Metzger, D.8    Hashimoto, S.9    Kato, S.10
  • 12
    • 79952148724 scopus 로고    scopus 로고
    • RNA helicases p68 and p72: Multifunctional proteins with important implications for cancer developmen
    • Fuller-Pace FV, Moore HC: RNA helicases p68 and p72: multifunctional proteins with important implications for cancer development. Future Oncol 2011, 7:239-251.
    • (2011) Future Oncol , vol.7 , pp. 239-251
    • Fuller-Pace, F.V.1    Moore, H.C.2
  • 13
    • 84878106232 scopus 로고    scopus 로고
    • Looking back on the birth of DEAD-box RNA helicases
    • Linder P, Fuller-Pace F: Looking back on the birth of DEAD-box RNA helicases. Biochim Biophys Acta 2013, 8:750-755.
    • (2013) Biochim Biophys Acta , vol.8 , pp. 750-755
    • Linder, P.1    Fuller-Pace, F.2
  • 14
    • 84867064003 scopus 로고    scopus 로고
    • Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p
    • Mallam AL, Del Campo M, Gilman B, Sidote DJ, Lambowitz AM: Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p. Nature 2012, 490:121-125.
    • (2012) Nature , vol.490 , pp. 121-125
    • Mallam, A.L.1    Del Campo, M.2    Gilman, B.3    Sidote, D.J.4    Lambowitz, A.M.5
  • 15
    • 84862975911 scopus 로고    scopus 로고
    • Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer
    • Andreou AZ, Klostermeier D: Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer. Methods Enzymol 2012, 511:75-109.
    • (2012) Methods Enzymol , vol.511 , pp. 75-109
    • Andreou, A.Z.1    Klostermeier, D.2
  • 16
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: A newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • Tanner NK, Cordin O, Banroques J, Doere M, Linder P: The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Molecular cell 2003, 11:127-138.
    • (2003) Molecular Cell , vol.11 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 17
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • Cordin O, Tanner NK, Doere M, Linder P, Banroques J: The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. The EMBO journal 2004, 23:2478-2487.
    • (2004) The EMBO Journal , vol.23 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroques, J.5
  • 18
    • 77950349699 scopus 로고    scopus 로고
    • Motif III in superfamily 2 helicases helps convert the binding energy of ATP into a high-affinity RNA binding site in the yeast DEAD-box protein Ded1
    • Banroques J, Doere M, Dreyfus M, Linder P, Tanner NK: Motif III in superfamily 2 "helicases" helps convert the binding energy of ATP into a high-affinity RNA binding site in the yeast DEAD-box protein Ded1. J Mol Biol 2010, 396:949-966.
    • (2010) J Mol Biol , vol.396 , pp. 949-966
    • Banroques, J.1    Doere, M.2    Dreyfus, M.3    Linder, P.4    Tanner, N.K.5
  • 19
    • 43249100378 scopus 로고    scopus 로고
    • A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins
    • Banroques J, Cordin O, Doere M, Linder P, Tanner NK: A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins. Mol Cell Biol 2008, 28:3359-3371.
    • (2008) Mol Cell Biol , vol.28 , pp. 3359-3371
    • Banroques, J.1    Cordin, O.2    Doere, M.3    Linder, P.4    Tanner, N.K.5
  • 20
    • 78650854687 scopus 로고    scopus 로고
    • RNA helicases at work: Binding and rearranging
    • Jankowsky E: RNA helicases at work: binding and rearranging. Trends Biochem Sci 2011, 36:19-29.
    • (2011) Trends Biochem Sci , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 21
    • 0024393487 scopus 로고
    • RNA helicase activity associated with the human p68 protein
    • Hirling H, Scheffner M, Restle T, Stahl H: RNA helicase activity associated with the human p68 protein. Nature 1989, 339:562-564.
    • (1989) Nature , vol.339 , pp. 562-564
    • Hirling, H.1    Scheffner, M.2    Restle, T.3    Stahl, H.4
  • 22
    • 0032537843 scopus 로고    scopus 로고
    • Spliceosome assembly: The unwinding role of DEAD-box proteins
    • Hamm J, Lamond AI: Spliceosome assembly: the unwinding role of DEAD-box proteins. Curr Biol 1998, 8:R532-R534.
    • (1998) Curr Biol , vol.8 , pp. R532-R534
    • Hamm, J.1    Lamond, A.I.2
  • 23
    • 0036315396 scopus 로고    scopus 로고
    • P68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5' splice site duplex
    • Liu ZR: p68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5' splice site duplex. Mol Cell Biol 2002, 22:5443-5450.
    • (2002) Mol Cell Biol , vol.22 , pp. 5443-5450
    • Liu, Z.R.1
  • 24
    • 23844448397 scopus 로고    scopus 로고
    • ATPase/helicase activities of p68 RNA helicase are required for pre-mRNA splicing but not for assembly of the spliceosome
    • Lin C, Yang L, Yang JJ, Huang Y, Liu ZR: ATPase/helicase activities of p68 RNA helicase are required for pre-mRNA splicing but not for assembly of the spliceosome. Mol Cell Biol 2005, 25:7484-7493.
    • (2005) Mol Cell Biol , vol.25 , pp. 7484-7493
    • Lin, C.1    Yang, L.2    Yang, J.J.3    Huang, Y.4    Liu, Z.R.5
  • 25
    • 79955379829 scopus 로고    scopus 로고
    • RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site
    • Kar A, Fushimi K, Zhou X, Ray P, Shi C, Chen X, Liu Z, Chen S, Wu JY: RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site. Mol Cell Biol 2011, 31:1812-1821.
    • (2011) Mol Cell Biol , vol.31 , pp. 1812-1821
    • Kar, A.1    Fushimi, K.2    Zhou, X.3    Ray, P.4    Shi, C.5    Chen, X.6    Liu, Z.7    Chen, S.8    Wu, J.Y.9
  • 26
    • 0344838611 scopus 로고    scopus 로고
    • Roles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulation
    • Guil S, Gattoni R, Carrascal M, Abian J, Stevenin J, Bach-Elias M: Roles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulation. Mol Cell Biol 2003, 23:2927-2941.
    • (2003) Mol Cell Biol , vol.23 , pp. 2927-2941
    • Guil, S.1    Gattoni, R.2    Carrascal, M.3    Abian, J.4    Stevenin, J.5    Bach-Elias, M.6
  • 27
    • 84862236784 scopus 로고    scopus 로고
    • Circulating microRNAs in cancer: Origin, function and application
    • Ma R, Jiang T, Kang X: Circulating microRNAs in cancer: origin, function and application. J Exp Clin Cancer Res 2012, 31:38.
    • (2012) J Exp Clin Cancer Res , vol.31 , pp. 38
    • Ma, R.1    Jiang, T.2    Kang, X.3
  • 28
    • 12544255565 scopus 로고    scopus 로고
    • Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha
    • Zeng Y, Yi R, Cullen BR: Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha. EMBO J 2005, 24:138-148.
    • (2005) EMBO J , vol.24 , pp. 138-148
    • Zeng, Y.1    Yi, R.2    Cullen, B.R.3
  • 32
    • 77955484492 scopus 로고    scopus 로고
    • Smad proteins bind a conserved RNA sequence to promote microRNA maturation by Drosha
    • Davis BN, Hilyard AC, Nguyen PH, Lagna G, Hata A: Smad proteins bind a conserved RNA sequence to promote microRNA maturation by Drosha. Mol Cell 2010, 39:373-384.
    • (2010) Mol Cell , vol.39 , pp. 373-384
    • Davis, B.N.1    Hilyard, A.C.2    Nguyen, P.H.3    Lagna, G.4    Hata, A.5
  • 33
    • 0034796243 scopus 로고    scopus 로고
    • Absence of Dbp2p alters both nonsense-mediated mRNA decay and rRNA processing
    • Bond AT, Mangus DA, He F, Jacobson A: Absence of Dbp2p alters both nonsense-mediated mRNA decay and rRNA processing. Mol Cell Biol 2001, 21:7366-7379.
    • (2001) Mol Cell Biol , vol.21 , pp. 7366-7379
    • Bond, A.T.1    Mangus, D.A.2    He, F.3    Jacobson, A.4
  • 34
    • 34547114282 scopus 로고    scopus 로고
    • Redundant role of DEAD box proteins p68 (Ddx5) and p72/p82 (Ddx17) in ribosome biogenesis and cell proliferation
    • Jalal C, Uhlmann-Schiffler H, Stahl H: Redundant role of DEAD box proteins p68 (Ddx5) and p72/p82 (Ddx17) in ribosome biogenesis and cell proliferation. Nucleic Acids Res 2007, 35:3590-3601.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3590-3601
    • Jalal, C.1    Uhlmann-Schiffler, H.2    Stahl, H.3
  • 36
    • 1642499357 scopus 로고    scopus 로고
    • Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23
    • Bertwistle D, Sugimoto M, Sherr CJ: Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23. Mol Cell Biol 2004, 24:985-996.
    • (2004) Mol Cell Biol , vol.24 , pp. 985-996
    • Bertwistle, D.1    Sugimoto, M.2    Sherr, C.J.3
  • 38
    • 0035929176 scopus 로고    scopus 로고
    • Expression of p68 RNA helicase is closely related to the early stage of adipocyte differentiation of mouse 3 T3-L1 cells
    • Kitamura A, Nishizuka M, Tominaga K, Tsuchiya T, Nishihara T, Imagawa M: Expression of p68 RNA helicase is closely related to the early stage of adipocyte differentiation of mouse 3 T3-L1 cells. Biochem Biophys Res Commun 2001, 287:435-439.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 435-439
    • Kitamura, A.1    Nishizuka, M.2    Tominaga, K.3    Tsuchiya, T.4    Nishihara, T.5    Imagawa, M.6
  • 39
    • 0036808714 scopus 로고    scopus 로고
    • Reduced levels of DEAD-box proteins DBP-RB and p72 in fetal Down syndrome brains
    • Kircher SG, Kim SH, Fountoulakis M, Lubec G: Reduced levels of DEAD-box proteins DBP-RB and p72 in fetal Down syndrome brains. Neurochem Res 2002, 27:1141-1146.
    • (2002) Neurochem Res , vol.27 , pp. 1141-1146
    • Kircher, S.G.1    Kim, S.H.2    Fountoulakis, M.3    Lubec, G.4
  • 40
    • 84884361485 scopus 로고    scopus 로고
    • Timchenko LT: Dysfunction of protein homeostasis in myotonic dystrophies
    • Meola G, Jones K, Wei C, Timchenko LT: Dysfunction of protein homeostasis in myotonic dystrophies. Histol Histopathol 2013,
    • (2013) Histol Histopathol
    • Meola, G.1    Jones, K.2    Wei, C.3
  • 42
    • 0029655361 scopus 로고    scopus 로고
    • Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues
    • Haines GK, Cajulis R, Hayden R, Duda R, Talamonti M, Radosevich JA: Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues. Tumour Biol 1996, 17:5-12.
    • (1996) Tumour Biol , vol.17 , pp. 5-12
    • Haines, G.K.1    Cajulis, R.2    Hayden, R.3    Duda, R.4    Talamonti, M.5    Radosevich, J.A.6
  • 44
    • 84870066484 scopus 로고    scopus 로고
    • Overexpression of RNA helicase p68 protein in cutaneous squamous cell carcinoma
    • Wang SJ, Zhang C, You Y, Shi CM: Overexpression of RNA helicase p68 protein in cutaneous squamous cell carcinoma. Clin Exp Dermatol 2012, 37:882-888.
    • (2012) Clin Exp Dermatol , vol.37 , pp. 882-888
    • Wang, S.J.1    Zhang, C.2    You, Y.3    Shi, C.M.4
  • 46
    • 34548007885 scopus 로고    scopus 로고
    • Involvement of RNA helicases p68 and p72 in colon cancer
    • Shin S, Rossow KL, Grande JP, Janknecht R: Involvement of RNA helicases p68 and p72 in colon cancer. Cancer Res 2007, 67:7572-7578.
    • (2007) Cancer Res , vol.67 , pp. 7572-7578
    • Shin, S.1    Rossow, K.L.2    Grande, J.P.3    Janknecht, R.4
  • 48
    • 84863043265 scopus 로고    scopus 로고
    • RNA helicase DDX5 regulates microRNA expression and contributes to cytoskeletal reorganization in basal breast cancer cells
    • Wang D, Huang J, Hu Z: RNA helicase DDX5 regulates microRNA expression and contributes to cytoskeletal reorganization in basal breast cancer cells. Mol Cell Proteomics 2012, 11:M111 011932.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.M111 , pp. 011932
    • Wang, D.1    Huang, J.2    Hu, Z.3
  • 50
    • 33745587030 scopus 로고    scopus 로고
    • Overexpression of p68 mRNA in head and neck squamous cell carcinoma cells
    • Beier UH, Maune S, Meyer JE, Gorogh T: Overexpression of p68 mRNA in head and neck squamous cell carcinoma cells. Anticancer Res 2006, 26:1941-1946.
    • (2006) Anticancer Res , vol.26 , pp. 1941-1946
    • Beier, U.H.1    Maune, S.2    Meyer, J.E.3    Gorogh, T.4
  • 51
  • 52
    • 84867512779 scopus 로고    scopus 로고
    • P68 RNA helicase promotes glioma cell proliferation in vitro and in vivo via direct regulation of NF-kappaB transcription factor p50
    • Wang R, Jiao Z, Li R, Yue H, Chen L: p68 RNA helicase promotes glioma cell proliferation in vitro and in vivo via direct regulation of NF-kappaB transcription factor p50. Neuro Oncol 2012, 14:1116-1124.
    • (2012) Neuro Oncol , vol.14 , pp. 1116-1124
    • Wang, R.1    Jiao, Z.2    Li, R.3    Yue, H.4    Chen, L.5
  • 54
    • 73449119972 scopus 로고    scopus 로고
    • Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential
    • Mooney SM, Grande JP, Salisbury JL, Janknecht R: Sumoylation of p68 and p72 RNA helicases affects protein stability and transactivation potential. Biochemistry 2010, 49:1-10.
    • (2010) Biochemistry , vol.49 , pp. 1-10
    • Mooney, S.M.1    Grande, J.P.2    Salisbury, J.L.3    Janknecht, R.4
  • 55
    • 77953015118 scopus 로고    scopus 로고
    • Analysis of the RNA helicase p68 (Ddx5) as a transcriptional regulator
    • Nicol SM, Fuller-Pace FV: Analysis of the RNA helicase p68 (Ddx5) as a transcriptional regulator. Methods Mol Biol 2010, 587:265-279.
    • (2010) Methods Mol Biol , vol.587 , pp. 265-279
    • Nicol, S.M.1    Fuller-Pace, F.V.2
  • 56
    • 70350379631 scopus 로고    scopus 로고
    • The small chromatin-binding protein p8 coordinates the association of anti-proliferative and pro-myogenic proteins at the myogenin promoter
    • Sambasivan R, Cheedipudi S, Pasupuleti N, Saleh A, Pavlath GK, Dhawan J: The small chromatin-binding protein p8 coordinates the association of anti-proliferative and pro-myogenic proteins at the myogenin promoter. J Cell Sci 2009, 122:3481-3491.
    • (2009) J Cell Sci , vol.122 , pp. 3481-3491
    • Sambasivan, R.1    Cheedipudi, S.2    Pasupuleti, N.3    Saleh, A.4    Pavlath, G.K.5    Dhawan, J.6
  • 57
    • 26444551757 scopus 로고    scopus 로고
    • The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner
    • Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV: The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner. BMC Mol Biol 2004, 5:11.
    • (2004) BMC Mol Biol , vol.5 , pp. 11
    • Wilson, B.J.1    Bates, G.J.2    Nicol, S.M.3    Gregory, D.J.4    Perkins, N.D.5    Fuller-Pace, F.V.6
  • 58
    • 84865088686 scopus 로고    scopus 로고
    • The role of estrogen receptor alpha in mediating chemoresistance in breast cancer cells
    • Jiang Z, Guo J, Shen J, Jin M, Xie S, Wang L: The role of estrogen receptor alpha in mediating chemoresistance in breast cancer cells. J Exp Clin Cancer Res 2012, 31:42.
    • (2012) J Exp Clin Cancer Res , vol.31 , pp. 42
    • Jiang, Z.1    Guo, J.2    Shen, J.3    Jin, M.4    Xie, S.5    Wang, L.6
  • 59
  • 62
    • 84872516964 scopus 로고    scopus 로고
    • P68/DdX5 supports beta-catenin & RNAP II during androgen receptor mediated transcription in prostate cancer
    • Clark EL, Hadjimichael C, Temperley R, Barnard A, Fuller-Pace FV, Robson CN: p68/DdX5 supports beta-catenin & RNAP II during androgen receptor mediated transcription in prostate cancer. PLoS One 2013, 8:e54150.
    • (2013) PLoS One , vol.8 , pp. e54150
    • Clark, E.L.1    Hadjimichael, C.2    Temperley, R.3    Barnard, A.4    Fuller-Pace, F.V.5    Robson, C.N.6
  • 64
    • 33846929645 scopus 로고    scopus 로고
    • Cell cycling and differentiation do not require the retinoblastoma protein during early Xenopus development
    • Cosgrove RA, Philpott A: Cell cycling and differentiation do not require the retinoblastoma protein during early Xenopus development. Dev Biol 2007, 303:311-324.
    • (2007) Dev Biol , vol.303 , pp. 311-324
    • Cosgrove, R.A.1    Philpott, A.2
  • 65
    • 0033768802 scopus 로고    scopus 로고
    • The role and regulation of D-type cyclins in the plant cell cycle
    • Meijer M, Murray JAH: The role and regulation of D-type cyclins in the plant cell cycle. Plant Mol Biol 2000, 43:621-633.
    • (2000) Plant Mol Biol , vol.43 , pp. 621-633
    • Meijer, M.1    Murray, J.A.H.2
  • 67
    • 78650029658 scopus 로고    scopus 로고
    • The RNA helicase p68 modulates expression and function of the Delta133 isoform(s) of p53, and is inversely associated with Delta133p53 expression in breast cancer
    • Moore HC, Jordan LB, Bray SE, Baker L, Quinlan PR, Purdie CA, Thompson AM, Bourdon JC, Fuller-Pace FV: The RNA helicase p68 modulates expression and function of the Delta133 isoform(s) of p53, and is inversely associated with Delta133p53 expression in breast cancer. Oncogene 2010, 29:6475-6484.
    • (2010) Oncogene , vol.29 , pp. 6475-6484
    • Moore, H.C.1    Jordan, L.B.2    Bray, S.E.3    Baker, L.4    Quinlan, P.R.5    Purdie, C.A.6    Thompson, A.M.7    Bourdon, J.C.8    Fuller-Pace, F.V.9
  • 68
    • 84880918955 scopus 로고    scopus 로고
    • The RNA helicase p68 (DDX5) is selectively required for the induction of p53-dependent p21 expression and cell-cycle arrest after DNA damage
    • Nicol SM, Bray SE, Black HD, Lorimore SA, Wright EG, Lane DP, Meek DW, Coates PJ, Fuller-Pace FV: The RNA helicase p68 (DDX5) is selectively required for the induction of p53-dependent p21 expression and cell-cycle arrest after DNA damage. Oncogene 2013, 32:3461-3469.
    • (2013) Oncogene , vol.32 , pp. 3461-3469
    • Nicol, S.M.1    Bray, S.E.2    Black, H.D.3    Lorimore, S.A.4    Wright, E.G.5    Lane, D.P.6    Meek, D.W.7    Coates, P.J.8    Fuller-Pace, F.V.9
  • 69
    • 34447134154 scopus 로고    scopus 로고
    • Phosphorylation of p68 RNA helicase plays a role in platelet-derived growth factor-induced cell proliferation by upregulating cyclin D1 and c-Myc expression
    • Yang L, Lin C, Zhao S, Wang H, Liu ZR: Phosphorylation of p68 RNA helicase plays a role in platelet-derived growth factor-induced cell proliferation by upregulating cyclin D1 and c-Myc expression. JBiolChem2007, 282:16811-16819.
    • (2007) J Biol Chem , vol.282 , pp. 16811-16819
    • Yang, L.1    Lin, C.2    Zhao, S.3    Wang, H.4    Liu, Z.R.5
  • 70
    • 84866599883 scopus 로고    scopus 로고
    • The beta-catenin/TCF complex as a novel target of resveratrol in the Wnt/beta-catenin signaling pathway
    • Chen HJ, Hsu LS, Shia YT, Lin MW, Lin CM: The beta-catenin/TCF complex as a novel target of resveratrol in the Wnt/beta-catenin signaling pathway. Biochem Pharmacol 2012, 84:1143-1153.
    • (2012) Biochem Pharmacol , vol.84 , pp. 1143-1153
    • Chen, H.J.1    Hsu, L.S.2    Shia, Y.T.3    Lin, M.W.4    Lin, C.M.5
  • 71
    • 84864607962 scopus 로고    scopus 로고
    • Mrhl RNA, a long noncoding RNA, negatively regulates Wnt signaling through its protein partner Ddx5/p68 in mouse spermatogonial cells
    • Arun G, Akhade VS, Donakonda S, Rao MR: mrhl RNA, a long noncoding RNA, negatively regulates Wnt signaling through its protein partner Ddx5/p68 in mouse spermatogonial cells. Mol Cell Biol 2012, 32:3140-3152.
    • (2012) Mol Cell Biol , vol.32 , pp. 3140-3152
    • Arun, G.1    Akhade, V.S.2    Donakonda, S.3    Rao, M.R.4
  • 74
    • 46449128469 scopus 로고    scopus 로고
    • SMAD proteins control DROSHA-mediated microRNA maturation
    • Davis BN, Hilyard AC, Lagna G, Hata A: SMAD proteins control DROSHA-mediated microRNA maturation. Nature 2008, 454:56-61.
    • (2008) Nature , vol.454 , pp. 56-61
    • Davis, B.N.1    Hilyard, A.C.2    Lagna, G.3    Hata, A.4
  • 75
    • 59449090107 scopus 로고    scopus 로고
    • TGF-beta-induced epithelial to mesenchymal transition
    • Xu J, Lamouille S, Derynck R: TGF-beta-induced epithelial to mesenchymal transition. Cell Res 2009, 19:156-172.
    • (2009) Cell Res , vol.19 , pp. 156-172
    • Xu, J.1    Lamouille, S.2    Derynck, R.3
  • 76
    • 77954167982 scopus 로고    scopus 로고
    • Transcriptional crosstalk between TGF-beta and stem cell pathways in tumor cell invasion: Role of EMT promoting Smad complexes
    • Fuxe J, Vincent T, Garcia de Herreros A: Transcriptional crosstalk between TGF-beta and stem cell pathways in tumor cell invasion: role of EMT promoting Smad complexes. Cell Cycle 2010, 9:2363-2374.
    • (2010) Cell Cycle , vol.9 , pp. 2363-2374
    • Fuxe, J.1    Vincent, T.2    De Garcia Herreros, A.3
  • 77
    • 60849098434 scopus 로고    scopus 로고
    • Integrin alpha3beta1-dependent beta-catenin phosphorylation links epithelial Smad signaling to cell contacts
    • Kim Y, Kugler MC, Wei Y, Kim KK, Li X, Brumwell AN, Chapman HA: Integrin alpha3beta1-dependent beta-catenin phosphorylation links epithelial Smad signaling to cell contacts. J Cell Biol 2009, 184:309-322.
    • (2009) J Cell Biol , vol.184 , pp. 309-322
    • Kim, Y.1    Kugler, M.C.2    Wei, Y.3    Kim, K.K.4    Li, X.5    Brumwell, A.N.6    Chapman, H.A.7
  • 79
    • 0028114964 scopus 로고
    • Regulation of p68 RNA helicase by calmodulin and protein kinase C
    • Buelt MK, Glidden BJ, Storm DR: Regulation of p68 RNA helicase by calmodulin and protein kinase C. J Biol Chem 1994, 269:29367-29370.
    • (1994) J Biol Chem , vol.269 , pp. 29367-29370
    • Buelt, M.K.1    Glidden, B.J.2    Storm, D.R.3
  • 80
    • 0347635408 scopus 로고    scopus 로고
    • Phosphorylation of p68 RNA helicase regulates RNA binding by the C-terminal domain of the protein
    • Yang L, Yang J, Huang Y, Liu ZR: Phosphorylation of p68 RNA helicase regulates RNA binding by the C-terminal domain of the protein. Biochem Biophys Res Commun 2004, 314:622-630.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 622-630
    • Yang, L.1    Yang, J.2    Huang, Y.3    Liu, Z.R.4
  • 81
    • 0023951717 scopus 로고
    • Nuclear protein with sequence homology to translation initiation factor eIF-4A
    • Ford MJ, Anton IA, Lane DP: Nuclear protein with sequence homology to translation initiation factor eIF-4A. Nature 1988, 332:736-738.
    • (1988) Nature , vol.332 , pp. 736-738
    • Ford, M.J.1    Anton, I.A.2    Lane, D.P.3
  • 82
    • 21344436082 scopus 로고    scopus 로고
    • Signaling to the DEAD box-regulation of DEAD-box p68 RNA helicase by protein phosphorylations
    • Yang L, Lin C, Liu ZR: Signaling to the DEAD box-regulation of DEAD-box p68 RNA helicase by protein phosphorylations. Cell Signal 2005, 17:1495-1504.
    • (2005) Cell Signal , vol.17 , pp. 1495-1504
    • Yang, L.1    Lin, C.2    Liu, Z.R.3
  • 83
    • 77957287427 scopus 로고    scopus 로고
    • Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA helicase
    • Mooney SM, Goel A, D'Assoro AB, Salisbury JL, Janknecht R: Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA helicase. J Biol Chem 2010, 285:30443-30452.
    • (2010) J Biol Chem , vol.285 , pp. 30443-30452
    • Mooney, S.M.1    Goel, A.2    D'Assoro, A.B.3    Salisbury, J.L.4    Janknecht, R.5
  • 84
    • 34548252476 scopus 로고    scopus 로고
    • SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1
    • Jacobs AM, Nicol SM, Hislop RG, Jaffray EG, Hay RT, Fuller-Pace FV: SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1. Oncogene 2007, 26:5866-5876.
    • (2007) Oncogene , vol.26 , pp. 5866-5876
    • Jacobs, A.M.1    Nicol, S.M.2    Hislop, R.G.3    Jaffray, E.G.4    Hay, R.T.5    Fuller-Pace, F.V.6
  • 85
    • 33749078750 scopus 로고    scopus 로고
    • P68 RNA helicase mediates PDGF-induced epithelial mesenchymal transition by displacing Axin from beta-catenin
    • Yang L, Lin C, Liu ZR: P68 RNA helicase mediates PDGF-induced epithelial mesenchymal transition by displacing Axin from beta-catenin. Cell 2006, 127:139-155.
    • (2006) Cell , vol.127 , pp. 139-155
    • Yang, L.1    Lin, C.2    Liu, Z.R.3
  • 86
    • 33749067198 scopus 로고    scopus 로고
    • Unwinding a path to nuclear beta-catenin
    • He X: Unwinding a path to nuclear beta-catenin. Cell 2006, 127:40-42.
    • (2006) Cell , vol.127 , pp. 40-42
    • He, X.1
  • 87
    • 84877911360 scopus 로고    scopus 로고
    • Interaction between p68 RNA helicase and Ca2 + -calmodulin promotes cell migration and metastasis
    • Wang H, Gao X, Yang JJ, Liu ZR: Interaction between p68 RNA helicase and Ca2 + -calmodulin promotes cell migration and metastasis. Nat Commun 2013, 4:1354.
    • (2013) Nat Commun , vol.4 , pp. 1354
    • Wang, H.1    Gao, X.2    Yang, J.J.3    Liu, Z.R.4
  • 90
    • 84906987053 scopus 로고
    • Histone deacetylase inhibitor induction of epithelial-mesenchymal transitions via up-regulation of Snail facilitates cancer progression
    • Jiang GM, Wang HS, Zhang F, Zhang KS, Liu ZC, Fang R, Wang H, Cai SH, Du J: Histone deacetylase inhibitor induction of epithelial-mesenchymal transitions via up-regulation of Snail facilitates cancer progression. Biochim Biophys Acta 1833, 2013:663-671.
    • (1833) Biochim Biophys Acta , vol.2013 , pp. 663-671
    • Jiang, G.M.1    Wang, H.S.2    Zhang, F.3    Zhang, K.S.4    Liu, Z.C.5    Fang, R.6    Wang, H.7    Cai, S.H.8    Du, J.9
  • 91
    • 77957605910 scopus 로고    scopus 로고
    • Phosphorylated p68 RNA helicase activates Snail1 transcription by promoting HDAC1 dissociation from the Snail1 promoter
    • Carter CL, Lin C, Liu CY, Yang L, Liu ZR: Phosphorylated p68 RNA helicase activates Snail1 transcription by promoting HDAC1 dissociation from the Snail1 promoter. Oncogene 2010, 29:5427-5436.
    • (2010) Oncogene , vol.29 , pp. 5427-5436
    • Carter, C.L.1    Lin, C.2    Liu, C.Y.3    Yang, L.4    Liu, Z.R.5
  • 92
    • 0346363757 scopus 로고    scopus 로고
    • Snail mediates E-cadherin repression by the recruitment of the Sin3A/histone deacetylase 1 (HDAC1)/HDAC2 complex
    • Peinado H, Ballestar E, Esteller M, Cano A: Snail mediates E-cadherin repression by the recruitment of the Sin3A/histone deacetylase 1 (HDAC1)/HDAC2 complex. Mol Cell Biol 2004, 24:306-319.
    • (2004) Mol Cell Biol , vol.24 , pp. 306-319
    • Peinado, H.1    Ballestar, E.2    Esteller, M.3    Cano, A.4
  • 93
    • 84880911745 scopus 로고    scopus 로고
    • Emerging role of cancer stem cells in the biology and treatment of ovarian cancer: Basic knowledge and therapeutic possibilities for an innovative approach
    • Tomao F, Papa A, Rossi L, Strudel M, Vici P: Lo Russo G. Tomao S: Emerging role of cancer stem cells in the biology and treatment of ovarian cancer: basic knowledge and therapeutic possibilities for an innovative approach. J Exp Clin Cancer Res 2013, 32:48.
    • (2013) J Exp Clin Cancer Res , vol.32 , pp. 48
    • Tomao, F.1    Papa, A.2    Rossi, L.3    Strudel, M.4    Vici, P.5    Lo Russo, G.6    Tomao, S.7
  • 94
    • 21344459251 scopus 로고    scopus 로고
    • Phosphorylations of DEAD box p68 RNA helicase are associated with cancer development and cell proliferation
    • Yang L, Lin C, Liu ZR: Phosphorylations of DEAD box p68 RNA helicase are associated with cancer development and cell proliferation. Mol Cancer Res 2005, 3:355-363.
    • (2005) Mol Cancer Res , vol.3 , pp. 355-363
    • Yang, L.1    Lin, C.2    Liu, Z.R.3
  • 95
    • 84868238154 scopus 로고    scopus 로고
    • Phosphorylation of p68 RNA helicase by p38 MAP kinase contributes to colon cancer cells apoptosis induced by oxaliplatin
    • Dey H, Liu ZR: Phosphorylation of p68 RNA helicase by p38 MAP kinase contributes to colon cancer cells apoptosis induced by oxaliplatin. BMC Cell Biol 2012, 13:27.
    • (2012) BMC Cell Biol , vol.13 , pp. 27
    • Dey, H.1    Liu, Z.R.2
  • 96
    • 34548497387 scopus 로고    scopus 로고
    • A double tyrosine phosphorylation of P68 RNA helicase confers resistance to TRAIL-induced apoptosis
    • Yang L, Lin C, Sun SY, Zhao S, Liu ZR: A double tyrosine phosphorylation of P68 RNA helicase confers resistance to TRAIL-induced apoptosis. Oncogene 2007, 26:6082-6092.
    • (2007) Oncogene , vol.26 , pp. 6082-6092
    • Yang, L.1    Lin, C.2    Sun, S.Y.3    Zhao, S.4    Liu, Z.R.5


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