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Volumn 32, Issue 5, 2008, Pages 605-615

The Control of mRNA Decapping and P-Body Formation

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; DEATH CASPASE 1; DEATH CASPASE 2; MESSENGER RNA; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 56849103665     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.11.001     Document Type: Review
Times cited : (325)

References (122)
  • 1
  • 2
    • 46249091565 scopus 로고    scopus 로고
    • Translation factors promote the formation of two states of the closed-loop mRNP
    • Amrani N., Ghosh S., Mangus D.A., and Jacobson A. Translation factors promote the formation of two states of the closed-loop mRNP. Nature 453 (2008) 1276-1280
    • (2008) Nature , vol.453 , pp. 1276-1280
    • Amrani, N.1    Ghosh, S.2    Mangus, D.A.3    Jacobson, A.4
  • 4
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson P., and Kedersha N. Stress granules: the Tao of RNA triage. Trends Biochem. Sci. 33 (2008) 141-150
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 5
    • 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., and Luhrmann R. A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA 11 (2005) 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
  • 6
    • 27544434940 scopus 로고    scopus 로고
    • A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans
    • Audhya A., Hyndman F., McLeod I.X., Maddox A.S., Yates III J.R., Desai A., and Oegema K. A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans. J. Cell. Biol. 171 (2005) 267-279
    • (2005) J. Cell. Biol. , vol.171 , pp. 267-279
    • Audhya, A.1    Hyndman, F.2    McLeod, I.X.3    Maddox, A.S.4    Yates III, J.R.5    Desai, A.6    Oegema, K.7
  • 7
    • 3042803133 scopus 로고    scopus 로고
    • Targeted mRNA degradation by deadenylation-independent decapping
    • Badis G., Saveanu C., Fromont-Racine M., and Jacquier A. Targeted mRNA degradation by deadenylation-independent decapping. Mol. Cell 15 (2004) 5-15
    • (2004) Mol. Cell , vol.15 , pp. 5-15
    • Badis, G.1    Saveanu, C.2    Fromont-Racine, M.3    Jacquier, A.4
  • 9
    • 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., and Heyer W.D. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J. Cell Biol. 136 (1997) 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
  • 10
    • 41649101221 scopus 로고    scopus 로고
    • The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies
    • Beckham C., Hilliker A., Cziko A.M., Noueiry A., Ramaswami M., and Parker R. The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies. Mol. Biol. Cell 19 (2008) 984-993
    • (2008) Mol. Biol. Cell , vol.19 , pp. 984-993
    • Beckham, C.1    Hilliker, A.2    Cziko, A.M.3    Noueiry, A.4    Ramaswami, M.5    Parker, R.6
  • 11
    • 0028225993 scopus 로고
    • Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA
    • Beelman C.A., and Parker R. Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA. J. Biol. Chem. 269 (1994) 9687-9692
    • (1994) J. Biol. Chem. , vol.269 , pp. 9687-9692
    • Beelman, C.A.1    Parker, R.2
  • 13
    • 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., and Filipowicz W. Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125 (2006) 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
  • 14
    • 0026668288 scopus 로고
    • The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA
    • Blanc A., Goyer C., and Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol. Cell. Biol. 12 (1992) 3390-3398
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3390-3398
    • Blanc, A.1    Goyer, C.2    Sonenberg, N.3
  • 15
    • 28844481062 scopus 로고    scopus 로고
    • A conserved RNA-protein complex component involved in physiological germline apoptosis regulation in C. elegans
    • Boag P.R., Nakamura A., and Blackwell T.K. A conserved RNA-protein complex component involved in physiological germline apoptosis regulation in C. elegans. Development 132 (2005) 4975-4986
    • (2005) Development , vol.132 , pp. 4975-4986
    • Boag, P.R.1    Nakamura, A.2    Blackwell, T.K.3
  • 16
    • 0033866402 scopus 로고    scopus 로고
    • The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p
    • Bonnerot C., Boeck R., and Lapeyre B. The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol. Cell. Biol. 20 (2000) 5939-5946
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5939-5946
    • Bonnerot, C.1    Boeck, R.2    Lapeyre, B.3
  • 17
    • 0034599976 scopus 로고    scopus 로고
    • A Sm-like protein complex that participates in mRNA degradation
    • Bouveret E., Rigaut G., Shevchenko A., Wilm M., and Seraphin B. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19 (2000) 1661-1671
    • (2000) EMBO J. , vol.19 , pp. 1661-1671
    • Bouveret, E.1    Rigaut, G.2    Shevchenko, A.3    Wilm, M.4    Seraphin, B.5
  • 18
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues M., Teixeira D., and Parker R. Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310 (2005) 486-489
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 19
    • 33646590585 scopus 로고    scopus 로고
    • Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay
    • Chou C.F., Mulky A., Maitra S., Lin W.J., Gherzi R., Kappes J., and Chen C.Y. Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay. Mol. Cell. Biol. 26 (2006) 3695-3706
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3695-3706
    • Chou, C.F.1    Mulky, A.2    Maitra, S.3    Lin, W.J.4    Gherzi, R.5    Kappes, J.6    Chen, C.Y.7
  • 20
    • 34250804009 scopus 로고    scopus 로고
    • The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs
    • Chowdhury A., Mukhopadhyay J., and Tharun S. The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA 13 (2007) 998-1016
    • (2007) RNA , vol.13 , pp. 998-1016
    • Chowdhury, A.1    Mukhopadhyay, J.2    Tharun, S.3
  • 21
    • 33745894330 scopus 로고    scopus 로고
    • Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54
    • Chu C.Y., and Rana T.M. Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54. PLoS Biol. 4 (2006) e210
    • (2006) PLoS Biol. , vol.4
    • Chu, C.Y.1    Rana, T.M.2
  • 22
    • 26444538927 scopus 로고    scopus 로고
    • Dcp2 Decaps m2,2,7GpppN-capped RNAs, and its activity is sequence and context dependent
    • Cohen L.S., Mikhli C., Jiao X., Kiledjian M., Kunkel G., and Davis R.E. Dcp2 Decaps m2,2,7GpppN-capped RNAs, and its activity is sequence and context dependent. Mol. Cell. Biol. 25 (2005) 8779-8791
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8779-8791
    • Cohen, L.S.1    Mikhli, C.2    Jiao, X.3    Kiledjian, M.4    Kunkel, G.5    Davis, R.E.6
  • 23
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J., and Parker R. General translational repression by activators of mRNA decapping. Cell 122 (2005) 875-886
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 24
    • 0035674477 scopus 로고    scopus 로고
    • The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes
    • Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., and Parker R. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 7 (2001) 1717-1727
    • (2001) RNA , vol.7 , pp. 1717-1727
    • Coller, J.M.1    Tucker, M.2    Sheth, U.3    Valencia-Sanchez, M.A.4    Parker, R.5
  • 25
    • 0034980436 scopus 로고    scopus 로고
    • The mechanism and regulation of deadenylation: identification and characterization of Xenopus PARN
    • Copeland P.R., and Wormington M. The mechanism and regulation of deadenylation: identification and characterization of Xenopus PARN. RNA 7 (2001) 875-886
    • (2001) RNA , vol.7 , pp. 875-886
    • Copeland, P.R.1    Wormington, M.2
  • 26
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • Cougot N., Babajko S., and Seraphin B. Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 165 (2004) 31-40
    • (2004) J. Cell Biol. , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Seraphin, B.3
  • 28
    • 33646091499 scopus 로고    scopus 로고
    • CAR-1 and trailer hitch: driving mRNP granule function at the ER?
    • Decker C.J., and Parker R. CAR-1 and trailer hitch: driving mRNP granule function at the ER?. J. Cell Biol. 173 (2006) 159-163
    • (2006) J. Cell Biol. , vol.173 , pp. 159-163
    • Decker, C.J.1    Parker, R.2
  • 29
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker C.J., Teixeira D., and Parker R. Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J. Cell Biol. 179 (2007) 437-449
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 32
    • 23744492247 scopus 로고    scopus 로고
    • The developmental timing regulator AIN-1 interacts with miRISCs and may target the argonaute protein ALG-1 to cytoplasmic P bodies in C. elegans
    • Ding L., Spencer A., Morita K., and Han M. The developmental timing regulator AIN-1 interacts with miRISCs and may target the argonaute protein ALG-1 to cytoplasmic P bodies in C. elegans. Mol. Cell 19 (2005) 437-447
    • (2005) Mol. Cell , vol.19 , pp. 437-447
    • Ding, L.1    Spencer, A.2    Morita, K.3    Han, M.4
  • 33
    • 33847059515 scopus 로고    scopus 로고
    • YRA1 autoregulation requires nuclear export and cytoplasmic Edc3p-mediated degradation of its pre-mRNA
    • Dong S., Li C., Zenklusen D., Singer R.H., Jacobson A., and He F. YRA1 autoregulation requires nuclear export and cytoplasmic Edc3p-mediated degradation of its pre-mRNA. Mol. Cell 25 (2007) 559-573
    • (2007) Mol. Cell , vol.25 , pp. 559-573
    • Dong, S.1    Li, C.2    Zenklusen, D.3    Singer, R.H.4    Jacobson, A.5    He, F.6
  • 34
    • 0033214061 scopus 로고    scopus 로고
    • The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
    • Dunckley T., and Parker R. The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO J. 18 (1999) 5411-5422
    • (1999) EMBO J. , vol.18 , pp. 5411-5422
    • Dunckley, T.1    Parker, R.2
  • 35
    • 0035148534 scopus 로고    scopus 로고
    • Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae
    • Dunckley T., Tucker M., and Parker R. Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Genetics 157 (2001) 27-37
    • (2001) Genetics , vol.157 , pp. 27-37
    • Dunckley, T.1    Tucker, M.2    Parker, R.3
  • 37
    • 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., and Izaurralde E. P-body formation is a consequence, not the cause, of RNA-mediated gene silencing. Mol. Cell. Biol. 27 (2007) 3970-3981
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3970-3981
    • Eulalio, A.1    Behm-Ansmant, I.2    Schweizer, D.3    Izaurralde, E.4
  • 39
    • 0036223709 scopus 로고    scopus 로고
    • A phosphorylated cytoplasmic autoantigen, GW182, associates with a unique population of human mRNAs within novel cytoplasmic speckles
    • Eystathioy T., Chan E.K., Tenenbaum S.A., Keene J.D., Griffith K., and Fritzler M.J. A phosphorylated cytoplasmic autoantigen, GW182, associates with a unique population of human mRNAs within novel cytoplasmic speckles. Mol. Biol. Cell 13 (2002) 1338-1351
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1338-1351
    • Eystathioy, T.1    Chan, E.K.2    Tenenbaum, S.A.3    Keene, J.D.4    Griffith, K.5    Fritzler, M.J.6
  • 40
    • 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., and Fritzler M.J. The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies. RNA 9 (2003) 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
  • 41
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • Fenger-Gron M., Fillman C., Norrild B., and Lykke-Andersen J. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell 20 (2005) 905-915
    • (2005) Mol. Cell , vol.20 , pp. 905-915
    • Fenger-Gron, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 42
    • 0037013898 scopus 로고    scopus 로고
    • The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1
    • Fischer N., and Weis K. The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1. EMBO J. 21 (2002) 2788-2797
    • (2002) EMBO J. , vol.21 , pp. 2788-2797
    • Fischer, N.1    Weis, K.2
  • 43
    • 33947301293 scopus 로고    scopus 로고
    • TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements
    • Franks T.M., and Lykke-Andersen J. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 21 (2007) 719-735
    • (2007) Genes Dev. , vol.21 , pp. 719-735
    • Franks, T.M.1    Lykke-Andersen, J.2
  • 44
    • 0027531522 scopus 로고
    • Unconventional processing of the 3′ termini of the Epstein-Barr virus DNA polymerase mRNA
    • Furnari F.B., Adams M.D., and Pagano J.S. Unconventional processing of the 3′ termini of the Epstein-Barr virus DNA polymerase mRNA. Proc. Natl. Acad. Sci. USA 90 (1993) 378-382
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 378-382
    • Furnari, F.B.1    Adams, M.D.2    Pagano, J.S.3
  • 45
    • 0035282971 scopus 로고    scopus 로고
    • A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements
    • Gao M., Wilusz C.J., Peltz S.W., and Wilusz J. A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J. 20 (2001) 1134-1143
    • (2001) EMBO J. , vol.20 , pp. 1134-1143
    • Gao, M.1    Wilusz, C.J.2    Peltz, S.W.3    Wilusz, J.4
  • 46
    • 1842578583 scopus 로고    scopus 로고
    • Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme
    • Ghosh T., Peterson B., Tomasevic N., and Peculis B.A. Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme. Mol. Cell 13 (2004) 817-828
    • (2004) Mol. Cell , vol.13 , pp. 817-828
    • Ghosh, T.1    Peterson, B.2    Tomasevic, N.3    Peculis, B.A.4
  • 48
    • 34447092677 scopus 로고    scopus 로고
    • The EJC factor eIF4AIII modulates synaptic strength and neuronal protein expression
    • Giorgi C., Yeo G.W., Stone M.E., Katz D.B., Burge C., Turrigiano G., and Moore M.J. The EJC factor eIF4AIII modulates synaptic strength and neuronal protein expression. Cell 130 (2007) 179-191
    • (2007) Cell , vol.130 , pp. 179-191
    • Giorgi, C.1    Yeo, G.W.2    Stone, M.E.3    Katz, D.B.4    Burge, C.5    Turrigiano, G.6    Moore, M.J.7
  • 50
    • 0032437667 scopus 로고    scopus 로고
    • Control of translation initiation in animals
    • Gray N.K., and Wickens M. Control of translation initiation in animals. Annu. Rev. Cell Dev. Biol. 14 (1998) 399-458
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 399-458
    • Gray, N.K.1    Wickens, M.2
  • 51
    • 0028948708 scopus 로고
    • Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen
    • He F., and Jacobson A. Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen. Genes Dev. 9 (1995) 437-454
    • (1995) Genes Dev. , vol.9 , pp. 437-454
    • He, F.1    Jacobson, A.2
  • 52
  • 53
    • 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., and Achsel T. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8 (2002) 1489-1501
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Luhrmann, R.3    Achsel, T.4
  • 54
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function
    • Isken O., and Maquat L.E. Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Genes Dev. 21 (2007) 1833-1856
    • (2007) Genes Dev. , vol.21 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2
  • 55
    • 41949113083 scopus 로고    scopus 로고
    • Upf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decay
    • Isken O., Kim Y.K., Hosoda N., Mayeur G.L., Hershey J.W., and Maquat L.E. Upf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decay. Cell 133 (2008) 314-327
    • (2008) Cell , vol.133 , pp. 314-327
    • Isken, O.1    Kim, Y.K.2    Hosoda, N.3    Mayeur, G.L.4    Hershey, J.W.5    Maquat, L.E.6
  • 56
    • 34248546224 scopus 로고    scopus 로고
    • Characterization of Arabidopsis decapping proteins AtDCP1 and AtDCP2, which are essential for post-embryonic development
    • Iwasaki S., Takeda A., Motose H., and Watanabe Y. Characterization of Arabidopsis decapping proteins AtDCP1 and AtDCP2, which are essential for post-embryonic development. FEBS Lett. 581 (2007) 2455-2459
    • (2007) FEBS Lett. , vol.581 , pp. 2455-2459
    • Iwasaki, S.1    Takeda, A.2    Motose, H.3    Watanabe, Y.4
  • 58
    • 33751541451 scopus 로고    scopus 로고
    • Identification of an mRNA-decapping regulator implicated in X-linked mental retardation
    • Jiao X., Wang Z., and Kiledjian M. Identification of an mRNA-decapping regulator implicated in X-linked mental retardation. Mol. Cell 24 (2006) 713-722
    • (2006) Mol. Cell , vol.24 , pp. 713-722
    • Jiao, X.1    Wang, Z.2    Kiledjian, M.3
  • 60
    • 1642343366 scopus 로고    scopus 로고
    • Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae
    • Kshirsagar M., and Parker R. Identification of Edc3p as an enhancer of mRNA decapping in Saccharomyces cerevisiae. Genetics 166 (2004) 729-739
    • (2004) Genetics , vol.166 , pp. 729-739
    • Kshirsagar, M.1    Parker, R.2
  • 61
    • 0032473359 scopus 로고    scopus 로고
    • Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme
    • LaGrandeur T.E., and Parker R. Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme. EMBO J. 17 (1998) 1487-1496
    • (1998) EMBO J. , vol.17 , pp. 1487-1496
    • LaGrandeur, T.E.1    Parker, R.2
  • 62
    • 28644447670 scopus 로고    scopus 로고
    • Caenorhabditis elegans decapping proteins: localization and functional analysis of Dcp1, Dcp2, and DcpS during embryogenesis
    • Lall S., Piano F., and Davis R.E. Caenorhabditis elegans decapping proteins: localization and functional analysis of Dcp1, Dcp2, and DcpS during embryogenesis. Mol. Biol. Cell 16 (2005) 5880-5890
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5880-5890
    • Lall, S.1    Piano, F.2    Davis, R.E.3
  • 63
    • 33845295461 scopus 로고    scopus 로고
    • Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules
    • Leung A.K., Calabrese J.M., and Sharp P.A. Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules. Proc. Natl. Acad. Sci. USA 103 (2006) 18125-18130
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18125-18130
    • Leung, A.K.1    Calabrese, J.M.2    Sharp, P.A.3
  • 64
    • 38549136876 scopus 로고    scopus 로고
    • Transcript-specific decapping and regulated stability by the human Dcp2 decapping protein
    • Li Y., Song M.G., and Kiledjian M. Transcript-specific decapping and regulated stability by the human Dcp2 decapping protein. Mol. Cell. Biol. 28 (2008) 939-948
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 939-948
    • Li, Y.1    Song, M.G.2    Kiledjian, M.3
  • 65
    • 53049095652 scopus 로고    scopus 로고
    • Drosophila processing bodies in oogenesis
    • 10.1016/j.ydbio.2008.07.033 in press. Published online August, 2008
    • Lin M.D., Jiao X., Grima D., Newbury S.F., Kiledjian M., and Chou T.B. Drosophila processing bodies in oogenesis. Dev. Biol. (2008) 10.1016/j.ydbio.2008.07.033 in press. Published online August, 2008
    • (2008) Dev. Biol.
    • Lin, M.D.1    Jiao, X.2    Grima, D.3    Newbury, S.F.4    Kiledjian, M.5    Chou, T.B.6
  • 67
    • 22144478256 scopus 로고    scopus 로고
    • MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies
    • Liu J., Valencia-Sanchez M.A., Hannon G.J., and Parker R. MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Nat. Cell Biol. 7 (2005) 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
  • 68
    • 0036888905 scopus 로고    scopus 로고
    • Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay
    • Lykke-Andersen J. Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol. Cell. Biol. 22 (2002) 8114-8121
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8114-8121
    • Lykke-Andersen, J.1
  • 69
    • 0035958843 scopus 로고    scopus 로고
    • The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation
    • Martinez J., Ren Y.G., Nilsson P., Ehrenberg M., and Virtanen A. The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J. Biol. Chem. 276 (2001) 27923-27929
    • (2001) J. Biol. Chem. , vol.276 , pp. 27923-27929
    • Martinez, J.1    Ren, Y.G.2    Nilsson, P.3    Ehrenberg, M.4    Virtanen, A.5
  • 70
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • McLennan A.G. The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63 (2006) 123-143
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 71
    • 2542580178 scopus 로고    scopus 로고
    • The active form of Xp54 RNA helicase in translational repression is an RNA-mediated oligomer
    • Minshall N., and Standart N. The active form of Xp54 RNA helicase in translational repression is an RNA-mediated oligomer. Nucleic Acids Res. 32 (2004) 1325-1334
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1325-1334
    • Minshall, N.1    Standart, N.2
  • 72
    • 0027932513 scopus 로고
    • Premature translational termination triggers mRNA decapping
    • Muhlrad D., and Parker R. Premature translational termination triggers mRNA decapping. Nature 370 (1994) 578-581
    • (1994) Nature , vol.370 , pp. 578-581
    • Muhlrad, D.1    Parker, R.2
  • 73
    • 0032880399 scopus 로고    scopus 로고
    • Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance
    • Muhlrad D., and Parker R. Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance. RNA 5 (1999) 1299-1307
    • (1999) RNA , vol.5 , pp. 1299-1307
    • Muhlrad, D.1    Parker, R.2
  • 74
    • 16344395154 scopus 로고    scopus 로고
    • The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p
    • Muhlrad D., and Parker R. The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p. EMBO J. 24 (2005) 1033-1045
    • (2005) EMBO J. , vol.24 , pp. 1033-1045
    • Muhlrad, D.1    Parker, R.2
  • 75
    • 0028202495 scopus 로고
    • Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript
    • Muhlrad D., Decker C.J., and Parker R. Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript. Genes Dev. 8 (1994) 855-866
    • (1994) Genes Dev. , vol.8 , pp. 855-866
    • Muhlrad, D.1    Decker, C.J.2    Parker, R.3
  • 76
    • 38149023239 scopus 로고    scopus 로고
    • Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5′ to 3′ and 3′ to 5′
    • Mullen T.E., and Marzluff W.F. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5′ to 3′ and 3′ to 5′. Genes Dev. 22 (2008) 50-65
    • (2008) Genes Dev. , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 77
    • 0034800019 scopus 로고    scopus 로고
    • Me31B silences translation of oocyte-localizing RNAs through the formation of cytoplasmic RNP complex during Drosophila oogenesis
    • Nakamura A., Amikura R., Hanyu K., and Kobayashi S. Me31B silences translation of oocyte-localizing RNAs through the formation of cytoplasmic RNP complex during Drosophila oogenesis. Development 128 (2001) 3233-3242
    • (2001) Development , vol.128 , pp. 3233-3242
    • Nakamura, A.1    Amikura, R.2    Hanyu, K.3    Kobayashi, S.4
  • 78
    • 23244451579 scopus 로고    scopus 로고
    • Requirement for P granules and meiosis for accumulation of the germline RNA helicase CGH-1
    • Navarro R.E., and Blackwell T.K. Requirement for P granules and meiosis for accumulation of the germline RNA helicase CGH-1. Genesis 42 (2005) 172-180
    • (2005) Genesis , vol.42 , pp. 172-180
    • Navarro, R.E.1    Blackwell, T.K.2
  • 79
    • 0034794426 scopus 로고    scopus 로고
    • cgh-1, a conserved predicted RNA helicase required for gametogenesis and protection from physiological germline apoptosis in C. elegans
    • Navarro R.E., Shim E.Y., Kohara Y., Singson A., and Blackwell T.K. cgh-1, a conserved predicted RNA helicase required for gametogenesis and protection from physiological germline apoptosis in C. elegans. Development 128 (2001) 3221-3232
    • (2001) Development , vol.128 , pp. 3221-3232
    • Navarro, R.E.1    Shim, E.Y.2    Kohara, Y.3    Singson, A.4    Blackwell, T.K.5
  • 80
    • 0038458311 scopus 로고    scopus 로고
    • East of EDEN was a poly(A) tail
    • Paillard L., and Osborne H.B. East of EDEN was a poly(A) tail. Biol. Cell 95 (2003) 211-219
    • (2003) Biol. Cell , vol.95 , pp. 211-219
    • Paillard, L.1    Osborne, H.B.2
  • 81
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R., and Sheth U. P bodies and the control of mRNA translation and degradation. Mol. Cell 25 (2007) 635-646
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 82
    • 33847779501 scopus 로고    scopus 로고
    • Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression
    • Parrish S., Resch W., and Moss B. Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression. Proc. Natl. Acad. Sci. USA 104 (2007) 2139-2144
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2139-2144
    • Parrish, S.1    Resch, W.2    Moss, B.3
  • 84
    • 0041832085 scopus 로고    scopus 로고
    • Functional characterization of the mammalian mRNA decapping enzyme hDcp2
    • Piccirillo C., Khanna R., and Kiledjian M. Functional characterization of the mammalian mRNA decapping enzyme hDcp2. RNA 9 (2003) 1138-1147
    • (2003) RNA , vol.9 , pp. 1138-1147
    • Piccirillo, C.1    Khanna, R.2    Kiledjian, M.3
  • 85
    • 38949151861 scopus 로고    scopus 로고
    • Pat1 contains distinct functional domains that promote P-body assembly and activation of decapping
    • Pilkington G.R., and Parker R. Pat1 contains distinct functional domains that promote P-body assembly and activation of decapping. Mol. Cell. Biol. 28 (2008) 1298-1312
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1298-1312
    • Pilkington, G.R.1    Parker, R.2
  • 87
    • 25844442472 scopus 로고    scopus 로고
    • A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-mediated gene silencing
    • Rehwinkel J., Behm-Ansmant I., Gatfield D., and Izaurralde E. A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-mediated gene silencing. RNA 11 (2005) 1640-1647
    • (2005) RNA , vol.11 , pp. 1640-1647
    • Rehwinkel, J.1    Behm-Ansmant, I.2    Gatfield, D.3    Izaurralde, E.4
  • 88
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • Reijns M.A., Alexander R.D., Spiller M.P., and Beggs J.D. A role for Q/N-rich aggregation-prone regions in P-body localization. J. Cell Sci. 121 (2008) 2463-2472
    • (2008) J. Cell Sci. , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 89
    • 14944354785 scopus 로고    scopus 로고
    • Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human
    • Sakuno T., Araki Y., Ohya Y., Kofuji S., Takahashi S., Hoshino S., and Katada T. Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human. J. Biochem. 136 (2004) 805-812
    • (2004) J. Biochem. , vol.136 , pp. 805-812
    • Sakuno, T.1    Araki, Y.2    Ohya, Y.3    Kofuji, S.4    Takahashi, S.5    Hoshino, S.6    Katada, T.7
  • 92
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae
    • Schwartz D.C., and Parker R. Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 (1999) 5247-5256
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5247-5256
    • Schwartz, D.C.1    Parker, R.2
  • 93
    • 0033773044 scopus 로고    scopus 로고
    • mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E
    • Schwartz D.C., and Parker R. mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 20 (2000) 7933-7942
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7933-7942
    • Schwartz, D.C.1    Parker, R.2
  • 94
    • 0037322952 scopus 로고    scopus 로고
    • The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate the activity of the decapping enzyme
    • Schwartz D., Decker C.J., and Parker R. The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate the activity of the decapping enzyme. RNA 9 (2003) 239-251
    • (2003) RNA , vol.9 , pp. 239-251
    • Schwartz, D.1    Decker, C.J.2    Parker, R.3
  • 95
    • 20444427566 scopus 로고    scopus 로고
    • Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies
    • Sen G.L., and Blau H.M. Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies. Nat. Cell Biol. 7 (2005) 633-636
    • (2005) Nat. Cell Biol. , vol.7 , pp. 633-636
    • Sen, G.L.1    Blau, H.M.2
  • 97
    • 30044439885 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe
    • She M., Decker C.J., Chen N., Tumati S., Parker R., and Song H. Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat. Struct. Mol. Biol. 13 (2006) 63-70
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 63-70
    • She, M.1    Decker, C.J.2    Chen, N.3    Tumati, S.4    Parker, R.5    Song, H.6
  • 99
    • 19644400971 scopus 로고    scopus 로고
    • Uridine addition after microRNA-directed cleavage
    • Shen B., and Goodman H.M. Uridine addition after microRNA-directed cleavage. Science 306 (2004) 997
    • (2004) Science , vol.306 , pp. 997
    • Shen, B.1    Goodman, H.M.2
  • 100
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth U., and Parker R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300 (2003) 805-808
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 101
    • 33744977432 scopus 로고    scopus 로고
    • Targeting of aberrant mRNAs to cytoplasmic processing bodies
    • Sheth U., and Parker R. Targeting of aberrant mRNAs to cytoplasmic processing bodies. Cell 125 (2006) 1095-1109
    • (2006) Cell , vol.125 , pp. 1095-1109
    • Sheth, U.1    Parker, R.2
  • 102
    • 36248947229 scopus 로고    scopus 로고
    • 3′ terminal oligo U-tract-mediated stimulation of decapping
    • Song M.G., and Kiledjian M. 3′ terminal oligo U-tract-mediated stimulation of decapping. RNA 13 (2007) 2356-2365
    • (2007) RNA , vol.13 , pp. 2356-2365
    • Song, M.G.1    Kiledjian, M.2
  • 104
    • 33646200678 scopus 로고    scopus 로고
    • ARE-mRNA degradation requires the 5′-3′ decay pathway
    • Stoecklin G., Mayo T., and Anderson P. ARE-mRNA degradation requires the 5′-3′ decay pathway. EMBO Rep. 7 (2006) 72-77
    • (2006) EMBO Rep. , vol.7 , pp. 72-77
    • Stoecklin, G.1    Mayo, T.2    Anderson, P.3
  • 105
    • 14744304265 scopus 로고    scopus 로고
    • The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: a unique viral response to host defense
    • Tang J., Naitow H., Gardner N.A., Kolesar A., Tang L., Wickner R.B., and Johnson J.E. The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: a unique viral response to host defense. J. Mol. Recognit. 18 (2005) 158-168
    • (2005) J. Mol. Recognit. , vol.18 , pp. 158-168
    • Tang, J.1    Naitow, H.2    Gardner, N.A.3    Kolesar, A.4    Tang, L.5    Wickner, R.B.6    Johnson, J.E.7
  • 106
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain nontranslating mRNAs
    • Teixeira D., Sheth U., Valencia-Sanchez M.A., Brengues M., and Parker R. Processing bodies require RNA for assembly and contain nontranslating mRNAs. RNA 11 (2005) 371-382
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 107
    • 0032940545 scopus 로고    scopus 로고
    • Analysis of mutations in the yeast mRNA decapping enzyme
    • Tharun S., and Parker R. Analysis of mutations in the yeast mRNA decapping enzyme. Genetics 151 (1999) 1273-1285
    • (1999) Genetics , vol.151 , pp. 1273-1285
    • Tharun, S.1    Parker, R.2
  • 108
    • 0035930337 scopus 로고    scopus 로고
    • Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs
    • Tharun S., and Parker R. Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8 (2001) 1075-1083
    • (2001) Mol. Cell , vol.8 , pp. 1075-1083
    • Tharun, S.1    Parker, R.2
  • 109
  • 110
    • 20444429430 scopus 로고    scopus 로고
    • Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3′ end protection
    • Tharun S., Muhlrad D., Chowdhury A., and Parker R. Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3′ end protection. Genetics 170 (2005) 33-46
    • (2005) Genetics , vol.170 , pp. 33-46
    • Tharun, S.1    Muhlrad, D.2    Chowdhury, A.3    Parker, R.4
  • 113
    • 8844245615 scopus 로고    scopus 로고
    • SMG7 acts as a molecular link between mRNA surveillance and mRNA decay
    • Unterholzner L., and Izaurralde E. SMG7 acts as a molecular link between mRNA surveillance and mRNA decay. Mol. Cell 16 (2004) 587-596
    • (2004) Mol. Cell , vol.16 , pp. 587-596
    • Unterholzner, L.1    Izaurralde, E.2
  • 114
    • 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., and Seraphin B. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21 (2002) 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
  • 115
    • 33947262696 scopus 로고    scopus 로고
    • AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2
    • Vasudevan S., and Steitz J.A. AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2. Cell 128 (2007) 1105-1118
    • (2007) Cell , vol.128 , pp. 1105-1118
    • Vasudevan, S.1    Steitz, J.A.2
  • 116
    • 0035861864 scopus 로고    scopus 로고
    • Functional link between the mammalian exosome and mRNA decapping
    • Wang Z., and Kiledjian M. Functional link between the mammalian exosome and mRNA decapping. Cell 107 (2001) 751-762
    • (2001) Cell , vol.107 , pp. 751-762
    • Wang, Z.1    Kiledjian, M.2
  • 118
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells S.E., Hillner P.E., Vale R.D., and Sachs A.B. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2 (1998) 135-140
    • (1998) Mol. Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 119
    • 33947540895 scopus 로고    scopus 로고
    • Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development
    • Xu J., Yang J.Y., Niu Q.W., and Chua N.H. Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development. Plant Cell 18 (2006) 3386-3398
    • (2006) Plant Cell , vol.18 , pp. 3386-3398
    • Xu, J.1    Yang, J.Y.2    Niu, Q.W.3    Chua, N.H.4
  • 121
    • 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., and Bloch D.B. Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body. RNA 11 (2005) 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
  • 122
    • 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., and Shyu A.B. Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J. Cell Biol. 182 (2008) 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


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