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Volumn 288, Issue 28, 2013, Pages 20723-20733

The nucleic acid-binding domain and translational repression activity of a Xenopus terminal uridylyl transferase

Author keywords

[No Author keywords available]

Indexed keywords

BASIC AMINO ACIDS; CATALYTIC CORE; MESSENGER RNA; MICRORNAS; MUTATIONAL ANALYSIS; SHORT SEGMENTS; XENOPUS LAEVIS; ZINC FINGER DOMAINS;

EID: 84880059154     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.455451     Document Type: Article
Times cited : (19)

References (69)
  • 1
    • 40549087668 scopus 로고    scopus 로고
    • Molecular biology. A tail tale for U
    • Wickens, M., and Kwak, J. E. (2008) Molecular biology. A tail tale for U. Science 319, 1344-1345
    • (2008) Science , vol.319 , pp. 1344-1345
    • Wickens, M.1    Kwak, J.E.2
  • 2
    • 77955947192 scopus 로고    scopus 로고
    • 3′ Uridylation and the regulation of RNA function in the cytoplasm
    • Norbury, C. J. (2010) 3′ Uridylation and the regulation of RNA function in the cytoplasm. Biochem. Soc. Trans. 38, 1150-1153
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1150-1153
    • Norbury, C.J.1
  • 3
    • 78650433004 scopus 로고    scopus 로고
    • Polyadenylation and beyond: Emerging roles for noncanonical poly(A) polymerases
    • Schmidt, M. J., and Norbury, C. J. (2010) Polyadenylation and beyond: emerging roles for noncanonical poly(A) polymerases. Wiley Interdiscip. Rev. RNA 1, 142-151
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 142-151
    • Schmidt, M.J.1    Norbury, C.J.2
  • 4
    • 79251485649 scopus 로고    scopus 로고
    • Modifications of small RNAs and their associated proteins
    • Kim, Y. K., Heo, I., and Kim, V. N. (2010) Modifications of small RNAs and their associated proteins. Cell 143, 703-709
    • (2010) Cell , vol.143 , pp. 703-709
    • Kim, Y.K.1    Heo, I.2    Kim, V.N.3
  • 5
    • 36248947229 scopus 로고    scopus 로고
    • 3′ Terminal oligo U-tract-mediated stimulation of decapping
    • Song, M. G., and Kiledjian, M. (2007) 3′ Terminal oligo U-tract-mediated stimulation of decapping. RNA 13, 2356-2365
    • (2007) RNA , vol.13 , pp. 2356-2365
    • Song, M.G.1    Kiledjian, M.2
  • 6
    • 34248225381 scopus 로고    scopus 로고
    • Efficient RNA polyuridylation by noncanonical poly(A) polymerases
    • DOI 10.1128/MCB.02209-06
    • Rissland, O. S., Mikulasova, A., and Norbury, C. J. (2007) Efficient RNA polyuridylation by noncanonical poly(A) polymerases. Mol. Cell. Biol. 27, 3612-3624 (Pubitemid 46726172)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.10 , pp. 3612-3624
    • Rissland, O.S.1    Mikulasova, A.2    Norbury, C.J.3
  • 7
    • 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. (2008) 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, 50-65
    • (2008) Genes Dev. , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 8
    • 66849122924 scopus 로고    scopus 로고
    • Decapping is preceded by 3′ uridylation in a novel pathway of bulk mRNA turnover
    • Rissland, O. S., and Norbury, C. J. (2009) Decapping is preceded by 3′ uridylation in a novel pathway of bulk mRNA turnover. Nat. Struct. Mol. Biol. 16, 616-623
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 616-623
    • Rissland, O.S.1    Norbury, C.J.2
  • 9
    • 78650446573 scopus 로고    scopus 로고
    • The human cytoplasmic RNA terminal U-transferase ZCCHC11 targets histone mRNAs for degradation
    • Schmidt, M. J., West, S., and Norbury, C. J. (2011) The human cytoplasmic RNA terminal U-transferase ZCCHC11 targets histone mRNAs for degradation. RNA 17, 39-44
    • (2011) RNA , vol.17 , pp. 39-44
    • Schmidt, M.J.1    West, S.2    Norbury, C.J.3
  • 12
    • 53949088050 scopus 로고    scopus 로고
    • Lin28 mediates the terminal uridylation of let-7 precursor microRNA
    • Heo, I., Joo, C., Cho, J., Ha, M., Han, J., and Kim, V. N. (2008) Lin28 mediates the terminal uridylation of let-7 precursor microRNA. Mol. Cell 32, 276-284
    • (2008) Mol. Cell , vol.32 , pp. 276-284
    • Heo, I.1    Joo, C.2    Cho, J.3    Ha, M.4    Han, J.5    Kim, V.N.6
  • 14
    • 70349820140 scopus 로고    scopus 로고
    • Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells
    • Hagan, J. P., Piskounova, E., and Gregory, R. I. (2009) Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells. Nat. Struct. Mol. Biol. 16, 1021-1025
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1021-1025
    • Hagan, J.P.1    Piskounova, E.2    Gregory, R.I.3
  • 15
    • 68749102148 scopus 로고    scopus 로고
    • TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation
    • Heo, I., Joo, C., Kim, Y. K., Ha, M., Yoon, M. J., Cho, J., Yeom, K. H., Han, J., and Kim, V. N. (2009) TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation. Cell 138, 696-708
    • (2009) Cell , vol.138 , pp. 696-708
    • Heo, I.1    Joo, C.2    Kim, Y.K.3    Ha, M.4    Yoon, M.J.5    Cho, J.6    Yeom, K.H.7    Han, J.8    Kim, V.N.9
  • 16
    • 84866597456 scopus 로고    scopus 로고
    • Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7)
    • Thornton, J. E., Chang, H. M., Piskounova, E., and Gregory, R. I. (2012) Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7). RNA 18, 1875-1885
    • (2012) RNA , vol.18 , pp. 1875-1885
    • Thornton, J.E.1    Chang, H.M.2    Piskounova, E.3    Gregory, R.I.4
  • 17
    • 84868153864 scopus 로고    scopus 로고
    • Mono-uridylation of pre-microRNA as a key step in the biogenesis of group II let-7 microRNAs
    • Heo, I., Ha, M., Lim, J., Yoon, M. J., Park, J. E., Kwon, S. C., Chang, H., and Kim, V. N. (2012) Mono-uridylation of pre-microRNA as a key step in the biogenesis of group II let-7 microRNAs. Cell 151, 521-532
    • (2012) Cell , vol.151 , pp. 521-532
    • Heo, I.1    Ha, M.2    Lim, J.3    Yoon, M.J.4    Park, J.E.5    Kwon, S.C.6    Chang, H.7    Kim, V.N.8
  • 18
    • 80053208703 scopus 로고    scopus 로고
    • Deep sequencing of microRNA precursors reveals extensive 3′ end modification
    • Newman, M. A., Mani, V., and Hammond, S. M. (2011) Deep sequencing of microRNA precursors reveals extensive 3′ end modification. RNA 17, 1795-1803
    • (2011) RNA , vol.17 , pp. 1795-1803
    • Newman, M.A.1    Mani, V.2    Hammond, S.M.3
  • 20
    • 77649255166 scopus 로고    scopus 로고
    • Uridylation of mature miRNAs and siRNAs by the MUT68 nucleotidyltransferase promotes their degradation in Chlamydomonas
    • Ibrahim, F., Rymarquis, L. A., Kim, E. J., Becker, J., Balassa, E., Green, P. J., and Cerutti, H. (2010) Uridylation of mature miRNAs and siRNAs by the MUT68 nucleotidyltransferase promotes their degradation in Chlamydomonas. Proc. Natl. Acad. Sci. U.S.A. 107, 3906-3911
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3906-3911
    • Ibrahim, F.1    Rymarquis, L.A.2    Kim, E.J.3    Becker, J.4    Balassa, E.5    Green, P.J.6    Cerutti, H.7
  • 21
    • 84860307087 scopus 로고    scopus 로고
    • Uridylation of miRNAs by hen1 suppressor1 in Arabidopsis
    • Ren, G., Chen, X., and Yu, B. (2012) Uridylation of miRNAs by hen1 suppressor1 in Arabidopsis. Curr. Biol. 22, 695-700
    • (2012) Curr. Biol. , vol.22 , pp. 695-700
    • Ren, G.1    Chen, X.2    Yu, B.3
  • 22
    • 84860301401 scopus 로고    scopus 로고
    • The Arabidopsis nucleotidyl transferase HESO1 uridylates unmethylated small RNAs to trigger their degradation
    • Zhao, Y., Yu, Y., Zhai, J., Ramachandran, V., Dinh, T. T., Meyers, B. C., Mo, B., and Chen, X. (2012) The Arabidopsis nucleotidyl transferase HESO1 uridylates unmethylated small RNAs to trigger their degradation. Curr. Biol. 22, 689-694
    • (2012) Curr. Biol. , vol.22 , pp. 689-694
    • Zhao, Y.1    Yu, Y.2    Zhai, J.3    Ramachandran, V.4    Dinh, T.T.5    Meyers, B.C.6    Mo, B.7    Chen, X.8
  • 25
    • 80052527459 scopus 로고    scopus 로고
    • Post-transcriptional generation of miRNA variants by multiple nucleotidyl transferases contributes to miRNA transcriptome complexity
    • Wyman, S. K., Knouf, E. C., Parkin, R. K., Fritz, B. R., Lin, D. W., Dennis, L. M., Krouse, M. A., Webster, P. J., and Tewari, M. (2011) Post-transcriptional generation of miRNA variants by multiple nucleotidyl transferases contributes to miRNA transcriptome complexity. Genome Res. 21, 1450-1461
    • (2011) Genome Res. , vol.21 , pp. 1450-1461
    • Wyman, S.K.1    Knouf, E.C.2    Parkin, R.K.3    Fritz, B.R.4    Lin, D.W.5    Dennis, L.M.6    Krouse, M.A.7    Webster, P.J.8    Tewari, M.9
  • 27
    • 27144545842 scopus 로고    scopus 로고
    • RNA uridylyltransferases
    • Aphasizhev, R. (2005) RNA uridylyltransferases. Cell. Mol. Life Sci. 62, 2194-2203
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2194-2203
    • Aphasizhev, R.1
  • 28
    • 35548959608 scopus 로고    scopus 로고
    • RNA-specific ribonucleotidyl transferases
    • DOI 10.1261/rna.652807
    • Martin, G., and Keller, W. (2007) RNA-specific ribonucleotidyl transferases. RNA 13, 1834-1849 (Pubitemid 350005209)
    • (2007) RNA , vol.13 , Issue.11 , pp. 1834-1849
    • Martin, G.1    Keller, W.2
  • 29
    • 34249026025 scopus 로고    scopus 로고
    • A family of poly(U) polymerases
    • Kwak, J. E., and Wickens, M. (2007) A family of poly(U) polymerases. RNA 13, 860-867
    • (2007) RNA , vol.13 , pp. 860-867
    • Kwak, J.E.1    Wickens, M.2
  • 31
    • 84868159990 scopus 로고    scopus 로고
    • Crystal structures of the Cid1 poly(U) polymerase reveal the mechanism for UTP selectivity
    • Lunde, B. M., Magler, I., and Meinhart, A. (2012) Crystal structures of the Cid1 poly(U) polymerase reveal the mechanism for UTP selectivity. Nucleic Acids Res. 40, 9815-9824
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9815-9824
    • Lunde, B.M.1    Magler, I.2    Meinhart, A.3
  • 32
    • 84861974528 scopus 로고    scopus 로고
    • Functional implications from the Cid1 poly(U) polymerase crystal structure
    • Munoz-Tello, P., Gabus, C., and Thore, S. (2012) Functional implications from the Cid1 poly(U) polymerase crystal structure. Structure 20, 977-986
    • (2012) Structure , vol.20 , pp. 977-986
    • Munoz-Tello, P.1    Gabus, C.2    Thore, S.3
  • 33
    • 41549109256 scopus 로고    scopus 로고
    • Determinants of substrate specificity in RNA-dependent nucleotidyl transferases
    • DOI 10.1016/j.bbagrm.2007.12.003, PII S1874939907001964
    • Martin, G., Doublié, S., and Keller, W. (2008) Determinants of substrate specificity in RNA-dependent nucleotidyl transferases. Biochim. Biophys Acta 1779, 206-216 (Pubitemid 351474487)
    • (2008) Biochimica et Biophysica Acta - Gene Regulatory Mechanisms , vol.1779 , Issue.4 , pp. 206-216
    • Martin, G.1    Doublie, S.2    Keller, W.3
  • 34
    • 52949091534 scopus 로고    scopus 로고
    • The let-7 family of microRNAs
    • Roush, S., and Slack, F. J. (2008) The let-7 family of microRNAs. Trends Cell Biol. 18, 505-516
    • (2008) Trends Cell Biol. , vol.18 , pp. 505-516
    • Roush, S.1    Slack, F.J.2
  • 35
    • 77956503398 scopus 로고    scopus 로고
    • Translational repression by deadenylases
    • Cooke, A., Prigge, A., and Wickens, M. (2010) Translational repression by deadenylases. J. Biol. Chem. 285, 28506-28513
    • (2010) J. Biol. Chem. , vol.285 , pp. 28506-28513
    • Cooke, A.1    Prigge, A.2    Wickens, M.3
  • 36
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan - An integration platform for the signature-recognition methods in InterPro
    • Zdobnov, E. M., and Apweiler, R. (2001) InterProScan - an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17, 847-848 (Pubitemid 32970486)
    • (2001) Bioinformatics , vol.17 , Issue.9 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 39
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 40
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • DOI 10.1101/gr.849004
    • Crooks, G. E., Hon, G., Chandonia, J. M., and Brenner, S. E. (2004) WebLogo: a sequence logo generator. Genome Res 14, 1188-1190 (Pubitemid 38811555)
    • (2004) Genome Research , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.-M.3    Brenner, S.E.4
  • 41
    • 0034282752 scopus 로고    scopus 로고
    • Multiple portions of poly(A)-binding protein stimulate translation in vivo
    • Gray, N. K., Coller, J. M., Dickson, K. S., and Wickens, M. (2000) Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 19, 4723-4733
    • (2000) EMBO J. , vol.19 , pp. 4723-4733
    • Gray, N.K.1    Coller, J.M.2    Dickson, K.S.3    Wickens, M.4
  • 42
    • 77952703757 scopus 로고    scopus 로고
    • Translational repression by PUF proteins in vitro
    • Chritton, J. J., and Wickens, M. (2010) Translational repression by PUF proteins in vitro. RNA 16, 1217-1225
    • (2010) RNA , vol.16 , pp. 1217-1225
    • Chritton, J.J.1    Wickens, M.2
  • 43
    • 80053159210 scopus 로고    scopus 로고
    • Targeted translational regulation using the PUF protein family scaffold
    • Cooke, A., Prigge, A., Opperman, L., and Wickens, M. (2011) Targeted translational regulation using the PUF protein family scaffold. Proc. Natl. Acad. Sci. U.S.A. 108, 15870-15875
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 15870-15875
    • Cooke, A.1    Prigge, A.2    Opperman, L.3    Wickens, M.4
  • 45
    • 2342437314 scopus 로고    scopus 로고
    • Cytoplasmic Polyadenylation Element (CPE)- and CPE-binding Protein (CPEB)-independent Mechanisms Regulate Early Class Maternal mRNA Translational Activation in Xenopus Oocytes
    • DOI 10.1074/jbc.M313837200
    • Charlesworth, A., Cox, L. L., and MacNicol, A. M. (2004) Cytoplasmic polyadenylation element (CPE)- and CPE-binding protein (CPEB)-independent mechanisms regulate early class maternal mRNA translational activation in Xenopus oocytes. J. Biol. Chem. 279, 17650-17659 (Pubitemid 38560530)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17650-17659
    • Charlesworth, A.1    Cox, L.L.2    MacNicol, A.M.3
  • 46
    • 34447503943 scopus 로고    scopus 로고
    • Two yeast PUF proteins negatively regulate a single mRNA
    • DOI 10.1074/jbc.M611253200
    • Hook, B. A., Goldstrohm, A. C., Seay, D. J., and Wickens, M. (2007) Two yeast PUF proteins negatively regulate a single mRNA. J. Biol. Chem. 282, 15430-15438 (Pubitemid 47093267)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.21 , pp. 15430-15438
    • Hook, B.A.1    Goldstrohm, A.C.2    Seay, D.J.3    Wickens, M.4
  • 47
    • 0037136552 scopus 로고    scopus 로고
    • A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans
    • Wang, L., Eckmann, C. R., Kadyk, L. C., Wickens, M., and Kimble, J. (2002) A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans. Nature 419, 312-316
    • (2002) Nature , vol.419 , pp. 312-316
    • Wang, L.1    Eckmann, C.R.2    Kadyk, L.C.3    Wickens, M.4    Kimble, J.5
  • 49
    • 0024434420 scopus 로고
    • Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif
    • DOI 10.1016/0092-8674(89)90882-9
    • Lazinski, D., Grzadzielska, E., and Das, A. (1989) Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif. Cell 59, 207-218 (Pubitemid 19248570)
    • (1989) Cell , vol.59 , Issue.1 , pp. 207-218
    • Lazinski, D.1    Gradzielska, E.2    Das, A.3
  • 50
    • 0025168740 scopus 로고
    • Fragments of the HIV-1 Tat protein specifically bind TAR RNA
    • Weeks, K. M., Ampe, C., Schultz, S. C., Steitz, T. A., and Crothers, D. M. (1990) Fragments of the HIV-1 Tat protein specifically bind TAR RNA. Science 249, 1281-1285
    • (1990) Science , vol.249 , pp. 1281-1285
    • Weeks, K.M.1    Ampe, C.2    Schultz, S.C.3    Steitz, T.A.4    Crothers, D.M.5
  • 51
    • 0026350074 scopus 로고
    • Arginine-mediated RNA recognition: The arginine fork
    • Calnan, B. J., Tidor, B., Biancalana, S., Hudson, D., and Frankel, A. D. (1991) Arginine-mediated RNA recognition: the arginine fork. Science 252, 1167-1171 (Pubitemid 21917028)
    • (1991) Science , vol.252 , Issue.5009 , pp. 1167-1171
    • Calnan, B.J.1    Tidor, B.2    Biancalana, S.3    Hudson, D.4    Frankel, A.D.5
  • 52
    • 84860390193 scopus 로고    scopus 로고
    • PAPD5, a non-canonical poly(A) polymerase with an unusual RNA-binding motif
    • Rammelt, C., Bilen, B., Zavolan, M., and Keller, W. (2011) PAPD5, a non-canonical poly(A) polymerase with an unusual RNA-binding motif. RNA 17, 1737-1746
    • (2011) RNA , vol.17 , pp. 1737-1746
    • Rammelt, C.1    Bilen, B.2    Zavolan, M.3    Keller, W.4
  • 54
    • 0035671046 scopus 로고    scopus 로고
    • A conserved role of a DEAD box helicase in mRNA masking
    • DOI 10.1017/S135583820101158X
    • Minshall, N., Thom, G., and Standart, N. (2001) A conserved role of a DEAD box helicase in mRNA masking. RNA 7, 1728-1742 (Pubitemid 34042288)
    • (2001) RNA , vol.7 , Issue.12 , pp. 1728-1742
    • Minshall, N.1    Thom, G.2    Standart, N.3
  • 55
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 56
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 57
    • 84864460609 scopus 로고    scopus 로고
    • COFACTOR: An accurate comparative algorithm for structure-based protein function annotation
    • Roy, A., Yang, J., and Zhang, Y. (2012) COFACTOR: an accurate comparative algorithm for structure-based protein function annotation. Nucleic Acids Res. 40, W471-W477
    • (2012) Nucleic Acids Res. , vol.40
    • Roy, A.1    Yang, J.2    Zhang, Y.3
  • 58
    • 82755167738 scopus 로고    scopus 로고
    • Terminal uridyltransferase enzyme Zcchc11 promotes cell proliferation independent of its uridyltransferase activity
    • Blahna, M. T., Jones, M. R., Quinton, L. J., Matsuura, K. Y., and Mizgerd, J. P. (2011) Terminal uridyltransferase enzyme Zcchc11 promotes cell proliferation independent of its uridyltransferase activity. J. Biol. Chem. 286, 42381-42389
    • (2011) J. Biol. Chem. , vol.286 , pp. 42381-42389
    • Blahna, M.T.1    Jones, M.R.2    Quinton, L.J.3    Matsuura, K.Y.4    Mizgerd, J.P.5
  • 61
    • 0032419957 scopus 로고    scopus 로고
    • RNA recognition by arginine-rich peptide motifs
    • Weiss, M. A., and Narayana, N. (1998) RNA recognition by arginine-rich peptide motifs. Biopolymers 48, 167-180
    • (1998) Biopolymers , vol.48 , pp. 167-180
    • Weiss, M.A.1    Narayana, N.2
  • 62
    • 28344450939 scopus 로고    scopus 로고
    • Arginine-rich motifs present multiple interfaces for specific binding by RNA
    • DOI 10.1261/rna.2167605
    • Bayer, T. S., Booth, L. N., Knudsen, S. M., and Ellington, A. D. (2005) Arginine-rich motifs present multiple interfaces for specific binding by RNA. RNA 11, 1848-1857 (Pubitemid 41720034)
    • (2005) RNA , vol.11 , Issue.12 , pp. 1848-1857
    • Bayer, T.S.1    Booth, L.N.2    Knudsen, S.M.3    Ellington, A.D.4
  • 63
    • 78549248443 scopus 로고    scopus 로고
    • Structural basis for cooperative RNA binding and export complex assembly by HIV Rev
    • Daugherty, M. D., Liu, B., and Frankel, A. D. (2010) Structural basis for cooperative RNA binding and export complex assembly by HIV Rev. Nat. Struct. Mol. Biol. 17, 1337-1342
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1337-1342
    • Daugherty, M.D.1    Liu, B.2    Frankel, A.D.3
  • 64
    • 0025100771 scopus 로고
    • Secondary structure is the major determinant for interaction of HIV rev protein with RNA
    • Olsen, H. S., Nelbock, P., Cochrane, A. W., and Rosen, C. A. (1990) Secondary structure is the major determinant for interaction of HIV rev protein with RNA. Science 247, 845-848
    • (1990) Science , vol.247 , pp. 845-848
    • Olsen, H.S.1    Nelbock, P.2    Cochrane, A.W.3    Rosen, C.A.4
  • 65
    • 0024836618 scopus 로고
    • Specific binding of HIV-1 recombinant Rev protein to the Rev-responsive element in vitro
    • DOI 10.1038/342816a0
    • Daly, T. J., Cook, K. S., Gray, G. S., Maione, T. E., and Rusche, J. R. (1989) Specific binding of HIV-1 recombinant Rev protein to the Rev-responsive element in vitro. Nature 342, 816-819 (Pubitemid 20023818)
    • (1989) Nature , vol.342 , Issue.6251 , pp. 816-819
    • Daly, T.J.1    Cook, K.S.2    Gray, G.S.3    Maione, T.E.4    Rusche, J.R.5
  • 66
  • 67
    • 79959936612 scopus 로고    scopus 로고
    • Single-molecule approach to immunoprecipitated protein complexes: Insights into miRNA uridylation
    • Yeom, K. H., Heo, I., Lee, J., Hohng, S., Kim, V. N., and Joo, C. (2011) Single-molecule approach to immunoprecipitated protein complexes: insights into miRNA uridylation. EMBO Rep 12, 690-696
    • (2011) EMBO Rep , vol.12 , pp. 690-696
    • Yeom, K.H.1    Heo, I.2    Lee, J.3    Hohng, S.4    Kim, V.N.5    Joo, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.