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Volumn 18, Issue 1, 2008, Pages 120-129

Towards deciphering the principles underlying an mRNA recognition code

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RIBOSOME PROTEIN; SINGLE STRANDED RNA;

EID: 39149119601     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.12.006     Document Type: Review
Times cited : (24)

References (60)
  • 1
    • 34548778155 scopus 로고    scopus 로고
    • Ribozymes, riboswitches and beyond: regulation of gene expression without proteins
    • Serganov A., and Patel D.J. Ribozymes, riboswitches and beyond: regulation of gene expression without proteins. Nat Rev Genet 8 (2007) 776-790
    • (2007) Nat Rev Genet , vol.8 , pp. 776-790
    • Serganov, A.1    Patel, D.J.2
  • 2
    • 33750222859 scopus 로고    scopus 로고
    • Sequence-specific binding of single-stranded RNA: is there a code for recognition?
    • Auweter S.D., Oberstrass F.C., and Allain F.H. Sequence-specific binding of single-stranded RNA: is there a code for recognition?. Nucleic Acids Res 34 (2006) 4943-4959
    • (2006) Nucleic Acids Res , vol.34 , pp. 4943-4959
    • Auweter, S.D.1    Oberstrass, F.C.2    Allain, F.H.3
  • 3
    • 33744800528 scopus 로고    scopus 로고
    • Structures of regulatory elements in mRNAs
    • Batey R.T. Structures of regulatory elements in mRNAs. Curr Opin Struct Biol 16 (2006) 299-306
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 299-306
    • Batey, R.T.1
  • 4
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: modular design for efficient function
    • Lunde B.M., Moore C., and Varani G. RNA-binding proteins: modular design for efficient function. Nat Rev Mol Cell Biol 8 (2007) 479-490
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 5
    • 17844404891 scopus 로고    scopus 로고
    • RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle
    • Stefl R., Skrisovska L., and Allain F. RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle. EMBO Rep 6 (2005) 33-38
    • (2005) EMBO Rep , vol.6 , pp. 33-38
    • Stefl, R.1    Skrisovska, L.2    Allain, F.3
  • 6
    • 34347401399 scopus 로고    scopus 로고
    • Riboswitches: small-molecule recognition by gene regulatory RNAs
    • Edwards T.E., Klein D.J., and Ferre-D'Amare A.R. Riboswitches: small-molecule recognition by gene regulatory RNAs. Curr Opin Struct Biol 17 (2007) 273-279
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 273-279
    • Edwards, T.E.1    Klein, D.J.2    Ferre-D'Amare, A.R.3
  • 7
    • 34548454557 scopus 로고    scopus 로고
    • Structural features of metabolite-sensing riboswitches
    • Wakeman C.A., Winkler W.C., and Dann III C.E. Structural features of metabolite-sensing riboswitches. Trends Biochem Sci 32 (2007) 415-424
    • (2007) Trends Biochem Sci , vol.32 , pp. 415-424
    • Wakeman, C.A.1    Winkler, W.C.2    Dann III, C.E.3
  • 8
    • 34247242053 scopus 로고    scopus 로고
    • Structures of RNA switches: insight into molecular recognition and tertiary structure
    • Schwalbe H., Buck J., Furtig B., Noeske J., and Wohnert J. Structures of RNA switches: insight into molecular recognition and tertiary structure. Angew Chem Int Ed Engl 46 (2007) 1212-1219
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 1212-1219
    • Schwalbe, H.1    Buck, J.2    Furtig, B.3    Noeske, J.4    Wohnert, J.5
  • 9
    • 9244225713 scopus 로고    scopus 로고
    • Structure of a natural guanine-responsive riboswitch complexed with the metabolite hypoxanthine
    • Batey R.T., Gilbert S.D., and Montange R.K. Structure of a natural guanine-responsive riboswitch complexed with the metabolite hypoxanthine. Nature 432 (2004) 411-415
    • (2004) Nature , vol.432 , pp. 411-415
    • Batey, R.T.1    Gilbert, S.D.2    Montange, R.K.3
  • 11
    • 33748300801 scopus 로고    scopus 로고
    • Crystal structures of the thi-box riboswitch bound to thiamine pyrophosphate analogs reveal adaptive RNA-small molecule recognition
    • Edwards T.E., and Ferre-D'Amare A.R. Crystal structures of the thi-box riboswitch bound to thiamine pyrophosphate analogs reveal adaptive RNA-small molecule recognition. Structure 14 (2006) 1459-1468
    • (2006) Structure , vol.14 , pp. 1459-1468
    • Edwards, T.E.1    Ferre-D'Amare, A.R.2
  • 12
    • 33745635350 scopus 로고    scopus 로고
    • Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch
    • Serganov A., Polonskaia A., Phan A.T., Breaker R.R., and Patel D.J. Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch. Nature 441 (2006) 1167-1171
    • (2006) Nature , vol.441 , pp. 1167-1171
    • Serganov, A.1    Polonskaia, A.2    Phan, A.T.3    Breaker, R.R.4    Patel, D.J.5
  • 13
    • 33744469562 scopus 로고    scopus 로고
    • Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand
    • Thore S., Leibundgut M., and Ban N. Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand. Science 312 (2006) 1208-1211
    • (2006) Science , vol.312 , pp. 1208-1211
    • Thore, S.1    Leibundgut, M.2    Ban, N.3
  • 14
    • 33745628336 scopus 로고    scopus 로고
    • Structure of the S-adenosylmethionine riboswitch regulatory mRNA element
    • Montange R.K., and Batey R.T. Structure of the S-adenosylmethionine riboswitch regulatory mRNA element. Nature 441 (2006) 1172-1175
    • (2006) Nature , vol.441 , pp. 1172-1175
    • Montange, R.K.1    Batey, R.T.2
  • 15
    • 33846279049 scopus 로고    scopus 로고
    • Structural investigation of the GlmS ribozyme bound to its catalytic cofactor
    • Cochrane J.C., Lipchock S.V., and Strobel S.A. Structural investigation of the GlmS ribozyme bound to its catalytic cofactor. Chem Biol 14 (2007) 97-105
    • (2007) Chem Biol , vol.14 , pp. 97-105
    • Cochrane, J.C.1    Lipchock, S.V.2    Strobel, S.A.3
  • 16
    • 33748325570 scopus 로고    scopus 로고
    • Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
    • Klein D.J., and Ferre-D'Amare A.R. Structural basis of glmS ribozyme activation by glucosamine-6-phosphate. Science 313 (2006) 1752-1756
    • (2006) Science , vol.313 , pp. 1752-1756
    • Klein, D.J.1    Ferre-D'Amare, A.R.2
  • 17
    • 33745744196 scopus 로고    scopus 로고
    • Molecular basis for temperature sensing by an RNA thermometer
    • Chowdhury S., Maris C., Allain F.H., and Narberhaus F. Molecular basis for temperature sensing by an RNA thermometer. EMBO J 25 (2006) 2487-2497
    • (2006) EMBO J , vol.25 , pp. 2487-2497
    • Chowdhury, S.1    Maris, C.2    Allain, F.H.3    Narberhaus, F.4
  • 18
    • 34548253368 scopus 로고    scopus 로고
    • Structure and mechanism of a metal-sensing regulatory RNA
    • The first structure of the natural magnesium-sensing RNA switch.
    • Dann III C.E., Wakeman C.A., Sieling C.L., Baker S.C., Irnov I., and Winkler W.C. Structure and mechanism of a metal-sensing regulatory RNA. Cell 130 (2007) 878-892. The first structure of the natural magnesium-sensing RNA switch.
    • (2007) Cell , vol.130 , pp. 878-892
    • Dann III, C.E.1    Wakeman, C.A.2    Sieling, C.L.3    Baker, S.C.4    Irnov, I.5    Winkler, W.C.6
  • 23
    • 0035976708 scopus 로고    scopus 로고
    • Interaction of the Bacillus stearothermophilus ribosomal protein S15 with its 5′-translational operator mRNA
    • Scott L.G., and Williamson J.R. Interaction of the Bacillus stearothermophilus ribosomal protein S15 with its 5′-translational operator mRNA. J Mol Biol 314 (2001) 413-422
    • (2001) J Mol Biol , vol.314 , pp. 413-422
    • Scott, L.G.1    Williamson, J.R.2
  • 24
    • 0037447159 scopus 로고    scopus 로고
    • Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA
    • Serganov A., Polonskaia A., Ehresmann B., Ehresmann C., and Patel D.J. Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA. EMBO J 22 (2003) 1898-1908
    • (2003) EMBO J , vol.22 , pp. 1898-1908
    • Serganov, A.1    Polonskaia, A.2    Ehresmann, B.3    Ehresmann, C.4    Patel, D.J.5
  • 25
    • 0028838032 scopus 로고
    • Molecular dissection of the pseudoknot governing the translational regulation of Escherichia coli ribosomal protein S15
    • Philippe C., Benard L., Portier C., Westhof E., Ehresmann B., and Ehresmann C. Molecular dissection of the pseudoknot governing the translational regulation of Escherichia coli ribosomal protein S15. Nucleic Acids Res 23 (1995) 18-28
    • (1995) Nucleic Acids Res , vol.23 , pp. 18-28
    • Philippe, C.1    Benard, L.2    Portier, C.3    Westhof, E.4    Ehresmann, B.5    Ehresmann, C.6
  • 26
    • 2442595013 scopus 로고    scopus 로고
    • Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation
    • Mathy N., Pellegrini O., Serganov A., Patel D.J., Ehresmann C., and Portier C. Specific recognition of rpsO mRNA and 16S rRNA by Escherichia coli ribosomal protein S15 relies on both mimicry and site differentiation. Mol Microbiol 52 (2004) 661-675
    • (2004) Mol Microbiol , vol.52 , pp. 661-675
    • Mathy, N.1    Pellegrini, O.2    Serganov, A.3    Patel, D.J.4    Ehresmann, C.5    Portier, C.6
  • 27
    • 0036077848 scopus 로고    scopus 로고
    • Do mRNA and rRNA binding sites of E.coli ribosomal protein S15 share common structural determinants?
    • Serganov A., Ennifar E., Portier C., Ehresmann B., and Ehresmann C. Do mRNA and rRNA binding sites of E.coli ribosomal protein S15 share common structural determinants?. J Mol Biol 320 (2002) 963-978
    • (2002) J Mol Biol , vol.320 , pp. 963-978
    • Serganov, A.1    Ennifar, E.2    Portier, C.3    Ehresmann, B.4    Ehresmann, C.5
  • 28
    • 0027288848 scopus 로고
    • Ribosomal protein S15 from Escherichia coli modulates its own translation by trapping the ribosome on the mRNA initiation loading site
    • Philippe C., Eyermann F., Benard L., Portier C., Ehresmann B., and Ehresmann C. Ribosomal protein S15 from Escherichia coli modulates its own translation by trapping the ribosome on the mRNA initiation loading site. Proc Natl Acad Sci U S A 90 (1993) 4394-4398
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 4394-4398
    • Philippe, C.1    Eyermann, F.2    Benard, L.3    Portier, C.4    Ehresmann, B.5    Ehresmann, C.6
  • 29
    • 34548788950 scopus 로고    scopus 로고
    • Structured mRNAs regulate translation initiation by binding to the platform of the ribosome
    • Cryo-EM structure of the S15-mRNA complex bound to the ribosome, explaining entrapment mechanism of translational control.
    • Marzi S., Myasnikov A.G., Serganov A., Ehresmann C., Romby P., Yusupov M., and Klaholz B.P. Structured mRNAs regulate translation initiation by binding to the platform of the ribosome. Cell 130 (2007) 1019-1031. Cryo-EM structure of the S15-mRNA complex bound to the ribosome, explaining entrapment mechanism of translational control.
    • (2007) Cell , vol.130 , pp. 1019-1031
    • Marzi, S.1    Myasnikov, A.G.2    Serganov, A.3    Ehresmann, C.4    Romby, P.5    Yusupov, M.6    Klaholz, B.P.7
  • 30
    • 33845865301 scopus 로고    scopus 로고
    • Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA
    • This structure uncovers details of the specific IRP-1-IRE recognition and demonstrates large conformational changes in the protein structure upon RNA binding.
    • Walden W.E., Selezneva A.I., Dupuy J., Volbeda A., Fontecilla-Camps J.C., Theil E.C., and Volz K. Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science 314 (2006) 1903-1908. This structure uncovers details of the specific IRP-1-IRE recognition and demonstrates large conformational changes in the protein structure upon RNA binding.
    • (2006) Science , vol.314 , pp. 1903-1908
    • Walden, W.E.1    Selezneva, A.I.2    Dupuy, J.3    Volbeda, A.4    Fontecilla-Camps, J.C.5    Theil, E.C.6    Volz, K.7
  • 32
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., and Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289 (2000) 905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 33
    • 0003695480 scopus 로고    scopus 로고
    • Transfer RNA recognition by aminoacyl-tRNA synthetases
    • Beuning P.J., and Musier-Forsyth K. Transfer RNA recognition by aminoacyl-tRNA synthetases. Biopolymers 52 (1999) 1-28
    • (1999) Biopolymers , vol.52 , pp. 1-28
    • Beuning, P.J.1    Musier-Forsyth, K.2
  • 34
    • 34548511320 scopus 로고    scopus 로고
    • Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA
    • This study describes unusual binding of the protein dimer with Shine-Dalgarno sequence.
    • Schubert M., Lapouge K., Duss O., Oberstrass F.C., Jelesarov I., Haas D., and Allain F.H. Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA. Nat Struct Mol Biol 14 (2007) 807-813. This study describes unusual binding of the protein dimer with Shine-Dalgarno sequence.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 807-813
    • Schubert, M.1    Lapouge, K.2    Duss, O.3    Oberstrass, F.C.4    Jelesarov, I.5    Haas, D.6    Allain, F.H.7
  • 35
    • 34047142206 scopus 로고    scopus 로고
    • The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
    • In this structure, sequence-specific RNA-recognition by RRM is complemented by shape-specific binding of β-hairpin to the major groove of RNA.
    • Skrisovska L., Bourgeois C.F., Stefl R., Grellscheid S.N., Kister L., Wenter P., Elliott D.J., Stevenin J., and Allain F.H. The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction. EMBO Rep 8 (2007) 372-379. In this structure, sequence-specific RNA-recognition by RRM is complemented by shape-specific binding of β-hairpin to the major groove of RNA.
    • (2007) EMBO Rep , vol.8 , pp. 372-379
    • Skrisovska, L.1    Bourgeois, C.F.2    Stefl, R.3    Grellscheid, S.N.4    Kister, L.5    Wenter, P.6    Elliott, D.J.7    Stevenin, J.8    Allain, F.H.9
  • 36
    • 4444367493 scopus 로고    scopus 로고
    • Determination and augmentation of RNA sequence specificity of the Nova K-homology domains
    • Musunuru K., and Darnell R.B. Determination and augmentation of RNA sequence specificity of the Nova K-homology domains. Nucleic Acids Res 32 (2004) 4852-4861
    • (2004) Nucleic Acids Res , vol.32 , pp. 4852-4861
    • Musunuru, K.1    Darnell, R.B.2
  • 37
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome
    • Lewis H.A., Musunuru K., Jensen K.B., Edo C., Chen H., Darnell R.B., and Burley S.K. Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome. Cell 100 (2000) 323-332
    • (2000) Cell , vol.100 , pp. 323-332
    • Lewis, H.A.1    Musunuru, K.2    Jensen, K.B.3    Edo, C.4    Chen, H.5    Darnell, R.B.6    Burley, S.K.7
  • 39
    • 34248181181 scopus 로고    scopus 로고
    • Structural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelB
    • Ose T., Soler N., Rasubala L., Kuroki K., Kohda D., Fourmy D., Yoshizawa S., and Maenaka K. Structural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelB. Structure 15 (2007) 577-586
    • (2007) Structure , vol.15 , pp. 577-586
    • Ose, T.1    Soler, N.2    Rasubala, L.3    Kuroki, K.4    Kohda, D.5    Fourmy, D.6    Yoshizawa, S.7    Maenaka, K.8
  • 41
    • 0032786907 scopus 로고    scopus 로고
    • Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro
    • Smibert C.A., Lie Y.S., Shillinglaw W., Henzel W.J., and Macdonald P.M. Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro. RNA 5 (1999) 1535-1547
    • (1999) RNA , vol.5 , pp. 1535-1547
    • Smibert, C.A.1    Lie, Y.S.2    Shillinglaw, W.3    Henzel, W.J.4    Macdonald, P.M.5
  • 44
    • 32244447225 scopus 로고    scopus 로고
    • Shape-specific recognition in the structure of the Vts1p SAM domain with RNA
    • See annotation to reference [42•]
    • Oberstrass F.C., Lee A., Stefl R., Janis M., Chanfreau G., and Allain F.H. Shape-specific recognition in the structure of the Vts1p SAM domain with RNA. Nat Struct Mol Biol 13 (2006) 160-167. See annotation to reference [42•]
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 160-167
    • Oberstrass, F.C.1    Lee, A.2    Stefl, R.3    Janis, M.4    Chanfreau, G.5    Allain, F.H.6
  • 45
    • 30444446153 scopus 로고    scopus 로고
    • Molecular basis of RNA recognition by the human alternative splicing factor Fox-1
    • This study has suggested a novel determinant of RNA recognition adjacent to canonical surface of RRM domain.
    • Auweter S.D., Fasan R., Reymond L., Underwood J.G., Black D.L., Pitsch S., and Allain F.H. Molecular basis of RNA recognition by the human alternative splicing factor Fox-1. EMBO J 25 (2006) 163-173. This study has suggested a novel determinant of RNA recognition adjacent to canonical surface of RRM domain.
    • (2006) EMBO J , vol.25 , pp. 163-173
    • Auweter, S.D.1    Fasan, R.2    Reymond, L.3    Underwood, J.G.4    Black, D.L.5    Pitsch, S.6    Allain, F.H.7
  • 46
    • 33750481849 scopus 로고    scopus 로고
    • Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8
    • A demonstration of a semi-sequence-specific mode of the RRM-RNA binding.
    • Hargous Y., Hautbergue G.M., Tintaru A.M., Skrisovska L., Golovanov A.P., Stevenin J., Lian L.Y., Wilson S.A., and Allain F.H. Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8. EMBO J 25 (2006) 5126-5137. A demonstration of a semi-sequence-specific mode of the RRM-RNA binding.
    • (2006) EMBO J , vol.25 , pp. 5126-5137
    • Hargous, Y.1    Hautbergue, G.M.2    Tintaru, A.M.3    Skrisovska, L.4    Golovanov, A.P.5    Stevenin, J.6    Lian, L.Y.7    Wilson, S.A.8    Allain, F.H.9
  • 47
    • 33745499067 scopus 로고    scopus 로고
    • Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65
    • This paper provides structural insights into recognition of semi-conserved polypyrimidine sequences.
    • Sickmier E.A., Frato K.E., Shen H., Paranawithana S.R., Green M.R., and Kielkopf C.L. Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65. Mol Cell 23 (2006) 49-59. This paper provides structural insights into recognition of semi-conserved polypyrimidine sequences.
    • (2006) Mol Cell , vol.23 , pp. 49-59
    • Sickmier, E.A.1    Frato, K.E.2    Shen, H.3    Paranawithana, S.R.4    Green, M.R.5    Kielkopf, C.L.6
  • 49
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang X., and Hall T.M. Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat Struct Biol 8 (2001) 141-145
    • (2001) Nat Struct Biol , vol.8 , pp. 141-145
    • Wang, X.1    Hall, T.M.2
  • 51
    • 33746296753 scopus 로고    scopus 로고
    • Grabbing the message: structural basis of mRNA 3′UTR recognition by Hrp1
    • This work rationalizes specific binding of AUAUAU sequence by RRM and further validates importance of the non-canonical RRM determinant for RNA binding.
    • Perez-Canadillas J.M. Grabbing the message: structural basis of mRNA 3′UTR recognition by Hrp1. EMBO J 25 (2006) 3167-3178. This work rationalizes specific binding of AUAUAU sequence by RRM and further validates importance of the non-canonical RRM determinant for RNA binding.
    • (2006) EMBO J , vol.25 , pp. 3167-3178
    • Perez-Canadillas, J.M.1
  • 53
    • 34250887075 scopus 로고    scopus 로고
    • X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2
    • Du Z., Lee J.K., Fenn S., Tjhen R., Stroud R.M., and James T.L. X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2. RNA 13 (2007) 1043-1051
    • (2007) RNA , vol.13 , pp. 1043-1051
    • Du, Z.1    Lee, J.K.2    Fenn, S.3    Tjhen, R.4    Stroud, R.M.5    James, T.L.6
  • 55
    • 33750477997 scopus 로고    scopus 로고
    • Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor
    • Skordalakes E., and Berger J.M. Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell 127 (2006) 553-564
    • (2006) Cell , vol.127 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 56
  • 58
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA
    • Bono F., Ebert J., Lorentzen E., and Conti E. The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 126 (2006) 713-725
    • (2006) Cell , vol.126 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 59
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T., Nureki O., Nakamura A., Kobayashi S., and Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125 (2006) 287-300
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 60
    • 31044448524 scopus 로고    scopus 로고
    • Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
    • Gan J., Tropea J.E., Austin B.P., Court D.L., Waugh D.S., and Ji X. Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell 124 (2006) 355-366
    • (2006) Cell , vol.124 , pp. 355-366
    • Gan, J.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.