메뉴 건너뛰기




Volumn 42, Issue 30, 2003, Pages 8966-8975

Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMICAL ENGINEERING; INITIATORS (CHEMICAL); MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; PROTEINS; SOLUTIONS;

EID: 0042666838     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034506g     Document Type: Article
Times cited : (22)

References (68)
  • 1
    • 0024998982 scopus 로고
    • Cloning and expression of eukaryotic initiation factor-4b Cdna-sequence determination identifies a common RNA recognition motif
    • Milburn, S. C., Hershey, J. W. B., Davies, M. V., Kelleher, K., and Kaufman, R. J. (1990) Cloning and Expression of Eukaryotic Initiation Factor-4b Cdna-Sequence Determination Identifies a Common Rna Recognition Motif, EMBO J. 9, 2783-2790.
    • (1990) EMBO J. , vol.9 , pp. 2783-2790
    • Milburn, S.C.1    Hershey, J.W.B.2    Davies, M.V.3    Kelleher, K.4    Kaufman, R.J.5
  • 2
    • 0018095166 scopus 로고
    • The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes
    • Benne, R., and Hershey, J. W. B. (1978) The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes, J. Biol. Chem. 253, 3078-3087.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3078-3087
    • Benne, R.1    Hershey, J.W.B.2
  • 3
    • 0017707116 scopus 로고
    • Initiation on mammalian protein synthesis: The assembly of the initiation complex with purified initiation factors
    • Trachsel, H., Erni, B., Schreier, M. H., and Staehelin, T. (1977) Initiation on mammalian protein synthesis: The assembly of the initiation complex with purified initiation factors, J. Mol. Biol. 116, 755-767.
    • (1977) J. Mol. Biol. , vol.116 , pp. 755-767
    • Trachsel, H.1    Erni, B.2    Schreier, M.H.3    Staehelin, T.4
  • 4
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen, F., Edery, I., Meerovitch, K., Dever, T. E., Merrick, W. C., and Sonenberg, N. (1990) Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F, Mol. Cell. Biol. 10, 1134-1344.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1134-1344
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 5
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation
    • Pause, A., Méthot, N., Svitkin, Y., Merrick, W. C., and Sonenberg, N. (1994) Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation, EMBO J. 13, 1205-1215.
    • (1994) EMBO J. , vol.13 , pp. 1205-1215
    • Pause, A.1    Méthot, N.2    Svitkin, Y.3    Merrick, W.C.4    Sonenberg, N.5
  • 6
    • 0029805730 scopus 로고    scopus 로고
    • In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: The role of the RNA recognition motif
    • Methot, N., Pickett, G., Keene, J. D., and Sonenberg, N. (1996) In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: The role of the RNA recognition motif, RNA 2, 38-50.
    • (1996) RNA , vol.2 , pp. 38-50
    • Methot, N.1    Pickett, G.2    Keene, J.D.3    Sonenberg, N.4
  • 7
    • 0028568642 scopus 로고
    • Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein
    • Naranda, T., MacMillan, S. E., and Hershey, J. W. (1994) Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein, J. Biol. Chem. 269, 32286-32292.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32286-32292
    • Naranda, T.1    MacMillan, S.E.2    Hershey, J.W.3
  • 8
    • 0028331455 scopus 로고
    • The translation initiation factor-Eif-4b contains an Rna-binding region that is distinct and independent from its ribonucleoprotein consensus sequence
    • Methot, N., Pause, A., Hershey, J. W. B., and Sonenberg, N. (1994) The Translation Initiation Factor-Eif-4b Contains an Rna-Binding Region That Is Distinct and Independent from Its Ribonucleoprotein Consensus Sequence, Mol. Cell. Biol. 14, 2307-2316.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2307-2316
    • Methot, N.1    Pause, A.2    Hershey, J.W.B.3    Sonenberg, N.4
  • 9
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3
    • Methot, N., Song, M. S., and Sonenberg, N. (1996) A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3, Mol. Cell. Biol. 16, 5328-5334.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5328-5334
    • Methot, N.1    Song, M.S.2    Sonenberg, N.3
  • 10
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • Le, H., Tanguay, R. L., Balasta, M. L., Wei, C. C., Browning, K. S., Metz, A. M., Goss, D. J., and Gallie, D. R. (1997) Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity, J. Biol. Chem. 272, 16247-16255.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16247-16255
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.C.4    Browning, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 11
    • 0035968267 scopus 로고    scopus 로고
    • Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages
    • Bushell, M., Wood, W., Carpenter, G., Pain, V. M., Morley, S. J., and Clemens, M. J. (2001) Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages, J. Biol. Chem. 276, 23922-23928.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23922-23928
    • Bushell, M.1    Wood, W.2    Carpenter, G.3    Pain, V.M.4    Morley, S.J.5    Clemens, M.J.6
  • 12
    • 0034625396 scopus 로고    scopus 로고
    • Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4F
    • Bi, X., and Goss, D. J. (2000) Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4F, J. Biol. Chem. 275, 17740-17746.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17740-17746
    • Bi, X.1    Goss, D.J.2
  • 13
    • 0034625414 scopus 로고    scopus 로고
    • The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B
    • Le, H., Browning, K. S., and Gallie, D. R. (2000) The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B, J. Biol. Chem. 275, 17452-17462.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17452-17462
    • Le, H.1    Browning, K.S.2    Gallie, D.R.3
  • 14
    • 0036298692 scopus 로고    scopus 로고
    • Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization
    • Groft, C. M., and Burley, S. K. (2002) Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization, Mol. Cell 9, 1273-1283.
    • (2002) Mol. Cell , vol.9 , pp. 1273-1283
    • Groft, C.M.1    Burley, S.K.2
  • 15
    • 0032990430 scopus 로고    scopus 로고
    • Interaction of eukaryotic initiation factor eIF4B with the internal ribosome entry site of foot-and-mouth disease virus is independent of the polypyrimidine tract-binding protein
    • Rust, R. C., Ochs, K., Meyer, K., Beck, E., and Niepmann, M. (1999) Interaction of eukaryotic initiation factor eIF4B with the internal ribosome entry site of foot-and-mouth disease virus is independent of the polypyrimidine tract-binding protein, J. Virol. 73, 6111-6113.
    • (1999) J. Virol. , vol.73 , pp. 6111-6113
    • Rust, R.C.1    Ochs, K.2    Meyer, K.3    Beck, E.4    Niepmann, M.5
  • 16
    • 0036173634 scopus 로고    scopus 로고
    • Interaction of translation initiation factor eIF4B with the poliovirus internal ribosome entry site
    • Ochs, K., Saleh, L., Bassili, G., Sonntag, V. H., Zeller, A., and Niepmann, M. (2002) Interaction of translation initiation factor eIF4B with the poliovirus internal ribosome entry site, J. Virol. 76, 2113-2122.
    • (2002) J. Virol. , vol.76 , pp. 2113-2122
    • Ochs, K.1    Saleh, L.2    Bassili, G.3    Sonntag, V.H.4    Zeller, A.5    Niepmann, M.6
  • 17
    • 0032865671 scopus 로고    scopus 로고
    • Translation initiation factor eIF4B interacts with a picomavirus internal ribosome entry site in both 48S and 80S initiation complexes independently of initiator AUG location
    • Ochs, K., Rust, R. C., and Niepmann, M. (1999) Translation initiation factor eIF4B interacts with a picomavirus internal ribosome entry site in both 48S and 80S initiation complexes independently of initiator AUG location, J. Virol. 73, 7505-7514.
    • (1999) J. Virol. , vol.73 , pp. 7505-7514
    • Ochs, K.1    Rust, R.C.2    Niepmann, M.3
  • 18
    • 0033623486 scopus 로고    scopus 로고
    • Interaction of the eIF4G initiation factor with the aphthovirus IRES is essential for internal translation initiation in vivo
    • Lopez de Quinto, S., and Martinez-Salas, E. (2000) Interaction of the eIF4G initiation factor with the aphthovirus IRES is essential for internal translation initiation in vivo, RNA 6, 1380-1392.
    • (2000) RNA , vol.6 , pp. 1380-1392
    • Lopez de Quinto, S.1    Martinez-Salas, E.2
  • 19
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • Pestova, T. V., Hellen, C. U. T., and Shatsky, I. N. (1996) Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry, Mol. Cell. Biol. 16, 6859-6869.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.T.2    Shatsky, I.N.3
  • 20
    • 0025761656 scopus 로고
    • RNA recognition: Towards identifying determinants of specificity
    • Kenan, D. J., Query, C. C., and Keene, J. D. (1991) RNA recognition: towards identifying determinants of specificity, Trends Biochem. Sci. 16, 214-220.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 214-220
    • Kenan, D.J.1    Query, C.C.2    Keene, J.D.3
  • 21
    • 0342927495 scopus 로고    scopus 로고
    • Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold
    • Conte, M. R., Grune, T., Ghuman, J., Kelly, G., Ladas, A., Matthews, S., and Curry, S. (2000) Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold, EMBO J. 19, 3132-3141.
    • (2000) EMBO J. , vol.19 , pp. 3132-3141
    • Conte, M.R.1    Grune, T.2    Ghuman, J.3    Kelly, G.4    Ladas, A.5    Matthews, S.6    Curry, S.7
  • 22
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domains of the U1 small nuclear ribonucleoprotein A
    • Nagai, K., Oubridge, C., Jessen, T. H., Li, J., and Evans, P. R. (1990) Crystal structure of the RNA-binding domains of the U1 small nuclear ribonucleoprotein A, Nature 348, 515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 23
    • 0028004607 scopus 로고
    • Crystal structure of the RNA-binding domains of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P. R., Teo, C.-H., and Nagai, K. (1995) Crystal structure of the RNA-binding domains of the U1A spliceosomal protein complexed with an RNA hairpin, Nature 372, 432-438.
    • (1995) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.-H.4    Nagai, K.5
  • 24
    • 0034070741 scopus 로고    scopus 로고
    • The NMR structure of the 38 kDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein
    • Varani, L., Gunderson, S. I., Mattaj, I. W., Kay, L. E., Neuhaus, D., and Varani, G. (2000) The NMR structure of the 38 kDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein, Nat. Struct. Biol. 7, 329-335.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 329-335
    • Varani, L.1    Gunderson, S.I.2    Mattaj, I.W.3    Kay, L.E.4    Neuhaus, D.5    Varani, G.6
  • 25
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang, X., and Tanaka Hall, T. M. (2001) Structural basis for recognition of AU-rich element RNA by the HuD protein, Nat. Struct. Biol. 8, 141-145.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 141-145
    • Wang, X.1    Tanaka Hall, T.M.2
  • 26
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo, R. C., Bonanno, J. B., Sonenberg, N., and Burley, S. K. (1999) Recognition of polyadenylate RNA by the poly(A)-binding protein, Cell 98, 835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 27
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J. Z., Hayashi, M. K., Zhang, Y., Manche, L., Krainer, A. R., and Xu, R. M. (1999) Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA, Genes Dev. 13, 1102-1115.
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.Z.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 28
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • Allain, F. H., Bouvet, P., Dieckmann, T., and Feigon, J. (2000) Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin, EMBO J. 19, 6870-6881.
    • (2000) EMBO J. , vol.19 , pp. 6870-6881
    • Allain, F.H.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 29
    • 0033560881 scopus 로고    scopus 로고
    • Structural basis for recognition of the tra mRNA precursor by the sex-lethal protein
    • Handa, N., Nureki, O., Kurimoto, K., Kim, I., Sakamoto, H., Shimura, Y., Muto, Y., and Yokoyama, S. (1999) Structural basis for recognition of the tra mRNA precursor by the sex-lethal protein, Nature 398, 579-585.
    • (1999) Nature , vol.398 , pp. 579-585
    • Handa, N.1    Nureki, O.2    Kurimoto, K.3    Kim, I.4    Sakamoto, H.5    Shimura, Y.6    Muto, Y.7    Yokoyama, S.8
  • 30
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B′′-U2A′ protein complex bound to a fragment of U2 small nuclear RNA
    • Price, S. R., Evens, P. R., and Nagai, K. (1998) Crystal structure of the spliceosomal U2B′′-U2A′ protein complex bound to a fragment of U2 small nuclear RNA, Nature 394, 645-650.
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.R.1    Evens, P.R.2    Nagai, K.3
  • 31
    • 0028215301 scopus 로고
    • RNA binding specificity of hnRNP A1: Significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing
    • Burd, C. G., and Dreyfuss, G. (1994) RNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing, EMBO J. 13, 1197-204.
    • (1994) EMBO J. , vol.13 , pp. 1197-1204
    • Burd, C.G.1    Dreyfuss, G.2
  • 32
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek, S., and Bax, A. (1992) An Efficient Experiment for Sequential Backbone Assignment of Medium-Sized Isotopically Enriched Proteins, J. Magn. Reson. 99, 201-207.
    • (1992) J. Magn. Reson. , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 33
    • 44049117010 scopus 로고
    • Improved 3d triple-resonance NMR techniques applied to a 31-Kda protein
    • Grzesiek, S., and Bax, A. (1992) Improved 3d Triple-Resonance NMR Techniques Applied to a 31-Kda Protein, J. Magn. Reson. 96, 432-440.
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 34
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and Kay, L. E. (1994) Gradient-Enhanced Triple-Resonance 3-Dimensional NMR Experiments with Improved Sensitivity, J. Magn. Reson., Ser. B 103, 203-216.
    • (1994) J. Magn. Reson., Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 35
    • 34447505016 scopus 로고
    • Enhanced-sensitivity triple-resonance spectroscopy with minimal H2o saturation
    • Kay, L. E., Xu, G. Y., and Yamazaki, T. (1994) Enhanced-Sensitivity Triple-Resonance Spectroscopy with Minimal H2o Saturation, J. Magn. Reson., Ser. A 109, 129-133.
    • (1994) J. Magn. Reson., Ser. A , vol.109 , pp. 129-133
    • Kay, L.E.1    Xu, G.Y.2    Yamazaki, T.3
  • 36
    • 44949288628 scopus 로고
    • H-1-H-1 correlation via isotropic mixing of C-13 magnetization, a new 3-dimensional approach for assigning H-1 and C-13 spectra of C-13-enriched proteins
    • Bax, A., Clore, G. M., and Gronenborn, A. M. (1990) H-1-H-1 Correlation Via Isotropic Mixing of C-13 Magnetization, a New 3-Dimensional Approach for Assigning H-1 and C-13 Spectra of C-13-Enriched Proteins, J. Magn. Reson. 88, 425-431.
    • (1990) J. Magn. Reson. , vol.88 , pp. 425-431
    • Bax, A.1    Clore, G.M.2    Gronenborn, A.M.3
  • 37
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Ruckert, M., and Otting, G. (2000) Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments, J. Am. Chem. Soc. 122, 7793-7797.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 38
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger, M., Delaglio, F., and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra, J. Magn. Reson. 131, 373-378.
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 39
    • 0033919516 scopus 로고    scopus 로고
    • A set of HNCO-based experiments for measurement of residual dipolar couplings in N-15, C-13, (H-2)-labeled proteins
    • Permi, P., Rosevear, P. R., and Annila, A. (2000) A set of HNCO-based experiments for measurement of residual dipolar couplings in N-15, C-13, (H-2)-labeled proteins, J. Biomol. NMR 17, 43-54.
    • (2000) J. Biomol. NMR , vol.17 , pp. 43-54
    • Permi, P.1    Rosevear, P.R.2    Annila, A.3
  • 40
    • 34249765651 scopus 로고
    • NMR view - A computer-program for the visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R. A. (1994) NMR View - a Computer-Program for the Visualization and Analysis of NMR Data, J. Biomol. NMR 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 41
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 43
    • 0029397360 scopus 로고
    • Direct evidence that polypyrimidine tract binding protein (PTB) is essential for internal initiation of translation of encephalomyocarditis virus RNA
    • Kaminski, A., Hunt, S. L., Patton, J. G., and Jackson, R. J. (1995) Direct evidence that polypyrimidine tract binding protein (PTB) is essential for internal initiation of translation of encephalomyocarditis virus RNA, RNA 1, 928-938.
    • (1995) RNA , vol.1 , pp. 928-938
    • Kaminski, A.1    Hunt, S.L.2    Patton, J.G.3    Jackson, R.J.4
  • 44
    • 0037079692 scopus 로고    scopus 로고
    • Chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein
    • Yuan, X., Davydova, N., Conte, M. R., Curry, S., and Matthews, S. (2002) Chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein, Nucleic Acids Res. 30, 456-462.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 456-462
    • Yuan, X.1    Davydova, N.2    Conte, M.R.3    Curry, S.4    Matthews, S.5
  • 45
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules 1. Theory and range of validity
    • Lipari, G., and Szabo, A. (1982) Model-Free Approach to the Interpretation of Nuclear Magnetic Resonance Relaxation in Macromolecules 1. Theory and Range of Validity, J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 46
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules 2. Analysis of experimental results
    • Lipari, G., and Szabo, A. (1982) Model-Free Approach to the Interpretation of Nuclear Magnetic Resonance Relaxation in Macromolecules 2. Analysis of Experimental Results, J. Am. Chem. Soc. 104, 4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 47
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia-coli ribonuclease Hi-correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G. (1995) Backbone Dynamics of Escherichia-Coli Ribonuclease Hi-Correlations with Structure and Function in an Active Enzyme, J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 48
    • 0027440362 scopus 로고
    • Protein-structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993) Protein-Structure Comparison by Alignment of Distance Matrices, J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 49
    • 0028871926 scopus 로고
    • Dali - A network tool for protein-structure comparison
    • Holm, L., and Sander, C. (1995) Dali - a Network Tool for Protein-Structure Comparison, Trends Biochem. Sci. 20, 478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 50
    • 0034100762 scopus 로고    scopus 로고
    • Eukaryotic translation initiation: There are (at least) two sides to every story
    • Sachs, A. B., and Varani, G. (2000) Eukaryotic translation initiation: there are (at least) two sides to every story, Nat. Struct. Biol. 7, 356-361.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 356-361
    • Sachs, A.B.1    Varani, G.2
  • 51
    • 0029978824 scopus 로고    scopus 로고
    • Solution structure of the N-terminal RNP domain of U1A protein: The role of C-terminal residues in structure stability and RNA binding
    • Avis, J. M., Allain, F. H. T., Howe, P. W. A., Varani, G., Nagai, K., and Neuhaus, D. (1996) Solution structure of the N-terminal RNP domain of U1A protein: The role of C-terminal residues in structure stability and RNA binding, J. Mol. Biol. 257, 398-411.
    • (1996) J. Mol. Biol. , vol.257 , pp. 398-411
    • Avis, J.M.1    Allain, F.H.T.2    Howe, P.W.A.3    Varani, G.4    Nagai, K.5    Neuhaus, D.6
  • 52
    • 0031565722 scopus 로고    scopus 로고
    • A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal
    • Inoue, M., Muto, Y., Sakamoto, H., Kigawa, T., Takio, K., Shimura, Y., and Yokoyama, S. (1997) A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal, J. Mol. Biol. 272, 82-94.
    • (1997) J. Mol. Biol. , vol.272 , pp. 82-94
    • Inoue, M.1    Muto, Y.2    Sakamoto, H.3    Kigawa, T.4    Takio, K.5    Shimura, Y.6    Yokoyama, S.7
  • 53
    • 0033575718 scopus 로고    scopus 로고
    • Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65))
    • Ito, T., Muto, Y., Green, M. R., and Yokoyama, S. (1999) Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65)), EMBO J. 18, 4523-4534.
    • (1999) EMBO J. , vol.18 , pp. 4523-4534
    • Ito, T.1    Muto, Y.2    Green, M.R.3    Yokoyama, S.4
  • 54
    • 0033605940 scopus 로고    scopus 로고
    • Structure, backbone dynamics and interactions with RNA of the C-terminal RNA-binding domain of a mouse neural RNA-binding protein, Musashi1
    • Nagata, T., Kanno, R., Kurihara, Y., Uesugi, S., Imai, T., Sakakibara, S., Okano, H., and Katahira, M. (1999) Structure, backbone dynamics and interactions with RNA of the C-terminal RNA-binding domain of a mouse neural RNA-binding protein, Musashi1, J. Mol. Biol. 287, 315-330.
    • (1999) J. Mol. Biol. , vol.287 , pp. 315-330
    • Nagata, T.1    Kanno, R.2    Kurihara, Y.3    Uesugi, S.4    Imai, T.5    Sakakibara, S.6    Okano, H.7    Katahira, M.8
  • 56
    • 0033544894 scopus 로고    scopus 로고
    • Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H
    • Richter, N. J., Rogers, G. W., Jr., Hensold, J. O., and Merrick, W. C. (1999) Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H, J. Biol. Chem. 274, 35415-35424.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35415-35424
    • Richter, N.J.1    Rogers G.W., Jr.2    Hensold, J.O.3    Merrick, W.C.4
  • 57
    • 0032571398 scopus 로고    scopus 로고
    • Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H
    • Richter-Cook, N. J., Dever, T. E., Hensold, J. O., and Merrick, W. C. (1998) Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H, J. Biol. Chem. 273, 7579-7587.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7579-7587
    • Richter-Cook, N.J.1    Dever, T.E.2    Hensold, J.O.3    Merrick, W.C.4
  • 58
    • 0030755124 scopus 로고    scopus 로고
    • Structural basis of the RNA-binding specificity of human U1A protein
    • Allain, F. H., Howe, P. W., Neuhaus, D., and Varani, G. (1997) Structural basis of the RNA-binding specificity of human U1A protein, EMBO J. 16, 5764-5772.
    • (1997) EMBO J. , vol.16 , pp. 5764-5772
    • Allain, F.H.1    Howe, P.W.2    Neuhaus, D.3    Varani, G.4
  • 59
    • 0025127420 scopus 로고
    • Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA
    • Lutz-Freyermuth, C., Query, C. C., and Keene, J. D. (1990) Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA, Proc. Natl. Acad. Sci. U.S.A. 87, 6393-6397.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6393-6397
    • Lutz-Freyermuth, C.1    Query, C.C.2    Keene, J.D.3
  • 60
    • 0027992089 scopus 로고
    • The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein-C proteins
    • Gorlach, M., Burd, C. G., and Dreyfuss, G. (1994) The Determinants of Rna-Binding Specificity of the Heterogeneous Nuclear Ribonucleoprotein-C Proteins, J. Biol. Chem. 269, 23074-23078.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23074-23078
    • Gorlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 61
    • 0024603237 scopus 로고
    • A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein
    • Query, C. C., Bentley, R. C., and Keene, J. D. (1989) A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein, Cell 57, 89-101.
    • (1989) Cell , vol.57 , pp. 89-101
    • Query, C.C.1    Bentley, R.C.2    Keene, J.D.3
  • 62
    • 0024851833 scopus 로고
    • Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA
    • Scherly, D., Boelens, W., van Venrooij, W. J., Dathan, N. A., Hamm, J., and Mattaj, I. W. (1989) Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA, EMBO J. 8, 4163-4170.
    • (1989) EMBO J. , vol.8 , pp. 4163-4170
    • Scherly, D.1    Boelens, W.2    Van Venrooij, W.J.3    Dathan, N.A.4    Hamm, J.5    Mattaj, I.W.6
  • 63
    • 0000178351 scopus 로고    scopus 로고
    • A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity
    • Simpson, P. J., Bolam, D. N., Cooper, A., Ciruela, A., Hazlewood, G. P., Gilbert, H. J., and Williamson, M. P. (1999) A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity, Structure 7, 853-864.
    • (1999) Structure , vol.7 , pp. 853-864
    • Simpson, P.J.1    Bolam, D.N.2    Cooper, A.3    Ciruela, A.4    Hazlewood, G.P.5    Gilbert, H.J.6    Williamson, M.P.7
  • 64
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and Thomton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thomton, J.M.5
  • 65
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 66
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced colouring capabilities
    • Esnouf, R. (1997) An extensively modified version of Molscript that includes greatly enhanced colouring capabilities, J. Mol. Graphics 15, 133-138.
    • (1997) J. Mol. Graphics , vol.15 , pp. 133-138
    • Esnouf, R.1
  • 67
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.