메뉴 건너뛰기




Volumn 44, Issue 10, 2005, Pages 3708-3717

NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: Contribution of a β hairpin to RNA binding

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CALORIMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RNA; TITRATION;

EID: 14844355725     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047450e     Document Type: Article
Times cited : (35)

References (62)
  • 1
    • 0033256023 scopus 로고    scopus 로고
    • A short review on the morphology of Trypanosoma cruzi: From 1909 to 1999
    • de Souza, W. (1999) A short review on the morphology of Trypanosoma cruzi: From 1909 to 1999, Mem. Inst. Oswaldo Cruz 94, Suppl. 1, 17-36.
    • (1999) Mem. Inst. Oswaldo Cruz , vol.94 , Issue.1 SUPPL. , pp. 17-36
    • De Souza, W.1
  • 2
    • 0028214539 scopus 로고
    • A common pyrimidine-rich motif governs trans-splicing and polyadenylation of tubulin polycistronic pre-mRNA in trypanosomes
    • Matthews, K. R., Tschudi, C., and Ullu, E. (1994) A common pyrimidine-rich motif governs trans-splicing and polyadenylation of tubulin polycistronic pre-mRNA in trypanosomes, Genes Dev. 8, 491-501.
    • (1994) Genes Dev. , vol.8 , pp. 491-501
    • Matthews, K.R.1    Tschudi, C.2    Ullu, E.3
  • 3
    • 0037090528 scopus 로고    scopus 로고
    • Life without transcriptional control? From fly to man and back again
    • Clayton, C. E. (2002) Life without transcriptional control? From fly to man and back again, EMBO J. 21, 1881-1888.
    • (2002) EMBO J. , vol.21 , pp. 1881-1888
    • Clayton, C.E.1
  • 4
    • 0030949303 scopus 로고    scopus 로고
    • Life and death in the cytoplasm: Messages from the 3′ end
    • Wickens, M., Anderson, P., and Jackson, R. J. (1997) Life and death in the cytoplasm: Messages from the 3′ end, Curr. Opin. Genet. Dev. 7, 220-232.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 220-232
    • Wickens, M.1    Anderson, P.2    Jackson, R.J.3
  • 5
    • 0037384759 scopus 로고    scopus 로고
    • RNA-binding proteins and mRNA turnover in trypanosomes
    • D'Orso, I., De Gaudenzi, J. G., and Frasch, A. C. (2003) RNA-binding proteins and mRNA turnover in trypanosomes, Trends Parasitol. 19, 151-155.
    • (2003) Trends Parasitol. , vol.19 , pp. 151-155
    • D'Orso, I.1    De Gaudenzi, J.G.2    Frasch, A.C.3
  • 6
    • 0000370303 scopus 로고
    • Identification of a common nucleotide sequence in the 3′-untranslated region of mRNA molecules specifying inflammatory mediators
    • Caput, D., Beutler, B., Hartog, K., Thayer, R., Brown-Shimer, S., and Cerami, A. (1986) Identification of a common nucleotide sequence in the 3′-untranslated region of mRNA molecules specifying inflammatory mediators, Proc. Natl. Acad. Sci. U.S.A. 83, 1670-1674.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 1670-1674
    • Caput, D.1    Beutler, B.2    Hartog, K.3    Thayer, R.4    Brown-Shimer, S.5    Cerami, A.6
  • 7
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw, G., and Kamen, R. (1986) A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation, Cell 46, 659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 8
    • 0030867877 scopus 로고    scopus 로고
    • Embryonic lethal abnormal visual RNA-binding proteins involved in growth, differentiation, and posttranscriptional gene expression
    • Antic, D., and Keene, J. D. (1997) Embryonic lethal abnormal visual RNA-binding proteins involved in growth, differentiation, and posttranscriptional gene expression, Am. J. Hum. Genet. 61, 273-278.
    • (1997) Am. J. Hum. Genet. , vol.61 , pp. 273-278
    • Antic, D.1    Keene, J.D.2
  • 9
    • 0030827809 scopus 로고    scopus 로고
    • Sequential expression and role of Hu RNA-binding proteins during neurogenesis
    • Wakamatsu, Y., and Weston, J. A. (1997) Sequential expression and role of Hu RNA-binding proteins during neurogenesis, Development 124, 3449-3460.
    • (1997) Development , vol.124 , pp. 3449-3460
    • Wakamatsu, Y.1    Weston, J.A.2
  • 10
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang, X., and 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    Hall, T.M.2
  • 11
    • 0036212521 scopus 로고    scopus 로고
    • Role of HuD and other RNA-binding proteins in neural development and plasticity
    • Perrone-Bizzozero, N., and Bolognani, F. (2002) Role of HuD and other RNA-binding proteins in neural development and plasticity, J. Neurosci. Res. 68, 121-126.
    • (2002) J. Neurosci. Res. , vol.68 , pp. 121-126
    • Perrone-Bizzozero, N.1    Bolognani, F.2
  • 12
    • 0031004560 scopus 로고    scopus 로고
    • Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation
    • Gunderson, S. I., Vagner, S., Polycarpou-Schwarz, M., and Mattaj, I. W. (1997) Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation, Genes Dev. 11, 761-773.
    • (1997) Genes Dev. , vol.11 , pp. 761-773
    • Gunderson, S.I.1    Vagner, S.2    Polycarpou-Schwarz, M.3    Mattaj, I.W.4
  • 14
    • 0027453554 scopus 로고
    • A complex secondary structure in U1A pre-mRNA that binds two molecules of U1A protein is required for regulation of polyadenylation
    • van Gelder, C. W., Gunderson, S. I., Jansen, E. J., Boelens, W. C., Polycarpou-Schwarz, M., Mattaj, I. W., and van Venrooij, W. J. (1993) A complex secondary structure in U1A pre-mRNA that binds two molecules of U1A protein is required for regulation of polyadenylation, EMBO J. 12, 5191-5200.
    • (1993) EMBO J. , vol.12 , pp. 5191-5200
    • Van Gelder, C.W.1    Gunderson, S.I.2    Jansen, E.J.3    Boelens, W.C.4    Polycarpou-Schwarz, M.5    Mattaj, I.W.6    Van Venrooij, W.J.7
  • 15
    • 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
  • 16
    • 0027523417 scopus 로고
    • Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences
    • Hamilton, B. J., Nagy, E., Malter, J. S., Arrick, B. A., and Rigby, W. F. (1993) Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences, J. Biol. Chem. 268, 8881-8887.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8881-8887
    • Hamilton, B.J.1    Nagy, E.2    Malter, J.S.3    Arrick, B.A.4    Rigby, W.F.5
  • 17
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J., 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.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 18
    • 0033951279 scopus 로고    scopus 로고
    • Single-stranded-RNA binding proteins
    • Antson, A. A. (2000) Single-stranded-RNA binding proteins, Curr. Opin. Struct. Biol. 10, 87-94.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 87-94
    • Antson, A.A.1
  • 19
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G., and Dreyfuss, G. (1994) Conserved structures and diversity of functions of RNA-binding proteins, Science 265, 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 20
    • 0035860828 scopus 로고    scopus 로고
    • TcUBP-1, a developmentally regulated U-rich RNA-binding protein involved in selective mRNA destabilization in trypanosomes
    • D'Orso, I., and Frasch, A. C. (2001) TcUBP-1, a developmentally regulated U-rich RNA-binding protein involved in selective mRNA destabilization in trypanosomes, J. Biol. Chem. 276, 34801-34809.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34801-34809
    • D'Orso, I.1    Frasch, A.C.2
  • 21
    • 0038482082 scopus 로고    scopus 로고
    • RNA recognition motif-type RNA-binding proteins in Trypanosoma cruzi form a family involved in the interaction with specific transcripts in vivo
    • De Gaudenzi, J. G., D'Orso, I., and Frasch, A. C. (2003) RNA recognition motif-type RNA-binding proteins in Trypanosoma cruzi form a family involved in the interaction with specific transcripts in vivo, J. Biol. Chem. 278, 18884-18894.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18884-18894
    • De Gaudenzi, J.G.1    D'Orso, I.2    Frasch, A.C.3
  • 22
    • 0037184949 scopus 로고    scopus 로고
    • TcUBP-1, an mRNA destabilizing factor from trypanosomes, homodimerizes and interacts with novel AU-rich element- and Poly(A)-binding proteins forming a ribonucleoprotein complex
    • D'Orso, I., and Frasch, A. C. (2002) TcUBP-1, an mRNA destabilizing factor from trypanosomes, homodimerizes and interacts with novel AU-rich element- and Poly(A)-binding proteins forming a ribonucleoprotein complex, J. Biol. Chem. 277, 50520-50528.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50520-50528
    • D'Orso, I.1    Frasch, A.C.2
  • 23
    • 0000477505 scopus 로고    scopus 로고
    • Gifa V.4: A complete package for NMR dataset processing
    • Pons, J. L., Malliavin, T. E., and Delsuc, M. A. (1996) Gifa V.4: A complete package for NMR dataset processing, J. Biomol. NMR 8, 445-452.
    • (1996) J. Biomol. NMR , vol.8 , pp. 445-452
    • Pons, J.L.1    Malliavin, T.E.2    Delsuc, M.A.3
  • 24
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T.-H., Billeter, M., Güntert, P., and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 5, 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 25
    • 44949291986 scopus 로고
    • Three-dimensional triple resonance NMR-spectroscopy of isotopically enriched proteins
    • Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (1990) Three-dimensional triple resonance NMR-spectroscopy of isotopically enriched proteins, J. Magn. Reson. 89, 496-514.
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 26
    • 0030624544 scopus 로고    scopus 로고
    • NMR methods for the study of protein structure and dynamics
    • Kay, L. E. (1997) NMR methods for the study of protein structure and dynamics, Biochem. Cell Biol. 75, 1-15.
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 1-15
    • Kay, L.E.1
  • 27
    • 43949167657 scopus 로고
    • HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α and β carbon resonances in proteins
    • Wittekind, M., and Mueller, L. (1993) HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α and β carbon resonances in proteins, J. Magn. Reson. B 101, 201-205.
    • (1993) J. Magn. Reson. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 28
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S., and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR, J. Am. Chem. Soc. 114, 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 29
    • 0026836698 scopus 로고
    • A refocused and optimized HNCA: Increased sensitivity and resolution in large macromolecules
    • Farmer, B. T., II, Venters, R. A., Spicer, L. D., Wittekind, M. G., and Mueller, L. (1992) A refocused and optimized HNCA: Increased sensitivity and resolution in large macromolecules, J. Biomol. NMR 2, 195-202.
    • (1992) J. Biomol. NMR , vol.2 , pp. 195-202
    • Farmer II, B.T.1    Venters, R.A.2    Spicer, L.D.3    Wittekind, M.G.4    Mueller, L.5
  • 32
    • 0028545648 scopus 로고
    • Measurement of HN-H alpha; J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • Kuboniwa, H., Grzesiek, S., Delaglio, F., and Bax, A. (1994) Measurement of HN-H alpha; J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods, J. Biomol. NMR 4, 871-878.
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 34
    • 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
  • 35
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • Peng, J. W., and Wagner, G. (1994) Investigation of protein motions via relaxation measurements, Methods Enzymol. 239, 563-596.
    • (1994) Methods Enzymol. , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 36
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges, M., Macias, M. J., O'Donoghue, S. I., and Oschkinat, H. (1997) Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin, J. Mol. Biol. 269, 408-422.
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 38
    • 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
  • 40
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55, 29-32.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 42
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain 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 domain 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
  • 43
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution
    • Shamoo, Y., Krueger, U., Rice, L. M., Williams, K. R., and Steitz, T. A. (1997) Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution, Nat. Struct. Biol. 4, 215-222.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 215-222
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 44
    • 0035823011 scopus 로고    scopus 로고
    • A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer
    • Kielkopf, C. L., Rodionova, N. A., Green, M. R., and Burley, S. K. (2001) A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer, Cell 106, 595-605.
    • (2001) Cell , vol.106 , pp. 595-605
    • Kielkopf, C.L.1    Rodionova, N.A.2    Green, M.R.3    Burley, S.K.4
  • 45
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez, C., Boelens, R., and Bonvin, A. M. (2003) HADDOCK: A protein-protein docking approach based on biochemical or biophysical information, J. Am. Chem. Soc. 125, 1731-1737.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 46
    • 0025938601 scopus 로고
    • Identification of molecular contacts between the U1 A small nuclear ribonucleoprotein and U1 RNA
    • Jessen, T. H., Oubridge, C., Teo, C. H., Pritchard, C., and Nagai, K. (1991) Identification of molecular contacts between the U1 A small nuclear ribonucleoprotein and U1 RNA, EMBO J. 10, 3447-3456.
    • (1991) EMBO J. , vol.10 , pp. 3447-3456
    • Jessen, T.H.1    Oubridge, C.2    Teo, C.H.3    Pritchard, C.4    Nagai, K.5
  • 47
    • 0025375223 scopus 로고
    • Major determinants of the specificity of interaction between small nuclear ribonucleoproteins U1A and U2B″ and their cognate RNAs
    • Scherly, D., Boelens, W., Dathan, N. A., van Venrooij, W. J., and Mattaj, I. W. (1990) Major determinants of the specificity of interaction between small nuclear ribonucleoproteins U1A and U2B″ and their cognate RNAs, Nature 345, 502-506.
    • (1990) Nature , vol.345 , pp. 502-506
    • Scherly, D.1    Boelens, W.2    Dathan, N.A.3    Van Venrooij, W.J.4    Mattaj, I.W.5
  • 49
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm, L., and Sander, C. (1994) The FSSP database of structurally aligned protein fold families, Nucleic Acids Res. 22, 3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 50
    • 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
  • 51
    • 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
  • 52
    • 0037507248 scopus 로고    scopus 로고
    • Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein
    • Perez Canadillas, J. M., and Varani, G. (2003) Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein, EMBO J. 22, 2821-2830.
    • (2003) EMBO J. , vol.22 , pp. 2821-2830
    • Perez Canadillas, J.M.1    Varani, G.2
  • 53
    • 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., Howe, P. W., 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.2    Howe, P.W.3    Varani, G.4    Nagai, K.5    Neuhaus, D.6
  • 54
    • 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
  • 55
    • 0038646814 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of human la protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element
    • Jacks, A., Babon, J., Kelly, G., Manolaridis, I., Cary, P. D., Curry, S., and Conte, M. R. (2003) Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element, Structure 11, 833-843.
    • (2003) Structure , vol.11 , pp. 833-843
    • Jacks, A.1    Babon, J.2    Kelly, G.3    Manolaridis, I.4    Cary, P.D.5    Curry, S.6    Conte, M.R.7
  • 56
    • 0035836759 scopus 로고    scopus 로고
    • Delivering messages from the 3′ end
    • Varani, G. (2001) Delivering messages from the 3′ end, Proc. Natl. Acad. Sci. U.S.A. 98, 4288-4289.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4288-4289
    • Varani, G.1
  • 57
    • 0041372953 scopus 로고    scopus 로고
    • Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein
    • Perez, I., McAfee, J. G., and Patton, J. G. (1997) Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein, Biochemistry 36, 11881-11890.
    • (1997) Biochemistry , vol.36 , pp. 11881-11890
    • Perez, I.1    McAfee, J.G.2    Patton, J.G.3
  • 59
    • 3042737403 scopus 로고    scopus 로고
    • U2AF homology motifs: Protein recognition in the RRM world
    • Kielkopf, C. L., Lucke, S., and Green, M. R. (2004) U2AF homology motifs: Protein recognition in the RRM world, Genes Dev. 18, 1513-1526.
    • (2004) Genes Dev. , vol.18 , pp. 1513-1526
    • Kielkopf, C.L.1    Lucke, S.2    Green, M.R.3
  • 60
    • 0034655951 scopus 로고    scopus 로고
    • NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C
    • Inoue, M., Muto, Y., Sakamoto, H., and Yokoyama, S. (2000) NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C, Nucleic Acids Res. 28, 1743-1750.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1743-1750
    • Inoue, M.1    Muto, Y.2    Sakamoto, H.3    Yokoyama, S.4
  • 61
    • 0026757694 scopus 로고
    • Interaction of the RNA-binding domain of the hnRNP C proteins with RNA
    • Gorlach, M., Wittekind, M., Beckman, R. A., Mueller, L., and Dreyfuss, G. (1992) Interaction of the RNA-binding domain of the hnRNP C proteins with RNA, EMBO J. 11, 3289-3295.
    • (1992) EMBO J. , vol.11 , pp. 3289-3295
    • Gorlach, M.1    Wittekind, M.2    Beckman, R.A.3    Mueller, L.4    Dreyfuss, G.5
  • 62
    • 0033559639 scopus 로고    scopus 로고
    • Chemical shift perturbation studies of the interactions of the second RNA-binding domain of the Drosophila sex-lethal protein with the transformer pre-mRNA polyuridine tract and 3′ splice-site sequences
    • Chi, S. W., Muto, Y., Inoue, M., Kim, I., Sakamoto, H., Shimura, Y., Yokoyama, S., Choi, B. S., and Kim, H. (1999) Chemical shift perturbation studies of the interactions of the second RNA-binding domain of the Drosophila sex-lethal protein with the transformer pre-mRNA polyuridine tract and 3′ splice-site sequences, Eur. J. Biochem. 260, 649-660.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 649-660
    • Chi, S.W.1    Muto, Y.2    Inoue, M.3    Kim, I.4    Sakamoto, H.5    Shimura, Y.6    Yokoyama, S.7    Choi, B.S.8    Kim, H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.