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Volumn 18, Issue 16, 1999, Pages 4523-4534

Solution structures of the first end second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF65)

Author keywords

Nuclear magnetic resonance; Protein; RNA binding; Splicing; Three dimensional structure; U2AF

Indexed keywords

PROTEIN SUBUNIT; RNA BINDING PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 0033575718     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.16.4523     Document Type: Article
Times cited : (42)

References (61)
  • 1
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
    • Allain, F.H.-T., Gubser, C.C., Howe, P.W.A., Nagai, K., Neuhaus, D. and Varani, G. (1996) Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature, 380, 646-650.
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.-T.1    Gubser, C.C.2    Howe, P.W.A.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 2
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. and Davis, D.G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson., 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 3
    • 0024245815 scopus 로고
    • Sex-lethal, a Drosophila sex determination switch gene, exhibits sex-specific RNA splicing and sequence similarity to RNA binding proteins
    • Bell, L.R., Maine, E.M., Schedl, P. and Cline, T.W. (1988) Sex-lethal, a Drosophila sex determination switch gene, exhibits sex-specific RNA splicing and sequence similarity to RNA binding proteins. Cell, 55, 1037-1046.
    • (1988) Cell , vol.55 , pp. 1037-1046
    • Bell, L.R.1    Maine, E.M.2    Schedl, P.3    Cline, T.W.4
  • 4
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney, E., Kumar, S. and Krainer, A.R. (1993) Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res., 21, 5803-5816.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 5
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. and Ruben, D.J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett., 69, 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 6
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear overhauser effects in the rotating frame
    • Bothner-By, A.A., Stephens, R.L., Lee, J.-m., Warren, C.D. and Jeanloz, R.W. (1984) Structure determination of a tetrasaccharide: transient nuclear overhauser effects in the rotating frame. J. Am. Chem. Soc., 106, 811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.-M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 8
    • 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
  • 9
    • 0024807032 scopus 로고
    • Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: A diversity of RNA binding proteins is generated by small peptide inserts
    • Burd, C.G., Swanson, M.S., Görlach, M. and Dreyfuss, G. (1989) Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. Proc. Natl Acad. Sci. USA, 86, 9788-9792.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9788-9792
    • Burd, C.G.1    Swanson, M.S.2    Görlach, M.3    Dreyfuss, G.4
  • 10
    • 33748476849 scopus 로고
    • Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence
    • Cavanagh, J. and Rance, M. (1992) Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J. Magn. Reson., 96, 670-678.
    • (1992) J. Magn. Reson. , vol.96 , pp. 670-678
    • Cavanagh, J.1    Rance, M.2
  • 11
    • 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
  • 12
    • 0023475020 scopus 로고
    • Three-dimensional structures of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G.M., Gronenborn, A.M., Nilges, M. and Ryan, C.A. (1987) Three-dimensional structures of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry, 26, 8012-8023.
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 13
    • 0025772135 scopus 로고
    • High-resolution three-dimensional structure of interleukin 1β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy
    • Clore, G.M., Wingfield, P.T. and Gronenborn, A.M. (1991) High-resolution three-dimensional structure of interleukin 1β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry, 30, 2315-2323.
    • (1991) Biochemistry , vol.30 , pp. 2315-2323
    • Clore, G.M.1    Wingfield, P.T.2    Gronenborn, A.M.3
  • 14
    • 0033609121 scopus 로고    scopus 로고
    • Absence of interdomian contacts in the crystal structure of the RNA recognition motifs of sex-lethal
    • Crowder, S.M., Kanaar, R., Rio, D.C. and Alber, T. (1999) Absence of interdomian contacts in the crystal structure of the RNA recognition motifs of Sex-lethal. Proc. Natl Acad. Sci. USA, 96, 4892-4897
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4892-4897
    • Crowder, S.M.1    Kanaar, R.2    Rio, D.C.3    Alber, T.4
  • 15
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc., 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 16
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX PIPES
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX PIPES. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 18
    • 0030611640 scopus 로고    scopus 로고
    • 65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction
    • 65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction. Genes Dev., 11, 1864-1872.
    • (1997) Genes Dev. , vol.11 , pp. 1864-1872
    • Fleckner, J.1    Zhang, M.2    Valcárcel, J.3    Green, M.R.4
  • 19
    • 0026757694 scopus 로고
    • Interaction of the RNA-binding domain of the hnRNP C proteins with RNA
    • Görlach, 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
    • Görlach, M.1    Wittekind, M.2    Beckman, R.A.3    Mueller, L.4    Dreyfuss, G.5
  • 20
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc., 115, 12593-12594.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 21
    • 0001240703 scopus 로고
    • Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy
    • Griesinger, C. and Ernst, R.R. (1987) Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy. J. Magn. Reson., 75, 261-271.
    • (1987) J. Magn. Reson. , vol.75 , pp. 261-271
    • Griesinger, C.1    Ernst, R.R.2
  • 22
    • 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
  • 23
    • 0025363553 scopus 로고
    • Binding of the Drosophila sex-lethal gene product to the alternative splice site of transformer primary transcript
    • Inoue, K., Hoshijima, K., Sakamoto, H. and Shimura, Y. (1990) Binding of the Drosophila Sex-lethal gene product to the alternative splice site of transformer primary transcript. Nature, 344, 461-463.
    • (1990) Nature , vol.344 , pp. 461-463
    • Inoue, K.1    Hoshijima, K.2    Sakamoto, H.3    Shimura, Y.4
  • 24
    • 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
  • 25
    • 0343359244 scopus 로고
    • Investigation of exchange process by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. and Ernst, R.R. (1979) Investigation of exchange process by two-dimensional NMR spectroscopy. J. Chem. Phys., 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 26
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. and Blevins, R.A. (1994) NMRView: 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
  • 27
    • 0027445241 scopus 로고
    • The conserved pre-mRNA splicing factor U2AF from Drosophila: Requirement for viability
    • Kanaar, R., Roche, S.E., Beall, E.L., Green, M.R. and Rio, D.C. (1993) The conserved pre-mRNA splicing factor U2AF from Drosophila: requirement for viability. Science, 262, 569-573.
    • (1993) Science , vol.262 , pp. 569-573
    • Kanaar, R.1    Roche, S.E.2    Beall, E.L.3    Green, M.R.4    Rio, D.C.5
  • 28
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • Kigawa, T., Muto, Y. and Yokoyama, S. (1995) Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J. Biomol. NMR, 6, 129-134.
    • (1995) J. Biomol. NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24. 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 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 Thornton, 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    Thornton, J.M.5
  • 31
    • 0028027496 scopus 로고
    • Resonance assignments and solution structure of the second RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic resonance
    • Lee, A.L., Kanaar, R., Rio, D.C. and Wemmer, D.E. (1994) Resonance assignments and solution structure of the second RNA-binding domain of Sex-lethal determined by multidimensional heteronuclear magnetic resonance. Biochemistry, 33, 13775-13786.
    • (1994) Biochemistry , vol.33 , pp. 13775-13786
    • Lee, A.L.1    Kanaar, R.2    Rio, D.C.3    Wemmer, D.E.4
  • 35
    • 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
  • 36
    • 0001877802 scopus 로고
    • Splicing of precursors to mRNA by the spliceosome
    • Gesteland, R.F. and Atkins, J.F. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Moore, M.J., Query, C.C. and Sharp, P.A. (1993) Splicing of precursors to mRNA by the spliceosome. In Gesteland, R.F. and Atkins, J.F. (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 303-357.
    • (1993) The RNA World , pp. 303-357
    • Moore, M.J.1    Query, C.C.2    Sharp, P.A.3
  • 37
    • 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
  • 39
    • 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, Musashi 1
    • Nagata, T., Kahno, R., Kurihara, Y., Uesugi, S., Imai, T., Sakakibara, S.-i., Okano, H. and Katahira, M. (1999b) Structure, backbone dynamics and interactions with RNA of the C-terminal RNA-binding domain of a mouse neural RNA-binding protein, Musashi 1. J. Mol. Biol., 287, 315-330.
    • (1999) J. Mol. Biol. , vol.287 , pp. 315-330
    • Nagata, T.1    Kahno, R.2    Kurihara, Y.3    Uesugi, S.4    Imai, T.5    Sakakibara, S.-I.6    Okano, H.7    Katahira, M.8
  • 41
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • Nilges, M., Clore, M. and Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. FEBS Lett., 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, M.2    Gronenborn, A.M.3
  • 42
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P.R., Teo, C.-H. and Nagai, K. (1994) Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature, 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.-H.4    Nagai, K.5
  • 43
    • 0027492990 scopus 로고
    • U2AF homolog required for splicing in vivo
    • Potashkin, J., Naik, K. and Wentz-Hunter, K. (1993) U2AF homolog required for splicing in vivo. Nature, 262, 573-575.
    • (1993) Nature , vol.262 , pp. 573-575
    • Potashkin, J.1    Naik, K.2    Wentz-Hunter, K.3
  • 44
    • 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., Evans, 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    Evans, P.R.2    Nagai, K.3
  • 46
    • 0023834880 scopus 로고
    • A factor, U2AF, is required for U2 snRNP binding and splicing complex assembly
    • Ruskin, B., Zamore, P.D. and Green, M.R. (1988) A factor, U2AF, is required for U2 snRNP binding and splicing complex assembly. Cell, 52, 207-219.
    • (1988) Cell , vol.52 , pp. 207-219
    • Ruskin, B.1    Zamore, P.D.2    Green, M.R.3
  • 48
    • 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. Nature Struct. Biol., 4, 215-222.
    • (1997) Nature 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
  • 49
    • 0023478466 scopus 로고
    • cDNA cloning of the human U1 snRNA-associated protein: Extensive homology between U1 and U2 snRNP-specific proteins
    • Sillekens, P.T. Habets, W.J., Beijer, R.P. and van Venrooij, W.J. (1987) cDNA cloning of the human U1 snRNA-associated protein: extensive homology between U1 and U2 snRNP-specific proteins. EMBO J., 6, 3841-3848.
    • (1987) EMBO J. , vol.6 , pp. 3841-3848
    • Sillekens, P.T.1    Habets, W.J.2    Beijer, R.P.3    Van Venrooij, W.J.4
  • 50
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tractbinding proteins
    • Singh, R., Valcárcel, J. and Green, M.R. (1995) Distinct binding specificities and functions of higher eukaryotic polypyrimidine tractbinding proteins. Science, 268, 1173-1176.
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcárcel, J.2    Green, M.R.3
  • 51
    • 0027400786 scopus 로고
    • The protein sex-lethal antagonizes the splicing factor U2AF to regulate alternative splicing of transformer pre-mRNA
    • Valcárcel, J., Singh, R., Zamore, P.D. and Green, M.R. (1993) The protein Sex-lethal antagonizes the splicing factor U2AF to regulate alternative splicing of transformer pre-mRNA. Nature, 362, 171-175.
    • (1993) Nature , vol.362 , pp. 171-175
    • Valcárcel, J.1    Singh, R.2    Zamore, P.D.3    Green, M.R.4
  • 53
    • 0029151591 scopus 로고
    • Synthesis, deprotection, analysis and purification of RNA and ribozymes
    • Wincott, F. et al. (1995) Synthesis, deprotection, analysis and purification of RNA and ribozymes. Nucleic Acids Res., 23, 2677-2684.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2677-2684
    • Wincott, F.1
  • 55
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton - Proton distance constraints with nuclear magnetic resonance
    • Wüthrich, K., Billeter, M. and Braun, W. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton - proton distance constraints with nuclear magnetic resonance. J. Mol. Biol., 169, 949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 56
    • 0031569797 scopus 로고    scopus 로고
    • Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs
    • Xu, R.-M., Jokhan, L., Cheng, X., Mayeda, A. and Krainer, A.R. (1997) Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs. Structure, 5, 559-570.
    • (1997) Structure , vol.5 , pp. 559-570
    • Xu, R.-M.1    Jokhan, L.2    Cheng, X.3    Mayeda, A.4    Krainer, A.R.5
  • 57
    • 0024408832 scopus 로고
    • Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor
    • Zamore, P.D. and Green, M.R. (1989) Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc. Natl Acad. Sci. USA, 86, 9243-9247.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9243-9247
    • Zamore, P.D.1    Green, M.R.2
  • 58
    • 0026026981 scopus 로고
    • Biochemical characterization of U2 snRNP auxiliary factor: An essential pre-mRNA splicing factor with a novel intranuclear distribution
    • Zamore, P.D. and Green, M.R. (1991) Biochemical characterization of U2 snRNP auxiliary factor: an essential pre-mRNA splicing factor with a novel intranuclear distribution. EMBO J., 10, 207-214.
    • (1991) EMBO J. , vol.10 , pp. 207-214
    • Zamore, P.D.1    Green, M.R.2
  • 59
    • 0026569967 scopus 로고
    • Cloning and domain structure of the mammalian splicing factor U2AF
    • Zamore, P.D., Patton, J.G. and Green, M.R. (1992) Cloning and domain structure of the mammalian splicing factor U2AF. Nature, 355, 609-614.
    • (1992) Nature , vol.355 , pp. 609-614
    • Zamore, P.D.1    Patton, J.G.2    Green, M.R.3
  • 60
    • 0026649523 scopus 로고
    • Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit
    • Zhang, M., Zamore, P.D., Carmo-Fonseca, M., Lamond, A.I. and Green, M.R. (1992) Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit. Proc. Natl Acad. Sci. USA, 89, 8769-8773.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8769-8773
    • Zhang, M.1    Zamore, P.D.2    Carmo-Fonseca, M.3    Lamond, A.I.4    Green, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.