메뉴 건너뛰기




Volumn 17, Issue 4, 2003, Pages 461-475

Structure and function of the PWI motif: A novel nucleic acid-binding domain that facilitates pre-MRNA processing

Author keywords

3 end cleavage; RNA binding domain; Spliceosome

Indexed keywords

DOUBLE STRANDED DNA; MESSENGER RNA; NUCLEIC ACID BINDING PROTEIN; PROTEIN PWI; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 0037443092     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1060403     Document Type: Article
Times cited : (47)

References (70)
  • 1
    • 0029812154 scopus 로고    scopus 로고
    • hnRNP A1 binds promiscuously to oligoribonucleotides: Utilization of random and homo-oligonucleotides to discriminate sequence from base-specific binding
    • Abdul-Manan, N. and Williams, K.R. 1996. hnRNP A1 binds promiscuously to oligoribonucleotides: Utilization of random and homo-oligonucleotides to discriminate sequence from base-specific binding. Nucleic Acids Res. 24: 4063-4070.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4063-4070
    • Abdul-Manan, N.1    Williams, K.R.2
  • 2
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding
    • Allain, F.H., Gubser, C.C., Howe, P.W., Nagai, K., Neuhaus, D., and Varani, G. 1996. Specificity of ribonucleoprotein interaction determined by RNA folding. Nature 380: 646-650.
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.1    Gubser, C.C.2    Howe, P.W.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 3
    • 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
  • 4
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T., Billeter, M., Güntert, P., and Wüthrich, K. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 6: 1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 5
    • 0029448154 scopus 로고
    • Assignment and modeling of the Rev Response Element RNA bound to a Rev peptide using 13C-heteronuclear NMR
    • Battiste, J.L., Tan, R., Frankel, A.D., and Williamson, J.R. 1995. Assignment and modeling of the Rev Response Element RNA bound to a Rev peptide using 13C-heteronuclear NMR. J. Biomol. NMR 6: 375-389.
    • (1995) J. Biomol. NMR , vol.6 , pp. 375-389
    • Battiste, J.L.1    Tan, R.2    Frankel, A.D.3    Williamson, J.R.4
  • 6
    • 0031026421 scopus 로고    scopus 로고
    • Solution structure of the ribosomal RNA binding protein S15 from Thermus
    • Berglund, H., Rak, A., Serganov, A., Garber, M., and Hard, T. 1997. Solution structure of the ribosomal RNA binding protein S15 from Thermus. Nat. Struct. Biol. 4: 20-23.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 20-23
    • Berglund, H.1    Rak, A.2    Serganov, A.3    Garber, M.4    Hard, T.5
  • 7
    • 0033133976 scopus 로고    scopus 로고
    • The PWI motif: A new protein domain in splicing factors
    • Blencowe, B.J. and Ouzounis, C.A. 1999. The PWI motif: A new protein domain in splicing factors. Trends Biochem. Sci. 24: 179-180.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 179-180
    • Blencowe, B.J.1    Ouzounis, C.A.2
  • 9
    • 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
  • 10
    • 0021111044 scopus 로고
    • Sequence-specific interaction of R17 coat protein with its ribonucleic acid binding site
    • Carey, J., Cameron, V., de Haseth, P.L., and Uhlenbeck, O.C. 1983. Sequence-specific interaction of R17 coat protein with its ribonucleic acid binding site. Biochemistry 22: 2601-2610.
    • (1983) Biochemistry , vol.22 , pp. 2601-2610
    • Carey, J.1    Cameron, V.2    De Haseth, P.L.3    Uhlenbeck, O.C.4
  • 11
    • 0028270469 scopus 로고
    • An RNA-binding peptide from bovine immunodeficiency virus Tat protein recognizes an unusual RNA structure
    • Chen, L. and Frankel, A.D. 1994. An RNA-binding peptide from bovine immunodeficiency virus Tat protein recognizes an unusual RNA structure. Biochemistry 33: 2708-2715.
    • (1994) Biochemistry , vol.33 , pp. 2708-2715
    • Chen, L.1    Frankel, A.D.2
  • 12
    • 0033575719 scopus 로고    scopus 로고
    • Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain
    • Chi, S.W., Ayed, A., and Arrowsmith, C.H. 1999. Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain. EMBO J. 18: 4438-4445.
    • (1999) EMBO J. , vol.18 , pp. 4438-4445
    • Chi, S.W.1    Ayed, A.2    Arrowsmith, C.H.3
  • 13
    • 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
  • 14
    • 0029030104 scopus 로고
    • Translational regulation in development
    • Curtis, D., Lehmann, R., and Zamore, P.D. 1995. Translational regulation in development. Cell 81: 171-178.
    • (1995) Cell , vol.81 , pp. 171-178
    • Curtis, D.1    Lehmann, R.2    Zamore, P.D.3
  • 17
    • 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
    • 0032727991 scopus 로고    scopus 로고
    • Themes in RNA-protein recognition
    • Draper, D.E. 1999. Themes in RNA-protein recognition. J. Mol. Biol. 293: 255-270.
    • (1999) J. Mol. Biol. , vol.293 , pp. 255-270
    • Draper, D.E.1
  • 19
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G., Kim, V.N., and Kataoka, N. 2002. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 3: 195-205.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 20
    • 0030059840 scopus 로고    scopus 로고
    • RNA recognition and translational regulation by a homeodomain protein
    • Dubnau, J. and Struhl, G. 1996. RNA recognition and translational regulation by a homeodomain protein. Nature 379: 694-699.
    • (1996) Nature , vol.379 , pp. 694-699
    • Dubnau, J.1    Struhl, G.2
  • 21
    • 0033022124 scopus 로고    scopus 로고
    • The SRm160/300 splicing coactivator is required for exon-enhancer function
    • Eldridge, A.G., Li, Y., Sharp, P.A., and Blencowe, B.J. 1999. The SRm160/300 splicing coactivator is required for exon-enhancer function. Proc. Natl. Acad. Sci. 96: 6125-6130.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 6125-6130
    • Eldridge, A.G.1    Li, Y.2    Sharp, P.A.3    Blencowe, B.J.4
  • 22
    • 0031763884 scopus 로고    scopus 로고
    • MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily
    • Guan, Y., Manuel, R.C., Arvai, A.S., Parikh, S.S., Mol, C.D., Miller, J.H., Lloyd, S., and Tainer, J.A. 1998. MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily. Nat. Struct. Biol. 5: 1058-1064.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1058-1064
    • Guan, Y.1    Manuel, R.C.2    Arvai, A.S.3    Parikh, S.S.4    Mol, C.D.5    Miller, J.H.6    Lloyd, S.7    Tainer, J.A.8
  • 23
    • 0031610367 scopus 로고    scopus 로고
    • U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U1 70K and poly(A) polymerase
    • Gunderson, S.I., Polycarpou-Schwarz, M., and Mattaj, I.W. 1998. U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U1 70K and poly(A) polymerase. Mol. Cell. 1: 255-264.
    • (1998) Mol. Cell , vol.1 , pp. 255-264
    • Gunderson, S.I.1    Polycarpou-Schwarz, M.2    Mattaj, I.W.3
  • 24
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C., and Wuthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 25
    • 0034651873 scopus 로고    scopus 로고
    • DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA
    • Hollis, T., Ichikawa, Y., and Ellenberger, T. 2000. DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA. EMBO J. 19: 758-766.
    • (2000) EMBO J. , vol.19 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 26
    • 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
  • 27
    • 0031440025 scopus 로고    scopus 로고
    • A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs
    • Horowitz, D.S., Kobayashi, R., and Krainer, A.R. 1997. A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. RNA 3: 1374-1387.
    • (1997) RNA , vol.3 , pp. 1374-1387
    • Horowitz, D.S.1    Kobayashi, R.2    Krainer, A.R.3
  • 28
    • 0033634824 scopus 로고    scopus 로고
    • Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm
    • Kataoka, N., Yong, J., Kim, V.N., Velazquez, F., Perkinson, R.A., Wang, F., and Dreyfuss, G. 2000. Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol Cell. 6: 673-682.
    • (2000) Mol. Cell , vol.6 , pp. 673-682
    • Kataoka, N.1    Yong, J.2    Kim, V.N.3    Velazquez, F.4    Perkinson, R.A.5    Wang, F.6    Dreyfuss, G.7
  • 29
    • 0035823150 scopus 로고    scopus 로고
    • Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
    • Kim, V.N., Kataoka, N., and Dreyfuss, G. 2001. Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. Science 293: 1832-1836.
    • (2001) Science , vol.293 , pp. 1832-1836
    • Kim, V.N.1    Kataoka, N.2    Dreyfuss, G.3
  • 30
    • 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. Graph. 14: 51-55.
    • (1996) J. Mol. Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 31
    • 0030749220 scopus 로고    scopus 로고
    • The human U4/U6 snRNP contains 60 and 90kD proteins that are structurally homologous to the yeast splicing factors Prp4p and Prp3p
    • Lauber, J., Plessel, G., Prehn, S., Will, C.L., Fabrizio, P., Groning, K., Lane, W.S., and Luhrmann, R. 1997. The human U4/U6 snRNP contains 60 and 90kD proteins that are structurally homologous to the yeast splicing factors Prp4p and Prp3p. RNA 3: 926-941.
    • (1997) RNA , vol.3 , pp. 926-941
    • Lauber, J.1    Plessel, G.2    Prehn, S.3    Will, C.L.4    Fabrizio, P.5    Groning, K.6    Lane, W.S.7    Luhrmann, R.8
  • 32
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir, H., Izaurralde, E., Maquat, L.E., and Moore, M.J. 2000a. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19: 6860-6869.
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 33
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junctions
    • Le Hir, H., Moore, M.J., and Maquat, L.E. 2000b. Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junctions. Genes & Dev. 14: 1098-1108.
    • (2000) Genes & Dev. , vol.14 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 34
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
    • Lejeune, F., Ishigaki, Y., Li, X., and Maquat, L.E. 2002. The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling. EMBO J. 21: 3536-3545.
    • (2002) EMBO J. , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 35
    • 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. 2000. Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome. Cell 100: 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
  • 36
    • 0032128255 scopus 로고    scopus 로고
    • Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins
    • Liu, H.-X., Zhang, M., and Krainer, A.R. 1998. Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins. Genes & Dev. 12: 1998-2012.
    • (1998) Genes & Dev. , vol.12 , pp. 1998-2012
    • Liu, H.-X.1    Zhang, M.2    Krainer, A.R.3
  • 37
    • 0035846545 scopus 로고    scopus 로고
    • Multiple interactions between SRm160 and SR family proteins in enhancer-dependent splicing and development of C. elegans
    • Longman, D., McGarvey, T., McCracken, S., Johnstone, I.L., Blencowe, B.J., and Caceres, J.F. 2001. Multiple interactions between SRm160 and SR family proteins in enhancer-dependent splicing and development of C. elegans. Curr. Biol. 11: 1923-1933.
    • (2001) Curr. Biol. , vol.11 , pp. 1923-1933
    • Longman, D.1    McGarvey, T.2    McCracken, S.3    Johnstone, I.L.4    Blencowe, B.J.5    Caceres, J.F.6
  • 38
    • 0031840978 scopus 로고    scopus 로고
    • Regulation of alternative polyadenylation by U1 snRNPs and SRp20
    • Lou, H., Neugebauer, K.M., Gagel, R.F., and Berget, S.M. 1998. Regulation of alternative polyadenylation by U1 snRNPs and SRp20. Mol. Cell Biol. 18: 4977-4985.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4977-4985
    • Lou, H.1    Neugebauer, K.M.2    Gagel, R.F.3    Berget, S.M.4
  • 39
    • 0030024350 scopus 로고    scopus 로고
    • Interaction between the U1 sn-RNP-A protein and the 160-kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation efficiency in vitro
    • Lutz, C.S., Murthy, K.G., Schek, N., O'Connor, J.P., Manley, J.L., and Alwine, J.C. 1996. Interaction between the U1 sn-RNP-A protein and the 160-kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation efficiency in vitro. Genes & Dev. 10: 325-337.
    • (1996) Genes & Dev. , vol.10 , pp. 325-337
    • Lutz, C.S.1    Murthy, K.G.2    Schek, N.3    O'Connor, J.P.4    Manley, J.L.5    Alwine, J.C.6
  • 40
    • 0034704201 scopus 로고    scopus 로고
    • Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon
    • Lykke-Andersen, J., Shu, M.D., and Steitz, J.A. 2000. Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell 103: 1121-1131.
    • (2000) Cell , vol.103 , pp. 1121-1131
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 41
    • 0035823247 scopus 로고    scopus 로고
    • Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1
    • -. 2001. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science 293: 1836-1839.
    • (2001) Science , vol.293 , pp. 1836-1839
  • 42
    • 0025190644 scopus 로고
    • HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence
    • Malim, M.H., Tiley, L.S., McCarn, D.F., Rusche, J.R., Hauber, J., and Cullen, B.R. 1990. HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence. Cell 60: 675-683.
    • (1990) Cell , vol.60 , pp. 675-683
    • Malim, M.H.1    Tiley, L.S.2    McCarn, D.F.3    Rusche, J.R.4    Hauber, J.5    Cullen, B.R.6
  • 43
    • 0036132667 scopus 로고    scopus 로고
    • SRm160 splicing coactivator promotes transcript 3′-end cleavage
    • McCracken, S., Lambermon, M., and Blencowe, B.J. 2002. SRm160 splicing coactivator promotes transcript 3′-end cleavage. Mol. Cell Biol. 22: 148-160.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 148-160
    • McCracken, S.1    Lambermon, M.2    Blencowe, B.J.3
  • 44
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller, J., McLachlan, A.D., and Klug, A. 1985. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 4: 1609-1614.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 45
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for nonhomologous sequences
    • Murzin, A.G. 1993. OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for nonhomologous sequences. EMBO J. 12: 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 46
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • Nash, H.M., Bruner, S.D., Scharer, O.D., Kawate, T., Addona, T.A., Spooner, E., Lane, W.S., and Verdine, G.L. 1996. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6: 968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 47
    • 0028010715 scopus 로고
    • Upstream introns influence the efficiency of final intron removal and RNA 3′-end formation
    • Nesic, D. and Maquat, L.E. 1994. Upstream introns influence the efficiency of final intron removal and RNA 3′-end formation. Genes & Dev. 8: 363-375.
    • (1994) Genes & Dev. , vol.8 , pp. 363-375
    • Nesic, D.1    Maquat, L.E.2
  • 48
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 A 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 A 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
  • 49
    • 43949161325 scopus 로고
    • Simultaneous acquisition of 15N-edited and 13C-edited NOE spectra of proteins dissolved in H20
    • Pascal, S.M., Muhandiram, D.R., Yamazaki, T., Forman-Kay, J.D., and Kay, L.E. 1994. Simultaneous acquisition of 15N-edited and 13C-edited NOE spectra of proteins dissolved in H20. J. Magn. Reson. 103: 197-201.
    • (1994) J. Magn. Reson. , vol.103 , pp. 197-201
    • Pascal, S.M.1    Muhandiram, D.R.2    Yamazaki, T.3    Forman-Kay, J.D.4    Kay, L.E.5
  • 51
    • 0028873824 scopus 로고
    • Dissecting RNA-protein interactions: RNA-RNA recognition by Rop
    • Predki, P.F., Nayak, L.M., Gottlieb, M.B., and Regan, L. 1995. Dissecting RNA-protein interactions: RNA-RNA recognition by Rop. Cell 80: 41-50.
    • (1995) Cell , vol.80 , pp. 41-50
    • Predki, P.F.1    Nayak, L.M.2    Gottlieb, M.B.3    Regan, L.4
  • 52
    • 0026651395 scopus 로고
    • Conformation of the TAR RNA-arginine complex by NMR spectroscopy
    • Puglisi, J.D., Ton, R., Calnan, B.J., Frankel, A.D., and Williamson, J.R. 1992. Conformation of the TAR RNA-arginine complex by NMR spectroscopy. Science 257: 76-80.
    • (1992) Science , vol.257 , pp. 76-80
    • Puglisi, J.D.1    Ton, R.2    Calnan, B.J.3    Frankel, A.D.4    Williamson, J.R.5
  • 53
    • 0028858599 scopus 로고
    • Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
    • Puglisi, J.D., Chen, L., Blanchard, S., and Frankel, A.D. 1995. Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Science 270: 1200-1203.
    • (1995) Science , vol.270 , pp. 1200-1203
    • Puglisi, J.D.1    Chen, L.2    Blanchard, S.3    Frankel, A.D.4
  • 54
    • 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
  • 55
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber, J., Ryder, U., Lamond, A.I., and Mann, M. 2002. Large-scale proteomic analysis of the human spliceosome. Genome Res. 12: 1231-1245.
    • (2002) Genome Res. , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 56
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter, J.M. and Schultz, S.C. 1998. Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA. EMBO J. 17: 7505-7513.
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 57
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of Proc
    • Schultz, J., Milpetz, F., Bork, P., and Ponting, C.P. 1998. SMART, a simple modular architecture research tool: Identification of Proc. Natl. Acad. Sci. 95: 5857-5864.
    • (1998) Natl. Acad. Sci. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 58
    • 0030858706 scopus 로고    scopus 로고
    • RNA-binding proteins as regulators of gene expression
    • Siomi, H. and Dreyfuss, G. 1997. RNA-binding proteins as regulators of gene expression. Curr. Opin. Genet. Dev. 7: 345-353.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 345-353
    • Siomi, H.1    Dreyfuss, G.2
  • 59
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi, H., Matunis, M.J., Michael, W.M., and Dreyfuss, G. 1993. The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res. 21: 1193-1198.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 61
    • 0018350826 scopus 로고
    • Functional domains of Escherichia coli ribosomal protein S1. Formation and characterization of a fragment with ribosome-binding properties
    • Suryanarayana, T. and Subramanian, A.R. 1979. Functional domains of Escherichia coli ribosomal protein S1. Formation and characterization of a fragment with ribosome-binding properties. J. Mol. Biol. 127: 41-54.
    • (1979) J. Mol. Biol. , vol.127 , pp. 41-54
    • Suryanarayana, T.1    Subramanian, A.R.2
  • 62
    • 0036513847 scopus 로고    scopus 로고
    • 1H, 13C, and 15N resonance assignments and secondary structure of the PWI domain from SRm160 using reduced dimensionality NMR
    • Szymczyna, B.R., Pineda-Lucena, A., Mills, J.L., Szyperski, T., and Arrowsmith, C.H. 2002. 1H, 13C, and 15N resonance assignments and secondary structure of the PWI domain from SRm160 using reduced dimensionality NMR. J. Biomol. NMR 22: 299-300.
    • (2002) J. Biomol. NMR , vol.22 , pp. 299-300
    • Szymczyna, B.R.1    Pineda-Lucena, A.2    Mills, J.L.3    Szyperski, T.4    Arrowsmith, C.H.5
  • 63
    • 0031037690 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by an SR protein requires RS domain
    • Tacke, R., Chen, Y., and Manley, J.L. 1997. Sequence-specific RNA binding by an SR protein requires RS domain. Proc. Natl. Acad. Sci. 94: 1148-1153.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 1148-1153
    • Tacke, R.1    Chen, Y.2    Manley, J.L.3
  • 64
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M.M., Ahem, H., Xing, D., Cunningham, R.P., and Tainer, J.A. 1995. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14: 4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahem, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 65
    • 0034008058 scopus 로고    scopus 로고
    • The carboxyl terminus of vertebrate poly(A) polymerase interacts with U2AF 65 to couple 3′-end processing and splicing
    • Vagner, S., Vagner, C., and Mattaj, I.W. 2000. The carboxyl terminus of vertebrate poly(A) polymerase interacts with U2AF 65 to couple 3′-end processing and splicing. Genes & Dev. 14: 403-413.
    • (2000) Genes & Dev. , vol.14 , pp. 403-413
    • Vagner, S.1    Vagner, C.2    Mattaj, I.W.3
  • 67
    • 0027153540 scopus 로고
    • Association with terminal exons in pre-mRNAs: A new role for the U1 snRNP?
    • Wassarman, K.M. and Steitz, J.A. 1993. Association with terminal exons in pre-mRNAs: A new role for the U1 snRNP? Genes & Dev. 7: 647-659.
    • (1993) Genes & Dev. , vol.7 , pp. 647-659
    • Wassarman, K.M.1    Steitz, J.A.2
  • 68
    • 0035213710 scopus 로고    scopus 로고
    • Defining cis-acting elements and trans-acting factors in RNA localization
    • Yaniv, K. and Yisraeli, J.K. 2001. Defining cis-acting elements and trans-acting factors in RNA localization. Int. Rev. Cytol. 203: 521-539.
    • (2001) Int. Rev. Cytol. , vol.203 , pp. 521-539
    • Yaniv, K.1    Yisraeli, J.K.2
  • 69
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou, Z., Luo, M.J., Straesser, K., Katahira, J., Hurt, E., and Reed, R. 2000. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 407: 401-405.
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1    Luo, M.J.2    Straesser, K.3    Katahira, J.4    Hurt, E.5    Reed, R.6
  • 70
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou, Z., Licklider, L.J., Gygi, S.P., and Reed, R. 2002. Comprehensive proteomic analysis of the human spliceosome. Nature 419: 182-185.
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.