메뉴 건너뛰기




Volumn 18, Issue 7, 1998, Pages 3991-4003

In vitro genetic analysis of the RNA binding site of vigilin, a multi- KH-domain protein

Author keywords

[No Author keywords available]

Indexed keywords

RNA BINDING PROTEIN; UNCLASSIFIED DRUG; VIGILIN;

EID: 0031862144     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.7.3991     Document Type: Article
Times cited : (49)

References (70)
  • 1
    • 0029949698 scopus 로고    scopus 로고
    • Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA
    • Arning, S., P. Grüter, G. Bilbe, and A. Krämer. 1996. Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA. RNA 2:794-810.
    • (1996) RNA , vol.2 , pp. 794-810
    • Arning, S.1    Grüter, P.2    Bilbe, G.3    Krämer, A.4
  • 2
    • 0027377580 scopus 로고
    • FMR1 protein: Conserved RNP family domains and selective RNA binding
    • Ashley, C. T., Jr., K. D. Wilkinson, D. Reines, and S. T. Warren. 1993. FMR1 protein: conserved RNP family domains and selective RNA binding. Science 262:563-566.
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley Jr., C.T.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 3
    • 0026045893 scopus 로고
    • HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA
    • Bartel, D. P., M. L. Zapp, M. R. Green, and J. W. Szostak. 1991. HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA. Cell 67:529-536.
    • (1991) Cell , vol.67 , pp. 529-536
    • Bartel, D.P.1    Zapp, M.L.2    Green, M.R.3    Szostak, J.W.4
  • 4
    • 0028268016 scopus 로고
    • Binding of an HIV Rev peptide to Rev responsive element RNA induces formation of purine-purine base pairs
    • Battiste, J. L., R. Tan, A. D. Frankel, and J. R. Williamson. 1994. Binding of an HIV Rev peptide to Rev responsive element RNA induces formation of purine-purine base pairs. Biochemistry 33:2741-2747.
    • (1994) Biochemistry , vol.33 , pp. 2741-2747
    • Battiste, J.L.1    Tan, R.2    Frankel, A.D.3    Williamson, J.R.4
  • 5
    • 0029053016 scopus 로고
    • Degradation of mRNA in eukaryotes
    • Beelman, C. A., and R. Parker. 1995. Degradation of mRNA in eukaryotes. Cell 81:179-183.
    • (1995) Cell , vol.81 , pp. 179-183
    • Beelman, C.A.1    Parker, R.2
  • 8
    • 0025572707 scopus 로고
    • Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection
    • Blackwell, T. K., and H. Weintraub. 1990. Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection. Science 250:1104-1110.
    • (1990) Science , vol.250 , pp. 1104-1110
    • Blackwell, T.K.1    Weintraub, H.2
  • 9
    • 0024351149 scopus 로고
    • Ribosome loading, but not protein synthesis, is required for estrogen stabilization of Xenopus laevis vitellogenin mRNA
    • Blume, J. E., and D. J. Shapiro. 1989. Ribosome loading, but not protein synthesis, is required for estrogen stabilization of Xenopus laevis vitellogenin mRNA. Nucleic Acids Res. 17:9003-9014.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9003-9014
    • Blume, J.E.1    Shapiro, D.J.2
  • 10
    • 0020804585 scopus 로고
    • Estrogen stabilizes vitellogenin mRNA against cytoplasmic degradation
    • Brock, M. L., and D. J. Shapiro. 1983. Estrogen stabilizes vitellogenin mRNA against cytoplasmic degradation. Cell 34:207-214.
    • (1983) Cell , vol.34 , pp. 207-214
    • Brock, M.L.1    Shapiro, D.J.2
  • 11
    • 0031005029 scopus 로고    scopus 로고
    • Single-stranded RNA recognition by the bacteriophage T4 translational repressor, regA
    • Brown, D., J. Brown, C. Kang, L. Gold, and P. Allen. 1997. Single-stranded RNA recognition by the bacteriophage T4 translational repressor, regA. J. Biol. Chem. 272:14969-14974.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14969-14974
    • Brown, D.1    Brown, J.2    Kang, C.3    Gold, L.4    Allen, P.5
  • 12
    • 0030992812 scopus 로고    scopus 로고
    • The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo
    • Buckanovich, R. J., and R. B. Darnell. 1997. The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo. Mol. Cell. Biol. 17:3194-3201.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3194-3201
    • Buckanovich, R.J.1    Darnell, R.B.2
  • 13
    • 0029875911 scopus 로고    scopus 로고
    • The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein, the activity of which is inhibited by paraneoplastic antibodies
    • Buckanovich, R. J., Y. Y. Yang, and R. B. Darnell. 1996. The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein, the activity of which is inhibited by paraneoplastic antibodies. J. Neurosci. 16:1114-1122.
    • (1996) J. Neurosci. , vol.16 , pp. 1114-1122
    • Buckanovich, R.J.1    Yang, Y.Y.2    Darnell, R.B.3
  • 14
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G., and G. Dreyfuss. 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
  • 15
    • 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 G. Dreyfuss. 1994. RNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing. EMBO J. 13:1197-1204.
    • (1994) EMBO J. , vol.13 , pp. 1197-1204
    • Burd, C.G.1    Dreyfuss, G.2
  • 16
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R. C., and G. F. Joyce. 1992. Randomization of genes by PCR mutagenesis. PCR Methods Appl. 2:28-33.
    • (1992) PCR Methods Appl. , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 17
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA
    • Casey, J. L., D. M. Koeller, V. C. Ramin, R. D. Klausner, and J. B. Harford. 1989. Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA. EMBO J. 8:3693-3699.
    • (1989) EMBO J. , vol.8 , pp. 3693-3699
    • Casey, J.L.1    Koeller, D.M.2    Ramin, V.C.3    Klausner, R.D.4    Harford, J.B.5
  • 18
    • 0030463479 scopus 로고    scopus 로고
    • Differential activity of ELAV-like RNA-binding proteins in human neuroblastoma
    • Chagnovich, D., B. E. Fayos, and S. L. Conn. 1996. Differential activity of ELAV-like RNA-binding proteins in human neuroblastoma. J. Biol. Chem. 271:33587-33591.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33587-33591
    • Chagnovich, D.1    Fayos, B.E.2    Conn, S.L.3
  • 19
    • 0028788194 scopus 로고
    • AU-rich elements: Characterization and importance in mRNA degradation
    • Chen, C. Y., and A. B. Shyu. 1995. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci. 20:465-470.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.B.2
  • 20
    • 0027566636 scopus 로고
    • Expression and purification of general transcription factors by FLAG epitope-tagging and peptide elution
    • Chiang, C. M., and R. G. Roeder. 1993. Expression and purification of general transcription factors by FLAG epitope-tagging and peptide elution. Peptide Res. 6:62-64.
    • (1993) Peptide Res. , vol.6 , pp. 62-64
    • Chiang, C.M.1    Roeder, R.G.2
  • 21
    • 0029858735 scopus 로고    scopus 로고
    • Characterisation of the nucleic-acid-binding activity of KH domains. Different properties of different domains
    • Dejgaard, K., and H. Leffers. 1996. Characterisation of the nucleic-acid-binding activity of KH domains. Different properties of different domains. Eur. J. Biochem. 241:425-431.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 425-431
    • Dejgaard, K.1    Leffers, H.2
  • 22
    • 15844383918 scopus 로고    scopus 로고
    • AUF1 binding affinity to A+U-rich elements correlates with rapid mRNA degradation
    • DeMaria, C. T., and G. Brewer. 1996. AUF1 binding affinity to A+U-rich elements correlates with rapid mRNA degradation. J. Biol. Chem. 271: 12179-12184.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12179-12184
    • DeMaria, C.T.1    Brewer, G.2
  • 23
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 24
    • 0029022283 scopus 로고
    • Tissue distribution, hormone regulation and evidence for a human homologue of the estrogen-inducible Xenopus laevis vitellogenin mRNA binding protein
    • Dodson, R. E., M. R. Acena, and D. J. Shapiro. 1995. Tissue distribution, hormone regulation and evidence for a human homologue of the estrogen-inducible Xenopus laevis vitellogenin mRNA binding protein. J. Steroid Biochem. Mol. Biol. 52:505-515.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.52 , pp. 505-515
    • Dodson, R.E.1    Acena, M.R.2    Shapiro, D.J.3
  • 25
    • 0028214848 scopus 로고
    • An estrogen-inducible protein binds specifically to a sequence in the 3′ untranslated region of estrogen-stabilized vitellogenin mRNA
    • Dodson, R. E., and D. J. Shapiro. 1994. An estrogen-inducible protein binds specifically to a sequence in the 3′ untranslated region of estrogen-stabilized vitellogenin mRNA. Mol. Cell. Biol. 14:3130-3138.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3130-3138
    • Dodson, R.E.1    Shapiro, D.J.2
  • 26
    • 0030973538 scopus 로고    scopus 로고
    • Vigilin, a ubiquitous protein with 14 K homology domains, is the estrogen-inducible vitellogenin mRNA 3′-untranslated region-binding protein
    • Dodson, R. E., and D. J. Shapiro. 1997. Vigilin, a ubiquitous protein with 14 K homology domains, is the estrogen-inducible vitellogenin mRNA 3′-untranslated region-binding protein. J. Biol. Chem. 272:12249-12252.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12249-12252
    • Dodson, R.E.1    Shapiro, D.J.2
  • 27
    • 0027258576 scopus 로고
    • The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator Nusa and is probably involved in binding to nucleic acid
    • Gibson, T. J., J. D. Thompson, and J. Heringa. 1993. The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid. FEBS Lett. 324: 361-366.
    • (1993) FEBS Lett. , vol.324 , pp. 361-366
    • Gibson, T.J.1    Thompson, J.D.2    Heringa, J.3
  • 29
    • 0027992089 scopus 로고
    • The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins
    • Görlach, M., C. G. Burd, and G. Dreyfuss. 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
    • Görlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 30
    • 0022653964 scopus 로고
    • Human oestrogen receptor cDNA: Sequence, expression and homology to v-erb-A
    • Green, S., P. Walter, V. Kumar, A. Krust, J. M. Bornert, P. Argos, and P. Chambon. 1986. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature 320:134-139.
    • (1986) Nature , vol.320 , pp. 134-139
    • Green, S.1    Walter, P.2    Kumar, V.3    Krust, A.4    Bornert, J.M.5    Argos, P.6    Chambon, P.7
  • 31
    • 0029114121 scopus 로고
    • The Drosophila SR protein RBP1 contributes to the regulation of doublesex alternative splicing by recognizing RBP1 RNA target sequences
    • Heinrichs, V., and B. S. Baker. 1995. The Drosophila SR protein RBP1 contributes to the regulation of doublesex alternative splicing by recognizing RBP1 RNA target sequences. EMBO J. 14:3987-1000.
    • (1995) EMBO J. , vol.14 , pp. 3987-11000
    • Heinrichs, V.1    Baker, B.S.2
  • 32
    • 0027361841 scopus 로고
    • High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding
    • Jellinek, D., C. K. Lynott, D. B. Rifkin, and N. Janjic. 1993. High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proc. Natl. Acad. Sci. USA 90:11227-11231.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11227-11231
    • Jellinek, D.1    Lynott, C.K.2    Rifkin, D.B.3    Janjic, N.4
  • 33
    • 0026540537 scopus 로고
    • Specific binding of a basic peptide from HIV-1 Rev
    • Kjems, J., B. J. Calnan, A. D. Frankel, and P. A. Sharp. 1992. Specific binding of a basic peptide from HIV-1 Rev. EMBO J. 11:1119-1129.
    • (1992) EMBO J. , vol.11 , pp. 1119-1129
    • Kjems, J.1    Calnan, B.J.2    Frankel, A.D.3    Sharp, P.A.4
  • 34
    • 0029847582 scopus 로고    scopus 로고
    • Evidence for a novel cytoplasmic tRNA-protein complex containing the KH-multidomain protein vigilin
    • Kruse, C., A. Grünweiler, H. Notbohm, S. Kügler, W. G. Purschke, and P. K. Müller. 1996. Evidence for a novel cytoplasmic tRNA-protein complex containing the KH-multidomain protein vigilin. Biochem. J. 320:247-252.
    • (1996) Biochem. J. , vol.320 , pp. 247-252
    • Kruse, C.1    Grünweiler, A.2    Notbohm, H.3    Kügler, S.4    Purschke, W.G.5    Müller, P.K.6
  • 35
    • 0343113370 scopus 로고    scopus 로고
    • Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus
    • Kügler, S., A. Grünweller, C. Probst, M. Klinger, P. K. Müller, and C. Kruse. 1996. Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus. FEBS Lett. 382:330-334.
    • (1996) FEBS Lett. , vol.382 , pp. 330-334
    • Kügler, S.1    Grünweller, A.2    Probst, C.3    Klinger, M.4    Müller, P.K.5    Kruse, C.6
  • 36
    • 0021174049 scopus 로고
    • Gene transfer, expression, and molecular cloning of the human transferrin receptor gene
    • Kühn, L. C., A. McClelland, and F. H. Ruddle. 1984. Gene transfer, expression, and molecular cloning of the human transferrin receptor gene. Cell 37:95-103.
    • (1984) Cell , vol.37 , pp. 95-103
    • Kühn, L.C.1    McClelland, A.2    Ruddle, F.H.3
  • 38
    • 0029076374 scopus 로고
    • Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains
    • Leffers, H., K. Dejgaard, and J. E. Celis. 1995. Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains. Eur. J. Biochem. 230:447-453.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 447-453
    • Leffers, H.1    Dejgaard, K.2    Celis, J.E.3
  • 39
    • 0027314350 scopus 로고
    • Hel-N1: An autoimmune RNA-binding protein with specificity for 3′ uridylate-rich untranslated regions of growth factor mRNAs
    • Levine, T. D., F. Gao, P. H. King, L. G. Andrews, and J. D. Keene. 1993. Hel-N1: an autoimmune RNA-binding protein with specificity for 3′ uridylate-rich untranslated regions of growth factor mRNAs. Mol. Cell. Biol. 13:3494-3504.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3494-3504
    • Levine, T.D.1    Gao, F.2    King, P.H.3    Andrews, L.G.4    Keene, J.D.5
  • 40
    • 0029072697 scopus 로고
    • The product of the pleiotropic Escherichia coli gene csrA modulates glycogen biosynthesis via effects on mRNA stability
    • Liu, M. Y., H. Yang, and T. Romeo. 1995. The product of the pleiotropic Escherichia coli gene csrA modulates glycogen biosynthesis via effects on mRNA stability. J. Bacteriol. 177:2663-2672.
    • (1995) J. Bacteriol. , vol.177 , pp. 2663-2672
    • Liu, M.Y.1    Yang, H.2    Romeo, T.3
  • 41
    • 0021931884 scopus 로고
    • Monoclonal antibody recognition of multiple forms of estrogen receptor tagged with [125I]methoxy-iodovinyl estradiol in ovarian carcinomas
    • Lorincz, M. A., J. A. Holt, and G. L. Greene. 1985. Monoclonal antibody recognition of multiple forms of estrogen receptor tagged with [125I]methoxy-iodovinyl estradiol in ovarian carcinomas. J. Clin. Endocrinol. Metab. 61:412-417.
    • (1985) J. Clin. Endocrinol. Metab. , vol.61 , pp. 412-417
    • Lorincz, M.A.1    Holt, J.A.2    Greene, G.L.3
  • 42
    • 0026515523 scopus 로고
    • Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein
    • Matunis, M. J., W. M. Michael, and G. Dreyfuss. 1992. Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein. Mol. Cell. Biol. 12:164-171.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 164-171
    • Matunis, M.J.1    Michael, W.M.2    Dreyfuss, G.3
  • 44
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Müllner, E. W., B. Neupert, and L. C. Kühn. 1989. A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58:373-382.
    • (1989) Cell , vol.58 , pp. 373-382
    • Müllner, E.W.1    Neupert, B.2    Kühn, L.C.3
  • 45
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco, G., G. Stier, C. Joseph, M. A. Castiglione Morelli, M. Nilges, T. J. Gibson, and A. Pastore. 1996. Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell 85: 237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Morelli, M.A.C.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 46
    • 0028919596 scopus 로고
    • Binding of a cell-type-specific RNA splicing factor to its target regulatory sequence
    • Nandabalan, K., and G. S. Roeder. 1995. Binding of a cell-type-specific RNA splicing factor to its target regulatory sequence. Mol. Cell. Biol. 15:1953-1960.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1953-1960
    • Nandabalan, K.1    Roeder, G.S.2
  • 47
    • 0027335767 scopus 로고
    • Vigilin is a cytoplasmic protein. A study on its expression in primary cells and in established cell lines of different species
    • Neu-Yilik, G., H. Zorbas, T. R. Gloe, H. M. Raabe, T. A. Hopp-Christensen, and P. K. Müller. 1993. Vigilin is a cytoplasmic protein. A study on its expression in primary cells and in established cell lines of different species. Eur. J. Biochem. 213:727-736.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 727-736
    • Neu-Yilik, G.1    Zorbas, H.2    Gloe, T.R.3    Raabe, H.M.4    Hopp-Christensen, T.A.5    Müller, P.K.6
  • 48
    • 0025064122 scopus 로고
    • Estradiol and estrogen receptor- Dependent stabilization of a minivitellogenin mRNA lacking 5,100 nucleotides of coding sequence
    • Nielsen, D. A., and D. J. Shapiro. 1990. Estradiol and estrogen receptor-dependent stabilization of a minivitellogenin mRNA lacking 5,100 nucleotides of coding sequence. Mol. Cell. Biol. 10:371-376.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 371-376
    • Nielsen, D.A.1    Shapiro, D.J.2
  • 49
    • 0027198073 scopus 로고
    • Expression of vigilin in chicken cartilage and bone
    • Plenz, G., Y. Gan, H. M. Raabe, and P. K. Müller. 1993. Expression of vigilin in chicken cartilage and bone. Cell Tissue Res 273:381-389.
    • (1993) Cell Tissue Res , vol.273 , pp. 381-389
    • Plenz, G.1    Gan, Y.2    Raabe, H.M.3    Müller, P.K.4
  • 50
    • 0028266032 scopus 로고
    • The human vigilin gene: Identification, chromosomal localization and expression pattern
    • Plenz, G., S. Kügler, S. Schnittger, H. Rieder, C. Fonatsch, and P. K. Müller. 1994. The human vigilin gene: identification, chromosomal localization and expression pattern. Hum. Genet. 93:575-582.
    • (1994) Hum. Genet. , vol.93 , pp. 575-582
    • Plenz, G.1    Kügler, S.2    Schnittger, S.3    Rieder, H.4    Fonatsch, C.5    Müller, P.K.6
  • 51
    • 0026668004 scopus 로고
    • Down-regulation of messenger ribonucleic acid (mRNA) for the estrogen receptor (ER) by phorbol ester requires ongoing RNA synthesis but not protein synthesis. Is hormonal control of ER mRNA degradation mediated by an RNA molecule?
    • Ree, A. H., H. K. Knutsen, B. F. Landmark, W. Eskild, and V. Hansson. 1992. Down-regulation of messenger ribonucleic acid (mRNA) for the estrogen receptor (ER) by phorbol ester requires ongoing RNA synthesis but not protein synthesis. Is hormonal control of ER mRNA degradation mediated by an RNA molecule? Endocrinology 131:1810-1814.
    • (1992) Endocrinology , vol.131 , pp. 1810-1814
    • Ree, A.H.1    Knutsen, H.K.2    Landmark, B.F.3    Eskild, W.4    Hansson, V.5
  • 52
    • 0029165020 scopus 로고
    • mRNA stability in mammalian cells
    • Ross, J. 1995. mRNA stability in mammalian cells. Microbiol. Rev. 59:423-450.
    • (1995) Microbiol. Rev. , vol.59 , pp. 423-450
    • Ross, J.1
  • 53
  • 54
    • 0026725013 scopus 로고
    • Complete cDNA sequence of chicken vigilin, a novel protein with amplified and evolutionary conserved domains
    • Schmidt, C., B. Henkel, E. Poschl, H. Zorbas, W. G. Purschke, T. R. Gloe, and P. K. Müller. 1992. Complete cDNA sequence of chicken vigilin, a novel protein with amplified and evolutionary conserved domains. Eur. J. Biochem. 206:625-634.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 625-634
    • Schmidt, C.1    Henkel, B.2    Poschl, E.3    Zorbas, H.4    Purschke, W.G.5    Gloe, T.R.6    Müller, P.K.7
  • 55
    • 0028914042 scopus 로고
    • Soma-specific expression and cloning of PSI, a negative regulator of P element pre-mRNA splicing
    • Siebel, C. W., A. Admon, and D. C. Rio. 1995. Soma-specific expression and cloning of PSI, a negative regulator of P element pre-mRNA splicing. Genes Dev. 9:269-283.
    • (1995) Genes Dev. , vol.9 , pp. 269-283
    • Siebel, C.W.1    Admon, A.2    Rio, D.C.3
  • 56
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh, R., J. Valcarcel, and M. R. Green. 1995. Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science 268:1173-1176.
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcarcel, J.2    Green, M.R.3
  • 57
    • 0028236525 scopus 로고
    • Essential role for KH domains in RNA binding: Impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome
    • Siomi, H., M. Choi, M. C. Siomi, R. L. Nussbaum, and G. Dreyfuss. 1994. Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome. Cell 77:33-39.
    • (1994) Cell , vol.77 , pp. 33-39
    • Siomi, H.1    Choi, M.2    Siomi, M.C.3    Nussbaum, R.L.4    Dreyfuss, G.5
  • 58
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi, H., M. J. Matunis, W. M. Michael, and G. Dreyfuss. 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
  • 60
    • 0029972935 scopus 로고    scopus 로고
    • Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them
    • Siomi, M. C., Y. Zhang, H. Siomi, and G. Dreyfuss. 1996. Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them. Mol. Cell. Biol. 16:3825-3832.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3825-3832
    • Siomi, M.C.1    Zhang, Y.2    Siomi, H.3    Dreyfuss, G.4
  • 61
    • 0024009108 scopus 로고
    • Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities
    • Swanson, M. S., and G. Dreyfuss. 1988. Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol. Cell. Biol. 8:2237-2241.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2237-2241
    • Swanson, M.S.1    Dreyfuss, G.2
  • 62
    • 0029064220 scopus 로고
    • The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities
    • Tacke, R., and J. L. Manley. 1995. The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities. EMBO J. 14:3540-3551.
    • (1995) EMBO J. , vol.14 , pp. 3540-3551
    • Tacke, R.1    Manley, J.L.2
  • 63
    • 0030920331 scopus 로고    scopus 로고
    • RNA recognition by the human polyadenylation factor CstF
    • Takagaki, Y., and J. L. Manley. 1997. RNA recognition by the human polyadenylation factor CstF. Mol. Cell. Biol. 17:3907-3914.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3907-3914
    • Takagaki, Y.1    Manley, J.L.2
  • 64
    • 0025863411 scopus 로고
    • U1-snRNP-A protein selects a ten nucleotide consensus sequence from a degenerate RNA pool presented in various structural contexts
    • Tsai, D. E., D. S. Harper, and J. D. Keene. 1991. U1-snRNP-A protein selects a ten nucleotide consensus sequence from a degenerate RNA pool presented in various structural contexts. Nucleic Acids Res. 19:4931-4936.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4931-4936
    • Tsai, D.E.1    Harper, D.S.2    Keene, J.D.3
  • 65
    • 0025372284 scopus 로고
    • Autogenous translational operator recognized by bacteriophage T4 DNA polymerase
    • Tuerk, C., S. Eddy, D. Parma, and L. Gold. 1990. Autogenous translational operator recognized by bacteriophage T4 DNA polymerase. J. Mol. Biol. 213:749-761.
    • (1990) J. Mol. Biol. , vol.213 , pp. 749-761
    • Tuerk, C.1    Eddy, S.2    Parma, D.3    Gold, L.4
  • 66
    • 0030772027 scopus 로고    scopus 로고
    • Sex-lethal interactions with protein and RNA. Roles of glycine-rich and RNA binding domains
    • Wang, J., Z. Dong, and L. R. Bell. 1997. Sex-lethal interactions with protein and RNA. Roles of glycine-rich and RNA binding domains. J. Biol. Chem. 272:22227-22235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22227-22235
    • Wang, J.1    Dong, Z.2    Bell, L.R.3
  • 67
    • 0028963413 scopus 로고
    • P62 association with RNA is regulated by tyrosine phosphorylation
    • Wang, L. L., S. Richard, and A. S. Shaw. 1995. P62 association with RNA is regulated by tyrosine phosphorylation. J. Biol. Chem. 270:2010-2013.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2010-2013
    • Wang, L.L.1    Richard, S.2    Shaw, A.S.3
  • 68
    • 0029814694 scopus 로고    scopus 로고
    • Complementary change in cis determinants and trans factors in the evolution of an mRNP stability complex
    • Wang, X., and S. A. Liebhaber. 1996. Complementary change in cis determinants and trans factors in the evolution of an mRNP stability complex. EMBO J. 15:5040-5051.
    • (1996) EMBO J. , vol.15 , pp. 5040-5051
    • Wang, X.1    Liebhaber, S.A.2
  • 69
    • 0029135214 scopus 로고
    • Scp160p, a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum, is necessary for maintenance of exact ploidy
    • Wintersberger, U., C. Kühne, and A. Karwan. 1995. Scp160p, a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum, is necessary for maintenance of exact ploidy. Yeast 11:929-944.
    • (1995) Yeast , vol.11 , pp. 929-944
    • Wintersberger, U.1    Kühne, C.2    Karwan, A.3
  • 70
    • 0024806949 scopus 로고
    • Computer prediction of RNA structure
    • Zuker, M. 1989. Computer prediction of RNA structure. Methods Enzymol. 180:262-288.
    • (1989) Methods Enzymol. , vol.180 , pp. 262-288
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.