메뉴 건너뛰기




Volumn 430, Issue 3, 2010, Pages 379-392

Functional diversity of the hnRNPs: Past, present and perspectives

Author keywords

Functional divergence; Heterogeneous nuclear ribonucleoprotein (hnRNP); RNA binding protein; Structural divergence

Indexed keywords

NUCLEIC ACIDS; RNA;

EID: 77956687928     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100396     Document Type: Review
Times cited : (420)

References (205)
  • 2
    • 0017744030 scopus 로고
    • Identification and characterization of packaging proteins of core 40S hnRNP particles
    • Beyer, A. L., Christensen, M. E., Walker, B. W. and Lestourgeon, W. M. (1977) Identification and characterization of packaging proteins of core 40S hnRNP particles. Cell 11, 127-138
    • (1977) Cell , vol.11 , pp. 127-138
    • Beyer, A.L.1    Christensen, M.E.2    Walker, B.W.3    Lestourgeon, W.M.4
  • 3
    • 0019464091 scopus 로고
    • Specificity in the interaction of hnRNA and mRNA with proteins as revealed by in vivo cross linking
    • DOI 10.1016/0014-5793(81)81125-8
    • van Eekelen, C. A., Riemen, T. and Van Venrooij, W. J. (1981) Specificity in the interaction of heterogeneous nuclear RNA and messenger RNA with proteins as revealed by in-vivo cross linking. FEBS Lett. 130, 223-226 (Pubitemid 11008560)
    • (1981) FEBS Letters , vol.130 , Issue.2 , pp. 223-226
    • Van Eekelen, C.A.1    Riemen, T.2    Van Venrooij, W.J.3
  • 4
    • 0023955859 scopus 로고
    • Immunopurification of heterogeneous nuclear ribonucleoprotein-particles reveals an assortment of RNA-binding proteins
    • Pinol-Roma, S., Choi, Y. D., Matunis, M. J. and Dreyfuss, G. (1988) Immunopurification of heterogeneous nuclear ribonucleoprotein-particles reveals an assortment of RNA-binding proteins. Genes Dev. 2, 215-227
    • (1988) Genes Dev. , vol.2 , pp. 215-227
    • Pinol-Roma, S.1    Choi, Y.D.2    Matunis, M.J.3    Dreyfuss, G.4
  • 5
    • 0025964204 scopus 로고
    • RNA-binding domain of the A-protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR-spectroscopy is structurally similar to ribosomal-proteins
    • Hoffman, D. W., Query, C. C., Golden, B. L., White, S. W. and Keene, J. D. (1991) RNA-binding domain of the A-protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR-spectroscopy is structurally similar to ribosomal-proteins. Proc. Natl. Acad. Sci. U.S.A. 88, 2495-2499
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2495-2499
    • Hoffman, D.W.1    Query, C.C.2    Golden, B.L.3    White, S.W.4    Keene, J.D.5
  • 6
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains - Conservation in metazoan pre-messenger-RNA 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-messenger-RNA 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
  • 7
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: Modular design for efficient function
    • Lunde, B. M., Moore, C. and Varani, G. (2007) RNA-binding proteins: modular design for efficient function. Nat. Rev. Mol. Cell Biol. 8, 479-490
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 8
    • 18544377013 scopus 로고    scopus 로고
    • The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression
    • Maris, C., Dominguez, C. and Allain, F. H.T. (2005) The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression. FEBS J. 272, 2118-2131
    • (2005) FEBS J. , vol.272 , pp. 2118-2131
    • Maris, C.1    Dominguez, C.2    Allain, F.H.T.3
  • 9
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde, R., Edwards, L. and Regan, L. (2008) Structure and function of KH domains. FEBS J. 275, 2712-2726
    • (2008) FEBS J. , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 10
    • 33747085899 scopus 로고    scopus 로고
    • NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: A novel mode of RNA recognition
    • Dominguez, C. and Allain, F. H. T. (2006) NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition. Nucleic Acids Res. 34, 3634-3645
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3634-3645
    • Dominguez, C.1    Allain, F.H.T.2
  • 12
    • 0026740718 scopus 로고
    • Primary structure and binding-activity of the hnRNP U-protein: Binding RNA through RGG box
    • Kiledjian, M. and Dreyfuss, G. (1992) Primary structure and binding-activity of the hnRNP U-protein: binding RNA through RGG box. EMBO J. 11, 2655-2664
    • (1992) EMBO J. , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 14
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma, S. and Dreyfuss, G. (1992) Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355, 730-732
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 15
    • 0035827321 scopus 로고    scopus 로고
    • The rules and roles of nucleocytoplasmic shuttling proteins
    • Gama-Carvalho, M. and Carmo-Fonseca, M. (2001) The rules and roles of nucleocytoplasmic shuttling proteins. FEBS Lett. 498, 157-163
    • (2001) FEBS Lett. , vol.498 , pp. 157-163
    • Gama-Carvalho, M.1    Carmo-Fonseca, M.2
  • 16
    • 0034607554 scopus 로고    scopus 로고
    • Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm
    • Kim, J. H., Hahm, B., Kim, Y. K., Choi, M. Y. and Jang, S. K. (2000) Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. J. Mol. Biol. 298, 395-405
    • (2000) J. Mol. Biol. , vol.298 , pp. 395-405
    • Kim, J.H.1    Hahm, B.2    Kim, Y.K.3    Choi, M.Y.4    Jang, S.K.5
  • 17
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • DOI 10.1016/j.neuron.2004.07.022, PII S0896627304004635
    • Kanai, Y., Dohmae, N. and Hirokawa, N. (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43, 513-525 (Pubitemid 39094678)
    • (2004) Neuron , vol.43 , Issue.4 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 18
    • 58149517727 scopus 로고    scopus 로고
    • hnRNPs relocalize to the cytoplasm following infection with vesicular stomatitis virus
    • Kneller, E. L. P., Connor, J. H. and Lyles, D. S. (2009) hnRNPs relocalize to the cytoplasm following infection with vesicular stomatitis virus. J. Virol. 83, 770-780
    • (2009) J. Virol. , vol.83 , pp. 770-780
    • Kneller, E.L.P.1    Connor, J.H.2    Lyles, D.S.3
  • 19
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: Master regulators of gene expression
    • Long, J. C. and Caceres, J. F. (2009) The SR protein family of splicing factors: master regulators of gene expression. Biochem. J. 417, 15-27
    • (2009) Biochem. J. , vol.417 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 20
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley, B. R. (2000) Sorting out the complexity of SR protein functions. RNA 6, 1197-1211
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 21
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres, J. F., Screaton, G. R. and Krainer, A. R. (1998) A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev. 12, 55-66
    • (1998) Genes Dev. , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 22
    • 0034791334 scopus 로고    scopus 로고
    • Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: Candidate intermediates in formation and export of mRNA
    • Mili, S., Shu, H. J., Zhao, Y. M. and Pinol-Roma, S. (2001) Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA. Mol. Cell. Biol. 21, 7307-7319
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7307-7319
    • Mili, S.1    Shu, H.J.2    Zhao, Y.M.3    Pinol-Roma, S.4
  • 24
    • 0024009108 scopus 로고
    • Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein-particles by RNA-binding specificities
    • Swanson, M. S. and Dreyfuss, G. (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
  • 25
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. and Gold, L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage-T4 DNA-polymerase. Science 249, 505-510 (Pubitemid 120031634)
    • (1990) Science , vol.249 , Issue.4968 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 26
    • 46549085105 scopus 로고    scopus 로고
    • Unwinding RNA's secrets: Advances in the biology, physics, and modeling of complex RNAs
    • Chu, V. B. and Herschlag, D. (2008) Unwinding RNA's secrets: advances in the biology, physics, and modeling of complex RNAs. Curr. Opin. Struct. Biol. 18, 305-314
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 305-314
    • Chu, V.B.1    Herschlag, D.2
  • 27
    • 1242274330 scopus 로고    scopus 로고
    • A guide to ions and RNA structure
    • Draper, D. E. (2004) A guide to ions and RNA structure. RNA 10, 335-343
    • (2004) RNA , vol.10 , pp. 335-343
    • Draper, D.E.1
  • 28
    • 0024835141 scopus 로고
    • A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts
    • Pinol-Roma, S., Swanson, M. S., Gall, J. G. and Dreyfuss, G. (1989) A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts. J. Cell Biol. 109, 2575-2587
    • (1989) J. Cell Biol. , vol.109 , pp. 2575-2587
    • Pinol-Roma, S.1    Swanson, M.S.2    Gall, J.G.3    Dreyfuss, G.4
  • 29
    • 0026660025 scopus 로고
    • hnRNP-I, the polypyrimidine tract-binding protein: Distinct nuclear-localization and association with hnRNAs
    • Ghetti, A., Pinolroma, S., Michael, W. M., Morandi, C. and Dreyfuss, G. (1992) hnRNP-I, the polypyrimidine tract-binding protein: distinct nuclear-localization and association with hnRNAs. Nucleic Acids Res. 20, 3671-3678
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3671-3678
    • Ghetti, A.1    Pinolroma, S.2    Michael, W.M.3    Morandi, C.4    Dreyfuss, G.5
  • 30
    • 0028356054 scopus 로고
    • The hnRNP F protein: Unique primary structure, nucleic acid-binding properties, and subcellular localization
    • Matunis, M. J., Xing, J. and Dreyfuss, G. (1994) The hnRNP F-protein: unique primary structure, nucleic acid-binding properties, and subcellular-localization. Nucleic Acids Res. 22, 1059-1067 (Pubitemid 24162170)
    • (1994) Nucleic Acids Research , vol.22 , Issue.6 , pp. 1059-1067
    • Matunis, M.J.1    Xing, J.2    Dreyfuss, G.3
  • 31
    • 0029934811 scopus 로고    scopus 로고
    • The human hnRNP-M proteins: Structure and relation with early heat shock-induced splicing arrest and chromosome mapping
    • Gattoni, R., Mahe, D., Mahl, P., Fischer, N., Mattei, M. G., Stevenin, J. and Fuchs, J. P. (1996) The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucleic Acids Res. 24, 2535-2542
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2535-2542
    • Gattoni, R.1    Mahe, D.2    Mahl, P.3    Fischer, N.4    Mattei, M.G.5    Stevenin, J.6    Fuchs, J.P.7
  • 32
    • 0034701246 scopus 로고    scopus 로고
    • RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2 beta and affect splicing
    • Venables, J. P., Elliott, D. J., Makarova, O. V., Makarov, E. M., Cooke, H. J. and Eperon, I. C. (2000) RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2 beta and affect splicing. Human Mol. Gen. 9, 685-694
    • (2000) Human Mol. Gen. , vol.9 , pp. 685-694
    • Venables, J.P.1    Elliott, D.J.2    Makarova, O.V.3    Makarov, E.M.4    Cooke, H.J.5    Eperon, I.C.6
  • 33
    • 0242333893 scopus 로고    scopus 로고
    • Surface expression of heterogeneous nuclear RNA binding protein M4 on Kupffer cell relates to its function as a carcinoembryonic antigen receptor
    • Bajenova, O., Stolper, E., Gapon, S., Sundina, N., Zimmer, R. and Thomas, P. (2003) Surface expression of heterogeneous nuclear RNA binding protein M4 on Kupffer cell relates to its function as a carcinoembryonic antigen receptor. Exp. Cell Res. 291, 228-241
    • (2003) Exp. Cell Res. , vol.291 , pp. 228-241
    • Bajenova, O.1    Stolper, E.2    Gapon, S.3    Sundina, N.4    Zimmer, R.5    Thomas, P.6
  • 34
    • 0034737604 scopus 로고    scopus 로고
    • SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms
    • Mizutani, A., Fukuda, M., Ibata, K., Shiraishi, Y. and Mikoshiba, K. (2000) SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms. J. Biol. Chem. 275, 9823-9831
    • (2000) J. Biol. Chem. , vol.275 , pp. 9823-9831
    • Mizutani, A.1    Fukuda, M.2    Ibata, K.3    Shiraishi, Y.4    Mikoshiba, K.5
  • 35
    • 0141640944 scopus 로고    scopus 로고
    • A molecular mechanism for mRNA trafficking in neuronal dendrites
    • Shan, J. G., Munro, T. P., Barbarese, E., Carson, J. H. and Smith, R. (2003) A molecular mechanism for mRNA trafficking in neuronal dendrites. J. Neurosci. 23, 8859-8866 (Pubitemid 37210898)
    • (2003) Journal of Neuroscience , vol.23 , Issue.26 , pp. 8859-8866
    • Shan, J.1    Munro, T.P.2    Barbarese, E.3    Carson, J.H.4    Smith, R.5
  • 36
    • 11144229414 scopus 로고    scopus 로고
    • An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites
    • Bannai, H., Fukatsu, K., Mizutani, A., Natsume, T., Iemura, S., Ikegami, T., Inouie, T. and Mikoshiba, K. (2004) An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites. J. Biol. Chem. 279, 53427-53434
    • (2004) J. Biol. Chem. , vol.279 , pp. 53427-53434
    • Bannai, H.1    Fukatsu, K.2    Mizutani, A.3    Natsume, T.4    Iemura, S.5    Ikegami, T.6    Inouie, T.7    Mikoshiba, K.8
  • 37
    • 48249083430 scopus 로고    scopus 로고
    • The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
    • Andersson, M. K., Stahlberg, A., Arvidsson, Y., Olofsson, A., Semb, H., Stenman, G., Nilsson, O. and Aman, P. (2008) The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response. BMC Cell Biol. 9, 37
    • (2008) BMC Cell Biol. , vol.9 , pp. 37
    • Andersson, M.K.1    Stahlberg, A.2    Arvidsson, Y.3    Olofsson, A.4    Semb, H.5    Stenman, G.6    Nilsson, O.7    Aman, P.8
  • 38
    • 0028157139 scopus 로고
    • The C-protein tetramer binds 230 to 240 nucleotides of premessenger RNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein- particles
    • Huang, M., Rech, J. E., Northington, S. J., Flicker, P. F., Mayeda, A., Krainer, A. R. and Lestourgeon, W. M. (1994) The C-protein tetramer binds 230 to 240 nucleotides of premessenger RNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein-particles. Mol. Cell. Biol. 14, 518-533
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 518-533
    • Huang, M.1    Rech, J.E.2    Northington, S.J.3    Flicker, P.F.4    Mayeda, A.5    Krainer, A.R.6    Lestourgeon, W.M.7
  • 39
    • 0034623948 scopus 로고    scopus 로고
    • Binding of an RNA trafficking response element to heterogeneous nuclear ribonucleoproteins A1 and A2
    • Shan, J. G., Moran-Jones, K., Munro, T. P., Kidd, G. J., Winzor, D. J., Hoek, K. S. and Smith, B. (2000) Binding of an RNA trafficking response element to heterogeneous nuclear ribonucleoproteins A1 and A2. J. Biol. Chem. 275, 38286-38295
    • (2000) J. Biol. Chem. , vol.275 , pp. 38286-38295
    • Shan, J.G.1    Moran-Jones, K.2    Munro, T.P.3    Kidd, G.J.4    Winzor, D.J.5    Hoek, K.S.6    Smith, B.7
  • 40
    • 0037124046 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A3, a novel RNA trafficking response element-binding protein
    • Ma, A. S. W., Moran-Jones, K., Shan, J., Munro, T. P., Snee, M. J., Hoek, K. S. and Smith, R. (2002) Heterogeneous nuclear ribonucleoprotein A3, a novel RNA trafficking response element-binding protein. J. Biol. Chem. 277, 18010-18020
    • (2002) J. Biol. Chem. , vol.277 , pp. 18010-18020
    • Ma, A.S.W.1    Moran-Jones, K.2    Shan, J.3    Munro, T.P.4    Snee, M.J.5    Hoek, K.S.6    Smith, R.7
  • 41
    • 0030952320 scopus 로고    scopus 로고
    • An intron element modulating 5′ splice site selection in the hnRNP A1 pre-mRNA interacts with hnRNP A1
    • Chabot, B., Blanchette, M., Lapierre, I. and LaBranche, H. (1997) An intron element modulating 5′ splice site selection in the hnRNP A1 pre-mRNA interacts with hnRNP A1. Mol. Cell. Biol. 17, 1776-1786
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1776-1786
    • Chabot, B.1    Blanchette, M.2    Lapierre, I.3    LaBranche, H.4
  • 42
    • 0037119437 scopus 로고    scopus 로고
    • Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5′ splice site selection in the hnRNP A1 mRNA precursor
    • Hutchison, S., LeBel, C., Blanchette, M. and Chabot, B. (2002) Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5′ splice site selection in the hnRNP A1 mRNA precursor. J. Biol. Chem. 277, 29745-29752
    • (2002) J. Biol. Chem. , vol.277 , pp. 29745-29752
    • Hutchison, S.1    LeBel, C.2    Blanchette, M.3    Chabot, B.4
  • 43
    • 21844480060 scopus 로고    scopus 로고
    • A combinatorial code for splicing silencing: UAGG and GGGG motifs
    • Han, K., Yeo, G., An, P., Burge, C. B. and Grabowski, P. J. (2005) A combinatorial code for splicing silencing: UAGG and GGGG motifs. PLoS Biol. 3, 843-860
    • (2005) PLoS Biol. , vol.3 , pp. 843-860
    • Han, K.1    Yeo, G.2    An, P.3    Burge, C.B.4    Grabowski, P.J.5
  • 44
    • 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
  • 45
    • 0026543785 scopus 로고
    • Regulation of alternative pre-messenger-RNA splicing by hnRNP-A1 and splicing factor-SF2
    • Mayeda, A. and Krainer, A. R. (1992) Regulation of alternative pre-messenger-RNA splicing by hnRNP-A1 and splicing factor-SF2. Cell 68, 365-375
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 46
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda, A., Munroe, S. H., Caceres, J. F. and Krainer, A. R. (1994) Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins. EMBO J. 13, 5483-5495
    • (1994) EMBO J. , vol.13 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 47
    • 0027209184 scopus 로고
    • Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain
    • Tingley, W. G., Roche, K. W., Thompson, A. K. and Huganir, R. L. (1993) Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature 364, 70-73
    • (1993) Nature , vol.364 , pp. 70-73
    • Tingley, W.G.1    Roche, K.W.2    Thompson, A.K.3    Huganir, R.L.4
  • 48
    • 0034886605 scopus 로고    scopus 로고
    • RNA splicing at human immunodeficiency virus type 1 3′ splice site A2 is regulated by binding of hnRNP A/B proteins to an exonic splicing silencer element
    • Bilodeau, P. S., Domsic, J. K., Mayeda, A., Krainer, A. R. and Stoltzfus, C. M. (2001) RNA splicing at human immunodeficiency virus type 1 3′ splice site A2 is regulated by binding of hnRNP A/B proteins to an exonic splicing silencer element. J. Virol. 75, 8487-8497
    • (2001) J. Virol. , vol.75 , pp. 8487-8497
    • Bilodeau, P.S.1    Domsic, J.K.2    Mayeda, A.3    Krainer, A.R.4    Stoltzfus, C.M.5
  • 49
    • 0242637344 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 hnRNP A/B-Dependent exonic splicing silencer ESSV antagonizes binding of U2AF65 to viral polypyrimidine tracts
    • Domsic, J. K., Wang, Y. B., Mayeda, A., Krainer, A. R. and Stoltzfus, C. M. (2003) Human immunodeficiency virus type 1 hnRNP A/B-Dependent exonic splicing silencer ESSV antagonizes binding of U2AF65 to viral polypyrimidine tracts. Mol. Cell. Biol. 23, 8762-8772
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8762-8772
    • Domsic, J.K.1    Wang, Y.B.2    Mayeda, A.3    Krainer, A.R.4    Stoltzfus, C.M.5
  • 50
    • 0037372109 scopus 로고    scopus 로고
    • Roles for SR proteins and hnRNP A1 in the regulation of c-src exon N1
    • Rooke, N., Markovtsov, V., Cagavi, E. and Black, D. L. (2003) Roles for SR proteins and hnRNP A1 in the regulation of c-src exon N1. Mol. Cell. Biol. 23, 1874-1884
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1874-1884
    • Rooke, N.1    Markovtsov, V.2    Cagavi, E.3    Black, D.L.4
  • 51
    • 0842289003 scopus 로고    scopus 로고
    • An extended inhibitory context causes skipping of exon 7 of SMN2 in spinal muscular atrophy
    • Singh, N. N., Androphy, E. J. and Singh, R. N. (2004) An extended inhibitory context causes skipping of exon 7 of SMN2 in spinal muscular atrophy. Biochem. Biophys. Res. Commun. 315, 381-388
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 381-388
    • Singh, N.N.1    Androphy, E.J.2    Singh, R.N.3
  • 52
    • 50849133904 scopus 로고    scopus 로고
    • A proteomic comparison of immature and mature mouse gonadotrophs reveals novel differentially expressed nuclear proteins that regulate gonadotropin gene transcription and RNA splicing
    • Feng, J., Lawson, M. A. and Melamed, P. (2008) A proteomic comparison of immature and mature mouse gonadotrophs reveals novel differentially expressed nuclear proteins that regulate gonadotropin gene transcription and RNA splicing. Biol. Reprod. 79, 546-561
    • (2008) Biol. Reprod. , vol.79 , pp. 546-561
    • Feng, J.1    Lawson, M.A.2    Melamed, P.3
  • 53
    • 44749089526 scopus 로고    scopus 로고
    • The pathological splicing mutation c.6792C>G in NF1 exon 37 causes a change of tenancy between antagonistic splicing factors
    • Skoko, N., Baralle, M., Buratti, E. and Baralle, F. E. (2008) The pathological splicing mutation c.6792C>G in NF1 exon 37 causes a change of tenancy between antagonistic splicing factors. FEBS Lett. 582, 2231-2236
    • (2008) FEBS Lett. , vol.582 , pp. 2231-2236
    • Skoko, N.1    Baralle, M.2    Buratti, E.3    Baralle, F.E.4
  • 54
    • 44349135730 scopus 로고    scopus 로고
    • Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant
    • Goina, E., Skoko, N. and Pagani, F. (2008) Binding of DAZAP1 and hnRNPA1/A2 to an exonic splicing silencer in a natural BRCA1 exon 18 mutant. Mol. Cell. Biol. 28, 3850-3860
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3850-3860
    • Goina, E.1    Skoko, N.2    Pagani, F.3
  • 56
  • 57
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J. Z., Hayashi, M. K., Zhang, Y., Manche, L., Krainer, A. R. and Xu, R. M. (1999) Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev. 13, 1102-1115
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.Z.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 58
    • 0031800617 scopus 로고    scopus 로고
    • Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase
    • LaBranche, H., Dupuis, S., Ben-David, Y., Bani, M. R., Wellinger, R. J. and Chabot, B. (1998) Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase. Nat. Gen. 19, 199-202
    • (1998) Nat. Gen. , vol.19 , pp. 199-202
    • LaBranche, H.1    Dupuis, S.2    Ben-David, Y.3    Bani, M.R.4    Wellinger, R.J.5    Chabot, B.6
  • 61
    • 0037148269 scopus 로고    scopus 로고
    • A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation
    • Ford, L. P., Wright, W. E. and Shay, J. W. (2002) A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation. Oncogene 21, 580-583
    • (2002) Oncogene , vol.21 , pp. 580-583
    • Ford, L.P.1    Wright, W.E.2    Shay, J.W.3
  • 63
    • 0032510715 scopus 로고    scopus 로고
    • hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA
    • Hoek, K. S., Kidd, G. J., Carson, J. H. and Smith, R. (1998) hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA. Biochemistry 37, 7021-7029
    • (1998) Biochemistry , vol.37 , pp. 7021-7029
    • Hoek, K.S.1    Kidd, G.J.2    Carson, J.H.3    Smith, R.4
  • 65
    • 0030770987 scopus 로고    scopus 로고
    • Translocation of myelin basic protein mRNA in oligodendrocytes requires microtubules and kinesin
    • Carson, J. H., Worboys, K., Ainger, K. and Barbarese, E. (1997) Translocation of myelin basic protein mRNA in oligodendrocytes requires microtubules and kinesin. Cell Motil. Cytoskel. 38, 318-328
    • (1997) Cell Motil. Cytoskel. , vol.38 , pp. 318-328
    • Carson, J.H.1    Worboys, K.2    Ainger, K.3    Barbarese, E.4
  • 66
    • 0033607521 scopus 로고    scopus 로고
    • Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking
    • Munro, T. P., Magee, R. J., Kidd, G. J., Carson, J. H., Barbarese, E., Smith, L. M. and Smith, R. (1999) Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking. J. Biol. Chem. 274, 34389-34395
    • (1999) J. Biol. Chem. , vol.274 , pp. 34389-34395
    • Munro, T.P.1    Magee, R.J.2    Kidd, G.J.3    Carson, J.H.4    Barbarese, E.5    Smith, L.M.6    Smith, R.7
  • 67
    • 47849125619 scopus 로고    scopus 로고
    • Multiplexed dendritic targeting of alpha-calcium calmodulin-dependent protein kinase II, neurogranin, and activity-regulated cytoskeleton-associated protein RNAs by the A2 pathway
    • Gao, Y., Tatavarty, V., Korza, G., Levin, M. K. and Carson, J. H. (2008) Multiplexed dendritic targeting of alpha-calcium calmodulin-dependent protein kinase II, neurogranin, and activity-regulated cytoskeleton-associated protein RNAs by the A2 pathway. Mol. Biol. Cell 19, 2311-2327
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2311-2327
    • Gao, Y.1    Tatavarty, V.2    Korza, G.3    Levin, M.K.4    Carson, J.H.5
  • 68
    • 33746581893 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs
    • Kosturko, L. D., Maggipinto, M. J., Korza, G., Lee, J. W., Carson, J. H. and Barbarese, E. (2006) Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs. Mol. Biol. Cell 17, 3521-3533
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3521-3533
    • Kosturko, L.D.1    Maggipinto, M.J.2    Korza, G.3    Lee, J.W.4    Carson, J.H.5    Barbarese, E.6
  • 69
    • 34447115822 scopus 로고    scopus 로고
    • The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a
    • Guil, S. and Caceres, J. F. (2007) The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a. Nat. Struct. Mol. Biol. 14, 591-596
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 591-596
    • Guil, S.1    Caceres, J.F.2
  • 70
    • 33746516731 scopus 로고    scopus 로고
    • hnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • Guil, S., Long, J. C. and Caceres, J. F. (2006) hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol. Cell. Biol. 26, 5744-5758
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Caceres, J.F.3
  • 71
    • 37049030005 scopus 로고    scopus 로고
    • Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs
    • Cammas, A., Pileur, F., Bonnal, S., Lewis, S. M., Leveque, N., Holcik, M. and Vagner, S. (2007) Cytoplasmic relocalization of heterogeneous nuclear ribonucleoprotein A1 controls translation initiation of specific mRNAs. Mol. Biol. Cell 18, 5048-5059
    • (2007) Mol. Biol. Cell , vol.18 , pp. 5048-5059
    • Cammas, A.1    Pileur, F.2    Bonnal, S.3    Lewis, S.M.4    Leveque, N.5    Holcik, M.6    Vagner, S.7
  • 72
    • 0038623773 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) binding to hormone response elements: A cause of vitamin D resistance
    • Chen, H., Hewison, M., Hu, B. and Adams, J. S. (2003) Heterogeneous nuclear ribonucleoprotein (hnRNP) binding to hormone response elements: A cause of vitamin D resistance. Proc. Natl. Acad. Sci. U.S.A. 100, 6109-6114
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6109-6114
    • Chen, H.1    Hewison, M.2    Hu, B.3    Adams, J.S.4
  • 73
    • 0348224064 scopus 로고    scopus 로고
    • Interaction and stimulation of human FEN-1 nuclease activities by heterogeneous nuclear ribonucleoprotein A1 in alpha-segment processing during Okazaki fragment maturation
    • Chai, Q., Zheng, L., Zhou, M., Turchi, J. J. and Shen, B. H. (2003) Interaction and stimulation of human FEN-1 nuclease activities by heterogeneous nuclear ribonucleoprotein A1 in alpha-segment processing during Okazaki fragment maturation. Biochemistry 42, 15045-15052
    • (2003) Biochemistry , vol.42 , pp. 15045-15052
    • Chai, Q.1    Zheng, L.2    Zhou, M.3    Turchi, J.J.4    Shen, B.H.5
  • 74
    • 0038239281 scopus 로고    scopus 로고
    • Specific interaction of heterogeneous nuclear ribonucleoprotein A1 with the -219T allelic form modulates APOE promoter activity
    • Campillos, M., Lamas, J. R. N., Garcia, M. A., Bullido, M. J., Valdivieso, F. and Vazquez, J. (2003) Specific interaction of heterogeneous nuclear ribonucleoprotein A1 with the -219T allelic form modulates APOE promoter activity. Nucleic Acids Res. 31, 3063-3070
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3063-3070
    • Campillos, M.1    Lamas, J.R.N.2    Garcia, M.A.3    Bullido, M.J.4    Valdivieso, F.5    Vazquez, J.6
  • 75
    • 0022520577 scopus 로고
    • Heterogeneous nuclear ribonucleoproteins: Role in RNA splicing
    • Choi, Y. D., Grabowski, P. J., Sharp, P. A. and Dreyfuss, G. (1986) Heterogeneous nuclear ribonucleoproteins: role in RNA splicing. Science 231, 1534-1539
    • (1986) Science , vol.231 , pp. 1534-1539
    • Choi, Y.D.1    Grabowski, P.J.2    Sharp, P.A.3    Dreyfuss, G.4
  • 76
    • 0024461542 scopus 로고
    • Primary structure differences between protein-C1 and protein-C2 of HeLa 40S nuclear ribonucleoprotein-particles
    • Merrill, B. M., Barnett, S. F., Lestourgeon, W. M. and Williams, K. R. (1989) Primary structure differences between protein-C1 and protein-C2 of HeLa 40S nuclear ribonucleoprotein-particles. Nucleic Acids Res. 17, 8441-8449
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8441-8449
    • Merrill, B.M.1    Barnett, S.F.2    Lestourgeon, W.M.3    Williams, K.R.4
  • 77
    • 0034068281 scopus 로고    scopus 로고
    • hnRNP C is required for postimplantation mouse development but is dispensable for cell viability
    • Williamson, D. J., Banik-Maiti, S., DeGregori, J. and Ruley, H. E. (2000) hnRNP C is required for postimplantation mouse development but is dispensable for cell viability. Mol. Cell. Biol. 20, 4094-4105
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4094-4105
    • Williamson, D.J.1    Banik-Maiti, S.2    DeGregori, J.3    Ruley, H.E.4
  • 78
    • 0023124596 scopus 로고
    • Primary structure of human nuclear ribonucleoprotein particle C-proteins: Conservation of sequence and domain-structures in heterogeneous nuclear-RNA, messenger-RNA, and pre-ribosomal-RNA-binding proteins
    • Swanson, M. S., Nakagawa, T. Y., Levan, K. and Dreyfuss, G. (1987) Primary structure of human nuclear ribonucleoprotein particle C-proteins: conservation of sequence and domain-structures in heterogeneous nuclear-RNA, messenger-RNA, and pre-ribosomal-RNA-binding proteins. Mol. Cell. Biol. 7, 1731-1739
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1731-1739
    • Swanson, M.S.1    Nakagawa, T.Y.2    Levan, K.3    Dreyfuss, G.4
  • 79
    • 0035951294 scopus 로고    scopus 로고
    • An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: A mechanism for RNA chaperonin activity
    • Shahied, L., Braswell, E. H., LeStourgeon, W. M. and Krezel, A. M. (2001) An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity. J. Mol. Biol. 305, 817-828
    • (2001) J. Mol. Biol. , vol.305 , pp. 817-828
    • Shahied, L.1    Braswell, E.H.2    LeStourgeon, W.M.3    Krezel, A.M.4
  • 80
    • 20444371580 scopus 로고    scopus 로고
    • Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: Implications for biological function
    • Whitson, S. R., LeStourgeon, W. M. and Krezel, A. M. (2005) Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function. J. Mol. Biol. 350, 319-337
    • (2005) J. Mol. Biol. , vol.350 , pp. 319-337
    • Whitson, S.R.1    LeStourgeon, W.M.2    Krezel, A.M.3
  • 82
    • 0032798596 scopus 로고    scopus 로고
    • Differentiation-induced internal translation of c-sis mRNA: Analysis of the cis elements and their differentiation-linked binding to the hnRNP C protein
    • Sella, O., Gerlitz, G., Le, S. Y. and Elroy-Stein, O. (1999) Differentiation-induced internal translation of c-sis mRNA: analysis of the cis elements and their differentiation-linked binding to the hnRNP C protein. Mol. Cell. Biol. 19, 5429-5440
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5429-5440
    • Sella, O.1    Gerlitz, G.2    Le, S.Y.3    Elroy-Stein, O.4
  • 83
    • 0037219006 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner
    • Kim, J. H., Paek, K. Y., Choi, K. B., Kim, T. D., Hahm, B. S., Kim, K. T. and Jang, S. K. (2003) Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner. Mol. Cell. Biol. 23, 708-720
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 708-720
    • Kim, J.H.1    Paek, K.Y.2    Choi, K.B.3    Kim, T.D.4    Hahm, B.S.5    Kim, K.T.6    Jang, S.K.7
  • 85
    • 0036223676 scopus 로고    scopus 로고
    • The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
    • Makeyev, A. V. and Liebhaber, S. A. (2002) The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms. RNA 8, 265-278
    • (2002) RNA , vol.8 , pp. 265-278
    • Makeyev, A.V.1    Liebhaber, S.A.2
  • 86
    • 0033066673 scopus 로고    scopus 로고
    • An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro
    • Wang, Z. R., Day, N., Trifillis, P. and Kiledjian, M. (1999) An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro. Mol. Cell. Biol. 19, 4552-4560
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4552-4560
    • Wang, Z.R.1    Day, N.2    Trifillis, P.3    Kiledjian, M.4
  • 89
    • 0031795447 scopus 로고    scopus 로고
    • Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2
    • Ostareck-Lederer, A., Ostareck, D. H. and Hentze, M. W. (1998) Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2. Trends Biochem. Sci. 23, 409-411
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 409-411
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Hentze, M.W.3
  • 90
    • 2942628000 scopus 로고    scopus 로고
    • Bag-1 internal ribosome entry segment activity is promoted by structural changes mediated by Poly(rC) binding protein 1 and recruitment of polypyrimidine tract binding protein 1
    • Pickering, B. M., Mitchell, S. A., Spriggs, K. A., Stoneley, M. and Willis, A. E. (2004) Bag-1 internal ribosome entry segment activity is promoted by structural changes mediated by Poly(rC) binding protein 1 and recruitment of polypyrimidine tract binding protein 1. Mol. Cell. Biol. 24, 5595-5605
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5595-5605
    • Pickering, B.M.1    Mitchell, S.A.2    Spriggs, K.A.3    Stoneley, M.4    Willis, A.E.5
  • 91
    • 0030772963 scopus 로고    scopus 로고
    • mRNA silencing in erythroid differentiation: HnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end
    • Ostareck, D. H., Ostareck-Lederer, A., Wilm, M., Thiele, B. J., Mann, M. and Hentze, M. W. (1997) mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89, 597-606
    • (1997) Cell , vol.89 , pp. 597-606
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Wilm, M.3    Thiele, B.J.4    Mann, M.5    Hentze, M.W.6
  • 92
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck, D. H., Ostareck-Lederer, A., Shatsky, I. N. and Hentze, M. W. (2001) Lipoxygenase mRNA silencing in erythroid differentiation: the 3′UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104, 281-290
    • (2001) Cell , vol.104 , pp. 281-290
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Shatsky, I.N.3    Hentze, M.W.4
  • 93
    • 34347264157 scopus 로고    scopus 로고
    • Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1
    • Meng, Q., Rayala, S. K., Gururaj, A. E., Talukder, A. H., O'Malley, B. W. and Kumar, R. (2007) Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1. Proc. Natl. Acad. Sci. U.S.A. 104, 5866-5871
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 5866-5871
    • Meng, Q.1    Rayala, S.K.2    Gururaj, A.E.3    Talukder, A.H.4    O'Malley, B.W.5    Kumar, R.6
  • 94
    • 42649123361 scopus 로고    scopus 로고
    • Protein-RNA tethering: The role of poly(C) binding protein 2 in poliovirus RNA replication
    • Spear, A., Sharma, N. and Flanegan, J. B. (2008) Protein-RNA tethering: the role of poly(C) binding protein 2 in poliovirus RNA replication. Virology 374, 280-291
    • (2008) Virology , vol.374 , pp. 280-291
    • Spear, A.1    Sharma, N.2    Flanegan, J.B.3
  • 95
    • 12844269244 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K represses transcription from a cytosine/thymidine-rich element in the osteocalcin promoter
    • DOI 10.1042/BJ20040680
    • Stains, J. P., Lecanda, F., Towler, D. A. and Civitelli, R. (2005) Heterogeneous nuclear ribonucleoprotein K represses transcription from a cytosine/thymidine-rich element in the osteocalcin promoter. Biochem. J. 385, 613-623 (Pubitemid 40165096)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 613-623
    • Stains, J.P.1    Lecanda, F.2    Towler, D.A.3    Civitelli, R.4
  • 96
    • 22544464680 scopus 로고    scopus 로고
    • hnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation
    • Lynch, M., Chen, L., Ravitz, M. J., Mehtani, S., Korenblat, K., Pazin, M. J. and Schmidt, E. V. (2005) hnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation. Mol. Cell. Biol. 25, 6436-6453
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6436-6453
    • Lynch, M.1    Chen, L.2    Ravitz, M.J.3    Mehtani, S.4    Korenblat, K.5    Pazin, M.J.6    Schmidt, E.V.7
  • 97
    • 0037053297 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken beta-tropomyosin pre-mRNA
    • Expert-Bezancon, A., Le Caer, J. P. and Marie, J. (2002) Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken beta-tropomyosin pre-mRNA. J. Biol. Chem. 277, 16614-16623
    • (2002) J. Biol. Chem. , vol.277 , pp. 16614-16623
    • Expert-Bezancon, A.1    Le Caer, J.P.2    Marie, J.3
  • 98
    • 60849103086 scopus 로고    scopus 로고
    • hnRNP K interacts with RNA binding motif protein 42 and functions in the maintenance of cellular ATP level during stress conditions
    • Fukuda, T., Naiki, T., Saito, M. and Irie, K. (2009) hnRNP K interacts with RNA binding motif protein 42 and functions in the maintenance of cellular ATP level during stress conditions. Genes Cells 14, 113-128
    • (2009) Genes Cells , vol.14 , pp. 113-128
    • Fukuda, T.1    Naiki, T.2    Saito, M.3    Irie, K.4
  • 101
    • 2942623743 scopus 로고    scopus 로고
    • hnRNP K: One protein multiple processes
    • Bomsztyk, K., Denisenko, O. and Ostrowski, J. (2004) hnRNP K: one protein multiple processes. BioEssays 26, 629-638
    • (2004) BioEssays , vol.26 , pp. 629-638
    • Bomsztyk, K.1    Denisenko, O.2    Ostrowski, J.3
  • 102
    • 28944446040 scopus 로고    scopus 로고
    • HnRNP K: An HDM2 target and transcriptional coactivator of p53 in response to DNA damage
    • DOI 10.1016/j.cell.2005.09.032, PII S009286740501038X
    • Moumen, A., Masterson, P., O'Connor, M. J. and Jackson, S. P. (2005) hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage. Cell 123, 1065-1078 (Pubitemid 41785421)
    • (2005) Cell , vol.123 , Issue.6 , pp. 1065-1078
    • Moumen, A.1    Masterson, P.2    O'Connor, M.J.3    Jackson, S.P.4
  • 103
    • 33644930270 scopus 로고    scopus 로고
    • The diverse involvement of heterogeneous nuclear ribonucleoprotein K in mitochondrial response to insulin
    • Dzwonek, A., Mikula, M. and Ostrowski, J. (2006) The diverse involvement of heterogeneous nuclear ribonucleoprotein K in mitochondrial response to insulin. FEBS Lett. 580, 1839-1845
    • (2006) FEBS Lett. , vol.580 , pp. 1839-1845
    • Dzwonek, A.1    Mikula, M.2    Ostrowski, J.3
  • 105
    • 0028811668 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein-H, ribonucleoprotein-H′, and ribonucleoprotein-F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes
    • Honore, B., Rasmussen, H. H., Vorum, H., Dejgaard, K., Liu, X. D., Gromov, P., Madsen, P., Gesser, B., Tommerup, N. and Celis, J. E. (1995) Heterogeneous nuclear ribonucleoprotein-H, ribonucleoprotein-H′, and ribonucleoprotein-F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes. J. Biol. Chem. 270, 28780-28789
    • (1995) J. Biol. Chem. , vol.270 , pp. 28780-28789
    • Honore, B.1    Rasmussen, H.H.2    Vorum, H.3    Dejgaard, K.4    Liu, X.D.5    Gromov, P.6    Madsen, P.7    Gesser, B.8    Tommerup, N.9    Celis, J.E.10
  • 106
    • 0034697726 scopus 로고    scopus 로고
    • The hnRNP 2H9 gene, which is involved in the splicing reaction, is a multiply spliced gene
    • Honore, B. (2000) The hnRNP 2H9 gene, which is involved in the splicing reaction, is a multiply spliced gene. Biochim. Biophys. Acta 1492, 108-119
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 108-119
    • Honore, B.1
  • 107
    • 1242339603 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins F and H/H′ show differential expression in normal and selected cancer tissues
    • Honore, B., Baandrup, U. and Vorum, H. (2004) Heterogeneous nuclear ribonucleoproteins F and H/H′ show differential expression in normal and selected cancer tissues. Exp. Cell Res. 294, 199-209
    • (2004) Exp. Cell Res. , vol.294 , pp. 199-209
    • Honore, B.1    Baandrup, U.2    Vorum, H.3
  • 108
    • 30044446861 scopus 로고    scopus 로고
    • The hnRNPs F and H2 bind to similar sequences to influence gene expression
    • Alkan, S. A., Martincic, K. and Milcarek, C. (2006) The hnRNPs F and H2 bind to similar sequences to influence gene expression. Biochem. J. 393, 361-371
    • (2006) Biochem. J. , vol.393 , pp. 361-371
    • Alkan, S.A.1    Martincic, K.2    Milcarek, C.3
  • 109
    • 0035941211 scopus 로고    scopus 로고
    • Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H′/F/2H9 family
    • Caputi, M. and Zahler, A. M. (2001) Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H′/F/2H9 family. J. Biol. Chem. 276, 43850-43859
    • (2001) J. Biol. Chem. , vol.276 , pp. 43850-43859
    • Caputi, M.1    Zahler, A.M.2
  • 110
    • 0035145592 scopus 로고    scopus 로고
    • hnRNP F influences binding of a 64-kilodalton subunit of cleavage stimulation factor to mRNA precursors in mouse B cells
    • Veraldi, K. L., Arhin, G. K., Martincic, K., Chung-Ganster, L. H., Wilusz, J. and Milcarek, C. (2001) hnRNP F influences binding of a 64-kilodalton subunit of cleavage stimulation factor to mRNA precursors in mouse B cells. Mol. Cell. Biol. 21, 1228-1238
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1228-1238
    • Veraldi, K.L.1    Arhin, G.K.2    Martincic, K.3    Chung-Ganster, L.H.4    Wilusz, J.5    Milcarek, C.6
  • 111
    • 0032953308 scopus 로고    scopus 로고
    • hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells
    • Chou, M. Y., Rooke, N., Turck, C. W. and Black, D. L. (1999) hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells. Mol. Cell. Biol. 19, 69-77
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 69-77
    • Chou, M.Y.1    Rooke, N.2    Turck, C.W.3    Black, D.L.4
  • 112
    • 0025856790 scopus 로고
    • Characterization and molecular-cloning of polypyrimidine tract-binding protein: A component of a complex necessary for pre-messenger RNA splicing
    • Patton, J. G., Mayer, S. A., Tempst, P. and Nadalginard, B. (1991) Characterization and molecular-cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-messenger RNA splicing. Genes Dev. 5, 1237-1251
    • (1991) Genes Dev. , vol.5 , pp. 1237-1251
    • Patton, J.G.1    Mayer, S.A.2    Tempst, P.3    Nadalginard, B.4
  • 114
    • 30444459024 scopus 로고    scopus 로고
    • Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling
    • Vitali, F., Henning, A., Oberstrass, F. C., Hargous, Y., Auweter, S. D., Erat, M. and Allain, F. H. T. (2006) Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling. EMBO J. 25, 150-162
    • (2006) EMBO J. , vol.25 , pp. 150-162
    • Vitali, F.1    Henning, A.2    Oberstrass, F.C.3    Hargous, Y.4    Auweter, S.D.5    Erat, M.6    Allain, F.H.T.7
  • 115
    • 38849187162 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome
    • Sharma, S., Kohlstaedt, L. A., Damianov, A., Rio, D. C. and Black, D. L. (2008) Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome. Nat. Struct. Mol. Biol. 15, 183-191
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 183-191
    • Sharma, S.1    Kohlstaedt, L.A.2    Damianov, A.3    Rio, D.C.4    Black, D.L.5
  • 116
    • 34447536429 scopus 로고    scopus 로고
    • Repression of alpha-actinin SM exon splicing by assisted binding of PTB to the polypyrimidine tract
    • Matlin, A. J., Southby, J., Gooding, C. and Smith, C. W. J. (2007) Repression of alpha-actinin SM exon splicing by assisted binding of PTB to the polypyrimidine tract. RNA 13, 1214-1223
    • (2007) RNA , vol.13 , pp. 1214-1223
    • Matlin, A.J.1    Southby, J.2    Gooding, C.3    Smith, C.W.J.4
  • 118
    • 72149117411 scopus 로고    scopus 로고
    • Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping
    • Xue, Y., Zhou, Y., Wu, T., Zhu, T., Ji, X., Kwon, Y., Zhang, C., Yeo, G., Black, D. L., Sun, H. et al. (2009) Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping. Mol. Cell 36, 996-1006
    • (2009) Mol. Cell , vol.36 , pp. 996-1006
    • Xue, Y.1    Zhou, Y.2    Wu, T.3    Zhu, T.4    Ji, X.5    Kwon, Y.6    Zhang, C.7    Yeo, G.8    Black, D.L.9    Sun, H.10
  • 121
    • 0042808438 scopus 로고    scopus 로고
    • Novel functional role of CA repeats and hnRNP L in RNA stability
    • DOI 10.1261/rna.5660803
    • Hui, J. Y., Reither, G. and Bindereif, A. (2003) Novel functional role of CA repeats and hnRNP L in RNA stability. RNA 9, 931-936 (Pubitemid 36899236)
    • (2003) RNA , vol.9 , Issue.8 , pp. 931-936
    • Hui, J.1    Reither, G.2    Bindereif, A.3
  • 122
    • 34748892292 scopus 로고    scopus 로고
    • Combinatorial control of signal-induced exon repression by hnRNP l and PSF
    • Melton, A. A., Jackson, J., Wang, J. and Lynch, K. W. (2007) Combinatorial control of signal-induced exon repression by hnRNP l and PSF. Mol. Cell. Biol. 27, 6972-6984
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6972-6984
    • Melton, A.A.1    Jackson, J.2    Wang, J.3    Lynch, K.W.4
  • 123
    • 74749089043 scopus 로고    scopus 로고
    • Context-dependent regulatory mechanism of the splicing factor hnRNP L
    • Motta-Mena, L. B., Heyd, F. and Lynch, K. W. Context-dependent regulatory mechanism of the splicing factor hnRNP L. Mol. Cell 37, 223-234
    • Mol. Cell , vol.37 , pp. 223-234
    • Motta-Mena, L.B.1    Heyd, F.2    Lynch, K.W.3
  • 124
    • 38649129366 scopus 로고    scopus 로고
    • Diverse roles of hnRNP L in mammalian mRNA processing: A combined microarray and RNAi analysis
    • Hung, L. H., Heiner, M., Hui, J. Y., Schreiner, S., Benes, V. and Bindereif, A. (2008) Diverse roles of hnRNP L in mammalian mRNA processing: a combined microarray and RNAi analysis. RNA 14, 284-296
    • (2008) RNA , vol.14 , pp. 284-296
    • Hung, L.H.1    Heiner, M.2    Hui, J.Y.3    Schreiner, S.4    Benes, V.5    Bindereif, A.6
  • 125
    • 0036070957 scopus 로고    scopus 로고
    • Inflammation modulates the interaction of heterogeneous nuclear ribonucleoprotein (hnRNP) I/polypyrimidine tract binding protein and hnRNP L with the 3′ untranslated region of the murine inducible nitric-oxide synthase mRNA
    • Soderberg, M., Raffalli-Mathieu, F. and Lang, M. A. (2002) Inflammation modulates the interaction of heterogeneous nuclear ribonucleoprotein (hnRNP) I/polypyrimidine tract binding protein and hnRNP L with the 3′ untranslated region of the murine inducible nitric-oxide synthase mRNA. Mol. Pharmacol. 62, 423-431
    • (2002) Mol. Pharmacol. , vol.62 , pp. 423-431
    • Soderberg, M.1    Raffalli-Mathieu, F.2    Lang, M.A.3
  • 126
    • 66349083910 scopus 로고    scopus 로고
    • The hnRNA-binding proteins hnRNP L and PTB are required for efficient translation of the Cat-1 arginine/lysine transporter mRNA during amino acid starvation
    • Majumder, M., Yaman, I., Gaccioli, F., Zeenko, V. V., Wang, C. P., Caprara, M. G., Venema, R. C., Komar, A. A., Snider, M. D. and Hatzoglou, M. (2009) The hnRNA-binding proteins hnRNP L and PTB are required for efficient translation of the Cat-1 arginine/lysine transporter mRNA during amino acid starvation. Mol. Cell. Biol. 29, 2899-2912
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2899-2912
    • Majumder, M.1    Yaman, I.2    Gaccioli, F.3    Zeenko, V.V.4    Wang, C.P.5    Caprara, M.G.6    Venema, R.C.7    Komar, A.A.8    Snider, M.D.9    Hatzoglou, M.10
  • 127
    • 0033800453 scopus 로고    scopus 로고
    • Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein
    • Markovtsov, V., Nikolic, J. M., Goldman, J. A., Turck, C. W., Chou, M. Y. and Black, D. L. (2000) Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. Mol. Cell. Biol. 20, 7463-7479
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7463-7479
    • Markovtsov, V.1    Nikolic, J.M.2    Goldman, J.A.3    Turck, C.W.4    Chou, M.Y.5    Black, D.L.6
  • 129
    • 0037101846 scopus 로고    scopus 로고
    • hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta 1
    • Hofmann, Y. and Wirth, B. (2002) hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta 1. Human Mol. Gen. 11, 2037-2049
    • (2002) Human Mol. Gen. , vol.11 , pp. 2037-2049
    • Hofmann, Y.1    Wirth, B.2
  • 130
    • 0037669004 scopus 로고    scopus 로고
    • HnRNP G and Tra2 beta: Opposite effects on splicing matched by antagonism in RNA binding
    • Nasim, M. T., Chernova, T. K., Chowdhury, H. M., Yue, B. G. and Eperon, I. C. (2003) HnRNP G and Tra2 beta: opposite effects on splicing matched by antagonism in RNA binding. Human Mol. Gen. 12, 1337-1348
    • (2003) Human Mol. Gen. , vol.12 , pp. 1337-1348
    • Nasim, M.T.1    Chernova, T.K.2    Chowdhury, H.M.3    Yue, B.G.4    Eperon, I.C.5
  • 131
    • 45449118260 scopus 로고    scopus 로고
    • hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip
    • Shin, K. H., Kim, R. H., Kang, M. K. and Park, N. H. (2008) hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip. Biochem. Biophys. Res. Comm. 372, 880-885
    • (2008) Biochem. Biophys. Res. Comm. , vol.372 , pp. 880-885
    • Shin, K.H.1    Kim, R.H.2    Kang, M.K.3    Park, N.H.4
  • 132
    • 47249104647 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein G, nitric oxide, and oral carcinogenesis
    • Shin, K. H., Kang, M. K. and Park, N. H. (2008) Heterogeneous nuclear ribonucleoprotein G, nitric oxide, and oral carcinogenesis. Nitric Oxide 19, 125-132
    • (2008) Nitric Oxide , vol.19 , pp. 125-132
    • Shin, K.H.1    Kang, M.K.2    Park, N.H.3
  • 136
    • 33744792903 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive effect against oral squamous cell carcinoma cells
    • Shin, K. H., Kang, M. K., Kim, R. H., Christensen, R. and Park, N. H. (2006) Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive effect against oral squamous cell carcinoma cells. Clin. Cancer Res. 12, 3222-3228
    • (2006) Clin. Cancer Res. , vol.12 , pp. 3222-3228
    • Shin, K.H.1    Kang, M.K.2    Kim, R.H.3    Christensen, R.4    Park, N.H.5
  • 137
    • 0034634614 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein A1 is part of an exon-specific splice-silencing complex controlled by oncogenic signaling pathways
    • Matter, N., Marx, M., Weg-Remers, S., Ponta, H., Herrlich, P. and Konig, H. (2000) Heterogeneous ribonucleoprotein A1 is part of an exon-specific splice-silencing complex controlled by oncogenic signaling pathways. J. Biol. Chem. 275, 35353-35360
    • (2000) J. Biol. Chem. , vol.275 , pp. 35353-35360
    • Matter, N.1    Marx, M.2    Weg-Remers, S.3    Ponta, H.4    Herrlich, P.5    Konig, H.6
  • 138
    • 0028867814 scopus 로고
    • The generally expressed hnRNP-F is involved in a neural-specific pre-messenger-RNA splicing event
    • Min, H. S., Chan, R. C. and Black, D. L. (1995) The generally expressed hnRNP-F is involved in a neural-specific pre-messenger-RNA splicing event. Genes Dev. 9, 2659-2671
    • (1995) Genes Dev. , vol.9 , pp. 2659-2671
    • Min, H.S.1    Chan, R.C.2    Black, D.L.3
  • 139
    • 0028909518 scopus 로고
    • Cellular nucleic-acid binding-protein regulates the CT element of the human c-myc protooncogene
    • Michelotti, E. F., Tomonaga, T., Krutzsch, H. and Levens, D. (1995) Cellular nucleic-acid binding-protein regulates the CT element of the human c-myc protooncogene. J. Biol. Chem. 270, 9494-9499
    • (1995) J. Biol. Chem. , vol.270 , pp. 9494-9499
    • Michelotti, E.F.1    Tomonaga, T.2    Krutzsch, H.3    Levens, D.4
  • 140
    • 0032479980 scopus 로고    scopus 로고
    • TLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis
    • DOI 10.1093/emboj/17.15.4442
    • Perrotti, D., Bonatti, S., Trotta, R., Martinez, R., Skorski, T., Salomoni, P., Grassilli, E., Iozzo, R. V., Cooper, D. R. and Calabretta, B. (1998) TLS/FUS, a pro-oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL-mediated leukemogenesis. EMBO J. 17, 4442-4455 (Pubitemid 28362633)
    • (1998) EMBO Journal , vol.17 , Issue.15 , pp. 4442-4455
    • Perrotti, D.1    Bonatti, S.2    Trotta, R.3    Martinez, R.4    Skorski, T.5    Salomoni, P.6    Grassilli, E.7    Iozzo, R.V.8    Cooper, D.R.9    Calabretta, B.10
  • 141
    • 0034053964 scopus 로고    scopus 로고
    • TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins
    • Yang, L., Embree, L. J. and Hickstein, D. D. (2000) TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins. Mol. Cell. Biol. 20, 3345-3354
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3345-3354
    • Yang, L.1    Embree, L.J.2    Hickstein, D.D.3
  • 143
    • 58249116717 scopus 로고    scopus 로고
    • The myxoid liposarcoma FUS-DDIT3 fusion oncoprotein deregulates NF-κB target genes by interaction with NFKBIZ
    • Goransson, M., Andersson, M. K., Forni, C., Stahlberg, A., Andersson, C., Olofsson, A., Mantovani, R. and Aman, P. (2009) The myxoid liposarcoma FUS-DDIT3 fusion oncoprotein deregulates NF-κB target genes by interaction with NFKBIZ. Oncogene 28, 270-278
    • (2009) Oncogene , vol.28 , pp. 270-278
    • Goransson, M.1    Andersson, M.K.2    Forni, C.3    Stahlberg, A.4    Andersson, C.5    Olofsson, A.6    Mantovani, R.7    Aman, P.8
  • 145
    • 36248987806 scopus 로고    scopus 로고
    • hnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing
    • Kashima, T., Rao, N., David, C. J. and Manley, J. L. (2007) hnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing. Human Mol. Genet. 16, 3149-3159
    • (2007) Human Mol. Genet. , vol.16 , pp. 3149-3159
    • Kashima, T.1    Rao, N.2    David, C.J.3    Manley, J.L.4
  • 146
    • 55849144692 scopus 로고    scopus 로고
    • The RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) gene
    • Chen, H. H., Chang, J. G., Lu, R. M., Peng, T. Y. and Tarn, W. Y. (2008) The RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) gene. Mol. Cell. Biol. 28, 6929-6938
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6929-6938
    • Chen, H.H.1    Chang, J.G.2    Lu, R.M.3    Peng, T.Y.4    Tarn, W.Y.5
  • 147
    • 23044501888 scopus 로고    scopus 로고
    • Immunohistochemical study of the hnRNP A2 and B1 in the hippocampal formations of brains with Alzheimer's disease
    • Mizukami, K., Ishikawa, M., Iwakiri, M., Ikonomovic, M. D., Dekosky, S. T., Kamma, H. and Asada, T. (2005) Immunohistochemical study of the hnRNP A2 and B1 in the hippocampal formations of brains with Alzheimer's disease. Neurosci. Letters. 386, 111-115
    • (2005) Neurosci. Letters , vol.386 , pp. 111-115
    • Mizukami, K.1    Ishikawa, M.2    Iwakiri, M.3    Ikonomovic, M.D.4    Dekosky, S.T.5    Kamma, H.6    Asada, T.7
  • 148
    • 26944489645 scopus 로고    scopus 로고
    • Building specificity with nonspecific RNA-binding proteins
    • Singh, R. and Valcarcel, J. (2005) Building specificity with nonspecific RNA-binding proteins. Nat. Struct. Mol. Biol. 12, 645-653
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 645-653
    • Singh, R.1    Valcarcel, J.2
  • 149
    • 51449100243 scopus 로고    scopus 로고
    • Rapid functional diversification in the structurally conserved ELAV family of neuronal RNA binding proteins
    • Samson, M. L. (2008) Rapid functional diversification in the structurally conserved ELAV family of neuronal RNA binding proteins. BMC Genomics 9, 392
    • (2008) BMC Genomics , vol.9 , pp. 392
    • Samson, M.L.1
  • 150
    • 0029015816 scopus 로고
    • A conserved family of ELAV-like genes in vertebrates
    • Good, P. J. (1995) A conserved family of ELAV-like genes in vertebrates. Proc. Natl. Acad. Sci. U.S.A. 92, 4557-4561
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4557-4561
    • Good, P.J.1
  • 151
    • 28544452904 scopus 로고    scopus 로고
    • Shared RNA-binding sites for interacting members of the Drosophila ELAV family of neuronal proteins
    • Borgeson, C. D. and Samson, M. L. (2005) Shared RNA-binding sites for interacting members of the Drosophila ELAV family of neuronal proteins. Nucleic Acids Res. 33, 6372-6383
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6372-6383
    • Borgeson, C.D.1    Samson, M.L.2
  • 153
    • 21744454842 scopus 로고    scopus 로고
    • X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids
    • Backe, P. H., Messias, A. C., Ravelli, R. B. G., Sattler, M. and Cusack, S. (2005) X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids. Structure 13, 1055-1067
    • (2005) Structure , vol.13 , pp. 1055-1067
    • Backe, P.H.1    Messias, A.C.2    Ravelli, R.B.G.3    Sattler, M.4    Cusack, S.5
  • 154
    • 57649120777 scopus 로고    scopus 로고
    • Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms
    • Du, Z. H., Fenn, S., Tjhen, R. and James, T. L. (2008) Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms. J. Biol. Chem. 283, 28757-28766
    • (2008) J. Biol. Chem. , vol.283 , pp. 28757-28766
    • Du, Z.H.1    Fenn, S.2    Tjhen, R.3    James, T.L.4
  • 155
    • 20444371580 scopus 로고    scopus 로고
    • Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: Implications for biological function
    • Whitson, S. R., LeStourgeon, W. M. and Krezel, A. M. (2005) Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function. J. Mol. Biol. 350, 319-337
    • (2005) J. Mol. Biol. , vol.350 , pp. 319-337
    • Whitson, S.R.1    LeStourgeon, W.M.2    Krezel, A.M.3
  • 156
    • 0025857630 scopus 로고
    • Glycine loops in proteins: Their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA-binding proteins
    • Steinert, P. M., Mack, J. W., Korge, B. P., Gan, S. Q., Haynes, S. R. and Steven, A. C. (1991) Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA-binding proteins. Int. J. Biol. Macromol. 13, 130-139
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 130-139
    • Steinert, P.M.1    Mack, J.W.2    Korge, B.P.3    Gan, S.Q.4    Haynes, S.R.5    Steven, A.C.6
  • 157
    • 33750736355 scopus 로고    scopus 로고
    • K-turn motifs in spatial RNA coding
    • Tiedge, H. (2006) K-turn motifs in spatial RNA coding. RNA Biol. 3, 133-139
    • (2006) RNA Biol. , vol.3 , pp. 133-139
    • Tiedge, H.1
  • 158
    • 33646894709 scopus 로고    scopus 로고
    • hnRNP A1 associates with telomere ends and stimulates telomerase activity
    • Zhang, Q. S., Manche, L., Xu, R. M. and Krainer, A. R. (2006) hnRNP A1 associates with telomere ends and stimulates telomerase activity. RNA 12, 1116-1128
    • (2006) RNA , vol.12 , pp. 1116-1128
    • Zhang, Q.S.1    Manche, L.2    Xu, R.M.3    Krainer, A.R.4
  • 159
    • 38349076683 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A3 binds single-stranded telomeric DNA and inhibits telomerase extension in vitro
    • Huang, P. R., Tsai, S. T., Hsieh, K. H. and Wang, T. C. V. (2008) Heterogeneous nuclear ribonucleoprotein A3 binds single-stranded telomeric DNA and inhibits telomerase extension in vitro. Biochim. Biophys. Acta 1783, 193-202
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 193-202
    • Huang, P.R.1    Tsai, S.T.2    Hsieh, K.H.3    Wang, T.C.V.4
  • 160
    • 75149150660 scopus 로고    scopus 로고
    • HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
    • David, C. J., Chen, M., Assanah, M., Canoll, P. and Manley, J. L. (2010) HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature 463, 364-368
    • (2010) Nature , vol.463 , pp. 364-368
    • David, C.J.1    Chen, M.2    Assanah, M.3    Canoll, P.4    Manley, J.L.5
  • 161
    • 73649084109 scopus 로고    scopus 로고
    • hnRNP A2 regulates alternative mRNA splicing of TP53INP2 to control invasive cell migration
    • Moran-Jones, K., Grindlay, J., Jones, M., Smith, R. and Norman, J. C. (2009) hnRNP A2 regulates alternative mRNA splicing of TP53INP2 to control invasive cell migration. Cancer Res. 69, 9219-9227
    • (2009) Cancer Res. , vol.69 , pp. 9219-9227
    • Moran-Jones, K.1    Grindlay, J.2    Jones, M.3    Smith, R.4    Norman, J.C.5
  • 162
    • 1642483507 scopus 로고    scopus 로고
    • S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages
    • Gao, C. J., Guo, H. T., Wei, J. P., Mi, Z. Y., Wai, P. and Kuo, P. C. (2004) S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages. J. Biol. Chem. 279, 11236-11243
    • (2004) J. Biol. Chem. , vol.279 , pp. 11236-11243
    • Gao, C.J.1    Guo, H.T.2    Wei, J.P.3    Mi, Z.Y.4    Wai, P.5    Kuo, P.C.6
  • 163
    • 0033105845 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein DOE is a sequence-specific DNA-binding protein
    • Tolnay, M., Vereshchagina, L. A. and Tsokos, G. C. (1999) Heterogeneous nuclear ribonucleoprotein DOE is a sequence-specific DNA-binding protein. Biochem. J. 338, 417-425
    • (1999) Biochem. J. , vol.338 , pp. 417-425
    • Tolnay, M.1    Vereshchagina, L.A.2    Tsokos, G.C.3
  • 164
    • 70350241253 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A2 is a common transcriptional coactivator in the nuclear transcription response to mitochondrial respiratory stress
    • Guha, M., Pan, H., Fang, J. K. and Avadhani, N. G. (2009) Heterogeneous nuclear ribonucleoprotein A2 is a common transcriptional coactivator in the nuclear transcription response to mitochondrial respiratory stress. Mol. Biol. Cell. 20, 4107-4119
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 4107-4119
    • Guha, M.1    Pan, H.2    Fang, J.K.3    Avadhani, N.G.4
  • 165
    • 0033524957 scopus 로고    scopus 로고
    • Synergistic stimulation of HIV-1 Rev-dependent export of unspliced mRNA to the cytoplasm by hnRNP A1
    • Najera, I., Krieg, M. and Karn, J. (1999) Synergistic stimulation of HIV-1 Rev-dependent export of unspliced mRNA to the cytoplasm by hnRNP A1. J. Mol. Biol. 285, 1951-1964
    • (1999) J. Mol. Biol. , vol.285 , pp. 1951-1964
    • Najera, I.1    Krieg, M.2    Karn, J.3
  • 167
    • 33646930155 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, α (I) mRNA stability
    • Fahling, M., Mrowka, R., Steege, A., Martinka, P., Persson, P. B. and Thiele, B. J. (2006) Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, α (I) mRNA stability. J. Biol. Chem. 281, 9279-9286
    • (2006) J. Biol. Chem. , vol.281 , pp. 9279-9286
    • Fahling, M.1    Mrowka, R.2    Steege, A.3    Martinka, P.4    Persson, P.B.5    Thiele, B.J.6
  • 168
    • 52049119758 scopus 로고    scopus 로고
    • AUF1 and HuR proteins stabilize interleukin-8 mRNA in human saliva
    • Palanisamy, V., Park, N. J., Wang, J. and Wong, D. T. (2008) AUF1 and HuR proteins stabilize interleukin-8 mRNA in human saliva. J. Dent. Res. 87, 772-776
    • (2008) J. Dent. Res. , vol.87 , pp. 772-776
    • Palanisamy, V.1    Park, N.J.2    Wang, J.3    Wong, D.T.4
  • 169
    • 34249875986 scopus 로고    scopus 로고
    • Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation
    • Liao, B. S., Hu, Y. and Brewer, G. (2007) Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation. Nat. Struct. Mol. Biol. 14, 511-518
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 511-518
    • Liao, B.S.1    Hu, Y.2    Brewer, G.3
  • 170
    • 59149101940 scopus 로고    scopus 로고
    • Similar regulation of human inducible nitric-oxide synthase expression by different isoforms of the RNA-binding protein AUF1
    • Pautz, A., Linker, K., Altenhofer, S., Heil, S., Schmidt, N., Art, J., Knauer, S., Stauber, R., Sadri, N., Pont, A. et al. (2009) Similar regulation of human inducible nitric-oxide synthase expression by different isoforms of the RNA-binding protein AUF1. J. Biol. Chem. 284, 2755-2766
    • (2009) J. Biol. Chem. , vol.284 , pp. 2755-2766
    • Pautz, A.1    Linker, K.2    Altenhofer, S.3    Heil, S.4    Schmidt, N.5    Art, J.6    Knauer, S.7    Stauber, R.8    Sadri, N.9    Pont, A.10
  • 171
    • 66149116780 scopus 로고    scopus 로고
    • hnRNP A1 interacts with the 5′ untranslated regions of enterovirus 71 and sindbis virus RNA and is required for viral replication
    • Lin, J. Y., Shih, S. R., Pan, M. J., Li, C., Lue, C. F., Stollar, V. and Li, M. L. (2009) hnRNP A1 interacts with the 5′ untranslated regions of enterovirus 71 and sindbis virus RNA and is required for viral replication. J. Virol. 83, 6106-6114
    • (2009) J. Virol. , vol.83 , pp. 6106-6114
    • Lin, J.Y.1    Shih, S.R.2    Pan, M.J.3    Li, C.4    Lue, C.F.5    Stollar, V.6    Li, M.L.7
  • 173
    • 57349133787 scopus 로고    scopus 로고
    • RNA-binding protein hnRNP D modulates internal ribosome entry site-dependent translation of hepatitis C virus RNA
    • Paek, K. Y., Kim, C. S., Park, S. M., Kim, J. H. and Jang, S. K. (2008) RNA-binding protein hnRNP D modulates internal ribosome entry site-dependent translation of hepatitis C virus RNA. J. Virol. 82, 12082-12093
    • (2008) J. Virol. , vol.82 , pp. 12082-12093
    • Paek, K.Y.1    Kim, C.S.2    Park, S.M.3    Kim, J.H.4    Jang, S.K.5
  • 174
    • 84925561981 scopus 로고    scopus 로고
    • Cloning of an apobec-1 interacting protein that also binds apoB mRNA
    • Lau, P. P., Zhu, H. J., Nakamuta, M. and Chan, L. (1996) Cloning of an apobec-1 interacting protein that also binds apoB mRNA. Circulation 94, 3683-3683
    • (1996) Circulation , vol.94 , pp. 3683-3683
    • Lau, P.P.1    Zhu, H.J.2    Nakamuta, M.3    Chan, L.4
  • 176
    • 27244449015 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region
    • Mahajan, M. C., Narlikar, G. J., Boyapaty, G., Kingston, R. E. and Weissman, S. M. (2005) Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region. Proc. Natl. Acad. Sci. U.S.A. 102, 15012-15017
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15012-15017
    • Mahajan, M.C.1    Narlikar, G.J.2    Boyapaty, G.3    Kingston, R.E.4    Weissman, S.M.5
  • 177
    • 33846029532 scopus 로고    scopus 로고
    • Functional characterization of heterogeneous nuclear ribonuclear protein C1/C2 in vitamin D resistance: A novel response element-binding protein
    • Chen, H., Hewison, M. and Adams, J. S. (2006) Functional characterization of heterogeneous nuclear ribonuclear protein C1/C2 in vitamin D resistance: a novel response element-binding protein. J. Biol. Chem. 281, 39114-39120
    • (2006) J. Biol. Chem. , vol.281 , pp. 39114-39120
    • Chen, H.1    Hewison, M.2    Adams, J.S.3
  • 179
    • 69249087295 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-x(S) splice isoform
    • Revil, T., Pelletier, J., Toutant, J., Cloutier, A. and Chabot, B. (2009) Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-x(S) splice isoform. J. Biol. Chem. 284, 21458-21467
    • (2009) J. Biol. Chem. , vol.284 , pp. 21458-21467
    • Revil, T.1    Pelletier, J.2    Toutant, J.3    Cloutier, A.4    Chabot, B.5
  • 181
    • 0036464533 scopus 로고    scopus 로고
    • Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter
    • Kuninger, D. T., Izumi, T., Papaconstantinou, J. and Mitra, S. (2002) Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter. Nucleic Acids Res. 30, 823-829 (Pubitemid 34679650)
    • (2002) Nucleic Acids Research , vol.30 , Issue.3 , pp. 823-829
    • Kuninger, D.T.1    Izumi, T.2    Papaconstantinou, J.3    Mitra, S.4
  • 182
    • 63149167398 scopus 로고    scopus 로고
    • Roles of polypyrimidine tract binding proteins in major immediate-early gene expression and viral replication of human cytomegalovirus
    • Cosme, R. S. C., Yamamura, Y. and Tang, Q. Y. (2009) Roles of polypyrimidine tract binding proteins in major immediate-early gene expression and viral replication of human cytomegalovirus. J. Virol. 83, 2839-2850
    • (2009) J. Virol. , vol.83 , pp. 2839-2850
    • Cosme, R.S.C.1    Yamamura, Y.2    Tang, Q.Y.3
  • 184
    • 22544468490 scopus 로고    scopus 로고
    • Binding of hnRNP L to the pre-mRNA processing enhancer of the herpes simplex virus thymidine kinase gene enhances both polyadenylation and nucleocytoplasmic export of intronless mRNAs
    • Guang, S. H., Felthauser, A. M. and Mertz, J. E. (2005) Binding of hnRNP L to the pre-mRNA processing enhancer of the herpes simplex virus thymidine kinase gene enhances both polyadenylation and nucleocytoplasmic export of intronless mRNAs. Mol. Cell. Biol. 25, 6303-6313
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6303-6313
    • Guang, S.H.1    Felthauser, A.M.2    Mertz, J.E.3
  • 186
    • 0033968408 scopus 로고    scopus 로고
    • Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death
    • Hicks, G. G., Singh, N., Nashabi, A., Mai, S., Bozek, G., Klewes, L., Arapovic, D., White, E. K., Koury, M. J., Oltz, E. M. et al. (2000) Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death. Nat. Genet. 24, 175-179
    • (2000) Nat. Genet. , vol.24 , pp. 175-179
    • Hicks, G.G.1    Singh, N.2    Nashabi, A.3    Mai, S.4    Bozek, G.5    Klewes, L.6    Arapovic, D.7    White, E.K.8    Koury, M.J.9    Oltz, E.M.10
  • 187
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • Mourelatos, Z., Abel, L., Yong, J. S., Kataoka, N. and Dreyfuss, G. (2001) SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J. 20, 5443-5452
    • (2001) EMBO J. , vol.20 , pp. 5443-5452
    • Mourelatos, Z.1    Abel, L.2    Yong, J.S.3    Kataoka, N.4    Dreyfuss, G.5
  • 188
    • 62749177960 scopus 로고    scopus 로고
    • SYNCRIP (synaptotagmin-binding, cytoplasmic RNA-interacting protein) is a host factor involved in hepatitis C virus RNA replication
    • Liu, H. M., Aizaki, H., Choi, K. S., Machida, K., Ou, J. J. H. and Lai, M. M. C. (2009) SYNCRIP (synaptotagmin-binding, cytoplasmic RNA-interacting protein) is a host factor involved in hepatitis C virus RNA replication. Virology 386, 249-256
    • (2009) Virology , vol.386 , pp. 249-256
    • Liu, H.M.1    Aizaki, H.2    Choi, K.S.3    Machida, K.4    Ou, J.J.H.5    Lai, M.M.C.6
  • 189
    • 0034730324 scopus 로고    scopus 로고
    • A mechanism for translationally coupled mRNA turnover: Interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex
    • Grosset, C., Chen, C. Y. A., Xu, N. H., Sonenberg, N., Jacquemin-Sablon, H. and Shyu, A. B. (2000) A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell 103, 29-40
    • (2000) Cell , vol.103 , pp. 29-40
    • Grosset, C.1    Chen, C.Y.A.2    Xu, N.H.3    Sonenberg, N.4    Jacquemin-Sablon, H.5    Shyu, A.B.6
  • 190
    • 0036154096 scopus 로고    scopus 로고
    • Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: A role for Smn in RNA processing in motor axons?
    • Rossoll, W., Kroning, A. K., Ohndorf, U. M., Steegborn, C., Jablonka, S. and Sendtner, M. (2002) Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons? Human Mol. Genet. 11, 93-105
    • (2002) Human Mol. Genet. , vol.11 , pp. 93-105
    • Rossoll, W.1    Kroning, A.K.2    Ohndorf, U.M.3    Steegborn, C.4    Jablonka, S.5    Sendtner, M.6
  • 191
    • 0027963330 scopus 로고
    • Purification of 2 isoforms of hnRNP-U and characterization of their nucleic-acid binding-activity
    • Fackelmayer, F. O. and Richter, A. (1994) Purification of 2 isoforms of hnRNP-U and characterization of their nucleic-acid binding-activity. Biochemistry 33, 10416-10422
    • (1994) Biochemistry , vol.33 , pp. 10416-10422
    • Fackelmayer, F.O.1    Richter, A.2
  • 192
    • 0032850595 scopus 로고    scopus 로고
    • hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation
    • Kim, M. K. and Nikodem, V. M. (1999) hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. Mol. Cell. Biol. 19, 6833-6844
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6833-6844
    • Kim, M.K.1    Nikodem, V.M.2
  • 194
    • 0027263365 scopus 로고
    • Nuclear proteins that bind the premessenger RNA 3′ splice-site sequence R(UUAG/G) and the human telomeric DNA-sequence D(TTAGGG)N
    • Ishikawa, F., Matunis, M. J., Dreyfuss, G. and Cech, T. R. (1993) Nuclear proteins that bind the premessenger RNA 3′ splice-site sequence R(UUAG/G) and the human telomeric DNA-sequence D(TTAGGG)N. Mol. Cell. Biol. 13, 4301-4310
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4301-4310
    • Ishikawa, F.1    Matunis, M.J.2    Dreyfuss, G.3    Cech, T.R.4
  • 195
    • 0034806974 scopus 로고    scopus 로고
    • Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover
    • Xu, N. H., Chen, C. Y. A. and Shyu, A. B. (2001) Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol. Cell. Biol. 21, 6960-6971
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6960-6971
    • Xu, N.H.1    Chen, C.Y.A.2    Shyu, A.B.3
  • 196
    • 0033927902 scopus 로고    scopus 로고
    • In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance
    • Eversole, A. and Maizels, N. (2000) In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance. Mol. Cell. Biol. 20, 5425-5432
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5425-5432
    • Eversole, A.1    Maizels, N.2
  • 197
    • 0036304118 scopus 로고    scopus 로고
    • Suppression of 15-lipoxygenase synthesis by hnRNP E1 is dependent on repetitive nature of LOX mRNA 3′-UTR control element DICE
    • Reimann, I., Huth, A., Thiele, H. and Thiele, B. J. (2002) Suppression of 15-lipoxygenase synthesis by hnRNP E1 is dependent on repetitive nature of LOX mRNA 3′-UTR control element DICE. J. Mol. Biol. 315, 965-974
    • (2002) J. Mol. Biol. , vol.315 , pp. 965-974
    • Reimann, I.1    Huth, A.2    Thiele, H.3    Thiele, B.J.4
  • 198
    • 0030987239 scopus 로고    scopus 로고
    • Four highly stable eukaryotic mRNAs assemble 3′ untranslated region RNA-protein complexes sharing cis and trans components
    • Holcik, M. and Liebhaber, S. A. (1997) Four highly stable eukaryotic mRNAs assemble 3′ untranslated region RNA-protein complexes sharing cis and trans components. Proc. Natl. Acad. Sci. U.S.A. 94, 2410-2414
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2410-2414
    • Holcik, M.1    Liebhaber, S.A.2
  • 200
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh, R., Valcarcel, J. and Green, M. R. (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
  • 201
    • 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
  • 202
    • 0030872401 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein binds upstream of neural cell-specific c-src exon N1 to repress the splicing of the intron downstream
    • Chan, R. C. C. and Black, D. L. (1997) The polypyrimidine tract binding protein binds upstream of neural cell-specific c-src exon N1 to repress the splicing of the intron downstream. Mol. Cell. Biol. 17, 4667-4676
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4667-4676
    • Chan, R.C.C.1    Black, D.L.2
  • 204
    • 0029917052 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K is a transcription factor
    • Michelotti, E. F., Michelotti, G. A., Aronsohn, A. I. and Levens, D. (1996) Heterogeneous nuclear ribonucleoprotein K is a transcription factor. Mol. Cell. Biol. 16, 2350-2360
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2350-2360
    • Michelotti, E.F.1    Michelotti, G.A.2    Aronsohn, A.I.3    Levens, D.4
  • 205
    • 77953030317 scopus 로고    scopus 로고
    • A rational nomenclature for serine/arginine-rich protein splicing factors (SR proteins)
    • Manley, J. L. and Krainer, A. R. (2010) A rational nomenclature for serine/arginine-rich protein splicing factors (SR proteins). Genes Dev. 24, 1073-1074
    • (2010) Genes Dev. , vol.24 , pp. 1073-1074
    • Manley, J.L.1    Krainer, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.