메뉴 건너뛰기




Volumn 16, Issue 8, 2010, Pages 1449-1462

Heterogeneous nuclear ribonucleoproteins (hnRNPs) in cellular processes: Focus on hnRNP E1's multifunctional regulatory roles

Author keywords

hnRNP; hnRNP E1; mRNA stability; PCBP1; Post transcriptional regulon; pre mRNA processing; Translation

Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN E1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN E2; MESSENGER RNA; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 77955110561     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2254110     Document Type: Review
Times cited : (222)

References (132)
  • 1
    • 0028232357 scopus 로고
    • Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid binding [oligo(dC)] protein related to the pre-mRNA binding protein K
    • Aasheim HC, Loukianova T, Deggerdal A, Smeland EB. 1994. Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid binding [oligo(dC)] protein related to the pre-mRNA binding protein K. Nucleic Acids Res 22: 959-964. (Pubitemid 24162155)
    • (1994) Nucleic Acids Research , vol.22 , Issue.6 , pp. 959-964
    • Aasheim, H.-C.1    Loukianova, T.2    Deggerdal, A.3    Smeland, E.B.4
  • 2
    • 34948821069 scopus 로고    scopus 로고
    • Pre-spliceosomal binding of U1 small nuclear ribonucleoprotein (RNP) and heterogenous nuclear RNP E1 is associated with suppression of a growth hormone receptor pseudoexon
    • Akker SA, Misra S, Aslam S, Morgan EL, Smith PJ, Khoo B, Chew SL. 2007. Pre-spliceosomal binding of U1 small nuclear ribonucleoprotein (RNP) and heterogenous nuclear RNP E1 is associated with suppression of a growth hormone receptor pseudoexon. Mol Endocrinol 21: 2529-2540.
    • (2007) Mol Endocrinol , vol.21 , pp. 2529-2540
    • Akker, S.A.1    Misra, S.2    Aslam, S.3    Morgan, E.L.4    Smith, P.J.5    Khoo, B.6    Chew, S.L.7
  • 3
    • 0026640733 scopus 로고
    • Independent deposition of heterogeneous nuclear ribonucleoproteins and small nuclear ribonucleoprotein particles at sites of transcription
    • Amero SA, Raychaudhuri G, Cass CL, van Venrooij WJ, Habets WJ, Krainer AR, Beyer AL. 1992. Independent deposition of heterogeneous nuclear ribonucleoproteins and small nuclear ribonucleoprotein particles at sites of transcription. Proc Natl Acad Sci 89: 8409-8413.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 8409-8413
    • Amero, S.A.1    Raychaudhuri, G.2    Cass, C.L.3    Van Venrooij, W.J.4    Habets, W.J.5    Krainer, A.R.6    Beyer, A.L.7
  • 4
    • 72949123583 scopus 로고    scopus 로고
    • Post-transcriptional regulons coordinate the initiation and resolution of inflammation
    • Anderson P. 2010. Post-transcriptional regulons coordinate the initiation and resolution of inflammation. Nat Rev Immunol 10: 24-35.
    • (2010) Nat Rev Immunol , vol.10 , pp. 24-35
    • Anderson, P.1
  • 6
    • 0024655246 scopus 로고
    • RNA-binding proteins as developmental regulators
    • Bandziulis RJ, Swanson MS, Dreyfuss G. 1989. RNA-binding proteins as developmental regulators. Genes Dev 3: 431-437.
    • (1989) Genes Dev , vol.3 , pp. 431-437
    • Bandziulis, R.J.1    Swanson, M.S.2    Dreyfuss, G.3
  • 7
    • 77649092427 scopus 로고    scopus 로고
    • MicroRNAs: From decay to decoy
    • Beitzinger M, Meister G. 2010. MicroRNAs: From decay to decoy. Cell 140: 612-614.
    • (2010) Cell , vol.140 , pp. 612-614
    • Beitzinger, M.1    Meister, G.2
  • 8
    • 0017744030 scopus 로고
    • Identification and characterization of the packaging proteins of core 40S hnRNP particles
    • Beyer AL, Christensen ME, Walker BW, LeStourgeon WM. 1977. Identification and characterization of the packaging proteins of core 40S hnRNP particles. Cell 11: 127-138. (Pubitemid 8126060)
    • (1977) Cell , vol.11 , Issue.1 , pp. 127-138
    • Beyer, A.L.1    Christensen, M.E.2    Walker, B.W.3    LeStourgeon, W.M.4
  • 10
    • 2942623743 scopus 로고    scopus 로고
    • hnRNP K: One protein multiple processes
    • Bomsztyk K, Denisenko O, 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
  • 11
    • 0019877875 scopus 로고
    • Structural investigation of nuclear RNP particles containing pre-mRNA by different fluorescence techniques
    • Borissova OF, Krichevskaya AA, Samarina OP. 1981. Structural investigation of nuclear RNP particles containing pre-mRNA by different fluorescence techniques. Nucleic Acids Res 9: 663-681.
    • (1981) Nucleic Acids Res , vol.9 , pp. 663-681
    • Borissova, O.F.1    Krichevskaya, A.A.2    Samarina, O.P.3
  • 12
    • 0030992812 scopus 로고    scopus 로고
    • The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo
    • Buckanovich RJ, Darnell RB. 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
    • 0027374048 scopus 로고
    • Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding protein and is specifically expressed in the developing motor system
    • Buckanovich RJ, Posner JB, Darnell RB. 1993. Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding protein and is specifically expressed in the developing motor system. Neuron 11: 657-672.
    • (1993) Neuron , vol.11 , pp. 657-672
    • Buckanovich, R.J.1    Posner, J.B.2    Darnell, R.B.3
  • 14
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd CG, Dreyfuss G. 1994. Conserved structures and diversity of functions of RNA-binding proteins. Science 265: 615-621. (Pubitemid 24268271)
    • (1994) Science , vol.265 , Issue.5172 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 15
    • 0028077730 scopus 로고
    • Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors
    • Caceres JF, Stamm S, Helfman DM, Krainer AR. 1994. Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265: 1706-1709. (Pubitemid 24314901)
    • (1994) Science , vol.265 , Issue.5179 , pp. 1706-1709
    • Caceres, J.F.1    Stamm, S.2    Helfman, D.M.3    Krainer, A.R.4
  • 16
    • 77949903837 scopus 로고    scopus 로고
    • Pluripotency-associated genes in human nasopharyngeal carcinoma CNE-2 cells are reactivated by a unique epigenetic sub-microenvironment
    • doi: 10.1186/1471-2407-10-68
    • Cao JX, Cui YX, Long ZJ, Dai ZM, Lin JY, Liang Y, Zheng FM, Zeng YX, Liu Q. 2010. Pluripotency-associated genes in human nasopharyngeal carcinoma CNE-2 cells are reactivated by a unique epigenetic sub-microenvironment. BMC Cancer 10: 68. doi: 10.1186/1471-2407-10-68.
    • (2010) BMC Cancer , vol.10 , pp. 68
    • Cao, J.X.1    Cui, Y.X.2    Long, Z.J.3    Dai, Z.M.4    Lin, J.Y.5    Liang, Y.6    Zheng, F.M.7    Zeng, Y.X.8    Liu, Q.9
  • 18
    • 77649261101 scopus 로고    scopus 로고
    • TGF-β-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI
    • Chaudhury A, Hussey GS, Ray PS, Jin G, Fox PL, Howe PH. 2010. TGF-β-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI. Nat Cell Biol 12: 286-293.
    • (2010) Nat Cell Biol , vol.12 , pp. 286-293
    • Chaudhury, A.1    Hussey, G.S.2    Ray, P.S.3    Jin, G.4    Fox, P.L.5    Howe, P.H.6
  • 19
    • 43549088269 scopus 로고    scopus 로고
    • Arginine methylation of hnRNP K enhances p53 transcriptional activity
    • Chen Y, Zhou X, Liu N, Wang C, Zhang L, Mo W, Hu G. 2008. Arginine methylation of hnRNP K enhances p53 transcriptional activity. FEBS Lett 582: 1761-1765.
    • (2008) FEBS Lett , vol.582 , pp. 1761-1765
    • Chen, Y.1    Zhou, X.2    Liu, N.3    Wang, C.4    Zhang, L.5    Mo, W.6    Hu, G.7
  • 20
    • 0242637418 scopus 로고    scopus 로고
    • A novel set of nuclear localization signals determine distributions of the αCP RNA-binding proteins
    • Chkheidze AN, Liebhaber SA. 2003. A novel set of nuclear localization signals determine distributions of the αCP RNA-binding proteins. Mol Cell Biol 23: 8405-8415.
    • (2003) Mol Cell Biol , vol.23 , pp. 8405-8415
    • Chkheidze, A.N.1    Liebhaber, S.A.2
  • 21
    • 0033031221 scopus 로고    scopus 로고
    • Assembly of the α-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3' untranslated region determinant and poly(C) binding protein αCP
    • Chkheidze AN, Lyakhov DL, Makeyev AV, Morales J, Kong J, Liebhaber SA. 1999. Assembly of the α-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3′ untranslated region determinant and poly(C) binding protein αCP. Mol Cell Biol 19: 4572-4581. (Pubitemid 29289495)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.7 , pp. 4572-4581
    • Chkheidze, A.N.1    Lyakhov, D.L.2    Makeyev, A.V.3    Morales, J.4    Kong, J.5    Liebhaber, S.A.6
  • 22
    • 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 MY, Rooke N, Turck CW, Black DL. 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. (Pubitemid 29018410)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 69-77
    • Chou, M.-Y.1    Rooke, N.2    Turck, C.W.3    Black, D.L.4
  • 23
    • 0032575526 scopus 로고    scopus 로고
    • Translational inhibition in vitro of human papillomavirus type 16 L2 mRNA mediated through interaction with heterogenous ribonucleoprotein K and poly(rC)-binding proteins 1 and 2
    • Collier B, Goobar-Larsson L, Sokolowski M, Schwartz S. 1998. Translational inhibition in vitro of human papillomavirus type 16 L2 mRNA mediated through interaction with heterogenous ribonucleoprotein K and poly(rC)-binding proteins 1 and 2. J Biol Chem 273: 22648-22656.
    • (1998) J Biol Chem , vol.273 , pp. 22648-22656
    • Collier, B.1    Goobar-Larsson, L.2    Sokolowski, M.3    Schwartz, S.4
  • 24
    • 0023872239 scopus 로고
    • ATP activates transcription initiation from promoters by RNA polymerase II in a reversible step prior to RNA synthesis
    • Conaway RC, Conaway JW. 1988. ATP activates transcription initiation from promoters by RNA polymerase II in a reversible step prior to RNA synthesis. J Biol Chem 263: 2962-2968.
    • (1988) J Biol Chem , vol.263 , pp. 2962-2968
    • Conaway, R.C.1    Conaway, J.W.2
  • 26
    • 0033559760 scopus 로고    scopus 로고
    • Identification of the poly(C) binding protein in the complex associated with the 3′ untranslated region of erythropoietin messenger RNA
    • Czyzyk-Krzeska MF, Bendixen AC. 1999. Identification of the poly(C) binding protein in the complex associated with the 3′ untranslated region of erythropoietin messenger RNA. Blood 93: 2111-2120.
    • (1999) Blood , vol.93 , pp. 2111-2120
    • Czyzyk-Krzeska, M.F.1    Bendixen, A.C.2
  • 27
    • 0030020622 scopus 로고    scopus 로고
    • Characterization of the hypoxia-inducible protein binding site within the pyrimidine-rich tract in the 3′-untranslated region of the tyrosine hydroxylase mRNA
    • Czyzyk-Krzeska MF, Beresh JE. 1996. Characterization of the hypoxiainducible protein binding site within the pyrimidine-rich tract in the 3′-untranslated region of the tyrosine hydroxylase mRNA. J Biol Chem 271: 3293-3299. (Pubitemid 126559196)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.6 , pp. 3293-3299
    • Czyzyk-Krzeska, M.F.1    Beresh, J.E.2
  • 28
    • 2542477014 scopus 로고    scopus 로고
    • RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers
    • de Hoog CL, Foster LJ, Mann M. 2004. RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117: 649-662.
    • (2004) Cell , vol.117 , pp. 649-662
    • De Hoog, C.L.1    Foster, L.J.2    Mann, M.3
  • 29
    • 0029858735 scopus 로고    scopus 로고
    • Characterization of the nucleic-acid-binding activity of KH domains. Different properties of different domains
    • Dejgaard K, Leffers H. 1996. Characterization 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
  • 30
    • 0033534467 scopus 로고    scopus 로고
    • G4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D: A role for G-G pairing in immunoglobulin switch recombination
    • Dempsey LA, Sun H, Hanakahi LA, Maizels N. 1999. G4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D: A role for G-G pairing in immunoglobulin switch recombination. J Biol Chem 274: 1066-1071.
    • (1999) J Biol Chem , vol.274 , pp. 1066-1071
    • Dempsey, L.A.1    Sun, H.2    Hanakahi, L.A.3    Maizels, N.4
  • 31
    • 0023919931 scopus 로고
    • Ribonucleoprotein particles in cellular processes
    • Dreyfuss G, Philipson L, Mattaj IW. 1988. Ribonucleoprotein particles in cellular processes. J Cell Biol 106: 1419-1425.
    • (1988) J Cell Biol , vol.106 , pp. 1419-1425
    • Dreyfuss, G.1    Philipson, L.2    Mattaj, I.W.3
  • 33
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • DOI 10.1038/nrm760
    • Dreyfuss G, Kim VN, Kataoka N. 2002. Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol 3: 195-205. (Pubitemid 37237142)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 35
    • 77049276231 scopus 로고
    • Small granules in the amphibian oocyte nucleus and their relationship to RNA
    • Gall JG. 1956. Small granules in the amphibian oocyte nucleus and their relationship to RNA. J Biophys Biochem Cytol 2: 393-396.
    • (1956) J Biophys Biochem Cytol , vol.2 , pp. 393-396
    • Gall, J.G.1
  • 36
    • 0035976612 scopus 로고    scopus 로고
    • Delineation of mRNA export pathways by the use of cell-permeable peptides
    • Gallouzi IE, Steitz JA. 2001. Delineation of mRNA export pathways by the use of cell-permeable peptides. Science 294: 1895-1901.
    • (2001) Science , vol.294 , pp. 1895-1901
    • Gallouzi, I.E.1    Steitz, J.A.2
  • 37
    • 0030861261 scopus 로고    scopus 로고
    • Two functional complexes formed by KH domain containing proteins with the 5' noncoding region of poliovirus RNA
    • Gamarnik AV, Andino R. 1997. Two functional complexes formed by KH domain containing proteins with the 59 noncoding region of poliovirus RNA. RNA 3: 882-892. (Pubitemid 27332738)
    • (1997) RNA , vol.3 , Issue.8 , pp. 882-892
    • Gamarnik, A.V.1    Andino, R.2
  • 38
    • 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 TJ, Thompson JD, Heringa J. 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
  • 39
    • 0026757694 scopus 로고
    • Interaction of the RNA-binding domain of the hnRNP C proteins with RNA
    • Gorlach M, Wittekind M, Beckman RA, Mueller L, Dreyfuss G. 1992. Interaction of the RNA-binding domain of the hnRNP C proteins with RNA. EMBO J 11: 3289-3295.
    • (1992) EMBO J , vol.11 , pp. 3289-3295
    • Gorlach, M.1    Wittekind, M.2    Beckman, R.A.3    Mueller, L.4    Dreyfuss, G.5
  • 40
    • 0035253621 scopus 로고    scopus 로고
    • KH domain: One motif, two folds
    • Grishin NV. 2001. KH domain: One motif, two folds. Nucleic Acids Res 29: 638-643.
    • (2001) Nucleic Acids Res , vol.29 , pp. 638-643
    • Grishin, N.V.1
  • 41
    • 0344838611 scopus 로고    scopus 로고
    • Roles of hnRNP A1, SR proteins, and p68 Helicase in c-H-ras alternative splicing regulation
    • Guil S, Gattoni R, Carrascal M, Abián J, Stévenin J, Bach-Elias M. 2003. Roles of hnRNP A1, SR proteins, and p68 Helicase in c-H-ras alternative splicing regulation. Mol Cell Biol 23: 2927-2941.
    • (2003) Mol Cell Biol , vol.23 , pp. 2927-2941
    • Guil, S.1    Gattoni, R.2    Carrascal, M.3    Abián, J.4    Stévenin, J.5    Bach-Elias, M.6
  • 43
    • 0032518188 scopus 로고    scopus 로고
    • Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimuune antibody: Immunological relationship with hnRNP P
    • Hassfeld W, Chan KLE, Mathison DA, Portman D, Dreyfuss G, Steiner G, Tan EM. 1998. Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimuune antibody: Immunological relationship with hnRNP P. Nucleic Acids Res 26: 439-445.
    • (1998) Nucleic Acids Res , vol.26 , pp. 439-445
    • Hassfeld, W.1    Chan, K.L.E.2    Mathison, D.A.3    Portman, D.4    Dreyfuss, G.5    Steiner, G.6    Tan, E.M.7
  • 45
    • 0034627232 scopus 로고    scopus 로고
    • Differentiation-dependent cytoplasmic distribution and in vivo RNA association of proteins recognized by the 3′-UTR stability element of a-globin mRNA in erythroleukemic cells
    • Henics T. 2000. Differentiation-dependent cytoplasmic distribution and in vivo RNA association of proteins recognized by the 3′-UTR stability element of a-globin mRNA in erythroleukemic cells. Biochem Biophys Res Commun 279: 40-46.
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 40-46
    • Henics, T.1
  • 46
    • 0032510715 scopus 로고    scopus 로고
    • hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA
    • Hoek KS, Kidd GJ, Carson JH, 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
  • 48
    • 37549039473 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein M is a splicing regulatory protein that can enhance or silence splicing of alternatively spliced exons
    • Hovhannisyan RH, Carstens RP. 2007. Heterogeneous ribonucleoprotein M is a splicing regulatory protein that can enhance or silence splicing of alternatively spliced exons. J Biol Chem 282: 36265-36274.
    • (2007) J Biol Chem , vol.282 , pp. 36265-36274
    • Hovhannisyan, R.H.1    Carstens, R.P.2
  • 50
    • 0027263365 scopus 로고
    • Nuclear proteins that bind the pre-mRNA 3′ splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
    • Ishikawa F, Matunis MJ, Dreyfuss G, Cech TR. 1993. Nuclear proteins that bind the pre-mRNA 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
  • 51
    • 0034705034 scopus 로고    scopus 로고
    • The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain
    • Jensen KB, Musunuru K, Lewis HA, Burley SK, Darnell RB. 2000. The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain. Proc Natl Acad Sci 97: 5740-5745.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 5740-5745
    • Jensen, K.B.1    Musunuru, K.2    Lewis, H.A.3    Burley, S.K.4    Darnell, R.B.5
  • 52
    • 0028881190 scopus 로고
    • Cell type-specific expression of hnRNP proteins
    • Kamma H, Portman DS, Dreyfuss G. 1995. Cell type-specific expression of hnRNP proteins. Exp Cell Res 221: 187-196.
    • (1995) Exp Cell Res , vol.221 , pp. 187-196
    • Kamma, H.1    Portman, D.S.2    Dreyfuss, G.3
  • 53
    • 0036289532 scopus 로고    scopus 로고
    • Eukaryotic mRNPs may represent posttranscriptional operons
    • Keene JD, Tenenbaum SA. 2002. Eukaryotic mRNPs may represent posttranscriptional operons. Mol Cell 9: 1161-1167.
    • (2002) Mol Cell , vol.9 , pp. 1161-1167
    • Keene, J.D.1    Tenenbaum, S.A.2
  • 54
    • 0030803670 scopus 로고    scopus 로고
    • Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3'-end formation in yeast
    • Kessler MM, Henry MF, Shen E, Zhao J, Gross S, Silver PA, Moore CL. 1997. Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′-end formation in yeast. Genes Dev 11: 2545-2556. (Pubitemid 27438835)
    • (1997) Genes and Development , vol.11 , Issue.19 , pp. 2545-2556
    • Kessler, M.M.1    Henry, M.F.2    Shen, E.3    Zhao, J.4    Gross, S.5    Silver, P.A.6    Moore, C.L.7
  • 55
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box
    • Kiledjian M, 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
  • 56
    • 0029125496 scopus 로고
    • Identification of two KH domain proteins in the α-globin mRNP stability complex
    • Kiledjian M, Wang X, Liebhaber SA. 1995. Identification of two KH domain proteins in the α-globin mRNP stability complex. EMBO J 14: 4357-4364.
    • (1995) EMBO J , vol.14 , pp. 4357-4364
    • Kiledjian, M.1    Wang, X.2    Liebhaber, S.A.3
  • 57
    • 0030856470 scopus 로고    scopus 로고
    • Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the a-globin mRNA stability complex
    • Kiledjian M, DeMaria CT, Brewer G, Novick K. 1997. Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the a-globin mRNA stability complex. Mol Cell Biol 17: 4870-4876.
    • (1997) Mol Cell Biol , vol.17 , pp. 4870-4876
    • Kiledjian, M.1    DeMaria, C.T.2    Brewer, G.3    Novick, K.4
  • 59
    • 23944467312 scopus 로고    scopus 로고
    • Poly(C) binding protein family is a transcription factor in μ-opioid receptor gene expression
    • Kim SS, Pandey KK, Choi HS, Kim SY, Law PY, Wei LN, Loh HH. 2005. Poly(C) binding protein family is a transcription factor in μ-opioid receptor gene expression. Mol Pharmacol 68: 729-736.
    • (2005) Mol Pharmacol , vol.68 , pp. 729-736
    • Kim, S.S.1    Pandey, K.K.2    Choi, H.S.3    Kim, S.Y.4    Law, P.Y.5    Wei, L.N.6    Loh, H.H.7
  • 60
    • 33746489363 scopus 로고    scopus 로고
    • Shared stabilization functions of pyrimidine-rich determinants in the erythroid 15-lipoxygenase and α-globin mRNAs
    • Kong J, Sumaroka M, Eastmond DL, Liebhaber SA. 2006. Shared stabilization functions of pyrimidine-rich determinants in the erythroid 15-lipoxygenase and α-globin mRNAs. Mol Cell Biol 26: 5603-5614.
    • (2006) Mol Cell Biol , vol.26 , pp. 5603-5614
    • Kong, J.1    Sumaroka, M.2    Eastmond, D.L.3    Liebhaber, S.A.4
  • 61
    • 33746581893 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs
    • Kosturko LD, Maggipinto MJ, Korza G, Lee JW, Carson JH, 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
  • 62
    • 0033153348 scopus 로고    scopus 로고
    • hnRNP complexes: Composition, structure, and function
    • Krecic AM, Swanson MS. 1999. hnRNP complexes: Composition, structure, and function. Curr Opin Cell Biol 11: 363-371.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 363-371
    • Krecic, A.M.1    Swanson, M.S.2
  • 63
    • 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 MR, Wellinger RJ, Chabot B. 1998. Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase. Nat Genet 19: 199-202.
    • (1998) Nat Genet , 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
  • 64
    • 0029076374 scopus 로고
    • Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains
    • Leffers H, Dejgaard K, Celis JE. 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
  • 66
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome
    • Lewis HA, Musunuru K, Jensen KB, Edo C, Chen H, Darnell RB, Burley SK. 2000. Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome. Cell 100: 323-332. (Pubitemid 30353088)
    • (2000) Cell , vol.100 , Issue.3 , pp. 323-332
    • Lewis, H.A.1    Musunuru, K.2    Jensen, K.B.3    Edo, C.4    Chen, H.5    Darnell, R.B.6    Burley, S.K.7
  • 67
    • 2942525287 scopus 로고    scopus 로고
    • Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis
    • Li T, Evdokimov E, Shen RF, Chao CC, Tekle E, Wang T, Stadtman ER, Yang DC, Chock PB. 2004. Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis. Proc Natl Acad Sci 101: 8551-8556.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 8551-8556
    • Li, T.1    Evdokimov, E.2    Shen, R.F.3    Chao, C.C.4    Tekle, E.5    Wang, T.6    Stadtman, E.R.7    Yang, D.C.8    Chock, P.B.9
  • 68
    • 0029043983 scopus 로고
    • NusA interferes with interactions between the nascent RNA and the C-terminal domain of the a subunit of RNA polymerase in Escherichia coli transcription complexes
    • Liu K, Hanna MM. 1995. NusA interferes with interactions between the nascent RNA and the C-terminal domain of the a subunit of RNA polymerase in Escherichia coli transcription complexes. Proc Natl Acad Sci 92: 5012-5016.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 5012-5016
    • Liu, K.1    Hanna, M.M.2
  • 69
    • 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 MJ, Mehtani S, Korenblat K, Pazin MJ, Schmidt EV. 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
  • 70
    • 0036223676 scopus 로고    scopus 로고
    • The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
    • Makeyev AV, Liebhaber SA. 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
  • 71
    • 0033609880 scopus 로고    scopus 로고
    • A set of highly conserved RNA-binding proteins, αCP-1 and αCP-2, implicated in mRNA stabilization, are coexpressed from an intronless gene and its intron-containing paralog
    • Makeyev AV, Chkheidze AN, Liebhaber SA. 1999. A set of highly conserved RNA-binding proteins, αCP-1 and αCP-2, implicated in mRNA stabilization, are coexpressed from an intronless gene and its intron-containing paralog. J Biol Chem 274: 24849-24857.
    • (1999) J Biol Chem , vol.274 , pp. 24849-24857
    • Makeyev, A.V.1    Chkheidze, A.N.2    Liebhaber, S.A.3
  • 73
    • 0026515523 scopus 로고
    • Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein
    • Matunis MJ, Michael WM, Dreyfuss G. 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
  • 74
    • 0027416787 scopus 로고
    • Association of individual hnRNP proteins and snRNPs with nascent transcripts
    • Matunis EL, Matunis MJ, Dreyfuss G. 1993. Association of individual hnRNP proteins and snRNPs with nascent transcripts. J Cell Biol 121: 219-228. (Pubitemid 23110868)
    • (1993) Journal of Cell Biology , vol.121 , Issue.2 , pp. 219-228
    • Matunis, E.L.1    Matunis, M.J.2    Dreyfuss, G.3
  • 75
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda A, Krainer AR. 1992. Regulation of alternative pre-mRNA 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
  • 76
    • 34347264157 scopus 로고    scopus 로고
    • Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1
    • Meng Q, Rayala SK, Gururaj AE, Talukder AH, O'Malley BW, Kumar R. 2007. Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1. Proc Natl Acad Sci 104: 5866-5871.
    • (2007) Proc Natl Acad Sci , 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
  • 77
    • 0032562765 scopus 로고    scopus 로고
    • Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPβ-mediated gene activation
    • Miau LH, Chang CJ, Shen BJ, Tsai WH, Lee SC. 1998. Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPβ-mediated gene activation. J Biol Chem 273: 10784-10791.
    • (1998) J Biol Chem , vol.273 , pp. 10784-10791
    • Miau, L.H.1    Chang, C.J.2    Shen, B.J.3    Tsai, W.H.4    Lee, S.C.5
  • 78
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated, temperature-dependent nuclear protein export pathway
    • Michael WM, Choi M, Dreyfuss G. 1995. A nuclear export signal in hnRNP A1: A signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83: 415-422.
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 79
    • 0030978415 scopus 로고    scopus 로고
    • The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein
    • Michael WM, Eder PS, Dreyfuss G. 1997. The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J 16: 3587-3598.
    • (1997) EMBO J , vol.16 , pp. 3587-3598
    • Michael, W.M.1    Eder, P.S.2    Dreyfuss, G.3
  • 80
    • 0015491070 scopus 로고
    • Morphological studies of transcription
    • Copenh
    • Miller OL Jr, Bakken AH. 1972. Morphological studies of transcription. Acta Endocrinol Suppl (Copenh) 168: 155-177.
    • (1972) Acta Endocrinol Suppl , vol.168 , pp. 155-177
    • Miller Jr., O.L.1    Bakken, A.H.2
  • 81
    • 0033517103 scopus 로고    scopus 로고
    • Purification and biochemical characterization of interchromatin granule clusters
    • Mintz PJ, Patterson SD, Neuwald AF, Spahr CS, Spector DL. 1999. Purification and biochemical characterization of interchromatin granule clusters. EMBO J 18: 4308-4320.
    • (1999) EMBO J , vol.18 , pp. 4308-4320
    • Mintz, P.J.1    Patterson, S.D.2    Neuwald, A.F.3    Spahr, C.S.4    Spector, D.L.5
  • 82
    • 15744390704 scopus 로고    scopus 로고
    • Genetic and physiological responses of Bacillus subtilis to metal ion stress
    • DOI 10.1111/j.1365-2958.2005.04642.x
    • Moore CM, Gaballa A, Hui M, Ye RW, Helmann JD. 2005. Genetic and physiological responses of Bacillus subtilis to metal ion stress. Mol Microbiol 57: 27-40. (Pubitemid 40896595)
    • (2005) Molecular Microbiology , vol.57 , Issue.1 , pp. 27-40
    • Moore, C.M.1    Gaballa, A.2    Hui, M.3    Ye, R.W.4    Helmann, J.D.5
  • 83
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • Mourelatos Z, Abel L, Yong J, Kataoka N, 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.3    Kataoka, N.4    Dreyfuss, G.5
  • 85
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A. 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    Castiglione Morelli, M.A.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 86
    • 0031230806 scopus 로고    scopus 로고
    • The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome
    • Musco G, Kharrat A, Stier G, Fraternali F, Gibson TJ, Nilges M, Pastore A. 1997. The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome. Nat Struct Biol 4: 712-716.
    • (1997) Nat Struct Biol , vol.4 , pp. 712-716
    • Musco, G.1    Kharrat, A.2    Stier, G.3    Fraternali, F.4    Gibson, T.J.5    Nilges, M.6    Pastore, A.7
  • 88
    • 0027321949 scopus 로고
    • Mutations in U1 snRNA bypass the requirement for a cell type-specific RNA splicing factor
    • DOI 10.1016/0092-8674(93)90239-M
    • Nandabalan K, Price L, Roeder GS. 1993. Mutations in U1 snRNA bypass the requirement for a cell type-specific RNA splicing factor. Cell 73: 407-415. (Pubitemid 23123317)
    • (1993) Cell , vol.73 , Issue.2 , pp. 407-415
    • Nandabalan, K.1    Price, L.2    Roeder, G.S.3
  • 89
    • 0033119019 scopus 로고    scopus 로고
    • Specific isoforms of squid, a Drosophila hnRNP, perform distinct roles in Gurken localization during oogenesis
    • Norvell A, Kelley RL, Wehr K, Schupbach T. 1999. Specific isoforms of squid, a Drosophila hnRNP, perform distinct roles in Gurken localization during oogenesis. Genes Dev 13: 864-876.
    • (1999) Genes Dev , vol.13 , pp. 864-876
    • Norvell, A.1    Kelley, R.L.2    Wehr, K.3    Schupbach, T.4
  • 90
    • 0030772963 scopus 로고    scopus 로고
    • MRNA silencing in erythroid differentiation: HnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end
    • Ostareck DH, Ostareck-Lederer A, Wilm M, Thiele BJ, Mann M, Hentze MW. 1997. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89: 597-606. (Pubitemid 27511770)
    • (1997) Cell , vol.89 , Issue.4 , 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
  • 91
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′ UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck DH, Ostareck-Lederer A, Shatsky IN, Hentze MW. 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
  • 92
    • 4344575965 scopus 로고    scopus 로고
    • Control of mRNA translation and stability in haematopoietic cells: The function of hnRNPs K and E1/E2
    • Ostareck-Lederer A, Ostareck DH. 2004. Control of mRNA translation and stability in haematopoietic cells: The function of hnRNPs K and E1/E2. Biol Cell 96: 407-411.
    • (2004) Biol Cell , vol.96 , pp. 407-411
    • Ostareck-Lederer, A.1    Ostareck, D.H.2
  • 93
    • 0028201735 scopus 로고
    • Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3' untranslated region
    • Ostareck-Lederer A, Ostareck DH, Standart N, Thiele BJ. 1994. Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region. EMBO J 13: 1476-1481. (Pubitemid 24090230)
    • (1994) EMBO Journal , vol.13 , Issue.6 , pp. 1476-1481
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Standart, N.3    Thiele, B.J.4
  • 94
    • 0031795447 scopus 로고    scopus 로고
    • Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2
    • Ostareck-Lederer A, Ostareck DH, Hentze MW. 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
  • 97
    • 0037440090 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG-1 IRES and stimulate its activity in vitro and in vivo
    • Pickering BM, Mitchell SA, Evans JR, Willis AE. 2003. Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG-1 IRES and stimulate its activity in vitro and in vivo. Nucleic Acids Res 31: 639-646.
    • (2003) Nucleic Acids Res , vol.31 , pp. 639-646
    • Pickering, B.M.1    Mitchell, S.A.2    Evans, J.R.3    Willis, A.E.4
  • 98
    • 0041589490 scopus 로고    scopus 로고
    • Expression of folate receptors and heterogeneous nuclear ribonucleoprotein E1 in women with human papillomavirus mediated transformation of cervical tissue to cancer
    • Pillai MR, Chacko P, Kesari LA, Jayaprakash PG, Jayaram HN, Antony AC. 2003. Expression of folate receptors and heterogeneous nuclear ribonucleoprotein E1 in women with human papillomavirus mediated transformation of cervical tissue to cancer. J Clin Pathol 56: 569-574.
    • (2003) J Clin Pathol , vol.56 , pp. 569-574
    • Pillai, M.R.1    Chacko, P.2    Kesari, L.A.3    Jayaprakash, P.G.4    Jayaram, H.N.5    Antony, A.C.6
  • 99
    • 0023955859 scopus 로고
    • Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins
    • Pinol-Roma S, Choi YD, Matunis MJ, 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
  • 100
    • 20444445870 scopus 로고    scopus 로고
    • Disabled-2 (Dab2) is required for transforming growth factor β-induced epithelial to mesenchymal transition (EMT)
    • Prunier C, Howe PH. 2005. Disabled-2 (Dab2) is required for transforming growth factor β-induced epithelial to mesenchymal transition (EMT). J Biol Chem 280: 17540-17548.
    • (2005) J Biol Chem , vol.280 , pp. 17540-17548
    • Prunier, C.1    Howe, P.H.2
  • 101
    • 0024603237 scopus 로고
    • A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein
    • Query CC, Bentley RC, Keene JD. 1989. A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein. Cell 57: 89-101.
    • (1989) Cell , vol.57 , pp. 89-101
    • Query, C.C.1    Bentley, R.C.2    Keene, J.D.3
  • 103
    • 0023088853 scopus 로고
    • Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1
    • Regnier P, Grunberg-Manago M, Portier C. 1987. Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1. J Biol Chem 262: 63-68. (Pubitemid 17235632)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.1 , pp. 63-68
    • Regnier, P.1    Grunberg-Manago, M.2    Portier, C.3
  • 104
    • 0014027576 scopus 로고
    • Nuclear ribonucleoprotein particles containing messenger ribonucleic acid
    • Samarina OP, Krichevskaya AA, Georgiev GP. 1966. Nuclear ribonucleoprotein particles containing messenger ribonucleic acid. Nature 210: 1319-1322.
    • (1966) Nature , vol.210 , pp. 1319-1322
    • Samarina, O.P.1    Krichevskaya, A.A.2    Georgiev, G.P.3
  • 105
    • 0014413547 scopus 로고
    • Structural organization of nuclear complexes containing DNA-like RNA
    • Samarina OP, Lukanidin EM, Molnar J, Georgiev GP. 1968. Structural organization of nuclear complexes containing DNA-like RNA. J Mol Biol 33: 251-263.
    • (1968) J Mol Biol , vol.33 , pp. 251-263
    • Samarina, O.P.1    Lukanidin, E.M.2    Molnar, J.3    Georgiev, G.P.4
  • 106
    • 0026725013 scopus 로고
    • Complete cDNA sequence of chicken vigilin, a novel protein with amplified and evolutionary conserved domains
    • Schmidt C, Henkel B, Poschl E, Zorbas H, Purschke WG, Gloe TR, Muller PK. 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    Muller, P.K.7
  • 107
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution
    • Shamoo Y, Krueger U, Rice LM, Williams KR, Steitz TA. 1997. Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution. Nat Struct Biol 4: 215-222.
    • (1997) Nat Struct Biol , vol.4 , pp. 215-222
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 109
    • 0028914042 scopus 로고
    • Soma-specific expression and cloning of PSI, a negative regulator of P element pre-mRNA splicing
    • Siebel CW, Admon A, Rio DC. 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
  • 110
    • 26944489645 scopus 로고    scopus 로고
    • Building specificity with nonspecific RNA-binding proteins
    • Singh R, 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
  • 111
    • 0028930155 scopus 로고
    • A nuclear localization domain in the hnRNP A1 protein
    • Siomi H, Dreyfuss G. 1995. A nuclear localization domain in the hnRNP A1 protein. J Cell Biol 129: 551-560.
    • (1995) J Cell Biol , vol.129 , pp. 551-560
    • Siomi, H.1    Dreyfuss, G.2
  • 112
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi H, Matunis MJ, Michael WM, Dreyfuss G. 1993a. The premRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res 21: 1193-1198. (Pubitemid 23155615)
    • (1993) Nucleic Acids Research , vol.21 , Issue.5 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 113
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
    • DOI 10.1016/0092-8674(93)90420-U
    • Siomi H, Siomi MC, Nussbaum RL, Dreyfuss G. 1993b. The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell 74: 291-298. (Pubitemid 23221705)
    • (1993) Cell , vol.74 , Issue.2 , pp. 291-298
    • Siomi, H.1    Siomi, M.C.2    Nussbaum, R.L.3    Dreyfuss, G.4
  • 114
    • 0037423817 scopus 로고    scopus 로고
    • Post-transcriptional control of renin synthesis: Identification of proteins interacting with renin mRNA 3́-untranslated region
    • Skalweit A, Doller A, Huth A, Kahne T, Persson PB, Thiele BJ. 2003. Post-transcriptional control of renin synthesis: Identification of proteins interacting with renin mRNA 3́-untranslated region. Circ Res 92: 419-427.
    • (2003) Circ Res , vol.92 , pp. 419-427
    • Skalweit, A.1    Doller, A.2    Huth, A.3    Kahne, T.4    Persson, P.B.5    Thiele, B.J.6
  • 115
    • 0019886296 scopus 로고
    • Structural organization of nascent transcripts and hnRNA molecules in amphibian oocytes
    • Sommerville J, Scheer U. 1981. Structural organization of nascent transcripts and hnRNA molecules in amphibian oocytes. Mol Biol Rep 7: 53-56.
    • (1981) Mol Biol Rep , vol.7 , pp. 53-56
    • Sommerville, J.1    Scheer, U.2
  • 116
    • 0020065680 scopus 로고
    • Mild nuclease treatment as a probe for a nonrandom distribution of adenovirus-specific RNA sequences and of cellular RNA in nuclear ribonucleoprotein fibrils
    • Stevenin J, Gattoni R, Keohavong P, Jacob M. 1982. Mild nuclease treatment as a probe for a nonrandom distribution of adenovirus-specific RNA sequences and of cellular RNA in nuclear ribonucleoprotein fibrils. J Mol Biol 155: 185-205.
    • (1982) J Mol Biol , vol.155 , pp. 185-205
    • Stevenin, J.1    Gattoni, R.2    Keohavong, P.3    Jacob, M.4
  • 117
    • 9344245694 scopus 로고    scopus 로고
    • RNA-binding proteins heterogeneous nuclear ribonucleoprotein A1, E1, and K are involved in post-transcriptional control of collagen I and III synthesis
    • Thiele BJ, Doller A, Kahne T, Pregla R, Hetzer R, Regitz-Zagrosek V. 2004. RNA-binding proteins heterogeneous nuclear ribonucleoprotein A1, E1, and K are involved in post-transcriptional control of collagen I and III synthesis. Circ Res 95: 1058-1066.
    • (2004) Circ Res , vol.95 , pp. 1058-1066
    • Thiele, B.J.1    Doller, A.2    Kahne, T.3    Pregla, R.4    Hetzer, R.5    Regitz-Zagrosek, V.6
  • 118
    • 9644268929 scopus 로고    scopus 로고
    • Phylogenetically conserved binding of specific K homology domain proteins to the 3́-untranslated region of the vertebrate middle neurofilament mRNA
    • Thyagarajan A, Szaro BG. 2004. Phylogenetically conserved binding of specific K homology domain proteins to the 3́-untranslated region of the vertebrate middle neurofilament mRNA. J Biol Chem 279: 49680-49688.
    • (2004) J Biol Chem , vol.279 , pp. 49680-49688
    • Thyagarajan, A.1    Szaro, B.G.2
  • 119
    • 44449098839 scopus 로고    scopus 로고
    • Dynamic endogenous association of neurofilament mRNAs with K-homology domain ribonucleoproteins in developing cerebral cortex
    • Thyagarajan A, Szaro BG. 2008. Dynamic endogenous association of neurofilament mRNAs with K-homology domain ribonucleoproteins in developing cerebral cortex. Brain Res 1189: 33-42.
    • (2008) Brain Res , vol.1189 , pp. 33-42
    • Thyagarajan, A.1    Szaro, B.G.2
  • 120
    • 0029866905 scopus 로고    scopus 로고
    • Assignment of human KH-box-containing genes by in situ hybridization: HNRNPK maps to 9q21.32-q21.33, PCBP1 to 2p12-p13, and PCBP2 to 12q13.12-q13.13, distal to FRA12A
    • Tommerup N, Leffers H. 1996. Assignment of human KH-box-containing genes by in situ hybridization: HNRNPK maps to 9q21.32-q21.33, PCBP1 to 2p12-p13, and PCBP2 to 12q13.12-q13.13, distal to FRA12A. Genomics 32: 297-298.
    • (1996) Genomics , vol.32 , pp. 297-298
    • Tommerup, N.1    Leffers, H.2
  • 121
    • 0029087624 scopus 로고
    • Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies
    • Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B. 1995. Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J 14: 4578-4588.
    • (1995) EMBO J , vol.14 , pp. 4578-4588
    • Urlaub, H.1    Kruft, V.2    Bischof, O.3    Muller, E.C.4    Wittmann-Liebold, B.5
  • 122
    • 0031451912 scopus 로고    scopus 로고
    • STAR, a gene family involved in signal transduction and activation of RNA
    • DOI 10.1016/S0168-9525(97)01269-9
    • Vernet C, Artzt K. 1997. STAR, a gene family involved in signal transduction and activation of RNA. Trends Genet 13: 479-484. (Pubitemid 28004921)
    • (1997) Trends in Genetics , vol.13 , Issue.12 , pp. 479-484
    • Vernet, C.1    Artzt, K.2
  • 124
    • 0038777186 scopus 로고    scopus 로고
    • Regulation of α-globin mRNA stability
    • Maywood
    • Waggoner SA, Liebhaber SA. 2003. Regulation of α-globin mRNA stability. Exp Biol Med (Maywood) 228: 387-395.
    • (2003) Exp Biol Med , vol.228 , pp. 387-395
    • Waggoner, S.A.1    Liebhaber, S.A.2
  • 125
    • 0034677202 scopus 로고    scopus 로고
    • Identification of an erythroid-enriched endoribonuclease activity involved in specific mRNA cleavage
    • Wang Z, Kiledjian M. 2000a. Identification of an erythroid-enriched endoribonuclease activity involved in specific mRNA cleavage. EMBO J 19: 295-305. (Pubitemid 30042711)
    • (2000) EMBO Journal , vol.19 , Issue.2 , pp. 295-305
    • Wang, Z.1    Kiledjian, M.2
  • 126
    • 0033847384 scopus 로고    scopus 로고
    • The poly(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity
    • Wang Z, Kiledjian M. 2000b. The poly(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity. Mol Cell Biol 20: 6334-6341.
    • (2000) Mol Cell Biol , vol.20 , pp. 6334-6341
    • Wang, Z.1    Kiledjian, M.2
  • 127
    • 0033066673 scopus 로고    scopus 로고
    • An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro
    • Wang Z, Day N, Trifillis P, 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.1    Day, N.2    Trifillis, P.3    Kiledjian, M.4
  • 128
    • 0030250111 scopus 로고    scopus 로고
    • The roles of heterogeneous nuclear ribonucleoproteins (hnRNP) in RNA metabolism
    • Weighardt F, Biamonti G, Riva S. 1996. The roles of heterogeneous nuclear ribonucleoproteins (hnRNP) in RNA metabolism. Bioessays 18: 747-756. (Pubitemid 26351967)
    • (1996) BioEssays , vol.18 , Issue.9 , pp. 747-756
    • Weighardt, F.1    Biamonti, G.2    Riva, S.3
  • 129
    • 0028148498 scopus 로고
    • Erythroid cell-specific determinants of α-globin mRNA stability
    • Weiss IM, Liebhaber SA. 1994. Erythroid cell-specific determinants of α-globin mRNA stability. Mol Cell Biol 14: 8123-8132.
    • (1994) Mol Cell Biol , vol.14 , pp. 8123-8132
    • Weiss, I.M.1    Liebhaber, S.A.2
  • 130
    • 0035873775 scopus 로고    scopus 로고
    • Il-10 up-regulates macrophage expression of the S100 protein S100A8
    • Xu K, Yen T, Geczy CL. 2001. Il-10 up-regulates macrophage expression of the S100 protein S100A8. J Immunol 166: 6358-6366.
    • (2001) J Immunol , vol.166 , pp. 6358-6366
    • Xu, K.1    Yen, T.2    Geczy, C.L.3
  • 132
    • 0034898553 scopus 로고    scopus 로고
    • Structural and functional analysis of an mRNP complex that mediates the high stability of human β-globin mRNA
    • Yu J, Russell JE. 2001. Structural and functional analysis of an mRNP complex that mediates the high stability of human β-globin mRNA. Mol Cell Biol 21: 5879-5888.
    • (2001) Mol Cell Biol , vol.21 , pp. 5879-5888
    • Yu, J.1    Russell, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.