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Volumn 90, Issue 5, 1998, Pages 407-426

Active nuclear import of single-stranded oligonucleotides and their complexes with non-karyophilic macromolecules

Author keywords

Nuclear import; Nuclear localization signal; Nuclear pore complex; Oligonucleotide; Oligonucleotide protein complex

Indexed keywords

BOVINE SERUM ALBUMIN; CELL PROTEIN; DIGITONIN; FLUORESCEIN ISOTHIOCYANATE; GOLD; GUANOSINE PHOSPHATE; N ETHYLMALEIMIDE; NUCLEIC ACID; OLIGODEOXYRIBONUCLEOTIDE; OLIGONUCLEOTIDE; PEROXIDASE; STREPTAVIDIN; WHEAT GERM AGGLUTININ;

EID: 0032158333     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0248-4900(98)80090-7     Document Type: Article
Times cited : (34)

References (89)
  • 1
    • 0029062194 scopus 로고
    • Extrachromosomal DNA elements in human tumor cells
    • Abken H (1995) Extrachromosomal DNA elements in human tumor cells. Cancer J 8, 94-102
    • (1995) Cancer J , vol.8 , pp. 94-102
    • Abken, H.1
  • 2
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope
    • Adam EJH and Adam SA (1994) Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J Cell Biol 125, 547-555
    • (1994) J Cell Biol , vol.125 , pp. 547-555
    • Adam, E.J.H.1    Adam, S.A.2
  • 3
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam SA, Sterne-Marr R and Gerace L (1990) Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J Cell Biol 111, 807-816
    • (1990) J Cell Biol , vol.111 , pp. 807-816
    • Adam, S.A.1    Sterne-Marr, R.2    Gerace, L.3
  • 4
    • 0029923398 scopus 로고    scopus 로고
    • Product of the oncogene-activating gene Tpr is a phosphorylated protein of the nuclear pore complex
    • Bangs PL, Sparks CA, Odgren PR and Fey EG (1996) Product of the oncogene-activating gene Tpr is a phosphorylated protein of the nuclear pore complex. J Cell Biochem 61, 48-60
    • (1996) J Cell Biochem , vol.61 , pp. 48-60
    • Bangs, P.L.1    Sparks, C.A.2    Odgren, P.R.3    Fey, E.G.4
  • 5
    • 0030951880 scopus 로고    scopus 로고
    • Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex
    • Bastos R, Ribas de Pouplana L, Enarson M, Bodoor K and Burke B (1997) Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex. J Cell Biol 137, 989-1000
    • (1997) J Cell Biol , vol.137 , pp. 989-1000
    • Bastos, R.1    De Ribas Pouplana, L.2    Enarson, M.3    Bodoor, K.4    Burke, B.5
  • 6
    • 0030769387 scopus 로고    scopus 로고
    • Vaccinia virion protein VP8, the 25 kDa product of the LHR gene, binds single-stranded DNA and RNA with similar affinity
    • Bayliss CD and Smith GL (1997) Vaccinia virion protein VP8, the 25 kDa product of the LHR gene, binds single-stranded DNA and RNA with similar affinity. Nucleic Acids Res 25, 3984-3990
    • (1997) Nucleic Acids Res , vol.25 , pp. 3984-3990
    • Bayliss, C.D.1    Smith, G.L.2
  • 7
    • 0027242052 scopus 로고
    • Electroporation enhances antisense oligodeoxynucleotide efficacy
    • Bergan R, Connell Y, Fahmy B and Neckers L (1993) Electroporation enhances antisense oligodeoxynucleotide efficacy. Nucleic Acids Res 21, 3567-3573
    • (1993) Nucleic Acids Res , vol.21 , pp. 3567-3573
    • Bergan, R.1    Connell, Y.2    Fahmy, B.3    Neckers, L.4
  • 8
    • 0032579254 scopus 로고    scopus 로고
    • The herpes simplex virus type-1 single-strand DNA-binding protein, ICP8, increases the processivity of the UL9 protein DNA helicase
    • Boehmer PE (1998) The herpes simplex virus type-1 single-strand DNA-binding protein, ICP8, increases the processivity of the UL9 protein DNA helicase. J Biol Chem 273, 2676-2683
    • (1998) J Biol Chem , vol.273 , pp. 2676-2683
    • Boehmer, P.E.1
  • 9
    • 0031043219 scopus 로고    scopus 로고
    • Nuclear localization signal peptides for the import of plasmid DNA in gene therapy (review)
    • Boulikas T (1997) Nuclear localization signal peptides for the import of plasmid DNA in gene therapy (review). Int J Oncol 10, 301-309
    • (1997) Int J Oncol , vol.10 , pp. 301-309
    • Boulikas, T.1
  • 10
    • 0025269856 scopus 로고
    • Facilitated nuclear transport of histone H1 and other small nucleophilic proteins
    • Breeuwer M and Goldfarb DS (1990) Facilitated nuclear transport of histone H1 and other small nucleophilic proteins. Cell 60, 999-1008
    • (1990) Cell , vol.60 , pp. 999-1008
    • Breeuwer, M.1    Goldfarb, D.S.2
  • 11
    • 0028345077 scopus 로고
    • Role of different domains in the self-association of rat nucleoporin p62
    • Buss F, Kent H, Stewart M, Bailer SM and Hanover JA (1994) Role of different domains in the self-association of rat nucleoporin p62. J Cell Sci 107, 631-638
    • (1994) J Cell Sci , vol.107 , pp. 631-638
    • Buss, F.1    Kent, H.2    Stewart, M.3    Bailer, S.M.4    Hanover, J.A.5
  • 12
    • 0028091980 scopus 로고
    • Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex
    • Byrd D, Sweet DJ, Panté N, Konstantinov KN, Guan T, Saphire ACS, Mitchell PJ, Cooper CS, Aebi U and Gerace L (1994) Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. J Cell Biol 127, 1515-1526
    • (1994) J Cell Biol , vol.127 , pp. 1515-1526
    • Byrd, D.1    Sweet, D.J.2    Panté, N.3    Konstantinov, K.N.4    Guan, T.5    Saphire, A.C.S.6    Mitchell, P.J.7    Cooper, C.S.8    Aebi, U.9    Gerace, L.10
  • 13
    • 0025669849 scopus 로고
    • Interaction of intermediate filaments with cell structures
    • Carmo-Fonseca M and David-Ferreira JF (1990) Interaction of intermediate filaments with cell structures. Electron Microsc Rev 3, 115-141
    • (1990) Electron Microsc Rev , vol.3 , pp. 115-141
    • Carmo-Fonseca, M.1    David-Ferreira, J.F.2
  • 15
    • 0027503286 scopus 로고
    • Characterization of the nuclear binding sites of oligodeoxyribonucleotides and their analogs
    • Clarenc J-P, Lebleu B and Léonetti J-P (1993) Characterization of the nuclear binding sites of oligodeoxyribonucleotides and their analogs. J Biol Chem 268, 5600-5604
    • (1993) J Biol Chem , vol.268 , pp. 5600-5604
    • Clarenc, J.-P.1    Lebleu, B.2    Léonetti, J.-P.3
  • 16
    • 0025915718 scopus 로고
    • Import of simian virus 40 virions through nuclear pore complexes
    • Clever J, Yamada M and Kasamatsu H (1991) Import of simian virus 40 virions through nuclear pore complexes. Proc Natl Acad Sci USA 88, 7333-7337
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7333-7337
    • Clever, J.1    Yamada, M.2    Kasamatsu, H.3
  • 17
    • 0029908918 scopus 로고    scopus 로고
    • Nuclear localization signal of SV40 T antigen directs import of plasmid DNA into sea urchin male pronuclei in vitro
    • Collas P and Aleström P (1996) Nuclear localization signal of SV40 T antigen directs import of plasmid DNA into sea urchin male pronuclei in vitro. Mol Reprod Dev 45, 431-438
    • (1996) Mol Reprod Dev , vol.45 , pp. 431-438
    • Collas, P.1    Aleström, P.2
  • 18
    • 0031317901 scopus 로고    scopus 로고
    • Nuclear localization signals: A driving force for nuclear transport of plasmid DNA in zebrafish
    • Collas P and Aleström P (1997) Nuclear localization signals: a driving force for nuclear transport of plasmid DNA in zebrafish. Biochem Cell Biol 75, 633-640
    • (1997) Biochem Cell Biol , vol.75 , pp. 633-640
    • Collas, P.1    Aleström, P.2
  • 19
    • 0025771404 scopus 로고
    • Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylated region
    • Cordes V, Waizenegger I and Krohne G (1991) Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylated region. Eur J Cell Biol 55, 31-47
    • (1991) Eur J Cell Biol , vol.55 , pp. 31-47
    • Cordes, V.1    Waizenegger, I.2    Krohne, G.3
  • 21
    • 0029045245 scopus 로고
    • The mechanism of nuclear transport of natural or artificial transport substrates in digitonin-permeabilized cells
    • Cserpán I and Udvardy A (1995) The mechanism of nuclear transport of natural or artificial transport substrates in digitonin-permeabilized cells. J Cell Sci 108, 1849-1861
    • (1995) J Cell Sci , vol.108 , pp. 1849-1861
    • Cserpán, I.1    Udvardy, A.2
  • 22
    • 0023854794 scopus 로고
    • Inhibition of nuclear accumulation of karyophilic proteins by microinjection of the lectin WGA
    • Dabauvalle M-C, Schultz B, Scheer U and Peters R (1988) Inhibition of nuclear accumulation of karyophilic proteins by microinjection of the lectin WGA. Exp Cell Res 174, 291-296
    • (1988) Exp Cell Res , vol.174 , pp. 291-296
    • Dabauvalle, M.-C.1    Schultz, B.2    Scheer, U.3    Peters, R.4
  • 23
    • 0019830409 scopus 로고
    • Localization of gold in biological tissue. A photochemical method for light and electronmicroscopy
    • Danscher G (1981) Localization of gold in biological tissue. A photochemical method for light and electronmicroscopy. Histochemistry 71, 81-88
    • (1981) Histochemistry , vol.71 , pp. 81-88
    • Danscher, G.1
  • 24
    • 0028893599 scopus 로고
    • Direct interaction of nucleoporin p62 with mRNA during its export from the nucleus
    • Dargemont C, Schmidt-Zachmann MS and Kühn LC (1995) Direct interaction of nucleoporin p62 with mRNA during its export from the nucleus. J Cell Sci 108, 257-263
    • (1995) J Cell Sci , vol.108 , pp. 257-263
    • Dargemont, C.1    Schmidt-Zachmann, M.S.2    Kühn, L.C.3
  • 25
    • 0018858340 scopus 로고
    • Laser temperature jump study of solvent effects on poly(adenylic acid) stacking
    • Dewey TG and Turner DH (1980) Laser temperature jump study of solvent effects on poly(adenylic acid) stacking. Biochemistry 19, 1681-1685
    • (1980) Biochemistry , vol.19 , pp. 1681-1685
    • Dewey, T.G.1    Turner, D.H.2
  • 26
    • 0009674815 scopus 로고
    • Fingers in the pore
    • Dingwall C (1993) Fingers in the pore. Curr Biol 3, 297-299
    • (1993) Curr Biol , vol.3 , pp. 297-299
    • Dingwall, C.1
  • 27
    • 0028940657 scopus 로고
    • Nuclear import of glycoconjugates is distinct from the classical NLS pathway
    • Duverger E, Pellerin-Mendes C, Mayer R, Roche A-C and Monsigny M (1995) Nuclear import of glycoconjugates is distinct from the classical NLS pathway. J Cell Sci 108, 1325-1332
    • (1995) J Cell Sci , vol.108 , pp. 1325-1332
    • Duverger, E.1    Pellerin-Mendes, C.2    Mayer, R.3    Roche, A.-C.4    Monsigny, M.5
  • 28
    • 0024094917 scopus 로고
    • The effects of variations in the number and sequence of targeting signals on nuclear uptake
    • Dworetzky SI, Lanford RE and Feldherr CM (1988) The effects of variations in the number and sequence of targeting signals on nuclear uptake. J Cell Biol 107, 1279-1287
    • (1988) J Cell Biol , vol.107 , pp. 1279-1287
    • Dworetzky, S.I.1    Lanford, R.E.2    Feldherr, C.M.3
  • 29
    • 0017608298 scopus 로고
    • Inhibition of ribonucleases by ribonucleotides and transition state analogs in cell-free extracts from Ehrlich ascites tumor cells
    • Egberts E, Hackert PB and Traub P (1977) Inhibition of ribonucleases by ribonucleotides and transition state analogs in cell-free extracts from Ehrlich ascites tumor cells. Hoppe Seller's Z Physiol Chem 358, 475-490
    • (1977) Hoppe Seller's Z Physiol Chem , vol.358 , pp. 475-490
    • Egberts, E.1    Hackert, P.B.2    Traub, P.3
  • 31
    • 0027978528 scopus 로고
    • Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif
    • Fabre E, Boelens WC, Wimmer C, Mattaj IW and Hurt EC (1994) Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell 78, 275-289
    • (1994) Cell , vol.78 , pp. 275-289
    • Fabre, E.1    Boelens, W.C.2    Wimmer, C.3    Mattaj, I.W.4    Hurt, E.C.5
  • 32
    • 0032510103 scopus 로고    scopus 로고
    • Nuclear localization-independent and importin/karyopherin-independent nuclear import of β-catenin
    • Fagotto F, Glück U and Gumbiner BM (1998) Nuclear localization-independent and importin/karyopherin-independent nuclear import of β-catenin. Curr Biol 8, 181-190
    • (1998) Curr Biol , vol.8 , pp. 181-190
    • Fagotto, F.1    Glück, U.2    Gumbiner, B.M.3
  • 33
    • 0023293153 scopus 로고
    • Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores
    • Finlay DR, Newmeyer DD, Price TM and Forbes DJ (1987) Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J Cell Biol 104, 189-200
    • (1987) J Cell Biol , vol.104 , pp. 189-200
    • Finlay, D.R.1    Newmeyer, D.D.2    Price, T.M.3    Forbes, D.J.4
  • 34
    • 0027181381 scopus 로고
    • Intracellular disposition and metabolism of fluorescently-labeled unmodified and modified oligonucleotides microinjected into mammalian cells
    • Fisher TL, Terhorst T, Cao X and Wagner RW (1993) Intracellular disposition and metabolism of fluorescently-labeled unmodified and modified oligonucleotides microinjected into mammalian cells. Nucleic Acids Res 21, 3857-3865
    • (1993) Nucleic Acids Res , vol.21 , pp. 3857-3865
    • Fisher, T.L.1    Terhorst, T.2    Cao, X.3    Wagner, R.W.4
  • 35
    • 0031053791 scopus 로고    scopus 로고
    • The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88
    • Fornerod M, van Deursen J, van Baal S, Reynolds A, Davis D, Murti KG, Fransen J and Grosveld G (1997) The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J 16, 807-816
    • (1997) EMBO J , vol.16 , pp. 807-816
    • Fornerod, M.1    Van Deursen, J.2    Van Baal, S.3    Reynolds, A.4    Davis, D.5    Murti, K.G.6    Fransen, J.7    Grosveld, G.8
  • 36
    • 0025672711 scopus 로고
    • Extrachromosomal circular DNAs and genomic sequence plasticity in eukaryotic cells
    • Gaubatz JW (1990) Extrachromosomal circular DNAs and genomic sequence plasticity in eukaryotic cells. Mutat Res 237, 271-292
    • (1990) Mutat Res , vol.237 , pp. 271-292
    • Gaubatz, J.W.1
  • 37
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich D and Mattaj IW (1996) Nucleocytoplasmic transport. Science 271, 1513-1518
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 38
    • 77956990599 scopus 로고
    • Spectrophotometric determination of avidin and biotin
    • Green NM (1970) Spectrophotometric determination of avidin and biotin. Methods Enzymol 18A, 418-424
    • (1970) Methods Enzymol , vol.18 A , pp. 418-424
    • Green, N.M.1
  • 40
    • 0031586032 scopus 로고    scopus 로고
    • Binding of fluorescence- and gold-labeled oligodeoxyribonucleotides to cytoplasmic intermediate filaments in epithelial and fibroblast cells
    • Hartig R, Huang Y, Janetzko A, Shoeman R, Grüb S and Traub P (1997) Binding of fluorescence- and gold-labeled oligodeoxyribonucleotides to cytoplasmic intermediate filaments in epithelial and fibroblast cells. Exp Cell Res 233, 169-186
    • (1997) Exp Cell Res , vol.233 , pp. 169-186
    • Hartig, R.1    Huang, Y.2    Janetzko, A.3    Shoeman, R.4    Grüb, S.5    Traub, P.6
  • 41
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw JE, Carragher BO and Milligan RA (1992) Architecture and design of the nuclear pore complex. Cell 69, 1133-1141
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, J.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 42
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetyl-glucosamine
    • Holt GD, Snow CM, Senior A, Haltiwanger RS, Gerace L and Hart GW (1987) Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetyl-glucosamine. J Cell Biol 104, 1157-1164
    • (1987) J Cell Biol , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3    Haltiwanger, R.S.4    Gerace, L.5    Hart, G.W.6
  • 43
    • 0029767680 scopus 로고    scopus 로고
    • Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins
    • Hu T, Guan T and Gerace L (1996) Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. J Cell Biol 134, 589-601
    • (1996) J Cell Biol , vol.134 , pp. 589-601
    • Hu, T.1    Guan, T.2    Gerace, L.3
  • 44
    • 0031959356 scopus 로고    scopus 로고
    • Nuclear transport factors: Function, behavior and interaction
    • Imamoto N, Kamei Y and Yoneda Y (1998) Nuclear transport factors: function, behavior and interaction. Eur J Histochem 42, 9-20
    • (1998) Eur J Histochem , vol.42 , pp. 9-20
    • Imamoto, N.1    Kamei, Y.2    Yoneda, Y.3
  • 45
    • 0028205891 scopus 로고
    • Nuclear export of different classes of RNA is mediated by specific factors
    • Jarmolowski A, Boelens WC, Izaurralde E and Mattaj IW (1994) Nuclear export of different classes of RNA is mediated by specific factors. J Cell Biol 124, 627-635
    • (1994) J Cell Biol , vol.124 , pp. 627-635
    • Jarmolowski, A.1    Boelens, W.C.2    Izaurralde, E.3    Mattaj, I.W.4
  • 46
    • 0030726210 scopus 로고    scopus 로고
    • Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex
    • Kose S, Imamoto N, Tachibana T, Shimamoto T and Yoneda Y (1997) Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex. J Cell Biol 139, 841-849
    • (1997) J Cell Biol , vol.139 , pp. 841-849
    • Kose, S.1    Imamoto, N.2    Tachibana, T.3    Shimamoto, T.4    Yoneda, Y.5
  • 47
    • 0024817060 scopus 로고
    • Complex formation between the adenovirus DNA-binding protein and single-stranded poly (rA). Cooperativity and salt dependence
    • Kuil ME, van Amerongen H, van der Vliet PC and van Grondell R (1989) Complex formation between the adenovirus DNA-binding protein and single-stranded poly (rA). Cooperativity and salt dependence. Biochemistry 28, 9795-9800
    • (1989) Biochemistry , vol.28 , pp. 9795-9800
    • Kuil, M.E.1    Van Amerongen, H.2    Van Der Vliet, P.C.A.3    Van Grondell, R.4
  • 48
    • 0030943467 scopus 로고    scopus 로고
    • Nuclear transport of H1 histones meets the criteria of a nuclearlocalization signal-mediated process
    • Kurz M, Doenecke D and Albig W (1997) Nuclear transport of H1 histones meets the criteria of a nuclearlocalization signal-mediated process. J Cell Biochem 64, 573-578
    • (1997) J Cell Biochem , vol.64 , pp. 573-578
    • Kurz, M.1    Doenecke, D.2    Albig, W.3
  • 49
    • 0022460644 scopus 로고
    • Induction of nuclear transport with a synthetic peptide homologous to the SV 40 T antigen transport signal
    • Lanford RE, Kanda P and Kennedy RC (1986) Induction of nuclear transport with a synthetic peptide homologous to the SV 40 T antigen transport signal. Cell 46, 575-582
    • (1986) Cell , vol.46 , pp. 575-582
    • Lanford, R.E.1    Kanda, P.2    Kennedy, R.C.3
  • 52
    • 0028267843 scopus 로고
    • Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup 153
    • McMorrow I, Bastos R, Horton H and Burke B (1994) Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup 153. Biochim Biophys Acta 1217, 219-223
    • (1994) Biochim Biophys Acta , vol.1217 , pp. 219-223
    • McMorrow, I.1    Bastos, R.2    Horton, H.3    Burke, B.4
  • 53
    • 0029042717 scopus 로고
    • Mechanisms of nuclear protein import
    • Melchior F and Gerace L (1995) Mechanisms of nuclear protein import. Curr Opin Cell Biol 7, 310-318
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 310-318
    • Melchior, F.1    Gerace, L.2
  • 54
    • 0027714921 scopus 로고
    • Inhibition of nuclear protein import by non-hydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor
    • Melchior F, Paschal B, Evans J and Gerace L (1993) Inhibition of nuclear protein import by non-hydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J Cell Biol 123, 1649-1659
    • (1993) J Cell Biol , vol.123 , pp. 1649-1659
    • Melchior, F.1    Paschal, B.2    Evans, J.3    Gerace, L.4
  • 55
    • 0025806713 scopus 로고
    • Nuclear pore complex: Structure, function and regulation
    • Miller M, Park MK and Hanover JA (1991) Nuclear pore complex: structure, function and regulation. Physiol Rev 71, 909-949
    • (1991) Physiol Rev , vol.71 , pp. 909-949
    • Miller, M.1    Park, M.K.2    Hanover, J.A.3
  • 56
    • 0026723508 scopus 로고
    • The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors
    • Moore MS and Blobel G (1992) The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors. Cell 69, 939-950
    • (1992) Cell , vol.69 , pp. 939-950
    • Moore, M.S.1    Blobel, G.2
  • 57
    • 0027376308 scopus 로고
    • The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
    • Moore MS and Blobel G (1993) The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature (Lond) 365, 661-663
    • (1993) Nature (Lond) , vol.365 , pp. 661-663
    • Moore, M.S.1    Blobel, G.2
  • 58
    • 0032518468 scopus 로고    scopus 로고
    • Import and export of the nuclear protein import receptor transportin by a mechanism independent of GTP hydrolysis
    • Nakielny S and Dreyfuss G (1997) Import and export of the nuclear protein import receptor transportin by a mechanism independent of GTP hydrolysis. Curr Biol 8, 89-95
    • (1997) Curr Biol , vol.8 , pp. 89-95
    • Nakielny, S.1    Dreyfuss, G.2
  • 59
    • 0020493789 scopus 로고
    • A rapid method for the large scale purification of the intermediate filament protein vimentin by single-stranded DNA-cellulose affinity chromatography
    • Nelson WJ, Vorgias CE and Traub P (1982) A rapid method for the large scale purification of the intermediate filament protein vimentin by single-stranded DNA-cellulose affinity chromatography. Biochem Biophys Res Commun 106, 1141-1147
    • (1982) Biochem Biophys Res Commun , vol.106 , pp. 1141-1147
    • Nelson, W.J.1    Vorgias, C.E.2    Traub, P.3
  • 60
    • 0024284086 scopus 로고
    • Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocation
    • Newmeyer DD and Forbes DJ (1988) Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation. Cell 52, 641-653
    • (1988) Cell , vol.52 , pp. 641-653
    • Newmeyer, D.D.1    Forbes, D.J.2
  • 61
    • 0025274481 scopus 로고
    • An N-ethylmaleimide-sensitive cytosolic factor necessary for nuclear protein import: Requirement in signal-mediated binding to the nuclear pore
    • Newmeyer DD and Forbes DJ (1990) An N-ethylmaleimide-sensitive cytosolic factor necessary for nuclear protein import: Requirement in signal-mediated binding to the nuclear pore. J Cell Biol 110, 547-557
    • (1990) J Cell Biol , vol.110 , pp. 547-557
    • Newmeyer, D.D.1    Forbes, D.J.2
  • 62
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg EA (1997) Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature (Lond) 386, 779-787
    • (1997) Nature (Lond) , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 63
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill RE, Jaskunas R, Blobel G, Palese P and Moroianu J (1995) Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J Biol Chem 270, 22701-22704
    • (1995) J Biol Chem , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3    Palese, P.4    Moroianu, J.5
  • 64
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno M, Fornerod M and Mattaj IW (1998) Nucleocytoplasmic transport: the last 200 nanometers. Cell 92, 327-336
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1    Fornerod, M.2    Mattaj, I.W.3
  • 65
    • 0029944335 scopus 로고    scopus 로고
    • RAN/TC4 mutants identify a common requirement for snRNP and protein import into the nucleus
    • Palacios I, Weis K, Klebe C, Mattaj IW and Dingwall C (1996) RAN/TC4 mutants identify a common requirement for snRNP and protein import into the nucleus. J Cell Biol 133, 485-494
    • (1996) J Cell Biol , vol.133 , pp. 485-494
    • Palacios, I.1    Weis, K.2    Klebe, C.3    Mattaj, I.W.4    Dingwall, C.5
  • 66
    • 0029922169 scopus 로고    scopus 로고
    • Molecular dissection of the nuclear pore complex
    • Panté N and Aebi U (1996a) Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol 31, 153-199
    • (1996) Crit Rev Biochem Mol Biol , vol.31 , pp. 153-199
    • Panté, N.1    Aebi, U.2
  • 67
    • 0029797940 scopus 로고    scopus 로고
    • Sequential binding of import ligands to distinct nucleopore regions during their nuclear import
    • Panté N and Aebi U (1996b) Sequential binding of import ligands to distinct nucleopore regions during their nuclear import. Science 273, 1729-1732
    • (1996) Science , vol.273 , pp. 1729-1732
    • Panté, N.1    Aebi, U.2
  • 68
    • 0029952023 scopus 로고    scopus 로고
    • Toward the molecular dissection of protein import into nuclei
    • Panté N and Aebi U (1996c) Toward the molecular dissection of protein import into nuclei. Curr Opin Cell Biol 8, 397-406
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 397-406
    • Panté, N.1    Aebi, U.2
  • 69
    • 0027931054 scopus 로고
    • Interactions and three-dimensional localization of a group of nuclear pore complex proteins
    • Panté N, Bastos R, McMorrow I, Burke B and Aebi U (1994) Interactions and three-dimensional localization of a group of nuclear pore complex proteins. J Cell Biol 126, 603-617
    • (1994) J Cell Biol , vol.126 , pp. 603-617
    • Panté, N.1    Bastos, R.2    McMorrow, I.3    Burke, B.4    Aebi, U.5
  • 71
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways
    • Powers MA, Forbes DJ, Dahlberg JE and Lund E (1997) The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J Cell Biol 136, 241-250
    • (1997) J Cell Biol , vol.136 , pp. 241-250
    • Powers, M.A.1    Forbes, D.J.2    Dahlberg, J.E.3    Lund, E.4
  • 72
    • 0029021567 scopus 로고
    • The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex
    • Radu A, Moore MS and Blobel G (1995) The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell 81, 215-222
    • (1995) Cell , vol.81 , pp. 215-222
    • Radu, A.1    Moore, M.S.2    Blobel, G.3
  • 73
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M and Blobel G (1995) Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83, 683-692
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 74
    • 0023852444 scopus 로고
    • Nuclear protein migration involves two steps: Rapid binding at the nuclear envelope followed by slower translocation through nuclear pores
    • Richardson WD, Mills AD, Dilworth SM, Laskey RA and Dingwall C (1988) Nuclear protein migration involves two steps: Rapid binding at the nuclear envelope followed by slower translocation through nuclear pores. Cell 52, 655-664
    • (1988) Cell , vol.52 , pp. 655-664
    • Richardson, W.D.1    Mills, A.D.2    Dilworth, S.M.3    Laskey, R.A.4    Dingwall, C.5
  • 75
    • 0031949939 scopus 로고    scopus 로고
    • Characterization of the single-stranded DNA binding protein encoded by the vaccinia virus I3 gene
    • Rochester SC and Traktman P (1998) Characterization of the single-stranded DNA binding protein encoded by the vaccinia virus I3 gene. J Virol 72, 2917-2926
    • (1998) J Virol , vol.72 , pp. 2917-2926
    • Rochester, S.C.1    Traktman, P.2
  • 76
    • 0030722506 scopus 로고    scopus 로고
    • A distinct nuclear import pathway used by ribosomal proteins
    • Rout MP, Blobel G and Aitchison JD (1997) A distinct nuclear import pathway used by ribosomal proteins. Cell 89, 715-725
    • (1997) Cell , vol.89 , pp. 715-725
    • Rout, M.P.1    Blobel, G.2    Aitchison, J.D.3
  • 77
    • 0031562696 scopus 로고    scopus 로고
    • Three-dimensional visualization of the route of protein import: The role of nuclear pore complex substructures
    • Rutherford SA, Goldberg MW and Allen TD (1997) Three-dimensional visualization of the route of protein import: The role of nuclear pore complex substructures. Exp Cell Res 232, 146-160
    • (1997) Exp Cell Res , vol.232 , pp. 146-160
    • Rutherford, S.A.1    Goldberg, M.W.2    Allen, T.D.3
  • 78
    • 0031826010 scopus 로고    scopus 로고
    • Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal
    • Schmalz D, Hucho F and Buchner K (1998) Nuclear import of protein kinase C occurs by a mechanism distinct from the mechanism used by proteins with a classical nuclear localization signal. J Cell Sci 111, 1823-1830
    • (1998) J Cell Sci , vol.111 , pp. 1823-1830
    • Schmalz, D.1    Hucho, F.2    Buchner, K.3
  • 79
    • 0030770579 scopus 로고    scopus 로고
    • Fluorescence microscopic comparison of the binding of phosphodiester and phophorothioate (antisense) oligodeoxyribonucleotides to subcellular structures, including intermediate filaments, the endoplasmic reticulum and the nuclear interior
    • Shoeman RL, Hartig R, Huang Y, Grüb S and Traub P (1997) Fluorescence microscopic comparison of the binding of phosphodiester and phophorothioate (antisense) oligodeoxyribonucleotides to subcellular structures, including intermediate filaments, the endoplasmic reticulum and the nuclear interior. Antisense Nucleic Acid Drug Dev 7, 291-308
    • (1997) Antisense Nucleic Acid Drug Dev , vol.7 , pp. 291-308
    • Shoeman, R.L.1    Hartig, R.2    Huang, Y.3    Grüb, S.4    Traub, P.5
  • 80
    • 0024230284 scopus 로고
    • The binding in vitro of the intermediate filament protein vimentin to synthetic oligonucleotides containing telomere sequences
    • Shoeman RL, Wadle S, Scherbarth A and Traub P (1988) The binding in vitro of the intermediate filament protein vimentin to synthetic oligonucleotides containing telomere sequences. J Biol Chem 263, 18744-18749
    • (1988) J Biol Chem , vol.263 , pp. 18744-18749
    • Shoeman, R.L.1    Wadle, S.2    Scherbarth, A.3    Traub, P.4
  • 81
    • 0029087973 scopus 로고
    • Nuclear delivery of antisense oligodeoxynucleotides through reversible permeabilization of human leukemia cells with streptolysin O
    • Spitler DG and Tidd DM (1995) Nuclear delivery of antisense oligodeoxynucleotides through reversible permeabilization of human leukemia cells with streptolysin O. Antisense Res Dev 5, 13-21
    • (1995) Antisense Res Dev , vol.5 , pp. 13-21
    • Spitler, D.G.1    Tidd, D.M.2
  • 82
    • 0027458374 scopus 로고
    • A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm
    • Sukegawa J and Blobel G (1993) A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Cell 72, 29-38
    • (1993) Cell , vol.72 , pp. 29-38
    • Sukegawa, J.1    Blobel, G.2
  • 83
    • 0028790401 scopus 로고
    • Taking from the cytoplasm and giving to the pore: Soluble transport factors in nuclear protein import
    • Sweet DJ and Gerace L (1995) Taking from the cytoplasm and giving to the pore: soluble transport factors in nuclear protein import. Trends Cell Biol 5, 444-447
    • (1995) Trends Cell Biol , vol.5 , pp. 444-447
    • Sweet, D.J.1    Gerace, L.2
  • 84
    • 0029905455 scopus 로고    scopus 로고
    • A GTPase distinct from Ran is involved in nuclear protein import
    • Sweet DJ and Gerace L (1996) A GTPase distinct from Ran is involved in nuclear protein import. J Cell Biol 133, 971-983
    • (1996) J Cell Biol , vol.133 , pp. 971-983
    • Sweet, D.J.1    Gerace, L.2
  • 85
    • 0032455645 scopus 로고    scopus 로고
    • Colocalization of single ribosomes with intermediate filaments in puromycin-treated and serum-starved mouse embryo fibroblasts
    • in press
    • Traub P, Bauer C, Hartig R, Grüb S and Stahl J (1998) Colocalization of single ribosomes with intermediate filaments in puromycin-treated and serum-starved mouse embryo fibroblasts. Biol Cell, in press
    • (1998) Biol Cell
    • Traub, P.1    Bauer, C.2    Hartig, R.3    Grüb, S.4    Stahl, J.5
  • 86
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region
    • Wu J, Matunis MJ, Kraemer D, Blobel G and Coutavas E (1995) Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J Biol Chem 270, 14209-14213
    • (1995) J Biol Chem , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5
  • 87
    • 0025299610 scopus 로고
    • Reconstitution of influenza virus RNA-nucleoprotein complexes structurally resembling native viral ribonucleoprotein cores
    • Yamanaka K, Ishihama A and Nagata K (1990) Reconstitution of influenza virus RNA-nucleoprotein complexes structurally resembling native viral ribonucleoprotein cores. J Biol Chem 265, 11151-11155
    • (1990) J Biol Chem , vol.265 , pp. 11151-11155
    • Yamanaka, K.1    Ishihama, A.2    Nagata, K.3
  • 88
    • 0030984329 scopus 로고    scopus 로고
    • Cloning and characterization of human karyopherin β
    • Yaseen NR and Blobel G (1997) Cloning and characterization of human karyopherin β. Proc Natl Acad Sci USA 94, 4451-4456
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4451-4456
    • Yaseen, N.R.1    Blobel, G.2


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