메뉴 건너뛰기




Volumn 3, Issue C, 1996, Pages 1-47

The nuclear pore complex. Toward its molecular architecture, structure, and function

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0344231927     PISSN: 1874592X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-592X(96)80003-5     Document Type: Review
Times cited : (1)

References (121)
  • 1
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear localization sequence-mediated binding to the nuclear envelope
    • Adam J.H., and Adam S.A. Identification of cytosolic factors required for nuclear localization sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125 (1994) 547-555
    • (1994) J. Cell Biol. , vol.125 , pp. 547-555
    • Adam, J.H.1    Adam, S.A.2
  • 2
    • 0026042170 scopus 로고
    • Cytosolic proteins that specifically bind nuclear localization signals are receptors for nuclear import
    • Adam S.A., and Gerace L. Cytosolic proteins that specifically bind nuclear localization signals are receptors for nuclear import. Cell 66 (1991) 837-847
    • (1991) Cell , vol.66 , pp. 837-847
    • Adam, S.A.1    Gerace, L.2
  • 3
    • 0024581538 scopus 로고
    • Identification of specifically binding proteins for a nuclear location sequence
    • Adam S.A., Lobl T.J., Mitchell M.A., and Gerace L. Identification of specifically binding proteins for a nuclear location sequence. Nature (London) 337 (1989) 276-279
    • (1989) Nature (London) , vol.337 , pp. 276-279
    • Adam, S.A.1    Lobl, T.J.2    Mitchell, M.A.3    Gerace, L.4
  • 4
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam S.A., Sterne-Marr R., and Gerace L. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111 (1990) 807-816
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Sterne-Marr, R.2    Gerace, L.3
  • 5
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi U., Cohn J., Buhle L., and Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature (London) 323 (1986) 560-564
    • (1986) Nature (London) , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 6
    • 0024417594 scopus 로고
    • Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy
    • Akey C.W. Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy. J. Cell Biol. 109 (1989) 955-970
    • (1989) J. Cell Biol. , vol.109 , pp. 955-970
    • Akey, C.W.1
  • 7
    • 0025180782 scopus 로고
    • Visualization of transport-related configurations of the nuclear pore transporter
    • Akey C.W. Visualization of transport-related configurations of the nuclear pore transporter. Biophys. J. 58 (1990) 341-355
    • (1990) Biophys. J. , vol.58 , pp. 341-355
    • Akey, C.W.1
  • 8
    • 0024438224 scopus 로고
    • Protein import through the nuclear pore complex is a multistep process
    • Akey C.W., and Goldfarb D.S. Protein import through the nuclear pore complex is a multistep process. J. Cell Biol. 109 (1989) 971-982
    • (1989) J. Cell Biol. , vol.109 , pp. 971-982
    • Akey, C.W.1    Goldfarb, D.S.2
  • 9
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey C.W., and Radermacher M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122 (1993) 1-19
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 10
    • 0025110034 scopus 로고
    • Cytoplasmic transport of ribosomal subunits microin-jected into the Xenopus laevis oocyte nucleus: A generalized, facilitated process
    • Bataillé N., Helser T., and Fried H.M. Cytoplasmic transport of ribosomal subunits microin-jected into the Xenopus laevis oocyte nucleus: A generalized, facilitated process. J. Cell Biol. 111 (1990) 1571-1582
    • (1990) J. Cell Biol. , vol.111 , pp. 1571-1582
    • Bataillé, N.1    Helser, T.2    Fried, H.M.3
  • 11
    • 0028064385 scopus 로고
    • Genetic and physical interactions between Srplp and nuclear pore complex proteins NUP1p and NUP2p
    • Belanger K.D., Kenna M.A., Wei S., and Davis L. Genetic and physical interactions between Srplp and nuclear pore complex proteins NUP1p and NUP2p. J. Cell Biol. 126 (1994) 619-630
    • (1994) J. Cell Biol. , vol.126 , pp. 619-630
    • Belanger, K.D.1    Kenna, M.A.2    Wei, S.3    Davis, L.4
  • 12
    • 0028345077 scopus 로고
    • Role of different domains in the self-association of rat nucleoporin p62
    • Buss F., Kent H., Stewart M., Bailer S.M., and Hanover J.A. Role of different domains in the self-association of rat nucleoporin p62. J. Cell Sci. 107 (1994) 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
  • 13
    • 0028091980 scopus 로고
    • Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kineses, is localized to the cytoplasmic surface of the nuclear pore complex
    • Byrd D., Sweet D.J., Panté N., Konstantinov K.N., Guan T., Saphire A.C.S., Mitchell P.J., Cooper C.S., Aebi U., and Gerace L. Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kineses, is localized to the cytoplasmic surface of the nuclear pore complex. J. Cell Biol. 127 (1994) 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
  • 14
    • 0025886328 scopus 로고
    • Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization
    • Carmo-Fonseca M., Kern H., and Hurt E.C. Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur. J. Cell Biol. 55 (1991) 17-30
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 17-30
    • Carmo-Fonseca, M.1    Kern, H.2    Hurt, E.C.3
  • 15
    • 0024411243 scopus 로고
    • Sequence requirements for synthetic peptide-mediated translocation to the nucleus
    • Chelsky D., Ralph R., and Jonak G. Sequence requirements for synthetic peptide-mediated translocation to the nucleus. Mol. Cell Biol. 9 (1989) 2487-2492
    • (1989) Mol. Cell Biol. , vol.9 , pp. 2487-2492
    • Chelsky, D.1    Ralph, R.2    Jonak, G.3
  • 16
    • 0027491276 scopus 로고
    • Localization of vault particles to the nuclear pore complex
    • Chugani D.C., Rome L.H., and Kedersha N.L. Localization of vault particles to the nuclear pore complex. J. Cell Sci. 106 (1993) 23-29
    • (1993) J. Cell Sci. , vol.106 , pp. 23-29
    • Chugani, D.C.1    Rome, L.H.2    Kedersha, N.L.3
  • 17
    • 0026766977 scopus 로고
    • Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman J.E. Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins. Annul Rev. Biochem. 61 (1992) 897-946
    • (1992) Annul Rev. Biochem. , vol.61 , pp. 897-946
    • Coleman, J.E.1
  • 18
    • 0025771404 scopus 로고
    • Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylation region
    • Cordes V., Waizenegger I., and Krohne G. Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylation region. Eur. J. Cell Biol. 55 (1991) 31-47
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 31-47
    • Cordes, V.1    Waizenegger, I.2    Krohne, G.3
  • 20
    • 0023823395 scopus 로고
    • r 68,000 pore complex protein interfere with nuclear protein uptake in Xenopus oocytes
    • r 68,000 pore complex protein interfere with nuclear protein uptake in Xenopus oocytes. Chromosoma 97 (1988) 193-197
    • (1988) Chromosoma , vol.97 , pp. 193-197
    • Dabauvalle, M.-C.1    Benevente, R.2    Chaly, N.3
  • 21
    • 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. Inhibition of nuclear accumulation of karyophilic proteins by microinjection of the lectin WGA. Exp. Cell Res. 174 (1988) 291-296
    • (1988) Exp. Cell Res. , vol.174 , pp. 291-296
    • Dabauvalle, M.-C.1    Schultz, B.2    Scheer, U.3    Peters, R.4
  • 22
    • 0025223824 scopus 로고
    • Identification of a soluble precursor complex essential for nuclear pore assemble in vitro
    • Dabauvalle M.-C., Loos K., and Scheer U. Identification of a soluble precursor complex essential for nuclear pore assemble in vitro. Chromosoma 100 (1990) 56-66
    • (1990) Chromosoma , vol.100 , pp. 56-66
    • Dabauvalle, M.-C.1    Loos, K.2    Scheer, U.3
  • 23
    • 0026636221 scopus 로고
    • Export of mRNA from microinjected nuclei of Xenopus laevis oocytes
    • Dargemont C., and Kühn L.C. Export of mRNA from microinjected nuclei of Xenopus laevis oocytes. J. Cell Biol. 118 (1992) 1-9
    • (1992) J. Cell Biol. , vol.118 , pp. 1-9
    • Dargemont, C.1    Kühn, L.C.2
  • 24
    • 0022458304 scopus 로고
    • Identification and characterization of a nuclear pore complex protein
    • Davis L.I., and Blobel G. Identification and characterization of a nuclear pore complex protein. Cell 45 (1986) 699-709
    • (1986) Cell , vol.45 , pp. 699-709
    • Davis, L.I.1    Blobel, G.2
  • 25
    • 0023449881 scopus 로고
    • The nuclear pore complex contains a family of glycoproteins that includes p62: Glycosylation through a previously unidentified cellular pathway
    • Davis L.I., and Blobel G. The nuclear pore complex contains a family of glycoproteins that includes p62: Glycosylation through a previously unidentified cellular pathway. Proc. Natl. Acad. Sci. USA 84 (1987) 7552-7556
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7552-7556
    • Davis, L.I.1    Blobel, G.2
  • 26
    • 0025367662 scopus 로고
    • The NUP1 gene encodes an essential component of the yeast nuclear pore complex
    • Davis L.I., and Fink G.R. The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Cell 61 (1990) 965-978
    • (1990) Cell , vol.61 , pp. 965-978
    • Davis, L.I.1    Fink, G.R.2
  • 28
    • 0025949412 scopus 로고
    • Nuclear targeting sequences-A consensus?
    • Dingwall C., and Laskey R.A. Nuclear targeting sequences-A consensus?. Trends Biochem. Sci. 16 (1991) 478-481
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 30
    • 0027978528 scopus 로고
    • Nupl45p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif
    • Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., and Hurt E.C. Nupl45p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell 78 (1994) 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
  • 31
    • 0024094997 scopus 로고
    • A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo
    • Featherstone C., Darby M.K., and Gerace L. A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo. J. Cell Biol. 107 (1988) 1289-1297
    • (1988) J. Cell Biol. , vol.107 , pp. 1289-1297
    • Featherstone, C.1    Darby, M.K.2    Gerace, L.3
  • 32
    • 0021717131 scopus 로고
    • Movement of a karyophilic protein through the nuclear pores of oocytes
    • Feldherr C.M., Kallenbach E., and Schultz N. Movement of a karyophilic protein through the nuclear pores of oocytes. J. Cell Biol. 99 (1984) 2216-2222
    • (1984) J. Cell Biol. , vol.99 , pp. 2216-2222
    • Feldherr, C.M.1    Kallenbach, E.2    Schultz, N.3
  • 33
    • 0023293153 scopus 로고
    • Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores
    • Finlay D.R., Newmeyer D.D., Price T.M., and Forbes D.J. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J. Cell Biol. 104 (1987) 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
  • 35
    • 0024999077 scopus 로고
    • 3G cap in the transport of U1 snRNPs to the nucleus
    • 3G cap in the transport of U1 snRNPs to the nucleus. Science 249 (1990) 786-790
    • (1990) Science , vol.249 , pp. 786-790
    • Fischer, U.1    Lührmann, R.2
  • 37
    • 0026676877 scopus 로고
    • Structure and function of the nuclear pore complex
    • Forbes D.J. Structure and function of the nuclear pore complex. Annul Rev. Cell Biol. 8 (1992) 495-527
    • (1992) Annul Rev. Cell Biol. , vol.8 , pp. 495-527
    • Forbes, D.J.1
  • 38
    • 0016326866 scopus 로고
    • Structure, biochemistry and functions of the nuclear envelope
    • Franke W.W. Structure, biochemistry and functions of the nuclear envelope. Int. Rev. Cytol. Suppl. 4 (1974) 71-236
    • (1974) Int. Rev. Cytol. Suppl. , vol.4 , pp. 71-236
    • Franke, W.W.1
  • 39
    • 0014736825 scopus 로고
    • The ultrastructure of the nuclear envelope of amphibian oocytes: A reinvestigation. I. The mature oocyte
    • Franke W.W., and Scheer U. The ultrastructure of the nuclear envelope of amphibian oocytes: A reinvestigation. I. The mature oocyte. J. Ultrastruct. Res. 30 (1970) 288-316
    • (1970) J. Ultrastruct. Res. , vol.30 , pp. 288-316
    • Franke, W.W.1    Scheer, U.2
  • 40
    • 0014739430 scopus 로고
    • The ultrastructure of the nuclear envelope of amphibian oocytes: A reinvestigation. II. The immature oocyte and dynamic aspects
    • Franke W.W., and Scheer U. The ultrastructure of the nuclear envelope of amphibian oocytes: A reinvestigation. II. The immature oocyte and dynamic aspects. J. Ultrastruct. Res. 30 (1970) 317-327
    • (1970) J. Ultrastruct. Res. , vol.30 , pp. 317-327
    • Franke, W.W.1    Scheer, U.2
  • 42
    • 0026909329 scopus 로고
    • Molecular trafficking across the nuclear pore complex
    • Gerace L. Molecular trafficking across the nuclear pore complex. Curr. Opin. Cell Biol. 4 (1992) 637-645
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 637-645
    • Gerace, L.1
  • 43
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace L., and Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19 (1980) 277-287
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 44
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L., and Burke B. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4 (1988) 335-374
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 45
    • 0020399177 scopus 로고
    • Identification of a major polypeptide of the nuclear pore complex
    • Gerace L., Ottaviano Y., and Kondor-Koch C. Identification of a major polypeptide of the nuclear pore complex. J. Cell Biol. 95 (1982) 826-837
    • (1982) J. Cell Biol. , vol.95 , pp. 826-837
    • Gerace, L.1    Ottaviano, Y.2    Kondor-Koch, C.3
  • 46
    • 0027104231 scopus 로고
    • High resolution scanning electron microscopy of the nuclear envelope: Demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores
    • Goldberg M.W., and Allen T.D. High resolution scanning electron microscopy of the nuclear envelope: Demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J. Cell Biol. 119 (1992) 1429-1440
    • (1992) J. Cell Biol. , vol.119 , pp. 1429-1440
    • Goldberg, M.W.1    Allen, T.D.2
  • 47
    • 0027525230 scopus 로고
    • The nuclear pore complex: Three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlaying structure uncovered by proteolysis
    • Goldberg M.W., and Allen T.D. The nuclear pore complex: Three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlaying structure uncovered by proteolysis. J. Cell Sci. 106 (1993) 261-274
    • (1993) J. Cell Sci. , vol.106 , pp. 261-274
    • Goldberg, M.W.1    Allen, T.D.2
  • 48
    • 0000473509 scopus 로고
    • Exploring native nuclear pore complex structure and conformation by scanning force microscopy in physiological buffers
    • Goldie K.N., Panté N., Engel A., and Aebi U. Exploring native nuclear pore complex structure and conformation by scanning force microscopy in physiological buffers. J. Vac. Sci. Technol. B 12 (1994) 1482-1485
    • (1994) J. Vac. Sci. Technol. B , vol.12 , pp. 1482-1485
    • Goldie, K.N.1    Panté, N.2    Engel, A.3    Aebi, U.4
  • 49
    • 0027291375 scopus 로고
    • Purification of NSP1 reveals complex formation with "GLFG" nucleoporins and a novel nuclear pore protein NIC96
    • Grandi P., Doye V., and Hurt E.C. Purification of NSP1 reveals complex formation with "GLFG" nucleoporins and a novel nuclear pore protein NIC96. EMBO J. 12 (1993) 3061-3071
    • (1993) EMBO J. , vol.12 , pp. 3061-3071
    • Grandi, P.1    Doye, V.2    Hurt, E.C.3
  • 50
    • 0026500909 scopus 로고
    • Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glicoprotein
    • Greber U.F., and Gerace L. Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glicoprotein. J. Cell Biol. 116 (1992) 15-30
    • (1992) J. Cell Biol. , vol.116 , pp. 15-30
    • Greber, U.F.1    Gerace, L.2
  • 51
    • 0025253486 scopus 로고
    • A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail
    • Greber U.F., Senior A., and Gerace L. A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. EMBO J. 9 (1990) 1495-1502
    • (1990) EMBO J. , vol.9 , pp. 1495-1502
    • Greber, U.F.1    Senior, A.2    Gerace, L.3
  • 52
    • 0028786983 scopus 로고
    • Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
    • Guan T., Müller S., Klier G., Panté N., Blevitt J.M., Haner M., Paschal B., Aebi U., and Gerace L. Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol. Biol. Cell 6 (1995) 1591-1603
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1591-1603
    • Guan, T.1    Müller, S.2    Klier, G.3    Panté, N.4    Blevitt, J.M.5    Haner, M.6    Paschal, B.7    Aebi, U.8    Gerace, L.9
  • 53
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg E., Wozniak R.W., and Blobel G. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J. Cell Biol. 122 (1993) 513-521
    • (1993) J. Cell Biol. , vol.122 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 54
    • 0025119137 scopus 로고
    • Monomethylated cap structures facilitate RNA export from the nucleus
    • Hamm J., and Mattaj I.W. Monomethylated cap structures facilitate RNA export from the nucleus. Cell 63 (1990) 109-118
    • (1990) Cell , vol.63 , pp. 109-118
    • Hamm, J.1    Mattaj, I.W.2
  • 55
    • 0025007910 scopus 로고
    • The trimethyguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal
    • Hamm J., Darzynkiewicz E., Tahara S.M., and Mattaj I.W. The trimethyguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal. Cell 62 (1990) 569-577
    • (1990) Cell , vol.62 , pp. 569-577
    • Hamm, J.1    Darzynkiewicz, E.2    Tahara, S.M.3    Mattaj, I.W.4
  • 56
    • 0023655430 scopus 로고
    • O-linked N-acetylglucosarnine is attached to proteins of the nuclear pore
    • Hanover J.A., Cohen C.K., Willingham M.C., and Park M.K. O-linked N-acetylglucosarnine is attached to proteins of the nuclear pore. J. Biol. Chem. 262 (1987) 9887-9894
    • (1987) J. Biol. Chem. , vol.262 , pp. 9887-9894
    • Hanover, J.A.1    Cohen, C.K.2    Willingham, M.C.3    Park, M.K.4
  • 57
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw J.E., Carragher B.O., and Milligan R.A. Architecture and design of the nuclear pore complex. Cell 69 (1992) 1133-1141
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, J.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 58
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • Holt G.D., Snow C.M., Senior A., Haltiwanger R.S., Gerace L., and Hart G.W. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J. Cell Biol. 104 (1987) 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
  • 59
    • 0024293481 scopus 로고
    • A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae
    • Hurt E.C. A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae. EMBO J. 7 (1988) 4323-4334
    • (1988) EMBO J. , vol.7 , pp. 4323-4334
    • Hurt, E.C.1
  • 60
    • 0025642478 scopus 로고
    • Targeting of a cytosolic protein to the nuclear periphery
    • Hurt E.C. Targeting of a cytosolic protein to the nuclear periphery. J. Cell Biol. 111 (1990) 2829-2837
    • (1990) J. Cell Biol. , vol.111 , pp. 2829-2837
    • Hurt, E.C.1
  • 62
    • 0026909630 scopus 로고
    • Transport of RNA between nucleus and cytoplasm
    • Izaurralde E., and Mattaj I.W. Transport of RNA between nucleus and cytoplasm. Semin. Cell Biol. 3 (1992) 279-288
    • (1992) Semin. Cell Biol. , vol.3 , pp. 279-288
    • Izaurralde, E.1    Mattaj, I.W.2
  • 63
    • 0026707360 scopus 로고
    • A cap binding protein that may mediate nuclear export of RNA polymerase II-transcribed RNAs
    • Izaurralde E., Stepinski J., Darzynkiewicz E., and Mattaj I.W. A cap binding protein that may mediate nuclear export of RNA polymerase II-transcribed RNAs. J. Cell Biol. 118 (1992) 1287-1295
    • (1992) J. Cell Biol. , vol.118 , pp. 1287-1295
    • Izaurralde, E.1    Stepinski, J.2    Darzynkiewicz, E.3    Mattaj, I.W.4
  • 64
    • 0028205891 scopus 로고
    • Nuclear export of different classes of RNA is mediated by specific factors
    • Jarmolowski A., Boelens W.C., Izaurralde E., and Mattaj I.W. Nuclear export of different classes of RNA is mediated by specific factors. J. Cell. Bio. 124 (1994) 627-635
    • (1994) J. Cell. Bio. , vol.124 , pp. 627-635
    • Jarmolowski, A.1    Boelens, W.C.2    Izaurralde, E.3    Mattaj, I.W.4
  • 65
    • 0026323478 scopus 로고
    • Toward a more complete 3-D structure of the nuclear pore complex
    • Jarnik M., and Aebi U. Toward a more complete 3-D structure of the nuclear pore complex. J. Struct. Biol. 107 (1991) 291-308
    • (1991) J. Struct. Biol. , vol.107 , pp. 291-308
    • Jarnik, M.1    Aebi, U.2
  • 66
    • 0026025407 scopus 로고
    • Vaults. III. Vault Ribonucleoprotein particles open into flower-like structures with octagonal symmetry
    • Kedersha N.L., Heuser J.E., Chugani D.C., and Rome L.H. Vaults. III. Vault Ribonucleoprotein particles open into flower-like structures with octagonal symmetry. J. Cell Biol. 112 (1991) 225-235
    • (1991) J. Cell Biol. , vol.112 , pp. 225-235
    • Kedersha, N.L.1    Heuser, J.E.2    Chugani, D.C.3    Rome, L.H.4
  • 67
    • 0027503111 scopus 로고
    • Purification and characterization of a nuclear pore glycoprotein complex containing p62
    • Kita K., Omata S., and Horigome T. Purification and characterization of a nuclear pore glycoprotein complex containing p62. J. Biochem. (Tokyo) 113 (1993) 377-382
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 377-382
    • Kita, K.1    Omata, S.2    Horigome, T.3
  • 68
    • 0027979480 scopus 로고
    • The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm
    • Kraemer D., Wozniak R.W., Blobel G., and Radu A. The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc. Natl. Acad. Sci. USA 91 (1994) 1519-1523
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1519-1523
    • Kraemer, D.1    Wozniak, R.W.2    Blobel, G.3    Radu, A.4
  • 69
    • 0027405398 scopus 로고
    • NUP2, a novel yeast nucleoporin, has functional overlap with others proteins of the nuclear pore complex
    • Loeb J.D.J., Davis L., and Fink G.F. NUP2, a novel yeast nucleoporin, has functional overlap with others proteins of the nuclear pore complex. Mol. Biol. Cell. 4 (1993) 209-222
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 209-222
    • Loeb, J.D.J.1    Davis, L.2    Fink, G.F.3
  • 70
    • 0027958413 scopus 로고
    • 3G-cap dependence of U1 and U2 snRNP transport
    • 3G-cap dependence of U1 and U2 snRNP transport. EMBO J. 13 (1994) 222-231
    • (1994) EMBO J. , vol.13 , pp. 222-231
    • Marshallsay, C.1    Lührmann, R.2
  • 72
    • 0017636049 scopus 로고
    • The nuclear and cytoplasmic pore complex. Structure, dynamics, distribution and evolution
    • Maul G.G. The nuclear and cytoplasmic pore complex. Structure, dynamics, distribution and evolution. Int. Rev. Cytol. Suppl. 6 (1977) 75-186
    • (1977) Int. Rev. Cytol. Suppl. , vol.6 , pp. 75-186
    • Maul, G.G.1
  • 73
    • 0028267843 scopus 로고
    • Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153
    • McMorrow I.M., Bastos R., Horton R., and Burke B. Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153. Biochim. Biophys. Acta 1217 (1994) 219-223
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 219-223
    • McMorrow, I.M.1    Bastos, R.2    Horton, R.3    Burke, B.4
  • 74
    • 0026704012 scopus 로고
    • Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography
    • Mehlin H., Daneholt B., and Skoglund U. Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography. Cell 69 (1992) 605-613
    • (1992) Cell , vol.69 , pp. 605-613
    • Mehlin, H.1    Daneholt, B.2    Skoglund, U.3
  • 75
    • 0027714921 scopus 로고
    • Inhibition of nuclear protein import by nonhydrolyzable 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. Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J. Cell Biol. 123 (1993) 1649-1659
    • (1993) J. Cell Biol. , vol.123 , pp. 1649-1659
    • Melchior, F.1    Paschal, B.2    Evans, J.3    Gerace, L.4
  • 76
    • 0026025536 scopus 로고
    • Multiple pathways in nuclear transport: the import of U2 snRNP occur by a novel kinetic pathway
    • Michaud N., and Goldfard D. Multiple pathways in nuclear transport: the import of U2 snRNP occur by a novel kinetic pathway. J. Cell Biol. 112 (1991) 215-223
    • (1991) J. Cell Biol. , vol.112 , pp. 215-223
    • Michaud, N.1    Goldfard, D.2
  • 77
    • 0026542398 scopus 로고
    • Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways
    • Michaud N., and Goldfard D. Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways. J. Cell Biol. 116 (1992) 851-861
    • (1992) J. Cell Biol. , vol.116 , pp. 851-861
    • Michaud, N.1    Goldfard, D.2
  • 78
    • 0026554284 scopus 로고
    • Nucleotide sequence analysis of human tpr cDNA clones
    • Mitchell P.J., and Cooper C.S. Nucleotide sequence analysis of human tpr cDNA clones. Oncogene 7 (1992) 383-388
    • (1992) Oncogene , vol.7 , pp. 383-388
    • Mitchell, P.J.1    Cooper, C.S.2
  • 79
    • 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 M.S., and Blobel G. The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors. Cell 68 (1992) 939-950
    • (1992) Cell , vol.68 , pp. 939-950
    • Moore, M.S.1    Blobel, G.2
  • 80
    • 0027376308 scopus 로고
    • The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
    • Moore M.S., and Blobel G. The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature (London) 365 (1993) 661-663
    • (1993) Nature (London) , vol.365 , pp. 661-663
    • Moore, M.S.1    Blobel, G.2
  • 81
    • 0027619054 scopus 로고
    • The nuclear pore complex and nucleocytoplasmic transport
    • Newmeyer D.D. The nuclear pore complex and nucleocytoplasmic transport. Curr. Opin. Cell Biol. 5 (1993) 395-407
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 395-407
    • Newmeyer, D.D.1
  • 82
    • 0024284086 scopus 로고
    • Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocation
    • Newmeyer D.D., and Forbes D.J. Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocation. Cell 52 (1988) 641-653
    • (1988) Cell , vol.52 , pp. 641-653
    • Newmeyer, D.D.1    Forbes, D.J.2
  • 83
    • 0025274481 scopus 로고
    • An N-ethylmaleimide-sensitive cytosolic factor necessary for nuclear protein import: Requirement in signal-mediated binding to the nuclear pore
    • Newmeyer D.D., and Forbes D.J. An N-ethylmaleimide-sensitive cytosolic factor necessary for nuclear protein import: Requirement in signal-mediated binding to the nuclear pore. J. Cell Biol. 110 (1990) 547-557
    • (1990) J. Cell Biol. , vol.110 , pp. 547-557
    • Newmeyer, D.D.1    Forbes, D.J.2
  • 84
    • 0022978288 scopus 로고
    • In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins
    • Newmeyer D.D., Finlay D.R., and Forbes D.J. In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins. J. Cell Biol. 103 (1986) 2091-2102
    • (1986) J. Cell Biol. , vol.103 , pp. 2091-2102
    • Newmeyer, D.D.1    Finlay, D.R.2    Forbes, D.J.3
  • 85
    • 0021955147 scopus 로고
    • Phosphorylation of the nuclear lamins during interphase and mitosis
    • Ottaviano Y., and Gerace L. Phosphorylation of the nuclear lamins during interphase and mitosis. J. Biol. Chem. 260 (1985) 624-632
    • (1985) J. Biol. Chem. , vol.260 , pp. 624-632
    • Ottaviano, Y.1    Gerace, L.2
  • 87
    • 0027199147 scopus 로고
    • The nuclear pore complex
    • Panté N., and Aebi U. The nuclear pore complex. J. Cell Biol. 122 (1993) 977-984
    • (1993) J. Cell Biol. , vol.122 , pp. 977-984
    • Panté, N.1    Aebi, U.2
  • 88
    • 0028316365 scopus 로고
    • Towards understanding the 3-D structure of the nuclear pore complex at the molecular level
    • Panté N., and Aebi U. Towards understanding the 3-D structure of the nuclear pore complex at the molecular level. Curr. Opin. Struct. Biol. 4 (1994) 187-196
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 187-196
    • Panté, N.1    Aebi, U.2
  • 89
    • 0027931054 scopus 로고
    • Interactions and three-dimensional localization of a group of nuclear complex proteins
    • Panté N., Bastos R., McMorrow I., Burke B., and Aebi U. Interactions and three-dimensional localization of a group of nuclear complex proteins. J. Cell Biol. 126 (1994) 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
  • 90
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Dorée M., Labbé J.C., and Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61 (1990) 591-602
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Dorée, M.3    Labbé, J.C.4    Nigg, E.A.5
  • 91
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase
    • Peter M., Heitliger E., Häner M., Aebi U., and Nigg E.A. Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J. 10 (1991) 1535-1544
    • (1991) EMBO J. , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitliger, E.2    Häner, M.3    Aebi, U.4    Nigg, E.A.5
  • 92
    • 0027395040 scopus 로고
    • Nup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGA
    • Radu A., Blobel G., and Wozniak R.W. Nup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGA. J. Cell Biol. 121 (1993) 1-9
    • (1993) J. Cell Biol. , vol.121 , pp. 1-9
    • Radu, A.1    Blobel, G.2    Wozniak, R.W.3
  • 93
    • 0028338928 scopus 로고
    • Nup107 is a novel nuclear pore complex protein that contains a leucine zipper
    • Radu A., Blobel G., and Wozniak R.W. Nup107 is a novel nuclear pore complex protein that contains a leucine zipper. J. Biol. Chem. 269 (1994) 17600-17605
    • (1994) J. Biol. Chem. , vol.269 , pp. 17600-17605
    • Radu, A.1    Blobel, G.2    Wozniak, R.W.3
  • 94
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex, and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E.L., Jarnik M., Engel A., and Aebi U. Correlation between structure and mass distribution of the nuclear pore complex, and of distinct pore complex components. J. Cell Biol. 110 (1990) 883-894
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 95
    • 0023852444 scopus 로고
    • Nuclear protein migration involves two steps: Rapid binding at the nuclear envelope followed by slower translocation through the nuclear pores
    • Richardson W.D., Mills A.D., Dilworth S.M., Laskey R.A., and Dingwall C. Nuclear protein migration involves two steps: Rapid binding at the nuclear envelope followed by slower translocation through the nuclear pores. Cell 52 (1988) 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
  • 96
    • 0002272634 scopus 로고
    • The 3-D structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy
    • Ris H. The 3-D structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy. EMSA Bull. 21 (1991) 54-56
    • (1991) EMSA Bull. , vol.21 , pp. 54-56
    • Ris, H.1
  • 97
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins J., Dilworth S.M., Laskey R.A., and Dingwall C. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence. Cell 64 (1991) 615-623
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 98
    • 0015541256 scopus 로고
    • Light and electron microscopy of rat kangaroo cells in mitosis 1: Formation and breakdown of the mitotic apparatus
    • Roos U.-P. Light and electron microscopy of rat kangaroo cells in mitosis 1: Formation and breakdown of the mitotic apparatus. Chromosoma 40 (1973) 43-82
    • (1973) Chromosoma , vol.40 , pp. 43-82
    • Roos, U.-P.1
  • 99
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout M.P., and Blobel G. Isolation of the yeast nuclear pore complex. J. Cell Biol. 123 (1993) 771-783
    • (1993) J. Cell Biol. , vol.123 , pp. 771-783
    • Rout, M.P.1    Blobel, G.2
  • 100
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70-kilodalton head shock protein or its cytoplasmic cognate
    • Shi Y., and Thomas J.O. The transport of proteins into the nucleus requires the 70-kilodalton head shock protein or its cytoplasmic cognate. Mol. Cell Biol. 12 (1992) 2186-2192
    • (1992) Mol. Cell Biol. , vol.12 , pp. 2186-2192
    • Shi, Y.1    Thomas, J.O.2
  • 101
    • 0023257987 scopus 로고
    • Monoclonal antibodies identify a group of nuclear pore complex glycoproteins
    • Snow C.M., Senior A., and Gerace L. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104 (1987) 1143-1156
    • (1987) J. Cell Biol. , vol.104 , pp. 1143-1156
    • Snow, C.M.1    Senior, A.2    Gerace, L.3
  • 102
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullan B., and Worman H.J. The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J. Cell Biol. 120 (1993) 1093-1100
    • (1993) J. Cell Biol. , vol.120 , pp. 1093-1100
    • Soullan, B.1    Worman, H.J.2
  • 103
    • 0025314491 scopus 로고
    • Primary sequence and heterologous expression of nuclear pore glycoprotein p62
    • Starr C.M., D'Onofrio M., Park M.K., and Hanover J.A. Primary sequence and heterologous expression of nuclear pore glycoprotein p62. J. Cell Biol. 110 (1990) 1861-1871
    • (1990) J. Cell Biol. , vol.110 , pp. 1861-1871
    • Starr, C.M.1    D'Onofrio, M.2    Park, M.K.3    Hanover, J.A.4
  • 104
    • 0026567673 scopus 로고
    • O-linked glycoproteins of the nuclear pore complex interact with a cytosolic factor required for nuclear protein import
    • Sterne-Marr R., Blevitt J.M., and Gerace L. O-linked glycoproteins of the nuclear pore complex interact with a cytosolic factor required for nuclear protein import. J. Cell Biol. 116 (1992) 271-280
    • (1992) J. Cell Biol. , vol.116 , pp. 271-280
    • Sterne-Marr, R.1    Blevitt, J.M.2    Gerace, L.3
  • 105
    • 0013957337 scopus 로고
    • RNA transport from nucleus to cytoplasm in Chironomus salivary glands
    • Stevens B.J., and Swift H. RNA transport from nucleus to cytoplasm in Chironomus salivary glands. J. Cell Biol. 31 (1966) 55-77
    • (1966) J. Cell Biol. , vol.31 , pp. 55-77
    • Stevens, B.J.1    Swift, H.2
  • 106
    • 1842357147 scopus 로고
    • The structure and interactions of components of nuclear envelopes from Xenopus oocyte germinal vesicles observed by heavy metal shadowing
    • Stewart M., and Whytock S. The structure and interactions of components of nuclear envelopes from Xenopus oocyte germinal vesicles observed by heavy metal shadowing. J. Cell Sci. 90 (1988) 409-423
    • (1988) J. Cell Sci. , vol.90 , pp. 409-423
    • Stewart, M.1    Whytock, S.2
  • 107
    • 0027458374 scopus 로고
    • A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm
    • Sukegawa J., and Blobel G. A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Cell 72 (1993) 29-38
    • (1993) Cell , vol.72 , pp. 29-38
    • Sukegawa, J.1    Blobel, G.2
  • 108
    • 0020472010 scopus 로고
    • A large particle associated with the perimeter of the nuclear pore complex
    • Unwin P.N.T., and Milligan R.A. A large particle associated with the perimeter of the nuclear pore complex. J. Cell Biol. 93 (1982) 63-75
    • (1982) J. Cell Biol. , vol.93 , pp. 63-75
    • Unwin, P.N.T.1    Milligan, R.A.2
  • 109
    • 0026560593 scopus 로고
    • The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA
    • Von Lindern M., Fornerod M., van Baal S., Jaegle M., de Wit T., Buijs A., and Groveld G. The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA. Mol. Cell Biol. 12 (1992) 1687-1697
    • (1992) Mol. Cell Biol. , vol.12 , pp. 1687-1697
    • Von Lindern, M.1    Fornerod, M.2    van Baal, S.3    Jaegle, M.4    de Wit, T.5    Buijs, A.6    Groveld, G.7
  • 110
    • 0025285068 scopus 로고
    • Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C
    • Ward G.E., and Kirschner M.W. Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C. Cell 61 (1990) 561-577
    • (1990) Cell , vol.61 , pp. 561-577
    • Ward, G.E.1    Kirschner, M.W.2
  • 111
    • 0027428431 scopus 로고
    • A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic
    • Wente S.R., and Blobel G. A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic. J. Cell Biol. 123 (1993) 275-284
    • (1993) J. Cell Biol. , vol.123 , pp. 275-284
    • Wente, S.R.1    Blobel, G.2
  • 112
    • 0028233485 scopus 로고
    • NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure
    • Wente S.R., and Blobel G. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J. Biol. 125 (1994) 955-969
    • (1994) J. Biol. , vol.125 , pp. 955-969
    • Wente, S.R.1    Blobel, G.2
  • 113
    • 0026463881 scopus 로고
    • A new family of yeast nuclear pore complex proteins
    • Wente S.R., Rout M.P., and Blobel G. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119 (1992) 705-723
    • (1992) J. Cell Biol. , vol.119 , pp. 705-723
    • Wente, S.R.1    Rout, M.P.2    Blobel, G.3
  • 115
    • 0027744056 scopus 로고
    • Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils
    • Wilken N., Kossner U., Senécal J.-L., Scheer U., and Dabauvalle M.-C. Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils. J. Cell Biol. 123 (1993) 1345-1354
    • (1993) J. Cell Biol. , vol.123 , pp. 1345-1354
    • Wilken, N.1    Kossner, U.2    Senécal, J.-L.3    Scheer, U.4    Dabauvalle, M.-C.5
  • 116
    • 0027049622 scopus 로고
    • A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1
    • Wimmer C., Doye V., Grandi P., Nehrbass U., and Hurt E.C. A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. EMBO J. 11 (1992) 5051-5061
    • (1992) EMBO J. , vol.11 , pp. 5051-5061
    • Wimmer, C.1    Doye, V.2    Grandi, P.3    Nehrbass, U.4    Hurt, E.C.5
  • 117
    • 0027043255 scopus 로고
    • The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope
    • Wozniak R.W., and Blobel G. The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. J. Cell Biol. 119 (1992) 1441-1449
    • (1992) J. Cell Biol. , vol.119 , pp. 1441-1449
    • Wozniak, R.W.1    Blobel, G.2
  • 118
    • 0024360678 scopus 로고
    • Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
    • Wozniak R.W., Bartnik E., and Blobel G. Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J. Cell Biol. 108 (1989) 2083-2092
    • (1989) J. Cell Biol. , vol.108 , pp. 2083-2092
    • Wozniak, R.W.1    Bartnik, E.2    Blobel, G.3
  • 119
    • 0028313943 scopus 로고
    • POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope
    • Wozniak R.W., Blobel G., and Rout M.P. POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope. J. Cell Biol. 125 (1994) 31-42
    • (1994) J. Cell Biol. , vol.125 , pp. 31-42
    • Wozniak, R.W.1    Blobel, G.2    Rout, M.P.3
  • 120
    • 0026490039 scopus 로고
    • Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae
    • Yano R., Oakes M., Yamaghishi M., Dodd J.A., and Nomura M. Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae. Mol. Cell. Biol. 12 (1992) 5640-5641
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5640-5641
    • Yano, R.1    Oakes, M.2    Yamaghishi, M.3    Dodd, J.A.4    Nomura, M.5
  • 121
    • 0021052942 scopus 로고
    • tRNA transport form the nucleus in a eukaryotic cell: Carrier-mediated translocation process
    • Zasloff M. tRNA transport form the nucleus in a eukaryotic cell: Carrier-mediated translocation process. Proc. Natl. Acad. Sci. USA 80 (1983) 6436-6440
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6436-6440
    • Zasloff, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.