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Volumn 144, Issue 6, 1999, Pages 1097-1112

A conserved biogenesis pathway for nucleoporins: Proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96

Author keywords

Nuclear pore complex; Nucleocytoplasmic transport; Nucleoporin; Proteolytic cleavage; RNA export

Indexed keywords

NUCLEOPORIN; RNA;

EID: 0033594084     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.6.1097     Document Type: Article
Times cited : (209)

References (66)
  • 1
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey, C.W., and M. Radermacher. 1993. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122:1-19.
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 2
    • 0032481309 scopus 로고    scopus 로고
    • Nup116p and Nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor Gle2p
    • Bailer, S.M., S. Siniossoglou, A. Podtelejnikov, A. Hellwig, M. Mann, and E. Hurt. 1998. Nup116p and Nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor Gle2p. EMBO (Eur. Mol. Biol. Organ.) J. 17:1107-1119.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 1107-1119
    • Bailer, S.M.1    Siniossoglou, S.2    Podtelejnikov, A.3    Hellwig, A.4    Mann, M.5    Hurt, E.6
  • 3
    • 0029197670 scopus 로고
    • Nuclear pore complex proteins
    • Bastos, R., N. Pante, and B. Burke. 1995. Nuclear pore complex proteins. Int. Rev. Cytol. 162B:257-302.
    • (1995) Int. Rev. Cytol. , vol.162 B , pp. 257-302
    • Bastos, R.1    Pante, N.2    Burke, B.3
  • 4
    • 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., L. Ribas de Pouplana, M. Enarson, K. Bodoor, and B. Burke. 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    Ribas De Pouplana, L.2    Enarson, M.3    Bodoor, K.4    Burke, B.5
  • 6
    • 37049251145 scopus 로고
    • Nuclei from rat liver: Isolation method that combines purity with high yield
    • Blobel, G., and V.R. Potter. 1966. Nuclei from rat liver: isolation method that combines purity with high yield. Science. 154:1662-1665.
    • (1966) Science , vol.154 , pp. 1662-1665
    • Blobel, G.1    Potter, V.R.2
  • 9
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown, M.S., and J.L. Goldstein. 1997. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell. 89:331-340.
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 10
    • 0031043895 scopus 로고    scopus 로고
    • Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments
    • Cordes, V.C., S. Reidenbach, H.R. Rackwitz, and W.W. Franke. 1997. Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol. 136:515-529.
    • (1997) J. Cell Biol. , vol.136 , pp. 515-529
    • Cordes, V.C.1    Reidenbach, S.2    Rackwitz, H.R.3    Franke, W.W.4
  • 11
    • 0022458304 scopus 로고
    • Identification and characterization of a nuclear pore complex protein
    • Davis, L.I., and G. Blobel. 1986. Identification and characterization of a nuclear pore complex protein. Cell. 45:699-709.
    • (1986) Cell , vol.45 , pp. 699-709
    • Davis, L.I.1    Blobel, G.2
  • 12
    • 0031038521 scopus 로고    scopus 로고
    • C-terminal truncations of the yeast nucleoporin Nup145pp produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure
    • Dockendorff, T.C., C.V. Heath, A.L. Goldstein, C.A. Snay, and C.N. Cole. 1997. C-terminal truncations of the yeast nucleoporin Nup145pp produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure. Mol. Cell. Biol. 17:906-920.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 906-920
    • Dockendorff, T.C.1    Heath, C.V.2    Goldstein, A.L.3    Snay, C.A.4    Cole, C.N.5
  • 13
    • 0021337080 scopus 로고
    • Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription
    • Dreyfuss, G., S.A. Adam, and Y.D. Choi. 1984. Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription. Mol. Cell. Biol. 4:415-423.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 415-423
    • Dreyfuss, G.1    Adam, S.A.2    Choi, Y.D.3
  • 14
    • 0023840074 scopus 로고
    • Translocation of RNA-coated gold particles through the nuclear pores of oocytes
    • Dworetzky, S., and C. Feldherr. 1988. Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J. Cell Biol. 106:575-584.
    • (1988) J. Cell Biol. , vol.106 , pp. 575-584
    • Dworetzky, S.1    Feldherr, C.2
  • 15
    • 0017134119 scopus 로고
    • A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei
    • Dwyer, N., and G. Blobel. 1976. A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei. J. Cell Biol. 70:581-591.
    • (1976) J. Cell Biol. , vol.70 , pp. 581-591
    • Dwyer, N.1    Blobel, G.2
  • 16
    • 0031004754 scopus 로고    scopus 로고
    • Defining the essential functional regions of the nucleoporin Nup145pp
    • Emtage, J.L.T., M. Bucci, J.L. Watkins, and S.R. Wente. 1997. Defining the essential functional regions of the nucleoporin Nup145pp. J. Cell Sci. 110: 911-925.
    • (1997) J. Cell Sci. , vol.110 , pp. 911-925
    • Emtage, J.L.T.1    Bucci, M.2    Watkins, J.L.3    Wente, S.R.4
  • 17
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G.I., G.K. Lewis, G. Ramsay, and J.M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 18
    • 0027978528 scopus 로고
    • Nup145pp is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif
    • Fabre, E., W.C. Boelens, C. Wimmer, I.W. Mattaj, and E.C. Hurt. 1994. Nup145pp 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
  • 19
    • 0031454975 scopus 로고    scopus 로고
    • The location of the transport gate in the nuclear pore complex
    • Feldherr, C.M., and D. Akin. 1997. The location of the transport gate in the nuclear pore complex. J. Cell Sci. 110:3065-3070.
    • (1997) J. Cell Sci. , vol.110 , pp. 3065-3070
    • Feldherr, C.M.1    Akin, D.2
  • 20
    • 0028207238 scopus 로고
    • An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis
    • Fernandez, J., L. Andrews, and S.M. Mische. 1994. An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis. Anal. Biochem. 218:112-117.
    • (1994) Anal. Biochem. , vol.218 , pp. 112-117
    • Fernandez, J.1    Andrews, L.2    Mische, S.M.3
  • 22
    • 0029869424 scopus 로고    scopus 로고
    • The nuclear pore complex and lamina: Three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy
    • Goldberg, M.W., and T.D. Allen. 1996. The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J. Mol. Biol. 257:848-865.
    • (1996) J. Mol. Biol. , vol.257 , pp. 848-865
    • Goldberg, M.W.1    Allen, T.D.2
  • 23
    • 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., S. Müller, G. Klier, N. Panté, J.M. Blevitt, M. Haner, B. Paschal, U. Aebi, and L. Gerace. 1995. 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. 6:1591-1603.
    • (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
  • 24
    • 0001823786 scopus 로고
    • Recombinant PCR
    • M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, editors. Academic Press, Inc., San Diego, CA
    • Higuchi, R. 1990. Recombinant PCR. In PCR Protocols. A Guide to Methods and Applications. M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, editors. Academic Press, Inc., San Diego, CA, 177-183.
    • (1990) PCR Protocols. A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 25
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw, J.E., B.O. Carragher, and R.A. Miligan. 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    Miligan, R.A.3
  • 26
    • 0029767680 scopus 로고    scopus 로고
    • Molecular and functional characterization of the p62 complex, an assembly of nuclear pore proteins
    • Hu, T. T. Guan, and L. Gerace. 1996. Molecular and functional characterization of the p62 complex, an assembly of nuclear pore proteins. J. Cell Biol. 134:589-601.
    • (1996) J. Cell Biol. , vol.134 , pp. 589-601
    • Hu, T.1    Guan, T.2    Gerace, L.3
  • 28
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon, D., B.L. Roberts, W.D. Richardson, and A.E. Smith. 1984. A short amino acid sequence able to specify nuclear location. Cell. 39:499-509.
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 29
    • 0030593472 scopus 로고    scopus 로고
    • RNP export is mediated by structural reorganization of the nuclear pore basket
    • Kiseleva, E., M.W. Goldberg, B. Daneholt, and T.D. Allen. 1996. RNP export is mediated by structural reorganization of the nuclear pore basket. J. Mol. Biol. 260:304-311.
    • (1996) J. Mol. Biol. , vol.260 , pp. 304-311
    • Kiseleva, E.1    Goldberg, M.W.2    Daneholt, B.3    Allen, T.D.4
  • 30
    • 0031907210 scopus 로고    scopus 로고
    • Active nuclear pore complexes in chironomus: Visualization of transporter configurations related to mRNP export
    • Kiseleva, E., M.W. Goldberg, T.D. Allen, and C.W. Akey. 1998. Active nuclear pore complexes in chironomus: visualization of transporter configurations related to mRNP export. J. Cell Sci. 111:223-236.
    • (1998) J. Cell Sci. , vol.111 , pp. 223-236
    • Kiseleva, E.1    Goldberg, M.W.2    Allen, T.D.3    Akey, C.W.4
  • 31
    • 0027979480 scopus 로고
    • The human CAN protein, a putative oncogene product associated with mycloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm
    • Kraemer, D., R.W. Wozniak, G. Blobel, and A. Radu. 1994. The human CAN protein, a putative oncogene product associated with mycloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc. Natl. Acad. Sci. USA. 91:1519-1523.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1519-1523
    • Kraemer, D.1    Wozniak, R.W.2    Blobel, G.3    Radu, A.4
  • 32
    • 0030420089 scopus 로고    scopus 로고
    • Intracellular transport of retroviral capsid components
    • Krausslich, H.-G., and R. Welker. 1996. Intracellular transport of retroviral capsid components. Curr. Top. Microbiol. Immunol. 214:25-63.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 25-63
    • Krausslich, H.-G.1    Welker, R.2
  • 33
    • 0028853451 scopus 로고
    • Differential mitotic phosphorylation of proteins of the nuclear pore complex
    • Macaulay, C. E. Meier, and D.J. Forbes. 1995. Differential mitotic phosphorylation of proteins of the nuclear pore complex. J. Biol. Chem. 270:254-262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 254-262
    • Macaulay, C.1    Meier, E.2    Forbes, D.J.3
  • 34
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M.J., E. Coutavas, and G. Blobel. 1996. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 35
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
    • Matunis, M.J., J. Wu, and G. Blobel. 1998. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140:499-509.
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 36
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj, I.W., and L. Englmeier. 1998. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67:265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 37
    • 0032080831 scopus 로고    scopus 로고
    • Two-way trafficking with ran
    • Melchior, F., and L. Gerace. 1998. Two-way trafficking with ran. Trends Cell Biol. 8:175-179.
    • (1998) Trends Cell Biol. , vol.8 , pp. 175-179
    • Melchior, F.1    Gerace, L.2
  • 38
    • 0028983494 scopus 로고
    • Mammalian karyopherin α1β and α2β heterodimers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins
    • Moroianu, J., M. Hijikata, G. Blobel, and A. Radu. 1995. Mammalian karyopherin α1β and α2β heterodimers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins. Proc. Natl. Acad. Sci. USA. 92:6532-6536.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6532-6536
    • Moroianu, J.1    Hijikata, M.2    Blobel, G.3    Radu, A.4
  • 41
    • 0025151610 scopus 로고
    • Identification of a receptor for protein import into mitochondria
    • Pain, D., H. Murakami, and G. Blobel. 1990. Identification of a receptor for protein import into mitochondria. Nature. 347:444-449.
    • (1990) Nature , vol.347 , pp. 444-449
    • Pain, D.1    Murakami, H.2    Blobel, G.3
  • 42
    • 0016652057 scopus 로고
    • Nuclear envelope permeability
    • Paine, P., L. Moore, and S. Horowitz. 1975. Nuclear envelope permeability. Nature. 254:109-114.
    • (1975) Nature , vol.254 , pp. 109-114
    • Paine, P.1    Moore, L.2    Horowitz, S.3
  • 44
    • 0028906840 scopus 로고
    • Reconstituted nuclei depleted of a vertebrate GLFG containing nuclear pore protein, p97, import but are defective in nuclear growth and replication
    • Powers, M.A., C. Macaulay, F. Masiarz, and D.J. Forbes. 1995. Reconstituted nuclei depleted of a vertebrate GLFG containing nuclear pore protein, p97, import but are defective in nuclear growth and replication. J. Cell Biol. 128: 721-736.
    • (1995) J. Cell Biol. , vol.128 , pp. 721-736
    • Powers, M.A.1    Macaulay, C.2    Masiarz, F.3    Forbes, D.J.4
  • 45
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate nucleoporin, Nup98, is an essential component of RNA export pathways
    • Powers, M.A., D.J. Forbes, J.E. Dahlberg, and E. Lund. 1997. The vertebrate nucleoporin, Nup98, is an essential component of 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
  • 46
    • 0028338928 scopus 로고
    • Nup107 is a novel nuclear pore complex protein that contains a leucine zipper
    • Radu, A., G. Blobel, and R. Wazniak. 1994. Nup107 is a novel nuclear pore complex protein that contains a leucine zipper. J. Biol. Chem. 269:17600-17605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17600-17605
    • Radu, A.1    Blobel, G.2    Wazniak, R.3
  • 47
    • 0029021567 scopus 로고
    • The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex
    • Radu, A., M.S. Moore, and G. Blobel. 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
  • 48
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt, R., A. Holzenburg, E.L Buhle, M. Jarnik, A. Engel, and U. Aebi. 1990. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110: 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
  • 49
    • 0027070310 scopus 로고
    • Novel proteases with unusual specificities
    • Resnick, N., and M.A. Zasloff. 1992. Novel proteases with unusual specificities. Curr. Biol. 4:1032-1036.
    • (1992) Curr. Biol. , vol.4 , pp. 1032-1036
    • Resnick, N.1    Zasloff, M.A.2
  • 50
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach, M., and G. Blobel. 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
  • 51
    • 0002272634 scopus 로고
    • The 3D-structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy
    • Ris, H. 1991. The 3D-structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy. EMSA Bull. 21:54-56.
    • (1991) EMSA Bull. , vol.21 , pp. 54-56
    • Ris, H.1
  • 52
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., S.M. Dilworth, R.A. Laskey, and C. Dingwall. 1991. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 64:615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 53
    • 0027989786 scopus 로고
    • Pores for thought: Nuclear pore complex proteins
    • Rout, M., and S.R. Wente. 1994. Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4:357-365.
    • (1994) Trends Cell Biol. , vol.4 , pp. 357-365
    • Rout, M.1    Wente, S.R.2
  • 54
    • 0030087693 scopus 로고    scopus 로고
    • The small GTPase Ran: How much does it run?
    • Rush, M.G., G. Drivas, and P. D'Eustachio. 1996. The small GTPase Ran: how much does it run? Bioessays. 18:103-112.
    • (1996) Bioessays , vol.18 , pp. 103-112
    • Rush, M.G.1    Drivas, G.2    D'Eustachio, P.3
  • 55
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signaling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E.H., J.A. Kisslinger, and R. Kopan. 1998. Notch-1 signaling requires ligand-induced proteolytic release of intracellular domain. Nature. 393:382-386.
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 56
    • 0343307146 scopus 로고    scopus 로고
    • Eukaryotic protein processing: Endoproteolysis of precursor proteins
    • Seidah, N.G., and M. Chretien. 1997. Eukaryotic protein processing: endoproteolysis of precursor proteins. Curr. Opin. Biotech. 8:602-607.
    • (1997) Curr. Opin. Biotech. , vol.8 , pp. 602-607
    • Seidah, N.G.1    Chretien, M.2
  • 57
    • 0028966452 scopus 로고
    • Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum
    • Shaywitz, D.A., L. Orci, M. Ravazzola, A. Swaroop, and C.A. Kaiser. 1995. Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum. J. Cell Biol. 128:769-777.
    • (1995) J. Cell Biol. , vol.128 , pp. 769-777
    • Shaywitz, D.A.1    Orci, L.2    Ravazzola, M.3    Swaroop, A.4    Kaiser, C.A.5
  • 58
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou, S., C. Wimmer, M. Rieger, V. Doye, H. Tekotte, C. Weise, S. Emig, A. Segref, and E. Hurt. 1996. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell. 84:265-275.
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.9
  • 59
    • 0027458374 scopus 로고
    • A nuclear pore complex protein that contains zinc finger motifs, binds DNA and faces the nucleoplasm
    • Sukegawa, J., and G. Blobel. 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
  • 60
    • 0000505092 scopus 로고    scopus 로고
    • The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Tang, B.L., F. Peter, J. Krijnse-Locker, S.H. Low, G. Griffiths, and W. Hong. 1997. The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol. Cell. Biol. 17:256-266.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 256-266
    • Tang, B.L.1    Peter, F.2    Krijnse-Locker, J.3    Low, S.H.4    Griffiths, G.5    Hong, W.6
  • 62
    • 0030886673 scopus 로고    scopus 로고
    • Nuclear export receptors: From importin to exportin
    • Ullman, K.S., M.A. Powers, and D.J. Forbes. 1997. Nuclear export receptors: from importin to exportin. Cell 90:967-970.
    • (1997) Cell , vol.90 , pp. 967-970
    • Ullman, K.S.1    Powers, M.A.2    Forbes, D.J.3
  • 63
    • 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., M.J. Matunis, D. Kraemer, G. Blobel, and E. Coutavas. 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
  • 64
    • 0029092146 scopus 로고
    • Differential expression of novel genes by bone marrow-derived macrophage populations
    • Yang, S.-D., L.B. Schook, and M.S. Rutherford. 1995. Differential expression of novel genes by bone marrow-derived macrophage populations. Mol. Immunol. 32:733-742.
    • (1995) Mol. Immunol. , vol.32 , pp. 733-742
    • Yang, S.-D.1    Schook, L.B.2    Rutherford, M.S.3
  • 65
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
    • Yang, Q., M.P. Rout, and C.W. Akey. 1998. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell. 1:223-234.
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3


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