메뉴 건너뛰기




Volumn 7, Issue 4, 1996, Pages 475-486

Reconstitution of nuclear pore assembly and function

Author keywords

Membrane; Nuclear transport; Nucleoporin; Pore

Indexed keywords


EID: 0000450002     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1996.0060     Document Type: Article
Times cited : (9)

References (107)
  • 1
    • 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 MW, Allen TD (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
  • 2
    • 0028652643 scopus 로고
    • Toward the molecular details of the nuclear pore complex
    • Pante N, Aebi U (1994) Toward the molecular details of the nuclear pore complex. J Struct Biol 113:179-189
    • (1994) J Struct Biol , vol.113 , pp. 179-189
    • Pante, N.1    Aebi, U.2
  • 3
    • 0027287349 scopus 로고
    • Architecture of the xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey CW, Radermacher M (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
  • 4
    • 0026634028 scopus 로고
    • The use of field emission in-lens scanning electron microscopy to study the steps of assembly of the nuclear envelope in vitro
    • Goldberg MW, Blow JJ, Allen TD (1992) The use of field emission in-lens scanning electron microscopy to study the steps of assembly of the nuclear envelope in vitro. J Struct Biol 108:257-268
    • (1992) J Struct Biol , vol.108 , pp. 257-268
    • Goldberg, M.W.1    Blow, J.J.2    Allen, T.D.3
  • 5
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw JE, Carragher BO, 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
  • 6
    • 0002272634 scopus 로고
    • The three-dimensional 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 three-dimensional 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
  • 7
    • 0026676877 scopus 로고
    • Structure and function of the nuclear pore complex
    • Forbes DJ (1992) Structure and function of the nuclear pore complex. Annu Rev Cell Biol 8:495-527
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 495-527
    • Forbes, D.J.1
  • 8
    • 0027989786 scopus 로고
    • Pores for thought: Nuclear pore complex proteins
    • Rout MP, Wente SR (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.P.1    Wente, S.R.2
  • 9
    • 0029015891 scopus 로고
    • Structural and functional organization of the nuclear envelope
    • Goldberg MW, Allen TD (1995) Structural and functional organization of the nuclear envelope. Curr Opin Cell Biol 7:301-309
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 301-309
    • Goldberg, M.W.1    Allen, T.D.2
  • 10
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis L (1995) The nuclear pore complex. Annu Rev Biochem 64:865-896
    • (1995) Annu Rev Biochem , vol.64 , pp. 865-896
    • Davis, L.1
  • 11
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout MP, Blobel G (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123:771-783
    • (1993) J Cell Biol , vol.123 , pp. 771-783
    • Rout, M.P.1    Blobel, G.2
  • 12
    • 0028887431 scopus 로고
    • Isolation and characterization of nuclear envelopes from the yeast saccharomyces
    • Strambio-de-Castillia C, Blobel G, Rout MP (1995) Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. J Cell Biol 131:19-31
    • (1995) J Cell Biol , vol.131 , pp. 19-31
    • Strambio-De-Castillia, C.1    Blobel, G.2    Rout, M.P.3
  • 13
    • 0027365762 scopus 로고
    • Nuclear localization signals (NLS)
    • Boulikas T (1993) Nuclear localization signals (NLS). Crit Rev Euk Gene Express 3:193-227
    • (1993) Crit Rev Euk Gene Express , vol.3 , pp. 193-227
    • Boulikas, T.1
  • 14
    • 0024284086 scopus 로고
    • Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocation
    • Newmeyer DD, 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
  • 15
    • 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, 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
  • 16
    • 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, 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
  • 17
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam SA, Marr RS, 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    Marr, R.S.2    Gerace, L.3
  • 18
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope
    • Adam EJ, 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.1    Adam, S.A.2
  • 19
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Görlich D, Prehn S, Laskey RA, Hartmann E (1994) Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79:767-778
    • (1994) Cell , vol.79 , pp. 767-778
    • Görlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 20
    • 0029115837 scopus 로고
    • Sequence and characterization of cytoplasmic nuclear protein import factor p97
    • Chi NC, Adam EJH, Adam SA (1995) Sequence and characterization of cytoplasmic nuclear protein import factor p97. J Cell Biol 130:265-274
    • (1995) J Cell Biol , vol.130 , pp. 265-274
    • Chi, N.C.1    Adam, E.J.H.2    Adam, S.A.3
  • 21
    • 0028950991 scopus 로고
    • Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins
    • Radu A, Blobel G, Moore MS (1995) Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc Nat Acad Sci 92:1769-1773
    • (1995) Proc Nat Acad Sci , vol.92 , pp. 1769-1773
    • Radu, A.1    Blobel, G.2    Moore, M.S.3
  • 22
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Görlich D, Kostka S, Kraft R, Dingwall C, Laskey RA, Hartmann E, Prehn S (1995) Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr Biol 5:383-392
    • (1995) Curr Biol , vol.5 , pp. 383-392
    • Görlich, D.1    Kostka, S.2    Kraft, R.3    Dingwall, C.4    Laskey, R.A.5    Hartmann, E.6    Prehn, S.7
  • 23
    • 0028962511 scopus 로고
    • Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes
    • Moroianu J, Blobel G, Radu A (1995) Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes. Proc Natl Acad Sci USA 92:2008-2011
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 24
    • 0024432012 scopus 로고
    • Yeast proteins that recognize nuclear localization sequences
    • Silver PA, Sadler I, Osborne MA (1989) Yeast proteins that recognize nuclear localization sequences. J Cell Biol 109:983-989
    • (1989) J Cell Biol , vol.109 , pp. 983-989
    • Silver, P.A.1    Sadler, I.2    Osborne, Ma.3
  • 25
    • 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 JA, Nomura M (1992) Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae. Mol Cell Biol 12:5640-5651
    • (1992) Mol Cell Biol , vol.12 , pp. 5640-5651
    • Yano, R.1    Oakes, M.2    Yamaghishi, M.3    Dodd, J.A.4    Nomura, M.5
  • 26
    • 0029059548 scopus 로고
    • Distinct functions for the two importin subunits in nuclear protein import
    • Görlich D, Vogel F, Mills AD, Hartmann E, Laskey RA (1995) Distinct functions for the two importin subunits in nuclear protein import. Nature 377:246-248
    • (1995) Nature , vol.377 , pp. 246-248
    • Görlich, D.1    Vogel, F.2    Mills, A.D.3    Hartmann, E.4    Laskey, R.A.5
  • 27
    • 0028983494 scopus 로고
    • Mammalian karyopherin α1b and α2b heterdomers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins
    • Moroianu J, Hijikata M, Blobel G, Radu A (1995) Mammalian karyopherin α1b and α2b heterdomers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins. Proc Nat Acad Sci 92:6532-6536
    • (1995) Proc Nat Acad Sci , vol.92 , pp. 6532-6536
    • Moroianu, J.1    Hijikata, M.2    Blobel, G.3    Radu, A.4
  • 28
    • 0027376308 scopus 로고
    • The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
    • Moore MS, Blobel G (1993) The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 365:661-663
    • (1993) Nature , vol.365 , pp. 661-663
    • Moore, M.S.1    Blobel, G.2
  • 29
    • 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, Gerace L (1993) 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 123:1649-1659
    • (1993) J Cell Biol , vol.123 , pp. 1649-1659
    • Melchior, F.1    Paschal, B.2    Evans, J.3    Gerace, L.4
  • 30
    • 0028559537 scopus 로고
    • Cytosolic factors in nuclear import: What's importin?
    • Powers MA, Forbes DJ (1994) Cytosolic factors in nuclear import: what's importin? Cell 79:931-934
    • (1994) Cell , vol.79 , pp. 931-934
    • Powers, M.A.1    Forbes, D.J.2
  • 31
    • 0028305912 scopus 로고
    • A g protein involved in nucleocytoplasmic transport: The role of Ran
    • Moore MS, Blobel G (1994) A G protein involved in nucleocytoplasmic transport: the role of Ran. Trends. Biochem Sci 19:211-216
    • (1994) Trends. Biochem Sci , vol.19 , pp. 211-216
    • Moore, M.S.1    Blobel, G.2
  • 33
    • 0029042717 scopus 로고
    • Mechanisms of nuclear protein import
    • Melchior F, 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
  • 34
    • 0028968743 scopus 로고
    • The importance of importin
    • Adam SA (1995) The importance of importin. Trends Cell Biol 5:189-191
    • (1995) Trends Cell Biol , vol.5 , pp. 189-191
    • Adam, S.A.1
  • 35
    • 0029089597 scopus 로고
    • Nucleocytoplasmic transport: Factors and mechanisms
    • Simos G, Hurt EC (1995) Nucleocytoplasmic transport: factors and mechanisms. FEBS Lett 369:107-112
    • (1995) FEBS Lett , vol.369 , pp. 107-112
    • Simos, G.1    Hurt, E.C.2
  • 36
    • 0028790401 scopus 로고
    • Taking from the cytoplasm and giving to the pore-soluble transport factors in nuclear protein import
    • Sweet DJ, 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
  • 37
    • 0030078822 scopus 로고    scopus 로고
    • Protein translocation-nuclear export -out of the dark
    • Moore MS (1996) Protein translocation-nuclear export -out of the dark. Curr Biol 6:137-140
    • (1996) Curr Biol , vol.6 , pp. 137-140
    • Moore, M.S.1
  • 38
    • 0029984570 scopus 로고    scopus 로고
    • Protein kinesis: Nucleocytoplasmic transport
    • Görlich D, Mattaj IW (1996) Protein kinesis: Nucleocytoplasmic transport. Science 271:1513-1518
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 39
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M, 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
  • 40
    • 0029920934 scopus 로고    scopus 로고
    • The nuclear transport factor karyopherin β binds stoichiometrically to Ran-GTP and inhibits the Ran GTPase activating protein
    • Floer M, Blobel G (1996) The nuclear transport factor karyopherin β binds stoichiometrically to Ran-GTP and inhibits the Ran GTPase activating protein. J Biol Chem 271:5313-5316
    • (1996) J Biol Chem , vol.271 , pp. 5313-5316
    • Floer, M.1    Blobel, G.2
  • 41
    • 0030028184 scopus 로고    scopus 로고
    • Ran binding domains promote the interaction of Ran with p97/β-karyopherin, linking the docking and translocation steps of nuclear import
    • Lounsbury KM, Richards SA, Perlungher RR, Macara IG (1996) Ran binding domains promote the interaction of Ran with p97/β-karyopherin, linking the docking and translocation steps of nuclear import. J Biol Chem 271:2357-2360
    • (1996) J Biol Chem , vol.271 , pp. 2357-2360
    • Lounsbury, K.M.1    Richards, S.A.2    Perlungher, R.R.3    Macara, I.G.4
  • 42
    • 0027165549 scopus 로고
    • Nucleocytoplasmic transport in the yeast Saccharomyces cerevisiae
    • Osborne MA, Silver PA (1993) Nucleocytoplasmic transport in the yeast Saccharomyces cerevisiae. Annu Rev Biochem 62:219-254
    • (1993) Annu Rev Biochem , vol.62 , pp. 219-254
    • Osborne, M.A.1    Silver, P.A.2
  • 43
    • 0025180782 scopus 로고
    • Visualization of transport-related configurations of the nuclear pore transporter
    • Akey CW (1990) Visualization of transport-related configurations of the nuclear pore transporter. Biophys J 58:341-355
    • (1990) Biophys J , vol.58 , pp. 341-355
    • Akey, C.W.1
  • 44
    • 0024438224 scopus 로고
    • Protein import through the nuclear pore complex is a multistep process
    • Akey CW, Goldfarb DS (1989) Protein import through the nuclear pore complex is a multistep process. J Cell Biol 109:971-982
    • (1989) J Cell Biol , vol.109 , pp. 971-982
    • Akey, C.W.1    Goldfarb, D.S.2
  • 45
    • 0024094917 scopus 로고
    • The effects of variations in the number and sequence of targeting signals on nuclear uptake
    • Dworetzky SI, Lanford RE, 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
  • 46
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka MJ, Masui Y (1983) Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220:719-721
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 47
    • 0021176610 scopus 로고
    • Roles of cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs
    • Lohka MI, Masui Y (1984) Roles of cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs. J Cell Biol 98:1222-1230
    • (1984) J Cell Biol , vol.98 , pp. 1222-1230
    • Lohka, M.I.1    Masui, Y.2
  • 48
    • 0023667788 scopus 로고
    • Nuclear reconstitution in vitro: Stages of assembly around protein-free DNA
    • Newport JW (1987) Nuclear reconstitution in vitro: stages of assembly around protein-free DNA. Cell 48:205-217
    • (1987) Cell , vol.48 , pp. 205-217
    • Newport, J.W.1
  • 49
    • 0023903495 scopus 로고
    • Steps in the assembly of replication-competent nuclei in a cell-free system from Xenopus eggs
    • Sheehan MA, Mills AD, Sleeman AM, Laskey RA, Blow JJ (1988) Steps in the assembly of replication-competent nuclei in a cell-free system from Xenopus eggs. J Cell Biol 106:1-12
    • (1988) J Cell Biol , vol.106 , pp. 1-12
    • Sheehan, M.A.1    Mills, A.D.2    Sleeman, A.M.3    Laskey, R.A.4    Blow, J.J.5
  • 50
    • 0027026664 scopus 로고
    • Nuclear envelope assembly following mitosis
    • Pfaller R, Newport JW (1992) Nuclear envelope assembly following mitosis. Methods Enzymol 219:60-72
    • (1992) Methods Enzymol , vol.219 , pp. 60-72
    • Pfaller, R.1    Newport, J.W.2
  • 51
    • 0026263951 scopus 로고
    • Systems for the study of nuclear assembly, DNA replication, and nuclear breakdown in Xenopus laevis egg extracts
    • Smythe C, Newport JW (1991) Systems for the study of nuclear assembly, DNA replication, and nuclear breakdown in Xenopus laevis egg extracts. Methods Cell Biol 35:449-468
    • (1991) Methods Cell Biol , vol.35 , pp. 449-468
    • Smythe, C.1    Newport, J.W.2
  • 52
    • 0026271470 scopus 로고
    • Egg extracts for nuclear import and nuclear assembly reactions
    • Newmeyer DD, Wilson KL (1991) Egg extracts for nuclear import and nuclear assembly reactions. Methods Cell Biol 36:607-634
    • (1991) Methods Cell Biol , vol.36 , pp. 607-634
    • Newmeyer, D.D.1    Wilson, K.L.2
  • 53
    • 0023293153 scopus 로고
    • Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores
    • Finlay DR, Newmeyer DD, Price TM, 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
  • 54
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • Holt GD, Snow CM, Senior A, Haltiwanger RS, Gerace L, Hart GW (1987) Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. 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
  • 55
    • 0023655430 scopus 로고
    • O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins
    • Hanover JA, Cohen CK, Willingham MC, Park MK (1987) O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J Biol Chem 262:9887-9894
    • (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
  • 56
    • 0022458304 scopus 로고
    • Identification and characterization of a nuclear pore complex protein
    • Davis LI, Blobel G (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
  • 57
    • 0025162266 scopus 로고
    • Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored
    • Finlay DR, Forbes DJ (1990) Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 60:17-29
    • (1990) Cell , vol.60 , pp. 17-29
    • Finlay, D.R.1    Forbes, D.J.2
  • 58
    • 0028906840 scopus 로고
    • Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication
    • Powers MA, Macaulay C, Masiarz F, Forbes DJ (1995) Reconstituted nuclei depleted of a vertebrate GLFG 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
  • 59
    • 0025223824 scopus 로고
    • Identification of a soluble precursor complex essential for nuclear pore assembly in vitro
    • Dabauvalle MC, Loos K, Scheer U (1990) Identification of a soluble precursor complex essential for nuclear pore assembly in vitro. Chromosoma 100:56-66
    • (1990) Chromosoma , vol.100 , pp. 56-66
    • Dabauvalle, M.C.1    Loos, K.2    Scheer, U.3
  • 60
    • 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 RW, Blobel G, Radu A (1994) The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc Nat Acad Sci 91:1519-1523
    • (1994) Proc Nat Acad Sci , vol.91 , pp. 1519-1523
    • Kraemer, D.1    Wozniak, R.W.2    Blobel, G.3    Radu, A.4
  • 61
    • 0027931054 scopus 로고
    • Interactions and three-dimensional localization of a group of nuclear pore complex proteins
    • Panté N, Bastos R, McMorrow I, Burke B, 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
  • 62
    • 0028853451 scopus 로고
    • Differential mototic phosphorylation of proteins of the nuclear pore complex
    • Macaulay C, Meier E, Forbes DJ (1995) Differential mototic phosphorylation of proteins of the nuclear pore complex. J Biol Chem 207:254-262
    • (1995) J Biol Chem , vol.207 , pp. 254-262
    • Macaulay, C.1    Meier, E.2    Forbes, D.J.3
  • 64
    • 0023823395 scopus 로고
    • Monoclonal antibodies to a Mr 68,000 pore complex glycoprotein interfere with nuclear protein uptake in Xenopus oocytes
    • Dabauvalle MC, Benavente R, Chaly N (1988) Monoclonal antibodies to a Mr 68,000 pore complex glycoprotein interfere with nuclear protein uptake in Xenopus oocytes. Chromosoma 97:193-197
    • (1988) Chromosoma , vol.97 , pp. 193-197
    • Dabauvalle, M.C.1    Benavente, R.2    Chaly, N.3
  • 65
    • 0029118089 scopus 로고
    • Mapping of nucleoporins to the center of the nuclear pore complex by post-embedding immunogold electron-microscopy
    • Grote M, Kubitscheck U, Reichelt R, Peters R (1995) Mapping of nucleoporins to the center of the nuclear pore complex by post-embedding immunogold electron-microscopy. J Cell Sci 108:2963-2972
    • (1995) J Cell Sci , vol.108 , pp. 2963-2972
    • Grote, M.1    Kubitscheck, U.2    Reichelt, R.3    Peters, R.4
  • 66
    • 0027503111 scopus 로고
    • Purification and characterization of a nuclear pore glycoprotein complex containing p62
    • Kita K, Omata S, Horigome T (1993) Purification and characterization of a nuclear pore glycoprotein complex containing p62. J Biochem 113:377-382
    • (1993) J Biochem , vol.113 , pp. 377-382
    • Kita, K.1    Omata, S.2    Horigome, T.3
  • 67
    • 0028900866 scopus 로고
    • Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: Binding of nucleoporin p54 to the rod domain of p62
    • Buss F, Stewart M (1995) Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: Binding of nucleoporin p54 to the rod domain of p62. J Cell Biol 128:251-261
    • (1995) J Cell Biol , vol.128 , pp. 251-261
    • Buss, F.1    Stewart, M.2
  • 68
    • 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 JM, Haner M, Paschal B, Aebi U, Gerace L (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
  • 69
    • 0025314491 scopus 로고
    • Primary sequence and heterologous expression of nuclear pore glycoprotein p62
    • Starr CM, D'Onofrio M, Park MK, Hanover JA (1990) Primary sequence and heterologous expression of nuclear pore glycoprotein p62. J Cell Biol 110:1861-1871
    • (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
  • 70
    • 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, Hurt EC (1991) Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur J Cell Biol 55:17-30
    • (1991) Eur J Cell Biol , vol.55 , pp. 17-30
    • Carmo-Fonseca, M.1    Kern, H.2    Hurt, E.C.3
  • 71
    • 0027291375 scopus 로고
    • Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96
    • Grandi P, Doye V, Hurt EC (1993) Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96. EMBO J 12:3061-3071
    • (1993) EMBO J , vol.12 , pp. 3061-3071
    • Grandi, P.1    Doye, V.2    Hurt, E.C.3
  • 72
    • 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, Wimmer C, Rieger M, Doye V, Tekotte H, Weise C, Emig S, Segref A, Hurt EC (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.C.9
  • 73
    • 0028365865 scopus 로고
    • Functional nuclear pores reconstituted with beta 14 galactose-modified O-linked N-acetylglucosamine modified glycoproteins
    • Miller MW, Hanover JA (1994) Functional nuclear pores reconstituted with beta 14 galactose-modified O-linked N-acetylglucosamine modified glycoproteins. J Biol Chem 269:9289-9297
    • (1994) J Biol Chem , vol.269 , pp. 9289-9297
    • Miller, M.W.1    Hanover, J.A.2
  • 74
    • 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, 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
  • 75
    • 0025612124 scopus 로고
    • A lamin-independent pathway for nuclear envelope assembly
    • Newport JW, Wilson KL, Dunphy WG (1990) A lamin-independent pathway for nuclear envelope assembly. J Cell Biol 111:2247-2259
    • (1990) J Cell Biol , vol.111 , pp. 2247-2259
    • Newport, J.W.1    Wilson, K.L.2    Dunphy, W.G.3
  • 76
    • 0027489289 scopus 로고
    • Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix
    • Jenkins H, Hölman T, Lyon C, Lane B, Stick R, Hutchison C (1993) Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix. J Cell Sci 106:275-285
    • (1993) J Cell Sci , vol.106 , pp. 275-285
    • Jenkins, H.1    Hölman, T.2    Lyon, C.3    Lane, B.4    Stick, R.5    Hutchison, C.6
  • 77
    • 0023765935 scopus 로고
    • A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro
    • Wilson KL, Newport JW (1988) A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro. J Cell Biol 107:57-68
    • (1988) J Cell Biol , vol.107 , pp. 57-68
    • Wilson, K.L.1    Newport, J.W.2
  • 78
    • 0025847037 scopus 로고
    • Assembly/disassembly of the nuclear envelope membrane: Cell cycle-dependent binding of nuclear membrane vesicles to chromatin in vitro
    • Pfaller R, Smythe C, Newport JW (1991) Assembly/disassembly of the nuclear envelope membrane: cell cycle-dependent binding of nuclear membrane vesicles to chromatin in vitro. Cell 65:209-217
    • (1991) Cell , vol.65 , pp. 209-217
    • Pfaller, R.1    Smythe, C.2    Newport, J.W.3
  • 79
    • 0026501103 scopus 로고
    • Characterization of the membrane binding and fusion events during nuclear envelope assembly using purified components
    • Newport JW, Dunphy W (1992) Characterization of the membrane binding and fusion events during nuclear envelope assembly using purified components. J Cell Biol 116:295-306
    • (1992) J Cell Biol , vol.116 , pp. 295-306
    • Newport, J.W.1    Dunphy, W.2
  • 80
    • 0030047960 scopus 로고    scopus 로고
    • Assembly of the nuclear pore: Biochemically distinct steps revealed with NEM, GTPgS, and BAPTA
    • Macaulay C, Forbes DJ (1996) Assembly of the nuclear pore: Biochemically distinct steps revealed with NEM, GTPgS, and BAPTA. J Cell Biol 132:5-20
    • (1996) J Cell Biol , vol.132 , pp. 5-20
    • Macaulay, C.1    Forbes, D.J.2
  • 81
    • 0026556684 scopus 로고
    • GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro
    • Boman AL, DelannoyMR, Wilson KL (1992) GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro. J Cell Biol 116:281-294
    • (1992) J Cell Biol , vol.116 , pp. 281-294
    • Boman, A.L.1    Delannoy, M.R.2    Wilson, K.L.3
  • 82
    • 0029021187 scopus 로고
    • Characterization of the membrane-chromatin interaction using partially purified regulatory enzymes
    • Pfaller R, Newport J (1995) Characterization of the membrane-chromatin interaction using partially purified regulatory enzymes. J Biol Chem 270:19066-19072
    • (1995) J Biol Chem , vol.270 , pp. 19066-19072
    • Pfaller, R.1    Newport, J.2
  • 83
    • 0026682791 scopus 로고
    • A role for ADP-ribosylation factor in nuclear vesicle dynamics
    • Boman AL, Taylor TC, Melancon P, Wilson KL (1992) A role for ADP-ribosylation factor in nuclear vesicle dynamics. Nature 358:512-514
    • (1992) Nature , vol.358 , pp. 512-514
    • Boman, A.L.1    Taylor, T.C.2    Melancon, P.3    Wilson, K.L.4
  • 84
    • 0027175035 scopus 로고
    • Calcium mobilization is required for nuclear vesicle fusion in vitro: Implications for membrane traffic and ip3 receptor function
    • Sullivan KM, Busa WB, Wilson KL (1993) Calcium mobilization is required for nuclear vesicle fusion in vitro: implications for membrane traffic and IP3 receptor function. Cell 73:1411-1422
    • (1993) Cell , vol.73 , pp. 1411-1422
    • Sullivan, K.M.1    Busa, W.B.2    Wilson, K.L.3
  • 85
    • 0025858293 scopus 로고
    • Sperm decondensation in Xenopus egg cytoplasm is mediated bynucleoplasmin
    • Philpott A, Leno GH, Laskey RA (1991) Sperm decondensation in Xenopus egg cytoplasm is mediated bynucleoplasmin. Cell 65:569-578
    • (1991) Cell , vol.65 , pp. 569-578
    • Philpott, A.1    Leno, G.H.2    Laskey, R.A.3
  • 86
    • 0015433823 scopus 로고
    • Time sequence of nuclear pore formation in phytohemagglutinin-stimulated lymphocytes and in HeLa cells during the cell cycle
    • Maul GG, Maul HM, Scogna JE, Lieberman GS, Stein GS, Hsu B.YL, Borun TW (1972) Time sequence of nuclear pore formation in phytohemagglutinin-stimulated lymphocytes and in HeLa cells during the cell cycle. J Cell Biol 55:433-447
    • (1972) J Cell Biol , vol.55 , pp. 433-447
    • Maul, G.G.1    Maul, H.M.2    Scogna, J.E.3    Lieberman, G.S.4    Stein, G.S.5    Hsu, B.Y.L.6    Borun, T.W.7
  • 88
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri F, Duguet M (1995) A 200-amino acid ATPase module in search of a basic function. Bioessays 17:639-650
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 89
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman JE, Wieland FT (1996) Protein sorting by transport vesicles. Science 272:227-234
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 90
    • 0030222308 scopus 로고    scopus 로고
    • Membrane fusion in organelle biogenesis
    • in press
    • Denesvre C, Malhotra V (1996) Membrane fusion in organelle biogenesis. Curr Opin Cell Biol 8:in press
    • (1996) Curr Opin Cell Biol , vol.8
    • Denesvre, C.1    Malhotra, V.2
  • 91
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters JM, Walsh MJ, Franke WW (1990) An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J 9:1757-1767
    • (1990) EMBO J , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 92
    • 0028904466 scopus 로고
    • ARF proteins: The membrane traffic police?
    • Boman AL, Kahn RA (1995) ARF proteins: the membrane traffic police? Trends Biochem Sci 20:147-150
    • (1995) Trends Biochem Sci , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 93
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures
    • Tsien RY (1980) New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures. Biochemistry 19:2396-2404
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 97
    • 0030067950 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor is located to the inner nuclear membrane vindicating regulation of nuclear calcium signaling by inositol 1,4,5-trisphosphate
    • Humbert JP, Matter N, Artault JC, Köppler P, Malviya AN (1996) Inositol 1,4,5-trisphosphate receptor is located to the inner nuclear membrane vindicating regulation of nuclear calcium signaling by inositol 1,4,5-trisphosphate. Proc Natl Acad Sci 271:478-485
    • (1996) Proc Natl Acad Sci , vol.271 , pp. 478-485
    • Humbert, J.P.1    Matter, N.2    Artault, J.C.3    Köppler, P.4    Malviya, A.N.5
  • 98
    • 0029027826 scopus 로고
    • Inhibition of nuclear vesicle fusion by antibodies that block activation of inositol 1,4,5-trisphosphate receptors
    • Sullivan KM, Lin DD, Wilson KL (1995) Inhibition of nuclear vesicle fusion by antibodies that block activation of inositol 1,4,5-trisphosphate receptors. Proc Nat Acad Sci 92:8611-8615
    • (1995) Proc Nat Acad Sci , vol.92 , pp. 8611-8615
    • Sullivan, K.M.1    Lin, D.D.2    Wilson, K.L.3
  • 99
    • 0026048152 scopus 로고
    • Assembly of nuclear pore complexes in Xenopus egg extract
    • Dabauvalle MC, Scheer U (1991) Assembly of nuclear pore complexes in Xenopus egg extract. Biol Cell 72:25-29
    • (1991) Biol Cell , vol.72 , pp. 25-29
    • Dabauvalle, M.C.1    Scheer, U.2
  • 100
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman JE, Warren G (1994) Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol 4:220-233
    • (1994) Curr Biol , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 101
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg E, Wozniak RW, Blobel G (1993) An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J Cell Biol 122:513-521
    • (1993) J Cell Biol , vol.122 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 102
    • 0020399177 scopus 로고
    • Identification of a major polypeptide of the nuclear pore complex
    • Gerace L, Ottaviano Y, Kondor-Koch C (1982) Identification of a major polypeptide of the nuclear pore complex. J Cell Biol 95:826-837
    • (1982) J Cell Biol , vol.95 , pp. 826-837
    • Gerace, L.1    Ottaviano, Y.2    Kondor-Koch, C.3
  • 103
    • 0024360678 scopus 로고
    • Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
    • Wozniak RW, Bartnik E, Blobel G (1989) Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J Cell Biol 108:2083-2092
    • (1989) J Cell Biol , vol.108 , pp. 2083-2092
    • Wozniak, R.W.1    Bartnik, E.2    Blobel, G.3
  • 104
    • 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 UF, Senior A, Gerace L (1990) 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 9:1495-1502
    • (1990) EMBO J , vol.9 , pp. 1495-1502
    • Greber, U.F.1    Senior, A.2    Gerace, L.3
  • 105
    • 0026071202 scopus 로고
    • A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs
    • Vigers GP, Lohka MJ (1991) A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs. J Cell Biol 112:545-556
    • (1991) J Cell Biol , vol.112 , pp. 545-556
    • Vigers, G.P.1    Lohka, M.J.2
  • 106
    • 0026650511 scopus 로고
    • Regulation of nuclear envelope precursor functions during cell division
    • Vigers GP, Lohka MJ (1992) Regulation of nuclear envelope precursor functions during cell division. J Cell Sci 102:273-284
    • (1992) J Cell Sci , vol.102 , pp. 273-284
    • Vigers, G.P.1    Lohka, M.J.2
  • 107
    • 0027275334 scopus 로고
    • Stepwise reassembly of the nuclear envelope at the end of mitosis
    • Chaudhary N, Courvalin JC (1993) Stepwise reassembly of the nuclear envelope at the end of mitosis. J Cell Biol 122:295-306
    • (1993) J Cell Biol , vol.122 , pp. 295-306
    • Chaudhary, N.1    Courvalin, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.