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1
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0029060051
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The nuclear pore complex
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Davis LA: The nuclear pore complex. Annu Rev Biochem 1995, 64:865-896. A comprehensive review of NPC structure, assembly and role in nucleocytoplasmic transport.
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(1995)
Annu Rev Biochem
, vol.64
, pp. 865-896
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Davis, L.A.1
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2
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0029015891
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Structural and functional organization of the nuclear envelope
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Goldberg MW, Allen TD: Structural and functional organization of the nuclear envelope. Curr Opin Cell Biol 1995, 7:301-309. This review concentrates on the structure of NPCs, especially surface features and the morphology of different components. It also discusses the possible role of more recently discovered peripheral fibrous elements in nuclear envelope structure.
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(1995)
Curr Opin Cell Biol
, vol.7
, pp. 301-309
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Goldberg, M.W.1
Allen, T.D.2
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3
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0029042717
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Mechanism of nuclear protein import
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Melchior F, Gerace L: Mechanism of nuclear protein import. Curr Opin Cell Biol 1995, 7:310-318. A comprehensive review of the molecular mechanisms underlying nucleocytoplasmic transport, in which the role of cytoplasmic factors and their interactions with both nuclear localization sequences and nucleoporins are discussed in considerable detail.
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(1995)
Curr Opin Cell Biol
, vol.7
, pp. 310-318
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Melchior, F.1
Gerace, L.2
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4
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0028316365
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Towards understanding the three-dimensional structure of the nuclear pore complex at the molecular level
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Pante N, Aebi U: Towards understanding the three-dimensional structure of the nuclear pore complex at the molecular level. Curr Opin Struct Biol 1994, 4:187-196. A review of NPC structure and its relationship to nucleocytoplasmic transport.
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(1994)
Curr Opin Struct Biol
, vol.4
, pp. 187-196
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Pante, N.1
Aebi, U.2
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5
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0029089597
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Nucleocytoplasmic transport: Factors and mechanisms
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Simos G, Hurt EC: Nucleocytoplasmic transport: factors and mechanisms. FEBS Lett 1995, 369:107-112. A comprehensive review of the structure of NPCs and nucleoporins, describing their involvement with a range of soluble factors in the import and export of macromolecules from the nucleus as well as the assembly of the nuclei after mitosis.
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(1995)
FEBS Lett
, vol.369
, pp. 107-112
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Simos, G.1
Hurt, E.C.2
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6
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0027989786
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Pores for thought: Nuclear pore complex proteins
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Rout MP, Wente SR: Pores for thought: nuclear pore complex proteins. Trends Cell Biol 1994, 4:357-365. A detailed catalogue of nucleoporins that have been identified and sequenced, with particular reference to the various repeating sequence motifs observed.
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(1994)
Trends Cell Biol
, vol.4
, pp. 357-365
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Rout, M.P.1
Wente, S.R.2
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7
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0028559537
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Cytosolic factors in nuclear transport: What's importin?
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Powers MA, Forbes DJ: Cytosolic factors in nuclear transport: what's importin? Cell 1994, 79:931-934. This is a comprehensive review of the role of cytosolic factors in the import of proteins into the nucleus.
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(1994)
Cell
, vol.79
, pp. 931-934
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Powers, M.A.1
Forbes, D.J.2
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8
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0029045334
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Protein export from the nucleus requires the GTPase Ran and GTP hydrolysis
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Moroianu J, Blobel G: Protein export from the nucleus requires the GTPase Ran and GTP hydrolysis. Proc Natl Acad Sci USA 1995, 92:4318-4322. This paper demonstrates that Ran and GTP hydrolysis are required for protein export from the nucleus.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 4318-4322
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Moroianu, J.1
Blobel, G.2
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9
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0026776959
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Architecture and design of the nuclear pore complex
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Hinshaw JE, Carragher BO, Milligan RA. Architecture and design of the nuclear pore complex. Cell 1992, 69:1133-1141.
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(1992)
Cell
, vol.69
, pp. 1133-1141
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Hinshaw, J.E.1
Carragher, B.O.2
Milligan, R.A.3
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10
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0027287349
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Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
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Akey CW, Radermacher M: Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J Cell Biol 1993, 12:1-19.
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(1993)
J Cell Biol
, vol.12
, pp. 1-19
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Akey, C.W.1
Radermacher, M.2
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11
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0029021928
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Structural plasticity of the nuclear pore complex
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Akey CW: Structural plasticity of the nuclear pore complex. J Mol Biol 1995, 248:273-293. A comprehensive statistical analysis of electron microscope images of vitrified nuclear envelopes indicates that, although the appearance of individual NPCs varies, the images can be classified into seven classes that form two major groups. Some of the structural changes may be due to NPC structure responding to nuclear envelope turgor pressure and could possibly be related to changes in NPC structure associated with transport.
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(1995)
J Mol Biol
, vol.248
, pp. 273-293
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Akey, C.W.1
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12
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0029118089
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Mapping of nucleoporins to the centre of the nuclear pore complex by post-embedding immunogold electron microscopy
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Grote M, Kubitscheck U, Reichelt R, Peters R: Mapping of nucleoporins to the centre of the nuclear pore complex by post-embedding immunogold electron microscopy. J Cell Sci 1995, 108:2963-2972. Immunoelectron microscopy indicates that epitopes shared by several nucleoporins that contain phenylalanine-rich sequence repeats, including p62, are located along the axis of the NPC.
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(1995)
J Cell Sci
, vol.108
, pp. 2963-2972
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Grote, M.1
Kubitscheck, U.2
Reichelt, R.3
Peters, R.4
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13
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0029021567
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The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex
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Radu A, Moore MS, Blobel G: The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell 1995, 81:215-222. The sequence of Nup98, which contains a number of phenylalanine-containing sequence repeats, is reported. It is proposed that these sequence repeats, together with those from other nucleoporins, mediate docking of transport substrates and that bidirectional transport across the NPC proceeds by repeated docking and undocking reactions.
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(1995)
Cell
, vol.81
, pp. 215-222
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Radu, A.1
Moore, M.S.2
Blobel, G.3
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14
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0028786983
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Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
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r 45 kDa, 54 kDa, 58 kDa and 62 kDa in equal proportions. The molecular weight of the intact complex indicates that probably one chain of each protein is present in the complex, and electron microscopy indicates that these particles have a doughnut-like shape that is about 15 nm in diameter.
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(1995)
Mol Biol Cell
, vol.6
, pp. 1591-1603
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Guan, T.1
Müller, S.2
Klier, G.3
Pante, N.4
Blevitt, J.M.5
Haner, M.6
Paschal, B.7
Aebi, U.8
Gerace, L.9
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15
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0027931054
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Interactions and three-dimensional localisation of a group of nuclear pore complex proteins
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Pante N, Bastos R, McMorrow I, Burke B, Aebi U: Interactions and three-dimensional localisation of a group of nuclear pore complex proteins. J Cell Biol 1994, 126:603-617. An analysis of macromolecular complexes from NPCs that contain O-linked N-acetyl-glucosamine residues. One of these is the p62-p58-p54 complex; whereas the others contain Nup153 and p250 in association with p75. Nup153 is located in the nucleocytoplasmic baskets, whereas p250 is located in the cytoplasmic fibrils.
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(1994)
J Cell Biol
, vol.126
, pp. 603-617
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Pante, N.1
Bastos, R.2
McMorrow, I.3
Burke, B.4
Aebi, U.5
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16
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0028091980
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Tpr, a large coiled-coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex
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Byrd DA, Sweet DJ, Pante N, Konstantinov KN, Guan T, Saphire ACS, Mitchell PJ, Cooper CS, Aebi U, Gerace L: Tpr, a large coiled-coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. J Cell Biol 1994, 127:1515-1526. Tpr contains a 1600-residue coiled coil and is located in the cytoplasmic fibres. At the end of mitosis, tpr becomes concentrated at the nuclear envelope significantly later than O-linked glycoproteins indicating a step-wise reassembly of NPCs.
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(1994)
J Cell Biol
, vol.127
, pp. 1515-1526
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Byrd, D.A.1
Sweet, D.J.2
Pante, 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
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17
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0025939317
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A complex of nuclear pore proteins required for pore function
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Finlay DR, Meier E, Bradley P, Horecka J, Forbes DJ: A complex of nuclear pore proteins required for pore function. J Cell Biol 1991, 114:169-183.
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(1991)
J Cell Biol
, vol.114
, pp. 169-183
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Finlay, D.R.1
Meier, E.2
Bradley, P.3
Horecka, J.4
Forbes, D.J.5
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18
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0027503111
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Purification and characterization of a nuclear pore glycoprotein complex containing p62
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Kita K, Omata S, Horigome T: Purification and characterization of a nuclear pore glycoprotein complex containing p62. J Biochem (Tokyo) 1993, 113:377-382.
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(1993)
J Biochem (Tokyo)
, vol.113
, pp. 377-382
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Kita, K.1
Omata, S.2
Horigome, T.3
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19
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0028853451
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Differential mitotic phosphorylation of proteins of the nuclear pore complex
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Macaulay C, Meier E, Forbes DJ: Differential mitotic phosphorylation of proteins of the nuclear pore complex. J Biol Chem 1995, 270:254-262. The Xenopus glycoprotein nucleoporins p200, p97 (Nup98) and p60 (equivalent to rat p62) form three separate macromolecular complexes in egg cytosol. The p200 and p97 nucleoporins are heavily phosphorylated at mitosis and are substrates for Cdc2 kinase, whereas p60 is not. The size of all three complexes does not change during the cell cycle, indicating that they represent stable multi-component modules into which the nucleus disassembles at mitosis.
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(1995)
J Biol Chem
, vol.270
, pp. 254-262
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Macaulay, C.1
Meier, E.2
Forbes, D.J.3
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20
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0028900866
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Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: Binding of nucleoporin p54 to the rod domain of p62
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Buss F, Stewart M: Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62. J Cell Biol 1995, 128:251-261. Nucleoporin p54, which forms a strong complex with p62 and p58 in rat NPCs, binds primarily to the coiled-coil rod domain of p62. As a result, many epitopes on p62 are masked in the complex. Conditions were established to enable partial exchange of endogenous p62 in the complex for bacterially-expressed material.
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(1995)
J Cell Biol
, vol.128
, pp. 251-261
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Buss, F.1
Stewart, M.2
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21
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0028345077
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Role of different domains in the self-association of rat nucleoporin p62
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Buss F, Kent HM, Stewart M, Bailer SM, Hanover JA: Role of different domains in the self-association of rat nucleoporin p62. J Cell Sci 1994, 107:631-638. This paper establishes that bacterially-expressed rat nucleoporin p62 is based on an α-helical C-terminal rod domain and N-terminal domains that are based on xFxFx repeats, which appear to contain some β conformation. The molecules formed by bacterially-expressed material self-associate using small regions at both ends of the rod domain.
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(1994)
J Cell Sci
, vol.107
, pp. 631-638
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Buss, F.1
Kent, H.M.2
Stewart, M.3
Bailer, S.M.4
Hanover, J.A.5
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22
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0028916742
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Analysis of nuclear pore protein p62 glycosylation
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Lubas WA, Smith M, Starr CM, Hanover JA: Analysis of nuclear pore protein p62 glycosylation. Biochemistry 1995, 34:1686-1694. A systematic analysis of the location of the sites to which O-linked N-acetylglucosamine residues are attached to on nucleoporin p62. The majority of these are attached to six clustered serine residues in the threonine-rich region that link the N-terminal domain to the C-terminal coiled-coil rod domain.
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(1995)
Biochemistry
, vol.34
, pp. 1686-1694
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Lubas, W.A.1
Smith, M.2
Starr, C.M.3
Hanover, J.A.4
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23
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0029027836
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Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62
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Paschal BM, Gerace L: Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. J Cell Biol 1995, 129:925-937. A 15 kDa protein, NTF2 (also called p10 and PP15), can be removed from cytosol using p62-affinity beads. The expressed protein can restore transport in extracts depleted by p62 beads and appears to interact with Ran after the importin complex docks at the NPC.
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(1995)
J Cell Biol
, vol.129
, pp. 925-937
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Paschal, B.M.1
Gerace, L.2
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24
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0027291375
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Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96
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Grandi P, Doye V, Hurt EC: Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96. EMBO J 1993 12:3061-3071.
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(1993)
EMBO J
, vol.12
, pp. 3061-3071
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Grandi, P.1
Doye, V.2
Hurt, E.C.3
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25
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0028893775
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Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1 p, Nup49p and a novel protein Nup57p
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Grandi P, Schlaich N, Tekotte H, Hurt EC: Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1 p, Nup49p and a novel protein Nup57p. EMBO J 1995, 14:76-87. Nic96p forms a tight complex with yeast nucleoporins Nsp1, Nup49p and Nup57p that appears to be required for protein import into the nucleus. Nup57p contains GLFG sequence repeats in its N-terminal domain, together with heptads characteristic of coiled coils at its C terminus, whereas the organization of Nic96p is more complex. It appears that many of the interactions in this complex are mediated by interactions between α helices.
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(1995)
EMBO J
, vol.14
, pp. 76-87
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Grandi, P.1
Schlaich, N.2
Tekotte, H.3
Hurt, E.C.4
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26
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0029129566
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A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p
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Grandi P, Eming S, Weise C, Hucho F, Pohl T, Hunt EC: A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J Cell Biol 1995, 130:1263-1273. Nsplp forms a separate complex with Nup82p that is distinct from that formed with Nup49p and Nup57p.
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(1995)
J Cell Biol
, vol.130
, pp. 1263-1273
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Grandi, P.1
Eming, S.2
Weise, C.3
Hucho, F.4
Pohl, T.5
Hunt, E.C.6
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27
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0029157330
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NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA export
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+ RNA export and is postulated to tether nucleoporins directly involved in transport to pore scaffolding proteins via its coiled-coil domain.
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(1995)
J Cell Biol
, vol.130
, pp. 1275-1281
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Hurwitz, M.E.1
Blobel, G.2
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28
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0028064385
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Genetic and physical interactions between Srp1 p and nuclear pore complex proteins Nup1p and Nup2p
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Belanger KD, Kenna MA, Wei S, Davis LA: Genetic and physical interactions between Srp1 p and nuclear pore complex proteins Nup1p and Nup2p. J Cell Biol 1994, 126:619-630. Srp1p, the yeast homolog of importin α, forms complexes with Nup1p and Nup2p that may be important for both NPC structure and transport.
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(1994)
J Cell Biol
, vol.126
, pp. 619-630
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Belanger, K.D.1
Kenna, M.A.2
Wei, S.3
Davis, L.A.4
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29
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0028217405
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Identification of cytosolic factors required for nuclear localization sequence - Mediated binding to the nuclear envelope
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Adam EJH, Adam SA: Identification of cytosolic factors required for nuclear localization sequence - mediated binding to the nuclear envelope. J Cell Biol 1994, 125:547-555.
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(1994)
J Cell Biol
, vol.125
, pp. 547-555
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Adam, E.J.H.1
Adam, S.A.2
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30
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0029115837
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Sequence and characterization of cytoplasmic nuclear protein import factor p97
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Chi NC, Adam EJH, Adam SA: Sequence and characterization of cytoplasmic nuclear protein import factor p97. J Cell Biol 1995, 130:265-274. This paper reports the sequence of importin β and shows that this 97 kDa protein is extracted from NPC with O-glycosylated proteins. The 97 kDa protein contain 23 cysteine residues and appears to bind zinc.
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(1995)
J Cell Biol
, vol.130
, pp. 265-274
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Chi, N.C.1
Adam, E.J.H.2
Adam, S.A.3
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31
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0027937653
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Isolation of a protein that is essential for the first step of nuclear protein import
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Görlich D, Prehn S, Laskey RA, Hartmann E: Isolation of a protein that is essential for the first step of nuclear protein import Cell 1994, 79:767-778. The identification of a 60 kDa protein, called importin, that is essential for import. Subsequently this protein was shown to be importin α and to require importin β and Ran, possibly together with other cytosolic factors, for import of proteins through the NPC.
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(1994)
Cell
, vol.79
, pp. 767-778
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Görlich, D.1
Prehn, S.2
Laskey, R.A.3
Hartmann, E.4
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32
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0029059548
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Distinct functions for the two importin subunits in nuclear protein import
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Görlich D, Vogel F, Mills AD, Hartmann E, Laskey RA: Distinct functions for the two importin subunits in nuclear protein import Nature 1995, 377:246-248. This paper demonstrates that importin α (60 kDa) is primarily responsible for NLS recognition. The complex formed by importin α, importin β (90 kDa) and the NLS-containing protein docks as a single entity to the NPC via importin β. Ran- and energy-dependent translocation results in the accumulation of importin a and import substrate in the nucleus whereas importin β remains on the nuclear envelope.
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(1995)
Nature
, vol.377
, pp. 246-248
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Görlich, D.1
Vogel, F.2
Mills, A.D.3
Hartmann, E.4
Laskey, R.A.5
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33
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0029278621
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Two different subunits of importin co-operate to recognise nuclear localization signals and bind them to the nuclear envelope
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Görlich D, Kosta S, Kraft R, Dingwall C, Laskey RA, Hartmann E, Prehn S: Two different subunits of importin co-operate to recognise nuclear localization signals and bind them to the nuclear envelope. Curr Biol 1995, 5:383-392. This paper demonstrates that importin a and β subunits constitute a cytosolic receptor for NLSs that enables import substrates to bind to the nuclear envelope.
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(1995)
Curr Biol
, vol.5
, pp. 383-392
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Görlich, D.1
Kosta, S.2
Kraft, R.3
Dingwall, C.4
Laskey, R.A.5
Hartmann, E.6
Prehn, S.7
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34
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0028970112
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A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding
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Imamoto N, Tachibana T, Matsubae M, Yoneda Y: A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding. J Biol Chem 1995, 270:8559-8565. Four proteins of 54 kDa, 56 kDa, 66 kDa and 9 kDa are identified that form a complex with proteins having an NLS. The 54 kDa and 90 kDa proteins are able to target NLS-containing proteins to the NPC.
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(1995)
J Biol Chem
, vol.270
, pp. 8559-8565
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Imamoto, N.1
Tachibana, T.2
Matsubae, M.3
Yoneda, Y.4
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35
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0029093824
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In vivo evidence for involvement of a 58 kDa component of the nuclear pore targeting complex in nuclear protein import
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Imamoto N, Shimamoto T, Takao T, Tachibana T, Kose S, Matsubae M, Sekimoto T, Shimonishi Y, Yoneda Y: In vivo evidence for involvement of a 58 kDa component of the nuclear pore targeting complex in nuclear protein import EMBO J 1995, 14:3617-3626. Transport assays indicate that importin a is required for nuclear import.
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(1995)
EMBO J
, vol.14
, pp. 3617-3626
-
-
Imamoto, N.1
Shimamoto, T.2
Takao, T.3
Tachibana, T.4
Kose, S.5
Matsubae, M.6
Sekimoto, T.7
Shimonishi, Y.8
Yoneda, Y.9
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36
-
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0028170744
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Purification of a Ran-interacting protein that is required for protein import into the nucleus
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Moore MS, Blobel G: Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc Natl Acad Sci USA 1994, 91:10212-10216. This paper shows that a small protein, homologous to PP15 (also called NTF2 [23••]), co-purifies with Ran from Xenopus oocytes and that this protein is necessary for Ran-mediated protein import into the nucleus in the presence of the importin subunits.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10212-10216
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Moore, M.S.1
Blobel, G.2
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37
-
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0028983494
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Mammalian karyopherin α1b and α2b heterodimers: α1 or α2 subunits bind nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins
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Moroianu J, Hijkata M, Blobel G, Radu A: Mammalian karyopherin α1b and α2b heterodimers: α1 or α2 subunits bind nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins. Proc Natl Acad Sci USA 1995, 92:6532-6536. This paper shows that there are two isoforms of importin a (karyopherin α), and that these primarily bind NLSs, whereas the β subunit (corresponding to importin β) binds the complex to the NPC by way of interactions with repeat-containing nucleoporins.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 6532-6536
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Moroianu, J.1
Hijkata, M.2
Blobel, G.3
Radu, A.4
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38
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0028950991
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Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins
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Radu A, Blobel G, Moore M: Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc Natl Acad Sci USA 1995, 92:1760-1773. A 9S protein complex from Xenopus cytosol containing 54 kDa, 56 kDa and 97 kDa proteins was isolated. This complex promoted the binding of a NLS-containing ligand to four nucleoporins and suggested that these, possibly together with other nucleoporins, act as multiple docking sites for importin-mediated transport of NLS-containing substrates through the NPC.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 1760-1773
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Radu, A.1
Blobel, G.2
Moore, M.3
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39
-
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0028929866
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Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form
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Scheffzek K, Klebe C, Fritz-Wolf K, Kabsch W, Wittinghofer A: Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 1995, 374:378-381. The high-resolution structure of Ran is reported and it is compared with that of Ras.
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(1995)
Nature
, vol.374
, pp. 378-381
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-
Scheffzek, K.1
Klebe, C.2
Fritz-Wolf, K.3
Kabsch, W.4
Wittinghofer, A.5
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40
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0029995424
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Crystallization and preliminary X-ray diffraction analysis of nuclear transport factor 2 (NTF2)
-
in press
-
Kent HM, Clarkson WD, Bullock TM, Stewart M: Crystallization and preliminary X-ray diffraction analysis of nuclear transport factor 2 (NTF2). J Struct Biol 1996, in press. This paper reports the production of NTF2 crystals that should enable their high-resolution structure to be determined.
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(1996)
J Struct Biol
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Kent, H.M.1
Clarkson, W.D.2
Bullock, T.M.3
Stewart, M.4
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41
-
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0029070074
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Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine rich region
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Wu J, Matunis MJ, Kraemer D, Blobel G, Coutavas E: 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 1995, 270:14209-14213. This paper describes the identification and characterization of a NPC Ran-binding protein that contains a wealth of different sequence motifs, outlined in the title (see also [42•]).
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(1995)
J Biol Chem
, vol.270
, pp. 14209-14213
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Wu, J.1
Matunis, M.J.2
Kraemer, D.3
Blobel, G.4
Coutavas, E.5
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42
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0029032954
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A giant nucleopore protein that binds Ran/TC4
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Yokoyama N, Hayashi N, Seki T, Pante N, Ohba T, Nishii K, Kuma K, Hayashida T, Miyata T, Aebi U et al.: A giant nucleopore protein that binds Ran/TC4. Nature 1995, 376:184-188. A 700-residue nucleoporin that binds Ran was identified using a two-hybrid screen. This protein binds to the cytoplasmic surface of the NPC and contains a range of different repeating sequence motifs including eight zinc-finger motifs and a leucine-zipper as well as a putative cyclophilin-binding domain (see also [41•]).
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(1995)
Nature
, vol.376
, pp. 184-188
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Yokoyama, N.1
Hayashi, N.2
Seki, T.3
Pante, N.4
Ohba, T.5
Nishii, K.6
Kuma, K.7
Hayashida, T.8
Miyata, T.9
Aebi, U.10
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43
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0001556063
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A Ran-binding motif in nuclear pore proteins
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Hartmann E, Görlich D: A Ran-binding motif in nuclear pore proteins. Trends Cell Biol 1995, 5:192-193. Several nucleoporins contain a consensus Ran-binding motif.
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(1995)
Trends Cell Biol
, vol.5
, pp. 192-193
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Hartmann, E.1
Görlich, D.2
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