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1
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0037459085
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Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle
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Weis K. Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle. Cell 112 (2003) 441-451
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(2003)
Cell
, vol.112
, pp. 441-451
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Weis, K.1
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2
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0345374584
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The structure of importin-β bound to SREBP-2: nuclear import of a transcription factor
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Lee S.J., Sekimoto T., Yamashita E., Nagoshi E., Nakagawa A., Imamoto N., Yoshimura M., Sakai H., Chong K.T., Tsukihara T., and Yoneda Y. The structure of importin-β bound to SREBP-2: nuclear import of a transcription factor. Science 302 (2003) 1571-1575
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(2003)
Science
, vol.302
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Lee, S.J.1
Sekimoto, T.2
Yamashita, E.3
Nagoshi, E.4
Nakagawa, A.5
Imamoto, N.6
Yoshimura, M.7
Sakai, H.8
Chong, K.T.9
Tsukihara, T.10
Yoneda, Y.11
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3
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0346457106
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Conformational variability of nucleo-cytoplasmic transport factors
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This study uses SAXS to demonstrate considerable variability between different β-karyopherins and also between the same karyopherin bound to different partners.
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Fukuhara N., Fernandez E., Ebert J., Conti E., and Svergun D. Conformational variability of nucleo-cytoplasmic transport factors. J Biol Chem 279 (2004) 2176-2181. This study uses SAXS to demonstrate considerable variability between different β-karyopherins and also between the same karyopherin bound to different partners.
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(2004)
J Biol Chem
, vol.279
, pp. 2176-2181
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Fukuhara, N.1
Fernandez, E.2
Ebert, J.3
Conti, E.4
Svergun, D.5
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4
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9744248734
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Architecture of CRM1/exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex
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A combination of X-ray crystallography, homology modelling and EM was employed to generate a structural model of human CRM1, the primary nuclear protein export factor. In contrast to other β-karyopherins, residues critical for the recognition of the leucine-rich NES are identified as being located on the outer convex surface of the molecule.
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Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U., Soler-Lopez M., Baudin F., Mattaj I.W., and Müller C.W. Architecture of CRM1/exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol Cell 16 (2004) 761-775. A combination of X-ray crystallography, homology modelling and EM was employed to generate a structural model of human CRM1, the primary nuclear protein export factor. In contrast to other β-karyopherins, residues critical for the recognition of the leucine-rich NES are identified as being located on the outer convex surface of the molecule.
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(2004)
Mol Cell
, vol.16
, pp. 761-775
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Petosa, C.1
Schoehn, G.2
Askjaer, P.3
Bauer, U.4
Moulin, M.5
Steuerwald, U.6
Soler-Lopez, M.7
Baudin, F.8
Mattaj, I.W.9
Müller, C.W.10
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5
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11144257756
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Structural basis for the assembly of a nuclear export complex
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The X-ray crystal structure of the Cse1p-RanGTP-Kap60p nuclear export complex shows the unusually large interaction interface between the three molecules. The paper proposes that the large energy of interaction may be balanced by mechanical distortion of Cse1p to generate a 'spring-loaded' molecule that can be easily disassembled following RanGTP hydrolysis in the cytoplasm.
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Matsuura Y., and Stewart M. Structural basis for the assembly of a nuclear export complex. Nature 432 (2004) 872-877. The X-ray crystal structure of the Cse1p-RanGTP-Kap60p nuclear export complex shows the unusually large interaction interface between the three molecules. The paper proposes that the large energy of interaction may be balanced by mechanical distortion of Cse1p to generate a 'spring-loaded' molecule that can be easily disassembled following RanGTP hydrolysis in the cytoplasm.
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(2004)
Nature
, vol.432
, pp. 872-877
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Matsuura, Y.1
Stewart, M.2
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6
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20844458749
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The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding
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The X-ray crystal structure of Cse1p alone shows a 'closed' structure in which the N terminus binds to a region around HEAT repeat 15 near the centre of the molecule. As a result, there is a considerable alteration in the Cse1p helicoidal pitch compared with its 'open' structure in the Cse1p-RanGTP-Kap60p complex.
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Cook A., Fernandez E., Lindner D., Ebert J., Schlenstedt G., and Conti E. The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Mol Cell 18 (2005) 355-367. The X-ray crystal structure of Cse1p alone shows a 'closed' structure in which the N terminus binds to a region around HEAT repeat 15 near the centre of the molecule. As a result, there is a considerable alteration in the Cse1p helicoidal pitch compared with its 'open' structure in the Cse1p-RanGTP-Kap60p complex.
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(2005)
Mol Cell
, vol.18
, pp. 355-367
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Cook, A.1
Fernandez, E.2
Lindner, D.3
Ebert, J.4
Schlenstedt, G.5
Conti, E.6
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7
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0001506297
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Structure of the nuclear transport complex karyopherin-β2-Ran x GppNHp
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Chook Y.M., and Blobel G. Structure of the nuclear transport complex karyopherin-β2-Ran x GppNHp. Nature 399 (1999) 230-237
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(1999)
Nature
, vol.399
, pp. 230-237
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Chook, Y.M.1
Blobel, G.2
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8
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0033587167
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Structure of importin-β bound to the IBB domain of importin-α
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Cingolani G., Petosa C., Weis K., and Muller C.W. Structure of importin-β bound to the IBB domain of importin-α. Nature 399 (1999) 221-229
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(1999)
Nature
, vol.399
, pp. 221-229
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Cingolani, G.1
Petosa, C.2
Weis, K.3
Muller, C.W.4
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9
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20444468112
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Structural basis for nuclear import complex dissociation by RanGTP
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The X-ray crystal structure of the yeast importin-β homologue, Kap95p, complexed with RanGTP shows how the pitch of the helicoid is increased due to an interaction between the Ran switch I loop and HEAT repeats 12-15 in the C-terminal arch. This change in helicoidal pitch is proposed to facilitate the release of the IBB domain when RanGTP binds in the nucleus.
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Lee S.J., Matsuura Y., Liu S.M., and Stewart M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 435 (2005) 693-696. The X-ray crystal structure of the yeast importin-β homologue, Kap95p, complexed with RanGTP shows how the pitch of the helicoid is increased due to an interaction between the Ran switch I loop and HEAT repeats 12-15 in the C-terminal arch. This change in helicoidal pitch is proposed to facilitate the release of the IBB domain when RanGTP binds in the nucleus.
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(2005)
Nature
, vol.435
, pp. 693-696
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Lee, S.J.1
Matsuura, Y.2
Liu, S.M.3
Stewart, M.4
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10
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19444383899
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Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p
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The X-ray crystal structure of Kap95p bound to the high-affinity site on nucleoporin Nup1p shows the basis of the increased strength of the interaction and indicates how such an interaction could accelerate import complex disassembly.
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Liu S.M., and Stewart M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J Mol Biol 349 (2005) 515-525. The X-ray crystal structure of Kap95p bound to the high-affinity site on nucleoporin Nup1p shows the basis of the increased strength of the interaction and indicates how such an interaction could accelerate import complex disassembly.
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(2005)
J Mol Biol
, vol.349
, pp. 515-525
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Liu, S.M.1
Stewart, M.2
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11
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0033612390
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Structural view of the Ran-importin β interaction at 2.3 Å resolution
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Vetter I.R., Arndt A., Kutay U., Görlich D., and Wittinghofer A. Structural view of the Ran-importin β interaction at 2.3 Å resolution. Cell 97 (1999) 635-646
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(1999)
Cell
, vol.97
, pp. 635-646
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Vetter, I.R.1
Arndt, A.2
Kutay, U.3
Görlich, D.4
Wittinghofer, A.5
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12
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0034616910
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Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking
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Bayliss R., Littlewood T., and Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell 102 (2000) 99-108
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(2000)
Cell
, vol.102
, pp. 99-108
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Bayliss, R.1
Littlewood, T.2
Stewart, M.3
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13
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0037184968
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GLFG and FxFG nucleoporins bind to overlapping sites on importin-β
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Bayliss R., Littlewood T., Strawn L.A., Wente S.R., and Stewart M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-β. J Biol Chem 277 (2002) 50597-50606
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(2002)
J Biol Chem
, vol.277
, pp. 50597-50606
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Bayliss, R.1
Littlewood, T.2
Strawn, L.A.3
Wente, S.R.4
Stewart, M.5
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14
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0036923972
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Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β
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Cingolani G., Bednenko J., Gillespie M.T., and Gerace L. Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β. Mol Cell 10 (2002) 1345-1353
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(2002)
Mol Cell
, vol.10
, pp. 1345-1353
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Cingolani, G.1
Bednenko, J.2
Gillespie, M.T.3
Gerace, L.4
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15
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0032563246
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Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin-α
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Conti E., Uy M., Leighton L., Blobel G., and Kuriyan J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin-α. Cell 94 (1998) 193-204
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(1998)
Cell
, vol.94
, pp. 193-204
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Conti, E.1
Uy, M.2
Leighton, L.3
Blobel, G.4
Kuriyan, J.5
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16
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0034646565
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Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α
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Fontes M.R., Teh T., and Kobe B. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α. J Mol Biol 297 (2000) 1183-1194
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J Mol Biol
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Fontes, M.R.1
Teh, T.2
Kobe, B.3
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17
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0032950628
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Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α
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Kobe B. Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α. Nat Struct Biol 6 (1999) 388-397
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(1999)
Nat Struct Biol
, vol.6
, pp. 388-397
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Kobe, B.1
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18
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0041731883
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Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport
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Bednenko J., Cingolani G., and Gerace L. Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport. J Cell Biol 162 (2003) 391-401
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(2003)
J Cell Biol
, vol.162
, pp. 391-401
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Bednenko, J.1
Cingolani, G.2
Gerace, L.3
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19
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1842300384
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A novel class of RanGTP binding proteins
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Görlich D., Dabrowski M., Bischoff F.R., Kutay U., Bork P., Hartmann E., Prehn S., and Izaurralde E. A novel class of RanGTP binding proteins. J Cell Biol 138 (1997) 65-80
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(1997)
J Cell Biol
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Görlich, D.1
Dabrowski, M.2
Bischoff, F.R.3
Kutay, U.4
Bork, P.5
Hartmann, E.6
Prehn, S.7
Izaurralde, E.8
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20
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0037018838
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Uncoupling Kapβ2 substrate dissociation from Ran binding
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Chook Y.M., Jung A., Rosen M.K., and Blobel B. Uncoupling Kapβ2 substrate dissociation from Ran binding. Biochemistry 41 (2002) 6955-6966
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(2002)
Biochemistry
, vol.41
, pp. 6955-6966
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Chook, Y.M.1
Jung, A.2
Rosen, M.K.3
Blobel, B.4
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21
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0344827223
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Molecular recognition in nuclear trafficking
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Stewart M. Molecular recognition in nuclear trafficking. Science 302 (2003) 1513-1514
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(2003)
Science
, vol.302
, pp. 1513-1514
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Stewart, M.1
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22
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0030960586
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Dominant negative mutants of importin-β block multiple pathways of import and export through the nuclear pore complex
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Kutay U., Izaurralde E., Bischoff R.L., Mattaj I.W., and Görlich D. Dominant negative mutants of importin-β block multiple pathways of import and export through the nuclear pore complex. EMBO J 16 (1997) 1153-1163
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EMBO J
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Kutay, U.1
Izaurralde, E.2
Bischoff, R.L.3
Mattaj, I.W.4
Görlich, D.5
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23
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15244359121
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Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy
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Golas M.M., Sander B., Will C.L., Lührmann R., and Stark H. Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy. Mol Cell 17 (2005) 869-883
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(2005)
Mol Cell
, vol.17
, pp. 869-883
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Golas, M.M.1
Sander, B.2
Will, C.L.3
Lührmann, R.4
Stark, H.5
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24
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9444273167
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Components of coated vesicles and nuclear pore complexes share a common molecular architecture
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Devos D., Dokudovskaya S., Alber F., Williams R., Chait B.T., Sali A., and Rout M.P. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol 2 (2004) e380
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(2004)
PLoS Biol
, vol.2
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Devos, D.1
Dokudovskaya, S.2
Alber, F.3
Williams, R.4
Chait, B.T.5
Sali, A.6
Rout, M.P.7
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25
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0141995069
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The nuclear pore complex: nucleocytoplasmic transport and beyond
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Fahrenkrog B., and Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol 4 (2003) 757-766
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(2003)
Nat Rev Mol Cell Biol
, vol.4
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Fahrenkrog, B.1
Aebi, U.2
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26
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8844226004
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Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
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Beck M., Forster F., Ecke M., Plitzko J.M., Melchior F., Gerisch G., Baumeister W., and Medalia O. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306 (2004) 1387-1390
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(2004)
Science
, vol.306
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Beck, M.1
Forster, F.2
Ecke, M.3
Plitzko, J.M.4
Melchior, F.5
Gerisch, G.6
Baumeister, W.7
Medalia, O.8
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