메뉴 건너뛰기




Volumn 12, Issue 3, 2000, Pages 302-307

The role of Ran in nuclear function

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; NUCLEAR PROTEIN; RAN GTPASE; UNCLASSIFIED DRUG;

EID: 0034065954     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00093-4     Document Type: Review
Times cited : (65)

References (48)
  • 1
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj I.W., Englmeier L. Nucleocytoplasmic transport: the soluble phase. Annu Rev Biochem. 67:1998;265-306.
    • (1998) Annu Rev Biochem , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 2
    • 0027389003 scopus 로고
    • Ran/TC4: A small nuclear GTP-binding protein that regulates DNA synthesis
    • Ren M., Drivas G., D'Eustachio P., Rush M.G. Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis. J Cell Biol. 120:1993;313-323.
    • (1993) J Cell Biol , vol.120 , pp. 313-323
    • Ren, M.1    Drivas, G.2    D'Eustachio, P.3    Rush, M.G.4
  • 3
    • 0024445582 scopus 로고
    • The RCC1 protein, a regulator for the onset of chromosome condensation locates in the nucleus and bind to DNA
    • Ohtsubo M., Okazaki H., Nishimoto T. The RCC1 protein, a regulator for the onset of chromosome condensation locates in the nucleus and bind to DNA. J Cell Biol. 109:1989;1389-1397.
    • (1989) J Cell Biol , vol.109 , pp. 1389-1397
    • Ohtsubo, M.1    Okazaki, H.2    Nishimoto, T.3
  • 4
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis M.J., Coutavas E., Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol. 135:1996;1457-1470.
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 5
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell. 88:1997;97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 6
    • 0032538803 scopus 로고    scopus 로고
    • NTF2 mediates nuclear import of Ran
    • This paper established the role of NTF2. It was the first paper to clearly demonstrate that Ran is recycled after each round of nuclear transport by NTF2, a Ran-GDP-binding protein that is essential for nuclear transport.
    • Ribbeck K., Lipowsky G., Kent H.M., Stewart M., Gorlich D. NTF2 mediates nuclear import of Ran. EMBO J. 17:1998;6587-6598. This paper established the role of NTF2. It was the first paper to clearly demonstrate that Ran is recycled after each round of nuclear transport by NTF2, a Ran-GDP-binding protein that is essential for nuclear transport.
    • (1998) EMBO J , vol.17 , pp. 6587-6598
    • Ribbeck, K.1    Lipowsky, G.2    Kent, H.M.3    Stewart, M.4    Gorlich, D.5
  • 7
    • 0032585533 scopus 로고    scopus 로고
    • Nuclear import of Ran is mediated by the transport factor NTF2
    • Smith A., Brownawell A., Macara I.G. Nuclear import of Ran is mediated by the transport factor NTF2. Curr Biol. 8:1998;1403-1406.
    • (1998) Curr Biol , vol.8 , pp. 1403-1406
    • Smith, A.1    Brownawell, A.2    Macara, I.G.3
  • 8
    • 0028955712 scopus 로고
    • The Ran/TC4 GTPase-binding domain: Identification by expression cloning and characterization of a conserved sequence motif
    • Beddow A.L., Richards S.A., Orem N.R., Macara I.G. The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif. Proc Natl Acad Sci USA. 92:1995;3328-3332.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3328-3332
    • Beddow, A.L.1    Richards, S.A.2    Orem, N.R.3    Macara, I.G.4
  • 9
    • 0028937195 scopus 로고
    • Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1
    • Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H. Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 14:1995;705-715.
    • (1995) EMBO J , vol.14 , pp. 705-715
    • Bischoff, F.R.1    Krebber, H.2    Smirnova, E.3    Dong, W.4    Ponstingl, H.5
  • 10
    • 0033118942 scopus 로고    scopus 로고
    • Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain
    • Nakielny S., Shaikh S., Burke B., Dreyfuss G. Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain. EMBO J. 18:1999;1982-1995.
    • (1999) EMBO J , vol.18 , pp. 1982-1995
    • Nakielny, S.1    Shaikh, S.2    Burke, B.3    Dreyfuss, G.4
  • 11
    • 0033545869 scopus 로고    scopus 로고
    • Two distinct classes of Ran-binding sites on the nucleoporin Nup-358
    • Yaseen N.R., Blobel G. Two distinct classes of Ran-binding sites on the nucleoporin Nup-358. Proc Natl Acad Sci USA. 96:1999;5516-5521.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5516-5521
    • Yaseen, N.R.1    Blobel, G.2
  • 12
    • 0028929866 scopus 로고
    • Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form
    • 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. 374:1995;378-381.
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritz-Wolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 13
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp
    • This report provides crystal structures for the importin-β-Ran-GppNHp complex. This reports provides insight into the capacity of Ran-GTP, but not Ran-GDP, to bind to transport receptors, as well as to the capacity of this complex to interact with RanBP1.
    • Chook Y.M., Blobel G. Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature. 399:1999;230-237. This report provides crystal structures for the importin-β-Ran-GppNHp complex. This reports provides insight into the capacity of Ran-GTP, but not Ran-GDP, to bind to transport receptors, as well as to the capacity of this complex to interact with RanBP1.
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 14
    • 0030941976 scopus 로고    scopus 로고
    • Different binding domains for Ran-GTP and Ran-GDP/RanBP1 on nuclear import factor p97
    • Chi N.C., Adam E.J.H., Adam S.A. Different binding domains for Ran-GTP and Ran-GDP/RanBP1 on nuclear import factor p97. J Biol Chem. 272:1997;6818-6822.
    • (1997) J Biol Chem , vol.272 , pp. 6818-6822
    • Chi, N.C.1    Adam, E.J.H.2    Adam, S.A.3
  • 15
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin beta interaction at 2.3 A resolution
    • Vetter I.R., Arndt A., Kutay U., Gorlich D., Wittinghofer A. Structural view of the Ran-importin beta interaction at 2.3 A resolution. Cell. 97:1999;635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 17
    • 0345647103 scopus 로고    scopus 로고
    • RanBP1 is crucial for the release of RanGTP from importin beta-related nuclear transport factors
    • Bischoff F.R., Gorlich D. RanBP1 is crucial for the release of RanGTP from importin beta-related nuclear transport factors. FEBS Lett. 419:1997;249-254.
    • (1997) FEBS Lett , vol.419 , pp. 249-254
    • Bischoff, F.R.1    Gorlich, D.2
  • 18
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: Implications for nuclear transport
    • This paper reports the crystal structure of the complex containing Ran and an isolated Ran-binding domain of RanBP2, as well as information regarding the conformational changes from the GDP-bound to the GppNHp-bound form of Ran. This information has been essential for modelling the interactions of RanBP1 with the switch I domain of Ran.
    • Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature. 398:1999;39-46. This paper reports the crystal structure of the complex containing Ran and an isolated Ran-binding domain of RanBP2, as well as information regarding the conformational changes from the GDP-bound to the GppNHp-bound form of Ran. This information has been essential for modelling the interactions of RanBP1 with the switch I domain of Ran.
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 19
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)
    • Bullock T.L., Clarkson W.D., Kent H.M., Stewart M. The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2). J Mol Biol. 260:1996;422-431.
    • (1996) J Mol Biol , vol.260 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 20
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran
    • Stewart M., Kent H.M., McCoy A.J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J Mol Biol. 277:1998;635-646.
    • (1998) J Mol Biol , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 21
    • 0032485075 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
    • Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., Wittinghofer A. The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature. 392:1998;97-101.
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1    Nassar, N.2    Vetter, I.3    Becker, J.4    Klebe, C.5    Roth, M.6    Wittinghofer, A.7
  • 22
    • 0032522343 scopus 로고    scopus 로고
    • Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p
    • This paper documents that Mtr10p is the transport receptor for the RNA-binding protein Npl3p. It demonstrates that Npl3p dissociates from Mtr10p only in the presence of both Ran-GTP and RNA. These results suggest that the release of some transport substrates may be dependent upon their association with the correct macromolecular complexes within nuclei.
    • Senger B., Simos G., Bischoff F.R., Podtelejnikov A., Mann M., Hurt E. Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. EMBO J. 17:1998;2196-2207. This paper documents that Mtr10p is the transport receptor for the RNA-binding protein Npl3p. It demonstrates that Npl3p dissociates from Mtr10p only in the presence of both Ran-GTP and RNA. These results suggest that the release of some transport substrates may be dependent upon their association with the correct macromolecular complexes within nuclei.
    • (1998) EMBO J , vol.17 , pp. 2196-2207
    • Senger, B.1    Simos, G.2    Bischoff, F.R.3    Podtelejnikov, A.4    Mann, M.5    Hurt, E.6
  • 23
    • 0033612576 scopus 로고    scopus 로고
    • Nuclear import of the TATA-binding protein: Mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting
    • Pemberton L.F., Rosenblum J.S., Blobel G. Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting. J Cell Biol. 145:1999;1407-1417.
    • (1999) J Cell Biol , vol.145 , pp. 1407-1417
    • Pemberton, L.F.1    Rosenblum, J.S.2    Blobel, G.3
  • 24
    • 0033578298 scopus 로고    scopus 로고
    • The direction of transport through the nuclear pore can be inverted
    • This paper demonstrates that the vectorial nature of nuclear transport is derived from the gradient of Ran-GTP. Inversion of the gradient can invert direction of nucleocytoplasmic transport in the permeabilized cell transport assay.
    • Nachury M.V., Weis K. The direction of transport through the nuclear pore can be inverted. Proc Natl Acad Sci USA. 96:1999;9622-9627. This paper demonstrates that the vectorial nature of nuclear transport is derived from the gradient of Ran-GTP. Inversion of the gradient can invert direction of nucleocytoplasmic transport in the permeabilized cell transport assay.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9622-9627
    • Nachury, M.V.1    Weis, K.2
  • 25
    • 0032933745 scopus 로고    scopus 로고
    • Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis
    • Englmeier L., Olivo J.C., Mattaj I.W. Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis. Curr Biol. 9:1999;30-41.
    • (1999) Curr Biol , vol.9 , pp. 30-41
    • Englmeier, L.1    Olivo, J.C.2    Mattaj, I.W.3
  • 26
    • 0032954291 scopus 로고    scopus 로고
    • The translocation of transportin-cargo complexes through nuclear pores is independent of both Ran and energy
    • Ribbeck K., Kutay U., Paraskeva E., Gorlich D. The translocation of transportin-cargo complexes through nuclear pores is independent of both Ran and energy. Curr Biol. 9:1999;47-50.
    • (1999) Curr Biol , vol.9 , pp. 47-50
    • Ribbeck, K.1    Kutay, U.2    Paraskeva, E.3    Gorlich, D.4
  • 27
    • 0032481125 scopus 로고    scopus 로고
    • Nuclear transport factor p10/NTF2 functions as a Ran-GDP dissociation inhibitor (Ran-GDI)
    • Yamada M., Tachibana T., Imamoto N., Yoneda Y. Nuclear transport factor p10/NTF2 functions as a Ran-GDP dissociation inhibitor (Ran-GDI). Curr Biol. 8:1998;1339-1342.
    • (1998) Curr Biol , vol.8 , pp. 1339-1342
    • Yamada, M.1    Tachibana, T.2    Imamoto, N.3    Yoneda, Y.4
  • 28
    • 0029798506 scopus 로고    scopus 로고
    • Nucleotide-specific interaction of Ran/TC4 with nuclear transport factors NTF2 and p97
    • Paschal B.M., Delphin C., Gerace L. Nucleotide-specific interaction of Ran/TC4 with nuclear transport factors NTF2 and p97. Proc Natl Acad Sci USA. 93:1996;7679-7683.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7679-7683
    • Paschal, B.M.1    Delphin, C.2    Gerace, L.3
  • 29
    • 0342505309 scopus 로고    scopus 로고
    • Identification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export
    • Black B.E., Levesque L., Holaska J.M., Wood T.C., Paschal B.M. Identification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export. Mol Cell Biol. 19:1999;8616-8624.
    • (1999) Mol Cell Biol , vol.19 , pp. 8616-8624
    • Black, B.E.1    Levesque, L.2    Holaska, J.M.3    Wood, T.C.4    Paschal, B.M.5
  • 31
    • 0030963425 scopus 로고    scopus 로고
    • RanBP2 associates with Ubc9p and a modified form of RanGAP1
    • Saitoh H., Pu R., Cavenagh M., Dasso M. RanBP2 associates with Ubc9p and a modified form of RanGAP1. Proc Natl Acad Sci USA. 94:1997;3736-3741.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3736-3741
    • Saitoh, H.1    Pu, R.2    Cavenagh, M.3    Dasso, M.4
  • 32
    • 0025734777 scopus 로고
    • Loss of RCC1, a nuclear DNA-binding protein, uncouples the completion of DNA replication from the activation of cdc2 protein kinase and mitosis
    • Nishitani H., Ohtsubo M., Yamashita K., Iida H., Pines J., Yasudo H., Shibata Y., Hunter T., Nishimoto T. Loss of RCC1, a nuclear DNA-binding protein, uncouples the completion of DNA replication from the activation of cdc2 protein kinase and mitosis. EMBO J. 10:1991;1555-1564.
    • (1991) EMBO J , vol.10 , pp. 1555-1564
    • Nishitani, H.1    Ohtsubo, M.2    Yamashita, K.3    Iida, H.4    Pines, J.5    Yasudo, H.6    Shibata, Y.7    Hunter, T.8    Nishimoto, T.9
  • 33
    • 0028318281 scopus 로고
    • Evidence for a dual role for TC4 protein in regulating nuclear structure and cell cycle progression
    • Kornbluth S., Dasso M., Newport J. Evidence for a dual role for TC4 protein in regulating nuclear structure and cell cycle progression. J Cell Biol. 125:1994;705-719.
    • (1994) J Cell Biol , vol.125 , pp. 705-719
    • Kornbluth, S.1    Dasso, M.2    Newport, J.3
  • 34
    • 0028910594 scopus 로고
    • Regulation of Cdc2/cyclin B activation by Ran, a Ras-related GTPase
    • Clarke P.R., Klebe C., Wittinghofer A., Karsenti E. Regulation of Cdc2/cyclin B activation by Ran, a Ras-related GTPase. J Cell Sci. 108:1995;1217-1225.
    • (1995) J Cell Sci , vol.108 , pp. 1217-1225
    • Clarke, P.R.1    Klebe, C.2    Wittinghofer, A.3    Karsenti, E.4
  • 35
    • 0033591373 scopus 로고    scopus 로고
    • Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran
    • This paper examines the role of Ran in spindle assembly. In particular, this paper documents that the asters induced by Ran-GTP contain centriolar proteins and form in a manner that is dependent upon many of the functions normally required for spindle assembly.
    • Wilde A., Zheng Y. Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran. Science. 284:1999;1359-1362. This paper examines the role of Ran in spindle assembly. In particular, this paper documents that the asters induced by Ran-GTP contain centriolar proteins and form in a manner that is dependent upon many of the functions normally required for spindle assembly.
    • (1999) Science , vol.284 , pp. 1359-1362
    • Wilde, A.1    Zheng, Y.2
  • 36
    • 0033591386 scopus 로고    scopus 로고
    • Self-organization of microtubule asters induced in Xenopus egg extracts by GTP-bound Ran
    • This paper examines the role of Ran in spindle assembly. In particular, it documents that RanGEF-depleted Xenopus egg extracts have defects in aster formation that can be restored through the addition of recombinant RanGEF.
    • Ohba T., Nakamura M., Nishitani H., Nishimoto T. Self-organization of microtubule asters induced in Xenopus egg extracts by GTP-bound Ran. Science. 284:1999;1356-1358. This paper examines the role of Ran in spindle assembly. In particular, it documents that RanGEF-depleted Xenopus egg extracts have defects in aster formation that can be restored through the addition of recombinant RanGEF.
    • (1999) Science , vol.284 , pp. 1356-1358
    • Ohba, T.1    Nakamura, M.2    Nishitani, H.3    Nishimoto, T.4
  • 37
    • 0033528994 scopus 로고    scopus 로고
    • The ran GTPase regulates mitotic spindle assembly
    • This paper examines the role of Ran in spindle assembly. In particular, it documents that excess RanBP1 can disrupt spindle assembly, whereas RanGEF or RanG19V-GTPγS cause microtubule polymerization and the formation of asters and spindle-like structures.
    • Kalab P., Pu R.T., Dasso M. The ran GTPase regulates mitotic spindle assembly. Curr Biol. 9:1999;481-484. This paper examines the role of Ran in spindle assembly. In particular, it documents that excess RanBP1 can disrupt spindle assembly, whereas RanGEF or RanG19V-GTPγS cause microtubule polymerization and the formation of asters and spindle-like structures.
    • (1999) Curr Biol , vol.9 , pp. 481-484
    • Kalab, P.1    Pu, R.T.2    Dasso, M.3
  • 38
    • 0033588949 scopus 로고    scopus 로고
    • Beyond nuclear transport. Ran-GTP as a determinant of spindle assembly
    • This paper gives a clear review of recent reports on the role of Ran in spindle assembly.
    • Kahana J.A., Cleveland D.W. Beyond nuclear transport. Ran-GTP as a determinant of spindle assembly. J Cell Biol. 146:1999;1205-1210. This paper gives a clear review of recent reports on the role of Ran in spindle assembly.
    • (1999) J Cell Biol , vol.146 , pp. 1205-1210
    • Kahana, J.A.1    Cleveland, D.W.2
  • 40
    • 0027397548 scopus 로고
    • NuMA is required for the proper completion of mitosis
    • Compton D.A., Cleveland D.W. NuMA is required for the proper completion of mitosis. J Cell Biol. 120:1993;947-957.
    • (1993) J Cell Biol , vol.120 , pp. 947-957
    • Compton, D.A.1    Cleveland, D.W.2
  • 41
    • 0031965380 scopus 로고    scopus 로고
    • The role of NuMA in the interphase nucleus
    • Merdes A., Cleveland D.W. The role of NuMA in the interphase nucleus. J Cell Sci. 111:1998;71-79.
    • (1998) J Cell Sci , vol.111 , pp. 71-79
    • Merdes, A.1    Cleveland, D.W.2
  • 42
    • 0023489384 scopus 로고
    • Periodic mitotic events induced in the absence of DNA replication
    • Schlegel R., Pardee A.B. Periodic mitotic events induced in the absence of DNA replication. Proc Natl Acad Sci USA. 84:1987;9025-9029.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 9025-9029
    • Schlegel, R.1    Pardee, A.B.2
  • 43
    • 0030775005 scopus 로고    scopus 로고
    • The balance of RanBP1 and RCC1 is critical for nuclear assembly and nuclear transport
    • Pu R.T., Dasso M. The balance of RanBP1 and RCC1 is critical for nuclear assembly and nuclear transport. Mol Biol Cell. 8:1997;1955-1970.
    • (1997) Mol Biol Cell , vol.8 , pp. 1955-1970
    • Pu, R.T.1    Dasso, M.2
  • 45
    • 0028926274 scopus 로고
    • Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport
    • Cheng Y., Dahlberg J.E., Lund E. Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport. Science. 267:1995;1807-1810.
    • (1995) Science , vol.267 , pp. 1807-1810
    • Cheng, Y.1    Dahlberg, J.E.2    Lund, E.3
  • 46
    • 0030879014 scopus 로고    scopus 로고
    • Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export
    • Richards S.A., Carey K.L., Macara I.G. Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export. Science. 276:1997;1842-1844.
    • (1997) Science , vol.276 , pp. 1842-1844
    • Richards, S.A.1    Carey, K.L.2    Macara, I.G.3
  • 47
    • 0030856315 scopus 로고    scopus 로고
    • The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
    • Izaurralde E., Kutay U., von Kobbe C., Mattaj I.W., Gorlich D. The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 16:1997;6535-6547.
    • (1997) EMBO J , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    Von Kobbe, C.3    Mattaj, I.W.4    Gorlich, D.5
  • 48
    • 0028102739 scopus 로고
    • Loss of RCC1 leads to suppression of nuclear protein import in living cells
    • Tachibana T., Imamoto N., Seino H., Nishimoto T., Yoneda Y. Loss of RCC1 leads to suppression of nuclear protein import in living cells. J Biol Chem. 269:1994;24542-24545.
    • (1994) J Biol Chem , vol.269 , pp. 24542-24545
    • Tachibana, T.1    Imamoto, N.2    Seino, H.3    Nishimoto, T.4    Yoneda, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.