메뉴 건너뛰기




Volumn 287, Issue , 2011, Pages 233-286

Nuclear Pore Complex. Biochemistry and Biophysics of Nucleocytoplasmic Transport in Health and Disease

Author keywords

Cancer; Exportin; Importin; Infectious disease; Karyopherins; Nuclear pore complexes; Nucleocytoplasmic transport; Ran

Indexed keywords

KARYOPHERIN; RAN PROTEIN;

EID: 79952578312     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386043-9.00006-2     Document Type: Chapter
Times cited : (86)

References (212)
  • 1
    • 0034806227 scopus 로고    scopus 로고
    • The nuclear pore complex
    • reviews0007.1-reviews0007.6.
    • Adam S.A. The nuclear pore complex. Genome Biol 2001, 2. reviews0007.1-reviews0007.6.
    • (2001) Genome Biol , vol.2
    • Adam, S.A.1
  • 2
    • 64749102559 scopus 로고    scopus 로고
    • Role of Vpr in HIV-1 nuclear import: therapeutic implications
    • Aida Y., Matsuda G. Role of Vpr in HIV-1 nuclear import: therapeutic implications. Curr. HIV Res. 2009, 7:136-143.
    • (2009) Curr. HIV Res. , vol.7 , pp. 136-143
    • Aida, Y.1    Matsuda, G.2
  • 3
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey C.W., Radermacher M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 1993, 122:1-19.
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 5
    • 27944457266 scopus 로고    scopus 로고
    • Intracellular trafficking of retroviral vectors: obstacles and advances
    • Anderson J.L., Hope T.J. Intracellular trafficking of retroviral vectors: obstacles and advances. Gene Ther 2005, 12:1667-1678.
    • (2005) Gene Ther , vol.12 , pp. 1667-1678
    • Anderson, J.L.1    Hope, T.J.2
  • 7
    • 34250824708 scopus 로고    scopus 로고
    • HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore
    • Arhel N.J., Souquere-Besse S., Munier S., Souque P., Guadagnini S., Rutherford S., et al. HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore. EMBO. J. 2007, 26:3025-3037.
    • (2007) EMBO. J. , vol.26 , pp. 3025-3037
    • Arhel, N.J.1    Souquere-Besse, S.2    Munier, S.3    Souque, P.4    Guadagnini, S.5    Rutherford, S.6
  • 8
    • 33750429598 scopus 로고    scopus 로고
    • RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolism
    • Aslanukov A., Bhowmick R., Guruju M., Oswald J., Raz D., Bush R.A., et al. RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolism. PLoS Genet. 2006, 2:1653-1665.
    • (2006) PLoS Genet. , vol.2 , pp. 1653-1665
    • Aslanukov, A.1    Bhowmick, R.2    Guruju, M.3    Oswald, J.4    Raz, D.5    Bush, R.A.6
  • 9
    • 77950854511 scopus 로고    scopus 로고
    • Venezuelan equine Encephalitis virus capsid protein forms a tetrameric complex with CRM1 and importin alpha/beta that obstructs nuclear pore complex function
    • Atasheva S., Fish A., Fornerod M., Frolova E.I. Venezuelan equine Encephalitis virus capsid protein forms a tetrameric complex with CRM1 and importin alpha/beta that obstructs nuclear pore complex function. J. Virol. 2010, 84:4158-4171.
    • (2010) J. Virol. , vol.84 , pp. 4158-4171
    • Atasheva, S.1    Fish, A.2    Fornerod, M.3    Frolova, E.I.4
  • 10
    • 34548087269 scopus 로고    scopus 로고
    • The two tempos of nuclear pore complex evolution: highly adapting proteins in an ancient frozen structure
    • Bapteste E., Charlebois R.L., MacLeod D., Brochier C. The two tempos of nuclear pore complex evolution: highly adapting proteins in an ancient frozen structure. Genome Biol. 2005, 6:R85.1-R85.15.
    • (2005) Genome Biol. , vol.6
    • Bapteste, E.1    Charlebois, R.L.2    MacLeod, D.3    Brochier, C.4
  • 12
    • 60649115824 scopus 로고    scopus 로고
    • Comparative proteomic analyses of the nuclear envelope and pore complex suggests a wide range of heretofore unexpected functions
    • Batrakou D.G., Kerr A.R., Schirmer E.C. Comparative proteomic analyses of the nuclear envelope and pore complex suggests a wide range of heretofore unexpected functions. J. Proteomics 2009, 72:56-70.
    • (2009) J. Proteomics , vol.72 , pp. 56-70
    • Batrakou, D.G.1    Kerr, A.R.2    Schirmer, E.C.3
  • 13
  • 14
    • 0041731883 scopus 로고    scopus 로고
    • Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • Bednenko J., Cingolani G., Gerace L. Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport. J. Cell Biol. 2003, 162:391-401.
    • (2003) J. Cell Biol. , vol.162 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 15
    • 0038701027 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: navigating the channel
    • Bednenko J., Cingolani G., Gerace L. Nucleocytoplasmic transport: navigating the channel. Traffic 2003, 4:127-135.
    • (2003) Traffic , vol.4 , pp. 127-135
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 16
    • 70450265538 scopus 로고    scopus 로고
    • Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr
    • Ben-Efraim I., Frosst P.D., Gerace L. Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr. BMC Cell Biol. 2009, 10:1-9.
    • (2009) BMC Cell Biol. , vol.10 , pp. 1-9
    • Ben-Efraim, I.1    Frosst, P.D.2    Gerace, L.3
  • 17
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import
    • Ben-Efraim I., Gerace L. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J. Cell Biol. 2001, 152:411-417.
    • (2001) J. Cell Biol. , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 18
    • 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. 1997, 419:249-254.
    • (1997) FEBS Lett. , vol.419 , pp. 249-254
    • Bischoff, F.R.1    Gorlich, D.2
  • 19
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: critical elements in the control of small G proteins
    • Bos J.L., Rehmann H., Wittinghofer A. GEFs and GAPs: critical elements in the control of small G proteins. Cell 2007, 129:865-877.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 20
    • 70350755470 scopus 로고    scopus 로고
    • Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice
    • Brohawn S.G., Schwartz T.U. Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice. Nat. Struct. Mol. Biol. 2009, 16:1173-1177.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1173-1177
    • Brohawn, S.G.1    Schwartz, T.U.2
  • 21
    • 77954763260 scopus 로고    scopus 로고
    • Tyr39 of ran preserves the Ran-GTP gradient by inhibiting GTP hydrolysis
    • Brucker S., Gerwert K., Kotting C. Tyr39 of ran preserves the Ran-GTP gradient by inhibiting GTP hydrolysis. J. Mol. Biol. 2010, 401:1-6.
    • (2010) J. Mol. Biol. , vol.401 , pp. 1-6
    • Brucker, S.1    Gerwert, K.2    Kotting, C.3
  • 22
    • 71749108548 scopus 로고    scopus 로고
    • An RNA recognition motif mediates the nucleocytoplasmic transport of a trypanosome RNA-binding protein
    • Cassola A., Frasch A.C. An RNA recognition motif mediates the nucleocytoplasmic transport of a trypanosome RNA-binding protein. J. Biol. Chem. 2009, 284:35015-35028.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35015-35028
    • Cassola, A.1    Frasch, A.C.2
  • 23
    • 0035823482 scopus 로고    scopus 로고
    • Biophysical characterization of interactions involving importin-alpha during nuclear import
    • Catimel B., Teh T., Fontes M.R., Jennings I.G., Jans D.A., Howlett G.J., et al. Biophysical characterization of interactions involving importin-alpha during nuclear import. J. Biol. Chem. 2001, 276:34189-34198.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34189-34198
    • Catimel, B.1    Teh, T.2    Fontes, M.R.3    Jennings, I.G.4    Jans, D.A.5    Howlett, G.J.6
  • 24
    • 77949910116 scopus 로고    scopus 로고
    • Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution
    • Cavalier-Smith T. Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution. Biol. Direct 2010, 5:1-78.
    • (2010) Biol. Direct , vol.5 , pp. 1-78
    • Cavalier-Smith, T.1
  • 25
    • 70349664476 scopus 로고    scopus 로고
    • Therapeutic targeting of nuclear protein import in pathological cell conditions
    • Chahine M.N., Pierce G.N. Therapeutic targeting of nuclear protein import in pathological cell conditions. Pharmacol. Rev. 2009, 61:358-372.
    • (2009) Pharmacol. Rev. , vol.61 , pp. 358-372
    • Chahine, M.N.1    Pierce, G.N.2
  • 26
    • 67650351062 scopus 로고    scopus 로고
    • Nuclear targeting of viral and non-viral DNA
    • Chowdhury E.H. Nuclear targeting of viral and non-viral DNA. Expert Opin. Drug Deliv. 2009, 6:697-703.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , pp. 697-703
    • Chowdhury, E.H.1
  • 27
    • 77955060044 scopus 로고    scopus 로고
    • [Organization and regulation of nucleocytoplasmic transport]
    • Chumakov S.P., Prasolov V.S. [Organization and regulation of nucleocytoplasmic transport]. Mol. Biol. (Mosk) 2010, 44:211-228.
    • (2010) Mol. Biol. (Mosk) , vol.44 , pp. 211-228
    • Chumakov, S.P.1    Prasolov, V.S.2
  • 28
    • 0036923972 scopus 로고    scopus 로고
    • Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta
    • Cingolani G., Bednenko J., Gillespie M.T., Gerace L. Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta. Mol. Cell 2002, 10:1345-1353.
    • (2002) Mol. Cell , vol.10 , pp. 1345-1353
    • Cingolani, G.1    Bednenko, J.2    Gillespie, M.T.3    Gerace, L.4
  • 29
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani G., Petosa C., Weis K., Muller C.W. Structure of importin-beta bound to the IBB domain of importin-alpha. Nature 1999, 399:221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 30
    • 77954592261 scopus 로고    scopus 로고
    • Charge as a Selection Criterion for Translocation through the Nuclear Pore Complex
    • Colwell L.J., Brenner M.P., Ribbeck K. Charge as a Selection Criterion for Translocation through the Nuclear Pore Complex. PLoS Comput. Biol. 2010, 6:1-8.
    • (2010) PLoS Comput. Biol. , vol.6 , pp. 1-8
    • Colwell, L.J.1    Brenner, M.P.2    Ribbeck, K.3
  • 31
    • 0034653375 scopus 로고    scopus 로고
    • Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha
    • Conti E., Kuriyan J. Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha. Structure 2000, 8:329-338.
    • (2000) Structure , vol.8 , pp. 329-338
    • Conti, E.1    Kuriyan, J.2
  • 32
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti E., Muller C.W., Stewart M. Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 2006, 16:237-244.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 237-244
    • Conti, E.1    Muller, C.W.2    Stewart, M.3
  • 33
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A., Bono F., Jinek M., Conti E. Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 2007, 76:647-671.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 34
    • 77951299111 scopus 로고    scopus 로고
    • Nuclear export complexes in the frame
    • Cook A.G., Conti E. Nuclear export complexes in the frame. Curr. Opin. Struct. Biol. 2010, 20:247-252.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 247-252
    • Cook, A.G.1    Conti, E.2
  • 36
    • 36348978046 scopus 로고    scopus 로고
    • The nuclear pore complex: disease associations and functional correlations
    • Cronshaw J.M., Matunis M.J. The nuclear pore complex: disease associations and functional correlations. Trends Endocrinol. Metab. 2004, 15:34-39.
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 34-39
    • Cronshaw, J.M.1    Matunis, M.J.2
  • 37
    • 33645962474 scopus 로고    scopus 로고
    • Nuclear pores form de novo from both sides of the nuclear envelope
    • D'Angelo M.A., Anderson D.J., Richard E., Hetzer M.W. Nuclear pores form de novo from both sides of the nuclear envelope. Science 2006, 312:440-443.
    • (2006) Science , vol.312 , pp. 440-443
    • D'Angelo, M.A.1    Anderson, D.J.2    Richard, E.3    Hetzer, M.W.4
  • 38
    • 33748594987 scopus 로고    scopus 로고
    • The central DNA flap of the human immunodeficiency virus type 1 is important for viral replication
    • De Rijck J., Debyser Z. The central DNA flap of the human immunodeficiency virus type 1 is important for viral replication. Biochem. Biophys. Res. Comm. 2006, 349:1100-1110.
    • (2006) Biochem. Biophys. Res. Comm. , vol.349 , pp. 1100-1110
    • De Rijck, J.1    Debyser, Z.2
  • 39
    • 71049191352 scopus 로고    scopus 로고
    • Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor
    • DeGrasse J.A., DuBois K.N., Devos D., Siegel T.N., Sali A., Field M.C., et al. Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor. Mol. Cell Proteomics 2009, 8:2119-2130.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 2119-2130
    • DeGrasse, J.A.1    DuBois, K.N.2    Devos, D.3    Siegel, T.N.4    Sali, A.5    Field, M.C.6
  • 40
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded
    • Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl. Acad. Sci. USA 2003, 100:2450-2455.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 41
    • 0037031842 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • Denning D.P., Uversky V., Patel S.S., Fink A.L., Rexach M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 2002, 277:33447-33455.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 43
    • 0035954435 scopus 로고    scopus 로고
    • Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex
    • Dilworth D.J., Suprapto A., Padovan J.C., Chait B.T., Wozniak R.W., Rout M.P., et al. Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex. J. Cell Biol. 2001, 153:1465-1478.
    • (2001) J. Cell Biol. , vol.153 , pp. 1465-1478
    • Dilworth, D.J.1    Suprapto, A.2    Padovan, J.C.3    Chait, B.T.4    Wozniak, R.W.5    Rout, M.P.6
  • 44
    • 44949122687 scopus 로고    scopus 로고
    • STRADalpha regulates LKB1 localization by blocking access to importin-alpha, and by association with Crm1 and exportin-7
    • Dorfman J., Macara G.I. STRADalpha regulates LKB1 localization by blocking access to importin-alpha, and by association with Crm1 and exportin-7. Mol. Biol. Cell 2008, 19:1614-1626.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1614-1626
    • Dorfman, J.1    Macara, G.I.2
  • 46
    • 77951884380 scopus 로고    scopus 로고
    • RCC1 uses a conformationally diverse loop region to interact with the nucleosome: a model for the RCC1-nucleosome complex
    • England J.R., Huang J., Jennings M.J., Makde R.D., Tan S. RCC1 uses a conformationally diverse loop region to interact with the nucleosome: a model for the RCC1-nucleosome complex. J. Mol. Biol. 2010, 398:518-529.
    • (2010) J. Mol. Biol. , vol.398 , pp. 518-529
    • England, J.R.1    Huang, J.2    Jennings, M.J.3    Makde, R.D.4    Tan, S.5
  • 48
    • 0031453253 scopus 로고    scopus 로고
    • Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking
    • Fabre E., Hurt E. Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu. Rev. Genet. 1997, 31:277-313.
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 277-313
    • Fabre, E.1    Hurt, E.2
  • 49
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: nucleocytoplasmic transport and beyond
    • Fahrenkrog B., Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat. Rev. Mol. Cell Biol. 2003, 4:757-766.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 50
    • 1842813943 scopus 로고    scopus 로고
    • The nuclear pore complex: a jack of all trades?
    • Fahrenkrog B., Koser J., Aebi U. The nuclear pore complex: a jack of all trades?. Trends Biochem. Sci. 2004, 29:175-182.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 175-182
    • Fahrenkrog, B.1    Koser, J.2    Aebi, U.3
  • 51
    • 0034647917 scopus 로고    scopus 로고
    • Quantitative analysis of nuclear localization signal (NLS)-importin alpha interaction through fluorescence depolarization - Evidence for auto-inhibitory regulation of NLS binding
    • Fanara P., Hodel M.R., Corbett A.H., Hodel A.E. Quantitative analysis of nuclear localization signal (NLS)-importin alpha interaction through fluorescence depolarization - Evidence for auto-inhibitory regulation of NLS binding. J. Biol. Chem. 2000, 275:21218-21223.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21218-21223
    • Fanara, P.1    Hodel, M.R.2    Corbett, A.H.3    Hodel, A.E.4
  • 53
    • 76449089008 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport in yeast: a few roles for many actors
    • Fiserova J., Goldberg M.W. Nucleocytoplasmic transport in yeast: a few roles for many actors. Biochem. Soc. Trans. 2010, 38:273-277.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 273-277
    • Fiserova, J.1    Goldberg, M.W.2
  • 54
    • 0041845285 scopus 로고    scopus 로고
    • Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha
    • Fontes M.R., Teh T., Jans D., Brinkworth R.I., Kobe B. Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha. J. Biol. Chem. 2003, 278:27981-27987.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27981-27987
    • Fontes, M.R.1    Teh, T.2    Jans, D.3    Brinkworth, R.I.4    Kobe, B.5
  • 55
    • 0034646565 scopus 로고    scopus 로고
    • Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha
    • Fontes M.R., Teh T., Kobe B. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha. J. Mol. Biol. 2000, 297:1183-1194.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    Teh, T.2    Kobe, B.3
  • 56
    • 53149119873 scopus 로고    scopus 로고
    • Kap95p binding induces the switch loops of RanGDP to adopt the GTP-bound conformation: implications for nuclear import complex assembly dynamics
    • Forwood J.K., Lonhienne T.G., Marfori M., Robin G., Meng W., Guncar G., et al. Kap95p binding induces the switch loops of RanGDP to adopt the GTP-bound conformation: implications for nuclear import complex assembly dynamics. J. Mol. Biol. 2008, 383:772-782.
    • (2008) J. Mol. Biol. , vol.383 , pp. 772-782
    • Forwood, J.K.1    Lonhienne, T.G.2    Marfori, M.3    Robin, G.4    Meng, W.5    Guncar, G.6
  • 57
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • Frenkiel-Krispin D., Maco B., Aebi U., Medalia O. Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture. J. Mol. Biol. 2010, 395:578-586.
    • (2010) J. Mol. Biol. , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    Maco, B.2    Aebi, U.3    Medalia, O.4
  • 58
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey S., Gorlich D. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 2007, 130:512-523.
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Gorlich, D.2
  • 59
    • 69849085462 scopus 로고    scopus 로고
    • FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties
    • Frey S., Gorlich D. FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties. EMBO J. 2009, 28:2554-2567.
    • (2009) EMBO J. , vol.28 , pp. 2554-2567
    • Frey, S.1    Gorlich, D.2
  • 60
    • 77649091127 scopus 로고    scopus 로고
    • Self-organization of intracellular gradients during mitosis
    • Fuller B.G. Self-organization of intracellular gradients during mitosis. Cell Div. 2010, 5:1-21.
    • (2010) Cell Div. , vol.5 , pp. 1-21
    • Fuller, B.G.1
  • 61
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L., Burke B. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 1988, 4:335-374.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 62
    • 17144377919 scopus 로고    scopus 로고
    • Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran
    • Geyer J.P., Doker R., Kremer W., Zhao X., Kuhlmann J., Kalbitzer H.R. Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran. J. Mol. Biol. 2005, 348:711-725.
    • (2005) J. Mol. Biol. , vol.348 , pp. 711-725
    • Geyer, J.P.1    Doker, R.2    Kremer, W.3    Zhao, X.4    Kuhlmann, J.5    Kalbitzer, H.R.6
  • 63
    • 73249126547 scopus 로고    scopus 로고
    • Recurrent acute necrotizing encephalopathy following influenza A in a genetically predisposed family
    • Gika A.D., Rich P., Gupta S., Neilson D.E., Clarke A. Recurrent acute necrotizing encephalopathy following influenza A in a genetically predisposed family. Dev. Med. Child. Neurol. 2010, 52:99-102.
    • (2010) Dev. Med. Child. Neurol. , vol.52 , pp. 99-102
    • Gika, A.D.1    Rich, P.2    Gupta, S.3    Neilson, D.E.4    Clarke, A.5
  • 64
    • 0345803001 scopus 로고    scopus 로고
    • Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm
    • Gilchrist D., Rexach M. Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm. J. Biol. Chem. 2003, 278:51937-51949.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51937-51949
    • Gilchrist, D.1    Rexach, M.2
  • 65
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • GoÈrlich D., Seewald M., Ribbeck K. Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J. 2003, 22:1088-1100.
    • (2003) EMBO J. , vol.22 , pp. 1088-1100
    • GoÈrlich, D.1    Seewald, M.2    Ribbeck, K.3
  • 67
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D., Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 1999, 15:607-660.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 68
    • 0038187637 scopus 로고    scopus 로고
    • Nuclear import of viral DNA genomes
    • Greber U.F., Fassati A. Nuclear import of viral DNA genomes. Traffic 2003, 4:136-143.
    • (2003) Traffic , vol.4 , pp. 136-143
    • Greber, U.F.1    Fassati, A.2
  • 70
    • 0036337963 scopus 로고    scopus 로고
    • Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus
    • Gustin K.E., Sarnow P. Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J. Virol. 2002, 76:8787-8796.
    • (2002) J. Virol. , vol.76 , pp. 8787-8796
    • Gustin, K.E.1    Sarnow, P.2
  • 71
    • 67649433126 scopus 로고    scopus 로고
    • Calmodulin-driven nuclear entry: trigger for sex determination and terminal differentiation
    • Hanover J.A., Love D.C., Prinz W.A. Calmodulin-driven nuclear entry: trigger for sex determination and terminal differentiation. J. Biol. Chem. 2009, 284:12593-12597.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12593-12597
    • Hanover, J.A.1    Love, D.C.2    Prinz, W.A.3
  • 72
    • 0034282097 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of APC regulates beta-catenin subcellular localization and turnover
    • Henderson B.R. Nuclear-cytoplasmic shuttling of APC regulates beta-catenin subcellular localization and turnover. Nat. Cell Biol. 2000, 2:653-660.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 653-660
    • Henderson, B.R.1
  • 74
    • 34548561643 scopus 로고    scopus 로고
    • A role for transportin in the nuclear import of adenovirus core proteins and DNA
    • Hindley C.E., Lawrence F.J., Matthews D.A. A role for transportin in the nuclear import of adenovirus core proteins and DNA. Traffic 2007, 8:1313-1322.
    • (2007) Traffic , vol.8 , pp. 1313-1322
    • Hindley, C.E.1    Lawrence, F.J.2    Matthews, D.A.3
  • 75
    • 0142091707 scopus 로고    scopus 로고
    • The interaction of animal cytoplasmic RNA viruses with the nucleus to facilitate replication
    • Hiscox J.A. The interaction of animal cytoplasmic RNA viruses with the nucleus to facilitate replication. Virus Res. 2003, 95:13-22.
    • (2003) Virus Res. , vol.95 , pp. 13-22
    • Hiscox, J.A.1
  • 77
    • 75749086867 scopus 로고    scopus 로고
    • Nups take leave of the nuclear envelope to regulate transcription
    • Hou C., Corces V.G. Nups take leave of the nuclear envelope to regulate transcription. Cell 2010, 140:306-308.
    • (2010) Cell , vol.140 , pp. 306-308
    • Hou, C.1    Corces, V.G.2
  • 78
    • 1542708371 scopus 로고    scopus 로고
    • Acute necrotizing encephalopathy of childhood associated with influenza type B virus infection in a 3-year-old girl
    • Huang S.M., Chen C.C., Chiu P.C., Cheng M.F., Lai P.H., Hsieh K.S. Acute necrotizing encephalopathy of childhood associated with influenza type B virus infection in a 3-year-old girl. J. Child Neurol. 2004, 19:64-67.
    • (2004) J. Child Neurol. , vol.19 , pp. 64-67
    • Huang, S.M.1    Chen, C.C.2    Chiu, P.C.3    Cheng, M.F.4    Lai, P.H.5    Hsieh, K.S.6
  • 79
    • 48249150289 scopus 로고    scopus 로고
    • The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import
    • Hutten S., Flotho A., Melchior F., Kehlenbach R.H. The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import. Mol. Biol. Cell 2008, 19:2300-2310.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2300-2310
    • Hutten, S.1    Flotho, A.2    Melchior, F.3    Kehlenbach, R.H.4
  • 80
    • 33846270287 scopus 로고    scopus 로고
    • Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
    • Isgro T., Schulten K. Association of nuclear pore FG-repeat domains to NTF2 import and export complexes. J. Mol. Biol. 2007, 366:330-345.
    • (2007) J. Mol. Biol. , vol.366 , pp. 330-345
    • Isgro, T.1    Schulten, K.2
  • 81
    • 68549083700 scopus 로고    scopus 로고
    • Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes
    • Kahms M., Lehrich P., Huve J., Sanetra N., Peters R. Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes. Traffic 2009, 10:1228-1242.
    • (2009) Traffic , vol.10 , pp. 1228-1242
    • Kahms, M.1    Lehrich, P.2    Huve, J.3    Sanetra, N.4    Peters, R.5
  • 82
    • 51049120110 scopus 로고    scopus 로고
    • A possible mechanism for self-coordination of bidirectional traffic across nuclear pores
    • Kapon R., Topchik A., Mukamel D., Reich Z. A possible mechanism for self-coordination of bidirectional traffic across nuclear pores. Phys. Biol. 2008, 5:036001.
    • (2008) Phys. Biol. , vol.5 , pp. 036001
    • Kapon, R.1    Topchik, A.2    Mukamel, D.3    Reich, Z.4
  • 83
    • 1042278767 scopus 로고    scopus 로고
    • Nuclear transport and cancer: from mechanism to intervention
    • Kau T., Way J., Silver P. Nuclear transport and cancer: from mechanism to intervention. Nat. Rev. Cancer 2004, 4:1-12.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 1-12
    • Kau, T.1    Way, J.2    Silver, P.3
  • 84
    • 0034725636 scopus 로고    scopus 로고
    • Truncated form of importin alpha identified in breast cancer cell inhibits nuclear import of p53
    • Kim I.S., Kim D.H., Han S.M., Chin M.U., Nam H.J., Cho H.P., et al. Truncated form of importin alpha identified in breast cancer cell inhibits nuclear import of p53. J. Biol. Chem. 2000, 275:23139-23145.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23139-23145
    • Kim, I.S.1    Kim, D.H.2    Han, S.M.3    Chin, M.U.4    Nam, H.J.5    Cho, H.P.6
  • 85
    • 70350128228 scopus 로고    scopus 로고
    • The nuclear pore complex protein ALADIN is anchored via NDC1 but not via POM121 and GP210 in the nuclear envelope
    • Kind B., Koehler K., Lorenz M., Huebner A. The nuclear pore complex protein ALADIN is anchored via NDC1 but not via POM121 and GP210 in the nuclear envelope. Biochem. Biophys. Res. Commun. 2009, 390:205-210.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 205-210
    • Kind, B.1    Koehler, K.2    Lorenz, M.3    Huebner, A.4
  • 86
    • 70449393271 scopus 로고    scopus 로고
    • Nuclear contour irregularity and abnormal transporter protein distribution in anterior horn cells in amyotrophic lateral sclerosis
    • Kinoshita Y., Ito H., Hirano A., Fujita K., Wate R., Nakamura M., et al. Nuclear contour irregularity and abnormal transporter protein distribution in anterior horn cells in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 2009, 68:1184-1192.
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 1184-1192
    • Kinoshita, Y.1    Ito, H.2    Hirano, A.3    Fujita, K.4    Wate, R.5    Nakamura, M.6
  • 89
    • 0028964821 scopus 로고
    • Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1
    • Klebe C., Bischoff F.R., Ponstingl H., Wittinghofer A. Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1. Biochemistry 1995, 34:639-647.
    • (1995) Biochemistry , vol.34 , pp. 639-647
    • Klebe, C.1    Bischoff, F.R.2    Ponstingl, H.3    Wittinghofer, A.4
  • 90
    • 77950347231 scopus 로고    scopus 로고
    • Gene regulation by nucleoporins and links to cancer
    • Kohler A., Hurt E. Gene regulation by nucleoporins and links to cancer. Mol. Cell 2010, 38:6-15.
    • (2010) Mol. Cell , vol.38 , pp. 6-15
    • Kohler, A.1    Hurt, E.2
  • 91
    • 35748981206 scopus 로고    scopus 로고
    • A pathway separate from the central channel through the nuclear pore complex for inorganic ions and small macromolecules
    • Kramer A., Ludwig Y., Shahin V., Oberleithner H. A pathway separate from the central channel through the nuclear pore complex for inorganic ions and small macromolecules. J. Biol. Chem. 2007, 282:31437-31443.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31437-31443
    • Kramer, A.1    Ludwig, Y.2    Shahin, V.3    Oberleithner, H.4
  • 92
    • 0342276108 scopus 로고    scopus 로고
    • Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor
    • Kutay U., Bischoff F.R., Kostka S., Kraft R., Gorlich D. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell 1997, 90:1061-1071.
    • (1997) Cell , vol.90 , pp. 1061-1071
    • Kutay, U.1    Bischoff, F.R.2    Kostka, S.3    Kraft, R.4    Gorlich, D.5
  • 93
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: born to be weak
    • Kutay U., Güttinger S. Leucine-rich nuclear-export signals: born to be weak. Trends in Cell Biol. 2005, 15:121-124.
    • (2005) Trends in Cell Biol. , vol.15 , pp. 121-124
    • Kutay, U.1    Güttinger, S.2
  • 95
    • 77950857472 scopus 로고    scopus 로고
    • Progress and prospects: nuclear import of nonviral vectors
    • Lam A.P., Dean D.A. Progress and prospects: nuclear import of nonviral vectors. Gene Ther 2010, 17:439-447.
    • (2010) Gene Ther , vol.17 , pp. 439-447
    • Lam, A.P.1    Dean, D.A.2
  • 96
    • 77949498332 scopus 로고    scopus 로고
    • Expanding the definition of the classical bipartite nuclear localization signal
    • Lange A., McLane L.M., Mills R.E., Devine S.E., Corbett A.H. Expanding the definition of the classical bipartite nuclear localization signal. Traffic 2010, 11:311-323.
    • (2010) Traffic , vol.11 , pp. 311-323
    • Lange, A.1    McLane, L.M.2    Mills, R.E.3    Devine, S.E.4    Corbett, A.H.5
  • 97
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: definition, function, and interaction with importin {alpha}
    • Lange A., Mills R., Lange C., Stewart M., Devine S., Corbett A. Classical nuclear localization signals: definition, function, and interaction with importin {alpha}. J. Biol. Chem. 2007, 282:5101-5105.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.2    Lange, C.3    Stewart, M.4    Devine, S.5    Corbett, A.6
  • 98
    • 77953302554 scopus 로고    scopus 로고
    • Escape of herpesviruses from the nucleus
    • Lee C.P., Chen M.R. Escape of herpesviruses from the nucleus. Rev. Med. Virol. 2010, 20:214-230.
    • (2010) Rev. Med. Virol. , vol.20 , pp. 214-230
    • Lee, C.P.1    Chen, M.R.2
  • 99
    • 33751182615 scopus 로고    scopus 로고
    • Aberrant localization of importin alpha1 in hippocampal neurons in Alzheimer disease
    • Lee H.G., Ueda M., Miyamoto Y., Yoneda Y., Perry G., Smith M.A., et al. Aberrant localization of importin alpha1 in hippocampal neurons in Alzheimer disease. Brain Res 2006, 1124:1-4.
    • (2006) Brain Res , vol.1124 , pp. 1-4
    • Lee, H.G.1    Ueda, M.2    Miyamoto, Y.3    Yoneda, Y.4    Perry, G.5    Smith, M.A.6
  • 100
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • Lee S., Matsuura Y., Liu S., Stewart M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 2005, 435:693-696.
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.1    Matsuura, Y.2    Liu, S.3    Stewart, M.4
  • 101
    • 48949106029 scopus 로고    scopus 로고
    • Biology and biophysics of the nuclear pore complex and its components
    • Lim R., Ullman K., Fahrenkrog B. Biology and biophysics of the nuclear pore complex and its components. Int. Rev. Cell Mol. Biol. 2008, 267:299.
    • (2008) Int. Rev. Cell Mol. Biol. , vol.267 , pp. 299
    • Lim, R.1    Ullman, K.2    Fahrenkrog, B.3
  • 103
    • 69249157304 scopus 로고    scopus 로고
    • Importin-beta Is a GDP-to-GTP exchange factor of Ran implications for the mechanism of nuclear import
    • Lonhienne T.G., Forwood J.K., Marfori M., Robin G., Kobe B., Carroll B.J. Importin-beta Is a GDP-to-GTP exchange factor of Ran implications for the mechanism of nuclear import. J. Biol. Chem. 2009, 284:22549-22558.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22549-22558
    • Lonhienne, T.G.1    Forwood, J.K.2    Marfori, M.3    Robin, G.4    Kobe, B.5    Carroll, B.J.6
  • 104
    • 77951575026 scopus 로고    scopus 로고
    • The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex
    • Lott K., Bhardwaj A., Mitrousis G., Pante N., Cingolani G. The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex. J. Biol. Chem. 2010, 285:13769-13780.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13769-13780
    • Lott, K.1    Bhardwaj, A.2    Mitrousis, G.3    Pante, N.4    Cingolani, G.5
  • 105
    • 0031016658 scopus 로고    scopus 로고
    • Ran-binding protein 1 (RanBP1) forms a ternary complex with Ran and karyopherin beta and reduces Ran GTPase-activating protein (RanGAP) inhibition by karyopherin beta
    • Lounsbury K.M., Macara I.G. Ran-binding protein 1 (RanBP1) forms a ternary complex with Ran and karyopherin beta and reduces Ran GTPase-activating protein (RanGAP) inhibition by karyopherin beta. J. Biol. Chem. 1997, 272:551-555.
    • (1997) J. Biol. Chem. , vol.272 , pp. 551-555
    • Lounsbury, K.M.1    Macara, I.G.2
  • 106
    • 77953403990 scopus 로고    scopus 로고
    • RanGTPase: A Key Regulator of Nucleocytoplasmic Trafficking
    • Lui K., Huang Y. RanGTPase: A Key Regulator of Nucleocytoplasmic Trafficking. Mol. Cell. Pharmacol. 2009, 1:148-156.
    • (2009) Mol. Cell. Pharmacol. , vol.1 , pp. 148-156
    • Lui, K.1    Huang, Y.2
  • 107
    • 34247364639 scopus 로고    scopus 로고
    • Highway to the inner nuclear membrane: rules for the road
    • Lusk C.P., Blobel G., King M.C. Highway to the inner nuclear membrane: rules for the road. Nat. Rev. Mol. Cell Biol. 2007, 8:414-420.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 414-420
    • Lusk, C.P.1    Blobel, G.2    King, M.C.3
  • 108
    • 0037402562 scopus 로고    scopus 로고
    • Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor
    • Ma Z., Hill D.A., Collins M.H., Morris S.W., Sumegi J., Zhou M., et al. Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor. Genes Chromosomes Cancer 2003, 37:98-105.
    • (2003) Genes Chromosomes Cancer , vol.37 , pp. 98-105
    • Ma, Z.1    Hill, D.A.2    Collins, M.H.3    Morris, S.W.4    Sumegi, J.5    Zhou, M.6
  • 109
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara I. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 2001, 65:570-594.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.1
  • 110
    • 33645015535 scopus 로고    scopus 로고
    • Nuclear transport is becoming crystal clear
    • Madrid A.S., Weis K. Nuclear transport is becoming crystal clear. Chromosoma 2006, 115:98-109.
    • (2006) Chromosoma , vol.115 , pp. 98-109
    • Madrid, A.S.1    Weis, K.2
  • 111
    • 0142073738 scopus 로고    scopus 로고
    • Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import
    • Matsuura Y., Lange A., Harreman M., Corbett A., Stewart M. Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import. EMBO J. 2003, 22:5358-5369.
    • (2003) EMBO J. , vol.22 , pp. 5358-5369
    • Matsuura, Y.1    Lange, A.2    Harreman, M.3    Corbett, A.4    Stewart, M.5
  • 112
    • 11144257756 scopus 로고    scopus 로고
    • Structural basis for the assembly of a nuclear export complex
    • Matsuura Y., Stewart M. Structural basis for the assembly of a nuclear export complex. Nature 2004, 432:872-877.
    • (2004) Nature , vol.432 , pp. 872-877
    • Matsuura, Y.1    Stewart, M.2
  • 113
    • 27744577638 scopus 로고    scopus 로고
    • Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling
    • Matsuura Y., Stewart M. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J. 2005, 24:3681-3689.
    • (2005) EMBO J. , vol.24 , pp. 3681-3689
    • Matsuura, Y.1    Stewart, M.2
  • 115
    • 61449201281 scopus 로고    scopus 로고
    • Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics
    • Miao L., Schulten K. Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics. Structure 2009, 17:449-459.
    • (2009) Structure , vol.17 , pp. 449-459
    • Miao, L.1    Schulten, K.2
  • 116
    • 0025806713 scopus 로고
    • Nuclear pore complex: structure, function, and regulation
    • Miller M., Park M.K., Hanover J.A. Nuclear pore complex: structure, function, and regulation. Physiol. Rev. 1991, 71:909-949.
    • (1991) Physiol. Rev. , vol.71 , pp. 909-949
    • Miller, M.1    Park, M.K.2    Hanover, J.A.3
  • 117
    • 75949103898 scopus 로고    scopus 로고
    • The Nup107-160 complex and gamma-TuRC regulate microtubule polymerization at kinetochores
    • Mishra R.K., Chakraborty P., Arnaoutov A., Fontoura B.M.A., Dasso M. The Nup107-160 complex and gamma-TuRC regulate microtubule polymerization at kinetochores. Nat. cell biol. 2010, 12:164-169.
    • (2010) Nat. cell biol. , vol.12 , pp. 164-169
    • Mishra, R.K.1    Chakraborty, P.2    Arnaoutov, A.3    Fontoura, B.M.A.4    Dasso, M.5
  • 118
    • 2942653489 scopus 로고    scopus 로고
    • Cellular stresses induce the nuclear accumulation of importin alpha and cause a conventional nuclear import block
    • Miyamoto Y., Saiwaki T., Yamashita J., Yasuda Y., Kotera I., Shibata S., et al. Cellular stresses induce the nuclear accumulation of importin alpha and cause a conventional nuclear import block. J. Cell Biol. 2004, 165:617-623.
    • (2004) J. Cell Biol. , vol.165 , pp. 617-623
    • Miyamoto, Y.1    Saiwaki, T.2    Yamashita, J.3    Yasuda, Y.4    Kotera, I.5    Shibata, S.6
  • 119
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr D., Frey S., Fischer T., Guttler T., Gorlich D. Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J. 2009, 28:2541-2553.
    • (2009) EMBO J. , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Guttler, T.4    Gorlich, D.5
  • 120
    • 0037307453 scopus 로고    scopus 로고
    • Npap60: a new player in nuclear protein import
    • Moore M.S. Npap60: a new player in nuclear protein import. Trends Cell Biol. 2003, 13:61-64.
    • (2003) Trends Cell Biol. , vol.13 , pp. 61-64
    • Moore, M.S.1
  • 121
    • 0028305912 scopus 로고
    • A G protein involved in nucleocytoplasmic transport: the role of Ran
    • Moore M.S., Blobel G. A G protein involved in nucleocytoplasmic transport: the role of Ran. Trends Biochem. Sci. 1994, 19:211-216.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 211-216
    • Moore, M.S.1    Blobel, G.2
  • 122
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: from nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast N., Pemberton L.F. Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 2004, 14:547-556.
    • (2004) Trends Cell Biol. , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 123
    • 79952598663 scopus 로고    scopus 로고
    • Biophysical Coarse-Grained Modeling Provides Insights into Transport through the Nuclear Pore Complex
    • Moussavi-Baygi R., Jamali Y., Karimi R., Mofrad M.R.K. Biophysical Coarse-Grained Modeling Provides Insights into Transport through the Nuclear Pore Complex. Biophys. J. 2011.
    • (2011) Biophys. J.
    • Moussavi-Baygi, R.1    Jamali, Y.2    Karimi, R.3    Mofrad, M.R.K.4
  • 124
    • 54949093203 scopus 로고    scopus 로고
    • Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase
    • Nagai S., Dubrana K., Tsai-Pflugfelder M., Davidson M.B., Roberts T.M., Brown G.W., et al. Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase. Science 2008, 322:597-602.
    • (2008) Science , vol.322 , pp. 597-602
    • Nagai, S.1    Dubrana, K.2    Tsai-Pflugfelder, M.3    Davidson, M.B.4    Roberts, T.M.5    Brown, G.W.6
  • 125
    • 33947522224 scopus 로고    scopus 로고
    • Passive and facilitated transport in nuclear pore complexes is largely uncoupled
    • Naim B., Brumfeld V., Kapon R., Kiss V., Nevo R., Reich Z. Passive and facilitated transport in nuclear pore complexes is largely uncoupled. J. Biol. Chem. 2007, 282:3881-3888.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3881-3888
    • Naim, B.1    Brumfeld, V.2    Kapon, R.3    Kiss, V.4    Nevo, R.5    Reich, Z.6
  • 126
    • 77951209602 scopus 로고    scopus 로고
    • Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis
    • Nakano H., Funasaka T., Hashizume C., Wong R.W. Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis. J. Biol. Chem. 2010, 285:10841-10849.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10841-10849
    • Nakano, H.1    Funasaka, T.2    Hashizume, C.3    Wong, R.W.4
  • 127
    • 58049220178 scopus 로고    scopus 로고
    • Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2
    • Neilson D.E., Adams M.D., Orr C.M., Schelling D.K., Eiben R.M., Kerr D.S., et al. Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2. Am. J. Hum. Genet. 2009, 84:44-51.
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 44-51
    • Neilson, D.E.1    Adams, M.D.2    Orr, C.M.3    Schelling, D.K.4    Eiben, R.M.5    Kerr, D.S.6
  • 128
    • 78149426167 scopus 로고    scopus 로고
    • Outsourcing the nucleus: nuclear pore complex genes are no longer encoded in nucleomorph genomes
    • Neumann N., Jeffares D.C., Poole A.M. Outsourcing the nucleus: nuclear pore complex genes are no longer encoded in nucleomorph genomes. Evol. Bioinform. Online 2006, 2:23-34.
    • (2006) Evol. Bioinform. Online , vol.2 , pp. 23-34
    • Neumann, N.1    Jeffares, D.C.2    Poole, A.M.3
  • 129
    • 0037398428 scopus 로고    scopus 로고
    • Ran's C-terminal, basic patch, and nucleotide exchange mechanisms in light of a canonical structure for Rab, Rho, Ras, and Ran GTPases
    • Neuwald A.F., Kannan N., Poleksic A., Hata N., Liu J.S. Ran's C-terminal, basic patch, and nucleotide exchange mechanisms in light of a canonical structure for Rab, Rho, Ras, and Ran GTPases. Genome Res. 2003, 13:673-692.
    • (2003) Genome Res. , vol.13 , pp. 673-692
    • Neuwald, A.F.1    Kannan, N.2    Poleksic, A.3    Hata, N.4    Liu, J.S.5
  • 130
    • 0033922776 scopus 로고    scopus 로고
    • Upstream and downstream of ran GTPase
    • Nishimoto T. Upstream and downstream of ran GTPase. Biol. Chem. 2000, 381:397-405.
    • (2000) Biol. Chem. , vol.381 , pp. 397-405
    • Nishimoto, T.1
  • 131
    • 0033979056 scopus 로고    scopus 로고
    • Nuclear pores collapse in response to CO2 imaged with atomic force microscopy
    • Oberleithner H., Schillers H., Wilhelmi M., Butzke D., Danker T. Nuclear pores collapse in response to CO2 imaged with atomic force microscopy. Pflugers Arch. 2000, 439:251-255.
    • (2000) Pflugers Arch. , vol.439 , pp. 251-255
    • Oberleithner, H.1    Schillers, H.2    Wilhelmi, M.3    Butzke, D.4    Danker, T.5
  • 132
    • 76649143068 scopus 로고    scopus 로고
    • Two isoforms of npap60 (nup50) differentially regulate nuclear protein import
    • Ogawa Y., Miyamoto Y., Asally M., Oka M., Yasuda Y., Yoneda Y. Two isoforms of npap60 (nup50) differentially regulate nuclear protein import. Mol. Biol. Cell 2010, 21:630-638.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 630-638
    • Ogawa, Y.1    Miyamoto, Y.2    Asally, M.3    Oka, M.4    Yasuda, Y.5    Yoneda, Y.6
  • 133
    • 55849144420 scopus 로고    scopus 로고
    • Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP
    • Otsuka S., Iwasaka S., Yoneda Y., Takeyasu K., Yoshimura S.H. Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP. Proc. Natl. Acad. Sci. USA 2008, 105:16101-16106.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16101-16106
    • Otsuka, S.1    Iwasaka, S.2    Yoneda, Y.3    Takeyasu, K.4    Yoshimura, S.H.5
  • 134
    • 38849138626 scopus 로고    scopus 로고
    • Differential targeting of nuclear pore complex proteins in poliovirus-infected cells
    • Park N., Katikaneni P., Skern T., Gustin K.E. Differential targeting of nuclear pore complex proteins in poliovirus-infected cells. J. Virol. 2008, 82:1647-1655.
    • (2008) J. Virol. , vol.82 , pp. 1647-1655
    • Park, N.1    Katikaneni, P.2    Skern, T.3    Gustin, K.E.4
  • 135
    • 39049094665 scopus 로고    scopus 로고
    • Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium
    • Patel S., Rexach M. Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium. Mol. Cell. Proteomics 2008, 7:121-131.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 121-131
    • Patel, S.1    Rexach, M.2
  • 136
    • 33748783074 scopus 로고    scopus 로고
    • Changes in nucleoporin domain topology in response to chemical effectors
    • Paulillo S., Powers M., Ullman K., Fahrenkrog B. Changes in nucleoporin domain topology in response to chemical effectors. J. Mol. Biol. 2006, 363:39-50.
    • (2006) J. Mol. Biol. , vol.363 , pp. 39-50
    • Paulillo, S.1    Powers, M.2    Ullman, K.3    Fahrenkrog, B.4
  • 137
    • 77954613984 scopus 로고    scopus 로고
    • Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex
    • Peleg O., Lim R.Y. Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex. Biol. Chem. 2010, 391:719-730.
    • (2010) Biol. Chem. , vol.391 , pp. 719-730
    • Peleg, O.1    Lim, R.Y.2
  • 138
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton L.F., Paschal B.M. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 2005, 6:187-198.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 141
    • 17444427382 scopus 로고    scopus 로고
    • Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality
    • Peters R. Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality. Traffic 2005, 6:421-427.
    • (2005) Traffic , vol.6 , pp. 421-427
    • Peters, R.1
  • 142
    • 69949094947 scopus 로고    scopus 로고
    • Functionalization of a nanopore: the nuclear pore complex paradigm
    • Peters R. Functionalization of a nanopore: the nuclear pore complex paradigm. Biochim. Biophys. Acta 2009, 1793:1533-1539.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1533-1539
    • Peters, R.1
  • 143
    • 65449152302 scopus 로고    scopus 로고
    • Translocation through the nuclear pore: Kaps pave the way
    • Peters R. Translocation through the nuclear pore: Kaps pave the way. Bioessays 2009, 31:466-477.
    • (2009) Bioessays , vol.31 , pp. 466-477
    • Peters, R.1
  • 144
    • 0034635401 scopus 로고    scopus 로고
    • Random mutagenesis and functional analysis of the Ran-binding protein. RanBP1
    • Petersen C., Orem N., Trueheart J., Thorner J.W., Macara I.G. Random mutagenesis and functional analysis of the Ran-binding protein. RanBP1. J. Biol. Chem. 2000, 275:4081-4091.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4081-4091
    • Petersen, C.1    Orem, N.2    Trueheart, J.3    Thorner, J.W.4    Macara, I.G.5
  • 145
    • 67649422214 scopus 로고    scopus 로고
    • DNA-tumor virus entry-From plasma membrane to the nucleus
    • Puntener D., Greber U. DNA-tumor virus entry-From plasma membrane to the nucleus. Semin. Cell. Develop. Biol. 2009, 20:631-642.
    • (2009) Semin. Cell. Develop. Biol. , vol.20 , pp. 631-642
    • Puntener, D.1    Greber, U.2
  • 146
    • 77949320905 scopus 로고    scopus 로고
    • Ran overexpression leads to diminished T cell responses and selectively modulates nuclear levels of c-Jun and c-Fos
    • Qiao X., Pham D.N., Luo H., Wu J. Ran overexpression leads to diminished T cell responses and selectively modulates nuclear levels of c-Jun and c-Fos. J. Biol. Chem. 2010, 285:5488-5496.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5488-5496
    • Qiao, X.1    Pham, D.N.2    Luo, H.3    Wu, J.4
  • 147
    • 0032523832 scopus 로고    scopus 로고
    • ATP-induced shape change of nuclear pores visualized with the atomic force microscope
    • Rakowska A., Danker T., Schneider S.W., Oberleithner H. ATP-induced shape change of nuclear pores visualized with the atomic force microscope. J. Membr. Biol. 1998, 163:129-136.
    • (1998) J. Membr. Biol. , vol.163 , pp. 129-136
    • Rakowska, A.1    Danker, T.2    Schneider, S.W.3    Oberleithner, H.4
  • 148
    • 77953800169 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1
    • Ren Y., Seo H.S., Blobel G., Hoelz A. Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1. Proc. Natl. Acad. Sci. USA 2010, 107:10406-10411.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 10406-10411
    • Ren, Y.1    Seo, H.S.2    Blobel, G.3    Hoelz, A.4
  • 149
    • 0035917523 scopus 로고    scopus 로고
    • Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)
    • Renault L., Kuhlmann J., Henkel A., Wittinghofer A. Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell 2001, 105:245-255.
    • (2001) Cell , vol.105 , pp. 245-255
    • Renault, L.1    Kuhlmann, J.2    Henkel, A.3    Wittinghofer, A.4
  • 150
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K., GoÈrlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 2001, 20:1320-1330.
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    GoÈrlich, D.2
  • 151
    • 73849091932 scopus 로고    scopus 로고
    • Analysis of the viral elements required in the nuclear import of HIV-1 DNA
    • Riviere L., Darlix J.L., Cimarelli A. Analysis of the viral elements required in the nuclear import of HIV-1 DNA. J. Virol. 2010, 84:729-739.
    • (2010) J. Virol. , vol.84 , pp. 729-739
    • Riviere, L.1    Darlix, J.L.2    Cimarelli, A.3
  • 152
    • 73449090103 scopus 로고    scopus 로고
    • Herpesviruses: an in-depth view
    • Rixon F.J. Herpesviruses: an in-depth view. Structure 2010, 18:2-4.
    • (2010) Structure , vol.18 , pp. 2-4
    • Rixon, F.J.1
  • 153
  • 154
    • 0030087693 scopus 로고    scopus 로고
    • The small nuclear GTPase Ran: how much does it run?
    • Rush M.G., Drivas G., D'Eustachio P. The small nuclear GTPase Ran: how much does it run?. Bioessays 1996, 18:103-112.
    • (1996) Bioessays , vol.18 , pp. 103-112
    • Rush, M.G.1    Drivas, G.2    D'Eustachio, P.3
  • 155
    • 59849102099 scopus 로고    scopus 로고
    • Adenoviruses: update on structure and function
    • Russell W.C. Adenoviruses: update on structure and function. J. Gen. Virol. 2009, 90:1-20.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1-20
    • Russell, W.C.1
  • 156
    • 59349098016 scopus 로고    scopus 로고
    • Structure, attachment and entry of polyoma- and papillomaviruses
    • Sapp M., Day P.M. Structure, attachment and entry of polyoma- and papillomaviruses. Virology 2009, 384:400-409.
    • (2009) Virology , vol.384 , pp. 400-409
    • Sapp, M.1    Day, P.M.2
  • 157
    • 33947434505 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the Importin-beta.Ran.GTP.RanBD1 complex
    • Saric M., Zhao X., Korner C., Nowak C., Kuhlmann J., Vetter I.R. Structural and biochemical characterization of the Importin-beta.Ran.GTP.RanBD1 complex. FEBS Lett. 2007, 581:1369-1376.
    • (2007) FEBS Lett. , vol.581 , pp. 1369-1376
    • Saric, M.1    Zhao, X.2    Korner, C.3    Nowak, C.4    Kuhlmann, J.5    Vetter, I.R.6
  • 158
    • 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 1995, 374:378-381.
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritz-Wolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 159
    • 77649199085 scopus 로고    scopus 로고
    • Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket
    • Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J., et al. Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket. PLoS Pathog. 2010, 6:1-15.
    • (2010) PLoS Pathog. , vol.6 , pp. 1-15
    • Schmitz, A.1    Schwarz, A.2    Foss, M.3    Zhou, L.4    Rabe, B.5    Hoellenriegel, J.6
  • 160
    • 46049092765 scopus 로고    scopus 로고
    • The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex
    • Schrader N., Koerner C., Koessmeier K., Bangert J.A., Wittinghofer A., Stoll R., et al. The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex. Structure 2008, 16:1116-1125.
    • (2008) Structure , vol.16 , pp. 1116-1125
    • Schrader, N.1    Koerner, C.2    Koessmeier, K.3    Bangert, J.A.4    Wittinghofer, A.5    Stoll, R.6
  • 161
    • 17044415652 scopus 로고    scopus 로고
    • Modularity within the architecture of the nuclear pore complex
    • Schwartz T.U. Modularity within the architecture of the nuclear pore complex. Curr. Opinion in Structural Biology 2005, 15:221-226.
    • (2005) Curr. Opinion in Structural Biology , vol.15 , pp. 221-226
    • Schwartz, T.U.1
  • 162
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • Seewald M.J., Korner C., Wittinghofer A., Vetter I.R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 2002, 415:662-666.
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1    Korner, C.2    Wittinghofer, A.3    Vetter, I.R.4
  • 163
    • 0242495687 scopus 로고    scopus 로고
    • Biochemical characterization of the Ran-RanBP1-RanGAP system: are RanBP proteins and the acidic tail of RanGAP required for the Ran-RanGAP GTPase reaction?
    • Seewald M.J., Kraemer A., Farkasovsky M., Korner C., Wittinghofer A., Vetter I.R. Biochemical characterization of the Ran-RanBP1-RanGAP system: are RanBP proteins and the acidic tail of RanGAP required for the Ran-RanGAP GTPase reaction?. Mol. Cell. Biol. 2003, 23:8124-8136.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8124-8136
    • Seewald, M.J.1    Kraemer, A.2    Farkasovsky, M.3    Korner, C.4    Wittinghofer, A.5    Vetter, I.R.6
  • 165
    • 0037221524 scopus 로고    scopus 로고
    • Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating
    • Shulga N., Goldfarb D.S. Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating. Mol. Cell. Biol. 2003, 23:534-542.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 534-542
    • Shulga, N.1    Goldfarb, D.S.2
  • 167
    • 0344827223 scopus 로고    scopus 로고
    • Structural biology. Nuclear trafficking
    • Stewart M. Structural biology. Nuclear trafficking. Science 2003, 302:1513-1514.
    • (2003) Science , vol.302 , pp. 1513-1514
    • Stewart, M.1
  • 168
    • 33751297809 scopus 로고    scopus 로고
    • Structural basis for the nuclear protein import cycle
    • Stewart M. Structural basis for the nuclear protein import cycle. Biochem. Soc. T. 2006, 34:701-704.
    • (2006) Biochem. Soc. T. , vol.34 , pp. 701-704
    • Stewart, M.1
  • 169
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart M. Molecular mechanism of the nuclear protein import cycle. Nature Reviews Molecular Cell Biol. 2007, 8:195-208.
    • (2007) Nature Reviews Molecular Cell Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 170
    • 0037453221 scopus 로고    scopus 로고
    • Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport
    • Stoffler D., Feja B., Fahrenkrog B., Walz J., Typke D., Aebi U. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 2003, 328:119-130.
    • (2003) J. Mol. Biol. , vol.328 , pp. 119-130
    • Stoffler, D.1    Feja, B.2    Fahrenkrog, B.3    Walz, J.4    Typke, D.5    Aebi, U.6
  • 171
    • 73249122503 scopus 로고    scopus 로고
    • Deficiency of ferritin heavy-chain nuclear import in triple a syndrome implies nuclear oxidative damage as the primary disease mechanism
    • Storr H.L., Kind B., Parfitt D.A., Chapple J.P., Lorenz M., Koehler K., et al. Deficiency of ferritin heavy-chain nuclear import in triple a syndrome implies nuclear oxidative damage as the primary disease mechanism. Mol. Endocrinol. 2009, 23:2086-2094.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 2086-2094
    • Storr, H.L.1    Kind, B.2    Parfitt, D.A.3    Chapple, J.P.4    Lorenz, M.5    Koehler, K.6
  • 172
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn L., Shen T., Shulga N., Goldfarb D., Wente S. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat. Cell Biol. 2004, 6:197-206.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 197-206
    • Strawn, L.1    Shen, T.2    Shulga, N.3    Goldfarb, D.4    Wente, S.5
  • 173
    • 0034913423 scopus 로고    scopus 로고
    • Importin-beta-like nuclear transport receptors
    • reviews3008.1-reviews3008.9
    • Strom A.C., Weis K. Importin-beta-like nuclear transport receptors. Genome Biol. 2001, 2. reviews3008.1-reviews3008.9.
    • (2001) Genome Biol. , vol.2
    • Strom, A.C.1    Weis, K.2
  • 174
    • 49649128856 scopus 로고    scopus 로고
    • Single-molecule measurements of importin /cargo complex dissociation at the nuclear pore
    • Sun C., Yang W., Tu L., Musser S. Single-molecule measurements of importin /cargo complex dissociation at the nuclear pore. Proc. Natl. Acad. Sci. 2008, 105:8613-8618.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 8613-8618
    • Sun, C.1    Yang, W.2    Tu, L.3    Musser, S.4
  • 175
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam M., Wente S.R. Peering through the pore: Nuclear pore complex structure, assembly, and function. Dev. Cell 2003, 4:775-789.
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 176
    • 60849111935 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 (HIV-1) nuclear import via Vpr-Importin alpha interactions as a novel HIV-1 therapy
    • Suzuki T., Yamamoto N., Nonaka M., Hashimoto Y., Matsuda G., Takeshima S.N., et al. Inhibition of human immunodeficiency virus type 1 (HIV-1) nuclear import via Vpr-Importin alpha interactions as a novel HIV-1 therapy. Biochem. Biophys. Res. Commun. 2009, 380:838-843.
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 838-843
    • Suzuki, T.1    Yamamoto, N.2    Nonaka, M.3    Hashimoto, Y.4    Matsuda, G.5    Takeshima, S.N.6
  • 177
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin - nuclear entry of retroviruses
    • Suzuki Y., Craigie R. The road to chromatin - nuclear entry of retroviruses. Nat. Rev. Microbiol. 2007, 5:187-196.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 178
    • 0036746827 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: More than the usual suspects
    • Swaminathan S., Melchior F. Nucleocytoplasmic transport: More than the usual suspects. Dev. Cell 2002, 3:304-306.
    • (2002) Dev. Cell , vol.3 , pp. 304-306
    • Swaminathan, S.1    Melchior, F.2
  • 179
    • 73749085583 scopus 로고    scopus 로고
    • Comparative and evolutionary aspects of macromolecular translocation across membranes
    • Tartakoff A.M., Tao T. Comparative and evolutionary aspects of macromolecular translocation across membranes. Int. J. Biochem. Cell Biol. 2010, 42:214-229.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 214-229
    • Tartakoff, A.M.1    Tao, T.2
  • 180
    • 73349134975 scopus 로고    scopus 로고
    • Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport
    • Terry L.J., Wente S.R. Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot. Cell 2009, 8:1814-1827.
    • (2009) Eukaryot. Cell , vol.8 , pp. 1814-1827
    • Terry, L.J.1    Wente, S.R.2
  • 181
    • 77955335145 scopus 로고    scopus 로고
    • Armadillo-repeat protein functions: questions for little creatures
    • Tewari R., Bailes E., Bunting K.A., Coates J.C. Armadillo-repeat protein functions: questions for little creatures. Trends Cell Biol. 2010, 20:470-481.
    • (2010) Trends Cell Biol. , vol.20 , pp. 470-481
    • Tewari, R.1    Bailes, E.2    Bunting, K.A.3    Coates, J.C.4
  • 182
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman L.C., Mosberger N., Fornerod M., Stidwill R.P., Greber U.F. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat. Cell Biol. 2001, 3:1092-1100.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 183
    • 0032911885 scopus 로고    scopus 로고
    • The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals
    • Truant R., Cullen B.R. The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals. Mol. Cell Biol. 1999, 19:1210-1217.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1210-1217
    • Truant, R.1    Cullen, B.R.2
  • 184
    • 77952662018 scopus 로고    scopus 로고
    • Differential detection of nuclear envelope autoantibodies in primary biliary cirrhosis using routine and alternative methods
    • Tsangaridou E., Polioudaki H., Sfakianaki R., Samiotaki M., Tzardi M., Koulentaki M., et al. Differential detection of nuclear envelope autoantibodies in primary biliary cirrhosis using routine and alternative methods. BMC Gastroenterol. 2010, 10:1-13.
    • (2010) BMC Gastroenterol. , vol.10 , pp. 1-13
    • Tsangaridou, E.1    Polioudaki, H.2    Sfakianaki, R.3    Samiotaki, M.4    Tzardi, M.5    Koulentaki, M.6
  • 185
  • 186
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter I.R., Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 2001, 294:1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 187
    • 0033636997 scopus 로고    scopus 로고
    • Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98
    • von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D., Bachi A., Wu X., et al. Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98. Mol. Cell 2000, 6:1243-1252.
    • (2000) Mol. Cell , vol.6 , pp. 1243-1252
    • von Kobbe, C.1    van Deursen, J.M.2    Rodrigues, J.P.3    Sitterlin, D.4    Bachi, A.5    Wu, X.6
  • 188
    • 77955311720 scopus 로고    scopus 로고
    • The Part and the Whole: functions of nucleoporins in nucleocytoplasmic transport
    • Walde S., Kehlenbach R.H. The Part and the Whole: functions of nucleoporins in nucleocytoplasmic transport. Trends Cell Biol. 2010, 20:461-469.
    • (2010) Trends Cell Biol. , vol.20 , pp. 461-469
    • Walde, S.1    Kehlenbach, R.H.2
  • 190
    • 0034717044 scopus 로고    scopus 로고
    • Gatekeepers of the nucleus
    • Wente S.R. Gatekeepers of the nucleus. Science 2000, 288:1374-1377.
    • (2000) Science , vol.288 , pp. 1374-1377
    • Wente, S.R.1
  • 191
    • 0030069730 scopus 로고    scopus 로고
    • The role of nuclear import and export in influenza virus infection
    • Whittaker G., Bui M., Helenius A. The role of nuclear import and export in influenza virus infection. Trends Cell Biol. 1996, 6:67-71.
    • (1996) Trends Cell Biol. , vol.6 , pp. 67-71
    • Whittaker, G.1    Bui, M.2    Helenius, A.3
  • 192
    • 50349086996 scopus 로고    scopus 로고
    • On the octagonal structure of the nuclear pore complex: insights from coarse-grained models
    • Wolf C., Mofrad M.R. On the octagonal structure of the nuclear pore complex: insights from coarse-grained models. Biophys. J. 2008, 95:2073-2085.
    • (2008) Biophys. J. , vol.95 , pp. 2073-2085
    • Wolf, C.1    Mofrad, M.R.2
  • 193
    • 79953848096 scopus 로고    scopus 로고
    • Mechanotransduction: role of nuclear pore mechanics and nucleocytoplasmic transport (Ch. 18)
    • Cambridge University Press, New York, M. Mofrad, R. Kamm (Eds.)
    • Wolf C., Mofrad M. Mechanotransduction: role of nuclear pore mechanics and nucleocytoplasmic transport (Ch. 18). Cellular mechanotransduction: diverse perspectives from molecules to tissues 2009, Cambridge University Press, New York. M. Mofrad, R. Kamm (Eds.).
    • (2009) Cellular mechanotransduction: diverse perspectives from molecules to tissues
    • Wolf, C.1    Mofrad, M.2
  • 194
    • 67349288596 scopus 로고    scopus 로고
    • Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1
    • Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A. Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1. J. Virol. 2009, 83:6522-6533.
    • (2009) J. Virol. , vol.83 , pp. 6522-6533
    • Woodward, C.L.1    Prakobwanakit, S.2    Mosessian, S.3    Chow, S.A.4
  • 195
    • 67650351106 scopus 로고    scopus 로고
    • The intracellular mobility of nuclear import receptors and NLS cargoes
    • Wu J., Corbett A.H., Berland K.M. The intracellular mobility of nuclear import receptors and NLS cargoes. Biophys. J. 2009, 96:3840-3849.
    • (2009) Biophys. J. , vol.96 , pp. 3840-3849
    • Wu, J.1    Corbett, A.H.2    Berland, K.M.3
  • 196
    • 67649989017 scopus 로고    scopus 로고
    • The directionality of the nuclear transport of the influenza A genome is driven by selective exposure of nuclear localization sequences on nucleoprotein
    • Wu W.W.H., Pante N. The directionality of the nuclear transport of the influenza A genome is driven by selective exposure of nuclear localization sequences on nucleoprotein. Virol. J. 2009, 6:1-12.
    • (2009) Virol. J. , vol.6 , pp. 1-12
    • Wu, W.W.H.1    Pante, N.2
  • 197
    • 1542284152 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of signal transducers
    • Xu L., Massagué J. Nucleocytoplasmic shuttling of signal transducers. Nature Rev. Mol. Cell Biol. 2004, 5:209-219.
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 209-219
    • Xu, L.1    Massagué, J.2
  • 198
    • 67649435612 scopus 로고    scopus 로고
    • Nuclear pore proteins and cancer
    • Xu S., Powers M.A. Nuclear pore proteins and cancer. Semin. Cell Dev. Biol. 2009, 20:620-630.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 620-630
    • Xu, S.1    Powers, M.A.2
  • 199
    • 58449089201 scopus 로고    scopus 로고
    • Adult neural stem cells and their role in brain pathology
    • Yadirgi G., Marino S. Adult neural stem cells and their role in brain pathology. J. Pathol. 2009, 217:242-253.
    • (2009) J. Pathol. , vol.217 , pp. 242-253
    • Yadirgi, G.1    Marino, S.2
  • 201
    • 77953750360 scopus 로고    scopus 로고
    • Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening
    • Yang S.N., Takeda A.A., Fontes M.R., Harris J.M., Jans D.A., Kobe B. Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening. J. Biol. Chem. 2010, 285:19935-19946.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19935-19946
    • Yang, S.N.1    Takeda, A.A.2    Fontes, M.R.3    Harris, J.M.4    Jans, D.A.5    Kobe, B.6
  • 202
    • 33749023069 scopus 로고    scopus 로고
    • Nuclear import time and transport efficiency depend on importin beta concentration
    • Yang W., Musser S.M. Nuclear import time and transport efficiency depend on importin beta concentration. J. Cell Biol. 2006, 174:951-961.
    • (2006) J. Cell Biol. , vol.174 , pp. 951-961
    • Yang, W.1    Musser, S.M.2
  • 203
    • 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 1999, 96:5516-5521.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5516-5521
    • Yaseen, N.R.1    Blobel, G.2
  • 204
    • 67649452381 scopus 로고    scopus 로고
    • The role of the nuclear transport system in cell differentiation
    • Yasuhara N., Oka M., Yoneda Y. The role of the nuclear transport system in cell differentiation. Semin. Cell Dev. Biol. 2009, 20:590-599.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 590-599
    • Yasuhara, N.1    Oka, M.2    Yoneda, Y.3
  • 205
    • 33845888271 scopus 로고    scopus 로고
    • Triggering neural differentiation of ES cells by subtype switching of importin-alpha
    • Yasuhara N., Shibazaki N., Tanaka S., Nagai M., Kamikawa Y., Oe S., et al. Triggering neural differentiation of ES cells by subtype switching of importin-alpha. Nat. Cell Biol. 2007, 9:72-79.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 72-79
    • Yasuhara, N.1    Shibazaki, N.2    Tanaka, S.3    Nagai, M.4    Kamikawa, Y.5    Oe, S.6
  • 206
    • 66149101014 scopus 로고    scopus 로고
    • Ran on tracks--cytoplasmic roles for a nuclear regulator
    • Yudin D., Fainzilber M. Ran on tracks--cytoplasmic roles for a nuclear regulator. J. Cell Sci. 2009, 122:587-593.
    • (2009) J. Cell Sci. , vol.122 , pp. 587-593
    • Yudin, D.1    Fainzilber, M.2
  • 207
    • 44649192390 scopus 로고    scopus 로고
    • Importin-beta: structural and dynamic determinants of a molecular spring
    • Zachariae U., Grubmuller H. Importin-beta: structural and dynamic determinants of a molecular spring. Structure 2008, 16:906-915.
    • (2008) Structure , vol.16 , pp. 906-915
    • Zachariae, U.1    Grubmuller, H.2
  • 208
    • 33748305808 scopus 로고    scopus 로고
    • A highly strained nuclear conformation of the exportin Cse1p revealed by molecular dynamics simulations
    • Zachariae U., Grubmüller H. A highly strained nuclear conformation of the exportin Cse1p revealed by molecular dynamics simulations. Structure 2006, 14:1469-1478.
    • (2006) Structure , vol.14 , pp. 1469-1478
    • Zachariae, U.1    Grubmüller, H.2
  • 209
    • 9444254054 scopus 로고    scopus 로고
    • The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo
    • Zeitler B., Weis K. The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo. J. Cell Biol. 2004, 167:583-590.
    • (2004) J. Cell Biol. , vol.167 , pp. 583-590
    • Zeitler, B.1    Weis, K.2
  • 211
    • 57349179985 scopus 로고    scopus 로고
    • Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death
    • Zhang X., Chen S., Yoo S., Chakrabarti S., Zhang T., Ke T., et al. Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death. Cell 2008, 135:1017-1027.
    • (2008) Cell , vol.135 , pp. 1017-1027
    • Zhang, X.1    Chen, S.2    Yoo, S.3    Chakrabarti, S.4    Zhang, T.5    Ke, T.6
  • 212
    • 34547597611 scopus 로고    scopus 로고
    • Efficiency, selectivity, and robustness of nucleocytoplasmic transport
    • Zilman A., Di Talia S., Chait B., Rout M., Magnasco M. Efficiency, selectivity, and robustness of nucleocytoplasmic transport. PLoS Comput. Biol. 2007, 3:1281-1290.
    • (2007) PLoS Comput. Biol. , vol.3 , pp. 1281-1290
    • Zilman, A.1    Di Talia, S.2    Chait, B.3    Rout, M.4    Magnasco, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.