메뉴 건너뛰기




Volumn 11, Issue 5, 2012, Pages 31-46

Nucleocytoplasmic transport: A role for nonspecific competition in karyopherin-nucleoporin interactions

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE; KARYOPHERIN; NUCLEOPORIN; PHENYLALANINE;

EID: 84861127061     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.013656     Document Type: Conference Paper
Times cited : (49)

References (126)
  • 1
    • 0016765049 scopus 로고
    • Nucleocytoplasmic movement of fluorescent tracers microinjected into living salivary gland cells
    • Paine, P. L. (1975) Nucleocytoplasmic movement of fluorescent tracers microinjected into living salivary gland cells. J. Cell Biol. 66, 652-657
    • (1975) J. Cell Biol. , vol.66 , pp. 652-657
    • Paine, P.L.1
  • 2
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • DOI 10.1126/science.1132516
    • Frey, S., Richter, R. P., and Görlich, D. (2006) FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314, 815-817 (Pubitemid 44706647)
    • (2006) Science , vol.314 , Issue.5800 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Gorlich, D.3
  • 3
    • 0023840074 scopus 로고
    • Translocation of RNA-coated gold particles through the nuclear pores of oocytes
    • Dworetzky, S. I., and Feldherr, C. M. (1988) Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J. Cell Biol. 106, 575-584 (Pubitemid 18089958)
    • (1988) Journal of Cell Biology , vol.106 , Issue.3 , pp. 575-584
    • Dworetzky, S.I.1    Feldherr, C.M.2
  • 4
    • 0026042170 scopus 로고
    • Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import
    • Adam, S. A., and Gerace, L. (1991) Cytosolic proteins that specifically bind nuclear localization signals are receptors for nuclear import. Cell 66, 837-847 (Pubitemid 121001719)
    • (1991) Cell , vol.66 , Issue.5 , pp. 837-847
    • Adam, S.A.1    Gerace, L.2
  • 5
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope
    • Adam, E. J., and Adam, S. A. (1994) Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125, 547-555 (Pubitemid 24149837)
    • (1994) Journal of Cell Biology , vol.125 , Issue.3 , pp. 547-555
    • Adam, E.J.H.1    Adam, S.A.2
  • 6
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • DOI 10.1016/0092-8674(94)90067-1
    • Görlich, D., Prehn, S., Laskey, R. A., and Hartmann, E. (1994) Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79, 767-778 (Pubitemid 24371968)
    • (1994) Cell , vol.79 , Issue.5 , pp. 767-778
    • Gorlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 7
    • 0029059548 scopus 로고
    • Distinct functions for the two importin subunits in nuclear protein import
    • Görlich, D., Vogel, F., Mills, A. D., Hartmann, E., and Laskey, R. A. (1995) Distinct functions for the two importin subunits in nuclear protein import. Nature 377, 246-248
    • (1995) Nature , vol.377 , pp. 246-248
    • Görlich, D.1    Vogel, F.2    Mills, A.D.3    Hartmann, E.4    Laskey, R.A.5
  • 8
    • 0036210710 scopus 로고    scopus 로고
    • Kap121p-mediated nuclear import is required for mating and cellular differentiation in yeast
    • DOI 10.1128/MCB.22.8.2544-2555.2002
    • Leslie, D. M., Grill, B., Rout, M. P., Wozniak, R. W., and Aitchison, J. D. (2002) Kap121p-mediated nuclear import is required for mating and cellular differentiation in yeast. Mol. Cell. Biol. 22, 2544-2555 (Pubitemid 34262977)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.8 , pp. 2544-2555
    • Leslie, D.M.1    Grill, B.2    Rout, M.P.3    Wozniak, R.W.4    Aitchison, J.D.5
  • 9
    • 0242391971 scopus 로고    scopus 로고
    • Virtual gating and nuclear transport: The hole picture
    • DOI 10.1016/j.tcb.2003.10.007
    • Rout, M. P., Aitchison, J. D., Magnasco, M. O., and Chait, B. T. (2003) Virtual gating and nuclear transport: The hole picture. Trends Cell Biol. 13, 622-628 (Pubitemid 37415027)
    • (2003) Trends in Cell Biology , vol.13 , Issue.12 , pp. 622-628
    • Rout, M.P.1    Aitchison, J.D.2    Magnasco, M.O.3    Chait, B.T.4
  • 10
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • DOI 10.1016/j.tcb.2004.09.004, PII S0962892404002363
    • Mosammaparast, N., and Pemberton, L. F. (2004) Karyopherins: From nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14, 547-556 (Pubitemid 39296617)
    • (2004) Trends in Cell Biology , vol.14 , Issue.10 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 11
    • 48349125312 scopus 로고    scopus 로고
    • The Ty1 integrase protein can exploit the classical nuclear protein import machinery for entry into the nucleus
    • McLane, L. M., Pulliam, K. F., Devine, S. E., and Corbett, A. H. (2008) The Ty1 integrase protein can exploit the classical nuclear protein import machinery for entry into the nucleus. Nucleic Acids Res. 36, 4317-4326
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4317-4326
    • McLane, L.M.1    Pulliam, K.F.2    Devine, S.E.3    Corbett, A.H.4
  • 12
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • Panté, N., and Kann, M. (2002) Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell 13, 425-434
    • (2002) Mol. Biol. Cell , vol.13 , pp. 425-434
    • Panté, N.1    Kann, M.2
  • 13
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara, I. G. (2001) Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65, 570-594
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 14
    • 34648816826 scopus 로고    scopus 로고
    • Exporting RNA from the nucleus to the cytoplasm
    • DOI 10.1038/nrm2255, PII NRM2255
    • Köhler, A., and Hurt, E. (2007) Exporting RNA from the nucleus to the cytoplasm. Nat. Rev. Mol. Cell Biol. 8, 761-773 (Pubitemid 47462133)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 761-773
    • Kohler, A.1    Hurt, E.2
  • 15
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. (2007) Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8, 195-208
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 16
    • 73349134975 scopus 로고    scopus 로고
    • Flexible gates: Dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport
    • Terry, L. J., and Wente, S. R. (2009) Flexible gates: Dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot. Cell 8, 1814-1827
    • (2009) Eukaryot. Cell , vol.8 , pp. 1814-1827
    • Terry, L.J.1    Wente, S.R.2
  • 17
    • 65449152302 scopus 로고    scopus 로고
    • Translocation through the nuclear pore: Kaps pave the way
    • Peters, R. (2009) Translocation through the nuclear pore: Kaps pave the way. Bioessays 31, 466-477
    • (2009) Bioessays , vol.31 , pp. 466-477
    • Peters, R.1
  • 18
    • 0027989786 scopus 로고
    • Pores for thought: Nuclear pore complex proteins
    • DOI 10.1016/0962-8924(94)90085-X
    • Rout, M. P., and Wente, S. R. (1994) Pores for thought: Nuclear pore complex proteins. Trends Cell Biol. 4, 357-365 (Pubitemid 24293338)
    • (1994) Trends in Cell Biology , vol.4 , Issue.10 , pp. 357-365
    • Rout, M.P.1    Wente, S.R.2
  • 19
    • 0035800787 scopus 로고    scopus 로고
    • Proteomic analysis of nucleoporin interacting proteins
    • Allen, N. P., Huang, L., Burlingame, A., Rexach, M. (2001) Proteomic analysis of nucleoporin interacting proteins. J. Biol. Chem. 276, 29268-29274
    • (2001) J. Biol. Chem. , vol.276 , pp. 29268-29274
    • Allen, N.P.1    Huang, L.2    Burlingame, A.3    Rexach, M.4
  • 20
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic Nuclear Pore Complexes: Life on the Edge
    • DOI 10.1016/j.cell.2006.05.027, PII S009286740600674X
    • Tran, E. J., and Wente, S. R. (2006) Dynamic nuclear pore complexes: Life on the edge. Cell 125, 1041-1053 (Pubitemid 43866205)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 22
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P., Aitchison, J. D., Suprapto, A., Hjertaas, K., Zhao, Y., and Chait, B. T. (2000) The yeast nuclear pore complex: Composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 23
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • DOI 10.1093/emboj/20.6.1320
    • Ribbeck, K., and Görlich, D. (2001) Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320-1330 (Pubitemid 32233972)
    • (2001) EMBO Journal , vol.20 , Issue.6 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 26
    • 61449201281 scopus 로고    scopus 로고
    • Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics
    • Miao, L., and Schulten, K. (2009) Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics. Structure 17, 449-459
    • (2009) Structure , vol.17 , pp. 449-459
    • Miao, L.1    Schulten, K.2
  • 27
    • 50949090481 scopus 로고    scopus 로고
    • Intramolecular cohesion of coils mediated by phenylalanine-glycine motifs in the natively unfolded domain of a nucleoporin
    • Krishnan, V. V., Lau, E. Y., Yamada, J., Denning, D. P., Patel, S. S., Colvin, M. E., and Rexach, M. F. (2008) Intramolecular cohesion of coils mediated by phenylalanine-glycine motifs in the natively unfolded domain of a nucleoporin. PLoS Comput. Biol. 4, e1000145
    • (2008) PLoS Comput. Biol. , vol.4
    • Krishnan, V.V.1    Lau, E.Y.2    Yamada, J.3    Denning, D.P.4    Patel, S.S.5    Colvin, M.E.6    Rexach, M.F.7
  • 29
    • 55849144420 scopus 로고    scopus 로고
    • Individual binding pockets of importin-β for FG-nucleoporins have different binding properties and different sensitivities to RanGTP
    • Otsuka, S., Iwasaka, S., Yoneda, Y., Takeyasu, K., and Yoshimura, S. H. (2008) Individual binding pockets of importin-β for FG-nucleoporins have different binding properties and different sensitivities to RanGTP. Proc. Natl. Acad. Sci. U.S.A. 105, 16101-16106
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 16101-16106
    • Otsuka, S.1    Iwasaka, S.2    Yoneda, Y.3    Takeyasu, K.4    Yoshimura, S.H.5
  • 30
    • 0032481309 scopus 로고    scopus 로고
    • Nup116p and Nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor Gle2p
    • DOI 10.1093/emboj/17.4.1107
    • Bailer, S. M., Siniossoglou, S., Podtelejnikov, A., Hellwig, A., Mann, M., and Hurt, E. (1998) Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p. EMBO J. 17, 1107-1119 (Pubitemid 28077664)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 1107-1119
    • Bailer, S.M.1    Siniossoglou, S.2    Podtelejnikov, A.3    Hellwig, A.4    Mann, M.5    Hurt, E.6
  • 31
    • 0033763895 scopus 로고    scopus 로고
    • Crystallization and initial x-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors
    • Bayliss, R., Kent, H. M., Corbett, A. H., and Stewart, M. (2000) Crystallization and initial x-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors. J. Struct. Biol. 131, 240-247
    • (2000) J. Struct. Biol. , vol.131 , pp. 240-247
    • Bayliss, R.1    Kent, H.M.2    Corbett, A.H.3    Stewart, M.4
  • 32
    • 0037124352 scopus 로고    scopus 로고
    • Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats
    • DOI 10.1093/emboj/cdf305
    • Bayliss, R., Leung, S. W., Baker, R. P., Quimby, B. B., Corbett, A. H., and Stewart, M. (2002) Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. EMBO J. 21, 2843-2853 (Pubitemid 34670369)
    • (2002) EMBO Journal , vol.21 , Issue.12 , pp. 2843-2853
    • Bayliss, R.1    Leung, S.W.2    Baker, R.P.3    Quimby, B.B.4    Corbett, A.H.5    Stewart, M.6
  • 33
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking
    • Bayliss, R., Littlewood, T., and Stewart, M. (2000) Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell 102, 99-108
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 34
  • 35
    • 0032589798 scopus 로고    scopus 로고
    • Interaction between NTFP and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP
    • DOI 10.1006/jmbi.1999.3166
    • Bayliss, R., Ribbeck, K., Akin, D., Kent, H. M., Feldherr, C. M., Gö rlich, D., and Stewart, M. (1999) Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP. J. Mol. Biol. 293, 579-593 (Pubitemid 29512058)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.3 , pp. 579-593
    • Bayliss, R.1    Ribbeck, K.2    Akin, D.3    Kent, H.M.4    Feldherr, C.M.5    Gorlich, D.6    Stewart, M.7
  • 36
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import
    • DOI 10.1083/jcb.152.2.411
    • Ben-Efraim, I., and Gerace, L. (2001) Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import. J. Cell Biol. 152, 411-417 (Pubitemid 34285609)
    • (2001) Journal of Cell Biology , vol.152 , Issue.2 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 37
    • 0037124045 scopus 로고    scopus 로고
    • Accelerating the rate of disassembly of karyopherin.cargo complexes
    • DOI 10.1074/jbc.M112306200
    • Gilchrist, D., Mykytka, B., and Rexach, M. (2002) Accelerating the rate of disassembly of karyopherin.cargo complexes. J. Biol. Chem. 277, 18161-18172 (Pubitemid 34967632)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 18161-18172
    • Gilchrist, D.1    Mykytka, B.2    Rexach, M.3
  • 38
    • 0345803001 scopus 로고    scopus 로고
    • Molecular Basis for the Rapid Dissociation of Nuclear Localization Signals from Karyopherin α in the Nucleoplasm
    • DOI 10.1074/jbc.M307371200
    • Gilchrist, D., and Rexach, M. (2003) Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin α in the nucleoplasm. J. Biol. Chem. 278, 51937-51949 (Pubitemid 38020441)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51937-51949
    • Gilchrist, D.1    Rexach, M.2
  • 39
    • 0037459067 scopus 로고    scopus 로고
    • Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1 A resolution
    • DOI 10.1016/S0022-2836(02)01474-2
    • Grant, R. P., Neuhaus, D., and Stewart, M. (2003) Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution. J. Mol. Biol. 326, 849-858 (Pubitemid 36279324)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.3 , pp. 849-858
    • Grant, R.P.1    Neuhaus, D.2    Stewart, M.3
  • 40
    • 0029558543 scopus 로고
    • The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor
    • DOI 10.1083/jcb.131.6.1699
    • Iovine, M. K., Watkins, J. L., and Wente, S. R. (1995) The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J. Cell Biol. 131, 1699-1713 (Pubitemid 26007968)
    • (1995) Journal of Cell Biology , vol.131 , Issue.6 II , pp. 1699-1713
    • Iovine, M.K.1    Watkins, J.L.2    Wente, S.R.3
  • 41
    • 34547657392 scopus 로고    scopus 로고
    • Cse1p-Binding Dynamics Reveal a Binding Pattern for FG-Repeat Nucleoporins on Transport Receptors
    • DOI 10.1016/j.str.2007.06.011, PII S0969212607002419
    • Isgro, T. A., and Schulten, K. (2007) Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors. Structure 15, 977-991 (Pubitemid 47212749)
    • (2007) Structure , vol.15 , Issue.8 , pp. 977-991
    • Isgro, T.A.1    Schulten, K.2
  • 42
    • 33846270287 scopus 로고    scopus 로고
    • Association of Nuclear Pore FG-repeat Domains to NTF2 Import and Export Complexes
    • DOI 10.1016/j.jmb.2006.11.048, PII S0022283606015889
    • Isgro, T. A., and Schulten, K. (2007) Association of nuclear pore FG-repeat domains to NTF2 import and export complexes. J. Mol. Biol. 366, 330-345 (Pubitemid 46123344)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 330-345
    • Isgro, T.A.1    Schulten, K.2
  • 43
    • 0032576573 scopus 로고    scopus 로고
    • Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p
    • DOI 10.1083/jcb.143.7.1813
    • Marelli, M., Aitchison, J. D., and Wozniak, R. W. (1998) Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J. Cell Biol. 143, 1813-1830 (Pubitemid 29022606)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1813-1830
    • Marelli, M.1    Aitchison, J.D.2    Wozniak, R.W.3
  • 44
    • 0141750584 scopus 로고    scopus 로고
    • Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats
    • DOI 10.1016/j.jmb.2003.08.050
    • Morrison, J., Yang, J. C., Stewart, M., and Neuhaus, D. (2003) Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats. J. Mol. Biol. 333, 587-603 (Pubitemid 37222408)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.3 , pp. 587-603
    • Morrison, J.1    Yang, J.-C.2    Stewart, M.3    Neuhaus, D.4
  • 45
    • 0035794237 scopus 로고    scopus 로고
    • The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex
    • Strawn, L. A., Shen, T., and Wente, S. R. (2001) The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. J. Biol. Chem. 276, 6445-6452
    • (2001) J. Biol. Chem. , vol.276 , pp. 6445-6452
    • Strawn, L.A.1    Shen, T.2    Wente, S.R.3
  • 46
    • 0028950991 scopus 로고
    • Identification of a protein complex that is required for nuclear-protein import and mediates docking of import substrate to distinct nucleoporins
    • Radu, A., Blobel, G., and Moore, M. S. (1995) Identification of a protein complex that is required for nuclear-protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Natl. Acad. Sci. U.S.A. 92, 1769-1773
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1769-1773
    • Radu, A.1    Blobel, G.2    Moore, M.S.3
  • 47
    • 0029021567 scopus 로고
    • The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear-pore complex
    • Radu, A., Moore, M. S., and Blobel, G. (1995) The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear-pore complex. Cell 81, 215-222
    • (1995) Cell , vol.81 , pp. 215-222
    • Radu, A.1    Moore, M.S.2    Blobel, G.3
  • 50
    • 0030826127 scopus 로고    scopus 로고
    • Enantioseparation using apoenzymes immobilized in a porous polymeric membrane
    • DOI 10.1038/41978
    • Lakshmi, B. B., and Martin, C. R. (1997) Enantioseparation using apoen-zymes immobilized in a porous polymeric membrane. Nature 388, 758-760 (Pubitemid 27375151)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 758-760
    • Lakshmi, B.B.1    Martin, C.R.2
  • 51
    • 58149288627 scopus 로고    scopus 로고
    • Synthetic mimic of selective transport through the nuclear pore complex
    • Caspi, Y., Zbaida, D., Cohen, H., and Elbaum, M. (2008) Synthetic mimic of selective transport through the nuclear pore complex. Nano. Lett. 8, 3728-3734
    • (2008) Nano. Lett. , vol.8 , pp. 3728-3734
    • Caspi, Y.1    Zbaida, D.2    Cohen, H.3    Elbaum, M.4
  • 52
    • 77949328500 scopus 로고    scopus 로고
    • The mysterious unfoldome: Structureless, underappreciated, yet vital part of any given proteome
    • Uversky, V. N. (2010) The mysterious unfoldome: Structureless, underappreciated, yet vital part of any given proteome. J. Biomed. Biotechnol. 2010, 568068
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 568068
    • Uversky, V.N.1
  • 53
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky, V. N., Gillespie, J. R., and Fink, A. L. (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41, 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 54
    • 0035824545 scopus 로고    scopus 로고
    • Residual structure and dynamics in Parkinson's disease-associated mutants of α-synuclein
    • Bussell, R., Jr., and Eliezer, D. (2001) Residual structure and dynamics in Parkinson's disease-associated mutants of α-synuclein. J. Biol. Chem. 276, 45996-46003
    • (2001) J. Biol. Chem. , vol.276 , pp. 45996-46003
    • Bussell Jr., R.1    Eliezer, D.2
  • 55
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • Eliezer, D. (2009) Biophysical characterization of intrinsically disordered proteins. Curr. Opin. Struct. Biol. 19, 23-30
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 57
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes
    • Uversky, V. N. (2011) Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes. Chem. Soc. Rev. 40, 1623-1634
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1623-1634
    • Uversky, V.N.1
  • 58
    • 77955327536 scopus 로고    scopus 로고
    • Intrinsically disordered proteins are potential drug targets
    • Metallo, S. J. (2010) Intrinsically disordered proteins are potential drug targets. Curr. Opin. Chem. Biol. 14, 481-488
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 481-488
    • Metallo, S.J.1
  • 59
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein nonfolding
    • Uversky, V. N., and Dunker, A. K. (2010) Understanding protein nonfolding. Biochim. Biophys. Acta 1804, 1231-1264
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 60
    • 77249105931 scopus 로고    scopus 로고
    • Protein intrinsic disorder and oligomericity in cell signaling
    • Sigalov, A. B. (2010) Protein intrinsic disorder and oligomericity in cell signaling. Mol. Biosyst. 6, 451-461
    • (2010) Mol. Biosyst. , vol.6 , pp. 451-461
    • Sigalov, A.B.1
  • 61
    • 68749093787 scopus 로고    scopus 로고
    • Predicting intrinsic disorder in proteins: An overview
    • He, B., Wang, K., Liu, Y., Xue, B., Uversky, V. N., and Dunker, A. K. (2009) Predicting intrinsic disorder in proteins: An overview. Cell Res. 19, 929-949
    • (2009) Cell Res. , vol.19 , pp. 929-949
    • He, B.1    Wang, K.2    Liu, Y.3    Xue, B.4    Uversky, V.N.5    Dunker, A.K.6
  • 62
    • 72449139985 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and their environment: Effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding
    • Uversky, V. N. (2009) Intrinsically disordered proteins and their environment: Effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding. Protein J. 28, 305-325
    • (2009) Protein J. , vol.28 , pp. 305-325
    • Uversky, V.N.1
  • 65
    • 77957370148 scopus 로고    scopus 로고
    • In vivo imaging of labelled endogenous B-actin mRNA during nucleocytoplasmic transport
    • Grünwald, D., and Singer, R. H. (2010) In vivo imaging of labelled endogenous B-actin mRNA during nucleocytoplasmic transport. Nature 467, 604-607
    • (2010) Nature , vol.467 , pp. 604-607
    • Grünwald, D.1    Singer, R.H.2
  • 66
    • 0034208665 scopus 로고    scopus 로고
    • The molecular mechanism of transport of macromolecules through nuclear pore complexes
    • Bayliss, R., Corbett, A. H., and Stewart, M. (2000) The molecular mechanism of transport of macromolecules through nuclear pore complexes. Traffic 1, 448-456
    • (2000) Traffic , vol.1 , pp. 448-456
    • Bayliss, R.1    Corbett, A.H.2    Stewart, M.3
  • 67
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-β
    • DOI 10.1016/j.str.2005.09.007, PII S0969212605003643
    • Isgro, T. A., and Schulten, K. (2005) Binding dynamics of isolated nucleoporin repeat regions to importin-β. Structure 13, 1869-1879 (Pubitemid 41772955)
    • (2005) Structure , vol.13 , Issue.12 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 68
    • 0142180053 scopus 로고    scopus 로고
    • A Gradient of Affinity for the Karyopherin Kap95p along the Yeast Nuclear Pore Complex
    • DOI 10.1074/jbc.M307135200
    • Pyhtila, B., and Rexach, M. (2003) A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J. Biol. Chem. 278, 42699-42709 (Pubitemid 37310545)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 69
    • 77951575026 scopus 로고    scopus 로고
    • The importin β binding domain modulates the avidity of importin β for the nuclear pore complex
    • Lott, K., Bhardwaj, A., Mitrousis, G., Pante, N., and Cingolani, G. (2010) The importin β binding domain modulates the avidity of importin β for the nuclear pore complex. J. Biol. Chem. 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
  • 71
    • 33751407500 scopus 로고    scopus 로고
    • Significant Proportions of Nuclear Transport Proteins with Reduced Intracellular Mobilities Resolved by Fluorescence Correlation Spectroscopy
    • DOI 10.1016/j.jmb.2006.09.089, PII S0022283606013246
    • Paradise, A., Levin, M. K., Korza, G., and Carson, J. H. (2007) Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy. J. Mol. Biol. 365, 50-65 (Pubitemid 44821209)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.1 , pp. 50-65
    • Paradise, A.1    Levin, M.K.2    Korza, G.3    Carson, J.H.4
  • 72
    • 33751222250 scopus 로고    scopus 로고
    • Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo
    • DOI 10.1083/jcb.200608141
    • Timney, B. L., Tetenbaum-Novatt, J., Agate, D. S., Williams, R., Zhang, W., Chait, B. T., and Rout, M. P. (2006) Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo. J. Cell Biol. 175, 579-593 (Pubitemid 44790612)
    • (2006) Journal of Cell Biology , vol.175 , Issue.4 , pp. 579-593
    • Timney, B.L.1    Tetenbaum-Novatt, J.2    Agate, D.S.3    Williams, R.4    Zhang, W.5    Chait, B.T.6    Rout, M.P.7
  • 73
    • 69949094947 scopus 로고    scopus 로고
    • Functionalization of a nanopore: The nuclear pore complex paradigm
    • Peters, R. (2009) Functionalization of a nanopore: The nuclear pore complex paradigm. Biochim. Biophys. Acta 1793, 1533-1539
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1533-1539
    • Peters, R.1
  • 74
    • 0030726210 scopus 로고    scopus 로고
    • Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex
    • Kose, S., Imamoto, N., Tachibana, T., Shimamoto, T., and Yoneda, Y. (1997) Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex. J. Cell Biol. 139, 841-849
    • (1997) J. Cell Biol. , vol.139 , pp. 841-849
    • Kose, S.1    Imamoto, N.2    Tachibana, T.3    Shimamoto, T.4    Yoneda, Y.5
  • 75
    • 53749102019 scopus 로고    scopus 로고
    • Autonomy and robustness of translocation through the nuclear pore complex: A single-molecule study
    • Dange, T., Grü nwald, D., Grü nwald, A., Peters, R., and Kubitscheck, U. (2008) Autonomy and robustness of translocation through the nuclear pore complex: A single-molecule study. J. Cell Biol. 183, 77-86
    • (2008) J. Cell Biol. , vol.183 , pp. 77-86
    • Dange, T.1    Grünwald, D.2    Grünwald, A.3    Peters, R.4    Kubitscheck, U.5
  • 76
    • 79960927256 scopus 로고    scopus 로고
    • Single molecule studies of nucleocytoplasmic transport
    • Tu, L. C., and Musser, S. M. (2011) Single molecule studies of nucleocytoplasmic transport. Biochim. Biophys. Acta 1813, 1607-1618
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1607-1618
    • Tu, L.C.1    Musser, S.M.2
  • 77
    • 34249939863 scopus 로고    scopus 로고
    • The adapter importin-α provides flexible control of nuclear import at the expense of efficiency
    • Riddick, G., and Macara, I. G. (2007) The adapter importin-α provides flexible control of nuclear import at the expense of efficiency. Mol. Syst. Biol. 3, 118
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 118
    • Riddick, G.1    Macara, I.G.2
  • 78
    • 16844374515 scopus 로고    scopus 로고
    • A systems analysis of importin-α-βmediated nuclear protein import
    • Riddick, G., and Macara, I. G. (2005) A systems analysis of importin-α-βmediated nuclear protein import. J. Cell Biol. 168, 1027-1038
    • (2005) J. Cell Biol. , vol.168 , pp. 1027-1038
    • Riddick, G.1    Macara, I.G.2
  • 80
    • 34547679515 scopus 로고    scopus 로고
    • A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes
    • DOI 10.1016/j.cell.2007.06.024, PII S009286740700791X
    • Frey, S., and Görlich, D. (2007) A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130, 512-523 (Pubitemid 47208521)
    • (2007) Cell , vol.130 , Issue.3 , pp. 512-523
    • Frey, S.1    Gorlich, D.2
  • 81
    • 69849085462 scopus 로고    scopus 로고
    • FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties
    • Frey, S., and Görlich, D. (2009) FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties. EMBO J. 28, 2554-2567
    • (2009) EMBO J. , vol.28 , pp. 2554-2567
    • Frey, S.1    Görlich, D.2
  • 82
    • 33947727395 scopus 로고    scopus 로고
    • Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex
    • DOI 10.1016/j.cell.2007.01.044, PII S0092867407003030
    • Patel, S. S., Belmont, B. J., Sante, J. M., and Rexach, M. F. (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129, 83-96 (Pubitemid 46507580)
    • (2007) Cell , vol.129 , Issue.1 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 83
    • 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
    • DOI 10.1074/mcp.M700407-MCP200
    • Patel, S. S., and Rexach, M. F. (2008) 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 7, 121-131 (Pubitemid 351248238)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.1 , pp. 121-131
    • Patel, S.S.1    Rexach, M.F.2
  • 84
    • 0018784168 scopus 로고
    • The effect of multivalency on the specificity of protein and cell interactions
    • Ehrlich, P. H. (1979) The effect of multivalency on the specificity of protein and cell interactions. J. Theor. Biol. 81, 123-127
    • (1979) J. Theor. Biol. , vol.81 , pp. 123-127
    • Ehrlich, P.H.1
  • 86
    • 19444383899 scopus 로고    scopus 로고
    • Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p
    • DOI 10.1016/j.jmb.2005.04.003, PII S0022283605004018
    • Liu, S. M., and Stewart, M. (2005) Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J. Mol. Biol. 349, 515-525 (Pubitemid 40724562)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.3 , pp. 515-525
    • Liu, S.M.1    Stewart, M.2
  • 87
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • DOI 10.1038/nature03578
    • Lee, S. J., Matsuura, Y., Liu, S. M., and Stewart, M. (2005) Structural basis for nuclear import complex dissociation by RanGTP. Nature 435, 693-696 (Pubitemid 40825515)
    • (2005) Nature , vol.435 , Issue.7042 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 88
    • 0030722506 scopus 로고    scopus 로고
    • A distinct nuclear import pathway used by ribosomal proteins
    • Rout, M. P., Blobel, G., and Aitchison, J. D. (1997) A distinct nuclear import pathway used by ribosomal proteins. Cell 89, 715-725 (Pubitemid 27516174)
    • (1997) Cell , vol.89 , Issue.5 , pp. 715-725
    • Rout, M.P.1    Blobel, G.2    Aitchison, J.D.3
  • 89
    • 4544352379 scopus 로고    scopus 로고
    • Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import
    • DOI 10.1128/MCB.24.19.8487-8503.2004
    • Leslie, D. M., Zhang, W., Timney, B. L., Chait, B. T., Rout, M. P., Wozniak, R. W., and Aitchison, J. D. (2004) Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import. Mol. Cell. Biol. 24, 8487-8503 (Pubitemid 39245071)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.19 , pp. 8487-8503
    • Leslie, D.M.1    Zhang, W.2    Timney, B.L.3    Chait, B.T.4    Rout, M.P.5    Wozniak, R.W.6    Aitchison, J.D.7
  • 90
    • 0032168565 scopus 로고    scopus 로고
    • Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121
    • Kaffman, A., Rank, N. M., and O'Shea, E. K. (1998) Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes Dev. 12, 2673-2683 (Pubitemid 28420648)
    • (1998) Genes and Development , vol.12 , Issue.17 , pp. 2673-2683
    • Kaffman, A.1    Rank, N.M.2    O'Shea, E.K.3
  • 91
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust, R. B., Tö zsér, J., Fox, J. D., Anderson, D. E., Cherry, S., Copeland, T. D., and Waugh, D. S. (2001) Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng. 14, 993-1000
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tözsér, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 94
    • 0027464867 scopus 로고
    • Polyvinylpyrrolidone as a blocking agent in immunochemical studies
    • Haycock, J. W. (1993) Polyvinylpyrrolidone as a blocking agent in immunochemical studies. Anal. Biochem. 208, 397-399
    • (1993) Anal. Biochem. , vol.208 , pp. 397-399
    • Haycock, J.W.1
  • 96
    • 0029845118 scopus 로고    scopus 로고
    • Kap104p: A karyopherin involved in the nuclear transport of messenger RNA binding proteins
    • DOI 10.1126/science.274.5287.624
    • Aitchison, J. D., Blobel, G., and Rout, M. P. (1996) Kap104p: A karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science 274, 624-627 (Pubitemid 26360444)
    • (1996) Science , vol.274 , Issue.5287 , pp. 624-627
    • Aitchison, J.D.1    Blobel, G.2    Rout, M.P.3
  • 98
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn, L. A., Shen, T., Shulga, N., Goldfarb, D. S., and Wente, S. R. (2004) Minimal nuclear pore complexes define FG repeat domains essential for transport. Nature Cell Biol. 6, 197-206 (Pubitemid 38344357)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 197-206
    • Strawn, L.A.1    Shen, T.2    Shulga, N.3    Goldfarb, D.S.4    Wente, S.R.5
  • 99
    • 38149118681 scopus 로고    scopus 로고
    • Structural basis of the nic96 subcomplex organization in the nuclear pore channel
    • Schrader, N., Stelter, P., Flemming, D., Kunze, R., Hurt, E., and Vetter, I. R. (2008) Structural basis of the nic96 subcomplex organization in the nuclear pore channel. Mol. Cell 29, 46-55
    • (2008) Mol. Cell , vol.29 , pp. 46-55
    • Schrader, N.1    Stelter, P.2    Flemming, D.3    Kunze, R.4    Hurt, E.5    Vetter, I.R.6
  • 100
    • 28844481936 scopus 로고    scopus 로고
    • Reduction of nonspecific binding proteins to self-assembled monolayer on gold surface
    • DOI 10.1016/j.bmc.2005.09.030, PII S096808960500876X
    • Furuya, M., Haramura, M., and Tanaka, A. (2006) Reduction of nonspecific binding proteins to self-assembled monolayer on gold surface. Bioorg. Med. Chem. 14, 537-543 (Pubitemid 41767614)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.2 , pp. 537-543
    • Furuya, M.1    Haramura, M.2    Tanaka, A.3
  • 101
    • 0036302861 scopus 로고    scopus 로고
    • A repressor protein, PhaR, regulates polyhydroxyalkanoate (PHA) synthesis via its direct interaction with PHA
    • DOI 10.1128/JB.184.14.3992-4002.2002
    • Maehara, A., Taguchi, S., Nishiyama, T., Yamane, T., and Doi, Y. (2002) A repressor protein, PhaR, regulates polyhydroxyalkanoate (PHA) synthesis via its direct interaction with PHA. J. Bacteriol. 184, 3992-4002 (Pubitemid 34705458)
    • (2002) Journal of Bacteriology , vol.184 , Issue.14 , pp. 3992-4002
    • Maehara, A.1    Taguchi, S.2    Nishiyama, T.3    Yamane, T.4    Doi, Y.5
  • 102
    • 79957787217 scopus 로고    scopus 로고
    • Macromolecular crowding fails to fold a globular protein in cells
    • Schlesinger, A. P., Wang, Y., Tadeo, X., Millet, O., and Pielak, G. J. (2011) Macromolecular crowding fails to fold a globular protein in cells. J. Am. Chem. Soc. 133, 8082-8085
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8082-8085
    • Schlesinger, A.P.1    Wang, Y.2    Tadeo, X.3    Millet, O.4    Pielak, G.J.5
  • 103
    • 84856381681 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy of intact nuclear pore complexes
    • Cardarelli, F., Lanzano, L., and Gratton, E. (2011) Fluorescence correlation spectroscopy of intact nuclear pore complexes. Biophys. J. 101, L27-L29
    • (2011) Biophys. J. , vol.101
    • Cardarelli, F.1    Lanzano, L.2    Gratton, E.3
  • 104
    • 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
    • DOI 10.1093/emboj/16.21.6535
    • Izaurralde, E., Kutay, U., von Kobbe, C., Mattaj, I. W., and Görlich, D. (1997) The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 16, 6535-6547 (Pubitemid 27483278)
    • (1997) EMBO Journal , vol.16 , Issue.21 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    Von Kobbe, C.3    Mattaj, L.W.4    Gorlich, D.5
  • 105
    • 0030851465 scopus 로고    scopus 로고
    • Disassembly of RangTP-karyopherin β complex, an intermediate in nuclear protein import
    • DOI 10.1074/jbc.272.31.19538
    • Floer, M., Blobel, G., and Rexach, M. (1997) Disassembly of RanGTP-karyopherin β complex, an intermediate in nuclear protein import. J. Biol. Chem. 272, 19538-19546 (Pubitemid 27337755)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19538-19546
    • Floer, M.1    Blobel, G.2    Rexach, M.3
  • 106
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach, M., and Blobel, G. (1995) Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83, 683-692
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 107
    • 0038701027 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Navigating the channel
    • Bednenko, J., Cingolani, G., and Gerace, L. (2003) Nucleocytoplasmic transport: Navigating the channel. Traffic 4, 127-135 (Pubitemid 36621705)
    • (2003) Traffic , vol.4 , Issue.3 , pp. 127-135
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 108
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen, M., Choi, S., and Whitesides, G. (1998) Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. Engl. 37, 2755-2794
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.2    Whitesides, G.3
  • 109
    • 0014235891 scopus 로고
    • The catalytic and regulatory properties of enzymes
    • Koshland, D. E., Jr., and Neet, K. E. (1968) The catalytic and regulatory properties of enzymes. Annu. Rev. Biochem. 37, 359-410
    • (1968) Annu. Rev. Biochem. , vol.37 , pp. 359-410
    • Koshland Jr., D.E.1    Neet, K.E.2
  • 110
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • Lomize, A. L., Pogozheva, I. D., Lomize, M. A., and Mosberg, H. I. (2007) The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct. Biol. 7, 44
    • (2007) BMC Struct. Biol. , vol.7 , pp. 44
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 111
    • 0036469888 scopus 로고    scopus 로고
    • Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains
    • Jäkel, S., Mingot, J. M., Schwarzmaier, P., Hartmann, E., and Görlich, D. (2002) Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains. EMBO J. 21, 377-386
    • (2002) EMBO J. , vol.21 , pp. 377-386
    • Jäkel, S.1    Mingot, J.M.2    Schwarzmaier, P.3    Hartmann, E.4    Görlich, D.5
  • 112
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou, H. X., Rivas, G., and Minton, A. P. (2008) Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 37, 375-397
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 113
    • 31344455700 scopus 로고    scopus 로고
    • From the trap to the basket: Getting to the bottom of the nuclear pore complex
    • DOI 10.1007/s00412-005-0037-1
    • Lim, R. Y., Aebi, U., and Stoffler, D. (2006) From the trap to the basket: Getting to the bottom of the nuclear pore complex. Chromosoma 115, 15-26 (Pubitemid 43138021)
    • (2006) Chromosoma , vol.115 , Issue.1 , pp. 15-26
    • Lim, R.Y.H.1    Aebi, U.2    Stoffler, D.3
  • 114
    • 35548946277 scopus 로고    scopus 로고
    • Nanomechanical basis of selective gating by the nuclear pore complex
    • DOI 10.1126/science.1145980
    • Lim, R. Y., Fahrenkrog, B., Köser, J., Schwarz-Herion, K., Deng, J., and Aebi, U. (2007) Nanomechanical basis of selective gating by the nuclear pore complex. Science 318, 640-643 (Pubitemid 350014836)
    • (2007) Science , vol.318 , Issue.5850 , pp. 640-643
    • Lim, R.Y.H.1    Fahrenkrog, B.2    Koser, J.3    Schwarz-Herion, K.4    Deng, J.5    Aebi, U.6
  • 115
    • 34447631998 scopus 로고    scopus 로고
    • Nanomechanical interactions of phenylalanine-glycine nucleoporins studied by single molecule force-volume spectroscopy
    • DOI 10.1016/j.jsb.2007.01.018, PII S1047847707000366
    • Lim, R. Y., Köser, J., Huang, N. P., Schwarz-Herion, K., and Aebi, U. (2007) Nanomechanical interactions of phenylalanine-glycine nucleoporins studied by single molecule force-volume spectroscopy. J. Struct. Biol. 159, 277-289 (Pubitemid 47095398)
    • (2007) Journal of Structural Biology , vol.159 , Issue.2 SPEC. ISS. , pp. 277-289
    • Lim, R.Y.H.1    Koser, J.2    Huang, N.-p.3    Schwarz-Herion, K.4    Aebi, U.5
  • 116
    • 70350630605 scopus 로고    scopus 로고
    • Interaction forces and reversible collapse of a polymer brush-gated nanopore
    • Lim, R. Y., and Deng, J. (2009) Interaction forces and reversible collapse of a polymer brush-gated nanopore. ACS Nano. 3, 2911-2918
    • (2009) ACS Nano. , vol.3 , pp. 2911-2918
    • Lim, R.Y.1    Deng, J.2
  • 117
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck, K., and Gö rlich, D. (2002) The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 21, 2664-2671
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 118
    • 17444427382 scopus 로고    scopus 로고
    • Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality
    • Peters, R. (2005) Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality. Traffic 6, 421-427
    • (2005) Traffic , vol.6 , pp. 421-427
    • Peters, R.1
  • 119
    • 77954613984 scopus 로고    scopus 로고
    • Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex
    • Peleg, O., and Lim, R. Y. (2010) Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex. Biol. Chem. 391, 719-730
    • (2010) Biol. Chem. , vol.391 , pp. 719-730
    • Peleg, O.1    Lim, R.Y.2
  • 120
    • 77952212806 scopus 로고    scopus 로고
    • Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots
    • Ma, J., and Yang, W. (2010) Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots. Proc. Natl. Acad. Sci. U.S.A. 107, 7305-7310
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7305-7310
    • Ma, J.1    Yang, W.2
  • 121
    • 62649117352 scopus 로고    scopus 로고
    • Effects of multiple occupancy and interparticle interactions on selective transport through narrow channels: Theory versus experiment
    • Zilman, A. (2009) Effects of multiple occupancy and interparticle interactions on selective transport through narrow channels: Theory versus experiment. Biophys. J. 96, 1235-1248
    • (2009) Biophys. J. , vol.96 , pp. 1235-1248
    • Zilman, A.1
  • 122
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • DOI 10.1016/S0955-0674(00)00213-1
    • Conti, E., and Izaurralde, E. (2001) Nucleocytoplasmic transport enters the atomic age. Curr. Opin. Cell Biol. 13, 310-319 (Pubitemid 32429495)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 124
    • 80052410893 scopus 로고    scopus 로고
    • The mechanism of nucleocytoplasmic transport through the nuclear pore complex
    • Tetenbaum-Novatt, J., and Rout, M. P. (2010) The mechanism of nucleocytoplasmic transport through the nuclear pore complex. Cold Spring Harbor Symp. Quant. Biol. 75, 567-584
    • (2010) Cold Spring Harbor Symp. Quant. Biol. , vol.75 , pp. 567-584
    • Tetenbaum-Novatt, J.1    Rout, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.