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Volumn 1793, Issue 10, 2009, Pages 1533-1539

Functionalization of a nanopore: The nuclear pore complex paradigm

Author keywords

Intrinsically disordered protein; Membrane transport; Nanopore; Nuclear pore complex; Reduction of dimensionality

Indexed keywords

PHENYLALANYLGLYCINE;

EID: 69949094947     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.06.003     Document Type: Review
Times cited : (24)

References (117)
  • 1
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • Rich A., and Davidson N. (Eds), W.H. Freeman & Co., New York
    • Adam G., and Delbrück M. Reduction of dimensionality in biological diffusion processes. In: Rich A., and Davidson N. (Eds). Structural Chemistry and Molecular Biology (1968), W.H. Freeman & Co., New York 198-215
    • (1968) Structural Chemistry and Molecular Biology , pp. 198-215
    • Adam, G.1    Delbrück, M.2
  • 2
    • 0025180782 scopus 로고
    • Visualization of transport-related configurations of the nuclear-pore transporter
    • Akey C.W. Visualization of transport-related configurations of the nuclear-pore transporter. Biophys. J. 58 (1990) 341-355
    • (1990) Biophys. J. , vol.58 , pp. 341-355
    • Akey, C.W.1
  • 5
    • 0034208665 scopus 로고    scopus 로고
    • The molecular mechanism of transport of macromolecules through nuclear pore complexes
    • Bayliss R., Corbett A.H., and Stewart M. The molecular mechanism of transport of macromolecules through nuclear pore complexes. Traffic 1 (2000) 448-456
    • (2000) Traffic , vol.1 , pp. 448-456
    • Bayliss, R.1    Corbett, A.H.2    Stewart, M.3
  • 6
    • 0037124352 scopus 로고    scopus 로고
    • Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats
    • Bayliss R., Leung S.W., Baker R.P., Quimby B.B., Corbett A.H., and Stewart M. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. EMBO J. 21 (2002) 2843-2853
    • (2002) EMBO J. , vol.21 , 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
  • 7
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • Bayliss R., Littlewood T., and Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell 102 (2000) 99-108
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 8
    • 0037184968 scopus 로고    scopus 로고
    • GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta
    • Bayliss R., Littlewood T., Strawn L.A., Wente S.R., and Stewart M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. J. Biol. Chem. 277 (2002) 50597-50606
    • (2002) J. Biol. Chem. , vol.277 , pp. 50597-50606
    • Bayliss, R.1    Littlewood, T.2    Strawn, L.A.3    Wente, S.R.4    Stewart, M.5
  • 9
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Forster F., Baumeister W., and Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 449 (2007) 611-615
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 10
    • 0041731883 scopus 로고    scopus 로고
    • Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • Bednenko J., Cingolani G., and Gerace L. Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport. J. Cell Biol. 162 (2003) 391-401
    • (2003) J. Cell Biol. , vol.162 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 11
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import
    • Ben-Efraim I., and Gerace L. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J. Cell Biol. 152 (2001) 411-417
    • (2001) J. Cell Biol. , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 13
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • Berg H.C., and Purcell E.M. Physics of chemoreception. Biophys. J. 20 (1977) 193-219
    • (1977) Biophys. J. , vol.20 , pp. 193-219
    • Berg, H.C.1    Purcell, E.M.2
  • 15
    • 0036924053 scopus 로고    scopus 로고
    • The nuclear pore complex mystery and anomalous diffusion in reversible gels
    • Bickel T., and Bruinsma R. The nuclear pore complex mystery and anomalous diffusion in reversible gels. Biophys. J. 83 (2002) 3079-3087
    • (2002) Biophys. J. , vol.83 , pp. 3079-3087
    • Bickel, T.1    Bruinsma, R.2
  • 16
    • 44949171609 scopus 로고    scopus 로고
    • Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex
    • Boehmer T., Jeudy S., Berke I.C., and Schwartz T.U. Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Mol. Cell 30 (2008) 721-731
    • (2008) Mol. Cell , vol.30 , pp. 721-731
    • Boehmer, T.1    Jeudy, S.2    Berke, I.C.3    Schwartz, T.U.4
  • 17
    • 34548445598 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex
    • Boehmer T., and Schwartz T.U. Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 63 (2007) 816-818
    • (2007) Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. , vol.63 , pp. 816-818
    • Boehmer, T.1    Schwartz, T.U.2
  • 19
    • 58149288627 scopus 로고    scopus 로고
    • Synthetic mimic of selective transport through the nuclear pore complex
    • Y. Caspi, D. Zbaida, H. Cohen, and M. Elbaum, Synthetic mimic of selective transport through the nuclear pore complex, Nano Lett. 8 (2008) 3728--3734.
    • (2008) Nano Lett , vol.8 , pp. 3728-3734
    • Caspi, Y.1    Zbaida, D.2    Cohen, H.3    Elbaum, M.4
  • 20
    • 0034007087 scopus 로고    scopus 로고
    • Dissecting the interactions between NTF2, RanGDP, and the nucleoporin XFXFG repeats
    • Chaillan-Huntington C., Braslavsky C.V., Kuhlmann J., and Stewart M. Dissecting the interactions between NTF2, RanGDP, and the nucleoporin XFXFG repeats. J. Biol. Chem. 275 (2000) 5874-5879
    • (2000) J. Biol. Chem. , vol.275 , pp. 5874-5879
    • Chaillan-Huntington, C.1    Braslavsky, C.V.2    Kuhlmann, J.3    Stewart, M.4
  • 22
    • 69949105732 scopus 로고    scopus 로고
    • A.V. Chechkin, I.M. Zaid, M.A. Lomholt, I.M. Sokolov, and R. Metzler, Bulk-mediated surface diffusion on a cylinder: propagators and crossovers, ArXiv:0812. 3627v1 [Cond-Mat. Stat-Mech] (2009).
    • A.V. Chechkin, I.M. Zaid, M.A. Lomholt, I.M. Sokolov, and R. Metzler, Bulk-mediated surface diffusion on a cylinder: propagators and crossovers, ArXiv:0812. 3627v1 [Cond-Mat. Stat-Mech] (2009).
  • 23
    • 0030910804 scopus 로고    scopus 로고
    • Functional domains in nuclear import factor p97 for binding the nuclear localization sequence receptor and the nuclear pore
    • Chi N.C., and Adam S.A. Functional domains in nuclear import factor p97 for binding the nuclear localization sequence receptor and the nuclear pore. Mol. Biol. Cell 8 (1997) 945-956
    • (1997) Mol. Biol. Cell , vol.8 , pp. 945-956
    • Chi, N.C.1    Adam, S.A.2
  • 25
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A., Bono F., Jinek M., and Conti E. Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76 (2007) 647-671
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 27
    • 0347990552 scopus 로고    scopus 로고
    • The dynamic association of RCC1 with chromatin is modulated by Ran-dependent nuclear transport
    • Cushman I., Stenoien D., and Moore M.S. The dynamic association of RCC1 with chromatin is modulated by Ran-dependent nuclear transport. Mol. Biol. Cell 15 (2004) 245-255
    • (2004) Mol. Biol. Cell , vol.15 , pp. 245-255
    • Cushman, I.1    Stenoien, D.2    Moore, M.S.3
  • 28
    • 53749102019 scopus 로고    scopus 로고
    • Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study
    • Dange T., Grunwald D., Grunwald A., Peters R., and Kubitscheck U. Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study. J. Cell Biol. 183 (2008) 77-86
    • (2008) J. Cell Biol. , vol.183 , pp. 77-86
    • Dange, T.1    Grunwald, D.2    Grunwald, A.3    Peters, R.4    Kubitscheck, U.5
  • 30
    • 0019018575 scopus 로고
    • The biophysics of ligand-receptor interactions
    • Delisi C. The biophysics of ligand-receptor interactions. Q. Rev. Biophys. 13 (1980) 201-230
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 201-230
    • Delisi, C.1
  • 31
    • 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., and Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 2450-2455
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 32
    • 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., and Rexach M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 277 (2002) 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
  • 34
    • 0032933745 scopus 로고    scopus 로고
    • Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis
    • Englmeier L., Olivo J.C., and Mattaj I.W. Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis. Curr. Biol. 9 (1999) 30-41
    • (1999) Curr. Biol. , vol.9 , pp. 30-41
    • Englmeier, L.1    Olivo, J.C.2    Mattaj, I.W.3
  • 35
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: nucleocytoplasmic transport and beyond
    • Fahrenkrog B., and Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat. Rev., Mol. Cell Biol. 4 (2003) 757-766
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 36
    • 1842813943 scopus 로고    scopus 로고
    • The nuclear pore complex: a jack of all trades?
    • Fahrenkrog B., Koser J., and Aebi U. The nuclear pore complex: a jack of all trades?. Trends Biochem. Sci. 29 (2004) 175-182
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 175-182
    • Fahrenkrog, B.1    Koser, J.2    Aebi, U.3
  • 37
    • 0031454975 scopus 로고    scopus 로고
    • The location of the transport gate in the nuclear pore complex
    • Feldherr C.M., and Akin D. The location of the transport gate in the nuclear pore complex. J. Cell Sci. 110 (1997) 3065-3070
    • (1997) J. Cell Sci. , vol.110 , pp. 3065-3070
    • Feldherr, C.M.1    Akin, D.2
  • 38
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink A.L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 15 (2005) 35-41
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 40
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey S., and Gorlich D. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130 (2007) 512-523
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Gorlich, D.2
  • 41
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey S., Richter R.P., and Gorlich D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314 (2006) 815-817
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Gorlich, D.3
  • 42
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich D., and Mattaj I.W. Nucleocytoplasmic transport. Science 271 (1996) 1513-1518
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 43
    • 49449107340 scopus 로고    scopus 로고
    • Visualizing one-dimensional diffusion of proteins along DNA
    • Gorman J., and Greene E.C. Visualizing one-dimensional diffusion of proteins along DNA. Nat. Struct. Mol. Biol. 15 (2008) 768-774
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 768-774
    • Gorman, J.1    Greene, E.C.2
  • 45
    • 0029118089 scopus 로고
    • Mapping of nucleoporins to the center of the nuclear-pore complex by postembedding immunogold electron-microscopy
    • Grote M., Kubitscheck U., Reichelt R., and Peters R. Mapping of nucleoporins to the center of the nuclear-pore complex by postembedding immunogold electron-microscopy. J. Cell Sci. 108 (1995) 2963-2972
    • (1995) J. Cell Sci. , vol.108 , pp. 2963-2972
    • Grote, M.1    Kubitscheck, U.2    Reichelt, R.3    Peters, R.4
  • 46
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford S.E., and Marko J.F. How do site-specific DNA-binding proteins find their targets?. Nucleic Acids Res. 32 (2004) 3040-3052
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 47
    • 37349098658 scopus 로고    scopus 로고
    • Molecular sieving using nanofilters: past, present and future
    • Han J.Y., Fu J.P., and Schoch R.B. Molecular sieving using nanofilters: past, present and future. Lab Chip 8 (2008) 23-33
    • (2008) Lab Chip , vol.8 , pp. 23-33
    • Han, J.Y.1    Fu, J.P.2    Schoch, R.B.3
  • 49
    • 37349009269 scopus 로고    scopus 로고
    • Architecture of a coat for the nuclear pore membrane
    • Hsia K.C., Stavropoulos P., Blobel G., and Hoelz A. Architecture of a coat for the nuclear pore membrane. Cell 131 (2007) 1313-1326
    • (2007) Cell , vol.131 , pp. 1313-1326
    • Hsia, K.C.1    Stavropoulos, P.2    Blobel, G.3    Hoelz, A.4
  • 50
    • 0020647920 scopus 로고
    • Functional-significance of flexibility in proteins
    • Huber R., and Bennett W.S. Functional-significance of flexibility in proteins. Biopolymers 22 (1983) 261-279
    • (1983) Biopolymers , vol.22 , pp. 261-279
    • Huber, R.1    Bennett, W.S.2
  • 51
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-beta
    • Isgro T.A., and Schulten K. Binding dynamics of isolated nucleoporin repeat regions to importin-beta. Structure 13 (2005) 1869-1879
    • (2005) Structure , vol.13 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 52
    • 34547657392 scopus 로고    scopus 로고
    • Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors
    • Isgro T.A., and Schulten K. Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors. Structure 15 (2007) 977-991
    • (2007) Structure , vol.15 , pp. 977-991
    • Isgro, T.A.1    Schulten, K.2
  • 53
    • 36849079742 scopus 로고    scopus 로고
    • Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture
    • Jeudy S., and Schwartz T.U. Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture. J. Biol. Chem. 282 (2007) 34904-34912
    • (2007) J. Biol. Chem. , vol.282 , pp. 34904-34912
    • Jeudy, S.1    Schwartz, T.U.2
  • 55
    • 0032974756 scopus 로고    scopus 로고
    • Permeability of single nuclear pores
    • Keminer O., and Peters R. Permeability of single nuclear pores. Biophys. J. 77 (1999) 217-228
    • (1999) Biophys. J. , vol.77 , pp. 217-228
    • Keminer, O.1    Peters, R.2
  • 56
    • 0031907210 scopus 로고    scopus 로고
    • Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNP export
    • Kiseleva E., Goldberg M.W., Allen T.D., and Akey C.W. Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNP export. J. Cell Sci. 111 (1998) 223-236
    • (1998) J. Cell Sci. , vol.111 , pp. 223-236
    • Kiseleva, E.1    Goldberg, M.W.2    Allen, T.D.3    Akey, C.W.4
  • 57
    • 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. Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex. J. Cell Biol. 139 (1997) 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
  • 58
    • 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. Intramolecular cohesion of coils mediated by phenylalanine-glycine motifs in the natively unfolded domain of a nucleoporin. PLoS Comput. Biol. 4 (2008) 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
  • 60
    • 40749104851 scopus 로고    scopus 로고
    • Chromatin dynamics and gene positioning
    • Kumaran R.I., Thakar R., and Spector D.L. Chromatin dynamics and gene positioning. Cell Cell 132 (2008) 929-934
    • (2008) Cell Cell , vol.132 , pp. 929-934
    • Kumaran, R.I.1    Thakar, R.2    Spector, D.L.3
  • 61
    • 1942455350 scopus 로고    scopus 로고
    • Metastable network model of protein transport through nuclear pores
    • Kustanovich T., and Rabin Y. Metastable network model of protein transport through nuclear pores. Biophys. J. 86 (2004) 2008-2016
    • (2004) Biophys. J. , vol.86 , pp. 2008-2016
    • Kustanovich, T.1    Rabin, Y.2
  • 62
    • 0030960586 scopus 로고    scopus 로고
    • Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex
    • Kutay U., Izaurralde E., Bischoff F.R., Mattaj I.W., and Gorlich D. Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. EMBO J. 16 (1997) 1153-1163
    • (1997) EMBO J. , vol.16 , pp. 1153-1163
    • Kutay, U.1    Izaurralde, E.2    Bischoff, F.R.3    Mattaj, I.W.4    Gorlich, D.5
  • 63
    • 39149125768 scopus 로고    scopus 로고
    • Towards reconciling structure and function in the nuclear pore complex
    • Lim R.Y., Aebi U., and Fahrenkrog B. Towards reconciling structure and function in the nuclear pore complex. Histochem. Cell Biol. 129 (2008) 105-116
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 105-116
    • Lim, R.Y.1    Aebi, U.2    Fahrenkrog, B.3
  • 64
  • 65
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara I.G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65 (2001) 570-594
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 66
    • 34547106022 scopus 로고    scopus 로고
    • Learning nature's way: biosensing with synthetic nanopores
    • Martin C.R., and Siwy Z.S. Learning nature's way: biosensing with synthetic nanopores. Science 317 (2007) 331-332
    • (2007) Science , vol.317 , pp. 331-332
    • Martin, C.R.1    Siwy, Z.S.2
  • 67
    • 0017636049 scopus 로고
    • The nuclear and cytoplasmic pore complex: structure, dynamics, distribution, and evolution.
    • Maul G.G. The nuclear and cytoplasmic pore complex: structure, dynamics, distribution, and evolution. Int. Rev. Cytol. Suppl. 6 (1977) 76-187
    • (1977) Int. Rev. Cytol. Suppl. , vol.6 , pp. 76-187
    • Maul, G.G.1
  • 68
    • 34047159864 scopus 로고    scopus 로고
    • Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding
    • Melcak I., Hoelz A., and Blobel G. Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding. Science 315 (2007) 1729-1732
    • (2007) Science , vol.315 , pp. 1729-1732
    • Melcak, I.1    Hoelz, A.2    Blobel, G.3
  • 69
    • 0141750584 scopus 로고    scopus 로고
    • Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats
    • Morrison J., Yang J.C., Stewart M., and Neuhaus D. Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats. J. Mol. Biol. 333 (2003) 587-603
    • (2003) J. Mol. Biol. , vol.333 , pp. 587-603
    • Morrison, J.1    Yang, J.C.2    Stewart, M.3    Neuhaus, D.4
  • 70
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: from nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast N., and Pemberton L.F. Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14 (2004) 547-556
    • (2004) Trends Cell Biol. , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 71
    • 33846906150 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN
    • Napetschnig J., Blobel G., and Hoelz A. Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 1783-1788
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 1783-1788
    • Napetschnig, J.1    Blobel, G.2    Hoelz, A.3
  • 72
    • 0016652057 scopus 로고
    • Nuclear envelope permeability
    • Paine P.L., Moore L.C., and Horowitz S.B. Nuclear envelope permeability. Nature 254 (1975) 109-114
    • (1975) Nature , vol.254 , pp. 109-114
    • Paine, P.L.1    Moore, L.C.2    Horowitz, S.B.3
  • 73
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of similar to 39 nm
    • Pante N., and Kann M. Nuclear pore complex is able to transport macromolecules with diameters of similar to 39 nm. Mol. Biol. Cell 13 (2002) 425-434
    • (2002) Mol. Biol. Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 74
    • 33751407500 scopus 로고    scopus 로고
    • Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy
    • Paradise A., Levin M.K., Korza G., and Carson J.H. Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy. J. Mol. Biol. 365 (2007) 50-65
    • (2007) J. Mol. Biol. , vol.365 , pp. 50-65
    • Paradise, A.1    Levin, M.K.2    Korza, G.3    Carson, J.H.4
  • 75
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel S.S., Belmont B.J., Sante J.M., and Rexach M.F. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129 (2007) 83-96
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 76
    • 0021100162 scopus 로고
    • Nuclear envelope permeability measured by fluorescence microphotolysis of single liver cell nuclei
    • Peters R. Nuclear envelope permeability measured by fluorescence microphotolysis of single liver cell nuclei. J. Biol. Chem. 258 (1983) 11427-11429
    • (1983) J. Biol. Chem. , vol.258 , pp. 11427-11429
    • Peters, R.1
  • 77
    • 0042855028 scopus 로고    scopus 로고
    • Optical single transporter recording: transport kinetics in microarrays of membrane patches
    • Peters R. Optical single transporter recording: transport kinetics in microarrays of membrane patches. Annu. Rev. Biophys. Biomol. Struct. 32 (2003) 47-67
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 47-67
    • Peters, R.1
  • 78
    • 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 6 (2005) 421-427
    • (2005) Traffic , vol.6 , pp. 421-427
    • Peters, R.1
  • 79
    • 34347243476 scopus 로고    scopus 로고
    • Single-molecule fluorescence analysis of cellular nanomachinery components
    • Peters R. Single-molecule fluorescence analysis of cellular nanomachinery components. Annu. Rev. Biophys. Biomol. Struct. 36 (2007) 371-394
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 371-394
    • Peters, R.1
  • 80
    • 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 31 (2009) 466-477
    • (2009) Bioessays , vol.31 , pp. 466-477
    • Peters, R.1
  • 81
    • 0142180053 scopus 로고    scopus 로고
    • A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex
    • Pyhtila B., and Rexach M. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J. Biol. Chem. 278 (2003) 42699-42709
    • (2003) J. Biol. Chem. , vol.278 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 82
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • 1114-1U27
    • Rabut G., Doye V., and Ellenberg J. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat. Cell Biol. 6 (2004) 1114-1U27
    • (2004) Nat. Cell Biol. , vol.6
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 83
    • 0025247954 scopus 로고
    • Correlation between structure and mass-distribution of the nuclear-pore complex and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E.L., Jarnik M., Engel A., and Aebi U. Correlation between structure and mass-distribution of the nuclear-pore complex and of distinct pore complex components. J. Cell Biol. 110 (1990) 883-894
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 84
    • 0028834428 scopus 로고
    • Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M., and Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83 (1995) 683-692
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 85
    • 65449152773 scopus 로고    scopus 로고
    • Molecular interactions at the nuclear pore complex and the mechanics of karyopherin movement
    • Rexach M.F., Allen N., Mykytka B., Huang L., Burlingame A., and Gilchrist D. Molecular interactions at the nuclear pore complex and the mechanics of karyopherin movement. FASEB J. 16 (2002) A892
    • (2002) FASEB J. , vol.16
    • Rexach, M.F.1    Allen, N.2    Mykytka, B.3    Huang, L.4    Burlingame, A.5    Gilchrist, D.6
  • 86
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K., and Gorlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20 (2001) 1320-1330
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 87
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck K., and Gorlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 21 (2002) 2664-2671
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 88
    • 0014945567 scopus 로고
    • The lac repressor-operator interaction. 3. Kinetic studies
    • Riggs A.D., Bourgeois S., and Cohn M. The lac repressor-operator interaction. 3. Kinetic studies. J. Mol. Biol. 53 (1970) 401-417
    • (1970) J. Mol. Biol. , vol.53 , pp. 401-417
    • Riggs, A.D.1    Bourgeois, S.2    Cohn, M.3
  • 89
    • 0035907248 scopus 로고    scopus 로고
    • The nuclear pore complex as a transport machine
    • Rout M.P., and Aitchison J.D. The nuclear pore complex as a transport machine. J. Biol. Chem. 276 (2001) 16593-16596
    • (2001) J. Biol. Chem. , vol.276 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 90
    • 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. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148 (2000) 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
  • 93
    • 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. Structural basis of the nic96 subcomplex organization in the nuclear pore channel. Mol. Cell 29 (2008) 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
  • 94
    • 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. Opin. Struct. Biol. 15 (2005) 221-226
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 221-226
    • Schwartz, T.U.1
  • 95
    • 0032567524 scopus 로고    scopus 로고
    • Ran-dependent signal-mediated nuclear import does not require GTP hydrolysis by Ran
    • Schwoebel E.D., Talcott B., Cushman I., and Moore M.S. Ran-dependent signal-mediated nuclear import does not require GTP hydrolysis by Ran. J. Biol. Chem. 273 (1998) 35170-35175
    • (1998) J. Biol. Chem. , vol.273 , pp. 35170-35175
    • Schwoebel, E.D.1    Talcott, B.2    Cushman, I.3    Moore, M.S.4
  • 96
    • 49649106438 scopus 로고    scopus 로고
    • A mechanism for asymmetric segregation of age during yeast budding
    • 728-U64
    • Shcheprova Z., Baldi S., Frei S.B., Gonnet G., and Barral Y. A mechanism for asymmetric segregation of age during yeast budding. Nature 454 (2008) 728-U64
    • (2008) Nature , vol.454
    • Shcheprova, Z.1    Baldi, S.2    Frei, S.B.3    Gonnet, G.4    Barral, Y.5
  • 97
    • 0034729194 scopus 로고    scopus 로고
    • Yeast nucleoporins involved in passive nuclear envelope permeability
    • Shulga N., Mosammaparast N., Wozniak R., and Goldfarb D.S. Yeast nucleoporins involved in passive nuclear envelope permeability. J. Cell Biol. 149 (2000) 1027-1038
    • (2000) J. Cell Biol. , vol.149 , pp. 1027-1038
    • Shulga, N.1    Mosammaparast, N.2    Wozniak, R.3    Goldfarb, D.S.4
  • 98
    • 0036748289 scopus 로고    scopus 로고
    • Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes
    • Siebrasse J.P., and Peters R. Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes. EMBO Rep. 3 (2002) 887-892
    • (2002) EMBO Rep. , vol.3 , pp. 887-892
    • Siebrasse, J.P.1    Peters, R.2
  • 99
    • 10044223573 scopus 로고    scopus 로고
    • Kinetics of protein-DNA interaction: facilitated target location in sequence-dependent potential
    • Slutsky M., and Mirny L.A. Kinetics of protein-DNA interaction: facilitated target location in sequence-dependent potential. Biophys. J. 87 (2004) 4021-4035
    • (2004) Biophys. J. , vol.87 , pp. 4021-4035
    • Slutsky, M.1    Mirny, L.A.2
  • 100
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart M. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8 (2007) 195-208
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 101
    • 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., and Aebi U. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 328 (2003) 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
  • 102
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., and Wente S.R. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat. Cell Biol. 6 (2004) 197-206
    • (2004) Nat. Cell Biol. , vol.6 , pp. 197-206
    • Strawn, L.A.1    Shen, T.X.2    Shulga, N.3    Goldfarb, D.S.4    Wente, S.R.5
  • 103
    • 39549091070 scopus 로고    scopus 로고
    • Structural constraints on autoprocessing of the human nucleoporin Nup98
    • Sun Y., and Guo H.C. Structural constraints on autoprocessing of the human nucleoporin Nup98. Protein Sci. 17 (2008) 494-505
    • (2008) Protein Sci. , vol.17 , pp. 494-505
    • Sun, Y.1    Guo, H.C.2
  • 104
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport
    • Terry L.J., Shows E.B., and Wente S.R. Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science 318 (2007) 1412-1416
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 105
    • 0031051658 scopus 로고    scopus 로고
    • Equilibrium, kinetics, diffusion and self-association of proteins at membrane surfaces: measurement by total internal reflection fluorescence microscopy
    • Thompson N.L., Drake A.W., Chen L., and Vanden B.W. Equilibrium, kinetics, diffusion and self-association of proteins at membrane surfaces: measurement by total internal reflection fluorescence microscopy. Photochem. Photobiol. 65 (1997) 39-46
    • (1997) Photochem. Photobiol. , vol.65 , pp. 39-46
    • Thompson, N.L.1    Drake, A.W.2    Chen, L.3    Vanden, B.W.4
  • 106
    • 38749118235 scopus 로고    scopus 로고
    • Highly inclined thin illumination enables clear single-molecule imaging in cells
    • Tokunaga M., Imamoto N., and Sakata-Sogawa K. Highly inclined thin illumination enables clear single-molecule imaging in cells. Nat. Methods 5 (2008) 159-161
    • (2008) Nat. Methods , vol.5 , pp. 159-161
    • Tokunaga, M.1    Imamoto, N.2    Sakata-Sogawa, K.3
  • 107
    • 0031789950 scopus 로고    scopus 로고
    • An optical method for recording the activity of single transporters in membrane patches
    • Tschodrich-Rotter M., and Peters R. An optical method for recording the activity of single transporters in membrane patches. J. Microsc. 192 (1998) 114-125
    • (1998) J. Microsc. , vol.192 , pp. 114-125
    • Tschodrich-Rotter, M.1    Peters, R.2
  • 108
    • 0020472010 scopus 로고
    • A large particle associated with the perimeter of the nuclear-pore complex
    • Unwin P.N.T., and Milligan R.A. A large particle associated with the perimeter of the nuclear-pore complex. J. Cell Biol. 93 (1982) 63-75
    • (1982) J. Cell Biol. , vol.93 , pp. 63-75
    • Unwin, P.N.T.1    Milligan, R.A.2
  • 109
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins-Struct. Funct. Genet. 41 (2000) 415-427
    • (2000) Proteins-Struct. Funct. Genet. , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 110
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337 (2004) 635-645
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 112
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 113
    • 0038342167 scopus 로고    scopus 로고
    • Mobility of adsorbed proteins studied by fluorescence recovery after photobleaching
    • Yuan Y.H., Velev O.D., and Lenhoff A.M. Mobility of adsorbed proteins studied by fluorescence recovery after photobleaching. Langmuir 19 (2003) 3705-3711
    • (2003) Langmuir , vol.19 , pp. 3705-3711
    • Yuan, Y.H.1    Velev, O.D.2    Lenhoff, A.M.3
  • 114
    • 9444254054 scopus 로고    scopus 로고
    • The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo
    • Zeitler B., and Weis K. The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo. J. Cell Biol. 167 (2004) 583-590
    • (2004) J. Cell Biol. , vol.167 , pp. 583-590
    • Zeitler, B.1    Weis, K.2
  • 115
    • 62649117352 scopus 로고    scopus 로고
    • Effects of multiple occupancy and interparticle interactions on selective transport through narrow channels: theory versus experiment
    • Zilman A. Effects of multiple occupancy and interparticle interactions on selective transport through narrow channels: theory versus experiment. Biophys. J. 96 (2009) 1235-1248
    • (2009) Biophys. J. , vol.96 , pp. 1235-1248
    • Zilman, A.1


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