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Volumn 32, Issue 2, 2013, Pages 204-218

Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes

Author keywords

exportin; FG hydrogel; importin; nuclear pore complex; O glycosylation

Indexed keywords

GREEN FLUORESCENT PROTEIN; KARYOPHERIN; NUCLEOPORIN 98;

EID: 84872847336     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2012.302     Document Type: Article
Times cited : (163)

References (80)
  • 2
    • 25144453329 scopus 로고    scopus 로고
    • Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy
    • Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M (2005) Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J Am Chem Soc 127: 12965-12974
    • (2005) J Am Chem Soc , vol.127 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 3
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated betasheet structure for amyloid
    • Balbirnie M, Grothe R, Eisenberg DS (2001) An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated betasheet structure for amyloid. Proc Natl Acad Sci USA 98: 2375-2380
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 4
    • 33646720540 scopus 로고    scopus 로고
    • Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the throughbond connectivity
    • Baldus M, Meier BH (1996) Total correlation spectroscopy in the solid state. The use of scalar couplings to determine the throughbond connectivity. J Magn Reson A 121: 65-69
    • (1996) J Magn Reson A , vol.121 , pp. 65-69
    • Baldus, M.1    Meier, B.H.2
  • 5
    • 0030951880 scopus 로고    scopus 로고
    • Nup84, a novel nucleoporin that is associated with CAN/ Nup214 on the cytoplasmic face of the nuclear pore complex
    • Bastos R, Ribas de Pouplana L, Enarson M, Bodoor K, Burke B (1997) Nup84, a novel nucleoporin that is associated with CAN/ Nup214 on the cytoplasmic face of the nuclear pore complex. J Cell Biol 137: 989-1000
    • (1997) J Cell Biol , vol.137 , pp. 989-1000
    • Bastos, R.1    Ribas De Pouplana, L.2    Enarson, M.3    Bodoor, K.4    Burke, B.5
  • 6
    • 0032589798 scopus 로고    scopus 로고
    • Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP
    • Bayliss R, Ribbeck K, Akin D, Kent HM, Feldherr CM, Görlich D, Stewart M (1999) Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP. J Mol Biol 293: 579-593
    • (1999) J Mol Biol , vol.293 , pp. 579-593
    • Bayliss, R.1    Ribbeck, K.2    Akin, D.3    Kent, H.M.4    Feldherr, C.M.5    Görlich, D.6    Stewart, M.7
  • 7
    • 33745866215 scopus 로고    scopus 로고
    • Nup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear export
    • Bernad R, Engelsma D, Sanderson H, Pickersgill H, Fornerod M (2006) Nup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear export. J Biol Chem 281: 19378-19386
    • (2006) J Biol Chem , vol.281 , pp. 19378-19386
    • Bernad, R.1    Engelsma, D.2    Sanderson, H.3    Pickersgill, H.4    Fornerod, M.5
  • 8
    • 1542374020 scopus 로고    scopus 로고
    • Nup358/ RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1- mediated nuclear protein export
    • Bernad R, van der Velde H, Fornerod M, Pickersgill H (2004) Nup358/ RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1- mediated nuclear protein export. Mol Cell Biol 24: 2373-2384
    • (2004) Mol Cell Biol , vol.24 , pp. 2373-2384
    • Bernad, R.1    Van Der Velde, H.2    Fornerod, M.3    Pickersgill, H.4
  • 10
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)
    • Bullock TL, Clarkson WD, Kent HM, Stewart M (1996) The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2). J Mol Biol 260: 422-431
    • (1996) J Mol Biol , vol.260 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 11
    • 0029115837 scopus 로고
    • Sequence and characterization of cytoplasmic nuclear protein import factor p97
    • Chi NC, Adam EJ, Adam SA (1995) Sequence and characterization of cytoplasmic nuclear protein import factor p97. J Cell Biol 130: 265-274
    • (1995) J Cell Biol , vol.130 , pp. 265-274
    • Chi, N.C.1    Adam, E.J.2    Adam, S.A.3
  • 12
    • 33748454737 scopus 로고    scopus 로고
    • Using peptide arrays to define nuclear carrier binding sites on nucleoporins
    • Cushman I, Palzkill T, Moore MS (2006) Using peptide arrays to define nuclear carrier binding sites on nucleoporins. Methods 39: 329-341
    • (2006) Methods , vol.39 , pp. 329-341
    • Cushman, I.1    Palzkill, T.2    Moore, M.S.3
  • 13
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED, Glenner GG (1968) X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 16: 673-677
    • (1968) J Histochem Cytochem , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 14
    • 0032933745 scopus 로고    scopus 로고
    • Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis
    • Englmeier L, Olivo JC, Mattaj IW (1999) Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis. Curr Biol 9: 30-41
    • (1999) Curr Biol , vol.9 , pp. 30-41
    • Englmeier, L.1    Olivo, J.C.2    Mattaj, I.W.3
  • 15
    • 0000484499 scopus 로고
    • Hydrophobic parameters pi of aminoacid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere JL, Pliska V (1983) Hydrophobic parameters pi of aminoacid side chains from the partitioning of N-acetyl-amino-acid amides. Eur J Med Chem 18: 369-375
    • (1983) Eur J Med Chem , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 17
    • 0023293153 scopus 로고
    • Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores
    • Finlay DR, Newmeyer DD, Price TM, Forbes DJ (1987) Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J Cell Biol 104: 189-200
    • (1987) J Cell Biol , vol.104 , pp. 189-200
    • Finlay, D.R.1    Newmeyer, D.D.2    Price, T.M.3    Forbes, D.J.4
  • 18
    • 0031053791 scopus 로고    scopus 로고
    • The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88
    • Fornerod M, van Deursen J, van Baal S, Reynolds A, Davis D, Murti KG, Fransen J, Grosveld G (1997) The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J 16: 807-816
    • (1997) EMBO J , vol.16 , pp. 807-816
    • Fornerod, M.1    Van Deursen, J.2    Van Baal, S.3    Reynolds, A.4    Davis, D.5    Murti, K.G.6    Fransen, J.7    Grosveld, G.8
  • 19
    • 69849085462 scopus 로고    scopus 로고
    • FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties
    • Frey S, 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
  • 20
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey S, Görlich D (2007) A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130: 512-523
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Görlich, D.2
  • 21
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey S, Richter RP, Görlich D (2006) FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314: 815-817
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Görlich, D.3
  • 22
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried H, Kutay U (2003) Nucleocytoplasmic transport: taking an inventory. Cell Mol Life Sci 60: 1659-1688
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 23
    • 0033629304 scopus 로고    scopus 로고
    • An improved broadband decoupling sequence for liquid crystals and solids
    • Fung BM, Khitrin AK, Ermolaev K (2000) An improved broadband decoupling sequence for liquid crystals and solids. J Magn Reson 142: 97-101
    • (2000) J Magn Reson , vol.142 , pp. 97-101
    • Fung, B.M.1    Khitrin, A.K.2    Ermolaev, K.3
  • 24
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a neutral, cytosolic beta- N-acetylglucosaminidase from human brain
    • Gao Y, Wells L, Comer FI, Parker GJ, Hart GW (2001) Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta- N-acetylglucosaminidase from human brain. J Biol Chem 276: 9838-9845
    • (2001) J Biol Chem , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 25
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Görlich D, Kostka S, Kraft R, Dingwall C, Laskey RA, Hartmann E, Prehn S (1995) Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr Biol 5: 383-392
    • (1995) Curr Biol , vol.5 , pp. 383-392
    • Görlich, D.1    Kostka, S.2    Kraft, R.3    Dingwall, C.4    Laskey, R.A.5    Hartmann, E.6    Prehn, S.7
  • 26
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Görlich D, Pante N, Kutay U, Aebi U, Bischoff FR (1996) Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J 15: 5584-5594
    • (1996) EMBO J , vol.15 , pp. 5584-5594
    • Görlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 27
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Randriven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • Görlich D, Seewald MJ, Ribbeck K (2003) Characterization of Randriven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J 22: 1088-1100
    • (2003) EMBO J , vol.22 , pp. 1088-1100
    • Görlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 28
    • 0037323478 scopus 로고    scopus 로고
    • Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes
    • Griffis ER, Xu S, Powers MA (2003) Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes. Mol Biol Cell 14: 600-610
    • (2003) Mol Biol Cell , vol.14 , pp. 600-610
    • Griffis, E.R.1    Xu, S.2    Powers, M.A.3
  • 29
    • 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, Peters R (1995) Mapping of nucleoporins to the center of the nuclear pore complex by postembedding immunogold electron microscopy. J Cell Sci 108: 2963-2972
    • (1995) J Cell Sci , vol.108 , pp. 2963-2972
    • Grote, M.1    Kubitscheck, U.2    Reichelt, R.3    Peters, R.4
  • 30
    • 0028786983 scopus 로고
    • Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
    • Guan T, Muller S, Klier G, Pante N, Blevitt JM, Haner M, Paschal B, Aebi U, Gerace L (1995) Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol Biol Cell 6: 1591-1603
    • (1995) Mol Biol Cell , vol.6 , pp. 1591-1603
    • Guan, T.1    Muller, S.2    Klier, G.3    Pante, N.4    Blevitt, J.M.5    Haner, M.6    Paschal, B.7    Aebi, U.8    Gerace, L.9
  • 31
    • 80052230265 scopus 로고    scopus 로고
    • Ran-dependent nuclear export mediators: A structural perspective
    • Gü ttler T, Görlich D (2011) Ran-dependent nuclear export mediators: a structural perspective. EMBO J 30: 3457-3474
    • (2011) EMBO J , vol.30 , pp. 3457-3474
    • Güttler, T.1    Görlich, D.2
  • 34
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger RS, Holt GD, Hart GW (1990) Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase. J Biol Chem 265: 2563-2568
    • (1990) J Biol Chem , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 35
    • 0023655430 scopus 로고
    • O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins
    • Hanover JA, Cohen CK, Willingham MC, Park MK (1987) O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J Biol Chem 262: 9887-9894
    • (1987) J Biol Chem , vol.262 , pp. 9887-9894
    • Hanover, J.A.1    Cohen, C.K.2    Willingham, M.C.3    Park, M.K.4
  • 36
    • 71549126814 scopus 로고    scopus 로고
    • Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes
    • Hetzer MW, Wente SR (2009) Border control at the nucleus: biogenesis and organization of the nuclear membrane and pore complexes. Dev Cell 17: 606-616
    • (2009) Dev Cell , vol.17 , pp. 606-616
    • Hetzer, M.W.1    Wente, S.R.2
  • 37
    • 0036672039 scopus 로고    scopus 로고
    • The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98
    • Hodel AE, Hodel MR, Griffis ER, Hennig KA, Ratner GA, Xu S, Powers MA (2002) The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98. Mol Cell 10: 347-358
    • (2002) Mol Cell , vol.10 , pp. 347-358
    • Hodel, A.E.1    Hodel, M.R.2    Griffis, E.R.3    Hennig, K.A.4    Ratner, G.A.5    Xu, S.6    Powers, M.A.7
  • 38
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • Holt GD, Snow CM, Senior A, Haltiwanger RS, Gerace L, Hart GW (1987) Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol 104: 1157-1164
    • (1987) J Cell Biol , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3    Haltiwanger, R.S.4    Gerace, L.5    Hart, G.W.6
  • 39
    • 84865260520 scopus 로고    scopus 로고
    • The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model
    • Hülsmann BB, Labokha AA, Görlich D (2012) The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150: 738-751
    • (2012) Cell , vol.150 , pp. 738-751
    • Hülsmann, B.B.1    Labokha, A.A.2    Görlich, D.3
  • 40
    • 0024293481 scopus 로고
    • A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae
    • Hurt EC (1988) A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae. EMBO J 7: 4323-4434
    • (1988) EMBO J , vol.7 , pp. 4323-4434
    • Hurt, E.C.1
  • 41
    • 33748657386 scopus 로고    scopus 로고
    • Nup214 is required for CRM1- dependent nuclear protein export in vivo
    • Hutten S, Kehlenbach RH (2006) Nup214 is required for CRM1- dependent nuclear protein export in vivo. Mol Cell Biol 26: 6772-6785
    • (2006) Mol Cell Biol , vol.26 , pp. 6772-6785
    • Hutten, S.1    Kehlenbach, R.H.2
  • 43
    • 0029558543 scopus 로고
    • The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor
    • Iovine MK,Watkins JL,Wente SR (1995) The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J Cell Biol 131: 1699-1713
    • (1995) J Cell Biol , vol.131 , pp. 1699-1713
    • Iovine, M.K.1    Watkins, J.L.2    Wente, S.R.3
  • 44
    • 0030856315 scopus 로고    scopus 로고
    • The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
    • Izaurralde E, Kutay U, von Kobbe C, Mattaj IW, 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
    • (1997) EMBO J , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    Von Kobbe, C.3    Mattaj, I.W.4    Görlich, D.5
  • 45
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli
    • Kanemori M, Nishihara K, Yanagi H, Yura T (1997) Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol 179: 7219-7225
    • (1997) J Bacteriol , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 46
    • 0027979480 scopus 로고
    • The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm
    • Kraemer D, Wozniak RW, Blobel G, Radu A (1994) The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc Natl Acad Sci USA 91: 1519-1523
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1519-1523
    • Kraemer, D.1    Wozniak, R.W.2    Blobel, G.3    Radu, A.4
  • 47
    • 4344700329 scopus 로고    scopus 로고
    • Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket
    • Krull S, Thyberg J, Bjorkroth B, Rackwitz HR, Cordes VC (2004) Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. Mol Biol Cell 15: 4261-4277
    • (2004) Mol Biol Cell , vol.15 , pp. 4261-4277
    • Krull, S.1    Thyberg, J.2    Bjorkroth, B.3    Rackwitz, H.R.4    Cordes, V.C.5
  • 49
    • 1942455350 scopus 로고    scopus 로고
    • Metastable network model of protein transport through nuclear pores
    • Kustanovich T, Rabin Y (2004) Metastable network model of protein transport through nuclear pores. Biophys J 86: 2008-2016
    • (2004) Biophys J , vol.86 , pp. 2008-2016
    • Kustanovich, T.1    Rabin, Y.2
  • 50
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
    • Lubas WA, Hanover JA (2000) Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J Biol Chem 275: 10983-10988
    • (2000) J Biol Chem , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 51
    • 0034846331 scopus 로고    scopus 로고
    • Secondary chemical shifts in immobilized peptides and membrane proteins: A qualitative basis for structure refinement under magic angle spinning
    • Luca S, Filippov DV, van Boom JH, Oschkinat H, de Groot HJM, Baldus M (2001) Secondary chemical shifts in immobilized peptides and membrane proteins: a qualitative basis for structure refinement under magic angle spinning. J Biomol. NMR 20: 325-331
    • (2001) J Biomol. NMR , vol.20 , pp. 325-331
    • Luca, S.1    Filippov, D.V.2    Van Boom, J.H.3    Oschkinat, H.4    De Groot Hjm5    Baldus, M.6
  • 52
    • 80053353760 scopus 로고    scopus 로고
    • Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153
    • Milles S, Lemke EA (2011) Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153. Biophys J 101: 1710-1719
    • (2011) Biophys J , vol.101 , pp. 1710-1719
    • Milles, S.1    Lemke, E.A.2
  • 53
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr D, Frey S, Fischer T, Gü ttler T, Görlich D (2009) Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J 28: 2541-2553
    • (2009) EMBO J , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Güttler, T.4    Görlich, D.5
  • 54
    • 0141750584 scopus 로고    scopus 로고
    • Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats
    • Morrison J, Yang JC, Stewart M, Neuhaus D (2003) Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats. J Mol Biol 333: 587-603
    • (2003) J Mol Biol , vol.333 , pp. 587-603
    • Morrison, J.1    Yang, J.C.2    Stewart, M.3    Neuhaus, D.4
  • 55
    • 0016190847 scopus 로고
    • Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding
    • Nagata Y, Burger MM (1974) Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J Biol Chem 249: 3116-3122
    • (1974) J Biol Chem , vol.249 , pp. 3116-3122
    • Nagata, Y.1    Burger, M.M.2
  • 56
    • 27644495950 scopus 로고    scopus 로고
    • Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos
    • Onischenko EA, Gubanova NV, Kiseleva EV, Hallberg E (2005) Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos. Mol Biol Cell 16: 5152-5162
    • (2005) Mol Biol Cell , vol.16 , pp. 5152-5162
    • Onischenko, E.A.1    Gubanova, N.V.2    Kiseleva, E.V.3    Hallberg, E.4
  • 57
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel SS, Belmont BJ, Sante JM, Rexach MF (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129: 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
  • 58
    • 84862118405 scopus 로고    scopus 로고
    • Structural characterization of nanoscale meshworks within a nucleoporin FG hydrogel
    • Petri M, Frey S, Menzel A, Görlich D, Techert S (2012) Structural characterization of nanoscale meshworks within a nucleoporin FG hydrogel. Biomacromolecules 13: 1882-1889
    • (2012) Biomacromolecules , vol.13 , pp. 1882-1889
    • Petri, M.1    Frey, S.2    Menzel, A.3    Görlich, D.4    Techert, S.5
  • 59
    • 0028906840 scopus 로고
    • Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication
    • Powers MA, Macaulay C, Masiarz FR, Forbes DJ (1995) Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication. J Cell Biol 128: 721-736
    • (1995) J Cell Biol , vol.128 , pp. 721-736
    • Powers, M.A.1    MacAulay, C.2    Masiarz, F.R.3    Forbes, D.J.4
  • 60
    • 0344171991 scopus 로고    scopus 로고
    • RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains
    • Pritchard CE, Fornerod M, Kasper LH, van Deursen JM (1999) RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. J Cell Biol 145: 237-254
    • (1999) J Cell Biol , vol.145 , pp. 237-254
    • Pritchard, C.E.1    Fornerod, M.2    Kasper, L.H.3    Van Deursen, J.M.4
  • 61
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M, 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
  • 62
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K, Görlich D (2001) Kinetic analysis of translocation through nuclear pore complexes. EMBO J 20: 1320-1330
    • (2001) EMBO J , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Görlich, D.2
  • 63
    • 0032954291 scopus 로고    scopus 로고
    • The translocation of transportin-cargo complexes through nuclear pores is independent of both Ran and energy
    • Ribbeck K, Kutay U, Paraskeva E, Görlich D (1999) The translocation of transportin-cargo complexes through nuclear pores is independent of both Ran and energy. Curr Biol 9: 47-50
    • (1999) Curr Biol , vol.9 , pp. 47-50
    • Ribbeck, K.1    Kutay, U.2    Paraskeva, E.3    Görlich, D.4
  • 66
    • 0034397884 scopus 로고    scopus 로고
    • Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch
    • Rüdiger S, Mayer MP, Schneider-Mergener J, Bukau B (2000) Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. J Mol Biol 304: 245-251
    • (2000) J Mol Biol , vol.304 , pp. 245-251
    • Rüdiger, S.1    Mayer, M.P.2    Schneider-Mergener, J.3    Bukau, B.4
  • 67
    • 46849110978 scopus 로고    scopus 로고
    • MIRROR recoupling and its application to spin diffusion under fast magicangle spinning
    • Scholz I, Huber M, Manolikas T, Meier BH, Ernst M (2008) MIRROR recoupling and its application to spin diffusion under fast magicangle spinning. Chem Phys Lett 460: 278-283
    • (2008) Chem Phys Lett , vol.460 , pp. 278-283
    • Scholz, I.1    Huber, M.2    Manolikas, T.3    Meier, B.H.4    Ernst, M.5
  • 68
    • 0032567524 scopus 로고    scopus 로고
    • Randependent signal-mediated nuclear import does not require GTP hydrolysis by Ran
    • Schwoebel ED, Talcott B, Cushman I, Moore MS (1998) Randependent signal-mediated nuclear import does not require GTP hydrolysis by Ran. J Biol Chem 273: 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
  • 69
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka AJ, Barker PB, Freeman R (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64: 547-552
    • (1985) J Magn Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 70
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner N, Campbell R, Steinbach P, Giepmans B, Palmer A, Tsien R (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22: 1567-1572
    • (2004) Nat Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.1    Campbell, R.2    Steinbach, P.3    Giepmans, B.4    Palmer, A.5    Tsien, R.6
  • 71
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR (2004) Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol 6: 197-206
    • (2004) Nat Cell Biol , vol.6 , pp. 197-206
    • Strawn, L.A.1    Shen, T.2    Shulga, N.3    Goldfarb, D.S.4    Wente, S.R.5
  • 72
    • 0027458374 scopus 로고
    • A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm
    • Sukegawa J, Blobel G (1993) A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Cell 72: 29-38
    • (1993) Cell , vol.72 , pp. 29-38
    • Sukegawa, J.1    Blobel, G.2
  • 73
    • 0035851914 scopus 로고    scopus 로고
    • Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export
    • Vasu S, Shah S, Orjalo A, Park M, Fischer WH, Forbes DJ (2001) Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. J Cell Biol 155: 339-354
    • (2001) J Cell Biol , vol.155 , pp. 339-354
    • Vasu, S.1    Shah, S.2    Orjalo, A.3    Park, M.4    Fischer, W.H.5    Forbes, D.J.6
  • 74
    • 62049084648 scopus 로고    scopus 로고
    • The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner
    • von Moeller H, Basquin C, Conti E (2009) The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner. Nat Struct Mol Biol 16: 247-254
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 247-254
    • Von Moeller, H.1    Basquin, C.2    Conti, E.3
  • 75
    • 0033674629 scopus 로고    scopus 로고
    • The structural basis for red fluorescence in the tetrameric GFP homolog DsRed
    • Wall MA, Socolich M, Ranganathan R (2000) The structural basis for red fluorescence in the tetrameric GFP homolog DsRed. Nat Struct Biol 7: 1133-1138
    • (2000) Nat Struct Biol , vol.7 , pp. 1133-1138
    • Wall, M.A.1    Socolich, M.2    Ranganathan, R.3
  • 77
    • 9744266768 scopus 로고    scopus 로고
    • The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore
    • Weirich CS, Erzberger JP, Berger JM, Weis K (2004) The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Mol Cell 16: 749-760
    • (2004) Mol Cell , vol.16 , pp. 749-760
    • Weirich, C.S.1    Erzberger, J.P.2    Berger, J.M.3    Weis, K.4
  • 78
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L, Vosseller K, Cole RN, Cronshaw JM, Matunis MJ, Hart GW (2002) Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol Cell Proteomics 1: 791-804
    • (2002) Mol Cell Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 80
    • 4444284306 scopus 로고    scopus 로고
    • Imaging of single-molecule translocation through nuclear pore complexes
    • Yang W, Gelles J, Musser SM (2004) Imaging of single-molecule translocation through nuclear pore complexes. Proc Natl Acad Sci USA 101: 12887-12892
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12887-12892
    • Yang, W.1    Gelles, J.2    Musser, S.M.3


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