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Volumn 98, Issue 11, 2010, Pages 2653-2661

Hydrophilic linkers and polar contacts affect aggregation of FG repeat peptides

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EID: 77953017595     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.02.049     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P., J. D. Aitchison, ..., B. T. Chait. 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    Chait, B.T.3
  • 2
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic nuclear pore complexes: Life on the edge
    • Tran, E. J., and S. R. Wente. 2006. Dynamic nuclear pore complexes: life on the edge. Cell. 125:1041-1053.
    • (2006) Cell. , vol.125 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 3
    • 8844226004 scopus 로고    scopus 로고
    • Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    • Beck, M., F. Förster, ..., O. Medalia. 2004. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science. 306:1387-1390.
    • (2004) Science , vol.306 , pp. 1387-1390
    • Beck, M.1    Förster, F.2    Medalia, O.3
  • 4
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck, M., V. Lucie, ..., O. Medalia. 2007. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature. 449:611-615.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucie, V.2    Medalia, O.3
  • 5
    • 36749045172 scopus 로고    scopus 로고
    • The molecular architecture of the nuclear pore complex
    • Alber, F., S. Dokudovskaya, ..., M. P. Rout. 2007. The molecular architecture of the nuclear pore complex. Nature. 450:695-701.
    • (2007) Nature , vol.450 , pp. 695-701
    • Alber, F.1    Dokudovskaya, S.2    Rout, M.P.3
  • 6
    • 69849083412 scopus 로고    scopus 로고
    • The nuclear pore complex has entered the atomic age
    • Brohawn, S. G., J. R. Partridge, ..., T. U. Schwartz. 2009. The nuclear pore complex has entered the atomic age. Structure. 17: 1156-1168.
    • (2009) Structure , vol.17 , pp. 1156-1168
    • Brohawn, S.G.1    Partridge, J.R.2    Schwartz, T.U.3
  • 7
    • 48949106029 scopus 로고    scopus 로고
    • Biology and biophysics of the nuclear pore complex and its components
    • Lim, R. Y. H., K. S. Ullman, and B. Fahrenkrog. 2008. Biology and biophysics of the nuclear pore complex and its components. Int. Rev. Cell Mol. Biol. 267:299-342.
    • (2008) Int. Rev. Cell Mol. Biol. , vol.267 , pp. 299-342
    • Lim, R.Y.H.1    Ullman, K.S.2    Fahrenkrog, B.3
  • 8
    • 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
  • 9
    • 0012186454 scopus 로고    scopus 로고
    • Deciphering networks of protein interactions at the nuclear pore complex
    • Allen, N. P. C., S. S. Patel, ..., M. Rexach. 2002. Deciphering networks of protein interactions at the nuclear pore complex. Mol. Cell. Proteomics. 1:930-946.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 930-946
    • Allen, N.P.C.1    Patel, S.S.2    Rexach, M.3
  • 10
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel, S. S., B. J. Belmont, ..., M. F. Rexach. 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    Rexach, M.F.3
  • 11
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • Denning, D. P., S. S. Patel, ..., M. Rexach. 2003. Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded. Proc. Natl. Acad. Sci. USA. 100:2450-2455.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Rexach, M.3
  • 12
    • 0034208665 scopus 로고    scopus 로고
    • The molecular mechanism of transport of macromolecules through nuclear pore complexes
    • Bayliss, R., A. H. Corbett, and M. Stewart. 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
  • 13
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn, L. A., T. Shen, ..., S. R. Wente. 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    Wente, S.R.3
  • 14
    • 0032589798 scopus 로고    scopus 로고
    • Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP
    • Bayliss, R., K. Ribbeck, ..., M. Stewart. 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    Stewart, M.3
  • 15
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • Bayliss, R., T. Littlewood, and M. Stewart. 2000. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell. 102:99-108.
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 16
    • 0037124352 scopus 로고    scopus 로고
    • Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats
    • Bayliss, R., S. W. Leung, ..., M. Stewart. 2002. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. EMBO J. 21:2843-2853.
    • (2002) EMBO J , vol.21 , pp. 2843-2853
    • Bayliss, R.1    Leung, S.W.2    Stewart, M.3
  • 17
    • 0037184968 scopus 로고    scopus 로고
    • GLFG and FxFG nucleoporins bind to overlapping sites on importin-β
    • Bayliss, R., T. Littlewood, ..., M. Stewart. 2002. GLFG and FxFG nucleoporins bind to overlapping sites on importin-β. J. Biol. Chem. 277:50597-50606.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50597-50606
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 18
    • 19444383899 scopus 로고    scopus 로고
    • Structural basis for the high-affinity binding of nucleoporin Nuplp to the Saccharomyces cerevisiae importin-β homologue, Kap95p
    • Liu, S. M., and M. Stewart. 2005. Structural basis for the high-affinity binding of nucleoporin Nuplp to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J. Mol. Biol. 349:515-525.
    • (2005) J Mol. Biol. , vol.349 , pp. 515-525
    • Liu, S.M.1    Stewart, M.2
  • 19
    • 39049094665 scopus 로고    scopus 로고
    • Discovering novel interactions at the nuclear pore complex using bead halo: A rapid method for detecting molecular interactions of high and low affinity at equilibrium
    • Patel, S. S., 61nd M. F. Rexach. 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.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 121-131
    • Patel, S.S.1    Rexach, M.F.2
  • 20
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-β
    • Isgro, T. A., and K. Schulten. 2005. Binding dynamics of isolated nucleoporin repeat regions to importin-β. Structure. 13:1869-1879.
    • (2005) Structure , vol.13 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 21
    • 33846270287 scopus 로고    scopus 로고
    • Association of nuclear pore FGrepeat domains to NTF2 import and export complexes
    • Isgro, T. A., and K. Schulten. 2007. Association of nuclear pore FGrepeat domains to NTF2 import and export complexes. J. Mol. Biol. 366:330-345.
    • (2007) J Mol. Biol. , vol.366 , pp. 330-345
    • Isgro, T.A.1    Schulten, K.2
  • 22
    • 34547657392 scopus 로고    scopus 로고
    • Cselp-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors
    • Isgro, T. A., and K. Schulten. 2007. Cselp-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors. Structure. 15:977-991.
    • (2007) Structure , vol.15 , pp. 977-991
    • Isgro, T.A.1    Schulten, K.2
  • 23
    • 0242391971 scopus 로고    scopus 로고
    • Virtual gating and nuclear transport: The hole picture
    • Rout, M. P., J. D. Aitchison, ..., B. T. Chait. 2003. Virtual gating and nuclear transport: The hole picture. Trends Cell Biol. 13:622-628.
    • (2003) Trends Cell Biol. , vol.13 , pp. 622-628
    • Rout, M.P.1    Aitchison, J.D.2    Chait, B.T.3
  • 24
    • 0142180053 scopus 로고    scopus 로고
    • A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex
    • Pyhtila, B., and M. Rexach. 2003. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J. Biol. Chem. 278:42699-42709.
    • (2003) J Biol. Chem. , vol.278 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 25
    • 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
  • 26
    • 33745451968 scopus 로고    scopus 로고
    • Flexible phenylalanineglycine nucleoporins as entropic barriers to nucleocytoplasmic transport
    • Lim, R. Y. H., N.-P. Huang, ..., U. Aebi. 2006. Flexible phenylalanineglycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl. Acad. Sci. USA. 103:9512-9517.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9512-9517
    • Lim, R.Y.H.1    Huang, N.-P.2    Aebi, U.3
  • 27
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck, K., and D. Görlich. 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
  • 28
    • 43149094411 scopus 로고    scopus 로고
    • Atomic force microscopy visualizes a hydrophobic meshwork in the central, channel of the nuclear pore
    • Kramer, A., I. Liashkovich, ..., V. Shahin. 2007. Atomic force microscopy visualizes a hydrophobic meshwork in the central, channel of the nuclear pore. Pfiugers Arch. 456:155-162.
    • (2007) Pfiugers Arch. , vol.456 , pp. 155-162
    • Kramer, A.1    Liashkovich, I.2    Shahin, V.3
  • 29
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck, K., and D. Görlich. 200.1, 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
  • 30
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey, S., R. P. Richter, and D. Görlich. 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
  • 31
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey, S., and D. Görlich. 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
  • 32
    • 13844264432 scopus 로고    scopus 로고
    • Nuclear transport of single molecules: Dwell times at the nuclear pore complex
    • Kubitscheck, U., D. Grünwald, ..., R. Peters. 2005. Nuclear transport of single molecules: dwell times at the nuclear pore complex. J. Cell Biol. 168:233-243.
    • (2005) J. Cell Biol. , vol.168 , pp. 233-243
    • Kubitscheck, U.1    Grünwald, D.2    Peters, R.3
  • 33
    • 4444284306 scopus 로고    scopus 로고
    • Imaging of single-molecule translocation through nuclear pore complexes
    • Yang, W., J. Gelles, and S. M. Musser. 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
  • 34
    • 61449201281 scopus 로고    scopus 로고
    • Transport-related structures and processes of the nuclear pore complex studied through, molecular dynamics
    • Miao, L., and K. Schulten. 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
  • 37
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W. L., D. S. Maxwell, and J. Tirado-Rives. 1996. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236.
    • (1996) J Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 38
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G. A., R. A. Friesner, ..., W. L. Jorgensen. 2001, Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105:6474-6487.
    • (2001) J Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Jorgensen, W.L.3
  • 39
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • B. Pullman, editor. Reidel, Dordrecht, The Netherlands
    • Berendsen, H. J. C., J. P. M. Postma, ..., J. Hermans. 1981, Interaction models for water in relation to protein hydration. In Intermolecular Forces. B. Pullman, editor. Reidel, Dordrecht, The Netherlands.
    • (1981) Intermolecular Forces
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Hermans, J.3
  • 40
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H. J. C., J. P. M. Postma, ..., J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81: 3684-3690.
    • (1984) J Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 41
    • 0029831680 scopus 로고    scopus 로고
    • An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies
    • Kelley, L. A., S. P. Gardner, and M. J. Sutcliffe. 1996. An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies. Protein Eng. 9: 1063-1065.
    • (1996) Protein Eng. , vol.9 , pp. 1063-1065
    • Kelley, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 42
    • 84986483798 scopus 로고
    • The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies
    • Eisenhaber, F., P. Lijnzaad, ..., M. Scharf. 1995. The double cubic lattice method: efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies. J. Comput. Chem. 16:273-284.
    • (1995) J. Comput. Chem. , vol.16 , pp. 273-284
    • Eisenhaber, F.1    Lijnzaad, P.2    Scharf, M.3
  • 43
    • 0032549195 scopus 로고    scopus 로고
    • Hydrogen bond strengths revealed by topological analyses of experimentally observed electron densities
    • Espinosa, E., E. Molins, and C. Lecomte. 1998. Hydrogen bond strengths revealed by topological analyses of experimentally observed electron densities. Chem. Phys. Lett. 285:170-173.
    • (1998) Chem. Phys. Lett. , vol.285 , pp. 170-173
    • Espinosa, E.1    Molins, E.2    Lecomte, C.3
  • 44
    • 0035970888 scopus 로고    scopus 로고
    • Extreme diversity, conservation, and convergence of spider silk fibroin sequences
    • Gatesy, J., C. Hayashi, ..., R. Lewis. 2001. Extreme diversity, conservation, and convergence of spider silk fibroin sequences. Science. 291:2603-2605.
    • (2001) Science , vol.291 , pp. 2603-2605
    • Gatesy, J.1    Hayashi, C.2    Lewis, R.3
  • 45
    • 33846250450 scopus 로고    scopus 로고
    • Proline and glycine control protein, self-organization into elastomeric or amyloid fibrils
    • Rauscher, S., S. Baud, ..., R. Pomès. 2006. Proline and glycine control protein, self-organization into elastomeric or amyloid fibrils. Structure. 14:1667-1676.
    • (2006) Structure , vol.14 , pp. 1667-1676
    • Rauscher, S.1    Baud, S.2    Pomès, R.3
  • 46
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and C. M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 47
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis confusion of the kinds?
    • Rousseau, F., J. Schymkowitz, and L. Serrano. 2006. Protein aggregation and amyloidosis: confusion of the kinds? Curr. Opin. Struct. Biol. 16:118-126.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3
  • 48
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/ asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch, M. D., and J. S. Weissman. 2000. A census of glutamine/ asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA. 97: 11910-11915.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 49
    • 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., E. Y. Lau, ..., M. F. Rexach. 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    Rexach, M.F.3


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