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Volumn 1853, Issue 11, 2015, Pages 3053-3064

Physical properties of cytoplasmic intermediate filaments

Author keywords

Assembly; Cell mechanics; Intermediate filament; Network; Persistence length; Polyelectrolyte

Indexed keywords

BIOPOLYMER; INTERMEDIATE FILAMENT PROTEIN; POLYELECTROLYTE;

EID: 84944147371     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.05.009     Document Type: Review
Times cited : (91)

References (99)
  • 2
    • 84903704807 scopus 로고    scopus 로고
    • Microtubule-dependent transport of vimentin filament precursors is regulated by actin and by the concerted action of Rho- and p21-activated kinases
    • Robert A., Herrmann H., Davidson M.W., Gelfand V.I. Microtubule-dependent transport of vimentin filament precursors is regulated by actin and by the concerted action of Rho- and p21-activated kinases. FASEB J. 2014, 28:2879-2890.
    • (2014) FASEB J. , vol.28 , pp. 2879-2890
    • Robert, A.1    Herrmann, H.2    Davidson, M.W.3    Gelfand, V.I.4
  • 3
    • 84929492895 scopus 로고    scopus 로고
    • Microtubule-dependent transport and dynamics of vimentin intermediate filaments
    • Hookway C., Ding L., Davidson M.W., Rappoport J.Z., Danuser G., Gelfand V.I. Microtubule-dependent transport and dynamics of vimentin intermediate filaments. Mol. Biol. Cell 2015, 26:1675-1686. http://www.molbiolcell.org/content/26/9/1675.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 1675-1686
    • Hookway, C.1    Ding, L.2    Davidson, M.W.3    Rappoport, J.Z.4    Danuser, G.5    Gelfand, V.I.6
  • 5
    • 84879796143 scopus 로고    scopus 로고
    • Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve
    • Castanon M.J., Walko G., Winter L., Wiche G. Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve. Histochem. Cell Biol. 2013, 140:33-53.
    • (2013) Histochem. Cell Biol. , vol.140 , pp. 33-53
    • Castanon, M.J.1    Walko, G.2    Winter, L.3    Wiche, G.4
  • 7
    • 34250867157 scopus 로고    scopus 로고
    • A quantitative kinetic model for the in vitro assembly of intermediate filaments from tetrameric vimentin
    • Kirmse R., Portet S., Mücke N., Aebi U., Herrmann H., Langowski J. A quantitative kinetic model for the in vitro assembly of intermediate filaments from tetrameric vimentin. J. Mol. Biol. 2007, 282:18563-18572.
    • (2007) J. Mol. Biol. , vol.282 , pp. 18563-18572
    • Kirmse, R.1    Portet, S.2    Mücke, N.3    Aebi, U.4    Herrmann, H.5    Langowski, J.6
  • 8
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann H., Häner M., Brettel M., Ku N.-O., Aebi U. Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 1999, 286:1403-1420.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Ku, N.-O.4    Aebi, U.5
  • 9
    • 84855850260 scopus 로고    scopus 로고
    • Complex formation and kinetics of filament assembly exhibited by the simple epithelial keratins K8 and K18
    • Lichtenstern T., Mücke N., Aebi U., Mauermann M., Herrmann H. Complex formation and kinetics of filament assembly exhibited by the simple epithelial keratins K8 and K18. J. Struct. Biol. 2012, 177:54-62.
    • (2012) J. Struct. Biol. , vol.177 , pp. 54-62
    • Lichtenstern, T.1    Mücke, N.2    Aebi, U.3    Mauermann, M.4    Herrmann, H.5
  • 10
    • 74249099760 scopus 로고    scopus 로고
    • Vimentin intermediate filament formation: in vitro measurement and mathematical modeling of the filament length distribution during assembly
    • Portet S., Mücke N., Kirmse R., Langowski J., Beil M., Herrmann H. Vimentin intermediate filament formation: in vitro measurement and mathematical modeling of the filament length distribution during assembly. Langmuir 2009, 25:8817-8823.
    • (2009) Langmuir , vol.25 , pp. 8817-8823
    • Portet, S.1    Mücke, N.2    Kirmse, R.3    Langowski, J.4    Beil, M.5    Herrmann, H.6
  • 12
    • 84897597282 scopus 로고    scopus 로고
    • Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering
    • Brennich M.E., Bauch S., Vainio U., Wedig T., Herrmann H., Köster S. Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering. Soft Matter 2014, 10:2059-2068.
    • (2014) Soft Matter , vol.10 , pp. 2059-2068
    • Brennich, M.E.1    Bauch, S.2    Vainio, U.3    Wedig, T.4    Herrmann, H.5    Köster, S.6
  • 14
    • 0021099704 scopus 로고
    • The distribution of mass in heteropolymer intermediate filaments assembled in vitro. Stem analysis of vimentin/desmin and bovine epidermal keratin
    • Steven A.C., Hainfeld J.F., Trus B.L., Wall J.S., Steinert P.M. The distribution of mass in heteropolymer intermediate filaments assembled in vitro. Stem analysis of vimentin/desmin and bovine epidermal keratin. J. Biol. Chem. 1983, 258:8323-8329.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8323-8329
    • Steven, A.C.1    Hainfeld, J.F.2    Trus, B.L.3    Wall, J.S.4    Steinert, P.M.5
  • 15
    • 0021968193 scopus 로고
    • Polymorphism of reconstituted human epidermal keratin filaments: determination of their mass-per-length and width by scanning transmission electron microscopy (STEM)
    • Engel A., Eichner R., Aebi U. Polymorphism of reconstituted human epidermal keratin filaments: determination of their mass-per-length and width by scanning transmission electron microscopy (STEM). J. Ultrastruct. Res. 1985, 90:323-335.
    • (1985) J. Ultrastruct. Res. , vol.90 , pp. 323-335
    • Engel, A.1    Eichner, R.2    Aebi, U.3
  • 16
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T., Kirschner M. Dynamic instability of microtubule growth. Nature 1984, 312:237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 17
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • Kuhn J.R., Pollard T.D. Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biochem. J. 2005, 88:1387-1402.
    • (2005) Biochem. J. , vol.88 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 18
    • 66349104792 scopus 로고    scopus 로고
    • Intermediate filaments exchange subunits along their length and elongate by end-to-end annealing
    • Çolakoğlu G., Brown A. Intermediate filaments exchange subunits along their length and elongate by end-to-end annealing. J. Cell Biol. 2009, 185:769-777.
    • (2009) J. Cell Biol. , vol.185 , pp. 769-777
    • Çolakoğlu, G.1    Brown, A.2
  • 21
    • 84920181574 scopus 로고    scopus 로고
    • Direct observation of subunit exchange along mature vimentin intermediate filaments
    • Nöding B., Herrmann H., Köster S. Direct observation of subunit exchange along mature vimentin intermediate filaments. Biochem. J. 2014, 107:2923-2931.
    • (2014) Biochem. J. , vol.107 , pp. 2923-2931
    • Nöding, B.1    Herrmann, H.2    Köster, S.3
  • 23
    • 0025190741 scopus 로고
    • Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly
    • Ngai J., Coleman T.R., Lazarides E. Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly. Cell 1990, 60:415-427.
    • (1990) Cell , vol.60 , pp. 415-427
    • Ngai, J.1    Coleman, T.R.2    Lazarides, E.3
  • 24
    • 0027064785 scopus 로고
    • Continuous growth of vimentin filaments in mouse fibroblasts
    • Coleman T.R., Lazarides E. Continuous growth of vimentin filaments in mouse fibroblasts. J. Cell Sci. 1992, 103:689-698.
    • (1992) J. Cell Sci. , vol.103 , pp. 689-698
    • Coleman, T.R.1    Lazarides, E.2
  • 25
    • 0022342580 scopus 로고
    • Identification of a distinct soluble subunit of an intermediate filament protein: tetrameric vimentin from living cells
    • Soellner P., Quinlan R.A., Franke W.W. Identification of a distinct soluble subunit of an intermediate filament protein: tetrameric vimentin from living cells. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:7929-7933.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 7929-7933
    • Soellner, P.1    Quinlan, R.A.2    Franke, W.W.3
  • 27
    • 0038709375 scopus 로고    scopus 로고
    • Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis
    • Chou Y.-H., Khuon S., Herrmann H., Goldman R.D. Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis. Mol. Biol. Cell 2003, 14:1468-1478.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1468-1478
    • Chou, Y.-H.1    Khuon, S.2    Herrmann, H.3    Goldman, R.D.4
  • 29
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18
    • Hesse M., Magin T.M., Weber K. Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J. Cell Sci. 2001, 114:2569-2575.
    • (2001) J. Cell Sci. , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 30
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • Omary M.B., Coulombe P.A., McLean W.H.Irwin Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 2004, 351:2087-2100.
    • (2004) N. Engl. J. Med. , vol.351 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2    McLean, W.H.I.3
  • 31
    • 68849106856 scopus 로고    scopus 로고
    • "IF-pathies": a broad spectrum of intermediate filament-associated diseases
    • Omary M.B. "IF-pathies": a broad spectrum of intermediate filament-associated diseases. J. Clin. Invest. 2009, 119:1756-1762.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1756-1762
    • Omary, M.B.1
  • 32
    • 79952062041 scopus 로고    scopus 로고
    • History and phylogeny of intermediate filaments: now in insects
    • Herrmann H., Strelkov S.V. History and phylogeny of intermediate filaments: now in insects. BMC Biol. 2011, 9:16.
    • (2011) BMC Biol. , vol.9 , pp. 16
    • Herrmann, H.1    Strelkov, S.V.2
  • 33
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes F., Mickey B., Nettleton J., Howard J. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 1993, 120:923-934.
    • (1993) J. Cell Biol. , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 34
    • 84857584670 scopus 로고    scopus 로고
    • Intermediate filaments in small configuration spaces
    • Nöding B., Köster S. Intermediate filaments in small configuration spaces. Phys. Rev. Lett 2012, 108:088101.
    • (2012) Phys. Rev. Lett , vol.108 , pp. 088101
    • Nöding, B.1    Köster, S.2
  • 35
    • 84925060211 scopus 로고    scopus 로고
    • Intermediate filament mechanics in vitro and in the cell: from coiled coils to filaments, fibers and networks
    • Köster S., Weitz D.A., Goldman R.D., Aebi U., Herrmann H. Intermediate filament mechanics in vitro and in the cell: from coiled coils to filaments, fibers and networks. Curr. Opin. Struct. Biol. 2015, 32C:82-91.
    • (2015) Curr. Opin. Struct. Biol. , vol.32C , pp. 82-91
    • Köster, S.1    Weitz, D.A.2    Goldman, R.D.3    Aebi, U.4    Herrmann, H.5
  • 36
    • 0041319662 scopus 로고    scopus 로고
    • The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads
    • Fudge D.S., Gardner K.H., Forsyth V.T., Riekel C., Gosline J.M. The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads. Biochem. J. 2003, 85:2015-2027.
    • (2003) Biochem. J. , vol.85 , pp. 2015-2027
    • Fudge, D.S.1    Gardner, K.H.2    Forsyth, V.T.3    Riekel, C.4    Gosline, J.M.5
  • 37
    • 84898871818 scopus 로고    scopus 로고
    • Attractive interactions among intermediate filaments determine network mechanics in vitro
    • Pawelzyk P., Mücke N., Herrmann H., Willenbacher N. Attractive interactions among intermediate filaments determine network mechanics in vitro. PLoS One 2014, 9:e93194.
    • (2014) PLoS One , vol.9 , pp. e93194
    • Pawelzyk, P.1    Mücke, N.2    Herrmann, H.3    Willenbacher, N.4
  • 38
    • 0032850141 scopus 로고    scopus 로고
    • Desmin filaments studied by quasi-elastic light scattering
    • Hohenadl M., Storz T., Kirpal H., Kroy K., Merkel R. Desmin filaments studied by quasi-elastic light scattering. Biochem. J. 1999, 77:2199-2209.
    • (1999) Biochem. J. , vol.77 , pp. 2199-2209
    • Hohenadl, M.1    Storz, T.2    Kirpal, H.3    Kroy, K.4    Merkel, R.5
  • 39
    • 63449103436 scopus 로고    scopus 로고
    • Desmin and vimentin intermediate filament networks: their viscoelastic properties investigated by mechanical rheometry
    • Schopferer M., Bär H., Hochstein B., Sharma S., Mücke N., Herrmann H., Willenbacher N. Desmin and vimentin intermediate filament networks: their viscoelastic properties investigated by mechanical rheometry. J. Mol. Biol. 2009, 388:133-143.
    • (2009) J. Mol. Biol. , vol.388 , pp. 133-143
    • Schopferer, M.1    Bär, H.2    Hochstein, B.3    Sharma, S.4    Mücke, N.5    Herrmann, H.6    Willenbacher, N.7
  • 44
    • 0001231059 scopus 로고    scopus 로고
    • Dynamic shear modulus of a semiflexible polymer network
    • Gittes F., MacKintosh F. Dynamic shear modulus of a semiflexible polymer network. Phys. Rev. E 1998, 58:R1241.
    • (1998) Phys. Rev. E , vol.58 , pp. R1241
    • Gittes, F.1    MacKintosh, F.2
  • 45
    • 34248578409 scopus 로고    scopus 로고
    • Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography
    • Goldie K.N., Wedig T., Mitra A.K., Aebi U., Herrmann H., Hoenger A. Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography. J. Struct. Biol. 2007, 158:378-385.
    • (2007) J. Struct. Biol. , vol.158 , pp. 378-385
    • Goldie, K.N.1    Wedig, T.2    Mitra, A.K.3    Aebi, U.4    Herrmann, H.5    Hoenger, A.6
  • 46
    • 27744588225 scopus 로고    scopus 로고
    • Exploring the mechanical behavior of single intermediate filaments
    • Kreplak L., Bär H., Leterrier J.F., Herrmann H., Aebi U. Exploring the mechanical behavior of single intermediate filaments. J. Mol. Biol. 2005, 354:569-577.
    • (2005) J. Mol. Biol. , vol.354 , pp. 569-577
    • Kreplak, L.1    Bär, H.2    Leterrier, J.F.3    Herrmann, H.4    Aebi, U.5
  • 47
    • 41649116913 scopus 로고    scopus 로고
    • Tensile properties of single desmin intermediate filaments
    • Kreplak L., Herrmann H., Aebi U. Tensile properties of single desmin intermediate filaments. Biochem. J. 2008, 94:2790-2799.
    • (2008) Biochem. J. , vol.94 , pp. 2790-2799
    • Kreplak, L.1    Herrmann, H.2    Aebi, U.3
  • 48
    • 33745674667 scopus 로고    scopus 로고
    • Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy
    • Guzmán C., Jeney S., Kreplak L., Kasas S., Kulik A.J., Aebi U., Forró L. Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy. J. Mol. Biol. 2006, 360:623-630.
    • (2006) J. Mol. Biol. , vol.360 , pp. 623-630
    • Guzmán, C.1    Jeney, S.2    Kreplak, L.3    Kasas, S.4    Kulik, A.J.5    Aebi, U.6    Forró, L.7
  • 50
    • 0000365266 scopus 로고
    • A quantitative X-ray diffraction study of the alpha-beta transformation in wool keratin
    • Bendit E.G. A quantitative X-ray diffraction study of the alpha-beta transformation in wool keratin. Text. Res. J. 1960, 30:547-555.
    • (1960) Text. Res. J. , vol.30 , pp. 547-555
    • Bendit, E.G.1
  • 51
    • 33846628445 scopus 로고    scopus 로고
    • Biomechanical properties of intermediate filaments: from tissues to single filaments and back
    • Kreplak L., Fudge D. Biomechanical properties of intermediate filaments: from tissues to single filaments and back. Bioessays 2007, 29:26-35.
    • (2007) Bioessays , vol.29 , pp. 26-35
    • Kreplak, L.1    Fudge, D.2
  • 52
    • 70349713574 scopus 로고    scopus 로고
    • Hierarchical structure controls nanomechanical properties of vimentin intermediate filaments
    • Qin Z., Kreplak L., Buehler M.J. Hierarchical structure controls nanomechanical properties of vimentin intermediate filaments. PLoS One 2009, 4:e7294.
    • (2009) PLoS One , vol.4 , pp. e7294
    • Qin, Z.1    Kreplak, L.2    Buehler, M.J.3
  • 53
    • 70349662344 scopus 로고    scopus 로고
    • Nanomechanical properties of vimentin intermediate filament dimers
    • Qin Z., Kreplak L., Buehler M.J. Nanomechanical properties of vimentin intermediate filament dimers. Nanotechnology 2009, 20:425101.
    • (2009) Nanotechnology , vol.20 , pp. 425101
    • Qin, Z.1    Kreplak, L.2    Buehler, M.J.3
  • 54
    • 78651420058 scopus 로고    scopus 로고
    • Structure and dynamics of human vimentin intermediate filament dimer and tetramer in explicit and implicit solvent models
    • Qin Z., Buehler M.J. Structure and dynamics of human vimentin intermediate filament dimer and tetramer in explicit and implicit solvent models. J. Mol. Model. 2011, 17:37-48.
    • (2011) J. Mol. Model. , vol.17 , pp. 37-48
    • Qin, Z.1    Buehler, M.J.2
  • 55
    • 84923328705 scopus 로고    scopus 로고
    • Competitive counterion binding regulates the aggregation onset of vimentin intermediate filaments
    • Dammann C., Herrmann H., Köster S. Competitive counterion binding regulates the aggregation onset of vimentin intermediate filaments. Isr. J. Chem. 2015, 10.1002/ijch.201400153.
    • (2015) Isr. J. Chem.
    • Dammann, C.1    Herrmann, H.2    Köster, S.3
  • 56
    • 84894221513 scopus 로고    scopus 로고
    • Polyelectrolyte properties of filamentous biopolymers and their consequences in biological fluids
    • Janmey P.A., Slochower D.R., Wang Y.-H., Wen Q., Cebers A. Polyelectrolyte properties of filamentous biopolymers and their consequences in biological fluids. Soft Matter 2014, 10:1439-1449.
    • (2014) Soft Matter , vol.10 , pp. 1439-1449
    • Janmey, P.A.1    Slochower, D.R.2    Wang, Y.-H.3    Wen, Q.4    Cebers, A.5
  • 58
    • 84863192745 scopus 로고    scopus 로고
    • Vimentin networks at tunable ion-concentration in microfluidic drops
    • Dammann C., Noding B., Köster S. Vimentin networks at tunable ion-concentration in microfluidic drops. Biomicrofluidics 2012, 6:22009-2200910.
    • (2012) Biomicrofluidics , vol.6 , pp. 22009-2200910
    • Dammann, C.1    Noding, B.2    Köster, S.3
  • 59
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann H., Aebi U. Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol. 1998, 8:177-185.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 60
    • 0023655822 scopus 로고
    • Effect of cations and temperature on kinetics of desmin assembly
    • Stromer M.H., Ritter M.A., Pang Y.Y., Robson R.M. Effect of cations and temperature on kinetics of desmin assembly. Biochem. J. 1987, 246:75-81.
    • (1987) Biochem. J. , vol.246 , pp. 75-81
    • Stromer, M.H.1    Ritter, M.A.2    Pang, Y.Y.3    Robson, R.M.4
  • 61
    • 0026343580 scopus 로고
    • Assembly and structure of calcium-induced thick vimentin filaments
    • Hofmann I., Herrmann H., Franke W.W. Assembly and structure of calcium-induced thick vimentin filaments. Eur. J. Cell Biol. 1991, 56:328-341.
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 328-341
    • Hofmann, I.1    Herrmann, H.2    Franke, W.W.3
  • 62
    • 0030930190 scopus 로고    scopus 로고
    • Transient electric birefringence study of intermediate filament formation from vimentin and glial fibrillary acidic protein
    • Kooijman M., Bloemendal M., Traub P., van Grondelle R., van Amerongen H. Transient electric birefringence study of intermediate filament formation from vimentin and glial fibrillary acidic protein. J. Biol. Chem. 1997, 272:22548-22555.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22548-22555
    • Kooijman, M.1    Bloemendal, M.2    Traub, P.3    van Grondelle, R.4    van Amerongen, H.5
  • 63
    • 0028850871 scopus 로고
    • Hydrodynamic and electrical characterization of T-vimentin dimers and tetramers by transient electric birefringence measurements
    • Kooijman M., Bloemendal M., Traub P., van Grondelle R., van Amerongen H. Hydrodynamic and electrical characterization of T-vimentin dimers and tetramers by transient electric birefringence measurements. J. Biol. Chem. 1995, 270:2931-2937.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2931-2937
    • Kooijman, M.1    Bloemendal, M.2    Traub, P.3    van Grondelle, R.4    van Amerongen, H.5
  • 65
    • 77951525622 scopus 로고    scopus 로고
    • Nanomechanics of vimentin intermediate filament networks
    • Köster S., Lin Y.-C., Herrmann H., Weitz D.A. Nanomechanics of vimentin intermediate filament networks. Soft Matter 2010, 6:1910-1914.
    • (2010) Soft Matter , vol.6 , pp. 1910-1914
    • Köster, S.1    Lin, Y.-C.2    Herrmann, H.3    Weitz, D.A.4
  • 66
    • 84886003891 scopus 로고    scopus 로고
    • The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks
    • Kayser J., Haslbeck M., Dempfle L., Krause M., Grashoff C., Buchner J., Herrmann H., Bausch A.R. The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. Biochem. J. 2013, 105:1778-1785.
    • (2013) Biochem. J. , vol.105 , pp. 1778-1785
    • Kayser, J.1    Haslbeck, M.2    Dempfle, L.3    Krause, M.4    Grashoff, C.5    Buchner, J.6    Herrmann, H.7    Bausch, A.R.8
  • 68
    • 84883365377 scopus 로고    scopus 로고
    • Mechanics of intermediate filament networks assembled from keratins K8 and K18
    • Pawelzyk P., Willenbacher N., Herrmann H. Mechanics of intermediate filament networks assembled from keratins K8 and K18. Soft Matter 2013, 9:8871-8880.
    • (2013) Soft Matter , vol.9 , pp. 8871-8880
    • Pawelzyk, P.1    Willenbacher, N.2    Herrmann, H.3
  • 69
    • 84925104796 scopus 로고    scopus 로고
    • Dynamics of counterion-induced attraction between vimentin filaments followed in microfluidic drops
    • Dammann C., Köster S. Dynamics of counterion-induced attraction between vimentin filaments followed in microfluidic drops. Lab Chip 2014, 14:2681-2687.
    • (2014) Lab Chip , vol.14 , pp. 2681-2687
    • Dammann, C.1    Köster, S.2
  • 71
    • 0025765110 scopus 로고
    • Viscoelastic properties of vimentin compared with other filamentous biopolymer networks
    • Janmey P.A., Euteneuer U., Traub P., Schliwa M. Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J. Cell Biol. 1991, 113:155-160.
    • (1991) J. Cell Biol. , vol.113 , pp. 155-160
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 72
    • 34347401911 scopus 로고    scopus 로고
    • Mechanical and structural properties of in vitro neurofilament hydrogels
    • Rammensee S., Janmey P.A., Bausch A.R. Mechanical and structural properties of in vitro neurofilament hydrogels. Eur. Biophys. J. 2007, 36:661-668.
    • (2007) Eur. Biophys. J. , vol.36 , pp. 661-668
    • Rammensee, S.1    Janmey, P.A.2    Bausch, A.R.3
  • 73
    • 0043169526 scopus 로고    scopus 로고
    • The mechanical properties of simple epithelial keratins 8 and 18: discriminating between interfacial and bulk elasticities
    • Yamada S., Wirtz D., Coulombe P.A. The mechanical properties of simple epithelial keratins 8 and 18: discriminating between interfacial and bulk elasticities. J. Struct. Biol. 2003, 143:45-55.
    • (2003) J. Struct. Biol. , vol.143 , pp. 45-55
    • Yamada, S.1    Wirtz, D.2    Coulombe, P.A.3
  • 76
    • 0035022929 scopus 로고    scopus 로고
    • A 'hot-spot' mutation alters the mechanical properties of keratin filament networks
    • Ma L., Yamada S., Wirtz D., Coulombe P.A. A 'hot-spot' mutation alters the mechanical properties of keratin filament networks. Nat. Cell Biol. 2001, 3:503-506.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 503-506
    • Ma, L.1    Yamada, S.2    Wirtz, D.3    Coulombe, P.A.4
  • 78
    • 0000156877 scopus 로고    scopus 로고
    • Entanglement, elasticity, and viscous relaxation of actin solutions
    • Hinner B., Tempel M., Sackmann E., Kroy K., Frey E. Entanglement, elasticity, and viscous relaxation of actin solutions. Phys. Rev. Lett. 1998, 81:2614-2617.
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 2614-2617
    • Hinner, B.1    Tempel, M.2    Sackmann, E.3    Kroy, K.4    Frey, E.5
  • 80
    • 25544458211 scopus 로고
    • Elasticity of semiflexible biopolymer networks
    • MacKintosh F.C., Käs J., Janmey P.A. Elasticity of semiflexible biopolymer networks. Phys. Rev. Lett. 1995, 75:4425-4428.
    • (1995) Phys. Rev. Lett. , vol.75 , pp. 4425-4428
    • MacKintosh, F.C.1    Käs, J.2    Janmey, P.A.3
  • 82
    • 0000616923 scopus 로고    scopus 로고
    • Dynamics and rheology of actin solutions
    • Isambert H., Maggs A.C. Dynamics and rheology of actin solutions. Macromolecules 1996, 29:1036-1040.
    • (1996) Macromolecules , vol.29 , pp. 1036-1040
    • Isambert, H.1    Maggs, A.C.2
  • 84
    • 0033516670 scopus 로고    scopus 로고
    • Keratin filament suspensions show unique micromechanical properties
    • Ma L., Xu J., Coulombe P.A., Wirtz D. Keratin filament suspensions show unique micromechanical properties. J. Biol. Chem. 1999, 274:19145-19151.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19145-19151
    • Ma, L.1    Xu, J.2    Coulombe, P.A.3    Wirtz, D.4
  • 85
    • 36949026410 scopus 로고    scopus 로고
    • The glassy wormlike chain
    • Kroy K., Glaser J. The glassy wormlike chain. New J. Phys. 2007, 9:416.
    • (2007) New J. Phys. , vol.9 , pp. 416
    • Kroy, K.1    Glaser, J.2
  • 87
    • 0036443637 scopus 로고    scopus 로고
    • Characterization of early assembly intermediates of recombinant human keratins
    • Herrmann H., Wedig T., Porter R.M., Lane E.B., Aebi U. Characterization of early assembly intermediates of recombinant human keratins. J. Struct. Biol. 2002, 137:82-96.
    • (2002) J. Struct. Biol. , vol.137 , pp. 82-96
    • Herrmann, H.1    Wedig, T.2    Porter, R.M.3    Lane, E.B.4    Aebi, U.5
  • 88
    • 84878537119 scopus 로고    scopus 로고
    • Keratins control intercellular adhesion involving PKC-α-mediated desmoplakin phosphorylation
    • Kröger C., Loschke F., Schwarz N., Windoffer R., Leube R.E., Magin T.M. Keratins control intercellular adhesion involving PKC-α-mediated desmoplakin phosphorylation. J. Cell Biol. 2013, 201:681-692.
    • (2013) J. Cell Biol. , vol.201 , pp. 681-692
    • Kröger, C.1    Loschke, F.2    Schwarz, N.3    Windoffer, R.4    Leube, R.E.5    Magin, T.M.6
  • 89
    • 84887459782 scopus 로고    scopus 로고
    • Keratins significantly contribute to cell stiffness and impact invasive behavior
    • Seltmann K., Fritsch A.W., Käs J.A., Magin T.M. Keratins significantly contribute to cell stiffness and impact invasive behavior. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:18507-18512.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 18507-18512
    • Seltmann, K.1    Fritsch, A.W.2    Käs, J.A.3    Magin, T.M.4
  • 93
    • 77953484480 scopus 로고    scopus 로고
    • Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition
    • Mendez M.G., Kojima S.-I., Goldman R.D. Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition. FASEB J. 2010, 24:1838-1851.
    • (2010) FASEB J. , vol.24 , pp. 1838-1851
    • Mendez, M.G.1    Kojima, S.-I.2    Goldman, R.D.3
  • 95
    • 80052624717 scopus 로고    scopus 로고
    • Cytoskeleton in motion: the dynamics of keratin intermediate filaments in epithelia
    • Windoffer R., Beil M., Magin T.M., Leube R.E. Cytoskeleton in motion: the dynamics of keratin intermediate filaments in epithelia. J. Cell Biol. 2011, 194:669-678.
    • (2011) J. Cell Biol. , vol.194 , pp. 669-678
    • Windoffer, R.1    Beil, M.2    Magin, T.M.3    Leube, R.E.4
  • 96
    • 84877805207 scopus 로고    scopus 로고
    • Influence of microfluidic shear on keratin networks in living cells
    • Nolting J.-F., Köster S. Influence of microfluidic shear on keratin networks in living cells. New J. Phys. 2013, 15:045025.
    • (2013) New J. Phys. , vol.15 , pp. 045025
    • Nolting, J.-F.1    Köster, S.2
  • 98
    • 84914127478 scopus 로고    scopus 로고
    • Mechanics of individual keratin bundles in living cells
    • Nolting J.-F., Möbius W., Köster S. Mechanics of individual keratin bundles in living cells. Biochem. J. 2014, 107:2693-2699.
    • (2014) Biochem. J. , vol.107 , pp. 2693-2699
    • Nolting, J.-F.1    Möbius, W.2    Köster, S.3


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