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Volumn 6, Issue 4, 2011, Pages

Deconstructing the late phase of vimentin assembly by total internal reflection fluorescence microscopy (TIRFM)

Author keywords

[No Author keywords available]

Indexed keywords

ALEXA 488 DYE; ALEXA 647 DYE; DYE; UNCLASSIFIED DRUG; VIMENTIN;

EID: 79955533597     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019202     Document Type: Article
Times cited : (73)

References (32)
  • 5
    • 0033039456 scopus 로고    scopus 로고
    • Diffusing wave spectroscopy microrheology of actin filament networks
    • Palmer A, Xu J, Kuo SC, Wirtz D, (1999) Diffusing wave spectroscopy microrheology of actin filament networks. Biophys J 76: 1063-1071.
    • (1999) Biophys J , vol.76 , pp. 1063-1071
    • Palmer, A.1    Xu, J.2    Kuo, S.C.3    Wirtz, D.4
  • 6
    • 33645778238 scopus 로고    scopus 로고
    • A bottom-up approach to cell mechanics
    • Bausch AR, Kroy K, (2006) A bottom-up approach to cell mechanics. Nature Physics 2: 231-238.
    • (2006) Nature Physics , vol.2 , pp. 231-238
    • Bausch, A.R.1    Kroy, K.2
  • 7
    • 0025765110 scopus 로고
    • Viscoelastic properties of vimentin compared with other filamentous biopolymer networks
    • Janmey PA, Euteneuer U, Traub P, Schliwa M, (1991) Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol 113.
    • (1991) J Cell Biol , vol.113
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 9
    • 77950519579 scopus 로고    scopus 로고
    • Mutations in Desmin's Carboxy-Terminal "Tail" Domain Severely Modify Filament and Network Mechanics
    • Bär H, Schopferer M, Sharma S, Hochstein B, Mücke N, et al. (2010) Mutations in Desmin's Carboxy-Terminal "Tail" Domain Severely Modify Filament and Network Mechanics. J Mol Biol 397: 1188-1198.
    • (2010) J Mol Biol , vol.397 , pp. 1188-1198
    • Bär, H.1    Schopferer, M.2    Sharma, S.3    Hochstein, B.4    Mücke, N.5
  • 10
    • 41649116913 scopus 로고    scopus 로고
    • Tensile properties of single desmin intermediate filaments
    • Kreplak L, Herrmann H, Aebi U, (2008) Tensile properties of single desmin intermediate filaments. Biophys J 94.
    • (2008) Biophys J , vol.94
    • Kreplak, L.1    Herrmann, H.2    Aebi, U.3
  • 11
    • 0026345962 scopus 로고
    • Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities
    • Bonifas JM, Rothman AL, Epstein EH Jr, (1991) Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities. Science 254: 1202-1205.
    • (1991) Science , vol.254 , pp. 1202-1205
    • Bonifas, J.M.1    Rothman, A.L.2    Epstein Jr., E.H.3
  • 12
    • 0028983054 scopus 로고
    • Hard alpha-keratin IF: a structural model lacking a head-to-tail molecular overlap but having hybrid features characteristic of both epidermal keratin and vimentin IF
    • Parry DA, (1995) Hard alpha-keratin IF: a structural model lacking a head-to-tail molecular overlap but having hybrid features characteristic of both epidermal keratin and vimentin IF. Proteins 22: 267-272.
    • (1995) Proteins , vol.22 , pp. 267-272
    • Parry, D.A.1
  • 13
    • 68849091625 scopus 로고    scopus 로고
    • Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility
    • Coulombe PA, Kerns ML, Fuchs E, (2009) Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility. J Clin Invest 119: 1784-1793.
    • (2009) J Clin Invest , vol.119 , pp. 1784-1793
    • Coulombe, P.A.1    Kerns, M.L.2    Fuchs, E.3
  • 14
    • 0027519337 scopus 로고
    • Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo
    • Herrmann H, Eckelt A, Brettel M, Grund C, Franke WW, (1993) Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo. J Mol Biol 234: 99-113.
    • (1993) J Mol Biol , vol.234 , pp. 99-113
    • Herrmann, H.1    Eckelt, A.2    Brettel, M.3    Grund, C.4    Franke, W.W.5
  • 15
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds
    • Herrmann H, Aebi U, (2004) Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu Rev Biochem 73: 749-789.
    • (2004) Annu Rev Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 16
    • 2942565983 scopus 로고    scopus 로고
    • Molecular and biophysical characterization of assembly-starter units of human vimentin
    • Mücke N, Wedig T, Bürer A, Marekov LN, Langowski J, et al. (2004) Molecular and biophysical characterization of assembly-starter units of human vimentin. J Mol Biol 340: 97-114.
    • (2004) J Mol Biol , vol.340 , pp. 97-114
    • Mücke, N.1    Wedig, T.2    Bürer, A.3    Marekov, L.N.4    Langowski, J.5
  • 17
    • 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, et al. (2009) Vimentin Intermediate Filament Formation: In Vitro Measurement and Mathematical Modeling of the Filament Length Distribution during Assembly. Langmuir 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
  • 18
    • 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, et al. (2007) A quantitative kinetic model for the in vitro assembly of intermediate filaments from tetrameric vimentin. J Biol Chem 282: 18563-18572.
    • (2007) J Biol Chem , vol.282 , pp. 18563-18572
    • Kirmse, R.1    Portet, S.2    Mücke, N.3    Aebi, U.4    Herrmann, H.5
  • 19
    • 59149083058 scopus 로고    scopus 로고
    • Near-UV circular dichroism reveals structural transitions of vimentin subunits during intermediate filament assembly
    • Georgakopoulou S, Möller D, Sachs N, Herrmann H, Aebi U, (2009) Near-UV circular dichroism reveals structural transitions of vimentin subunits during intermediate filament assembly. J Mol Biol 386.
    • (2009) J Mol Biol , vol.386
    • Georgakopoulou, S.1    Möller, D.2    Sachs, N.3    Herrmann, H.4    Aebi, U.5
  • 20
    • 14844362394 scopus 로고    scopus 로고
    • Characterization of the in vitro co-assembly process of the intermediate filament proteins vimentin and desmin: mixed polymers at all stages of assembly
    • Wickert U, Mücke N, Wedig T, Müller SA, Aebi U, et al. (2005) Characterization of the in vitro co-assembly process of the intermediate filament proteins vimentin and desmin: mixed polymers at all stages of assembly. Eur J Cell Biol 84: 379-391.
    • (2005) Eur J Cell Biol , vol.84 , pp. 379-391
    • Wickert, U.1    Mücke, N.2    Wedig, T.3    Müller, S.A.4    Aebi, U.5
  • 21
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann H, Haner M, Brettel M, Ku NO, Aebi U, (1999) Characterization of distinct early assembly units of different intermediate filament proteins. J Mol Biol 286: 1403-1420.
    • (1999) J Mol Biol , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5
  • 22
    • 0023655822 scopus 로고
    • Effect of cations and temperature on kinetics of desmin assembly
    • Stromer MH, Ritter MA, Pang YY, Robson RM, (1987) Effect of cations and temperature on kinetics of desmin assembly. Biochem J 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
  • 23
    • 14244253598 scopus 로고    scopus 로고
    • Isolation, characterization, and in vitro assembly of intermediate filaments
    • Herrmann H, Kreplak L, Aebi U, (2004) Isolation, characterization, and in vitro assembly of intermediate filaments. Methods Cell Biol 78: 3-24.
    • (2004) Methods Cell Biol , vol.78 , pp. 3-24
    • Herrmann, H.1    Kreplak, L.2    Aebi, U.3
  • 24
    • 5144230784 scopus 로고    scopus 로고
    • Assessing the flexibility of intermediate filaments by atomic force microscopy
    • Mücke N, Kreplak L, Kirmse R, Wedig T, Herrmann H, et al. (2004) Assessing the flexibility of intermediate filaments by atomic force microscopy. J Mol Biol 335: 1241-1250.
    • (2004) J Mol Biol , vol.335 , pp. 1241-1250
    • Mücke, N.1    Kreplak, L.2    Kirmse, R.3    Wedig, T.4    Herrmann, H.5
  • 25
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains
    • Herrmann H, Haner M, Brettel M, Müller SA, Goldie KN, et al. (1996) Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J Mol Biol 264: 933-953.
    • (1996) J Mol Biol , vol.264 , pp. 933-953
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Müller, S.A.4    Goldie, K.N.5
  • 26
    • 0035696945 scopus 로고    scopus 로고
    • Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: sequence, expression patterns and in vitro assembly
    • Schaffeld M, Herrmann H, Schultess J, Markl J, (2001) Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: sequence, expression patterns and in vitro assembly. Eur J Cell Biol 80.
    • (2001) Eur J Cell Biol , vol.80
    • Schaffeld, M.1    Herrmann, H.2    Schultess, J.3    Markl, J.4
  • 27
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann H, Aebi U, (1998) Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions. Curr Opin Struct Biol 8: 177-185.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 28
    • 0029585540 scopus 로고
    • In vivo assembly kinetics of fluorescently labeled Xenopus lamin A mutants
    • Schmidt M, Krohne G, (1995) In vivo assembly kinetics of fluorescently labeled Xenopus lamin A mutants. Eur J Cell Biol 68: 345-354.
    • (1995) Eur J Cell Biol , vol.68 , pp. 345-354
    • Schmidt, M.1    Krohne, G.2
  • 29
    • 0030198631 scopus 로고    scopus 로고
    • Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels
    • Rogers KR, Herrmann H, Franke WW, (1996) Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels. J Struct Biol 117.
    • (1996) J Struct Biol , vol.117
    • Rogers, K.R.1    Herrmann, H.2    Franke, W.W.3
  • 30
    • 0029940902 scopus 로고    scopus 로고
    • Vimentin in a cold-water fish, the rainbow trout: highly conserved primary structure but unique assembly properties
    • Herrmann H, Munick MD, Brettel M, Fouquet B, Markl J, (1996) Vimentin in a cold-water fish, the rainbow trout: highly conserved primary structure but unique assembly properties. J Cell Sci 109 (Pt 3): 569-578.
    • (1996) J Cell Sci , vol.109 , Issue.Pt 3 , pp. 569-578
    • Herrmann, H.1    Munick, M.D.2    Brettel, M.3    Fouquet, B.4    Markl, J.5
  • 31
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • Rivetti C, Guthold M, Bustamante C, (1996) Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis. J Mol Biol 264: 919-932.
    • (1996) J Mol Biol , vol.264 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 32
    • 70449433045 scopus 로고    scopus 로고
    • Filamentous Biopolymers on surfaces: Atomic Force Microscopy images compared with Brownian dynamics simulation of filament deposition
    • Mücke N, Klenin K, Kirmse R, Bussiek M, Herrmann H, et al. (2009) Filamentous Biopolymers on surfaces: Atomic Force Microscopy images compared with Brownian dynamics simulation of filament deposition. Plos ONE 4: 7756-7763.
    • (2009) Plos ONE , vol.4 , pp. 7756-7763
    • Mücke, N.1    Klenin, K.2    Kirmse, R.3    Bussiek, M.4    Herrmann, H.5


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