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Volumn 4, Issue 10, 2009, Pages

Hierarchical structure controls nanomechanical properties of vimentin intermediate filaments

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; TETRAMER; VIMENTIN;

EID: 70349713574     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007294     Document Type: Article
Times cited : (168)

References (55)
  • 1
    • 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. Annual Review of Biochemistry 73: 749-789.
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 2
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison CJ (2002) Lamins: Building blocks or regulators of gene expression? Nature Reviews Molecular Cell Biology 3: 848-858.
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 4
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • Wang N, Butler JP, Ingber DE (1993) Mechanotransduction across the cell surface and through the cytoskeleton. Science 260: 1124-1127.
    • (1993) Science , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 7
    • 0042668480 scopus 로고    scopus 로고
    • Concentric intermediate filament lattice links to specialized Z-band junctional complexes in sonic muscle fibers of the type I male midshipman fish
    • Lewis MK, Nahirney PC, Chen V, Adhikari BB, Wright J, et al. (2003) Concentric intermediate filament lattice links to specialized Z-band junctional complexes in sonic muscle fibers of the type I male midshipman fish. Journal Of Structural Biology 143: 56-71.
    • (2003) Journal Of Structural Biology , vol.143 , pp. 56-71
    • Lewis, M.K.1    Nahirney, P.C.2    Chen, V.3    Adhikari, B.B.4    Wright, J.5
  • 8
    • 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. Biophysical Journal 94: 2790-2799.
    • (2008) Biophysical Journal , vol.94 , pp. 2790-2799
    • Kreplak, L.1    Herrmann, H.2    Aebi, U.3
  • 9
    • 4544228141 scopus 로고    scopus 로고
    • The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
    • Dahl KN, Kahn SM, Wilson KL, Discher DE (2004) The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. Journal of Cell Science 117: 4779-4786.
    • (2004) Journal of Cell Science , vol.117 , pp. 4779-4786
    • Dahl, K.N.1    Kahn, S.M.2    Wilson, K.L.3    Discher, D.E.4
  • 10
    • 0035831041 scopus 로고    scopus 로고
    • Lamins and disease: Insights into nuclear infrastructure
    • Wilson KL, Zastrow MS, Lee KK (2001) Lamins and disease: Insights into nuclear infrastructure. Cell 104: 647-650.
    • (2001) Cell , vol.104 , pp. 647-650
    • Wilson, K.L.1    Zastrow, M.S.2    Lee, K.K.3
  • 12
    • 0035163913 scopus 로고    scopus 로고
    • Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease
    • Brenner M, Johnson AB, Boespflug-Tanguy O, Rodriguez D, Goldman JE, et al. (2001) Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease. Nature Genetics 27: 117-120.
    • (2001) Nature Genetics , vol.27 , pp. 117-120
    • Brenner, M.1    Johnson, A.B.2    Boespflug-Tanguy, O.3    Rodriguez, D.4    Goldman, J.E.5
  • 13
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • Omary MB, Coulombe PA, McLean WH (2004) Intermediate filament proteins and their associated diseases. N Engl J Med 351: 2087-2100.
    • (2004) N Engl J Med , vol.351 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2    McLean, W.H.3
  • 16
    • 0035793704 scopus 로고    scopus 로고
    • Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments
    • Strelkov SV, Herrmann H, Geisler N, Lustig A, Ivaninskii S, et al. (2001) Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. Journal of Molecular Biology 306: 773-781.
    • (2001) Journal of Molecular Biology , vol.306 , pp. 773-781
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Lustig, A.4    Ivaninskii, S.5
  • 17
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • Strelkov SV, Herrmann H, Geisler N, Wedig T, Zimbelmann R, et al. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. Embo Journal 21: 1255-1266.
    • (2002) Embo Journal , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5
  • 18
    • 2942651057 scopus 로고    scopus 로고
    • The intermediate filament architecture as determined by X-ray diffraction modeling of hard alpha-keratin
    • Rafik ME, Doucet J, Briki F (2004) The intermediate filament architecture as determined by X-ray diffraction modeling of hard alpha-keratin. Biophysical Journal 86: 3893-3904.
    • (2004) Biophysical Journal , vol.86 , pp. 3893-3904
    • Rafik, M.E.1    Doucet, J.2    Briki, F.3
  • 19
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • Luca S, Yau WM, Leapman R, Tycko R (2007) Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR. Biochemistry 46: 13505-13522.
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Leapman, R.3    Tycko, R.4
  • 20
    • 34248578409 scopus 로고    scopus 로고
    • Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography
    • Goldie KN, Wedig T, Mitra AK, Aebi U, Herrmann H, et al. (2007) Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography. Journal Of Structural Biology 158: 378-385.
    • (2007) Journal Of Structural Biology , vol.158 , pp. 378-385
    • Goldie, K.N.1    Wedig, T.2    Mitra, A.K.3    Aebi, U.4    Herrmann, H.5
  • 22
    • 0031465967 scopus 로고    scopus 로고
    • New view of protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis T, Karplus M (1997) "New view" of protein folding reconciled with the old through multiple unfolding simulations. Science 278: 1928-1931.
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 27
  • 28
    • 6344291659 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the assembly of intermediate filaments
    • Kreplak L, Aebi U, Herrmann H (2004) Molecular mechanisms underlying the assembly of intermediate filaments. Experimental Cell Research 301: 77-83.
    • (2004) Experimental Cell Research , vol.301 , pp. 77-83
    • Kreplak, L.1    Aebi, U.2    Herrmann, H.3
  • 29
    • 18744388274 scopus 로고    scopus 로고
    • Sequence comparisons of intermediate filament chains: Evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1
    • Smith TA, Strelkov SV, Burkhard P, Aebi U, Parry DAD (2002) Sequence comparisons of intermediate filament chains: Evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1. Journal of Structural Biology 137: 128-145.
    • (2002) Journal of Structural Biology , vol.137 , pp. 128-145
    • Smith, T.A.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4    Parry, D.A.D.5
  • 31
    • 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, Muller 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. Journal of Molecular Biology 264: 933-953.
    • (1996) Journal of Molecular Biology , vol.264 , pp. 933-953
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Muller, S.A.4    Goldie, K.N.5
  • 32
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism
    • Parry DAD, Steinert PM (1999) Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism. Quarterly Reviews of Biophysics 32: 99-187.
    • (1999) Quarterly Reviews of Biophysics , vol.32 , pp. 99-187
    • Parry, D.A.D.1    Steinert, P.M.2
  • 33
    • 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. Journal of Molecular Biology 286: 1403-1420.
    • (1999) Journal of Molecular Biology , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5
  • 34
    • 0041319662 scopus 로고    scopus 로고
    • The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads
    • Fudge DS, Gardner KH, Forsyth VT, Riekel C, Gosline JM (2003) The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads. Biophysical Journal 85: 2015-2027.
    • (2003) Biophysical Journal , vol.85 , pp. 2015-2027
    • Fudge, D.S.1    Gardner, K.H.2    Forsyth, V.T.3    Riekel, C.4    Gosline, J.M.5
  • 36
    • 34548407835 scopus 로고    scopus 로고
    • Superelasticity, energy dissipation and strain hardening of vimentin coiled-coil intermediate filaments: Atomistic and continuum studies
    • Ackbarow T, Buehler MJ (2007) Superelasticity, energy dissipation and strain hardening of vimentin coiled-coil intermediate filaments: Atomistic and continuum studies. Journal of Materials Science 42: 8771-8787.
    • (2007) Journal of Materials Science , vol.42 , pp. 8771-8787
    • Ackbarow, T.1    Buehler, M.J.2
  • 38
    • 33745674667 scopus 로고    scopus 로고
    • Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy
    • Guzman C, Jeney S, Kreplak L, Kasas S, Kulik AJ, et al. (2006) Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy. Journal of Molecular Biology 360: 623-630.
    • (2006) Journal of Molecular Biology , vol.360 , pp. 623-630
    • Guzman, C.1    Jeney, S.2    Kreplak, L.3    Kasas, S.4    Kulik, A.J.5
  • 39
    • 0034029857 scopus 로고    scopus 로고
    • A critical review of the structural mechanics of wool and hair fibres
    • Hearle JWS (2000) A critical review of the structural mechanics of wool and hair fibres. International Journal of Biological Macromolecules 27: 123-138.
    • (2000) International Journal of Biological Macromolecules , vol.27 , pp. 123-138
    • Hearle, J.W.S.1
  • 40
    • 0027533269 scopus 로고
    • Flexural Rigidity of Microtubules and Actin-Filaments Measured from Thermal Fluctuations in Shape
    • Gittes F, Mickey B, Nettleton J, Howard J (1993) Flexural Rigidity of Microtubules and Actin-Filaments Measured from Thermal Fluctuations in Shape. Journal of Cell Biology 120: 923-934.
    • (1993) Journal of Cell Biology , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 41
    • 0035052403 scopus 로고    scopus 로고
    • Unraveling double stranded alpha-helical coiled coils: An x-ray diffraction study on hard alpha-keratin fibers
    • Kreplak L, Doucet J, Briki F (2001) Unraveling double stranded alpha-helical coiled coils: An x-ray diffraction study on hard alpha-keratin fibers. Biopolymers 58: 526-533.
    • (2001) Biopolymers , vol.58 , pp. 526-533
    • Kreplak, L.1    Doucet, J.2    Briki, F.3
  • 42
    • 3042816944 scopus 로고    scopus 로고
    • New aspects of the alpha-helix to beta-sheet transition in stretched hard alpha-keratin fibers
    • Kreplak L, Doucet J, Dumas P, Briki F (2004) New aspects of the alpha-helix to beta-sheet transition in stretched hard alpha-keratin fibers. Biophysical Journal 87: 640-647.
    • (2004) Biophysical Journal , vol.87 , pp. 640-647
    • Kreplak, L.1    Doucet, J.2    Dumas, P.3    Briki, F.4
  • 43
    • 58149352273 scopus 로고    scopus 로고
    • Severe Myopathy Mutations Modify the Nanomechanics of Desmin Intermediate Filaments
    • Kreplak L, Bar H (2009) Severe Myopathy Mutations Modify the Nanomechanics of Desmin Intermediate Filaments. Journal Of Molecular Biology 385: 1043-1051.
    • (2009) Journal Of Molecular Biology , vol.385 , pp. 1043-1051
    • Kreplak, L.1    Bar, H.2
  • 44
    • 0036217572 scopus 로고    scopus 로고
    • A new deformation model of hard alpha-keratin fibers at the nanometer scale: Implications for hard alpha-keratin intermediate filament mechanical properties
    • Kreplak L, Franbourg A, Briki F, Leroy F, Dalle D, et al. (2002) A new deformation model of hard alpha-keratin fibers at the nanometer scale: implications for hard alpha-keratin intermediate filament mechanical properties. Biophys J 82: 2265-2274.
    • (2002) Biophys J , vol.82 , pp. 2265-2274
    • Kreplak, L.1    Franbourg, A.2    Briki, F.3    Leroy, F.4    Dalle, D.5
  • 45
    • 58949097134 scopus 로고    scopus 로고
    • Molecular mechanics of stutter defects in vimentin intermediate filaments
    • Ackbarow T, Buehler MJ (2009) Molecular mechanics of stutter defects in vimentin intermediate filaments. Experimental Mechanics 49: 79-89.
    • (2009) Experimental Mechanics , vol.49 , pp. 79-89
    • Ackbarow, T.1    Buehler, M.J.2
  • 46
    • 40449091784 scopus 로고    scopus 로고
    • Geometric Confinement Governs the Rupture Strength of H-bond Assemblies at a Critical Length Scale
    • Keten S, Buehler MJ (2008) Geometric Confinement Governs the Rupture Strength of H-bond Assemblies at a Critical Length Scale. Nano Letters 8: 743-748.
    • (2008) Nano Letters , vol.8 , pp. 743-748
    • Keten, S.1    Buehler, M.J.2
  • 47
    • 34548319464 scopus 로고    scopus 로고
    • Computational models of molecular self-organization in cellular environments
    • LeDuc P, Schwartz R (2007) Computational models of molecular self-organization in cellular environments. Cell Biochem Biophys 48: 16-31.
    • (2007) Cell Biochem Biophys , vol.48 , pp. 16-31
    • LeDuc, P.1    Schwartz, R.2
  • 48
    • 0034612284 scopus 로고    scopus 로고
    • Unfolding proteins by external forces and temperature: The importance of topology and energetics
    • Paci E, Karplus M (2000) Unfolding proteins by external forces and temperature: the importance of topology and energetics. Proc Natl Acad Sci U S A 97: 6521-6526.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6521-6526
    • Paci, E.1    Karplus, M.2
  • 49
    • 33748153236 scopus 로고    scopus 로고
    • The folding mechanism of collagen-like model peptides explored through detailed molecular simulations
    • Stultz CM (2006) The folding mechanism of collagen-like model peptides explored through detailed molecular simulations. Protein Science 15: 2166-2177.
    • (2006) Protein Science , vol.15 , pp. 2166-2177
    • Stultz, C.M.1
  • 51
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor M, Schulten K (2007) Single-molecule experiments in vitro and in silico. Science 316: 1144-1148.
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 52
    • 43449096360 scopus 로고    scopus 로고
    • Asymptotic strength limit of hydrogen-bond assemblies in proteins at vanishing pulling rates
    • Keten S, Buehler MJ (2008) Asymptotic strength limit of hydrogen-bond assemblies in proteins at vanishing pulling rates. Physical Review Letters 100: 198301.
    • (2008) Physical Review Letters , vol.100 , pp. 198301
    • Keten, S.1    Buehler, M.J.2
  • 53
    • 34547673274 scopus 로고    scopus 로고
    • Mechanical stretching of proteins - a theoretical survey of the Protein Data Bank
    • Sulkowska JI, Cieplak M (2007) Mechanical stretching of proteins - a theoretical survey of the Protein Data Bank. Journal of Physics-Condensed Matter 19: 283201.
    • (2007) Journal of Physics-Condensed Matter , vol.19 , pp. 283201
    • Sulkowska, J.I.1    Cieplak, M.2


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