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Volumn 43, Issue 1, 2010, Pages 15-22

A multi-scale approach to understand the mechanobiology of intermediate filaments

Author keywords

Active remodeling; Molecular slippage; Multi scale modeling; Shear stress; Stretch sensor; Tensile stress

Indexed keywords

ACTIN MICROFILAMENTS; ACTIVE REMODELING; ANIMAL CELLS; CYTOSKELETONS; DOMAIN STRUCTURE; EXPERIMENTAL DATA; IN-VIVO; INTERMEDIATE FILAMENTS; MECHANICAL DESIGN; MECHANICAL FORCE; MECHANICAL INTEGRITY; MECHANO-BIOLOGY; MICROTUBULES; MOLECULAR SLIPPAGE; MULTI-SCALE APPROACHES; MULTI-SCALE MODELING; PASSIVE ELEMENTS;

EID: 72449133271     PISSN: 00219290     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiomech.2009.09.004     Document Type: Article
Times cited : (53)

References (93)
  • 1
    • 36749062973 scopus 로고    scopus 로고
    • Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of alpha-helical and beta-sheet protein domains
    • Ackbarow T., Chen X., et al. Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of alpha-helical and beta-sheet protein domains. Proc. Natl. Acad. Sci. USA 104 42 (2007) 16410-16415
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.42 , pp. 16410-16415
    • Ackbarow, T.1    Chen, X.2
  • 2
    • 67650337244 scopus 로고    scopus 로고
    • Alpha-helical protein networks are self protective and flaw tolerant
    • Ackbarow T., Sen D., et al. Alpha-helical protein networks are self protective and flaw tolerant. PLoS ONE 4 6 (2009) e6015
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Ackbarow, T.1    Sen, D.2
  • 3
    • 0028303541 scopus 로고
    • Cytoskeleton of cartilage cells
    • Benjamin M., Archer C.W., et al. Cytoskeleton of cartilage cells. Microsc. Res. Tech. 28 5 (1994) 372-377
    • (1994) Microsc. Res. Tech. , vol.28 , Issue.5 , pp. 372-377
    • Benjamin, M.1    Archer, C.W.2
  • 4
    • 68349087878 scopus 로고    scopus 로고
    • Atomistically informed mesoscale model of alpha-helical protein domains
    • Bertaud J., Qin Z., et al. Atomistically informed mesoscale model of alpha-helical protein domains. Int. J. Multiscale Comput. Eng 7 3 (2009) 237-250
    • (2009) Int. J. Multiscale Comput. Eng , vol.7 , Issue.3 , pp. 237-250
    • Bertaud, J.1    Qin, Z.2
  • 5
    • 67650558915 scopus 로고    scopus 로고
    • Recruitment of vimentin to the cell surface by {beta}3 integrin and plectin mediates adhesion strength
    • Bhattacharya R., Gonzalez A.M., et al. Recruitment of vimentin to the cell surface by {beta}3 integrin and plectin mediates adhesion strength. J. Cell Sci. (2009)
    • (2009) J. Cell Sci.
    • Bhattacharya, R.1    Gonzalez, A.M.2
  • 6
    • 0030272704 scopus 로고    scopus 로고
    • Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes
    • Bloom S., Lockard V.G., et al. Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes. J. Mol. Cell Cardiol. 28 10 (1996) 2123-2127
    • (1996) J. Mol. Cell Cardiol. , vol.28 , Issue.10 , pp. 2123-2127
    • Bloom, S.1    Lockard, V.G.2
  • 7
    • 49249114201 scopus 로고    scopus 로고
    • Keratin contribution to cellular mechanical stress response at focal adhesions as assayed by laser tweezers
    • Bordeleau F., Bessard J., et al. Keratin contribution to cellular mechanical stress response at focal adhesions as assayed by laser tweezers. Biochem. Cell Biol. 86 4 (2008) 352-359
    • (2008) Biochem. Cell Biol. , vol.86 , Issue.4 , pp. 352-359
    • Bordeleau, F.1    Bessard, J.2
  • 8
    • 34547675884 scopus 로고    scopus 로고
    • Fracture mechanics of protein materials
    • Buehler M.J., and Ackbarow T. Fracture mechanics of protein materials. Mater. Today 10 9 (2007) 46-58
    • (2007) Mater. Today , vol.10 , Issue.9 , pp. 46-58
    • Buehler, M.J.1    Ackbarow, T.2
  • 9
    • 60949107887 scopus 로고    scopus 로고
    • Deformation and failure of protein materials in physiologically extreme conditions and disease
    • Buehler M.J., and Yung Y.C. Deformation and failure of protein materials in physiologically extreme conditions and disease. Nat. Mater. 8 3 (2009) 175-188
    • (2009) Nat. Mater. , vol.8 , Issue.3 , pp. 175-188
    • Buehler, M.J.1    Yung, Y.C.2
  • 10
    • 0019482237 scopus 로고
    • Self-assembly of fibrin monomer. a light scattering and electron microscopic investigation
    • Cavazza B., Cuniberti C., et al. Self-assembly of fibrin monomer. a light scattering and electron microscopic investigation. Ital. J. Biochem. 30 1 (1981) 75-89
    • (1981) Ital. J. Biochem. , vol.30 , Issue.1 , pp. 75-89
    • Cavazza, B.1    Cuniberti, C.2
  • 11
    • 59149084777 scopus 로고    scopus 로고
    • Functions of the nuclear envelope and lamina in development and disease
    • Cohen T.V., Hernandez L., et al. Functions of the nuclear envelope and lamina in development and disease. Biochem. Soc. Trans. 36 Pt 6 (2008) 1329-1334
    • (2008) Biochem. Soc. Trans. , vol.36 , Issue.PART 6 , pp. 1329-1334
    • Cohen, T.V.1    Hernandez, L.2
  • 12
    • 67650541328 scopus 로고    scopus 로고
    • Mechanosensing in actin stress fibers revealed by a close correlation between force and protein localization
    • Colombelli J., Besser A., et al. Mechanosensing in actin stress fibers revealed by a close correlation between force and protein localization. J. Cell Sci. 122 Pt 10 (2009) 1665-1679
    • (2009) J. Cell Sci. , vol.122 , Issue.PART 10 , pp. 1665-1679
    • Colombelli, J.1    Besser, A.2
  • 13
    • 29944445023 scopus 로고    scopus 로고
    • Coupling of the nucleus and cytoplasm: role of the LINC complex
    • Crisp M., Liu Q., et al. Coupling of the nucleus and cytoplasm: role of the LINC complex. J. Cell Biol. 172 1 (2006) 41-53
    • (2006) J. Cell Biol. , vol.172 , Issue.1 , pp. 41-53
    • Crisp, M.1    Liu, Q.2
  • 14
    • 33744483759 scopus 로고    scopus 로고
    • Evaluation of tension in actin bundle of endothelial cells based on preexisting strain and tensile properties measurements
    • Deguchi S., Ohashi T., et al. Evaluation of tension in actin bundle of endothelial cells based on preexisting strain and tensile properties measurements. Mol. Cell Biomech. 2 3 (2005) 125-133
    • (2005) Mol. Cell Biomech. , vol.2 , Issue.3 , pp. 125-133
    • Deguchi, S.1    Ohashi, T.2
  • 15
    • 33749077090 scopus 로고    scopus 로고
    • Tensile properties of single stress fibers isolated from cultured vascular smooth muscle cells
    • Deguchi S., Ohashi T., et al. Tensile properties of single stress fibers isolated from cultured vascular smooth muscle cells. J. Biomech. 39 14 (2006) 2603-2610
    • (2006) J. Biomech. , vol.39 , Issue.14 , pp. 2603-2610
    • Deguchi, S.1    Ohashi, T.2
  • 16
    • 0033571984 scopus 로고    scopus 로고
    • alphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis
    • Djabali K., Piron G., et al. alphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis. Exp. Cell Res. 253 2 (1999) 649-662
    • (1999) Exp. Cell Res. , vol.253 , Issue.2 , pp. 649-662
    • Djabali, K.1    Piron, G.2
  • 17
    • 42749104581 scopus 로고    scopus 로고
    • Scaling the microrheology of living cells
    • Fabry B., Maksym G.N., et al. Scaling the microrheology of living cells. Phys. Rev. Lett. 87 14 (2001) 148102
    • (2001) Phys. Rev. Lett. , vol.87 , Issue.14 , pp. 148102
    • Fabry, B.1    Maksym, G.N.2
  • 18
    • 68549096323 scopus 로고    scopus 로고
    • Insights into the mechanical properties of epithelial cells: the effects of shear stress on the assembly and remodeling of keratin intermediate filaments
    • Flitney E.W., Kuczmarski E.R., et al. Insights into the mechanical properties of epithelial cells: the effects of shear stress on the assembly and remodeling of keratin intermediate filaments. FASEB J. 23 7 (2009) 2110-2119
    • (2009) FASEB J. , vol.23 , Issue.7 , pp. 2110-2119
    • Flitney, E.W.1    Kuczmarski, E.R.2
  • 19
    • 0028283501 scopus 로고
    • Intermediate filaments: structure, dynamics, function, and disease
    • Fuchs E., and Weber K. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63 (1994) 345-382
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 20
    • 48449103125 scopus 로고    scopus 로고
    • The intermediate filament network in cultured human keratinocytes is remarkably extensible and resilient
    • Fudge D., Russell D., et al. The intermediate filament network in cultured human keratinocytes is remarkably extensible and resilient. PLoS ONE 3 6 (2008) e2327
    • (2008) PLoS ONE , vol.3 , Issue.6
    • Fudge, D.1    Russell, D.2
  • 21
    • 0041319662 scopus 로고    scopus 로고
    • The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads
    • Fudge D.S., Gardner K.H., et al. The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads. Biophys. J. 85 3 (2003) 2015-2027
    • (2003) Biophys. J. , vol.85 , Issue.3 , pp. 2015-2027
    • Fudge, D.S.1    Gardner, K.H.2
  • 22
    • 58249086114 scopus 로고    scopus 로고
    • Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed
    • Gardel M.L., Sabass B., et al. Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed. J. Cell Biol. 183 6 (2008) 999-1005
    • (2008) J. Cell Biol. , vol.183 , Issue.6 , pp. 999-1005
    • Gardel, M.L.1    Sabass, B.2
  • 23
    • 39849097562 scopus 로고    scopus 로고
    • Desmosome structure, composition and function
    • Garrod D., and Chidgey M. Desmosome structure, composition and function. Biochim. Biophys. Acta 1778 3 (2008) 572-587
    • (2008) Biochim. Biophys. Acta , vol.1778 , Issue.3 , pp. 572-587
    • Garrod, D.1    Chidgey, M.2
  • 24
    • 59149083058 scopus 로고    scopus 로고
    • Near-UV circular dichroism reveals structural transitions of vimentin subunits during intermediate filament assembly
    • Georgakopoulou S., Moller D., et al. Near-UV circular dichroism reveals structural transitions of vimentin subunits during intermediate filament assembly. J. Mol. Biol. 386 2 (2009) 544-553
    • (2009) J. Mol. Biol. , vol.386 , Issue.2 , pp. 544-553
    • Georgakopoulou, S.1    Moller, D.2
  • 25
    • 0037113967 scopus 로고    scopus 로고
    • The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton
    • Haddad L.A., Smith N., et al. The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton. J. Biol. Chem. 277 46 (2002) 44180-44186
    • (2002) J. Biol. Chem. , vol.277 , Issue.46 , pp. 44180-44186
    • Haddad, L.A.1    Smith, N.2
  • 26
    • 0033621703 scopus 로고    scopus 로고
    • AlphaB-crystallin regulates intermediate filament organization in situ
    • Head M.W., Hurwitz L., et al. AlphaB-crystallin regulates intermediate filament organization in situ. Neuroreport 11 2 (2000) 361-365
    • (2000) Neuroreport , vol.11 , Issue.2 , pp. 361-365
    • Head, M.W.1    Hurwitz, L.2
  • 27
    • 0037630089 scopus 로고    scopus 로고
    • Lamin mutations come of age
    • Hegele R.A. Lamin mutations come of age. Nat. Med. 9 6 (2003) 644-645
    • (2003) Nat. Med. , vol.9 , Issue.6 , pp. 644-645
    • Hegele, R.A.1
  • 28
    • 36849027690 scopus 로고    scopus 로고
    • Phenomics, lamin A/C, and metabolic disease
    • Hegele R.A. Phenomics, lamin A/C, and metabolic disease. J. Clin. Endocrinol. Metab. 92 12 (2007) 4566-4568
    • (2007) J. Clin. Endocrinol. Metab. , vol.92 , Issue.12 , pp. 4566-4568
    • Hegele, R.A.1
  • 29
    • 0034647012 scopus 로고    scopus 로고
    • Rapid displacement of vimentin intermediate filaments in living endothelial cells exposed to flow
    • Helmke B.P., Goldman R.D., et al. Rapid displacement of vimentin intermediate filaments in living endothelial cells exposed to flow. Circ. Res. 86 7 (2000) 745-752
    • (2000) Circ. Res. , vol.86 , Issue.7 , pp. 745-752
    • Helmke, B.P.1    Goldman, R.D.2
  • 30
    • 0035139085 scopus 로고    scopus 로고
    • Spatiotemporal analysis of flow-induced intermediate filament displacement in living endothelial cells
    • Helmke B.P., Thakker D.B., et al. Spatiotemporal analysis of flow-induced intermediate filament displacement in living endothelial cells. Biophys. J. 80 1 (2001) 184-194
    • (2001) Biophys. J. , vol.80 , Issue.1 , pp. 184-194
    • Helmke, B.P.1    Thakker, D.B.2
  • 31
    • 34250880140 scopus 로고    scopus 로고
    • Intermediate filaments: from cell architecture to nanomechanics
    • Herrmann H., Bar H., et al. Intermediate filaments: from cell architecture to nanomechanics. Nat. Rev. Mol. Cell Biol. 8 7 (2007) 562-573
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , Issue.7 , pp. 562-573
    • Herrmann, H.1    Bar, H.2
  • 32
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann H., Haner M., et al. Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286 5 (1999) 1403-1420
    • (1999) J. Mol. Biol. , vol.286 , Issue.5 , pp. 1403-1420
    • Herrmann, H.1    Haner, M.2
  • 33
    • 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., et al. Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J. Mol. Biol. 264 5 (1996) 933-953
    • (1996) J. Mol. Biol. , vol.264 , Issue.5 , pp. 933-953
    • Herrmann, H.1    Haner, M.2
  • 34
    • 7244221578 scopus 로고    scopus 로고
    • Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance
    • Hess J.F., Budamagunta M.S., et al. Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance. J. Biol. Chem. 279 43 (2004) 44841-44846
    • (2004) J. Biol. Chem. , vol.279 , Issue.43 , pp. 44841-44846
    • Hess, J.F.1    Budamagunta, M.S.2
  • 35
    • 44449140379 scopus 로고    scopus 로고
    • Providing cellular signposts-post-translational modifications of intermediate filaments
    • Hyder C.L., Pallari H.M., et al. Providing cellular signposts-post-translational modifications of intermediate filaments. FEBS Lett. 582 14 (2008) 2140-2148
    • (2008) FEBS Lett. , vol.582 , Issue.14 , pp. 2140-2148
    • Hyder, C.L.1    Pallari, H.M.2
  • 36
    • 0027221483 scopus 로고
    • Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton
    • Ingber D.E. Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 104 Pt 3 (1993) 613-627
    • (1993) J. Cell Sci. , vol.104 , Issue.PART 3 , pp. 613-627
    • Ingber, D.E.1
  • 37
    • 0014335827 scopus 로고
    • Mitosis and intermediate-sized filaments in developing skeletal muscle
    • Ishikawa H., Bischoff R., et al. Mitosis and intermediate-sized filaments in developing skeletal muscle. J. Cell Biol. 38 (1968) 538-555
    • (1968) J. Cell Biol. , vol.38 , pp. 538-555
    • Ishikawa, H.1    Bischoff, R.2
  • 38
    • 40449091784 scopus 로고    scopus 로고
    • Geometric confinement governs the rupture strength of H-bond assemblies at a critical length scale
    • Keten S., and Buehler M.J. Geometric confinement governs the rupture strength of H-bond assemblies at a critical length scale. Nano Lett. 8 2 (2008) 743-748
    • (2008) Nano Lett. , vol.8 , Issue.2 , pp. 743-748
    • Keten, S.1    Buehler, M.J.2
  • 39
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm
    • Kim S., and Coulombe P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 21 13 (2007) 1581-1597
    • (2007) Genes Dev. , vol.21 , Issue.13 , pp. 1581-1597
    • Kim, S.1    Coulombe, P.A.2
  • 40
    • 34948845678 scopus 로고    scopus 로고
    • Interaction between the keratin cytoskeleton and eEF1Bgamma affects protein synthesis in epithelial cells
    • Kim S., Kellner J., et al. Interaction between the keratin cytoskeleton and eEF1Bgamma affects protein synthesis in epithelial cells. Nat. Struct. Mol. Biol. 14 10 (2007) 982-983
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , Issue.10 , pp. 982-983
    • Kim, S.1    Kellner, J.2
  • 41
    • 34250867157 scopus 로고    scopus 로고
    • A quantitative kinetic model for the in vitro assembly of intermediate filaments from tetrameric vimentin
    • Kirmse R., Portet S., et al. A quantitative kinetic model for the in vitro assembly of intermediate filaments from tetrameric vimentin. J. Biol. Chem. 282 25 (2007) 18563-18572
    • (2007) J. Biol. Chem. , vol.282 , Issue.25 , pp. 18563-18572
    • Kirmse, R.1    Portet, S.2
  • 42
    • 6344291659 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the assembly of intermediate filaments
    • Kreplak L., Aebi U., et al. Molecular mechanisms underlying the assembly of intermediate filaments. Exp. Cell Res. 301 1 (2004) 77-83
    • (2004) Exp. Cell Res. , vol.301 , Issue.1 , pp. 77-83
    • Kreplak, L.1    Aebi, U.2
  • 43
    • 58149352273 scopus 로고    scopus 로고
    • Severe myopathy mutations modify the nanomechanics of desmin intermediate filaments
    • Kreplak L., and Bar H. Severe myopathy mutations modify the nanomechanics of desmin intermediate filaments. J. Mol. Biol. 385 4 (2009) 1043-1051
    • (2009) J. Mol. Biol. , vol.385 , Issue.4 , pp. 1043-1051
    • Kreplak, L.1    Bar, H.2
  • 44
    • 27744588225 scopus 로고    scopus 로고
    • Exploring the mechanical behavior of single intermediate filaments
    • Kreplak L., Bar H., et al. Exploring the mechanical behavior of single intermediate filaments. J. Mol. Biol. 354 3 (2005) 569-577
    • (2005) J. Mol. Biol. , vol.354 , Issue.3 , pp. 569-577
    • Kreplak, L.1    Bar, H.2
  • 45
    • 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., et al. New aspects of the alpha-helix to beta-sheet transition in stretched hard alpha-keratin fibers. Biophys. J. 87 1 (2004) 640-647
    • (2004) Biophys. J. , vol.87 , Issue.1 , pp. 640-647
    • Kreplak, L.1    Doucet, J.2
  • 46
    • 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., et al. 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 4 (2002) 2265-2274
    • (2002) Biophys. J. , vol.82 , Issue.4 , pp. 2265-2274
    • Kreplak, L.1    Franbourg, A.2
  • 47
    • 33846628445 scopus 로고    scopus 로고
    • Biomechanical properties of intermediate filaments: from tissues to single filaments and back
    • Kreplak L., and Fudge D. Biomechanical properties of intermediate filaments: from tissues to single filaments and back. Bioessays 29 1 (2007) 26-35
    • (2007) Bioessays , vol.29 , Issue.1 , pp. 26-35
    • Kreplak, L.1    Fudge, D.2
  • 48
    • 41649116913 scopus 로고    scopus 로고
    • Tensile properties of single desmin intermediate filaments
    • Kreplak L., Herrmann H., et al. Tensile properties of single desmin intermediate filaments. Biophys. J. 94 7 (2008) 2790-2799
    • (2008) Biophys. J. , vol.94 , Issue.7 , pp. 2790-2799
    • Kreplak, L.1    Herrmann, H.2
  • 49
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • Lazarides E. Intermediate filaments as mechanical integrators of cellular space. Nature 283 5744 (1980) 249-256
    • (1980) Nature , vol.283 , Issue.5744 , pp. 249-256
    • Lazarides, E.1
  • 50
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis T., and Karplus M. Effective energy function for proteins in solution. Proteins 35 2 (1999) 133-152
    • (1999) Proteins , vol.35 , Issue.2 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 51
    • 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 M.K., Nahirney P.C., et al. Concentric intermediate filament lattice links to specialized Z-band junctional complexes in sonic muscle fibers of the type I male midshipman fish. J. Struct. Biol. 143 1 (2003) 56-71
    • (2003) J. Struct. Biol. , vol.143 , Issue.1 , pp. 56-71
    • Lewis, M.K.1    Nahirney, P.C.2
  • 52
    • 0035142293 scopus 로고    scopus 로고
    • Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7
    • Lin L., Holbro T., et al. Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7. J. Cell Biochem. 80 4 (2001) 483-490
    • (2001) J. Cell Biochem. , vol.80 , Issue.4 , pp. 483-490
    • Lin, L.1    Holbro, T.2
  • 53
    • 0032438942 scopus 로고    scopus 로고
    • Keratin filament deployment and cytoskeletal networking in a sensory epithelium that vibrates during hearing
    • Mogensen M.M., Henderson C.G., et al. Keratin filament deployment and cytoskeletal networking in a sensory epithelium that vibrates during hearing. Cell Motil. Cytoskeleton 41 2 (1998) 138-153
    • (1998) Cell Motil. Cytoskeleton , vol.41 , Issue.2 , pp. 138-153
    • Mogensen, M.M.1    Henderson, C.G.2
  • 54
    • 5144230784 scopus 로고    scopus 로고
    • Assessing the flexibility of intermediate filaments by atomic force microscopy
    • Mucke N., Kreplak L., et al. Assessing the flexibility of intermediate filaments by atomic force microscopy. J. Mol. Biol. 335 5 (2004) 1241-1250
    • (2004) J. Mol. Biol. , vol.335 , Issue.5 , pp. 1241-1250
    • Mucke, N.1    Kreplak, L.2
  • 55
    • 2942565983 scopus 로고    scopus 로고
    • Molecular and biophysical characterization of assembly-starter units of human vimentin
    • Mucke N., Wedig T., et al. Molecular and biophysical characterization of assembly-starter units of human vimentin. J. Mol. Biol. 340 1 (2004) 97-114
    • (2004) J. Mol. Biol. , vol.340 , Issue.1 , pp. 97-114
    • Mucke, N.1    Wedig, T.2
  • 56
    • 65649130513 scopus 로고    scopus 로고
    • Plectin contributes to mechanical properties of living cells
    • Na S., Chowdhury F., et al. Plectin contributes to mechanical properties of living cells. Am. J. Physiol. Cell Physiol. 296 4 (2009) C868-C877
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296 , Issue.4
    • Na, S.1    Chowdhury, F.2
  • 57
    • 0032950844 scopus 로고    scopus 로고
    • Biology and function of hemidesmosomes
    • Nievers M.G., Schaapveld R.Q., et al. Biology and function of hemidesmosomes. Matrix Biol. 18 1 (1999) 5-17
    • (1999) Matrix Biol. , vol.18 , Issue.1 , pp. 5-17
    • Nievers, M.G.1    Schaapveld, R.Q.2
  • 58
    • 60749134035 scopus 로고    scopus 로고
    • The LINC-less granulocyte nucleus
    • Olins A.L., Hoang T.V., et al. The LINC-less granulocyte nucleus. Eur. J. Cell Biol. 88 4 (2009) 203-214
    • (2009) Eur. J. Cell Biol. , vol.88 , Issue.4 , pp. 203-214
    • Olins, A.L.1    Hoang, T.V.2
  • 59
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • Omary M.B., Coulombe P.A., et al. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351 20 (2004) 2087-2100
    • (2004) N. Engl. J. Med. , vol.351 , Issue.20 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2
  • 60
    • 33745873555 scopus 로고    scopus 로고
    • "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights
    • Omary M.B., Ku N.O., et al. "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights. Trends Biochem. Sci. 31 7 (2006) 383-394
    • (2006) Trends Biochem. Sci. , vol.31 , Issue.7 , pp. 383-394
    • Omary, M.B.1    Ku, N.O.2
  • 61
    • 34248182865 scopus 로고    scopus 로고
    • Intermediate filaments as signaling platforms
    • Pallari H.M., and Eriksson J.E. Intermediate filaments as signaling platforms. Sci. STKE 2006 366 (2006) pe53
    • (2006) Sci. STKE , vol.2006 , Issue.366
    • Pallari, H.M.1    Eriksson, J.E.2
  • 62
    • 34249750035 scopus 로고    scopus 로고
    • Towards a molecular description of intermediate filament structure and assembly
    • Parry D.A., Strelkov S.V., et al. Towards a molecular description of intermediate filament structure and assembly. Exp. Cell Res. 313 10 (2007) 2204-2216
    • (2007) Exp. Cell Res. , vol.313 , Issue.10 , pp. 2204-2216
    • Parry, D.A.1    Strelkov, S.V.2
  • 63
    • 70350248115 scopus 로고    scopus 로고
    • Robustness-strength performance of hierachical alpha-helical protein filaments
    • Qin Z., Cranford S., et al. Robustness-strength performance of hierachical alpha-helical protein filaments. Int. J. Appl. Mech. 1 1 (2009) 85-112
    • (2009) Int. J. Appl. Mech. , vol.1 , Issue.1 , pp. 85-112
    • Qin, Z.1    Cranford, S.2
  • 65
    • 70349662344 scopus 로고    scopus 로고
    • Nanomechanical properties of vimentin intermediate filament dimers
    • Qin Z., Kreplak L., et al. Nanomechanical properties of vimentin intermediate filament dimers. Nanotechnology 20 42 (2009) 425101
    • (2009) Nanotechnology , vol.20 , Issue.42 , pp. 425101
    • Qin, Z.1    Kreplak, L.2
  • 66
    • 24044510445 scopus 로고    scopus 로고
    • Keratin 8 phosphorylation by protein kinase C delta regulates shear stress-mediated disassembly of keratin intermediate filaments in alveolar epithelial cells
    • Ridge K.M., Linz L., et al. Keratin 8 phosphorylation by protein kinase C delta regulates shear stress-mediated disassembly of keratin intermediate filaments in alveolar epithelial cells. J. Biol. Chem. 280 34 (2005) 30400-30405
    • (2005) J. Biol. Chem. , vol.280 , Issue.34 , pp. 30400-30405
    • Ridge, K.M.1    Linz, L.2
  • 67
    • 33646172749 scopus 로고    scopus 로고
    • Coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and alpha-helices of myosin
    • Root D.D., Yadavalli V.K., et al. Coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and alpha-helices of myosin. Biophys. J. 90 8 (2006) 2852-2866
    • (2006) Biophys. J. , vol.90 , Issue.8 , pp. 2852-2866
    • Root, D.D.1    Yadavalli, V.K.2
  • 68
    • 0036977558 scopus 로고    scopus 로고
    • The myosin coiled-coil is a truly elastic protein structure
    • Schwaiger I., Sattler C., et al. The myosin coiled-coil is a truly elastic protein structure. Nat. Mater. 1 4 (2002) 232-235
    • (2002) Nat. Mater. , vol.1 , Issue.4 , pp. 232-235
    • Schwaiger, I.1    Sattler, C.2
  • 69
    • 0026442554 scopus 로고
    • Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers
    • Seifert G.J., Lawson D., et al. Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers. Eur. J. Cell Biol. 59 1 (1992) 138-147
    • (1992) Eur. J. Cell Biol. , vol.59 , Issue.1 , pp. 138-147
    • Seifert, G.J.1    Lawson, D.2
  • 70
    • 38949216806 scopus 로고    scopus 로고
    • Micromechanical properties of keratin intermediate filament networks
    • Sivaramakrishnan S., DeGiulio J.V., et al. Micromechanical properties of keratin intermediate filament networks. Proc. Natl. Acad. Sci. USA 105 3 (2008) 889-894
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.3 , pp. 889-894
    • Sivaramakrishnan, S.1    DeGiulio, J.V.2
  • 71
    • 66349108388 scopus 로고    scopus 로고
    • Shear stress induced reorganization of the keratin intermediate filament network requires phosphorylation by PKC {zeta}
    • Sivaramakrishnan S., Schneider J.L., et al. Shear stress induced reorganization of the keratin intermediate filament network requires phosphorylation by PKC {zeta}. Mol. Biol. Cell 20 11 (2009) 2755-2765
    • (2009) Mol. Biol. Cell , vol.20 , Issue.11 , pp. 2755-2765
    • Sivaramakrishnan, S.1    Schneider, J.L.2
  • 72
    • 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 T.A., Strelkov S.V., et al. Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1. J. Struct. Biol. 137 1-2 (2002) 128-145
    • (2002) J. Struct. Biol. , vol.137 , Issue.1-2 , pp. 128-145
    • Smith, T.A.1    Strelkov, S.V.2
  • 73
    • 33750843407 scopus 로고    scopus 로고
    • Monitoring intermediate filament assembly by small-angle X-ray scattering reveals the molecular architecture of assembly intermediates
    • Sokolova A.V., Kreplak L., et al. Monitoring intermediate filament assembly by small-angle X-ray scattering reveals the molecular architecture of assembly intermediates. Proc. Natl. Acad. Sci. USA 103 44 (2006) 16206-16211
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.44 , pp. 16206-16211
    • Sokolova, A.V.1    Kreplak, L.2
  • 74
    • 64149095084 scopus 로고    scopus 로고
    • Stretching, unfolding, and deforming protein filaments adsorbed at solid-liquid interfaces using the tip of an atomic-force microscope
    • Staple D., Loparic M., et al. Stretching, unfolding, and deforming protein filaments adsorbed at solid-liquid interfaces using the tip of an atomic-force microscope. Phys. Rev. Lett. 102 (2009) 128302
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 128302
    • Staple, D.1    Loparic, M.2
  • 75
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments.
    • Steinert P.M., Marekov L.N., et al. Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J. Biol. Chem. 268 33 (1993) 24916-24925
    • (1993) J. Biol. Chem. , vol.268 , Issue.33 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2
  • 76
    • 42649137624 scopus 로고    scopus 로고
    • Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness
    • Stewart-Hutchinson P.J., Hale C.M., et al. Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness. Exp. Cell Res. 314 8 (2008) 1892-1905
    • (2008) Exp. Cell Res. , vol.314 , Issue.8 , pp. 1892-1905
    • Stewart-Hutchinson, P.J.1    Hale, C.M.2
  • 77
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • Strelkov S.V., Herrmann H., et al. Molecular architecture of intermediate filaments. Bioessays 25 3 (2003) 243-251
    • (2003) Bioessays , vol.25 , Issue.3 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2
  • 78
    • 0035793704 scopus 로고    scopus 로고
    • Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments
    • Strelkov S.V., Herrmann H., et al. Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J. Mol. Biol. 306 4 (2001) 773-781
    • (2001) J. Mol. Biol. , vol.306 , Issue.4 , pp. 773-781
    • Strelkov, S.V.1    Herrmann, H.2
  • 79
    • 33748175926 scopus 로고    scopus 로고
    • Lamin A/C and cardiac diseases
    • Sylvius N., and Tesson F. Lamin A/C and cardiac diseases. Curr. Opin. Cardiol. 21 3 (2006) 159-165
    • (2006) Curr. Opin. Cardiol. , vol.21 , Issue.3 , pp. 159-165
    • Sylvius, N.1    Tesson, F.2
  • 80
    • 0032455645 scopus 로고    scopus 로고
    • Colocalization of single ribosomes with intermediate filaments in puromycin-treated and serum-starved mouse embryo fibroblasts
    • Traub P., Bauer C., et al. Colocalization of single ribosomes with intermediate filaments in puromycin-treated and serum-starved mouse embryo fibroblasts. Biol. Cell 90 4 (1998) 319-337
    • (1998) Biol. Cell , vol.90 , Issue.4 , pp. 319-337
    • Traub, P.1    Bauer, C.2
  • 81
    • 0027468175 scopus 로고
    • Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage
    • Troyanovsky S.M., Eshkind L.G., et al. Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage. Cell 72 4 (1993) 561-574
    • (1993) Cell , vol.72 , Issue.4 , pp. 561-574
    • Troyanovsky, S.M.1    Eshkind, L.G.2
  • 82
    • 33644866797 scopus 로고    scopus 로고
    • Stress response role of small GTPases in endothelial Cytoskeletal dynamics and the shear
    • Tzima E. Stress response role of small GTPases in endothelial Cytoskeletal dynamics and the shear. Circ. Res. 98 (2006) 176-185
    • (2006) Circ. Res. , vol.98 , pp. 176-185
    • Tzima, E.1
  • 83
    • 0037183491 scopus 로고    scopus 로고
    • Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy
    • van der Kooi A.J., Bonne G., et al. Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy. Neurology 59 4 (2002) 620-623
    • (2002) Neurology , vol.59 , Issue.4 , pp. 620-623
    • van der Kooi, A.J.1    Bonne, G.2
  • 84
    • 34250166469 scopus 로고    scopus 로고
    • Lamins and lamin-associated proteins in aging and disease
    • Vlcek S., and Foisner R. Lamins and lamin-associated proteins in aging and disease. Curr. Opin. Cell Biol. 19 3 (2007) 298-304
    • (2007) Curr. Opin. Cell Biol. , vol.19 , Issue.3 , pp. 298-304
    • Vlcek, S.1    Foisner, R.2
  • 85
    • 0027189534 scopus 로고
    • Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring
    • Wang K., McCarter R., et al. Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring. Biophys. J. 64 4 (1993) 1161-1177
    • (1993) Biophys. J. , vol.64 , Issue.4 , pp. 1161-1177
    • Wang, K.1    McCarter, R.2
  • 86
    • 0020639339 scopus 로고
    • A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle
    • Wang K., and Ramirez-Mitchell R. A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle. J. Cell Biol. 96 2 (1983) 562-570
    • (1983) J. Cell Biol. , vol.96 , Issue.2 , pp. 562-570
    • Wang, K.1    Ramirez-Mitchell, R.2
  • 87
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • Wang N., Butler J.P., et al. Mechanotransduction across the cell surface and through the cytoskeleton. Science 260 5111 (1993) 1124-1127
    • (1993) Science , vol.260 , Issue.5111 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2
  • 88
    • 0033855271 scopus 로고    scopus 로고
    • Contribution of intermediate filaments to cell stiffness, stiffening, and growth
    • Wang N., and Stamenovic D. Contribution of intermediate filaments to cell stiffness, stiffening, and growth. Am. J. Physiol. Cell Physiol. 279 1 (2000) C188-C194
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279 , Issue.1
    • Wang, N.1    Stamenovic, D.2
  • 89
    • 0037569616 scopus 로고    scopus 로고
    • Mechanics of vimentin intermediate filaments
    • Wang N., and Stamenovic D. Mechanics of vimentin intermediate filaments. J. Muscle Res. Cell Motil. 23 5-6 (2002) 535-540
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , Issue.5-6 , pp. 535-540
    • Wang, N.1    Stamenovic, D.2
  • 90
    • 28544437813 scopus 로고    scopus 로고
    • Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
    • Wilhelmsen K., Litjens S.H., et al. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J. Cell Biol. 171 5 (2005) 799-810
    • (2005) J. Cell Biol. , vol.171 , Issue.5 , pp. 799-810
    • Wilhelmsen, K.1    Litjens, S.H.2
  • 91
    • 45349095416 scopus 로고    scopus 로고
    • Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape
    • Winter L., Abrahamsberg C., et al. Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape. J. Cell Biol. 181 6 (2008) 903-911
    • (2008) J. Cell Biol. , vol.181 , Issue.6 , pp. 903-911
    • Winter, L.1    Abrahamsberg, C.2
  • 92
    • 0015847573 scopus 로고
    • The self-assembly of collagen molecules
    • Yuan L., and Veis A. The self-assembly of collagen molecules. Biopolymers 12 6 (1973) 1437-1444
    • (1973) Biopolymers , vol.12 , Issue.6 , pp. 1437-1444
    • Yuan, L.1    Veis, A.2
  • 93
    • 67649399290 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of cardiac titin's N2B element-effects of the molecular chaperone alpha B-crystallin with disease causing mutations
    • Zhu Y., Boglomovas J., et al. Single molecule force spectroscopy of cardiac titin's N2B element-effects of the molecular chaperone alpha B-crystallin with disease causing mutations. J. Biol. Chem. 284 20 (2009) 13914-13923
    • (2009) J. Biol. Chem. , vol.284 , Issue.20 , pp. 13914-13923
    • Zhu, Y.1    Boglomovas, J.2


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