메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Mechanical forces regulate the interactions of fibronectin and collagen i in extracellular matrix

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; COLLAGEN TYPE 1; FIBRONECTIN; HYDROXYPROLINE; PEPTIDE; R1R2 PEPTIDE; UNCLASSIFIED DRUG;

EID: 84939447610     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9026     Document Type: Article
Times cited : (253)

References (67)
  • 1
    • 77951234989 scopus 로고    scopus 로고
    • The extracellular matrix in development and morphogenesis: A dynamic view
    • Rozario, T. & DeSimone, D. W. The extracellular matrix in development and morphogenesis: a dynamic view. Dev. Biol. 341, 126-140 (2010).
    • (2010) Dev. Biol , vol.341 , pp. 126-140
    • Rozario, T.1    DeSimone, D.W.2
  • 2
    • 77956611459 scopus 로고    scopus 로고
    • Physico-mechanical aspects of extracellular matrix influences on tumorigenic behaviors
    • Cukierman, E. & Bassi, D. E. Physico-mechanical aspects of extracellular matrix influences on tumorigenic behaviors. Semin. Cancer Biol. 20, 139-145 (2010).
    • (2010) Semin. Cancer Biol , vol.20 , pp. 139-145
    • Cukierman, E.1    Bassi, D.E.2
  • 3
    • 77957221459 scopus 로고    scopus 로고
    • Dynamic interplay between the collagen scaffold and tumor evolution
    • Egeblad, M., Rasch, M. G. & Weaver, V. M. Dynamic interplay between the collagen scaffold and tumor evolution. Curr. Opin. Cell Biol. 22, 697-706 (2010).
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 697-706
    • Egeblad, M.1    Rasch, M.G.2    Weaver, V.M.3
  • 4
    • 84863862833 scopus 로고    scopus 로고
    • Mammary gland ECM remodeling, stiffness, and mechanosignaling in normal development and tumor progression
    • Schedin, P. & Keely, P. J. Mammary gland ECM remodeling, stiffness, and mechanosignaling in normal development and tumor progression. Cold Spring Harb. Perspect Biol. 3, a003228 (2011).
    • (2011) Cold Spring Harb. Perspect Biol , vol.3 , pp. a003228
    • Schedin, P.1    Keely, P.J.2
  • 5
    • 84894565577 scopus 로고    scopus 로고
    • Insidious changes in stromal matrix fuel cancer progression
    • Miles, F. L. & Sikes, R. A. Insidious changes in stromal matrix fuel cancer progression. Mol. Cancer Res. 12, 297-312 (2014).
    • (2014) Mol. Cancer Res , vol.12 , pp. 297-312
    • Miles, F.L.1    Sikes, R.A.2
  • 6
    • 67650763823 scopus 로고    scopus 로고
    • Fibronectins in vascular morphogenesis
    • Astrof, S. & Hynes, R. O. Fibronectins in vascular morphogenesis. Angiogenesis 12, 165-175 (2009).
    • (2009) Angiogenesis , vol.12 , pp. 165-175
    • Astrof, S.1    Hynes, R.O.2
  • 8
    • 47749139256 scopus 로고    scopus 로고
    • Cancer as an overhealing wound: An old hypothesis revisited
    • Schafer, M. & Werner, S. Cancer as an overhealing wound: an old hypothesis revisited. Nat. Rev. Mol. Cell Biol. 9, 628-638 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 628-638
    • Schafer, M.1    Werner, S.2
  • 9
    • 84863748841 scopus 로고    scopus 로고
    • Wound repair and regeneration
    • Reinke, J. M. & Sorg, H. Wound repair and regeneration. Eur. Surg. Res. 49, 35 (2012).
    • (2012) Eur. Surg. Res , vol.49 , pp. 35
    • Reinke, J.M.1    Sorg, H.2
  • 10
    • 84879458462 scopus 로고    scopus 로고
    • Regulation of tissue fibrosis by the biomechanical environment
    • Carver, W. & Goldsmith, E. C. Regulation of tissue fibrosis by the biomechanical environment. BioMed Res. Int. 2013, 10 (2013).
    • (2013) BioMed Res. Int , vol.2013 , pp. 10
    • Carver, W.1    Goldsmith, E.C.2
  • 11
    • 50849145156 scopus 로고    scopus 로고
    • Collagen fibrillogenesis: Fibronectin, integrins, and minor collagens as organizers and nucleators
    • Kadler, K. E., Hill, A. & Canty-Laird, E. G. Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators. Curr. Opin. Cell Biol. 20, 495-501 (2008).
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 495-501
    • Kadler, K.E.1    Hill, A.2    Canty-Laird, E.G.3
  • 12
    • 84862702111 scopus 로고    scopus 로고
    • Engineering biomaterials to integrate and heal: The biocompatibility paradigm shifts
    • Bryers, J. D., Giachelli, C. M. & Ratner, B. D. Engineering biomaterials to integrate and heal: the biocompatibility paradigm shifts. Biotechnol. Bioeng. 109, 1898-1911 (2012).
    • (2012) Biotechnol. Bioeng , vol.109 , pp. 1898-1911
    • Bryers, J.D.1    Giachelli, C.M.2    Ratner, B.D.3
  • 14
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting force into biochemical signals
    • Vogel, V. Mechanotransduction involving multimodular proteins: converting force into biochemical signals. Annu. Rev. Biophys. Biomol. Struct. 35, 459-488 (2006).
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 459-488
    • Vogel, V.1
  • 15
    • 79955441991 scopus 로고    scopus 로고
    • Balancing forces: Architectural control of mechanotransduction
    • Dufort, C. C., Paszek, M. J. & Weaver, V. M. Balancing forces: architectural control of mechanotransduction. Nat. Rev. Mol. Cell Biol. 12, 308-319 (2011).
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 308-319
    • Dufort, C.C.1    Paszek, M.J.2    Weaver, V.M.3
  • 17
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C. et al. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551 (1998).
    • (1998) J. Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1
  • 18
    • 0033515070 scopus 로고    scopus 로고
    • Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein
    • Ohashi, T., Kiehart, D. P. & Erickson, H. P. Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein. Proc. Natl Acad. Sci. USA 96, 2153-2158 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2153-2158
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 19
    • 45049084735 scopus 로고    scopus 로고
    • Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage
    • Little, W. C., Smith, M. L., Ebneter, U. & Vogel, V. Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage. Matrix Biol. 27, 451-461 (2008).
    • (2008) Matrix Biol , vol.27 , pp. 451-461
    • Little, W.C.1    Smith, M.L.2    Ebneter, U.3    Vogel, V.4
  • 20
    • 21444434608 scopus 로고    scopus 로고
    • Fibronectin regulates latent transforming growth factor-beta (TGF beta) by controlling matrix assembly of latent TGF beta-binding protein-1
    • Dallas, S. L. et al. Fibronectin regulates latent transforming growth factor-beta (TGF beta) by controlling matrix assembly of latent TGF beta-binding protein-1. J. Biol. Chem. 280, 18871-18880 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 18871-18880
    • Dallas, S.L.1
  • 21
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx, G., Baugh, L. & Vogel, V. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc. Natl Acad. Sci. USA 99, 5139-5143 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 22
    • 70849127367 scopus 로고    scopus 로고
    • Fibronectin forms the most extensible biological fibers displaying switchable force-exposed cryptic binding sites
    • Klotzsch, E. et al. Fibronectin forms the most extensible biological fibers displaying switchable force-exposed cryptic binding sites. Proc. Natl Acad. Sci. USA 106, 18267-18272 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18267-18272
    • Klotzsch, E.1
  • 23
    • 35648954122 scopus 로고    scopus 로고
    • Force-induced unfolding of fibronectin in the extracellular matrix of living cells
    • Smith, M. L. et al. Force-induced unfolding of fibronectin in the extracellular matrix of living cells. PLoS Biol. 5, e268 (2007).
    • (2007) PLoS Biol , vol.5 , pp. e268
    • Smith, M.L.1
  • 24
    • 80053369769 scopus 로고    scopus 로고
    • Contribution of unfolding and intermolecular architecture to fibronectin fiber extensibility
    • Bradshaw, M. J. & Smith, M. L. Contribution of unfolding and intermolecular architecture to fibronectin fiber extensibility. Biophys. J. 101, 1740 (2011).
    • (2011) Biophys. J , vol.101 , pp. 1740
    • Bradshaw, M.J.1    Smith, M.L.2
  • 25
    • 71949122441 scopus 로고    scopus 로고
    • Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein
    • Little, W. C., Schwartlander, R., Smith, M. L., Gourdon, D. & Vogel, V. Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein. Nano Lett. 9, 4158-4167 (2009).
    • (2009) Nano Lett , vol.9 , pp. 4158-4167
    • Little, W.C.1    Schwartlander, R.2    Smith, M.L.3    Gourdon, D.4    Vogel, V.5
  • 26
    • 84880260541 scopus 로고    scopus 로고
    • Stretching fibronectin fibres disrupts binding of bacterial adhesins by physically destroying an epitope
    • Chabria, M., Hertig, S., Smith, M. L. & Vogel, V. Stretching fibronectin fibres disrupts binding of bacterial adhesins by physically destroying an epitope. Nat. Commun. 1, 135 (2010).
    • (2010) Nat. Commun , vol.1 , pp. 135
    • Chabria, M.1    Hertig, S.2    Smith, M.L.3    Vogel, V.4
  • 27
    • 84867437035 scopus 로고    scopus 로고
    • Engineering mechanosensitive multivalent receptor-ligand interactions: Why the nanolinker regions of bacterial adhesins matter
    • Hertig, S., Chabria, M. & Vogel, V. Engineering mechanosensitive multivalent receptor-ligand interactions: why the nanolinker regions of bacterial adhesins matter. Nano Lett. 12, 5162 (2012).
    • (2012) Nano Lett , vol.12 , pp. 5162
    • Hertig, S.1    Chabria, M.2    Vogel, V.3
  • 28
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • Sottile, J. & Hocking, D. C. Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol. Biol. Cell 13, 3546-3559 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3546-3559
    • Sottile, J.1    Hocking, D.C.2
  • 29
    • 79955444776 scopus 로고    scopus 로고
    • A fibronectin-independent mechanism of collagen fibrillogenesis in adult liver remodeling
    • Moriya, K. et al. A fibronectin-independent mechanism of collagen fibrillogenesis in adult liver remodeling. Gastroenterology 140, 1653 (2011).
    • (2011) Gastroenterology , vol.140 , pp. 1653
    • Moriya, K.1
  • 30
    • 0020072924 scopus 로고
    • Role of fibronectin in collagen deposition: Fab' to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix
    • McDonald, J. A., Kelley, D. G. & Broekelmann, T. J. Role of fibronectin in collagen deposition: Fab' to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix. J. Cell Biol. 92, 485-492 (1982).
    • (1982) J. Cell Biol , vol.92 , pp. 485-492
    • McDonald, J.A.1    Kelley, D.G.2    Broekelmann, T.J.3
  • 31
    • 0018190692 scopus 로고
    • Localization of binding-site for cell attachment in alpha-1(I) chain of collagen
    • Kleinman, H. K. et al. Localization of binding-site for cell attachment in alpha-1(I) chain of collagen. J. Biol. Chem. 253, 5642-5656 (1978).
    • (1978) J. Biol. Chem , vol.253 , pp. 5642-5656
    • Kleinman, H.K.1
  • 32
    • 0041924762 scopus 로고    scopus 로고
    • Vascular smooth muscle cells orchestrate the assembly of type i collagen via alpha 2 beta 1 integrin, RhoA, and fibronectin polymerization
    • Li, S. H., Van den Diepstraten, C., D'Souza, S. J., Chan, B. M. C. & Pickering, J. G. Vascular smooth muscle cells orchestrate the assembly of type I collagen via alpha 2 beta 1 integrin, RhoA, and fibronectin polymerization. Am. J. Pathol. 163, 1045-1056 (2003).
    • (2003) Am. J. Pathol , vol.163 , pp. 1045-1056
    • Li, S.H.1    Van Den Diepstraten, C.2    D'souza, S.J.3    Chan, B.M.C.4    Pickering, J.G.5
  • 33
    • 84918581674 scopus 로고    scopus 로고
    • Disentangling the multifactorial contributions of fibronectin, collagen and cyclic strain on MMP expression and extracellular matrix remodeling by fibroblasts
    • Zhang, Y. et al. Disentangling the multifactorial contributions of fibronectin, collagen and cyclic strain on MMP expression and extracellular matrix remodeling by fibroblasts. Matrix Biol. 40, 62 (2014).
    • (2014) Matrix Biol , vol.40 , pp. 62
    • Zhang, Y.1
  • 34
    • 0018383990 scopus 로고
    • Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin
    • Hahn, L. H. & Yamada, K. M. Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin. Proc. Natl Acad. Sci. USA 76, 1160-1163 (1979).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1160-1163
    • Hahn, L.H.1    Yamada, K.M.2
  • 35
    • 77958593285 scopus 로고    scopus 로고
    • Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI
    • Erat, M. C. et al. Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI. J. Biol. Chem. 285, 33764-33770 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 33764-33770
    • Erat, M.C.1
  • 36
    • 63149115283 scopus 로고    scopus 로고
    • Identification and structural analysis of type i collagen sites in complex with fibronectin fragments
    • Erat, M. C. et al. Identification and structural analysis of type I collagen sites in complex with fibronectin fragments. Proc. Natl Acad. Sci. USA 106, 4195-4200 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4195-4200
    • Erat, M.C.1
  • 37
    • 0019467882 scopus 로고
    • The removal of extracellular fibronectin from areas of cell-substrate contact
    • Avnur, Z. & Geiger, B. The removal of extracellular fibronectin from areas of cell-substrate contact. Cell 25, 121-132 (1981).
    • (1981) Cell , vol.25 , pp. 121-132
    • Avnur, Z.1    Geiger, B.2
  • 38
    • 0014028481 scopus 로고
    • Collagen synthesis in fibroblasts transformed by oncogenic viruses
    • Green, H., Todaro, G. J. & Goldberg, B. Collagen synthesis in fibroblasts transformed by oncogenic viruses. Nature 209, 916-917 (1966).
    • (1966) Nature , vol.209 , pp. 916-917
    • Green, H.1    Todaro, G.J.2    Goldberg, B.3
  • 39
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • Canty, E. G. & Kadler, K. E. Procollagen trafficking, processing and fibrillogenesis. J. Cell Sci. 118, 1341-1353 (2005).
    • (2005) J. Cell Sci , vol.118 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 40
    • 0035807873 scopus 로고    scopus 로고
    • Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer
    • Baneyx, G., Baugh, L. & Vogel, V. Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer. Proc. Natl Acad. Sci. USA 98, 14464-14468 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14464-14468
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 41
    • 0027308871 scopus 로고
    • Fibronectin binding site in type i collagen regulates fibronectin fibril formation
    • Dzamba, B. J., Wu, H., Jaenisch, R. & Peters, D. M. Fibronectin binding site in type I collagen regulates fibronectin fibril formation. J. Cell. Biol. 121, 1165-1172 (1993).
    • (1993) J. Cell. Biol , vol.121 , pp. 1165-1172
    • Dzamba, B.J.1    Wu, H.2    Jaenisch, R.3    Peters, D.M.4
  • 42
    • 50549163600 scopus 로고
    • Collagen formation in vitro by established mammalian cell lines
    • Goldberg, B., Green, H. & Todaro, G. J. Collagen formation in vitro by established mammalian cell lines. Exp. Cell Res. 31, 444-447 (1963).
    • (1963) Exp. Cell Res , vol.31 , pp. 444-447
    • Goldberg, B.1    Green, H.2    Todaro, G.J.3
  • 44
    • 78649717029 scopus 로고    scopus 로고
    • Measurement of mechanical tractions exerted by cells in three-dimensional matrices
    • Legant, W. R. et al. Measurement of mechanical tractions exerted by cells in three-dimensional matrices. Nat. Methods 7, 969-971 (2010).
    • (2010) Nat. Methods , vol.7 , pp. 969-971
    • Legant, W.R.1
  • 45
    • 50849090315 scopus 로고    scopus 로고
    • Fibronectin in aging extracellular matrix fibrils is progressively unfolded by cells and elicits an enhanced rigidity response
    • Antia, M., Baneyx, G., Kubow, K. E. & Vogel, V. Fibronectin in aging extracellular matrix fibrils is progressively unfolded by cells and elicits an enhanced rigidity response. Faraday Discuss. 139, 229-249 (2008).
    • (2008) Faraday Discuss , vol.139 , pp. 229-249
    • Antia, M.1    Baneyx, G.2    Kubow, K.E.3    Vogel, V.4
  • 46
    • 77649223377 scopus 로고    scopus 로고
    • Crosslinking of cell-derived 3D scaffolds up-regulates the stretching and unfolding of new extracellular matrix assembled by reseeded cells
    • Kubow, K. E. et al. Crosslinking of cell-derived 3D scaffolds up-regulates the stretching and unfolding of new extracellular matrix assembled by reseeded cells. Integr. Biol. 1, 635-648 (2009).
    • (2009) Integr. Biol , vol.1 , pp. 635-648
    • Kubow, K.E.1
  • 47
    • 84874439260 scopus 로고    scopus 로고
    • Force-induced fibronectin assembly and matrix remodeling in a 3D microtissue model of tissue morphogenesis
    • Legant, W. R., Chen, C. S. & Vogel, V. Force-induced fibronectin assembly and matrix remodeling in a 3D microtissue model of tissue morphogenesis. Integr. Biol. 4, 1164 (2012).
    • (2012) Integr. Biol , vol.4 , pp. 1164
    • Legant, W.R.1    Chen, C.S.2    Vogel, V.3
  • 48
    • 36949024693 scopus 로고    scopus 로고
    • A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers
    • Guthold, M. et al. A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers. Cell Biochem. Biophys. 49, 165-181 (2007).
    • (2007) Cell Biochem. Biophys , vol.49 , pp. 165-181
    • Guthold, M.1
  • 49
    • 2442697771 scopus 로고    scopus 로고
    • Structural changes of fibronectin adsorbed to model surfaces probed by fluorescence resonance energy transfer
    • Baugh, L. & Vogel, V. Structural changes of fibronectin adsorbed to model surfaces probed by fluorescence resonance energy transfer. J. Biomed. Mater. Res. 69A, 525-534 (2004).
    • (2004) J. Biomed. Mater. Res. , vol.69 A , pp. 525-534
    • Baugh, L.1    Vogel, V.2
  • 50
    • 0018124578 scopus 로고
    • Codistribution of pericellular matrix proteins in cultured fibroblasts and loss of in transformation: Fibronectin and procollagen
    • Vaheri, A., Kurkinen, M., Lehto, V.-P., Linder, E. & Timpl, R. Codistribution of pericellular matrix proteins in cultured fibroblasts and loss of in transformation: fibronectin and procollagen. Proc. Natl Acad. Sci. USA 75, 4944-4948 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 4944-4948
    • Vaheri, A.1    Kurkinen, M.2    Lehto, V.-P.3    Linder, E.4    Timpl, R.5
  • 51
    • 0032900509 scopus 로고    scopus 로고
    • SFS a novel fibronectin-binding protein from streptococcus equi, inhibits the binding between fibronectin and collagen
    • Lindmark, H. & Guss, B. SFS, a novel fibronectin-binding protein from streptococcus equi, inhibits the binding between fibronectin and collagen. Infect. Immun. 67, 2383-2388 (1999).
    • (1999) Infect. Immun , vol.67 , pp. 2383-2388
    • Lindmark, H.1    Guss, B.2
  • 52
    • 37149027051 scopus 로고    scopus 로고
    • Fibronectin-dependent collagen i deposition modulates the cell response to fibronectin
    • Sottile, J. et al. Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin. Am. J. Physiol. Cell Physiol. 293, C1934-C1946 (2007).
    • (2007) Am. J. Physiol. Cell Physiol , vol.293 , pp. C1934-C1946
    • Sottile, J.1
  • 53
    • 0034285218 scopus 로고    scopus 로고
    • Time-lapse confocal reflection microscopy of collagen fibrillogenesis and extracellular matrix assembly in vitro
    • Brightman, A. O. et al. Time-lapse confocal reflection microscopy of collagen fibrillogenesis and extracellular matrix assembly in vitro. Biopolymers 54, 222-234 (2000).
    • (2000) Biopolymers , vol.54 , pp. 222-234
    • Brightman, A.O.1
  • 54
    • 84921972328 scopus 로고    scopus 로고
    • The ultrastructure of fibronectin fibers pulled from a protein monolayer at the air-liquid interface and the mechanism of the sheet-to-fiber transition
    • Mitsi, M. et al. The ultrastructure of fibronectin fibers pulled from a protein monolayer at the air-liquid interface and the mechanism of the sheet-to-fiber transition. Biomaterials 36, 66-79 (2015).
    • (2015) Biomaterials , vol.36 , pp. 66-79
    • Mitsi, M.1
  • 56
    • 84930622055 scopus 로고    scopus 로고
    • Molecular architecture of native fibronectin fibrils
    • Fruh, S. M., Schoen, I., Ries, J. & Vogel, V. Molecular architecture of native fibronectin fibrils. Nat. Commun. 6, 7275 (2015).
    • (2015) Nat. Commun , vol.6 , pp. 7275
    • Fruh, S.M.1    Schoen, I.2    Ries, J.3    Vogel, V.4
  • 57
    • 79951874643 scopus 로고    scopus 로고
    • Adipose progenitor cells increase fibronectin matrix strain and unfolding in breast tumors
    • Chandler, E. M., Saunders, M. P., Yoon, C. J., Gourdon, D. & Fischbach, C. Adipose progenitor cells increase fibronectin matrix strain and unfolding in breast tumors. Phys. Biol. 8, 015008 (2011).
    • (2011) Phys. Biol , vol.8 , pp. 015008
    • Chandler, E.M.1    Saunders, M.P.2    Yoon, C.J.3    Gourdon, D.4    Fischbach, C.5
  • 58
    • 68549112897 scopus 로고    scopus 로고
    • Mechanics, malignancy, and metastasis: The force journey of a tumor cell
    • Kumar, S. & Weaver, V. M. Mechanics, malignancy, and metastasis: the force journey of a tumor cell. Cancer Metastasis Rev. 28, 113-127 (2009).
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 113-127
    • Kumar, S.1    Weaver, V.M.2
  • 59
    • 84900307376 scopus 로고    scopus 로고
    • Heparindependent regulation of fibronectin matrix conformation
    • Hubbard, B., Buczek-Thomas, J. A., Nugent, M. A. & Smith, M. L. Heparindependent regulation of fibronectin matrix conformation. Matrix Biol. 34, 124 (2014).
    • (2014) Matrix Biol , vol.34 , pp. 124
    • Hubbard, B.1    Buczek-Thomas, J.A.2    Nugent, M.A.3    Smith, M.L.4
  • 60
    • 39449085655 scopus 로고    scopus 로고
    • Extracellular matrix fibronectin mechanically couples skeletal muscle contraction with local vasodilation
    • Hocking, D. C., Titus, P. A., Sumagin, R. & Sarelius, I. H. Extracellular matrix fibronectin mechanically couples skeletal muscle contraction with local vasodilation. Circ. Res. 102, 372-379 (2008).
    • (2008) Circ. Res , vol.102 , pp. 372-379
    • Hocking, D.C.1    Titus, P.A.2    Sumagin, R.3    Sarelius, I.H.4
  • 63
    • 19944428596 scopus 로고    scopus 로고
    • Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion
    • Yeung, T. et al. Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion. Cell Motil. Cytoskeleton 60, 24-34 (2005).
    • (2005) Cell Motil. Cytoskeleton , vol.60 , pp. 24-34
    • Yeung, T.1
  • 64
    • 33646155963 scopus 로고    scopus 로고
    • Rigidity sensing at the leading edge through (alpha) v(beta)3 integrins and RPTP(alpha)
    • Jiang, G., Huang, A. H., Cai, Y., Tanase, M. & Sheetz, M. P. Rigidity sensing at the leading edge through (alpha)v(beta)3 integrins and RPTP(alpha).Biophys. J. 90, 1804-1809 (2006).
    • (2006) Biophys J. , vol.90 , pp. 1804-1809
    • Jiang, G.1    Huang, A.H.2    Cai, Y.3    Tanase, M.4    Sheetz, M.P.5
  • 65
    • 33744772918 scopus 로고    scopus 로고
    • Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge
    • Kostic, A. & Sheetz, M. P. Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge. Mol. Biol. Cell 17, 2684-2695 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2684-2695
    • Kostic, A.1    Sheetz, M.P.2
  • 66
    • 84888340452 scopus 로고    scopus 로고
    • Distinct biophysical mechanisms of focal adhesion kinase mechanoactivation by different extracellular matrix proteins
    • Seong, J. et al. Distinct biophysical mechanisms of focal adhesion kinase mechanoactivation by different extracellular matrix proteins. Proc. Natl Acad. Sci. USA 110, 19372-19377 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 19372-19377
    • Seong, J.1
  • 67
    • 34547094812 scopus 로고    scopus 로고
    • Micro-well arrays for 3D shape control and high resolution analysis of single cells
    • Ochsner, M. et al. Micro-well arrays for 3D shape control and high resolution analysis of single cells. Lab Chip 7, 1074-1077 (2007).
    • (2007) Lab Chip , vol.7 , pp. 1074-1077
    • Ochsner, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.