메뉴 건너뛰기




Volumn 106, Issue 43, 2009, Pages 18267-18272

Fibronectin forms the most extensible biological fibers displaying switchable force-exposed cryptic binding sites

Author keywords

Fibrillogenesis; Matrix biology; Mechanotransduction; Multimodular proteins; Supramolecular assembly

Indexed keywords

BIOMATERIAL; EPITOPE; FIBRONECTIN; PLASTIC;

EID: 70849127367     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0907518106     Document Type: Article
Times cited : (219)

References (37)
  • 2
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: From fibroin sequence to mechanical function
    • Gosline JM, Guerette PA, Ortlepp CS, Savage KN (1999) The mechanical design of spider silks: From fibroin sequence to mechanical function. J Exp Biol 202:3295-3303.
    • (1999) J Exp Biol , vol.202 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Ortlepp, C.S.3    Savage, K.N.4
  • 5
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu H, Isralewitz B, Krammer A, Vogel V, Schulten K (1998) Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys J 75:662-671. (Pubitemid 28357508)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 7
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting force into biochemical signals
    • Vogel V (2006) Mechanotransduction involving multimodular proteins: Converting force into biochemical signals. Annu Rev Biophys Biomol Struct 35:459-488.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 459-488
    • Vogel, V.1
  • 8
    • 43149084573 scopus 로고    scopus 로고
    • Pulling single molecules of titin by AFM - Recent advances and physiological implications
    • Linke WA, Grutzner A (2008) Pulling single molecules of titin by AFM - recent advances and physiological implications. Pflugers Arch 456:101-115.
    • (2008) Pflugers Arch , vol.456 , pp. 101-115
    • Linke, W.A.1    Grutzner, A.2
  • 9
    • 43249101994 scopus 로고    scopus 로고
    • Cooperative retraction of bundled type IV pili enables nanonewton force generation
    • DOI 10.1371/journal.pbio.0060087, e87
    • Biais N, Ladoux B, Higashi D, So M, Sheetz M (2008) Cooperative retraction of bundled type IV pili enables nanonewton force generation. PLoS Biol 6:907-913. (Pubitemid 351649321)
    • (2008) PLoS Biology , vol.6 , Issue.4 , pp. 907-913
    • Biais, N.1    Ladoux, B.2    Higashi, D.3    So, M.4    Sheetz, M.5
  • 10
    • 33748628507 scopus 로고    scopus 로고
    • Uncoiling mechanics of Escherichia coli type I fimbriae are optimized for catch bonds
    • Forero M, Yakovenko O, Sokurenko EV, Thomas WE, Vogel V (2006) Uncoiling mechanics of Escherichia coli type I fimbriae are optimized for catch bonds. PLoS Biol 4:e298.
    • (2006) PLoS Biol , vol.4
    • Forero, M.1    Yakovenko, O.2    Sokurenko, E.V.3    Thomas, W.E.4    Vogel, V.5
  • 12
    • 0037087773 scopus 로고    scopus 로고
    • Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
    • Ohashi T, Kiehart DP, Erickson HP (2002) Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants. J Cell Sci 115:1221-1229. (Pubitemid 34272486)
    • (2002) Journal of Cell Science , vol.115 , Issue.6 , pp. 1221-1229
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 16
    • 0033607139 scopus 로고    scopus 로고
    • Self-assembly of fibronectin into fibrillar networks underneath dipalmitoyl phosphatidylcholine monolayers: Role of lipid matrix and tensile forces
    • DOI 10.1073/pnas.96.22.12518
    • Baneyx G, Vogel V (1999) Self-assembly of fibronectin into fibrillar networks underneath dipalmitoyl phosphatidylcholine monolayers: Role of lipid matrix and tensile forces. Proc Natl Acad Sci USA 96:12518-12523. (Pubitemid 29513534)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.22 , pp. 12518-12523
    • Baneyx, G.1    Vogel, V.2
  • 17
    • 52149109153 scopus 로고    scopus 로고
    • Force-induced fibronectin fibrillogenesis in vitro
    • Ulmer J, Geiger B, Spatz JP (2008) Force-induced fibronectin fibrillogenesis in vitro. Soft Matter 4:1998-2007.
    • (2008) Soft Matter , vol.4 , pp. 1998-2007
    • Ulmer, J.1    Geiger, B.2    Spatz, J.P.3
  • 18
    • 45049084735 scopus 로고    scopus 로고
    • Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage
    • Little WC, Smith ML, Ebneter U, Vogel V (2008) Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage. Matrix Biol 27:451-461.
    • (2008) Matrix Biol , vol.27 , pp. 451-461
    • Little, W.C.1    Smith, M.L.2    Ebneter, U.3    Vogel, V.4
  • 19
    • 35648954122 scopus 로고    scopus 로고
    • Force-induced unfolding of fibronectin in the extracellular matrix of living cells
    • Smith ML, et al. (2007) Force-induced unfolding of fibronectin in the extracellular matrix of living cells. PLoS Biol 5:e268.
    • (2007) PLoS Biol , vol.5
    • Smith, M.L.1
  • 20
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer MS, Smith SB, Granzier HL, Bustamante C (1997) Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276:1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 22
    • 0035002155 scopus 로고    scopus 로고
    • Force and focal adhesion assembly: A close relationship studied using elastic micropatterned substrates
    • Balaban NQ, et al. (2001) Force and focal adhesion assembly: A close relationship studied using elastic micropatterned substrates. Nat Cell Biol 3:466-472.
    • (2001) Nat Cell Biol , vol.3 , pp. 466-472
    • Balaban, N.Q.1
  • 23
    • 34547824364 scopus 로고    scopus 로고
    • Forced unfolding of proteins within cells
    • DOI 10.1126/science.1139857
    • Johnson CP, Tang HY, Carag C, Speicher DW, Discher DE (2007) Forced unfolding of proteins within cells. Science 317:663-666. (Pubitemid 47229965)
    • (2007) Science , vol.317 , Issue.5838 , pp. 663-666
    • Johnson, C.P.1    Tang, H.-Y.2    Carag, C.3    Speicher, D.W.4    Discher, D.E.5
  • 24
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the Mechanical Stability of Fibronectin Type III Modules through Sequence Variations
    • DOI 10.1016/j.str.2003.11.024
    • Craig D, Gao M, Schulten K, Vogel V (2004) Tuning the mechanical stability of fibronectin type III modules through sequence variations. Structure 12:21-30. (Pubitemid 38114803)
    • (2004) Structure , vol.12 , Issue.1 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 25
    • 25444512161 scopus 로고    scopus 로고
    • Biochemistry: Direct observation of the three-state folding of a single protein molecule
    • DOI 10.1126/science.1116702
    • Cecconi C, Shank EA, Bustamante C, Marqusee S (2005) Direct observation of the three-state folding of a single protein molecule. Science 309:2057-2060. (Pubitemid 41362324)
    • (2005) Science , vol.309 , Issue.5743 , pp. 2057-2060
    • Cecconi, G.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 26
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez JM, Li H (2004) Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 303:1674-1678.
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 27
    • 30444455738 scopus 로고    scopus 로고
    • Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions
    • Li MS, Hu CK, Klimov DK, Thirumalai D (2006) Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions. Proc Natl Acad Sci USA 103:93-98.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 93-98
    • Li, M.S.1    Hu, C.K.2    Klimov, D.K.3    Thirumalai, D.4
  • 28
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type III domain of human tenascin
    • DOI 10.1006/jmbi.1997.1147
    • Clarke J, Hamill SJ, Johnson CM (1997) Folding and stability of a fibronectin type III domain of human tenascin. J Mol Biol 270:771-778. (Pubitemid 27332066)
    • (1997) Journal of Molecular Biology , vol.270 , Issue.5 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 30
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules
    • DOI 10.1006/jmbi.1997.1148
    • Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM (1997) A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. J Mol Biol 270:763-770. (Pubitemid 27332065)
    • (1997) Journal of Molecular Biology , vol.270 , Issue.5 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 31
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou HX, Rivas G, Minton AP (2008) Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 37:375-397.
    • (2008) Annu Rev Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 32
    • 64549127723 scopus 로고    scopus 로고
    • Optimization strategies for electrospun silk fibroin tissue engineering scaffolds
    • Meinel AJ, et al. (2009) Optimization strategies for electrospun silk fibroin tissue engineering scaffolds. Biomaterials 30:3058-3067.
    • (2009) Biomaterials , vol.30 , pp. 3058-3067
    • Meinel, A.J.1
  • 33
    • 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 KE, Vogel V (2008) Fibronectin in aging extracellular matrix fibrils is progressively unfolded by cells and elicits an enhanced rigidity response. Faraday Discuss 139:229-249.
    • (2008) Faraday Discuss , vol.139 , pp. 229-249
    • Antia, M.1    Baneyx, G.2    Kubow, K.E.3    Vogel, V.4
  • 34
    • 11144297253 scopus 로고    scopus 로고
    • Assembly and remodeling of the fibrillar fibronectin extracellular matrix during gastrulation and neurulation in Xenopus laevis
    • DOI 10.1002/dvdy.20217
    • Davidson LA, Keller R, DeSimone DW (2004) Assembly and remodeling of the fibrillar fibronectin extracellular matrix during gastrulation and neurulation in Xenopus laevis. Dev Dyn 231:888-895. (Pubitemid 40022750)
    • (2004) Developmental Dynamics , vol.231 , Issue.4 , pp. 888-895
    • Davidson, L.A.1    Keller, R.2    Desimone, D.W.3
  • 35
    • 34547094812 scopus 로고    scopus 로고
    • Micro-well arrays for 3D shape control and high resolution analysis of single cells
    • Ochsner M, et al. (2007) Micro-well arrays for 3D shape control and high resolution analysis of single cells. Lab Chip 7:1074-1077.
    • (2007) Lab Chip , vol.7 , pp. 1074-1077
    • Ochsner, M.1
  • 36
    • 0027642088 scopus 로고
    • Production of artificial-orientated mats and strands from plasma fibronectin: A morphological study
    • DOI 10.1016/0142-9612(93)90038-4
    • Ejim OS, Blunn GW, Brown RA (1993) Production of artificial-orientated mats and strands from plasma fibronectin: A morphological study. Biomaterials 14:743-748. (Pubitemid 23247500)
    • (1993) Biomaterials , vol.14 , Issue.10 , pp. 743-748
    • Ejim, O.S.1    Blunn, G.W.2    Brown, R.A.3
  • 37
    • 33947219854 scopus 로고    scopus 로고
    • Monolithically fabricated microgripper with integrated force sensor for manipulating microobjects and biological cells aligned in an ultrasonic field
    • DOI 10.1109/JMEMS.2006.885853
    • Beyeler F, et al. (2007) Monolithically fabricated microgripper with integrated force sensor for manipulating microobjects and biological cells aligned in an ultrasonic field. J Microelectromech Syst 16:7-15. (Pubitemid 46431399)
    • (2007) Journal of Microelectromechanical Systems , vol.16 , Issue.1 , pp. 7-15
    • Beyeler, F.1    Neild, A.2    Oberti, S.3    Bell, D.J.4    Sun, Y.5    Dual, J.6    Nelson, B.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.