메뉴 건너뛰기




Volumn 35, Issue , 2006, Pages 459-488

Mechanotransduction involving multimodular proteins: Converting force into biochemical signals

Author keywords

helical bundles; sheets; Cell adhesion molecules; Fibronectin; Random coil; Spectrin family members; Titin

Indexed keywords

CELL ADHESION MOLECULE; INTEGRIN; ION CHANNEL; MEMBRANE PROTEIN; PROTEIN; SCLEROPROTEIN;

EID: 33645780908     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.35.040405.102013     Document Type: Review
Times cited : (376)

References (147)
  • 1
    • 27744581873 scopus 로고    scopus 로고
    • Ligand binding modulates the mechanical stability of dihydrofolate reductase (DHFR)
    • Aihavarapu SR, Li L, Badilla CL, Fernandez JM. 2005. Ligand binding modulates the mechanical stability of dihydrofolate reductase (DHFR). Biophys. J. 89:3337-44
    • (2005) Biophys. J. , vol.89 , pp. 3337-3344
    • Aihavarapu, S.R.1    Li, L.2    Badilla, C.L.3    Fernandez, J.M.4
  • 2
    • 0036045690 scopus 로고    scopus 로고
    • Pathways and intermediates in forced unfolding of spectrin repeats
    • Altmann SM, Grunberg RG, Lenne PF, Ylanne J, Raae A, et al. 2002. Pathways and intermediates in forced unfolding of spectrin repeats. Structure 10:1085-96
    • (2002) Structure , vol.10 , pp. 1085-1096
    • Altmann, S.M.1    Grunberg, R.G.2    Lenne, P.F.3    Ylanne, J.4    Raae, A.5
  • 3
    • 26944495707 scopus 로고    scopus 로고
    • Single molecule fluorescence studies of surface-adsorbed fibronectin
    • Antia M, Islas LD, Boness DA, Baneyx G, Vogel V. 2006. Single molecule fluorescence studies of surface-adsorbed fibronectin. Biomaterials 27: 679-90
    • (2006) Biomaterials , vol.27 , pp. 679-690
    • Antia, M.1    Islas, L.D.2    Boness, D.A.3    Baneyx, G.4    Vogel, V.5
  • 4
    • 0036421529 scopus 로고    scopus 로고
    • The extracellular matrix as a scaffold for tissue reconstruction
    • Badylak SF. 2002. The extracellular matrix as a scaffold for tissue reconstruction. Semin. Cell Dev. Biol. 13:377-83
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 377-383
    • Badylak, S.F.1
  • 5
    • 0035002155 scopus 로고    scopus 로고
    • Force and focal adhesion assembly: A close relationship studied using elastic micropatterned substrates
    • Balaban NQ, Schwarz US, Riveline D, Goichberg P, Tzur G, et al. 2001. Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates. Nat. Cell Biol. 3:466-72
    • (2001) Nat. Cell Biol. , vol.3 , pp. 466-472
    • Balaban, N.Q.1    Schwarz, U.S.2    Riveline, D.3    Goichberg, P.4    Tzur, G.5
  • 6
    • 21644470619 scopus 로고    scopus 로고
    • Application of microscope-based FRET to study molecular interactions in focal adhesions of live cells
    • Ballestrem C, Geiger B. 2005. Application of microscope-based FRET to study molecular interactions in focal adhesions of live cells. Methods Mol. Biol. 294:321-34
    • (2005) Methods Mol. Biol. , vol.294 , pp. 321-334
    • Ballestrem, C.1    Geiger, B.2
  • 7
    • 0035807873 scopus 로고    scopus 로고
    • Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer
    • Baneyx G, Baugh L, Vogel V. 2001. Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 98:14464-68
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14464-14468
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 8
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G, Baugh L, Vogel V. 2002. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc. Natl. Acad. Sci. USA 99:5139-43
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 9
    • 27744606970 scopus 로고    scopus 로고
    • SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity
    • Barker TH, Baneyx G, Cardo-Vila M, Workman GA, Weaver M, et al. 2005. SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity. J. Biol. Chem. 280:36483-93
    • (2005) J. Biol. Chem. , vol.280 , pp. 36483-36493
    • Barker, T.H.1    Baneyx, G.2    Cardo-Vila, M.3    Workman, G.A.4    Weaver, M.5
  • 10
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo KA, Dembo M, Kaverina I, Small JV, Wang YL. 2001. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153:881-88
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 11
    • 0036469826 scopus 로고    scopus 로고
    • Flexible substrata for the detection of cellular traction forces
    • Beningo KA, Wang YL. 2002. Flexible substrata for the detection of cellular traction forces. Trends Cell Biol. 12:79-84
    • (2002) Trends Cell Biol. , vol.12 , pp. 79-84
    • Beningo, K.A.1    Wang, Y.L.2
  • 13
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best RB, Li B, Steward A, Daggett V, Clarke J. 2001. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2344-56
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 14
    • 8544278061 scopus 로고    scopus 로고
    • Chemistry on a single protein, vascular cell adhesion molecule-1, during forced unfolding
    • Bhasin N, Carl P, Harper S, Feng G, Lu H, et al. 2004. Chemistry on a single protein, vascular cell adhesion molecule-1, during forced unfolding. J. Biol. Chem. 279:45865-74
    • (2004) J. Biol. Chem. , vol.279 , pp. 45865-45874
    • Bhasin, N.1    Carl, P.2    Harper, S.3    Feng, G.4    Lu, H.5
  • 15
    • 0042235309 scopus 로고    scopus 로고
    • Anastellin, an Fn3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors
    • Briknarova K, Akerman ME, Hoyt DW, Ruoslahti E, Ely KR. 2003. Anastellin, an Fn3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors. J. Mol. Biol. 332:205-15
    • (2003) J. Mol. Biol. , vol.332 , pp. 205-215
    • Briknarova, K.1    Akerman, M.E.2    Hoyt, D.W.3    Ruoslahti, E.4    Ely, K.R.5
  • 17
    • 0026476010 scopus 로고
    • The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence
    • Carnemolla B, Leprini A, Allemanni G, Saginati M, Zardi L. 1992. The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence. J. Biol. Chem. 267:24689-92
    • (1992) J. Biol. Chem. , vol.267 , pp. 24689-24692
    • Carnemolla, B.1    Leprini, A.2    Allemanni, G.3    Saginati, M.4    Zardi, L.5
  • 18
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fi-bronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr PA, Erickson HP, Palmer AG 3rd. 1997. Backbone dynamics of homologous fi-bronectin type III cell adhesion domains from fibronectin and tenascin. Structure 5:949-59
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer III, A.G.3
  • 21
    • 0036109559 scopus 로고    scopus 로고
    • Single cell mechanotransduction and its modulation analyzed by atomic force microscope indentation
    • Charras GT, Horton MA. 2002. Single cell mechanotransduction and its modulation analyzed by atomic force microscope indentation. Biophys. J. 82:2970-81
    • (2002) Biophys. J. , vol.82 , pp. 2970-2981
    • Charras, G.T.1    Horton, M.A.2
  • 23
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet D, Felsenfeld DP, Sheetz MP. 1997. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 88:39-48
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 24
    • 9144228666 scopus 로고    scopus 로고
    • PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation
    • Chou FL, Hill JM, Hsieh JC, Pouyssegur J, Branet A, et al. 2003. PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation. J. Biol. Chem. 278:52587-97
    • (2003) J. Biol. Chem. , vol.278 , pp. 52587-52597
    • Chou, F.L.1    Hill, J.M.2    Hsieh, J.C.3    Pouyssegur, J.4    Branet, A.5
  • 25
    • 7944225864 scopus 로고    scopus 로고
    • Structural insights into how the MIDAS ion stabilizes integrin binding to an RGD peptide under force
    • Craig D, Gao M, Schulten K, Vogel V. 2004. Structural insights into how the MIDAS ion stabilizes integrin binding to an RGD peptide under force. Structure 12:2049-58
    • (2004) Structure , vol.12 , pp. 2049-2058
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 26
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the mechanical stability of fibronectin type III modules through sequence variations
    • Craig D, Gao M, Schulten IC, Vogel V. 2004. Tuning the mechanical stability of fibronectin type III modules through sequence variations. Structure 12:21-30
    • (2004) Structure , vol.12 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, I.C.3    Vogel, V.4
  • 27
    • 0035826819 scopus 로고    scopus 로고
    • Comparison of the early stages of forced unfolding for fibronectin type III modules
    • Craig D, Krammer A, Schulten K, Vogel V. 2001. Comparison of the early stages of forced unfolding for fibronectin type III modules. Proc. Natl. Acad. Sci. USA 98:5590-95
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5590-5595
    • Craig, D.1    Krammer, A.2    Schulten, K.3    Vogel, V.4
  • 28
    • 0028216926 scopus 로고
    • Crystal structure of the tenth type III cell adhesion module of human fibronectin
    • Dickinson CD, Veerapandian B, Dai XP, Hamlin RC, Xuong NH, et al. 1994. Crystal structure of the tenth type III cell adhesion module of human fibronectin. J. Mol. Biol. 236:1079-92
    • (1994) J. Mol. Biol. , vol.236 , pp. 1079-1092
    • Dickinson, C.D.1    Veerapandian, B.2    Dai, X.P.3    Hamlin, R.C.4    Xuong, N.H.5
  • 29
    • 9944258521 scopus 로고    scopus 로고
    • New insights into FAK signaling and localization based on detection of a FAT domain folding intermediate
    • Dixon RD, Chen Y, Ding F, Khare SD, Prutzman KC, et al. 2004. New insights into FAK signaling and localization based on detection of a FAT domain folding intermediate. Structure 12:2161-71
    • (2004) Structure , vol.12 , pp. 2161-2171
    • Dixon, R.D.1    Chen, Y.2    Ding, F.3    Khare, S.D.4    Prutzman, K.C.5
  • 31
    • 4544264684 scopus 로고    scopus 로고
    • Myotubes differentiate optimally on substrates with tissue-like stiffness: Pathological implications for soft or stiff microenvironments
    • Engler AJ, Griffin MA, Sen S, Bonnemann CG, Sweeney HL, Discher DE. 2004. Myotubes differentiate optimally on substrates with tissue-like stiffness: pathological implications for soft or stiff microenvironments. J. Cell Biol. 166:877-87
    • (2004) J. Cell Biol. , vol.166 , pp. 877-887
    • Engler, A.J.1    Griffin, M.A.2    Sen, S.3    Bonnemann, C.G.4    Sweeney, H.L.5    Discher, D.E.6
  • 32
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force-lifetime-and chemistry in single molecular bonds
    • Evans E. 2001. Probing the relation between force-lifetime-and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30:105-28
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 33
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajec-tory of a single protein
    • Fernandez JM, Li H. 2004. Force-clamp spectroscopy monitors the folding trajec-tory of a single protein. Science 303:1674-78
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 34
    • 19444372522 scopus 로고    scopus 로고
    • The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction
    • Forman JR, Qamar S, Paci E, Sandford RN, Clarke J. 2005. The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction. J. Mol. Biol. 349:861-71
    • (2005) J. Mol. Biol. , vol.349 , pp. 861-871
    • Forman, J.R.1    Qamar, S.2    Paci, E.3    Sandford, R.N.4    Clarke, J.5
  • 35
    • 0036389817 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering
    • Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, et al. 2002. Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J. Mol. Biol. 322:841-49
    • (2002) J. Mol. Biol. , vol.322 , pp. 841-849
    • Fowler, S.B.1    Best, R.B.2    Toca Herrera, J.L.3    Rutherford, T.J.4    Steward, A.5
  • 36
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith CG, Yamada KM, Sheetz MP. 2002. The relationship between force and focal complex development. J. Cell Biol. 159:695-705
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 37
    • 0344736695 scopus 로고    scopus 로고
    • Structure and functional significance of mechanically unfolded fibronectin type III intermediates
    • Gao M, Craig D, Lequin O, Campbell ID, Vogel V, Schulten K. 2003. Structure and functional significance of mechanically unfolded fibronectin type III intermediates. Proc. Natl. Acad. Sci. USA 100:14784-89
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14784-14789
    • Gao, M.1    Craig, D.2    Lequin, O.3    Campbell, I.D.4    Vogel, V.5    Schulten, K.6
  • 38
    • 0036428792 scopus 로고    scopus 로고
    • Identifying unfolding intermediates of FN-III(10) by steered molecular dynamics
    • Gao M, Craig D, Vogel V, Schulten K. 2002. Identifying unfolding intermediates of FN-III(10) by steered molecular dynamics. J. Mol. Biol. 323:939-50
    • (2002) J. Mol. Biol. , vol.323 , pp. 939-950
    • Gao, M.1    Craig, D.2    Vogel, V.3    Schulten, K.4
  • 39
    • 0037569632 scopus 로고    scopus 로고
    • Unfolding of titin domains studied by molecular dynamics simulations
    • Gao M, Lu H, Schulten K. 2002. Unfolding of titin domains studied by molecular dynamics simulations. J. Muscle Res. Cell Motil. 23:513-21
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , pp. 513-521
    • Gao, M.1    Lu, H.2    Schulten, K.3
  • 40
    • 0036924186 scopus 로고    scopus 로고
    • Steered molecular dynamics studies of titin Il domain unfolding
    • Gao M, Wilmanns M, Schulten K. 2002. Steered molecular dynamics studies of titin Il domain unfolding. Biophys. J. 83:3435-45
    • (2002) Biophys. J. , vol.83 , pp. 3435-3445
    • Gao, M.1    Wilmanns, M.2    Schulten, K.3
  • 41
    • 2142826563 scopus 로고    scopus 로고
    • Stick and grip: Measurement systems and quantitative analyses of integrin-mediated cell adhesion strength
    • Garcia AJ, Gallant ND. 2003. Stick and grip: measurement systems and quantitative analyses of integrin-mediated cell adhesion strength. Cell Biocbem. Biophys. 39:61-73
    • (2003) Cell Biocbem. Biophys. , vol.39 , pp. 61-73
    • Garcia, A.J.1    Gallant, N.D.2
  • 42
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B, Bershadsky A. 2001. Assembly and mechanosensory function of focal contacts. Curr. Opin. Cell Biol. 13:584-92
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 43
    • 0037178784 scopus 로고    scopus 로고
    • Exploring the neighborhood: Adhesion-coupled cell mechanosensors
    • Geiger B, Bershadsky A. 2002. Exploring the neighborhood: adhesion-coupled cell mechanosensors. Cell 110:139-42
    • (2002) Cell , vol.110 , pp. 139-142
    • Geiger, B.1    Bershadsky, A.2
  • 44
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
    • Geiger B, Bershadsky A, Pankov R, Yamada KM. 2001. Transmembrane crosstalk between the extracellular matrix and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 2:793-805
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 45
    • 15444368220 scopus 로고    scopus 로고
    • Cell type-specific response to growth on soft materials
    • Georges PC, Janmey PA. 2005. Cell type-specific response to growth on soft materials. J. Appl. Physiol. 98:1547-53
    • (2005) J. Appl. Physiol. , vol.98 , pp. 1547-1553
    • Georges, P.C.1    Janmey, P.A.2
  • 47
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation
    • Giannone G, Jiang G, Sutton DH, Critchley DR, Sheetz MP. 2003. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J. Cell Biol. 163:409-19
    • (2003) J. Cell Biol. , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 48
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations
    • Grater F, Shen J, Jiang H, Gautel M, Grabmuller H. 2005. Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations. Biophys. J. 88:790-804
    • (2005) Biophys. J. , vol.88 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautel, M.4    Grabmuller, H.5
  • 49
    • 1842504023 scopus 로고    scopus 로고
    • Towards a regional approach to cell mechanics
    • Heidemann SR, Wirtz D. 2004. Towards a regional approach to cell mechanics. Trends Cell Biol. 14:160-66
    • (2004) Trends Cell Biol. , vol.14 , pp. 160-166
    • Heidemann, S.R.1    Wirtz, D.2
  • 50
    • 0037043337 scopus 로고    scopus 로고
    • A cryptic fragment from fibronectin's III1 module localizes to lipid rafts and stimulates cell growth and contractility
    • Hocking DC, Kowalski K. 2002. A cryptic fragment from fibronectin's III1 module localizes to lipid rafts and stimulates cell growth and contractility. J. Cell Biol. 158:175-84
    • (2002) J. Cell Biol. , vol.158 , pp. 175-184
    • Hocking, D.C.1    Kowalski, K.2
  • 51
    • 0024315634 scopus 로고
    • Mechanochemical switching between growth and differentiation during fibroblast growth factor-stimulated angiogenesis in vitro: Role of extracellular matrix
    • Ingber DE, Folkman J. 1989. Mechanochemical switching between growth and differentiation during fibroblast growth factor-stimulated angiogenesis in vitro: role of extracellular matrix. J. Cell Biol. 109:317-30
    • (1989) J. Cell Biol. , vol.109 , pp. 317-330
    • Ingber, D.E.1    Folkman, J.2
  • 52
    • 3142655415 scopus 로고    scopus 로고
    • Localization of a cryptic binding site for tenascin on fibronectin
    • Ingham KC, Brew SA, Erickson HP. 2004. Localization of a cryptic binding site for tenascin on fibronectin. J. Biol. Chem. 279:28132-35
    • (2004) J. Biol. Chem. , vol.279 , pp. 28132-28135
    • Ingham, K.C.1    Brew, S.A.2    Erickson, H.P.3
  • 53
    • 0031036225 scopus 로고    scopus 로고
    • Cryptic self-association sites in type III modules of fibronectin
    • Ingham KC, Brew SA, Huff S, Litvinovich SV. 1997. Cryptic self-association sites in type III modules of fibronectin. J. Biol. Chem. 272:1718-24
    • (1997) J. Biol. Chem. , vol.272 , pp. 1718-1724
    • Ingham, K.C.1    Brew, S.A.2    Huff, S.3    Litvinovich, S.V.4
  • 54
    • 3242796694 scopus 로고    scopus 로고
    • Dealing with mechanics: Mechanisms offeree transduction in cells
    • Janmey PA, Weitz DA. 2004. Dealing with mechanics: mechanisms offeree transduction in cells. Trends Biochem. Sci. 29:364-70
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 364-370
    • Janmey, P.A.1    Weitz, D.A.2
  • 55
    • 0041461882 scopus 로고    scopus 로고
    • Two-picoNewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Deleted in proof
    • Jiang G, Giannone G, Critchley DR, Fukumoto E, Sheetz MP. 2003. Two-picoNewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424:334-37 56. Deleted in proof
    • (2003) Nature , vol.424 , pp. 334-3756
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 56
    • 20444465227 scopus 로고    scopus 로고
    • Integrin activation and matrix binding mediate cellular responses to mechanical stretch
    • Katsumi A, Naoe T, Matsushita T, Kaibuchi K, Schwartz MA. 2005. Integrin activation and matrix binding mediate cellular responses to mechanical stretch. J. Biol. Chem. 280:16546-49
    • (2005) J. Biol. Chem. , vol.280 , pp. 16546-16549
    • Katsumi, A.1    Naoe, T.2    Matsushita, T.3    Kaibuchi, K.4    Schwartz, M.A.5
  • 57
    • 0034114114 scopus 로고    scopus 로고
    • Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions
    • Katz BZ, Zamir E, Bershadsky A, Kam Z, Yamada KM, Geiger B. 2000. Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions. Mol. Biol. Cell 11:1047-60
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1047-1060
    • Katz, B.Z.1    Zamir, E.2    Bershadsky, A.3    Kam, Z.4    Yamada, K.M.5    Geiger, B.6
  • 58
    • 0038740870 scopus 로고    scopus 로고
    • Mechanics and structure of titin oligomers explored with atomic force microscopy
    • Kellermayer MS, Bustamante C, Granzier HL. 2003. Mechanics and structure of titin oligomers explored with atomic force microscopy. Biochim. Biophys. Acta 1604:105-14
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 105-114
    • Kellermayer, M.S.1    Bustamante, C.2    Granzier, H.L.3
  • 60
  • 61
    • 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 276:1112-16
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 62
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston JA, Baker TA, Fernandez JM, Sauer RT. 2003. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114:511-20
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 63
    • 17844376765 scopus 로고    scopus 로고
    • Integrin binding specificity regulates biomaterial surface chemistry effects on cell differentiation
    • Keselowsky BG, Collard DM, Garcia AJ. 2005. Integrin binding specificity regulates biomaterial surface chemistry effects on cell differentiation. Proc. Natl. Acad. Sci. USA 102:5953-57
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5953-5957
    • Keselowsky, B.G.1    Collard, D.M.2    Garcia, A.J.3
  • 64
    • 0030943627 scopus 로고    scopus 로고
    • Force effects on biochemical kinetics
    • Khan S, Sheetz MP. 1997. Force effects on biochemical kinetics. Annu. Rev. Biochem. 66:785-805
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 785-805
    • Khan, S.1    Sheetz, M.P.2
  • 65
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface
    • Koide A, Jordan MR, Horner SR, Batori V, Koide S. 2001. Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. Biochemistry 40:10326-33
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1    Jordan, M.R.2    Horner, S.R.3    Batori, V.4    Koide, S.5
  • 66
    • 0027267959 scopus 로고
    • Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library
    • Koivunen E, Gay DA, Ruoslahti E. 1993. Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library. J. Biol. Chem. 268:20205-10
    • (1993) J. Biol. Chem. , vol.268 , pp. 20205-20210
    • Koivunen, E.1    Gay, D.A.2    Ruoslahti, E.3
  • 67
    • 0036171809 scopus 로고    scopus 로고
    • A structural model for force regulated integrin binding to fibronectin's RGD-synergy site
    • Krammer A, Craig D, Thomas WE, Schulten K, Vogel V. 2002. A structural model for force regulated integrin binding to fibronectin's RGD-synergy site. Matrix Biol. 21:139-47
    • (2002) Matrix Biol. , vol.21 , pp. 139-147
    • Krammer, A.1    Craig, D.2    Thomas, W.E.3    Schulten, K.4    Vogel, V.5
  • 68
    • 0033573912 scopus 로고    scopus 로고
    • Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch
    • Krammer A, Lu H, Isralewitz B, Schulten K, Vogel V. 1999. Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch. Proc. Natl. Acad. Sci. USA 96:1351-56
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1351-1356
    • Krammer, A.1    Lu, H.2    Isralewitz, B.3    Schulten, K.4    Vogel, V.5
  • 69
    • 0033548441 scopus 로고    scopus 로고
    • Identification of protein-disulfide isomerase activity in fibronectin
    • Langenbach KJ, Sottile J. 1999. Identification of protein-disulfide isomerase activity in fibronectin. J. Biol. Chem. 274:7032-38
    • (1999) J. Biol. Chem. , vol.274 , pp. 7032-7038
    • Langenbach, K.J.1    Sottile, J.2
  • 71
    • 1942501650 scopus 로고    scopus 로고
    • Influence of lateral association on forced unfolding of antiparallel spectrin heterodimers
    • Law R, Harper S, Speicher DW, Discher DE. 2004. Influence of lateral association on forced unfolding of antiparallel spectrin heterodimers. J. Biol. Chem. 279:16410-16
    • (2004) J. Biol. Chem. , vol.279 , pp. 16410-16416
    • Law, R.1    Harper, S.2    Speicher, D.W.3    Discher, D.E.4
  • 72
    • 0036369182 scopus 로고    scopus 로고
    • Use of micropatterned adhesive surfaces for control of cell behavior
    • LeDuc P, Ostuni E, Whitesides G, Ingber D. 2002. Use of micropatterned adhesive surfaces for control of cell behavior. Methods Cell Biol. 69:385-401
    • (2002) Methods Cell Biol. , vol.69 , pp. 385-401
    • Leduc, P.1    Ostuni, E.2    Whitesides, G.3    Ingber, D.4
  • 73
    • 0029587579 scopus 로고
    • Integrin signaling: Roles for the cytoplasmic tails of alpha lib beta 3 in the tyrosine phosphorylation of pp125FAK
    • Leong L, Hughes PE, Schwartz MA, Ginsberg MH, Shattil SJ. 1995. Integrin signaling: roles for the cytoplasmic tails of alpha lib beta 3 in the tyrosine phosphorylation of pp125FAK. J. Cell Sci. 108(Pt. 12):3817-25
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 12 , pp. 3817-3825
    • Leong, L.1    Hughes, P.E.2    Schwartz, M.A.3    Ginsberg, M.H.4    Shattil, S.J.5
  • 74
    • 0142195769 scopus 로고    scopus 로고
    • Mechanical design of the first proximal Ig domain of human cardiac titin revealed by single molecule force spectroscopy
    • Li H, Fernandez JM. 2003. Mechanical design of the first proximal Ig domain of human cardiac titin revealed by single molecule force spectroscopy. J. Mol. Biol. 334:75-86
    • (2003) J. Mol. Biol. , vol.334 , pp. 75-86
    • Li, H.1    Fernandez, J.M.2
  • 76
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module
    • Li L, Huang HH, Badilla CL, Fernandez JM. 2005. Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module. J. Mol. Biol. 345:817-26
    • (2005) J. Mol. Biol. , vol.345 , pp. 817-826
    • Li, L.1    Huang, H.H.2    Badilla, C.L.3    Fernandez, J.M.4
  • 77
    • 0036443942 scopus 로고    scopus 로고
    • PEVK domain of titin: An entropie spring with actin-binding properties
    • Linke WA, Kulke M, Li H, Fujita-Becker S, Neagoe C, et al. 2002. PEVK domain of titin: an entropie spring with actin-binding properties. J. Struct. Biol. 137:194-205
    • (2002) J. Struct. Biol. , vol.137 , pp. 194-205
    • Linke, W.A.1    Kulke, M.2    Li, H.3    Fujita-Becker, S.4    Neagoe, C.5
  • 78
    • 0033538859 scopus 로고    scopus 로고
    • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure
    • Linke WA, Rudy DE, Centner T, Gautel M, Witt C, et al. 1999. I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure. J. Cell Biol. 146:631-44
    • (1999) J. Cell Biol. , vol.146 , pp. 631-644
    • Linke, W.A.1    Rudy, D.E.2    Centner, T.3    Gautel, M.4    Witt, C.5
  • 79
    • 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. 75:662-71
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 80
    • 0033151955 scopus 로고    scopus 로고
    • Steered molecular dynamics simulations of force-induced protein domain unfolding
    • Lu H, Schulten K. 1999. Steered molecular dynamics simulations of force-induced protein domain unfolding. Proteins 35:453-63
    • (1999) Proteins , vol.35 , pp. 453-463
    • Lu, H.1    Schulten, K.2
  • 81
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma K, Kan L, Wang K. 2001. Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. Biochemistry 40:3427-38
    • (2001) Biochemistry , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.2    Wang, K.3
  • 82
    • 0035799317 scopus 로고    scopus 로고
    • Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat
    • MacDonald RI, Pozharski EV. 2001. Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat. Biochemistry 40:3974-84
    • (2001) Biochemistry , vol.40 , pp. 3974-3984
    • MacDonald, R.I.1    Pozharski, E.V.2
  • 85
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans O, van der Ven PF, Wilm M, Mues A, Young P, et al. 1998. Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395:863-69
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1    Van Der Ven, P.F.2    Wilm, M.3    Mues, A.4    Young, P.5
  • 86
    • 1842426730 scopus 로고    scopus 로고
    • Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment
    • McBeath R, Pirone DM, Nelson CM, Bhadriraju K, Chen CS. 2004. Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment. Dev. Cell 6:483-95
    • (2004) Dev. Cell , vol.6 , pp. 483-495
    • McBeath, R.1    Pirone, D.M.2    Nelson, C.M.3    Bhadriraju, K.4    Chen, C.S.5
  • 87
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel R, Nassoy P, Leung A, Ritchie K, Evans E. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397:50-53
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 88
    • 0347382333 scopus 로고    scopus 로고
    • A targeted deletion of the C-terminal end of titin, including the titin kinase domain, impairs myofibrillogenesis
    • Miller G, Musa H, Gautel M, Peckham M. 2003. A targeted deletion of the C-terminal end of titin, including the titin kinase domain, impairs myofibrillogenesis. J. Cell Sci. 116:4811-19
    • (2003) J. Cell Sci. , vol.116 , pp. 4811-4819
    • Miller, G.1    Musa, H.2    Gautel, M.3    Peckham, M.4
  • 89
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla A, Zhang Z, Ruoslahti E. 1994. Superfibronectin is a functionally distinct form of fibronectin. Nature 367:193-96
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 90
    • 0025932687 scopus 로고
    • Identification of a novel recognition sequence for the integrin alpha 4 beta 1 in the COOH-terminal heparin-binding domain of fibronectin
    • Mould AP, Humphries MJ. 1991. Identification of a novel recognition sequence for the integrin alpha 4 beta 1 in the COOH-terminal heparin-binding domain of fibronectin. EMBO J. 10:4089-95
    • (1991) EMBO J. , vol.10 , pp. 4089-4095
    • Mould, A.P.1    Humphries, M.J.2
  • 91
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: The unfolding pathway of a mill domain probed by protein engineering, AFM and MD simulation
    • Ng SP, Rounsevell RW, Steward A, Geierhaas CD, Williams PM, et al. 2005. Mechanical unfolding of TNfn3: the unfolding pathway of a mill domain probed by protein engineering, AFM and MD simulation. J. Mol. Biol. 350:776-89
    • (2005) J. Mol. Biol. , vol.350 , pp. 776-789
    • Ng, S.P.1    Rounsevell, R.W.2    Steward, A.3    Geierhaas, C.D.4    Williams, P.M.5
  • 93
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature 393:181-85
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 95
    • 0033531973 scopus 로고    scopus 로고
    • Forced unfolding of fibronectin type 3 modules: An analysis by biased molecular dynamics simulations
    • Paci E, Karplus M. 1999. Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations. J. Mol. Biol. 288:441-59
    • (1999) J. Mol. Biol. , vol.288 , pp. 441-459
    • Paci, E.1    Karplus, M.2
  • 96
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R, Yamada KM. 2002. Fibronectin at a glance. J. Cell Sci. 115:3861-63
    • (2002) J. Cell Sci. , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 98
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham RJ Jr, Wang Y. 1997. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl. Acad. Sci. USA 94:13661-65
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13661-13665
    • Pelham Jr., R.J.1    Wang, Y.2
  • 99
    • 0031569351 scopus 로고    scopus 로고
    • Solution structure of a type 2 module from fibronectin: Implications for the structure and function of the gelatin-binding domain
    • Pickford AR, Potts JR, Bright JR, Phan I, Campbell ID. 1997. Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin-binding domain. Structure 5:359-70
    • (1997) Structure , vol.5 , pp. 359-370
    • Pickford, A.R.1    Potts, J.R.2    Bright, J.R.3    Phan, I.4    Campbell, I.D.5
  • 100
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309:30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 101
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher MD, Ruoslahti E. 1987. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262:17294-98
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 103
    • 0034678405 scopus 로고    scopus 로고
    • Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis
    • Redick SD, Settles DL, Briscoe G, Erickson HP. 2000. Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis. J. Cell Biol. 149:521-27
    • (2000) J. Cell Biol. , vol.149 , pp. 521-527
    • Redick, S.D.1    Settles, D.L.2    Briscoe, G.3    Erickson, H.P.4
  • 104
    • 0034472157 scopus 로고    scopus 로고
    • Unfolding forces of titin and fibronectin domains directly measured by AFM
    • Rief M, Gautel M, Gaub HE. 2000. Unfolding forces of titin and fibronectin domains directly measured by AFM. Adv. Exp. Med. Biol. 481:129-41
    • (2000) Adv. Exp. Med. Biol. , vol.481 , pp. 129-141
    • Rief, M.1    Gautel, M.2    Gaub, H.E.3
  • 105
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-12
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 106
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • Rief M, Gautel M, Schemmel A, Gaub HE. 1998. The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. Biophys. J. 75:3008-14
    • (1998) Biophys. J. , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 107
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief M, Pascual J, Saraste M, Gaub HE. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-61
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 108
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism
    • Riveline D, Zamir E, Balaban NQ, Schwarz US, Ishizaki T, et al. 2001. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism. J. Cell Biol. 153:1175-86
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5
  • 109
    • 0033064934 scopus 로고    scopus 로고
    • Unraveling proteins: A molecular mechanics study
    • Rohs R, Etchebest C, Lavery R. 1999. Unraveling proteins: a molecular mechanics study. Biophys. J. 76:2760-68
    • (1999) Biophys. J. , vol.76 , pp. 2760-2768
    • Rohs, R.1    Etchebest, C.2    Lavery, R.3
  • 110
    • 1642452668 scopus 로고    scopus 로고
    • FnIII domains: Predicting mechanical stability
    • Rounsevell RW, Clarke J. 2004. FnIII domains: predicting mechanical stability. Structure 12:4-5
    • (2004) Structure , vol.12 , pp. 4-5
    • Rounsevell, R.W.1    Clarke, J.2
  • 111
    • 20544435808 scopus 로고    scopus 로고
    • Biophysical investigations of engineered polyproteins: Implications for force data
    • Rounsevell RW, Steward A, Clarke J. 2005. Biophysical investigations of engineered polyproteins: implications for force data. Biophys. J. 88:2022-29
    • (2005) Biophys. J. , vol.88 , pp. 2022-2029
    • Rounsevell, R.W.1    Steward, A.2    Clarke, J.3
  • 112
    • 0037184907 scopus 로고    scopus 로고
    • Mapping the heparin-binding site on the 13-14F3 fragment of fibronectin
    • Sachchidanand, Lequin O, Staunton D, Mulloy B, Forster MJ, et al. 2002. Mapping the heparin-binding site on the 13-14F3 fragment of fibronectin. J. Biol. Chem. 277:50629-35
    • (2002) J. Biol. Chem. , vol.277 , pp. 50629-50635
    • Sachchidanand1    Lequin, O.2    Staunton, D.3    Mulloy, B.4    Forster, M.J.5
  • 113
    • 14844297706 scopus 로고    scopus 로고
    • The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy
    • Sarkar A, Caamano S, Fernandez JM. 2005. The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy. J. Biol. Chem. 280:6261-64
    • (2005) J. Biol. Chem. , vol.280 , pp. 6261-6264
    • Sarkar, A.1    Caamano, S.2    Fernandez, J.M.3
  • 114
    • 0035074552 scopus 로고    scopus 로고
    • Rap1 is involved in cell stretching modulation of p38 but not ERK or JNKMAP kinase.y
    • Sawada Y, Nakamura K, Doi K, Takeda K, Tobiume K, et al. 2001. Rap1 is involved in cell stretching modulation of p38 but not ERK or JNKMAP kinase.y. Cell Sci. 114:1221-27
    • (2001) Cell Sci. , vol.114 , pp. 1221-1227
    • Sawada, Y.1    Nakamura, K.2    Doi, K.3    Takeda, K.4    Tobiume, K.5
  • 115
    • 0037128202 scopus 로고    scopus 로고
    • Force transduction by Triton cytoskeletons
    • Sawada Y, Sheetz MP. 2002. Force transduction by Triton cytoskeletons. J. Cell Biol. 156:609-15
    • (2002) J. Cell Biol. , vol.156 , pp. 609-615
    • Sawada, Y.1    Sheetz, M.P.2
  • 117
    • 0027393671 scopus 로고
    • Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa
    • Scarborough RM, Naughton MA, Teng W, Rose JW, Phillips DR, et al. 1993. Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa. J. Biol. Chem. 268:1066-73
    • (1993) J. Biol. Chem. , vol.268 , pp. 1066-1073
    • Scarborough, R.M.1    Naughton, M.A.2    Teng, W.3    Rose, J.W.4    Phillips, D.R.5
  • 118
    • 0034467924 scopus 로고    scopus 로고
    • The proteolytic activity of the recombinant cryptic human fibronectin type W collagenase from E. coli expression
    • Schnepel J, Tschesche H. 2000. The proteolytic activity of the recombinant cryptic human fibronectin type W collagenase from E. coli expression. J. Protein Chem. 19:685-92
    • (2000) J. Protein Chem. , vol.19 , pp. 685-692
    • Schnepel, J.1    Tschesche, H.2
  • 119
    • 0035700629 scopus 로고    scopus 로고
    • Recombinant cryptic human fibronectinase cleaves actin and myosin: Substrate specificity and possible role in muscular dystrophy
    • Schnepel J, Unger J, Tschesche H. 2001. Recombinant cryptic human fibronectinase cleaves actin and myosin: substrate specificity and possible role in muscular dystrophy. Biol. Chem. 382:1707-14
    • (2001) Biol. Chem. , vol.382 , pp. 1707-1714
    • Schnepel, J.1    Unger, J.2    Tschesche, H.3
  • 121
    • 0036304229 scopus 로고    scopus 로고
    • Titin: A multidomain protein that behaves as the sum of its parts
    • Scott KA, Steward A, Fowler SB, Clarke J. 2002. Titin: a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315:819-29
    • (2002) J. Mol. Biol. , vol.315 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 122
    • 0035802114 scopus 로고    scopus 로고
    • A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly
    • Sechler JL, Rao H, Cumiskey AM, Vega-Colon I, Smith MS, et al. 2001. A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly. J. Cell Biol. 154:1081-88
    • (2001) J. Cell Biol. , vol.154 , pp. 1081-1088
    • Sechler, J.L.1    Rao, H.2    Cumiskey, A.M.3    Vega-Colon, I.4    Smith, M.S.5
  • 123
    • 0033559259 scopus 로고    scopus 로고
    • Crystal structure of a heparin- and integrin-binding segment of human fibronectin
    • Sharma A, Askari JA, Humphries MJ, Jones EY, Stuart DI. 1999. Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 18:1468-79
    • (1999) EMBO J. , vol.18 , pp. 1468-1479
    • Sharma, A.1    Askari, J.A.2    Humphries, M.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 124
    • 0141429921 scopus 로고    scopus 로고
    • A novel mode for integrin-mediated signaling: Tethering is required for phosphorylation of FAK Y397
    • Shi Q, Boettiger D. 2003. A novel mode for integrin-mediated signaling: tethering is required for phosphorylation of FAK Y397. Mol. Biol. Cell 14:4306-15
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4306-4315
    • Shi, Q.1    Boettiger, D.2
  • 125
    • 2142803260 scopus 로고    scopus 로고
    • Mechanosensitive channels: Multiplicity of families and gating paradigms
    • Sukharev S, Corey DP. 2004. Mechanosensitive channels: multiplicity of families and gating paradigms. Sci. STKE 2004:re4
    • (2004) Sci. STKE , vol.2004
    • Sukharev, S.1    Corey, D.P.2
  • 126
    • 21244472677 scopus 로고    scopus 로고
    • JNK1 and JNK2 oppositely regulate p53 in signaling linked to apoptosis triggered by an altered fibronectin matrix: JNK links FAKand p53
    • Tafolla E, Wang S, Wong B, Leong J, Kapila YL. 2005. JNK1 and JNK2 oppositely regulate p53 in signaling linked to apoptosis triggered by an altered fibronectin matrix: JNK links FAKand p53. J. Biol. Chem. 280:19992-99
    • (2005) J. Biol. Chem. , vol.280 , pp. 19992-19999
    • Tafolla, E.1    Wang, S.2    Wong, B.3    Leong, J.4    Kapila, Y.L.5
  • 127
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5 beta1 in complex with fibronectin
    • Takagi J, Strokovich K, Springer TA, Walz T. 2003. Structure of integrin alpha5 beta1 in complex with fibronectin. EMBO J. 22:4607-15
    • (2003) EMBO J. , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 128
    • 7744232293 scopus 로고    scopus 로고
    • Activation of a signaling cascade by cytoskeleton stretch
    • Tamada M, Sheetz MP, Sawada Y. 2004. Activation of a signaling cascade by cytoskeleton stretch. Dev. Cell 7:709-18
    • (2004) Dev. Cell , vol.7 , pp. 709-718
    • Tamada, M.1    Sheetz, M.P.2    Sawada, Y.3
  • 130
    • 2442457727 scopus 로고    scopus 로고
    • Mechanotransduction through growth-factor shedding into the extracellular space
    • Tschumperlin DJ, Dai G, Maly IV, Kikuchi T, Laiho LH, et al. 2004. Mechanotransduction through growth-factor shedding into the extracellular space. Nature 429:83-86
    • (2004) Nature , vol.429 , pp. 83-86
    • Tschumperlin, D.J.1    Dai, G.2    Maly, I.V.3    Kikuchi, T.4    Laiho, L.H.5
  • 131
    • 0036926739 scopus 로고    scopus 로고
    • Micromechanical mapping of live cells by multiple-particle-tracking microrheology
    • Tseng Y, Kole TP, Wirtz D. 2002. Micromechanical mapping of live cells by multiple-particle-tracking microrheology. Biophys. J. 83:3162-76
    • (2002) Biophys. J. , vol.83 , pp. 3162-3176
    • Tseng, Y.1    Kole, T.P.2    Wirtz, D.3
  • 133
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova L, Trinick J, Sleep JA, Simmons RM. 1997. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387:308-12
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 134
    • 5044226624 scopus 로고    scopus 로고
    • Mechanical properties, proteolytic degradability and biological modifications affect angiogenic process extension into native and modified fibrin matrices in vitro
    • Urech L, Bittermann AG, Hubbell JA, Hall H. 2005. Mechanical properties, proteolytic degradability and biological modifications affect angiogenic process extension into native and modified fibrin matrices in vitro. Biomaterials 26:1369-79
    • (2005) Biomaterials , vol.26 , pp. 1369-1379
    • Urech, L.1    Bittermann, A.G.2    Hubbell, J.A.3    Hall, H.4
  • 136
    • 0036127725 scopus 로고    scopus 로고
    • Function of linear and cyclic RGD-containing peptides in osteoprogenitor cells adhesion process
    • Verrier S, Pallu S, Bareille R, Jonczyk A, Meyer J, et al. 2002. Function of linear and cyclic RGD-containing peptides in osteoprogenitor cells adhesion process. Biomaterials 23:585-96
    • (2002) Biomaterials , vol.23 , pp. 585-596
    • Verrier, S.1    Pallu, S.2    Bareille, R.3    Jonczyk, A.4    Meyer, J.5
  • 137
    • 0642336162 scopus 로고    scopus 로고
    • The tissue engineering puzzle: A molecular perspective
    • Vogel V, Baneyx G. 2003. The tissue engineering puzzle: a molecular perspective. Annu. Rev. Biomed. Eng. 5:441-63
    • (2003) Annu. Rev. Biomed. Eng. , vol.5 , pp. 441-463
    • Vogel, V.1    Baneyx, G.2
  • 138
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V, Sheetz MP. 2006. Local force and geometry sensing regulate cell functions. Nat. Rev. Mol. Cell Biol. 7:1-11
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 1-11
    • Vogel, V.1    Sheetz, M.P.2
  • 139
    • 0141865507 scopus 로고    scopus 로고
    • Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2
    • von Wiehert G, Haimovich B, Feng GS, Sheetz MP. 2003. Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2. EMBO J. 22:5023-35
    • (2003) EMBO J. , vol.22 , pp. 5023-5035
    • Von Wiehert, G.1    Haimovich, B.2    Feng, G.S.3    Sheetz, M.P.4
  • 140
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • von Wiehert G, Jiang G, Kostic A, De Vos K, Sap J, Sheetz MP. 2003. RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin- cytoskeleton linkages. J. Cell Biol. 161:143-53
    • (2003) J. Cell Biol. , vol.161 , pp. 143-153
    • Von Wiehert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 141
    • 18744374455 scopus 로고    scopus 로고
    • Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments
    • Watanabe K, Muhle-Goll C, Kellermayer MS, Labeit S, Granzier H. 2002. Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments. J. Struct. Biol. 137:248-58
    • (2002) J. Struct. Biol. , vol.137 , pp. 248-258
    • Watanabe, K.1    Muhle-Goll, C.2    Kellermayer, M.S.3    Labeit, S.4    Granzier, H.5
  • 142
    • 0027205405 scopus 로고
    • Secondary structure of a pair of fibronectin type 1 modules by two-dimensional nuclear magnetic resonance
    • Williams MJ, Phan I, Baron M, Driscoll PC, Campbell ID. 1993. Secondary structure of a pair of fibronectin type 1 modules by two-dimensional nuclear magnetic resonance. Biochemistry 32:7388-95
    • (1993) Biochemistry , vol.32 , pp. 7388-7395
    • Williams, M.J.1    Phan, I.2    Baron, M.3    Driscoll, P.C.4    Campbell, I.D.5
  • 144
    • 19944428596 scopus 로고    scopus 로고
    • Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion
    • Yeung T, Georges PC, Flanagan LA, Marg B, Ortiz M, et al. 2005. Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion. Cell Motil. Cytoskelet. 60:24-34
    • (2005) Cell Motil. Cytoskelet. , vol.60 , pp. 24-34
    • Yeung, T.1    Georges, P.C.2    Flanagan, L.A.3    Marg, B.4    Ortiz, M.5
  • 146
  • 147
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C, Chrzanowska-Wodnicka M, Brown J, Shaub A, Belkin AM, Burridge K. 1998. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141:539-51
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.