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Volumn 3, Issue 5, 2011, Pages 1-21

Molecular architecture and function of matrix adhesions

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; INTEGRIN;

EID: 80053298724     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a005033     Document Type: Article
Times cited : (412)

References (144)
  • 1
    • 0014750098 scopus 로고
    • The locomotion of fibroblasts in culture. I. Movements of the leading edge
    • Abercrombie M, Heaysman JE, Pegrum SM. 1970. The locomotion of fibroblasts in culture. I. Movements of the leading edge. Exp Cell Res 59: 393-398.
    • (1970) Exp Cell Res , vol.59 , pp. 393-398
    • Abercrombie, M.1    Heaysman, J.E.2    Pegrum, S.M.3
  • 2
    • 67650716492 scopus 로고    scopus 로고
    • The ins and outs of leukocyte integrin signaling
    • Abram CL, Lowell CA. 2009. The ins and outs of leukocyte integrin signaling. Annu Rev Immunol 27: 339-362.
    • (2009) Annu Rev Immunol , vol.27 , pp. 339-362
    • Abram, C.L.1    Lowell, C.A.2
  • 3
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama SK, Yamada SS, Chen WT, Yamada KM. 1989. Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J Cell Biol 109: 863-875.
    • (1989) J Cell Biol , vol.109 , pp. 863-875
    • Akiyama, S.K.1    Yamada, S.S.2    Chen, W.T.3    Yamada, K.M.4
  • 5
    • 52449089651 scopus 로고    scopus 로고
    • Comparative dynamics of retrograde actin flow and focal adhesions: Formation of nascent adhesions triggers transition from fast to slow flow
    • Alexandrova AY, Arnold K, Schaub S, Vasiliev JM, Meister JJ, Bershadsky AD, Verkhovsky AB. 2008. Comparative dynamics of retrograde actin flow and focal adhesions: Formation of nascent adhesions triggers transition from fast to slow flow. PLoS ONE 3: e3234.
    • (2008) PLoS ONE , vol.3
    • Alexandrova, A.Y.1    Arnold, K.2    Schaub, S.3    Vasiliev, J.M.4    Meister, J.J.5    Bershadsky, A.D.6    Verkhovsky, A.B.7
  • 6
    • 24644466511 scopus 로고    scopus 로고
    • Stroma-derived three-dimensional matrices are necessary and sufficient to promote desmoplastic differentiation of normal fibroblasts
    • Amatangelo MD, Bassi DE, Klein-Szanto AJ, Cukierman E. 2005. Stroma-derived three-dimensional matrices are necessary and sufficient to promote desmoplastic differentiation of normal fibroblasts. Am J Pathol 167: 475-488.
    • (2005) Am J Pathol , vol.167 , pp. 475-488
    • Amatangelo, M.D.1    Bassi, D.E.2    Klein-Szanto, A.J.3    Cukierman, E.4
  • 7
    • 79151475365 scopus 로고    scopus 로고
    • Dynamic membrane remodeling at invadopodia differentiates invadopodia from podosomes
    • Artym VV, Matsumoto K, Mueller SC, Yamada KM. 2011. Dynamic membrane remodeling at invadopodia differentiates invadopodia from podosomes. Eur J Cell Biol 90: 172-180.
    • (2011) Eur J Cell Biol , vol.90 , pp. 172-180
    • Artym, V.V.1    Matsumoto, K.2    Mueller, S.C.3    Yamada, K.M.4
  • 8
    • 23244433980 scopus 로고    scopus 로고
    • Substratum roughness alters the growth, area, and focal adhesions of epithelial cells, and their proximity to titanium surfaces
    • Baharloo B, Textor M, Brunette DM. 2005. Substratum roughness alters the growth, area, and focal adhesions of epithelial cells, and their proximity to titanium surfaces. J Biomed Mater Res A 74: 12-22.
    • (2005) J Biomed Mater Res A , vol.74 , pp. 12-22
    • Baharloo, B.1    Textor, M.2    Brunette, D.M.3
  • 10
    • 33645234372 scopus 로고    scopus 로고
    • Molecular mapping of tyrosine-phosphorylated proteins in focal adhesions using fluorescence resonance energy transfer
    • Ballestrem C, Erez N, Kirchner J, Kam Z, Bershadsky A, Geiger B. 2006. Molecular mapping of tyrosine-phosphorylated proteins in focal adhesions using fluorescence resonance energy transfer. J Cell Sci 119: 866-875.
    • (2006) J Cell Sci , vol.119 , pp. 866-875
    • Ballestrem, C.1    Erez, N.2    Kirchner, J.3    Kam, Z.4    Bershadsky, A.5    Geiger, B.6
  • 11
    • 0035945353 scopus 로고    scopus 로고
    • Marching at the front and dragging behind: Differential αVβ3-integrin turnover regulates focal adhesion behavior
    • Ballestrem C, Hinz B, Imhof BA, Wehrle-Haller B. 2001. Marching at the front and dragging behind: Differential αVβ3-integrin turnover regulates focal adhesion behavior. J Cell Biol 155: 1319-1332.
    • (2001) J Cell Biol , vol.155 , pp. 1319-1332
    • Ballestrem, C.1    Hinz, B.2    Imhof, B.A.3    Wehrle-Haller, B.4
  • 12
    • 23744432972 scopus 로고    scopus 로고
    • Stromagenesis: The changing face of fibroblastic microenvironments during tumor progression
    • Beacham DA, Cukierman E. 2005. Stromagenesis: The changing face of fibroblastic microenvironments during tumor progression. Semin Cancer Biol 15: 329-341.
    • (2005) Semin Cancer Biol , vol.15 , pp. 329-341
    • Beacham, D.A.1    Cukierman, E.2
  • 16
    • 0028171951 scopus 로고
    • Integrin αvβ3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor α5β1
    • Blystone SD, Graham IL, Lindberg FP, Brown EJ. 1994. Integrin αvβ3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor α5β1. J Cell Biol 127: 1129-1137.
    • (1994) J Cell Biol , vol.127 , pp. 1129-1137
    • Blystone, S.D.1    Graham, I.L.2    Lindberg, F.P.3    Brown, E.J.4
  • 17
    • 0033577813 scopus 로고    scopus 로고
    • A molecular mechanism of integrin crosstalk: αvβ3 suppression of calcium/calmodulin-dependent protein kinase II regulates α5β1 function
    • Blystone SD, Slater SE, Williams MP, Crow MT, Brown EJ. 1999. A molecular mechanism of integrin crosstalk: αvβ3 suppression of calcium/calmodulin-dependent protein kinase II regulates α5β1 function. J Cell Biol 145: 889-897.
    • (1999) J Cell Biol , vol.145 , pp. 889-897
    • Blystone, S.D.1    Slater, S.E.2    Williams, M.P.3    Crow, M.T.4    Brown, E.J.5
  • 19
  • 21
    • 84863900703 scopus 로고    scopus 로고
    • Integrin structure, activation, and interactions
    • doi:10.1101/cshperspect.a004994
    • Campbell ID, Humphries MJ. 2011. Integrin structure, activation, and interactions. Cold Spring Harb Perspect Biol doi:10.1101/cshperspect.a004994.
    • (2011) Cold Spring Harb Perspect Biol
    • Campbell, I.D.1    Humphries, M.J.2
  • 22
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty EG, Lu Y, Meadows RS, Shaw MK, Holmes DF, Kadler KE. 2004. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J Cell Biol 165: 553-563.
    • (2004) J Cell Biol , vol.165 , pp. 553-563
    • Canty, E.G.1    Lu, Y.2    Meadows, R.S.3    Shaw, M.K.4    Holmes, D.F.5    Kadler, K.E.6
  • 24
    • 0027967292 scopus 로고
    • A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK
    • Chan PY, Kanner SB, Whitney G, Aruffo A. 1994. A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK. J Biol Chem 269: 20567-20574.
    • (1994) J Biol Chem , vol.269 , pp. 20567-20574
    • Chan, P.Y.1    Kanner, S.B.2    Whitney, G.3    Aruffo, A.4
  • 25
    • 77954977386 scopus 로고    scopus 로고
    • Type I PIPK-α regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation
    • Chao WT, Daquinag AC, Ashcroft F, Kunz J. 2010. Type I PIPK-α regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation. J Cell Biol 190: 247-262.
    • (2010) J Cell Biol , vol.190 , pp. 247-262
    • Chao, W.T.1    Daquinag, A.C.2    Ashcroft, F.3    Kunz, J.4
  • 26
    • 0020411692 scopus 로고
    • Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts
    • Chen WT, Singer SJ. 1982. Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts. J Cell Biol 95: 205-222.
    • (1982) J Cell Biol , vol.95 , pp. 205-222
    • Chen, W.T.1    Singer, S.J.2
  • 27
  • 28
    • 51049104617 scopus 로고    scopus 로고
    • Actin and α-actinin orchestrate the assembly andmaturation of nascent adhesions in amyosin II motor-independent manner
    • Choi CK, Vicente-Manzanares M, Zareno J, Whitmore LA, Mogilner A, Horwitz AR. 2008. Actin and α-actinin orchestrate the assembly andmaturation of nascent adhesions in amyosin II motor-independent manner. Nat Cell Biol 10: 1039-1050.
    • (2008) Nat Cell Biol , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 29
    • 0037780985 scopus 로고    scopus 로고
    • The liberation of CD44
    • Cichy J, Pure E. 2003. The liberation of CD44. J Cell Biol 161: 839-843.
    • (2003) J Cell Biol , vol.161 , pp. 839-843
    • Cichy, J.1    Pure, E.2
  • 30
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. 1995. Integrins and signal transduction pathways: The road taken. Science 268: 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 33
    • 33744929406 scopus 로고    scopus 로고
    • A conformational switch in vinculin drives formation and dynamics of a talin-vinculin complex at focal adhesions
    • Cohen DM, Kutscher B, Chen H, Murphy DB, Craig SW. 2006. A conformational switch in vinculin drives formation and dynamics of a talin-vinculin complex at focal adhesions. J Biol Chem 281: 16006-16015.
    • (2006) J Biol Chem , vol.281 , pp. 16006-16015
    • Cohen, D.M.1    Kutscher, B.2    Chen, H.3    Murphy, D.B.4    Craig, S.W.5
  • 34
    • 0018651705 scopus 로고
    • The behaviour of fibroblasts migrating from chick heart explants: Changes in adhesion, locomotion and growth, and in the distribution of actomyosin and fibronectin
    • Couchman JR, Rees DA. 1979. The behaviour of fibroblasts migrating from chick heart explants: Changes in adhesion, locomotion and growth, and in the distribution of actomyosin and fibronectin. J Cell Sci 39: 149-165.
    • (1979) J Cell Sci , vol.39 , pp. 149-165
    • Couchman, J.R.1    Rees, D.A.2
  • 35
    • 8744300054 scopus 로고    scopus 로고
    • Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion
    • Critchley DR. 2004. Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. Biochem Soc Trans 32: 831-836.
    • (2004) Biochem Soc Trans , vol.32 , pp. 831-836
    • Critchley, D.R.1
  • 36
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • Cukierman E, Pankov R, Stevens DR, Yamada KM. 2001. Taking cell-matrix adhesions to the third dimension. Science 294: 1708-1712.
    • (2001) Science , vol.294 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 37
    • 0031421084 scopus 로고    scopus 로고
    • Topographical control of cells
    • Curtis A, Wilkinson C. 1997. Topographical control of cells. Biomaterials 18: 1573-1583.
    • (1997) Biomaterials , vol.18 , pp. 1573-1583
    • Curtis, A.1    Wilkinson, C.2
  • 38
    • 0021957079 scopus 로고
    • Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture
    • Damsky CH, Knudsen KA, BradleyD, BuckCA, Horwitz AF. 1985. Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture. J Cell Biol 100: 1528-1539.
    • (1985) J Cell Biol , vol.100 , pp. 1528-1539
    • Damsky, C.H.1    Knudsen, K.A.2    Bradley, D.3    Buck, C.A.4    Horwitz, A.F.5
  • 39
    • 0028219509 scopus 로고
    • Quantitative studies of endothelial cell adhesion. Directional remodeling of focal adhesion sites in response to flow forces
    • Davies PF, Robotewskyj A, Griem ML. 1994. Quantitative studies of endothelial cell adhesion. Directional remodeling of focal adhesion sites in response to flow forces. J Clin Invest 93: 2031-2038.
    • (1994) J Clin Invest , vol.93 , pp. 2031-2038
    • Davies, P.F.1    Robotewskyj, A.2    Griem, M.L.3
  • 41
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher DE, Janmey P, Wang YL. 2005. Tissue cells feel and respond to the stiffness of their substrate. Science 310: 1139-1143.
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.L.3
  • 42
    • 67649920749 scopus 로고    scopus 로고
    • Growth factors, matrices, and forces combine and control stem cells
    • Discher DE, Mooney DJ, Zandstra PW. 2009. Growth factors, matrices, and forces combine and control stem cells. Science 324: 1673-1677.
    • (2009) Science , vol.324 , pp. 1673-1677
    • Discher, D.E.1    Mooney, D.J.2    Zandstra, P.W.3
  • 43
    • 61449181308 scopus 로고    scopus 로고
    • One-dimensional topography underlies threedimensional fibrillar cell migration
    • Doyle AD, Wang FW, Matsumoto K, Yamada KM. 2009. One-dimensional topography underlies threedimensional fibrillar cell migration. J Cell Biol 184: 481-490.
    • (2009) J Cell Biol , vol.184 , pp. 481-490
    • Doyle, A.D.1    Wang, F.W.2    Matsumoto, K.3    Yamada, K.M.4
  • 45
    • 0032032879 scopus 로고    scopus 로고
    • Michael Abercrombie: The pioneer ethologist of cells
    • Dunn G, Jones G. 1998. Michael Abercrombie: The pioneer ethologist of cells. Trends Cell Biol 8: 124-126.
    • (1998) Trends Cell Biol , vol.8 , pp. 124-126
    • Dunn, G.1    Jones, G.2
  • 46
    • 0015402532 scopus 로고
    • Collagen substrata for studies on cell behavior
    • Elsdale T, Bard J. 1972. Collagen substrata for studies on cell behavior. J Cell Biol 54: 626-637.
    • (1972) J Cell Biol , vol.54 , pp. 626-637
    • Elsdale, T.1    Bard, J.2
  • 49
    • 9644289575 scopus 로고    scopus 로고
    • Integrins: Versatile integrators of extracellular signals
    • Ffrench-Constant C, Colognato H. 2004. Integrins: Versatile integrators of extracellular signals. Trends Cell Biol 14: 678-686.
    • (2004) Trends Cell Biol , vol.14 , pp. 678-686
    • Ffrench-Constant, C.1    Colognato, H.2
  • 50
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls α5β1 function
    • Friedland JC, Lee MH, BoettigerD. 2009. Mechanically activated integrin switch controls α5β1 function. Science 323: 642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 51
    • 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
  • 53
    • 77951764386 scopus 로고    scopus 로고
    • Nano-topography sensing by osteoclasts
    • Geblinger D, Addadi L, Geiger B. 2010. Nano-topography sensing by osteoclasts. J Cell Sci 123: 1503-1510.
    • (2010) J Cell Sci , vol.123 , pp. 1503-1510
    • Geblinger, D.1    Addadi, L.2    Geiger, B.3
  • 54
    • 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
  • 56
  • 59
    • 0028898814 scopus 로고
    • Shear stress modulates endothelial cell morphology and F-actin organization through the regulation of focal adhesion-associated proteins
    • Girard PR, Nerem RM. 1995. Shear stress modulates endothelial cell morphology and F-actin organization through the regulation of focal adhesion-associated proteins. J Cell Physiol 163: 179-193.
    • (1995) J Cell Physiol , vol.163 , pp. 179-193
    • Girard, P.R.1    Nerem, R.M.2
  • 60
    • 75049085620 scopus 로고    scopus 로고
    • Transdominant regulation of integrin function: Mechanisms of crosstalk
    • Gonzalez AM, Bhattacharya R, deHart GW, Jones JC. 2010. Transdominant regulation of integrin function: Mechanisms of crosstalk. Cell Signal 22: 578-583.
    • (2010) Cell Signal , vol.22 , pp. 578-583
    • Gonzalez, A.M.1    Bhattacharya, R.2    deHart, G.W.3    Jones, J.C.4
  • 61
    • 0012077872 scopus 로고
    • Permissive effect of the extracellular matrix on cell proliferation in vitro
    • Gospodarowicz D, Delgado D, Vlodavsky I. 1980. Permissive effect of the extracellular matrix on cell proliferation in vitro. Proc Natl Acad Sci 77: 4094-4098.
    • (1980) Proc Natl Acad Sci , vol.77 , pp. 4094-4098
    • Gospodarowicz, D.1    Delgado, D.2    Vlodavsky, I.3
  • 63
    • 78049365986 scopus 로고    scopus 로고
    • Cell motility and mechanics in three-dimensional collagen matrices
    • Grinnell F, PetrollWM.2010. Cell motility and mechanics in three-dimensional collagen matrices. Annu Rev Cell Dev Biol 26: 335-361.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 335-361
    • Grinnell, F.1    Petroll, W.M.2
  • 65
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger DS, Calderwood DA. 2009. Integrin signalling at a glance. J Cell Sci 122: 159-163.
    • (2009) J Cell Sci , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 67
    • 0015939746 scopus 로고
    • Early contacts between fibroblasts: An ultrastructural study
    • Heaysman J. 1973. Early contacts between fibroblasts: An ultrastructural study. Exp Cell Res 78: 71-78.
    • (1973) Exp Cell Res , vol.78 , pp. 71-78
    • Heaysman, J.1
  • 73
    • 66849101632 scopus 로고    scopus 로고
    • Adhesion signaling-crosstalk between integrins, Src and Rho
    • Huveneers S, Danen EH. 2009. Adhesion signaling-crosstalk between integrins, Src and Rho. J Cell Sci 122: 1059-1069.
    • (2009) J Cell Sci , vol.122 , pp. 1059-1069
    • Huveneers, S.1    Danen, E.H.2
  • 74
    • 84863872223 scopus 로고    scopus 로고
    • Overview of the matrisome-ECM inventory
    • doi:10.1101/cshperspect.a004903
    • Hynes RO. 2011. Overview of the matrisome-ECM inventory. Cold Spring Harb Perspect Biol doi:10.1101/cshperspect.a004903.
    • (2011) Cold Spring Harb Perspect Biol
    • Hynes, R.O.1
  • 75
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. 2002. Integrins: Bidirectional, allosteric signaling machines. Cell 110: 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 76
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • Hynes RO. 2009. The extracellular matrix: Not just pretty fibrils. Science 326: 1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 77
    • 0018036788 scopus 로고
    • Relationships between fibronectin (LETS protein) and actin
    • Hynes RO, Destree AT. 1978. Relationships between fibronectin (LETS protein) and actin. Cell 15: 875-886.
    • (1978) Cell , vol.15 , pp. 875-886
    • Hynes, R.O.1    Destree, A.T.2
  • 78
    • 0017143820 scopus 로고
    • Cell-to-substrate contacts in living fibroblasts: An interference reflexion study with an evaluation of the technique
    • Izzard CS, Lochner LR. 1976. Cell-to-substrate contacts in living fibroblasts: An interference reflexion study with an evaluation of the technique. J Cell Sci 21: 129-159.
    • (1976) J Cell Sci , vol.21 , pp. 129-159
    • Izzard, C.S.1    Lochner, L.R.2
  • 79
    • 67650999875 scopus 로고    scopus 로고
    • The basics of epithelialmesenchymal transition
    • Kalluri R, Weinberg RA. 2009. The basics of epithelialmesenchymal transition. J Clin Invest 119: 1420-1428.
    • (2009) J Clin Invest , vol.119 , pp. 1420-1428
    • Kalluri, R.1    Weinberg, R.A.2
  • 80
  • 81
    • 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: 1047-1060.
    • (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
  • 84
    • 2442519018 scopus 로고    scopus 로고
    • Selectins in T-cell recruitment to non-lymphoid tissues and sites of inflammation
    • Ley K, Kansas GS. 2004. Selectins in T-cell recruitment to non-lymphoid tissues and sites of inflammation. Nat Rev Immunol 4: 325-335.
    • (2004) Nat Rev Immunol , vol.4 , pp. 325-335
    • Ley, K.1    Kansas, G.S.2
  • 86
    • 0025881229 scopus 로고
    • An RGD spacing of 440 nm is sufficient for integrin αvβ3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation
    • Massia SP, Hubbell JA. 1991. An RGD spacing of 440 nm is sufficient for integrin αvβ3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation. J Cell Biol 114: 1089-1100.
    • (1991) J Cell Biol , vol.114 , pp. 1089-1100
    • Massia, S.P.1    Hubbell, J.A.2
  • 87
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra SK, Schlaepfer DD. 2006. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr Opin Cell Biol 18: 516-523.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 89
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto S, Teramoto H, Gutkind JS, Yamada KM. 1996. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors. J Cell Biol 135: 1633-1642.
    • (1996) J Cell Biol , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 92
    • 84863878959 scopus 로고    scopus 로고
    • Cross talk among TGF signaling pathways, integrins, and the extracellular matrix
    • doi:10.1101/cshperspect.a005017
    • Munger JS, Sheppard D. 2011. Cross talk among TGF signaling pathways, integrins, and the extracellular matrix. Cold Spring Harb Perspect Biol doi:10.1101/cshperspect.a005017.
    • (2011) Cold Spring Harb Perspect Biol
    • Munger, J.S.1    Sheppard, D.2
  • 93
    • 33748967069 scopus 로고    scopus 로고
    • Of extracellular matrix, scaffolds, and signaling: Tissue architecture regulates development, homeostasis, and cancer
    • Nelson CM, Bissell MJ. 2006. Of extracellular matrix, scaffolds, and signaling: Tissue architecture regulates development, homeostasis, and cancer. Annu Rev Cell Dev Biol 22: 287-309.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 287-309
    • Nelson, C.M.1    Bissell, M.J.2
  • 94
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81: 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 96
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of α(5)β(1) integrins promotes early fibronectin fibrillogenesis
    • Pankov R, Cukierman E, Katz BZ, Matsumoto K, Lin DC, Lin S, Hahn C, Yamada KM. 2000. Integrin dynamics and matrix assembly: Tensin-dependent translocation of α(5)β(1) integrins promotes early fibronectin fibrillogenesis. J Cell Biol 148: 1075-1090.
    • (2000) J Cell Biol , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5    Lin, S.6    Hahn, C.7    Yamada, K.M.8
  • 98
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham RJJr, Wang Y. 1997. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc Natl Acad Sci 94: 13661-13665.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 13661-13665
    • Pelham Jr., R.J.1    Wang, Y.2
  • 99
  • 100
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia
    • Poincloux R, Lizarraga F, Chavrier P. 2009. Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia. J Cell Sci 122: 3015-3024.
    • (2009) J Cell Sci , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizarraga, F.2    Chavrier, P.3
  • 103
    • 60549092844 scopus 로고    scopus 로고
    • Rheostatic signaling by CD44 and hyaluronan
    • Pure E, Assoian RK. 2009. Rheostatic signaling by CD44 and hyaluronan. Cell Signal 21: 651-655.
    • (2009) Cell Signal , vol.21 , pp. 651-655
    • Pure, E.1    Assoian, R.K.2
  • 105
    • 0023851499 scopus 로고
    • Contact formation during fibroblast locomotion: Involvement of membrane ruffles and microtubules
    • Rinnerthaler G, Geiger B, Small JV. 1988. Contact formation during fibroblast locomotion: Involvement of membrane ruffles and microtubules. J Cell Biol 106: 747-760.
    • (1988) J Cell Biol , vol.106 , pp. 747-760
    • Rinnerthaler, G.1    Geiger, B.2    Small, J.V.3
  • 106
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner K, Hall A, Small JV. 1999. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr Biol 9: 640-648.
    • (1999) Curr Biol , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 109
    • 79952598024 scopus 로고    scopus 로고
    • Integrins and extracellular matrix in mechanotransduction
    • Schwartz MA. 2010. Integrins and extracellular matrix in mechanotransduction. Cold Spring Harb Perspect Biol 2010 2:a005066
    • (2010) Cold Spring Harb Perspect Biol 2010 , vol.2
    • Schwartz, M.A.1
  • 110
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz MA, Ginsberg MH. 2002. Networks and crosstalk: Integrin signalling spreads. Nat Cell Biol 4: E65-E68.
    • (2002) Nat Cell Biol , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 112
    • 84863875404 scopus 로고    scopus 로고
    • Fibronectins, their fibrillogenesis, and in vivo functions
    • doi:10.1101/cshperspect.a005041
    • Schwarzbauer JE, DeSimone DW. 2011. Fibronectins, their fibrillogenesis, and in vivo functions. Cold Spring Harb Perspect Biol doi:10.1101/cshperspect.a005041.
    • (2011) Cold Spring Harb Perspect Biol
    • Schwarzbauer, J.E.1    DeSimone, D.W.2
  • 115
    • 0018344535 scopus 로고
    • The fibronexus: A transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts
    • Singer II. 1979. The fibronexus: A transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts. Cell 16: 675-685.
    • (1979) Cell , vol.16 , pp. 675-685
    • Singer, I.I.1
  • 116
    • 0037221714 scopus 로고    scopus 로고
    • Microtubules meet substrate adhesions to arrange cell polarity
    • Small JV, Kaverina I. 2003. Microtubules meet substrate adhesions to arrange cell polarity. Curr Opin Cell Biol 15: 40-47.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 40-47
    • Small, J.V.1    Kaverina, I.2
  • 117
    • 0022647386 scopus 로고
    • Localization of filamin in smooth muscle
    • Small JV, Furst DO, De Mey J. 1986. Localization of filamin in smooth muscle. J Cell Biol 102: 210-220.
    • (1986) J Cell Biol , vol.102 , pp. 210-220
    • Small, J.V.1    Furst, D.O.2    de Mey, J.3
  • 118
    • 33644945032 scopus 로고    scopus 로고
    • Podosomes as smart regulators of cellular adhesion
    • Spinardi L, Marchisio PC. 2006. Podosomes as smart regulators of cellular adhesion. Eur J Cell Biol 85: 191-194.
    • (2006) Eur J Cell Biol , vol.85 , pp. 191-194
    • Spinardi, L.1    Marchisio, P.C.2
  • 119
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • Streuli CH, Akhtar N. 2009. Signal co-operation between integrins and other receptor systems. Biochem J 418: 491-506.
    • (2009) Biochem J , vol.418 , pp. 491-506
    • Streuli, C.H.1    Akhtar, N.2
  • 121
  • 122
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery JP, Acloque H, Huang RY, Nieto MA. 2009. Epithelial-mesenchymal transitions in development and disease. Cell 139: 871-890.
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2    Huang, R.Y.3    Nieto, M.A.4
  • 123
    • 0037085254 scopus 로고    scopus 로고
    • Signaling properties of hyaluronan receptors
    • Turley EA, Noble PW, Bourguignon LY. 2002. Signaling properties of hyaluronan receptors. J Biol Chem 277: 4589-4592.
    • (2002) J Biol Chem , vol.277 , pp. 4589-4592
    • Turley, E.A.1    Noble, P.W.2    Bourguignon, L.Y.3
  • 124
    • 0034973825 scopus 로고    scopus 로고
    • Combinatorial signals by inflammatory cytokines and chemokines mediate leukocyte interactions with extracellular matrix
    • Vaday GG, Franitza S, Schor H, Hecht I, Brill A, Cahalon L, Hershkoviz R, Lider O. 2001. Combinatorial signals by inflammatory cytokines and chemokines mediate leukocyte interactions with extracellular matrix. J Leukoc Biol 69: 885-892.
    • (2001) J Leukoc Biol , vol.69 , pp. 885-892
    • Vaday, G.G.1    Franitza, S.2    Schor, H.3    Hecht, I.4    Brill, A.5    Cahalon, L.6    Hershkoviz, R.7    Lider, O.8
  • 125
    • 3042831741 scopus 로고    scopus 로고
    • Simultaneous mapping of filamentous actin flow and turnover in migrating cells by quantitative fluorescent speckle microscopy
    • Vallotton P, Gupton SL, Waterman-Storer CM, Danuser G. 2004. Simultaneous mapping of filamentous actin flow and turnover in migrating cells by quantitative fluorescent speckle microscopy. Proc Natl Acad Sci 101: 9660-9665.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 9660-9665
    • Vallotton, P.1    Gupton, S.L.2    Waterman-Storer, C.M.3    Danuser, G.4
  • 126
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Vestweber D, Blanks JE. 1999. Mechanisms that regulate the function of the selectins and their ligands. Physiol Rev 79: 181-213.
    • (1999) Physiol Rev , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 127
    • 33646341752 scopus 로고    scopus 로고
    • Sensing extracellular matrix: An update on discoidin domain receptor function
    • Vogel WF, Abdulhussein R, Ford CE. 2006. Sensing extracellular matrix: An update on discoidin domain receptor function. Cell Signal 18: 1108-1116.
    • (2006) Cell Signal , vol.18 , pp. 1108-1116
    • Vogel, W.F.1    Abdulhussein, R.2    Ford, C.E.3
  • 128
    • 0031964849 scopus 로고    scopus 로고
    • Integrin expression in developing smooth muscle cells
    • Wang R, Stromer MH, HuiattTW. 1998. Integrin expression in developing smooth muscle cells. J Histochem Cytochem 46: 119-126.
    • (1998) J Histochem Cytochem , vol.46 , pp. 119-126
    • Wang, R.1    Stromer, M.H.2    Huiatt, T.W.3
  • 129
    • 84863872233 scopus 로고    scopus 로고
    • Cell-extracellular matrix interactions in normal and diseased skin
    • doi:10.1101/cshperspect.a005124
    • Watt FM, Fujiwara H. 2011. Cell-extracellular matrix interactions in normal and diseased skin. Cold Spring Harb Perspect Biol doi:10.1101/cshperspect.a005124.
    • (2011) Cold Spring Harb Perspect Biol
    • Watt, F.M.1    Fujiwara, H.2
  • 130
    • 0020018204 scopus 로고
    • In memory of Michael Abercrombie
    • Weston JA. 1982. In memory of Michael Abercrombie. Prog Clin Biol Res 85: 1-4.
    • (1982) Prog Clin Biol Res , vol.85 , pp. 1-4
    • Weston, J.A.1
  • 132
    • 68549107934 scopus 로고    scopus 로고
    • Multiparametric analysis of focal adhesion formation by RNAi-mediated gene knockdown
    • Winograd-Katz SE, Itzkovitz S, KamZ, Geiger B. 2009. Multiparametric analysis of focal adhesion formation by RNAi-mediated gene knockdown. J Cell Biol 186: 423-436.
    • (2009) J Cell Biol , vol.186 , pp. 423-436
    • Winograd-Katz, S.E.1    Itzkovitz, S.2    Kam, Z.3    Geiger, B.4
  • 133
    • 70350235056 scopus 로고    scopus 로고
    • The heel and toe of the cell's foot: A multifaceted approach for understanding the structure and dynamics of focal adhesions
    • Wolfenson H, Henis YI, Geiger B, Bershadsky AD. 2009a. The heel and toe of the cell's foot: A multifaceted approach for understanding the structure and dynamics of focal adhesions. Cell Motil Cytoskeleton 66: 1017-1029.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 1017-1029
    • Wolfenson, H.1    Henis, Y.I.2    Geiger, B.3    Bershadsky, A.D.4
  • 134
  • 135
    • 34547931078 scopus 로고    scopus 로고
    • Modeling tissue morphogenesis and cancer in 3D
    • Yamada KM, Cukierman E. 2007. Modeling tissue morphogenesis and cancer in 3D. Cell 130: 601-610.
    • (2007) Cell , vol.130 , pp. 601-610
    • Yamada, K.M.1    Cukierman, E.2
  • 136
    • 84861222127 scopus 로고    scopus 로고
    • Basement membranes: Cell scaffoldings and signaling platforms
    • doi:10.1101/cshperspect.a004911
    • Yurchenco PD. 2011. Basement membranes: cell scaffoldings and signaling platforms. Cold Spring Harb Perspect Biol doi:10.1101/cshperspect.a004911.
    • (2011) Cold Spring Harb Perspect Biol
    • Yurchenco, P.D.1
  • 137
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • Zaidel-Bar R, Geiger B. 2010. The switchable integrin adhesome. J Cell Sci 123: 1385-1388.
    • (2010) J Cell Sci , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 138
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar R, Ballestrem C, Kam Z, Geiger B. 2003. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J Cell Sci 116: 4605-4613.
    • (2003) J Cell Sci , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 140
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar R, Milo R, Kam Z, Geiger B. 2007b. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J Cell Sci 120: 137-148.
    • (2007) J Cell Sci , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 141
    • 44849102214 scopus 로고    scopus 로고
    • Quantitative multicolor compositional imaging resolves molecular domains in cell-matrix adhesions
    • Zamir E, Geiger B, Kam Z. 2008. Quantitative multicolor compositional imaging resolves molecular domains in cell-matrix adhesions. PLoS ONE 3: e1901.
    • (2008) PLoS ONE , vol.3
    • Zamir, E.1    Geiger, B.2    Kam, Z.3
  • 143
    • 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: 539-551.
    • (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
  • 144
    • 0036218443 scopus 로고    scopus 로고
    • Initial stages of cell-matrix adhesion can be mediated and modulated by cell-surface hyaluronan
    • Zimmerman E, Geiger B, Addadi L. 2002. Initial stages of cell-matrix adhesion can be mediated and modulated by cell-surface hyaluronan. Biophys J 82: 1848-1857.
    • (2002) Biophys J , vol.82 , pp. 1848-1857
    • Zimmerman, E.1    Geiger, B.2    Addadi, L.3


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