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Volumn 126, Issue , 2014, Pages 55-73

Focal adhesions function as a mechanosensor

Author keywords

Cell migration; Focal adhesions; Integrins; Mechanosensitivity

Indexed keywords

INTEGRIN RECEPTOR;

EID: 84905194922     PISSN: 18771173     EISSN: 18780814     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394624-9.00003-8     Document Type: Chapter
Times cited : (34)

References (131)
  • 2
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • K. Burridge, K. Fath, T. Kelly, G. Nuckolls, and C. Turner Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton Annu Rev Cell Biol 4 1988 487 525 (Pubitemid 19139264)
    • (1988) Annual Review of Cell Biology , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 3
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • R.O. Hynes Integrins: bidirectional, allosteric signaling machines Cell 110 2002 673 687 (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 5
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • DOI 10.1016/j.ceb.2007.08.002, PII S0955067407001196, Cell to Cell Contact and Extracellular Matrix
    • M.A. Arnaout, S.L. Goodman, and J.P. Xiong Structure and mechanics of integrin-based cell adhesion Curr Opin Cell Biol 19 2007 495 507 (Pubitemid 350019555)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.-P.3
  • 7
    • 0033617417 scopus 로고    scopus 로고
    • Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations
    • T.M. Leisner, J.D. Wencel-Drake, W. Wang, and S.C. Lam Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations J Biol Chem 274 1999 12945 12949
    • (1999) J Biol Chem , vol.274 , pp. 12945-12949
    • Leisner, T.M.1    Wencel-Drake, J.D.2    Wang, W.3    Lam, S.C.4
  • 8
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • R. Zaidel-Bar, and B. Geiger The switchable integrin adhesome J Cell Sci 123 2010 1385 1388
    • (2010) J Cell Sci , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 10
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • DOI 10.1074/jbc.R900037199
    • D.A. Calderwood, S.J. Shattil, and M.H. Ginsberg Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling J Biol Chem 275 2000 22607 22610 (Pubitemid 30646138)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 11
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • M. Moser, K.R. Legate, R. Zent, and R. Fassler The tail of integrins, talin, and kindlins Science 324 2009 895 899
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 13
    • 0022973726 scopus 로고
    • Isolation and characterization of a conserved actin-binding domain from rat hepatic actinogelin, rat skeletal muscle, and chicken gizzard α-actinins
    • N. Mimura, and A. Asano Isolation and characterization of a conserved actin-binding domain from rat hepatic actinogelin, rat skeletal muscle, and chicken gizzard alpha-actinins J Biol Chem 261 1986 10680 10687 (Pubitemid 17194851)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.23 , pp. 10680-10687
    • Mimura, N.1    Asano, A.2
  • 14
    • 0023216026 scopus 로고
    • Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and α-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking
    • N. Mimura, and A. Asano Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and alpha-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking J Biol Chem 262 1987 4717 4723 (Pubitemid 17102843)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.10 , pp. 4717-4723
    • Mimura, N.1    Asano, A.2
  • 15
    • 0025291522 scopus 로고
    • An interaction between alpha-actinin and the beta 1 integrin subunit in vitro
    • C.A. Otey, F.M. Pavalko, and K. Burridge An interaction between alpha-actinin and the beta 1 integrin subunit in vitro J Cell Biol 111 1990 721 729
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 18
    • 0032483459 scopus 로고    scopus 로고
    • 1- integrin: Identification of amino acids responsible for this interaction
    • DOI 10.1074/jbc.273.36.23304
    • D.T. Loo, S.B. Kanner, and A. Aruffo Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction J Biol Chem 273 1998 23304 23312 (Pubitemid 28417517)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.36 , pp. 23304-23312
    • Loo, D.T.1    Kanner, S.B.2    Aruffo, A.3
  • 19
    • 0032513019 scopus 로고    scopus 로고
    • Integrin β cytoplasmic domains differentially bind to cytoskeletal proteins
    • DOI 10.1074/jbc.273.11.6104
    • M. Pfaff, S. Liu, D.J. Erle, and M.H. Ginsberg Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins J Biol Chem 273 1998 6104 6109 (Pubitemid 28144690)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.11 , pp. 6104-6109
    • Pfaff, M.1    Liu, S.2    Erle, D.J.3    Ginsberg, M.H.4
  • 21
    • 0033551783 scopus 로고    scopus 로고
    • The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation
    • C. Bachmann, L. Fischer, U. Walter, and M. Reinhard The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation J Biol Chem 274 1999 23549 23557
    • (1999) J Biol Chem , vol.274 , pp. 23549-23557
    • Bachmann, C.1    Fischer, L.2    Walter, U.3    Reinhard, M.4
  • 22
    • 0030790004 scopus 로고    scopus 로고
    • Ligand recruitment by vinculin domains in transfected cells
    • P. Bubeck, S. Pistor, J. Wehland, and B.M. Jockusch Ligand recruitment by vinculin domains in transfected cells J Cell Sci 110 Pt 12 1997 1361 1371 (Pubitemid 27299932)
    • (1997) Journal of Cell Science , vol.110 , Issue.12 , pp. 1361-1371
    • Bubeck, P.1    Pistor, S.2    Wehland, J.3    Jockusch, B.M.4
  • 23
    • 0033531927 scopus 로고    scopus 로고
    • An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment
    • M. Reinhard, J. Zumbrunn, D. Jaquemar, M. Kuhn, U. Walter, and B. Trueb An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment J Biol Chem 274 1999 13410 13418
    • (1999) J Biol Chem , vol.274 , pp. 13410-13418
    • Reinhard, M.1    Zumbrunn, J.2    Jaquemar, D.3    Kuhn, M.4    Walter, U.5    Trueb, B.6
  • 25
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • DOI 10.1016/S0962-8924(01)02154-7, PII S0962892401021547
    • T. Pawson, G.D. Gish, and P. Nash SH2 domains, interaction modules and cellular wiring Trends Cell Biol 11 2001 504 511 (Pubitemid 33079144)
    • (2001) Trends in Cell Biology , vol.11 , Issue.12 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 26
    • 0028915798 scopus 로고
    • Proline-rich sequences that bind to Src homology 3 domains with individual specificities
    • K. Alexandropoulos, G. Cheng, and D. Baltimore Proline-rich sequences that bind to Src homology 3 domains with individual specificities Proc Natl Acad Sci USA 92 1995 3110 3114
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3110-3114
    • Alexandropoulos, K.1    Cheng, G.2    Baltimore, D.3
  • 27
    • 0030583283 scopus 로고    scopus 로고
    • The pleckstrin homology domain of human βIΣII spectrin is targeted to the plasma membrane in vivo
    • DOI 10.1006/bbrc.1996.1189
    • D.S. Wang, R. Miller, R. Shaw, and G. Shaw The pleckstrin homology domain of human beta I sigma II spectrin is targeted to the plasma membrane in vivo Biochem Biophys Res Commun 225 1996 420 426 (Pubitemid 26355617)
    • (1996) Biochemical and Biophysical Research Communications , vol.225 , Issue.2 , pp. 420-426
    • Wang, D.-S.1    Miller, R.2    Shaw, R.3    Shaw, G.4
  • 28
    • 0029563928 scopus 로고
    • The association of the C-terminal region of beta i sigma II spectrin to brain membranes is mediated by a PH domain, does not require membrane proteins, and coincides with a inositol-1,4,5 triphosphate binding site
    • D.S. Wang, and G. Shaw The association of the C-terminal region of beta I sigma II spectrin to brain membranes is mediated by a PH domain, does not require membrane proteins, and coincides with a inositol-1,4,5 triphosphate binding site Biochem Biophys Res Commun 217 1995 608 615
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 608-615
    • Wang, D.S.1    Shaw, G.2
  • 29
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • M.A. Pearson, D. Reczek, A. Bretscher, and P.A. Karplus Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain Cell 101 2000 259 270
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 30
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler Syndrome Protein Is Regulated by Transforming Growth Factor-β and Involved in Integrin-mediated Adhesion
    • DOI 10.1074/jbc.M307978200
    • S. Kloeker, M.B. Major, D.A. Calderwood, M.H. Ginsberg, D.A. Jones, and M.C. Beckerle The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion J Biol Chem 279 2004 6824 6833 (Pubitemid 38248824)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6824-6833
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 32
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • DOI 10.1038/nm1722, PII NM1722
    • M. Moser, B. Nieswandt, S. Ussar, M. Pozgajova, and R. Fassler Kindlin-3 is essential for integrin activation and platelet aggregation Nat Med 14 2008 325 330 (Pubitemid 351347914)
    • (2008) Nature Medicine , vol.14 , Issue.3 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 34
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • J. Castresana, and M. Saraste Does Vav bind to F-actin through a CH domain? FEBS Lett 374 1995 149 151
    • (1995) FEBS Lett , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 35
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • DOI 10.1038/nrm1499
    • J.L. Kadrmas, and M.C. Beckerle The LIM domain: from the cytoskeleton to the nucleus Nat Rev Mol Cell Biol 5 2004 920 931 (Pubitemid 39486543)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.11 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 36
    • 0037441865 scopus 로고    scopus 로고
    • Zyxin and paxillin proteins: Focal adhesion plaque LIM domain proteins go nuclear
    • DOI 10.1016/S0167-4889(02)00349-X
    • Y. Wang, and T.D. Gilmore Zyxin and paxillin proteins: focal adhesion plaque LIM domain proteins go nuclear Biochim Biophys Acta 1593 2003 115 120 (Pubitemid 36173479)
    • (2003) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1593 , Issue.2-3 , pp. 115-120
    • Wang, Y.1    Gilmore, T.D.2
  • 37
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • DOI 10.1083/jcb.133.6.1403
    • M. Chrzanowska-Wodnicka, and K. Burridge Rho-stimulated contractility drives the formation of stress fibers and focal adhesions J Cell Biol 133 1996 1403 1415 (Pubitemid 26192339)
    • (1996) Journal of Cell Biology , vol.133 , Issue.6 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 38
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • C.D. Nobes, and A. Hall Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia Cell 81 1995 53 62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 39
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • DOI 10.1016/S0960-9822(99)80286-3
    • K. Rottner, A. Hall, and J.V. Small Interplay between Rac and Rho in the control of substrate contact dynamics Curr Biol 9 1999 640 648 (Pubitemid 29291944)
    • (1999) Current Biology , vol.9 , Issue.12 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 40
    • 36348966706 scopus 로고    scopus 로고
    • Rho GTPases: Functions and association with cancer
    • DOI 10.1007/s10585-007-9119-1
    • S.I. Ellenbroek, and J.G. Collard Rho GTPases: functions and association with cancer Clin Exp Metastasis 24 2007 657 672 (Pubitemid 50002983)
    • (2007) Clinical and Experimental Metastasis , vol.24 , Issue.8 , pp. 657-672
    • Ellenbroek, S.I.J.1    Collard, J.G.2
  • 41
    • 27844604200 scopus 로고    scopus 로고
    • Rho GTPases and the control of cell behaviour
    • DOI 10.1042/BST20050891
    • A. Hall Rho GTPases and the control of cell behaviour Biochem Soc Trans 33 2005 891 895 (Pubitemid 41659073)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.5 , pp. 891-895
    • Hall, A.1
  • 43
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain
    • A. Bhatt, I. Kaverina, C. Otey, and A. Huttenlocher Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain J Cell Sci 115 2002 3415 3425 (Pubitemid 34994031)
    • (2002) Journal of Cell Science , vol.115 , Issue.17 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 44
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp 125(FAK), paxillin, and talin
    • N.O. Carragher, B. Levkau, R. Ross, and E.W. Raines Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp 125(FAK), paxillin, and talin J Cell Biol 147 1999 619 630
    • (1999) J Cell Biol , vol.147 , pp. 619-630
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 45
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • DOI 10.1242/jcs.02562
    • S.J. Franco, and A. Huttenlocher Regulating cell migration: calpains make the cut J Cell Sci 118 2005 3829 3838 (Pubitemid 41410267)
    • (2005) Journal of Cell Science , vol.118 , Issue.17 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 47
    • 0032860769 scopus 로고    scopus 로고
    • Calpain cleavage of integrin β cytoplasmic domains
    • DOI 10.1016/S0014-5793(99)01250-8, PII S0014579399012508
    • M. Pfaff, X. Du, and M.H. Ginsberg Calpain cleavage of integrin beta cytoplasmic domains FEBS Lett 460 1999 17 22 (Pubitemid 29479236)
    • (1999) FEBS Letters , vol.460 , Issue.1 , pp. 17-22
    • Pfaff, M.1    Du, X.2    Ginsberg, M.H.3
  • 49
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src
    • DOI 10.1016/S0960-9822(03)00544-X
    • N.O. Carragher, M.A. Westhoff, V.J. Fincham, M.D. Schaller, and M.C. Frame A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src Curr Biol 13 2003 1442 1450 (Pubitemid 37029436)
    • (2003) Current Biology , vol.13 , Issue.16 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 50
    • 77951242361 scopus 로고    scopus 로고
    • Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK)
    • K.T. Chan, D.A. Bennin, and A. Huttenlocher Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK) J Biol Chem 285 2010 11418 11426
    • (2010) J Biol Chem , vol.285 , pp. 11418-11426
    • Chan, K.T.1    Bennin, D.A.2    Huttenlocher, A.3
  • 51
    • 0034936674 scopus 로고    scopus 로고
    • Calpain function in the modulation of signal transduction molecules
    • DOI 10.1515/BC.2001.090
    • K. Sato, and S. Kawashima Calpain function in the modulation of signal transduction molecules Biol Chem 382 2001 743 751 (Pubitemid 32631711)
    • (2001) Biological Chemistry , vol.382 , Issue.5 , pp. 743-751
    • Sato, K.1    Kawashima, S.2
  • 53
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal Feedback between Actomyosin and Focal-Adhesion Systems Optimizes Rapid Cell Migration
    • DOI 10.1016/j.cell.2006.05.029, PII S0092867406007197
    • S.L. Gupton, and C.M. Waterman-Storer Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration Cell 125 2006 1361 1374 (Pubitemid 43929092)
    • (2006) Cell , vol.125 , Issue.7 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 54
    • 79952598024 scopus 로고    scopus 로고
    • Integrins and extracellular matrix in mechanotransduction
    • M.A. Schwartz Integrins and extracellular matrix in mechanotransduction Cold Spring Harb Perspect Biol 2 2010 a005066
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. 005066
    • Schwartz, M.A.1
  • 56
    • 44849102214 scopus 로고    scopus 로고
    • Quantitative multicolor compositional imaging resolves molecular domains in cell-matrix adhesions
    • E. Zamir, B. Geiger, and Z. Kam Quantitative multicolor compositional imaging resolves molecular domains in cell-matrix adhesions PLoS One 3 2008 e1901
    • (2008) PLoS One , vol.3 , pp. 1901
    • Zamir, E.1    Geiger, B.2    Kam, Z.3
  • 57
    • 79953325280 scopus 로고    scopus 로고
    • A role for actin arcs in the leading-edge advance of migrating cells
    • D.T. Burnette, S. Manley, and P. Sengupta et al. A role for actin arcs in the leading-edge advance of migrating cells Nat Cell Biol 13 2011 371 381
    • (2011) Nat Cell Biol , vol.13 , pp. 371-381
    • Burnette, D.T.1    Manley, S.2    Sengupta, P.3
  • 58
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • C.K. Choi, M. Vicente-Manzanares, J. Zareno, L.A. Whitmore, A. Mogilner, and A.R. Horwitz Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner Nat Cell Biol 10 2008 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
  • 60
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • DOI 10.1016/S0092-8674(03)00120-X
    • T.D. Pollard, and G.G. Borisy Cellular motility driven by assembly and disassembly of actin filaments Cell 112 2003 453 465 (Pubitemid 36263079)
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 61
    • 0036498546 scopus 로고    scopus 로고
    • The lamellipodium: Where motility begins
    • DOI 10.1016/S0962-8924(01)02237-1, PII S0962892401022371
    • J.V. Small, T. Stradal, E. Vignal, and K. Rottner The lamellipodium: where motility begins Trends Cell Biol 12 2002 112 120 (Pubitemid 34164650)
    • (2002) Trends in Cell Biology , vol.12 , Issue.3 , pp. 112-120
    • Small J.Victor1    Stradal, T.2    Vignal, E.3    Rottner, K.4
  • 65
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • J.T. Parsons, A.R. Horwitz, and M.A. Schwartz Cell adhesion: integrating cytoskeletal dynamics and cellular tension Nat Rev Mol Cell Biol 11 2010 633 643
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 66
    • 0030615004 scopus 로고    scopus 로고
    • P160(ROCK), a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • DOI 10.1016/S0014-5793(97)00107-5, PII S0014579397001075
    • T. Ishizaki, M. Naito, and K. Fujisawa et al. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions FEBS Lett. 404 1997 118 124 (Pubitemid 27113436)
    • (1997) FEBS Letters , vol.404 , Issue.2-3 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6    Narumiya, S.7
  • 67
    • 67650407445 scopus 로고    scopus 로고
    • Epidermal growth factor-induced contraction regulates paxillin phosphorylation to temporally separate traction generation from de-adhesion
    • I.C. Schneider, C.K. Hays, and C.M. Waterman Epidermal growth factor-induced contraction regulates paxillin phosphorylation to temporally separate traction generation from de-adhesion Mol Biol Cell 20 2009 3155 3167
    • (2009) Mol Biol Cell , vol.20 , pp. 3155-3167
    • Schneider, I.C.1    Hays, C.K.2    Waterman, C.M.3
  • 68
    • 84887408822 scopus 로고    scopus 로고
    • A directional switch of integrin signalling and a new anti-thrombotic strategy
    • B. Shen, X. Zhao, and K.A. O'Brien et al. A directional switch of integrin signalling and a new anti-thrombotic strategy Nature 503 2013 131 135
    • (2013) Nature , vol.503 , pp. 131-135
    • Shen, B.1    Zhao, X.2    O'Brien, K.A.3
  • 69
    • 84888358481 scopus 로고    scopus 로고
    • Cell adhesion: The 'ins' and 'outs' of integrin signalling
    • K.H. Wrighton Cell adhesion: The 'ins' and 'outs' of integrin signalling Nat Rev Mol Cell Biol 14 2013 752 753
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 752-753
    • Wrighton, K.H.1
  • 70
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • T. Leung, X.Q. Chen, E. Manser, and L. Lim The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton Mol Cell Biol 16 1996 5313 5327 (Pubitemid 26315050)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5313-5327
    • Leung, T.1    Chen, X.-Q.2    Manser, E.3    Lim, L.4
  • 72
    • 33747152561 scopus 로고    scopus 로고
    • Matrix Elasticity Directs Stem Cell Lineage Specification
    • DOI 10.1016/j.cell.2006.06.044, PII S0092867406009615
    • A.J. Engler, S. Sen, H.L. Sweeney, and D.E. Discher Matrix elasticity directs stem cell lineage specification Cell 126 2006 677 689 (Pubitemid 44233625)
    • (2006) Cell , vol.126 , Issue.4 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 73
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • C.G. Galbraith, K.M. Yamada, and M.P. Sheetz The relationship between force and focal complex development J Cell Biol 159 2002 695 705
    • (2002) J Cell Biol , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 75
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • N. Wang, J.P. Butler, and D.E. Ingber Mechanotransduction across the cell surface and through the cytoskeleton Science 260 1993 1124 1127 (Pubitemid 23186787)
    • (1993) Science , vol.260 , Issue.5111 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 76
    • 79955538660 scopus 로고    scopus 로고
    • Actomyosin-generated tension controls the molecular kinetics of focal adhesions
    • H. Wolfenson, A. Bershadsky, Y.I. Henis, and B. Geiger Actomyosin-generated tension controls the molecular kinetics of focal adhesions J Cell Sci 124 2011 1425 1432
    • (2011) J Cell Sci , vol.124 , pp. 1425-1432
    • Wolfenson, H.1    Bershadsky, A.2    Henis, Y.I.3    Geiger, B.4
  • 78
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation
    • J.C. Kuo, X. Han, C.T. Hsiao, J.R. Yates III, and C.M. Waterman Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation Nat Cell Biol 13 2011 383 393
    • (2011) Nat Cell Biol , vol.13 , pp. 383-393
    • Kuo, J.C.1    Han, X.2    Hsiao, C.T.3    Yates III, J.R.4    Waterman, C.M.5
  • 79
    • 79952283069 scopus 로고    scopus 로고
    • Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins
    • H.B. Schiller, C.C. Friedel, C. Boulegue, and R. Fassler Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins EMBO Rep 12 2011 259 266
    • (2011) EMBO Rep , vol.12 , pp. 259-266
    • Schiller, H.B.1    Friedel, C.C.2    Boulegue, C.3    Fassler, R.4
  • 80
    • 85027945680 scopus 로고    scopus 로고
    • The myosin-II-responsive focal adhesion proteome: A tour de force?
    • L. Gallegos, M.R. Ng, and J.S. Brugge The myosin-II-responsive focal adhesion proteome: a tour de force? Nat Cell Biol 13 2011 344 346
    • (2011) Nat Cell Biol , vol.13 , pp. 344-346
    • Gallegos, L.1    Ng, M.R.2    Brugge, J.S.3
  • 81
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • C. Grashoff, B.D. Hoffman, and M.D. Brenner et al. Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics Nature 466 2010 263 266
    • (2010) Nature , vol.466 , pp. 263-266
    • Grashoff, C.1    Hoffman, B.D.2    Brenner, M.D.3
  • 82
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • DOI 10.1038/nature01805
    • G. Jiang, G. Giannone, D.R. Critchley, E. Fukumoto, and M.P. Sheetz Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin Nature 424 2003 334 337 (Pubitemid 36899377)
    • (2003) Nature , vol.424 , Issue.6946 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheet, M.P.5
  • 83
    • 33751335857 scopus 로고    scopus 로고
    • Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas
    • DOI 10.1016/j.cell.2006.09.044, PII S009286740601405X
    • Y. Sawada, M. Tamada, and B.J. Dubin-Thaler et al. Force sensing by mechanical extension of the Src family kinase substrate p130Cas Cell 127 2006 1015 1026 (Pubitemid 44803062)
    • (2006) Cell , vol.127 , Issue.5 , pp. 1015-1026
    • Sawada, Y.1    Tamada, M.2    Dubin-Thaler, B.J.3    Cherniavskaya, O.4    Sakai, R.5    Tanaka, S.6    Sheetz, M.P.7
  • 84
    • 33751206869 scopus 로고    scopus 로고
    • A Role for p130Cas in Mechanotransduction
    • DOI 10.1016/j.cell.2006.11.020, PII S0092867406014760
    • B. Geiger A role for p130Cas in mechanotransduction Cell 127 2006 879 881 (Pubitemid 44792262)
    • (2006) Cell , vol.127 , Issue.5 , pp. 879-881
    • Geiger, B.1
  • 86
    • 80054043810 scopus 로고    scopus 로고
    • Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A
    • A.J. Ehrlicher, F. Nakamura, J.H. Hartwig, D.A. Weitz, and T.P. Stossel Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A Nature 478 2011 260 263
    • (2011) Nature , vol.478 , pp. 260-263
    • Ehrlicher, A.J.1    Nakamura, F.2    Hartwig, J.H.3    Weitz, D.A.4    Stossel, T.P.5
  • 87
    • 49149086522 scopus 로고    scopus 로고
    • Plectin deposition at podosome rings requires myosin contractility
    • A. Gad, S. Lach, L. Crimaldi, and M. Gimona Plectin deposition at podosome rings requires myosin contractility Cell Motil Cytoskeleton 65 2008 614 625
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 614-625
    • Gad, A.1    Lach, S.2    Crimaldi, L.3    Gimona, M.4
  • 88
    • 0033790713 scopus 로고    scopus 로고
    • Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts
    • E. Zamir, M. Katz, and Y. Posen et al. Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts Nat Cell Biol 2 2000 191 196
    • (2000) Nat Cell Biol , vol.2 , pp. 191-196
    • Zamir, E.1    Katz, M.2    Posen, Y.3
  • 89
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • DOI 10.1242/jcs.00792
    • R. Zaidel-Bar, C. Ballestrem, Z. Kam, and B. Geiger Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells J Cell Sci 116 2003 4605 4613 (Pubitemid 37461615)
    • (2003) Journal of Cell Science , vol.116 , Issue.22 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 90
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • DOI 10.1083/jcb.200206043
    • K.A. DeMali, C.A. Barlow, and K. Burridge Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion J Cell Biol 159 2002 881 891 (Pubitemid 36008369)
    • (2002) Journal of Cell Biology , vol.159 , Issue.5 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 91
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: New members to the club of focal adhesion proteins
    • A. Meves, C. Stremmel, K. Gottschalk, and R. Fassler The Kindlin protein family: new members to the club of focal adhesion proteins Trends Cell Biol 19 2009 504 513
    • (2009) Trends Cell Biol , vol.19 , pp. 504-513
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fassler, R.4
  • 92
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • DOI 10.1016/S0092-8674(03)00163-6
    • Y. Tu, S. Wu, X. Shi, K. Chen, and C. Wu Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation Cell 113 2003 37 47 (Pubitemid 36411958)
    • (2003) Cell , vol.113 , Issue.1 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 93
    • 34548565712 scopus 로고    scopus 로고
    • ZRP-1 controls Rho GTPase-mediated actin reorganization by localizing at cell-matrix and cell-cell adhesions
    • DOI 10.1242/jcs.03477
    • C.Y. Bai, M. Ohsugi, Y. Abe, and T. Yamamoto ZRP-1 controls Rho GTPase-mediated actin reorganization by localizing at cell-matrix and cell-cell adhesions J Cell Sci 120 2007 2828 2837 (Pubitemid 47394257)
    • (2007) Journal of Cell Science , vol.120 , Issue.16 , pp. 2828-2837
    • Bai, C.-Y.1    Ohsugi, M.2    Abe, Y.3    Yamamoto, T.4
  • 94
    • 14644404268 scopus 로고    scopus 로고
    • RNAi knockdown of the focal adhesion protein TES reveals its role in actin stress fibre organisation
    • DOI 10.1002/cm.20052
    • E. Griffith, A.S. Coutts, and D.M. Black RNAi knockdown of the focal adhesion protein TES reveals its role in actin stress fibre organisation Cell Motil Cytoskeleton 60 2005 140 152 (Pubitemid 40316154)
    • (2005) Cell Motility and the Cytoskeleton , vol.60 , Issue.3 , pp. 140-152
    • Griffith, E.1    Coutts, A.S.2    Black, D.M.3
  • 95
    • 0032567341 scopus 로고    scopus 로고
    • Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases
    • DOI 10.1074/jbc.273.52.34954
    • Y. Ren, R. Li, Y. Zheng, and H. Busch Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases J Biol Chem 273 1998 34954 34960 (Pubitemid 29028193)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.52 , pp. 34954-34960
    • Ren, Y.1    Li, R.2    Zheng, Y.3    Busch, H.4
  • 96
    • 2442481067 scopus 로고    scopus 로고
    • α-actinin revisited: A fresh look at an old player
    • DOI 10.1002/cm.20007
    • C.A. Otey, and O. Carpen Alpha-actinin revisited: a fresh look at an old player Cell Motil Cytoskeleton 58 2004 104 111 (Pubitemid 38697587)
    • (2004) Cell Motility and the Cytoskeleton , vol.58 , Issue.2 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 97
    • 58149134377 scopus 로고    scopus 로고
    • In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2
    • M.M. Schroeter, B. Beall, H.W. Heid, and J.M. Chalovich In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2 Biosci Rep 28 2008 195 203
    • (2008) Biosci Rep , vol.28 , pp. 195-203
    • Schroeter, M.M.1    Beall, B.2    Heid, H.W.3    Chalovich, J.M.4
  • 100
    • 79953293637 scopus 로고    scopus 로고
    • Zyxin emerges as a key player in the mechanotransduction at cell adhesive structures
    • H. Hirata, H. Tatsumi, and M. Sokabe Zyxin emerges as a key player in the mechanotransduction at cell adhesive structures Commun Integr Biol 1 2008 192 195
    • (2008) Commun Integr Biol , vol.1 , pp. 192-195
    • Hirata, H.1    Tatsumi, H.2    Sokabe, M.3
  • 101
    • 53349090308 scopus 로고    scopus 로고
    • Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner
    • H. Hirata, H. Tatsumi, and M. Sokabe Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner J Cell Sci 121 2008 2795 2804
    • (2008) J Cell Sci , vol.121 , pp. 2795-2804
    • Hirata, H.1    Tatsumi, H.2    Sokabe, M.3
  • 102
    • 0034740693 scopus 로고    scopus 로고
    • Mechanisma and role of PDZ domains in signaling complex assembly
    • B.Z. Harris, and W.A. Lim Mechanism and role of PDZ domains in signaling complex assembly J Cell Sci 114 2001 3219 3231 (Pubitemid 32998900)
    • (2001) Journal of Cell Science , vol.114 , Issue.18 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 103
    • 57649245603 scopus 로고    scopus 로고
    • A new model for asymmetric spindle positioning in mouse oocytes
    • M. Schuh, and J. Ellenberg A new model for asymmetric spindle positioning in mouse oocytes Curr Biol 18 2008 1986 1992
    • (2008) Curr Biol , vol.18 , pp. 1986-1992
    • Schuh, M.1    Ellenberg, J.2
  • 104
    • 39149094614 scopus 로고    scopus 로고
    • Asymmetric focal adhesion disassembly in motile cells
    • J.A. Broussard, D.J. Webb, and I. Kaverina Asymmetric focal adhesion disassembly in motile cells Curr Opin Cell Biol 20 2008 85 90
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 85-90
    • Broussard, J.A.1    Webb, D.J.2    Kaverina, I.3
  • 105
    • 0028841220 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal tension regulate the release of fibroblast adhesions
    • E. Crowley, and A.F. Horwitz Tyrosine phosphorylation and cytoskeletal tension regulate the release of fibroblast adhesions J Cell Biol 131 1995 525 537
    • (1995) J Cell Biol , vol.131 , pp. 525-537
    • Crowley, E.1    Horwitz, A.F.2
  • 106
  • 107
    • 74049160017 scopus 로고    scopus 로고
    • Clathrin mediates integrin endocytosis for focal adhesion disassembly in migrating cells
    • E.J. Ezratty, C. Bertaux, E.E. Marcantonio, and G.G. Gundersen Clathrin mediates integrin endocytosis for focal adhesion disassembly in migrating cells J Cell Biol 187 2009 733 747
    • (2009) J Cell Biol , vol.187 , pp. 733-747
    • Ezratty, E.J.1    Bertaux, C.2    Marcantonio, E.E.3    Gundersen, G.G.4
  • 108
    • 79955478657 scopus 로고    scopus 로고
    • Cell migration: Keeping young and mobile with beta-PIX
    • K. Legg Cell migration: keeping young and mobile with beta-PIX Nat Rev Mol Cell Biol 12 278 2011
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.278
    • Legg, K.1
  • 109
    • 33644539533 scopus 로고    scopus 로고
    • Targeting and activation of Rac1 are mediated by the exchange factor beta-Pix
    • J.P. ten Klooster, Z.M. Jaffer, J. Chernoff, and P.L. Hordijk Targeting and activation of Rac1 are mediated by the exchange factor beta-Pix J Cell Biol 172 2006 759 769
    • (2006) J Cell Biol , vol.172 , pp. 759-769
    • Ten Klooster, J.P.1    Jaffer, Z.M.2    Chernoff, J.3    Hordijk, P.L.4
  • 112
    • 0035930585 scopus 로고    scopus 로고
    • Protein kinase A regulates Rac and is required for the growth factor-stimulated migration of carcinoma cells
    • K.L. O'Connor, and A.M. Mercurio Protein kinase A regulates Rac and is required for the growth factor-stimulated migration of carcinoma cells J Biol Chem 276 2001 47895 47900
    • (2001) J Biol Chem , vol.276 , pp. 47895-47900
    • O'Connor, K.L.1    Mercurio, A.M.2
  • 113
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • DOI 10.1038/35047107
    • H. Miki, H. Yamaguchi, S. Suetsugu, and T. Takenawa IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling Nature 408 2000 732 735 (Pubitemid 32015990)
    • (2000) Nature , vol.408 , Issue.6813 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 114
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • S. Eden, R. Rohatgi, A.V. Podtelejnikov, M. Mann, and M.W. Kirschner Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck Nature 418 2002 790 793
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 115
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • S.A. Weed, A.V. Karginov, and D.A. Schafer et al. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex J Cell Biol 151 2000 29 40
    • (2000) J Cell Biol , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3
  • 116
    • 71749095987 scopus 로고    scopus 로고
    • The cofilin activity cycle in lamellipodia and invadopodia
    • M. Oser, and J. Condeelis The cofilin activity cycle in lamellipodia and invadopodia J Cell Biochem 108 2009 1252 1262
    • (2009) J Cell Biochem , vol.108 , pp. 1252-1262
    • Oser, M.1    Condeelis, J.2
  • 117
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated Protein 1 (CAP1) Promotes Cofilin-induced Actin Dynamics in Mammalian Nonmuscle Cells
    • DOI 10.1091/mbc.E04-01-0048
    • E. Bertling, P. Hotulainen, P.K. Mattila, T. Matilainen, M. Salminen, and P. Lappalainen Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells Mol Biol Cell 15 2004 2324 2334 (Pubitemid 38580649)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2324-2334
    • Bertling, E.1    Hotulainen, P.2    Mattila, P.K.3    Matilainen, T.4    Salminen, M.5    Lappalainen, P.6
  • 118
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: Biomaterials for stimulated cell adhesion and beyond
    • DOI 10.1016/S0142-9612(03)00343-0
    • U. Hersel, C. Dahmen, and H. Kessler RGD modified polymers: biomaterials for stimulated cell adhesion and beyond Biomaterials 24 2003 4385 4415 (Pubitemid 36960136)
    • (2003) Biomaterials , vol.24 , Issue.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 119
    • 0036013933 scopus 로고    scopus 로고
    • In vitro reaction of endothelial cells to polymer demixed nanotopography
    • DOI 10.1016/S0142-9612(01)00424-0, PII S0142961201004240
    • M.J. Dalby, M.O. Riehle, H. Johnstone, S. Affrossman, and A.S. Curtis In vitro reaction of endothelial cells to polymer demixed nanotopography Biomaterials 23 2002 2945 2954 (Pubitemid 34497086)
    • (2002) Biomaterials , vol.23 , Issue.14 , pp. 2945-2954
    • Dalby, M.J.1    Riehle, M.O.2    Johnstone, H.3    Affrossman, S.4    Curtis, A.S.G.5
  • 120
    • 4444285115 scopus 로고    scopus 로고
    • Mechanotransduction at cell-matrix and cell-cell contacts
    • DOI 10.1146/annurev.bioeng.6.040803.140040
    • C.S. Chen, J. Tan, and J. Tien Mechanotransduction at cell-matrix and cell-cell contacts Annu Rev Biomed Eng 6 2004 275 302 (Pubitemid 39209500)
    • (2004) Annual Review of Biomedical Engineering , vol.6 , pp. 275-302
    • Chen, C.S.1    Tan, J.2    Tien, J.3
  • 121
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • DOI 10.1126/science.1064829
    • E. Cukierman, R. Pankov, D.R. Stevens, and K.M. Yamada Taking cell-matrix adhesions to the third dimension Science 294 2001 1708 1712 (Pubitemid 33104840)
    • (2001) Science , vol.294 , Issue.5547 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 123
    • 33646861953 scopus 로고    scopus 로고
    • Cell distribution of stress fibres in response to the geometry of the adhesive environment
    • DOI 10.1002/cm.20126
    • M. Thery, A. Pepin, E. Dressaire, Y. Chen, and M. Bornens Cell distribution of stress fibres in response to the geometry of the adhesive environment Cell Motil Cytoskeleton 63 2006 341 355 (Pubitemid 43787719)
    • (2006) Cell Motility and the Cytoskeleton , vol.63 , Issue.6 , pp. 341-355
    • Thery, M.1    Pepin, A.2    Dressaire, E.3    Chen, Y.4    Bornens, M.5
  • 124
    • 1842426730 scopus 로고    scopus 로고
    • Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment
    • DOI 10.1016/S1534-5807(04)00075-9, PII S1534580704000759
    • R. McBeath, D.M. Pirone, C.M. Nelson, K. Bhadriraju, and C.S. Chen Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment Dev Cell 6 2004 483 495 (Pubitemid 38456178)
    • (2004) Developmental Cell , vol.6 , Issue.4 , pp. 483-495
    • McBeath, R.1    Pirone, D.M.2    Nelson, C.M.3    Bhadriraju, K.4    Chen, C.S.5
  • 125
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • DOI 10.1016/j.ceb.2006.12.013, PII S0955067406001943
    • I. Delon, and N.H. Brown Integrins and the actin cytoskeleton Curr Opin Cell Biol 19 2007 43 50 (Pubitemid 46123977)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.1 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 126
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • B. Geiger, A. Bershadsky, R. Pankov, and K.M. Yamada Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk Nat Rev Mol Cell Biol 2 2001 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
  • 127
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails
    • K.R. Legate, and R. Fassler Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails J Cell Sci 122 2009 187 198
    • (2009) J Cell Sci , vol.122 , pp. 187-198
    • Legate, K.R.1    Fassler, R.2
  • 128
    • 77951153298 scopus 로고    scopus 로고
    • Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6
    • J.D. Humphries, A. Byron, and M.D. Bass et al. Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6 Sci Signal 2 2009 ra51
    • (2009) Sci Signal , vol.2 , pp. 51
    • Humphries, J.D.1    Byron, A.2    Bass, M.D.3
  • 129
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - Over and over and over again
    • D.J. Webb, J.T. Parsons, and A.F. Horwitz Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again Nat Cell Biol 4 2002 E97 E100
    • (2002) Nat Cell Biol , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 130
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • K.R. Levental, H. Yu, and L. Kass et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling Cell 139 2009 891 906
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1    Yu, H.2    Kass, L.3


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