메뉴 건너뛰기




Volumn 7, Issue 1, 2012, Pages 29-48

Intracellular modelling of cell-matrix adhesion during cancer cell invasion

Author keywords

Actin; Cancer invasion; Cell matrix adhesion; Fibronectin; Integrins

Indexed keywords

ACTIN; CANCER INVASION; CELL-MATRIX ADHESION; FIBRONECTIN; INTEGRINS;

EID: 84856507894     PISSN: 09735348     EISSN: 17606101     Source Type: Journal    
DOI: 10.1051/mmnp/20127103     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 0032819362 scopus 로고    scopus 로고
    • The actin-based nanomachine at the leading edge of migrating cells
    • V. C. Abraham, V. Krishnamurthi, D. L. Taylor, F. Lanni. The actin-based nanomachine at the leading edge of migrating cells. Biophys. J., 77 (1999) No. 3, 1721-1732. (Pubitemid 29407343)
    • (1999) Biophysical Journal , vol.77 , Issue.3 , pp. 1721-1732
    • Abraham, V.C.1    Krishnamurthi, V.2    Lansing Taylor, D.3    Lanni, F.4
  • 2
    • 79960323501 scopus 로고    scopus 로고
    • Cooperativity between integrin activation and mechanical stress leads to integrin clustering
    • O. Ali, H. Guillou, O. Destaing, C. Albiges-Rizo, M. R. Block, B. Fourcade. Cooperativity between integrin activation and mechanical stress leads to integrin clustering. Biophys. J., 100 (2011), No. 11, 2595-2604.
    • (2011) Biophys. J. , vol.100 , Issue.11 , pp. 2595-2604
    • Ali, O.1    Guillou, H.2    Destaing, O.3    Albiges-Rizo, C.4    Block, M.R.5    Fourcade, B.6
  • 3
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho- kinase
    • DOI 10.1126/science.275.5304.1308
    • M. Amano, K. Chihara, K. Kimura, Y. Fukata, N. Nakamura, Y. Matsuura, K. Kaibuchi. Formation of actin stress fibers and focal adhesions enhanced by rho-kinase. Science, 297 (1997), No. 5304, 1308-1311. (Pubitemid 27114159)
    • (1997) Science , vol.275 , Issue.5304 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Kimura, K.3    Fukata, Y.4    Nakamura, N.5    Matsuura, Y.6    Kaibuchi, K.7
  • 6
    • 31944450466 scopus 로고    scopus 로고
    • Purified integrin adhesion complexes exhibit actin-polymerization activity
    • DOI 10.1016/j.cub.2005.12.033, PII S0960982205015952
    • B. Butler, C. Gao, A. T. Mersich, S. D. Blystone. Purified integrin adhesion complexes exhibit actin-polymerization activity. Curr. Biol., 16 (2006), No. 3, 242-251. (Pubitemid 43190223)
    • (2006) Current Biology , vol.16 , Issue.3 , pp. 242-251
    • Butler, B.1    Gao, C.2    Mersich, A.T.3    Blystone, S.D.4
  • 7
    • 0000678946 scopus 로고    scopus 로고
    • Multiple activation states of integrin ′4 ′1 detected through their different affinities for a small molecule ligand
    • L. L. Chen, A. Whitty, R. R. Lobb, S. P. Adams, R. B. Pepinsky. Multiple activation states of integrin ′4 ′1 detected through their different affinities for a small molecule ligand. J. Biol. Chem., 274 (1999), No. 19, 13167-13175.
    • (1999) J. Biol. Chem. , vol.274 , Issue.19 , pp. 13167-13175
    • Chen, L.L.1    Whitty, A.2    Lobb, R.R.3    Adams, S.P.4    Pepinsky, R.B.5
  • 8
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin- cytoskeleton linkages
    • D. Choquet, D. P. Felsenfeld, M. P. Sheetz. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell, 88 (1997), No. 1, 39-48. (Pubitemid 27180329)
    • (1997) Cell , vol.88 , Issue.1 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 9
    • 27544442354 scopus 로고    scopus 로고
    • The mechanisms and dynamics of αvβ3 integrin clustering in living cells
    • DOI 10.1083/jcb.200503017
    • C. Cluzel, F. Saltel, J. Lussi, F. Paulhe, B. A. Imhof, B. Wehrle-Haller. The mechanisms and dynamics of αvβ3 integrin clustering in living cells. J. Cell. Biol., 171 (2005), No. 2, 383-392. (Pubitemid 41540029)
    • (2005) Journal of Cell Biology , vol.171 , Issue.2 , pp. 383-392
    • Cluzel, C.1    Saltel, F.2    Lussi, J.3    Paulhe, F.4    Imhof, B.A.5    Wehrle-Haller, B.6
  • 10
    • 78649728329 scopus 로고    scopus 로고
    • Autocrine fibronectin directs matrix assembly and crosstalk between cell-matrix and cell-cell adhesion in vascular endothelial cells
    • B. Cseh, S. Fernandez-Sauze, D. Grall, S. Schaub, E. Doma, E. van Obberghen-Schilling. Autocrine fibronectin directs matrix assembly and crosstalk between cell-matrix and cell-cell adhesion in vascular endothelial cells. J. Cell Sci., 123 (2010), No. 22, 3989-3999.
    • (2010) J. Cell Sci. , vol.123 , Issue.22 , pp. 3989-3999
    • Cseh, B.1    Fernandez-Sauze, S.2    Grall, D.3    Schaub, S.4    Doma, E.5    Van Obberghen-Schilling, E.6
  • 11
    • 0025886995 scopus 로고
    • Mathematical model for the effects of adhesion and mechanics on cell migration speed
    • P. A. DiMilla, K. Barbee, D. A. Lauffenburger. Mathematical model for the effects of adhesion and mechanics on cell migration speed. Biophys. J., 60 (1991), No. 1, 15-37.
    • (1991) Biophys. J. , vol.60 , Issue.1 , pp. 15-37
    • Dimilla, P.A.1    Barbee, K.2    Lauffenburger, D.A.3
  • 12
    • 81755172054 scopus 로고    scopus 로고
    • The endocytic protein GRAF1 is directed to cell-matrix adhesion sites and regulates cell spreading
    • G. J. Doherty, M. K. Ahlund, M. T. Howes, B. Moren, R. G. Parton, H. T. McMahon, R. Lundmark. The endocytic protein GRAF1 is directed to cell-matrix adhesion sites and regulates cell spreading. Mol. Biol. Cell, 22 (2011), No. 22, 4380-4389.
    • (2011) Mol. Biol. Cell , vol.22 , Issue.22 , pp. 4380-4389
    • Doherty, G.J.1    Ahlund, M.K.2    Howes, M.T.3    Moren, B.4    Parton, R.G.5    McMahon, H.T.6    Lundmark, R.7
  • 13
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escape mechanisms
    • DOI 10.1038/nrc1075
    • P. Friedl, K. Wolf. Tumour-cell invasion and migration : diversity and escape mechanisms. Nat. Rev. Cancer, 3 (2003), No. 5, 362-374. (Pubitemid 37328856)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.5 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 14
    • 0033925842 scopus 로고    scopus 로고
    • A mathematical model of caspase function in apoptosis
    • DOI 10.1038/77589
    • M. Fussenegger, J. E. Bailey, J. Varner. A mathematical model of caspase function in apoptosis. Nat. Biotechnol., 18 (2000), 768-774. (Pubitemid 30460695)
    • (2000) Nature Biotechnology , vol.18 , Issue.7 , pp. 768-774
    • Fussenegger, M.1    Bailey, J.E.2    Varner, J.3
  • 15
    • 24344434553 scopus 로고    scopus 로고
    • Cell adhesion strengthening: Contributions of adhesive area, integrin binding, and focal adhesion assembly
    • DOI 10.1091/mbc.E05-02-0170
    • N. D. Gallant, K. E. Michael, A. J. García. Cell adhesion strengthening : contributions of adhesive area, integrin binding, and focal adhesion assembly. Mol. Biol. Cell, 16 (2005), No. 9, 4329-4340. (Pubitemid 41262900)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 4329-4340
    • Gallant, N.D.1    Michael, K.E.2    Garcia, A.J.3
  • 16
    • 0032753925 scopus 로고    scopus 로고
    • Integrin-fibronectin interactions at the cell-material interface : Initial integrin binding and signaling
    • A. J. García, D. Boettiger. Integrin-fibronectin interactions at the cell-material interface : initial integrin binding and signaling. Biomaterials, 20 (1999), No. 23-24, 2427-2433.
    • (1999) Biomaterials , vol.20 , Issue.23-24 , pp. 2427-2433
    • García, A.J.1    Boettiger, D.2
  • 17
    • 0032079456 scopus 로고    scopus 로고
    • 1 integrin-fibronectin bonds in intact adherent cells is sensitive to integrin activation state
    • DOI 10.1074/jbc.273.18.10988
    • A. J. García, F. Huber, D. Boettiger. Force required to break α5β1 integrin-fibronectin bonds in intact adherent cells is sensitive to integrin activation state. J. Biol. Chem., 273 (1998), No. 18, 10988-10993. (Pubitemid 28204939)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10988-10993
    • Garcia, A.J.1    Huber, F.2    Boettiger, D.3
  • 18
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • F. G. Giancotti, E. Ruoslahti. Integrin signaling. Science, 285 (1999), No. 5430, 1028-1032.
    • (1999) Science , vol.285 , Issue.5430 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 19
    • 5644298698 scopus 로고    scopus 로고
    • Adhesion-independent α6β4 integrin clustering is mediated by phosphatidylinositol 3-kinase
    • M. Z. Gilcrease, X. Zhou, K. Welch. Adhesion-independent α6β4 integrin clustering is mediated by phosphatidylinositol 3-kinase. Cancer Res., 64 (2004), 7395.
    • (2004) Cancer Res. , vol.64 , pp. 7395
    • Gilcrease, M.Z.1    Zhou, X.2    Welch, K.3
  • 20
    • 35848967591 scopus 로고    scopus 로고
    • Retrograde fluxes of focal adhesion proteins in response to cell migration and mechanical signals
    • W. H. Guo, Y. L. Wang. Retrograde fluxes of focal adhesion proteins in response to cell migration and mechanical signals. Mol. Biol. Cell, 18 (2007), No. 11, 4519-4527.
    • (2007) Mol. Biol. Cell , vol.18 , Issue.11 , pp. 4519-4527
    • Guo, W.H.1    Wang, Y.L.2
  • 21
    • 0023405068 scopus 로고
    • A dynamical model for receptor-mediated cell adhesion to surfaces
    • D. A. Hammer, D. A. Lauffenburger. A dynamical model for receptor-mediated cell adhesion to surfaces. Biophys. J., 53 (1987), No. 3, 475-487.
    • (1987) Biophys. J. , vol.53 , Issue.3 , pp. 475-487
    • Hammer, D.A.1    Lauffenburger, D.A.2
  • 22
    • 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), No. 6, 673-687. (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 23
    • 0034793912 scopus 로고    scopus 로고
    • Dynamics of integrin clustering at focal contacts of endothelial cells studied by multimode imaging microscopy
    • K. Kawakami, H. Tatsumi, M. Sokabe. Dynamics of integrin clustering at focal contacts of endothelial cells studied by multimode imaging microscopy. J. Cell Sci., 114 (2001), No. 17, 3125-3135. (Pubitemid 32910467)
    • (2001) Journal of Cell Science , vol.114 , Issue.17 , pp. 3125-3135
    • Kawakami, K.1    Tatsumi, H.2    Sokabe, M.3
  • 24
    • 84856503786 scopus 로고    scopus 로고
    • Integrins in cancer cell invasion. Cell invasion
    • P. Koistinen, J. Heino. Integrins in cancer cell invasion. Cell invasion. Landes Bioscience, 2002.
    • (2002) Landes Bioscience
    • Koistinen, P.1    Heino, J.2
  • 25
    • 79955026585 scopus 로고    scopus 로고
    • Clustered integrin alpha-5-beta-1 ligand displays model fibronectin-mediated adhesion of human endometrial stromal cells
    • Z. H. Li, M. Kreiner, C. F. van der Walle, H. J. Mardon. Clustered integrin alpha-5-beta-1 ligand displays model fibronectin-mediated adhesion of human endometrial stromal cells. Biochem. Biophys. Res. Comm., 407 (2011), No. 4, 777-782.
    • (2011) Biochem. Biophys. Res. Comm. , vol.407 , Issue.4 , pp. 777-782
    • Li, Z.H.1    Kreiner, M.2    Walle Der Van, C.F.3    Mardon, H.J.4
  • 26
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization
    • DOI 10.1083/jcb.138.4.913
    • L. M. Machesky, A. Hall. Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization. J. Cell. Biol., 138 (1997), No. 4, 913-926. (Pubitemid 27365052)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 27
    • 0032825265 scopus 로고    scopus 로고
    • Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
    • DOI 10.1083/jcb.146.5.1097
    • A. Mallavarapu, T. Mitchison. Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J. Cell. Biol., 146 (1999), No. 5, 1097-1106. (Pubitemid 29430450)
    • (1999) Journal of Cell Biology , vol.146 , Issue.5 , pp. 1097-1106
    • Mallavarapu, A.1    Mitchison, T.2
  • 28
    • 80053365121 scopus 로고    scopus 로고
    • The candidate tumor suppressor SASH1 interacts with the actin cytoskeleton and stimulates cell-matrix adhesion
    • M. Martini, A. Gnann, D. Scheiki, B. Holzmann, K. P. Janssen. The candidate tumor suppressor SASH1 interacts with the actin cytoskeleton and stimulates cell-matrix adhesion. Int. J. Biochem. Cell. Biol., 43 (2011), No. 11, 1630-1640.
    • (2011) Int. J. Biochem. Cell. Biol. , vol.43 , Issue.11 , pp. 1630-1640
    • Martini, M.1    Gnann, A.2    Scheiki, D.3    Holzmann, B.4    Janssen, K.P.5
  • 29
    • 0347723887 scopus 로고    scopus 로고
    • The Receptor for Urokinase-type Plasminogen Activator Regulates Fibronectin Matrix Assembly in Human Skin Fibroblasts
    • DOI 10.1074/jbc.M310374200
    • E. Monaghan, V. Gueorguiev, C. Wilkins-Port. The receptor for urokinase-type plasminogen activator regulates fibronectin matrix assembly in human skin fibroblasts. J. Biol. Chem., 279 (2004), No. 2, 1400-1407. (Pubitemid 38082667)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1400-1407
    • Monaghan, E.1    Gueorguiev, V.2    Wilkins-Port, C.3    McKeown-Longo, P.J.4
  • 30
    • 34948854409 scopus 로고    scopus 로고
    • A major fraction of fibronectin present in the extracellular matrix of tissues is plasma-derived
    • DOI 10.1074/jbc.M611315200
    • F. A. Moretti, A. K. Chauhan, A. Iaconcig, F. Porro, F. E. Baralle, A. F. Muro. A major fraction of fibronectin present in the extracellular matrix of tissues is plasma-derived. J. Biol. Chem., 282 (2007), No. 38, 28057-28062. (Pubitemid 47529518)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 28057-28062
    • Moretti, F.A.1    Chauhan, A.K.2    Iaconcig, A.3    Porro, F.4    Baralle, F.E.5    Muro, A.F.6
  • 31
    • 81555220916 scopus 로고    scopus 로고
    • Integrin-mediated cell-matrix interaction in physiological and pathological blood vessel formation
    • Epub 2011 Sep 18
    • S. Niland, J. A. Eble. Integrin-mediated cell-matrix interaction in physiological and pathological blood vessel formation. J. Oncol., (2012), Epub 2011 Sep 18, 125278.
    • (2012) J. Oncol. , pp. 125278
    • Niland, S.1    Eble, J.A.2
  • 33
    • 0030845190 scopus 로고    scopus 로고
    • Epidermal growth factor modulates tyrosine phosphorylation of p130(Cas). Involvement of phosphatidylinositol 3'-kinase and actin cytoskeleton
    • DOI 10.1074/jbc.272.41.25993
    • M. Ojaniemi, K. Vuori. Epidermal growth factor modulates tyrosine phosphorylation of p130Cas. Involvement of phophatidylinositol 3'-kinase and actin cytoskeleton. J. Biol. Chem., 272 (1997), No. 41, 25993-25998. (Pubitemid 27438927)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25993-25998
    • Ojaniemi, M.1    Vuori, K.2
  • 35
    • 0033094580 scopus 로고    scopus 로고
    • Kinetic Model for Integrin-mediated Adhesion Release during Cell Migration
    • S. P. Palecek, A. F. Horwitz, D. A. Lauffenburger. Kinetic model for integrin-mediated adhesion release during cell migration. Ann. Biomed. Eng., 27 (1999), No. 2, 219-235. (Pubitemid 129600223)
    • (1999) Annals of Biomedical Engineering , vol.27 , Issue.2 , pp. 219-235
    • Palecek, S.P.1    Horwitz, A.F.2    Lauffenburger, D.A.3
  • 36
    • 0031976733 scopus 로고    scopus 로고
    • Physical and biochemical regulation of integrin release during rear detachment of migrating cells
    • S. P. Palecek, A. Huttenlocher, A. F. Horwitz, D. A. Lauffenburger. Physical and biochemical regulation of integrin release during rear detachment of migrating cells. J. Cell Sci., 111 (1998), 929-940. (Pubitemid 28196076)
    • (1998) Journal of Cell Science , vol.111 , Issue.7 , pp. 929-940
    • Palecek, S.P.1    Huttenlocher, A.2    Horwitz, A.F.3    Lauffenburger, D.A.4
  • 37
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • DOI 10.1038/385537a0
    • S. P. Palecek, J. C. Loftus, M. H. Ginsberg, D. A. Lauffenburger, A. F. Horwitz. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature, 385 (1997), No. 6616, 537-540. (Pubitemid 27074672)
    • (1997) Nature , vol.385 , Issue.6616 , pp. 537-540
    • Palecek, S.P.1    Loftust, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 38
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • DOI 10.1242/jcs.00059
    • R. Pankov, K. M. Yamada. Fibronectin at a glance. J. Cell Sci., 115 (2002), No. 20, 3861-3863. (Pubitemid 35256486)
    • (2002) Journal of Cell Science , vol.115 , Issue.20 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 39
    • 74549222971 scopus 로고    scopus 로고
    • Integrin clustering is driven by mechanical resistance from the glycocalyx and the substrate
    • M. J. Paszek, D. Boettiger, V. M. Weaver, D. A. Hammer. Integrin clustering is driven by mechanical resistance from the glycocalyx and the substrate. PLoS Comput. Biol., 5 (2009), No. 12, e1000604.
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.12
    • Paszek, M.J.1    Boettiger, D.2    Weaver, V.M.3    Hammer, D.A.4
  • 40
    • 0019495845 scopus 로고
    • Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores
    • DOI 10.1083/jcb.88.3.654
    • T. D. Pollard, M. S. Mooseker. Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores. J. Cell Biol., 88 (1981), No. 3, 654-659. (Pubitemid 11097958)
    • (1981) Journal of Cell Biology , vol.88 , Issue.3 , pp. 654-659
    • Pollard, T.D.1    Mooseker, M.S.2
  • 41
    • 0026462867 scopus 로고
    • Dynamics of α1 integrin-mediated adhesive contacts in motile fibroblasts
    • C. M. Regen, A. F. Horwitz. Dynamics of α1 integrin-mediated adhesive contacts in motile fibroblasts. J. Cell Biol., 119 (1992), No. 5, 1347-1359.
    • (1992) J. Cell Biol. , vol.119 , Issue.5 , pp. 1347-1359
    • Regen, C.M.1    Horwitz, A.F.2
  • 43
    • 32544443964 scopus 로고    scopus 로고
    • Systems Biology Toolbox for MATLAB: A computational platform for research in systems biology
    • DOI 10.1093/bioinformatics/bti799
    • H. Schmidt, M. Jirstrand. Systems Biology Toolbox for MATLAB : a computational platform for research in systems biology. Bioinformatics, 22 (2006), No. 4, 514-515. (Pubitemid 43231434)
    • (2006) Bioinformatics , vol.22 , Issue.4 , pp. 514-515
    • Schmidt, H.1    Jirstrand, M.2
  • 44
    • 0030036963 scopus 로고    scopus 로고
    • Altered rate of fibronectin matrix assembly by deletion of the first type III repeats
    • DOI 10.1083/jcb.134.2.573
    • J. L. Sechler, Y. Takada, J. E. Schwarzbauer. Altered rate of fibronectin matrix assembly by deletion of the first type III repeats. J. Cell Biol., 134 (1996), No. 2, 573-583. (Pubitemid 26255270)
    • (1996) Journal of Cell Biology , vol.134 , Issue.2 , pp. 573-583
    • Sechler, J.L.1    Takada, Y.2    Schwarzbauer, J.E.3
  • 45
    • 79251547965 scopus 로고    scopus 로고
    • Phosphorylation of trask by src kinases inhibits integrin clustering and functions in exclusion with focal adhesion signaling
    • D. S. Spassov, C. H. Wong, N. Sergina, D. Ahuja, M. Fried, D. Sheppard, M. M. Moasser. Phosphorylation of trask by src kinases inhibits integrin clustering and functions in exclusion with focal adhesion signaling. Mol. Cell. Biol., 31 (2011), No. 4, 766-782.
    • (2011) Mol. Cell. Biol. , vol.31 , Issue.4 , pp. 766-782
    • Spassov, D.S.1    Wong, C.H.2    Sergina, N.3    Ahuja, D.4    Fried, M.5    Sheppard, D.6    Moasser, M.M.7
  • 47
    • 0020569136 scopus 로고
    • Plasma fibronectin is synthesized and secreted by hepatocytes
    • J. W. Tamkun, R. O. Hynes. Plasma fibronectin is synthesized and secreted by hepatocytes. J. Biol. Chem., 258 (1983), No. 7, 4641-4647. (Pubitemid 13080691)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.7 , pp. 4641-4647
    • Tamkun, J.W.1    Hynes, R.O.2
  • 49
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - Over and over and over again
    • DOI 10.1038/ncb0402-e97
    • D. J. Webb, J. T. Parsons, A. R. Horwitz. Adhesion assembly, disassembly and turnover in migrating cells-over and over and over again. Nat. Cell Biol., 4 (2002), No. 4, E97-E100. (Pubitemid 34308850)
    • (2002) Nature Cell Biology , vol.4 , Issue.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 50
    • 84856503784 scopus 로고    scopus 로고
    • Analysis of integrin dynamics by fluorescence recovery after photobleaching
    • Springer
    • B. Wehrle-Haller. Analysis of integrin dynamics by fluorescence recovery after photobleaching. Adhesion Protein Protocols. Springer, 2007.
    • (2007) Adhesion Protein Protocols
    • Wehrle-Haller, B.1
  • 51
    • 0037211938 scopus 로고    scopus 로고
    • Actin, microtubules and focal adhesion dynamics during cell migration
    • DOI 10.1016/S1357-2725(02)00071-7, PII S1357272502000717
    • B. Wehrle-Haller, B. A. Imhof. Actin, microtubules and focal adhesion dynamics during cell migration. Int. J. Biochem. Cell Biol., 35 (2003), No. 1, 39-50. (Pubitemid 35449172)
    • (2003) International Journal of Biochemistry and Cell Biology , vol.35 , Issue.1 , pp. 39-50
    • Wehrle-Haller, B.1    Imhof, B.A.2
  • 52
    • 70349528156 scopus 로고    scopus 로고
    • Quantitative statistical description of integrin clusters in adherent cells
    • E. S. Welf, B. A. Ogunnaike, U. P. Naik. Quantitative statistical description of integrin clusters in adherent cells. IET Sys. Biol., 3 (2009), No. 5, 307-316.
    • (2009) IET Sys. Biol. , vol.3 , Issue.5 , pp. 307-316
    • Welf, E.S.1    Ogunnaike, B.A.2    Naik, U.P.3
  • 53
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs of fibronectin matrix assembly
    • DOI 10.1242/jcs.00670
    • I. Wierzbicka-Patynowski, J. Schwarzbauer. The ins and outs of fibronectin matrix assembly. J. Cell Sci., 116 (2003), No. 16, 3269-3276. (Pubitemid 37038975)
    • (2003) Journal of Cell Science , vol.116 , Issue.16 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 54
    • 10944269216 scopus 로고    scopus 로고
    • Spatial mapping of integrin interactions and dynamics during cell migration by image correlation microscopy
    • DOI 10.1242/jcs.01416
    • P. W. Wiseman, C. M. Brown, D. J. Webb, B. Hebert, N. L. Johnson, J. A. Squier, M. H. Ellisman, A. F. Horwitz. Spatial mapping of integrin interactions and dynamics during cell migration by image correlation microscopy. J. Cell Sci., 117 (2004), No. 23, 5521-5534. (Pubitemid 40012199)
    • (2004) Journal of Cell Science , vol.117 , Issue.23 , pp. 5521-5534
    • Wiseman, P.W.1    Brown, C.M.2    Webb, D.J.3    Hebert, B.4    Johnson, N.L.5    Squier, J.A.6    Ellisman, M.H.7    Horwitz, A.F.8
  • 55
    • 77955863885 scopus 로고    scopus 로고
    • Affinity lateral mobility, and clustering contribute independently to β2-integrin-mediated adhesion
    • T. Yu, X. Wu, K. B. Gupta, D. F. Kucik. Affinity, lateral mobility, and clustering contribute independently to β2-integrin-mediated adhesion. Am. J. Physiol. Cell Physiol., 299 (2010), No. 2, C399-C410.
    • (2010) Am. J. Physiol. Cell Physiol. , vol.299 , Issue.2
    • Yu, T.1    Wu, X.2    Gupta, K.B.3    Kucik, D.F.4
  • 56
    • 80054092429 scopus 로고    scopus 로고
    • Tetraspanin CD151 maintains vascular stability by balancing the forces of cell adhesion and cytoskeletal tension
    • F. Zhang, J. E. Michaelson, S. Moshiach, N. Sachs, W. Zhao, Y. Sun, A. Sonnenberg, J. M. Lahti, H. Huang, X. A. Zhang. Tetraspanin CD151 maintains vascular stability by balancing the forces of cell adhesion and cytoskeletal tension. Blood, 118 (2011), No. 15, 4274-4284.
    • (2011) Blood , vol.118 , Issue.15 , pp. 4274-4284
    • Zhang, F.1    Michaelson, J.E.2    Moshiach, S.3    Sachs, N.4    Zhao, W.5    Sun, Y.6    Sonnenberg, A.7    Lahti, J.M.8    Huang, H.9    Zhang, X.A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.