메뉴 건너뛰기




Volumn 274, Issue 1, 2011, Pages 120-130

Integrin organization: Linking adhesion ligand nanopatterns with altered cell responses

Author keywords

Colloid; Focal adhesion kinase; Osteocalcin; Osteogenic differentiation; RGD peptide

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; BIOMATERIAL; FOCAL ADHESION KINASE; INTEGRIN;

EID: 79251610923     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2011.01.007     Document Type: Article
Times cited : (34)

References (72)
  • 3
    • 0036696097 scopus 로고    scopus 로고
    • Integrin structure: new twists and turns in dynamic cell adhesion
    • Arnaout M.A. Integrin structure: new twists and turns in dynamic cell adhesion. Immunol. Rev. 2002, 186:125-140.
    • (2002) Immunol. Rev. , vol.186 , pp. 125-140
    • Arnaout, M.A.1
  • 5
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G.I. Models for the specific adhesion of cells to cells. Science 1978, 200:618.
    • (1978) Science , vol.200 , pp. 618
    • Bell, G.I.1
  • 6
    • 0035131130 scopus 로고    scopus 로고
    • Patterns of integrin expression in a human mandibular explant model of osteoblast differentiation
    • Bennett J.H., Carter D.H., Alavi A.L., Beresford J.N., Walsh S. Patterns of integrin expression in a human mandibular explant model of osteoblast differentiation. Arch. Oral Biol. 2001, 46:229-238.
    • (2001) Arch. Oral Biol. , vol.46 , pp. 229-238
    • Bennett, J.H.1    Carter, D.H.2    Alavi, A.L.3    Beresford, J.N.4    Walsh, S.5
  • 8
    • 21844461558 scopus 로고    scopus 로고
    • Integrin dimerization and ligand organization: key components in integrin clustering for cell adhesion
    • Brinkerhoff C., Linderman J. Integrin dimerization and ligand organization: key components in integrin clustering for cell adhesion. Tissue Eng. 2005, 11:865-876.
    • (2005) Tissue Eng. , vol.11 , pp. 865-876
    • Brinkerhoff, C.1    Linderman, J.2
  • 9
    • 16644376489 scopus 로고    scopus 로고
    • Monte Carlo simulations of receptor dynamics: insights into cell signaling
    • Brinkerhoff C.J., Woolf P.J., Linderman J.J. Monte Carlo simulations of receptor dynamics: insights into cell signaling. J. Mol. Histol. 2004, 35:667-677.
    • (2004) J. Mol. Histol. , vol.35 , pp. 667-677
    • Brinkerhoff, C.J.1    Woolf, P.J.2    Linderman, J.J.3
  • 13
    • 34547676091 scopus 로고    scopus 로고
    • Engineering RGD nanopatterned hydrogels to control preosteoblast behavior: a combined computational and experimental approach
    • Comisar W.A., Kazmers N.H., Mooney D.J., Linderman J.J. Engineering RGD nanopatterned hydrogels to control preosteoblast behavior: a combined computational and experimental approach. Biomaterials 2007, 28:4409-4417.
    • (2007) Biomaterials , vol.28 , pp. 4409-4417
    • Comisar, W.A.1    Kazmers, N.H.2    Mooney, D.J.3    Linderman, J.J.4
  • 14
    • 28844472910 scopus 로고    scopus 로고
    • Multi-scale modeling to predict ligand presentation within RGD nanopatterned hydrogels
    • Comisar W.A., Hsiong S.X., Kong H.J., Mooney D.J., Linderman J.J. Multi-scale modeling to predict ligand presentation within RGD nanopatterned hydrogels. Biomaterials 2006, 27:2322-2329.
    • (2006) Biomaterials , vol.27 , pp. 2322-2329
    • Comisar, W.A.1    Hsiong, S.X.2    Kong, H.J.3    Mooney, D.J.4    Linderman, J.J.5
  • 15
    • 0034579141 scopus 로고    scopus 로고
    • Integrin-mediated signaling regulates AP-1 transcription factors and proliferation in osteoblasts
    • Cowles E.A., Brailey L.L., Gronowicz G.A. Integrin-mediated signaling regulates AP-1 transcription factors and proliferation in osteoblasts. J. Biomed. Mater. Res. 2000, 52:725-737.
    • (2000) J. Biomed. Mater. Res. , vol.52 , pp. 725-737
    • Cowles, E.A.1    Brailey, L.L.2    Gronowicz, G.A.3
  • 16
    • 8744300054 scopus 로고    scopus 로고
    • Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion
    • Critchley D.R. Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. Biochem. Soc. Trans. 2004, 32:831-836.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 831-836
    • Critchley, D.R.1
  • 17
    • 0037404371 scopus 로고    scopus 로고
    • Engineering cell adhesive surfaces that direct integrin alpha5beta1 binding using a recombinant fragment of fibronectin
    • Cutler S.M., Garcia A.J. Engineering cell adhesive surfaces that direct integrin alpha5beta1 binding using a recombinant fragment of fibronectin. Biomaterials 2003, 24:1759-1770.
    • (2003) Biomaterials , vol.24 , pp. 1759-1770
    • Cutler, S.M.1    Garcia, A.J.2
  • 18
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Danen E.H., Yamada K.M. Fibronectin, integrins, and growth control. J. Cell. Physiol. 2001, 189:1-13.
    • (2001) J. Cell. Physiol. , vol.189 , pp. 1-13
    • Danen, E.H.1    Yamada, K.M.2
  • 19
    • 0033373538 scopus 로고    scopus 로고
    • Reduced expression of (alpha)5(beta)1 integrin prevents spreading-dependent cell proliferation
    • Davey G., Buzzai M., Assoian R.K. Reduced expression of (alpha)5(beta)1 integrin prevents spreading-dependent cell proliferation. J. Cell. Sci. 1999, 112(Part 24):4663-4672.
    • (1999) J. Cell. Sci. , vol.112 , Issue.PART 24 , pp. 4663-4672
    • Davey, G.1    Buzzai, M.2    Assoian, R.K.3
  • 20
    • 33750273869 scopus 로고    scopus 로고
    • Structure and dynamics of colloidal depletion gels: coincidence of transitions and heterogeneity
    • 041403-1-041403-11
    • Dibble C.J., Kogan M., Solomon M.J. Structure and dynamics of colloidal depletion gels: coincidence of transitions and heterogeneity. Phys. Rev. E 2006, 74. 041403-1-041403-11.
    • (2006) Phys. Rev. E , vol.74
    • Dibble, C.J.1    Kogan, M.2    Solomon, M.J.3
  • 21
    • 0030611604 scopus 로고    scopus 로고
    • Integrin RIIb 3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding
    • Erb E., Tangemann K., Bohrmann B., Mueller B., Engel J. Integrin RIIb 3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. Biochemistry 1997, 36:7395-7402.
    • (1997) Biochemistry , vol.36 , pp. 7395-7402
    • Erb, E.1    Tangemann, K.2    Bohrmann, B.3    Mueller, B.4    Engel, J.5
  • 22
    • 0037241624 scopus 로고    scopus 로고
    • Multiple signaling pathways converge on the Cbfa1/Runx2 transcription factor to regulate osteoblast differentiation
    • Franceschi R.T., Xiao G., Jiang D., Gopalakrishnan R., Yang S., Reith E. Multiple signaling pathways converge on the Cbfa1/Runx2 transcription factor to regulate osteoblast differentiation. Connect. Tissue Res. 2003, 44:109-116.
    • (2003) Connect. Tissue Res. , vol.44 , pp. 109-116
    • Franceschi, R.T.1    Xiao, G.2    Jiang, D.3    Gopalakrishnan, R.4    Yang, S.5    Reith, E.6
  • 23
    • 33947716334 scopus 로고    scopus 로고
    • Model of integrin-mediated cell adhesion strengthening
    • Gallant N.D., Garcia A.J. Model of integrin-mediated cell adhesion strengthening. J. Biomech 2006, 40:1301-1309.
    • (2006) J. Biomech , vol.40 , pp. 1301-1309
    • Gallant, N.D.1    Garcia, A.J.2
  • 24
    • 24344434553 scopus 로고    scopus 로고
    • Cell adhesion strengthening: contributions of adhesive area, integrin binding, and focal adhesion assembly
    • Gallant N.D., Michael K.E., Garcia A.J. Cell adhesion strengthening: contributions of adhesive area, integrin binding, and focal adhesion assembly. Mol. Biol. Cell 2005, 16:4329-4340.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4329-4340
    • Gallant, N.D.1    Michael, K.E.2    Garcia, A.J.3
  • 25
    • 0344306509 scopus 로고    scopus 로고
    • Biomimetic peptides that engage specific integrin-dependent signaling pathways and bind to calcium phosphate surfaces
    • Gilbert M., Giachelli C.M., Stayton P.S. Biomimetic peptides that engage specific integrin-dependent signaling pathways and bind to calcium phosphate surfaces. J. Biomed. Mater. Res. A 2003, 67:69-77.
    • (2003) J. Biomed. Mater. Res. A , vol.67 , pp. 69-77
    • Gilbert, M.1    Giachelli, C.M.2    Stayton, P.S.3
  • 26
    • 30944452186 scopus 로고    scopus 로고
    • Focal adhesion size controls tension-dependent recruitment of alpha-smooth muscle actin stress fibers
    • Goffin J.M., Pittet P., Csucs G., Lussi J.W., Meister J.J., Hinz B. Focal adhesion size controls tension-dependent recruitment of alpha-smooth muscle actin stress fibers. J. Cell Biol. 2006, 172:259-268.
    • (2006) J. Cell Biol. , vol.172 , pp. 259-268
    • Goffin, J.M.1    Pittet, P.2    Csucs, G.3    Lussi, J.W.4    Meister, J.J.5    Hinz, B.6
  • 27
    • 0034091670 scopus 로고    scopus 로고
    • Time and force dependence of the rupture of glycoprotein IIb-IIIa-fibrinogen bonds between latex spheres
    • Goldsmith H.L., McIntosh F.A., Shahin J., Frojmovic M.M. Time and force dependence of the rupture of glycoprotein IIb-IIIa-fibrinogen bonds between latex spheres. Biophys. J. 2000, 78:1195.
    • (2000) Biophys. J. , vol.78 , pp. 1195
    • Goldsmith, H.L.1    McIntosh, F.A.2    Shahin, J.3    Frojmovic, M.M.4
  • 28
    • 33749534490 scopus 로고    scopus 로고
    • Modeling the size distribution of focal adhesions
    • Gov N.S. Modeling the size distribution of focal adhesions. Biophys. J. 2006, 91:2844-2847.
    • (2006) Biophys. J. , vol.91 , pp. 2844-2847
    • Gov, N.S.1
  • 29
    • 0030772959 scopus 로고    scopus 로고
    • Role of focal adhesion kinase in integrin signaling
    • Guan J.L. Role of focal adhesion kinase in integrin signaling. Int. J. Biochem. Cell Biol. 1997, 29:1085-1096.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 1085-1096
    • Guan, J.L.1
  • 30
    • 28844489128 scopus 로고    scopus 로고
    • The effect of ligand type and density on osteoblast adhesion, proliferation, and matrix mineralization
    • Harbers G.M., Healy K.E. The effect of ligand type and density on osteoblast adhesion, proliferation, and matrix mineralization. J. Biomed. Mater. Res. A 2005, 75:855-869.
    • (2005) J. Biomed. Mater. Res. A , vol.75 , pp. 855-869
    • Harbers, G.M.1    Healy, K.E.2
  • 33
    • 3042522702 scopus 로고    scopus 로고
    • Monoclonal antibodies as probes of integrin priming and activation
    • Humphries M.J. Monoclonal antibodies as probes of integrin priming and activation. Biochem. Soc. Trans. 2004, 32:407-411.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 407-411
    • Humphries, M.J.1
  • 34
    • 0034893617 scopus 로고    scopus 로고
    • Nanoscale clustering of RGD peptides at surfaces using comb polymers. 1. Synthesis and characterization of comb thin films
    • Irvine D.J., Mayes A.M., Griffith L.G. Nanoscale clustering of RGD peptides at surfaces using comb polymers. 1. Synthesis and characterization of comb thin films. Biomacromolecules 2001, 2:85-94.
    • (2001) Biomacromolecules , vol.2 , pp. 85-94
    • Irvine, D.J.1    Mayes, A.M.2    Griffith, L.G.3
  • 35
    • 0036214480 scopus 로고    scopus 로고
    • Simulations of cell-surface integrin binding to nanoscale-clustered adhesion ligands
    • Irvine D., Hue K., Mayes A., Griffith L. Simulations of cell-surface integrin binding to nanoscale-clustered adhesion ligands. Biophys. J. 2002, 82:120-132.
    • (2002) Biophys. J. , vol.82 , pp. 120-132
    • Irvine, D.1    Hue, K.2    Mayes, A.3    Griffith, L.4
  • 36
    • 1542267780 scopus 로고    scopus 로고
    • Using model substrates to study the dependence of focal adhesion formation on the affinity of integrin-ligand complexes
    • Kato M., Mrksich M. Using model substrates to study the dependence of focal adhesion formation on the affinity of integrin-ligand complexes. Biochemistry 2004, 43:2699-2707.
    • (2004) Biochemistry , vol.43 , pp. 2699-2707
    • Kato, M.1    Mrksich, M.2
  • 37
    • 33845500925 scopus 로고    scopus 로고
    • Quantifying the relation between adhesion ligand-receptor bond formation and cell phenotype
    • Kong H.J., Boontheekul T., Mooney D.J. Quantifying the relation between adhesion ligand-receptor bond formation and cell phenotype. Proc. Natl. Acad. Sci. 2006, 103:18534-18539.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 18534-18539
    • Kong, H.J.1    Boontheekul, T.2    Mooney, D.J.3
  • 38
    • 33846871232 scopus 로고    scopus 로고
    • Nanoscale cell adhesion ligand presentation regulates nonviral gene delivery and expression
    • Kong H.J., Hsiong S., Mooney D.J. Nanoscale cell adhesion ligand presentation regulates nonviral gene delivery and expression. Nano Letters 2007, 7(1):161-166.
    • (2007) Nano Letters , vol.7 , Issue.1 , pp. 161-166
    • Kong, H.J.1    Hsiong, S.2    Mooney, D.J.3
  • 39
    • 15444367409 scopus 로고    scopus 로고
    • FRET measurements of cell-traction forces and nano-scale clustering of adhesion ligands varied by substrate stiffness
    • Kong H.J., Polte T.R., Alsberg E., Mooney D.J. FRET measurements of cell-traction forces and nano-scale clustering of adhesion ligands varied by substrate stiffness. Proc. Natl. Acad. Sci. USA 2005, 102:4300-4305.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4300-4305
    • Kong, H.J.1    Polte, T.R.2    Alsberg, E.3    Mooney, D.J.4
  • 40
    • 0036538656 scopus 로고    scopus 로고
    • Co-regulation of cell adhesion by nanoscale RGD organization and mechanical stimulus
    • Koo L., Irvine D., Mayes A., Lauffenburger D., Griffith L. Co-regulation of cell adhesion by nanoscale RGD organization and mechanical stimulus. J. Cell Sci. 2002, 115:1423-1433.
    • (2002) J. Cell Sci. , vol.115 , pp. 1423-1433
    • Koo, L.1    Irvine, D.2    Mayes, A.3    Lauffenburger, D.4    Griffith, L.5
  • 42
    • 0035501388 scopus 로고    scopus 로고
    • Force measurements on the molecular interactions between ligand (RGD) and human platelet αIIbΒ3 receptor system
    • Lee I., Marchant R.E. Force measurements on the molecular interactions between ligand (RGD) and human platelet αIIbΒ3 receptor system. Surf. Sci. 2001, 491:433.
    • (2001) Surf. Sci. , vol.491 , pp. 433
    • Lee, I.1    Marchant, R.E.2
  • 43
    • 4444348678 scopus 로고    scopus 로고
    • Nanoscale adhesion ligand organization regulates osteoblast proliferation and differentiation
    • Lee K.Y., Alsberg E., Hsiong S., Comisar W., Linderman J., Ziff R., Mooney D. Nanoscale adhesion ligand organization regulates osteoblast proliferation and differentiation. Nano Letters 2004, 4:1501-1506.
    • (2004) Nano Letters , vol.4 , pp. 1501-1506
    • Lee, K.Y.1    Alsberg, E.2    Hsiong, S.3    Comisar, W.4    Linderman, J.5    Ziff, R.6    Mooney, D.7
  • 44
    • 0033575007 scopus 로고    scopus 로고
    • Single integrin molecule adhesion forces in intact cells measured by atomic force microscopy
    • Lehenkari P.P., Horton M.A. Single integrin molecule adhesion forces in intact cells measured by atomic force microscopy. Biochem. Biophys. Res. Commun. 1999, 259:645-650.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 645-650
    • Lehenkari, P.P.1    Horton, M.A.2
  • 45
    • 3042565187 scopus 로고    scopus 로고
    • Structural basis for integrin alphaIIbbeta3 clustering
    • Li R., Bennett J.S., DeGrado W.F. Structural basis for integrin alphaIIbbeta3 clustering. Biochem. Soc. Trans. 2004, 32:412-415.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 412-415
    • Li, R.1    Bennett, J.S.2    DeGrado, W.F.3
  • 46
    • 0038644597 scopus 로고    scopus 로고
    • Oligomerization of the integrin αIIbΒ3 by modulation of transmembrane helix associations
    • Li R.H., Babu C.R., Lear J.D., Wand A.J., Bennett J.S., DeGrado W.F. Oligomerization of the integrin αIIbΒ3 by modulation of transmembrane helix associations. Science 2001, 300:795.
    • (2001) Science , vol.300 , pp. 795
    • Li, R.H.1    Babu, C.R.2    Lear, J.D.3    Wand, A.J.4    Bennett, J.S.5    DeGrado, W.F.6
  • 47
    • 57049149152 scopus 로고    scopus 로고
    • Cell response to RGD density in cross-linked artificial extracellular matrix protein films
    • Liu J.C., Tirrell D.A. Cell response to RGD density in cross-linked artificial extracellular matrix protein films. Biomacromolecules 2008, 9:2984-2988.
    • (2008) Biomacromolecules , vol.9 , pp. 2984-2988
    • Liu, J.C.1    Tirrell, D.A.2
  • 49
    • 75749129840 scopus 로고    scopus 로고
    • Controlling stem cell fate with material design
    • Marklein R.A., Burdick J.A. Controlling stem cell fate with material design. Adv. Mater. 2010, 22:175-189.
    • (2010) Adv. Mater. , vol.22 , pp. 175-189
    • Marklein, R.A.1    Burdick, J.A.2
  • 51
    • 0028954797 scopus 로고
    • Synergistic role for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto S., Akiyama S., Yamada K. Synergistic role for receptor occupancy and aggregation in integrin transmembrane function. Science 1995, 267:883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.2    Yamada, K.3
  • 52
    • 0036898944 scopus 로고    scopus 로고
    • What can surface chemistry do for cell biology?
    • Mrksich M. What can surface chemistry do for cell biology?. Curr. Opin. Chem. Biol. 2002, 6:794-797.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 794-797
    • Mrksich, M.1
  • 53
    • 0024293497 scopus 로고
    • Electron microscopy and structural model of human fibronectin receptor
    • Nermut M.V., Green N.M., Eason P., Yamada S.S., Yamada K.M. Electron microscopy and structural model of human fibronectin receptor. EMBO J. 1988, 7:4093-4099.
    • (1988) EMBO J. , vol.7 , pp. 4093-4099
    • Nermut, M.V.1    Green, N.M.2    Eason, P.3    Yamada, S.S.4    Yamada, K.M.5
  • 54
    • 4344596239 scopus 로고    scopus 로고
    • Cell mechanosensitivity controls the anisotropy of focal adhesions
    • Nicolas A., Geiger B., Safran S.A. Cell mechanosensitivity controls the anisotropy of focal adhesions. Proc. Natl. Acad. Sci. 2004, 101:12520-12525.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 12520-12525
    • Nicolas, A.1    Geiger, B.2    Safran, S.A.3
  • 55
    • 33646196554 scopus 로고    scopus 로고
    • Limitation of cell adhesion by the elasticity of the extracellular matrix
    • Nicolas A., Safran S.A. Limitation of cell adhesion by the elasticity of the extracellular matrix. Biophys. J. 2006, 91:61-73.
    • (2006) Biophys. J. , vol.91 , pp. 61-73
    • Nicolas, A.1    Safran, S.A.2
  • 56
    • 0034494961 scopus 로고    scopus 로고
    • Focal adhesions: structure and dynamics
    • Petit V., Thiery J.P. Focal adhesions: structure and dynamics. Biol. Cell. 2000, 92:477-494.
    • (2000) Biol. Cell. , vol.92 , pp. 477-494
    • Petit, V.1    Thiery, J.P.2
  • 57
    • 33746255971 scopus 로고    scopus 로고
    • Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports
    • Petrie T.A., Capadona J.R., Reyes C.D., Garcia A.J. Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports. Biomaterials 2006, 27:5459-5470.
    • (2006) Biomaterials , vol.27 , pp. 5459-5470
    • Petrie, T.A.1    Capadona, J.R.2    Reyes, C.D.3    Garcia, A.J.4
  • 58
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., Ruoslahiti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984, 309:30.
    • (1984) Nature , vol.309 , pp. 30
    • Pierschbacher, M.D.1    Ruoslahiti, E.2
  • 59
    • 2942536146 scopus 로고    scopus 로고
    • Alpha2beta1 integrin-specific collagen-mimetic surfaces supporting osteoblastic differentiation
    • Reyes C.D., Garcia A.J. Alpha2beta1 integrin-specific collagen-mimetic surfaces supporting osteoblastic differentiation. J. Biomed. Mater. Res. A 2004, 69:591-600.
    • (2004) J. Biomed. Mater. Res. A , vol.69 , pp. 591-600
    • Reyes, C.D.1    Garcia, A.J.2
  • 62
    • 0036010014 scopus 로고    scopus 로고
    • Enhanced expression of the osteoblastic phenotype on substrates that modulate fibronectin conformation and integrin receptor binding
    • Stephansson S.N., Byers B.A., Garcia A.J. Enhanced expression of the osteoblastic phenotype on substrates that modulate fibronectin conformation and integrin receptor binding. Biomaterials 2002, 23:2527-2534.
    • (2002) Biomaterials , vol.23 , pp. 2527-2534
    • Stephansson, S.N.1    Byers, B.A.2    Garcia, A.J.3
  • 63
    • 0030719465 scopus 로고    scopus 로고
    • Differentiation and transforming growth factor-beta receptor down-regulation by collagen-alpha2beta1 integrin interaction is mediated by focal adhesion kinase and its downstream signals in murine osteoblastic cells
    • Takeuchi Y., Suzawa M., Kikuchi T., Nishida E., Fujita T., Matsumoto T. Differentiation and transforming growth factor-beta receptor down-regulation by collagen-alpha2beta1 integrin interaction is mediated by focal adhesion kinase and its downstream signals in murine osteoblastic cells. J. Biol. Chem. 1997, 272:29309-29316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29309-29316
    • Takeuchi, Y.1    Suzawa, M.2    Kikuchi, T.3    Nishida, E.4    Fujita, T.5    Matsumoto, T.6
  • 64
    • 0037417907 scopus 로고    scopus 로고
    • Direct visualization of long-range heterogeneous structure in dense colloidal gels
    • Varadan P., Solomon M.J. Direct visualization of long-range heterogeneous structure in dense colloidal gels. Langmuir. 2003, 19:509-512.
    • (2003) Langmuir. , vol.19 , pp. 509-512
    • Varadan, P.1    Solomon, M.J.2
  • 65
    • 2942696577 scopus 로고    scopus 로고
    • Beta-1 integrin-mediated adhesion may be initiated by multiple incomplete bonds, thus accounting for the functional importance of receptor clustering
    • Vitte J., Benoliel A., Eymeric P., Bongrand P., Pierres A. Beta-1 integrin-mediated adhesion may be initiated by multiple incomplete bonds, thus accounting for the functional importance of receptor clustering. Biophys. J. 2004, 86:4059-4074.
    • (2004) Biophys. J. , vol.86 , pp. 4059-4074
    • Vitte, J.1    Benoliel, A.2    Eymeric, P.3    Bongrand, P.4    Pierres, A.5
  • 67
    • 0028187505 scopus 로고
    • Focal contact assembly through cytoskeletal polymerization: steady-state analysis
    • Ward M.D., Hammer D.A. Focal contact assembly through cytoskeletal polymerization: steady-state analysis. J. Math. Biol. 1994, 32:677.
    • (1994) J. Math. Biol. , vol.32 , pp. 677
    • Ward, M.D.1    Hammer, D.A.2
  • 69
    • 0037678455 scopus 로고    scopus 로고
    • Self organization of membrane proteins via dimerization
    • Woolf P.J., Linderman J.J. Self organization of membrane proteins via dimerization. Biophys. J. 2003, 104:217.
    • (2003) Biophys. J. , vol.104 , pp. 217
    • Woolf, P.J.1    Linderman, J.J.2
  • 70
    • 20444395813 scopus 로고    scopus 로고
    • The effect of incorporating RGD adhesive peptide in polyethylene glycol diacrylate hydrogel on osteogenesis of bone marrow stromal cells
    • Yang F., Williams C.G., Wang D., Lee H., Manson P.N., Elisseeff J. The effect of incorporating RGD adhesive peptide in polyethylene glycol diacrylate hydrogel on osteogenesis of bone marrow stromal cells. Biomaterials 2005, 26:5991-5998.
    • (2005) Biomaterials , vol.26 , pp. 5991-5998
    • Yang, F.1    Williams, C.G.2    Wang, D.3    Lee, H.4    Manson, P.N.5    Elisseeff, J.6
  • 71
    • 0030840113 scopus 로고    scopus 로고
    • Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding
    • Yauch R.L., Felsenfeld D.P., Draeft S.K., Chen L.B., Sheetz M.P., Hemler M.E. Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding. J. Exp. Med. 1997, 186:1347-1355.
    • (1997) J. Exp. Med. , vol.186 , pp. 1347-1355
    • Yauch, R.L.1    Felsenfeld, D.P.2    Draeft, S.K.3    Chen, L.B.4    Sheetz, M.P.5    Hemler, M.E.6
  • 72
    • 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. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 2007, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.