메뉴 건너뛰기




Volumn 118, Issue , 2012, Pages 44-52

Nanoscale characterization of cell receptors and binding sites on cell-derived extracellular matrices

Author keywords

Cell adhesion; Electric field; Electrostatic force microscopy; Fibronectin; Immunogold; Integrin; Scanning force microscopy

Indexed keywords

ADHESION BEHAVIORS; ADHESION RECEPTORS; CELL RECEPTORS; CORRELATION ANALYSIS; ELECTROSTATIC FORCE MICROSCOPY; EXTERNAL INFLUENCES; EXTRACELLULAR; EXTRACELLULAR LIGANDS; EXTRACELLULAR MATRICES; FIBRONECTIN; IMMUNOGOLD; IMMUNOLABELING; INTEGRINS; MATRIX PROTEINS; MOLECULAR ASSEMBLY; NANOSCALE CHARACTERIZATION; POLYMER SCAFFOLDS; TUNABLE PROPERTIES;

EID: 84862338425     PISSN: 03043991     EISSN: 18792723     Source Type: Journal    
DOI: 10.1016/j.ultramic.2012.04.011     Document Type: Article
Times cited : (7)

References (35)
  • 4
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao Y., Schwarzbauer J.E. Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biology 2005, 24:389-399.
    • (2005) Matrix Biology , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 6
    • 53849147849 scopus 로고    scopus 로고
    • The impact of primary and secondary ligand coupling on extracellular matrix characteristics and formation of endothelial capillaries
    • Herklotz M., Werner C., Pompe T. The impact of primary and secondary ligand coupling on extracellular matrix characteristics and formation of endothelial capillaries. Biomaterials 2009, 30:35-44.
    • (2009) Biomaterials , vol.30 , pp. 35-44
    • Herklotz, M.1    Werner, C.2    Pompe, T.3
  • 9
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
    • Hell S.W., Wichmann J. Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Optics Letters 1994, 19:780-782.
    • (1994) Optics Letters , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 10
    • 0031200818 scopus 로고    scopus 로고
    • High-resolution cryo-scanning electron microscopy study of the macromolecular structure of fibronectin fibrils
    • Chen Y., Zardi L., Peters D.M. High-resolution cryo-scanning electron microscopy study of the macromolecular structure of fibronectin fibrils. Scanning 1997, 19:349-355.
    • (1997) Scanning , vol.19 , pp. 349-355
    • Chen, Y.1    Zardi, L.2    Peters, D.M.3
  • 11
    • 0025940655 scopus 로고
    • Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures
    • Dzamba B.J., Peters D.M. Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures. Journal of Cell Science 1991, 100(Pt 3):605-612.
    • (1991) Journal of Cell Science , vol.100 , Issue.PART 3 , pp. 605-612
    • Dzamba, B.J.1    Peters, D.M.2
  • 13
    • 11244279569 scopus 로고    scopus 로고
    • Nanoscale features of fibronectin fibrillogenesis depend on protein-substrate interaction and cytoskeleton structure
    • Pompe T., Renner L., Werner C. Nanoscale features of fibronectin fibrillogenesis depend on protein-substrate interaction and cytoskeleton structure. Biophysical Journal 2005, 88:527-534.
    • (2005) Biophysical Journal , vol.88 , pp. 527-534
    • Pompe, T.1    Renner, L.2    Werner, C.3
  • 16
    • 23144456804 scopus 로고    scopus 로고
    • AFM imaging of ligand binding to platelet integrin alphaIIbbeta3 receptors reconstituted into planar lipid bilayers
    • Hussain M.A., Agnihotri A., Siedlecki C.A. AFM imaging of ligand binding to platelet integrin alphaIIbbeta3 receptors reconstituted into planar lipid bilayers. Langmuir 2005, 21:6979-6986.
    • (2005) Langmuir , vol.21 , pp. 6979-6986
    • Hussain, M.A.1    Agnihotri, A.2    Siedlecki, C.A.3
  • 19
    • 2042450432 scopus 로고
    • Purification of human plasma fibronectin
    • Brew S.A., Ingram K.C. Purification of human plasma fibronectin. Methods in Cell Science 1994, 16:197-199.
    • (1994) Methods in Cell Science , vol.16 , pp. 197-199
    • Brew, S.A.1    Ingram, K.C.2
  • 20
    • 1842640370 scopus 로고    scopus 로고
    • Dynamic alterations of fibronectin layers on copolymer substrates with graded physicochemical characteristics
    • Renner L., Pompe T., Salchert K., Werner C. Dynamic alterations of fibronectin layers on copolymer substrates with graded physicochemical characteristics. Langmuir 2004, 20:2928-2933.
    • (2004) Langmuir , vol.20 , pp. 2928-2933
    • Renner, L.1    Pompe, T.2    Salchert, K.3    Werner, C.4
  • 21
    • 0026098597 scopus 로고
    • Improved method of human umbilical arterial endothelial cell culture
    • Weis J.R., Sun B., Rodgers G.M. Improved method of human umbilical arterial endothelial cell culture. Thrombosis Research 1991, 61:171-173.
    • (1991) Thrombosis Research , vol.61 , pp. 171-173
    • Weis, J.R.1    Sun, B.2    Rodgers, G.M.3
  • 22
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha(5)beta(1) function
    • Friedland J.C., Lee M.H., Boettiger D. Mechanically activated integrin switch controls alpha(5)beta(1) function. Science 2009, 323:642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 23
    • 0032753925 scopus 로고    scopus 로고
    • Integrin-fibronectin interactions at the cell-material interface: initial integrin binding and signaling
    • Garcia A.J., Boettiger D. Integrin-fibronectin interactions at the cell-material interface: initial integrin binding and signaling. Biomaterials 1999, 20:2427-2433.
    • (1999) Biomaterials , vol.20 , pp. 2427-2433
    • Garcia, A.J.1    Boettiger, D.2
  • 24
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis
    • Pankov R., Cukierman E., Katz B.Z., Matsumoto K., Lin D.C., Lin S., Hahn C., Yamada K.M. Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. Journal of Cell Biology 2000, 148:1075-1090.
    • (2000) Journal of Cell Biology , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5    Lin, S.6    Hahn, C.7    Yamada, K.M.8
  • 25
    • 27744560439 scopus 로고    scopus 로고
    • Fibronectin fibril pattern displays the force balance of cell-matrix adhesion
    • Pompe T., Keller K., Mitdank C., Werner C. Fibronectin fibril pattern displays the force balance of cell-matrix adhesion. European Biophysics Journal 2005, 34:1049-1056.
    • (2005) European Biophysics Journal , vol.34 , pp. 1049-1056
    • Pompe, T.1    Keller, K.2    Mitdank, C.3    Werner, C.4
  • 27
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • Cukierman E., Pankov R., Stevens D.R., Yamada K.M. Taking cell-matrix adhesions to the third dimension. Science 2001, 294:1708-1712.
    • (2001) Science , vol.294 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 28
    • 0034114114 scopus 로고    scopus 로고
    • Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions
    • Katz B.Z., Zamir E., Bershadsky A., Kam Z., Yamada K.M., Geiger B. Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions. Molecular Biology of the Cell 2000, 11:1047-1060.
    • (2000) Molecular Biology of the Cell , vol.11 , pp. 1047-1060
    • Katz, B.Z.1    Zamir, E.2    Bershadsky, A.3    Kam, Z.4    Yamada, K.M.5    Geiger, B.6
  • 34
    • 33645417227 scopus 로고    scopus 로고
    • Understanding the elasticity of fibronectin fibrils: unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy
    • Abu-Lail N.I., Ohashi T., Clark R.L., Erickson H.P., Zauscher S. Understanding the elasticity of fibronectin fibrils: unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy. Matrix Biology 2006, 25:175-184.
    • (2006) Matrix Biology , vol.25 , pp. 175-184
    • Abu-Lail, N.I.1    Ohashi, T.2    Clark, R.L.3    Erickson, H.P.4    Zauscher, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.