메뉴 건너뛰기




Volumn 63, Issue , 2015, Pages 47-57

Poly-l-arginine based materials as instructive substrates for fibroblast synthesis of collagen

Author keywords

Cell morphology; Collagen; Collagen structure; Fibroblast

Indexed keywords

AMINO ACIDS; ARGININE; ARTIFICIAL ORGANS; BIOMATERIALS; CELL CULTURE; CELLS; COLLAGEN; CYTOLOGY; DEPOSITION; ENDOTHELIAL CELLS; FIBROBLASTS; MORPHOLOGY; TISSUE; TISSUE ENGINEERING;

EID: 84952683408     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2015.05.045     Document Type: Article
Times cited : (24)

References (53)
  • 1
    • 76549136166 scopus 로고    scopus 로고
    • Influence of nanoscale surface topography on protein adsorption and cellular response
    • Lord M.S., Foss M., Besenbacher F. Influence of nanoscale surface topography on protein adsorption and cellular response. Nano Today 2010, 5:66-78. 10.1016/j.nantod.2010.01.001.
    • (2010) Nano Today , vol.5 , pp. 66-78
    • Lord, M.S.1    Foss, M.2    Besenbacher, F.3
  • 2
    • 53449088719 scopus 로고    scopus 로고
    • Adhesive substrate-modulation of adaptive immune responses
    • Acharya A.P., Dolgova N.V., Clare-Salzler M.J., Keselowsky B.G. Adhesive substrate-modulation of adaptive immune responses. Biomaterials 2008, 29:4736-4750. 10.1016/j.biomaterials.2008.08.040.
    • (2008) Biomaterials , vol.29 , pp. 4736-4750
    • Acharya, A.P.1    Dolgova, N.V.2    Clare-Salzler, M.J.3    Keselowsky, B.G.4
  • 3
    • 54049109170 scopus 로고    scopus 로고
    • In vivo cytokine-associated responses to biomaterials
    • Schutte R.J., Xie L., Klitzman B., Reichert W.M. In vivo cytokine-associated responses to biomaterials. Biomaterials 2009, 30:160-168. 10.1016/j.biomaterials.2008.09.026.
    • (2009) Biomaterials , vol.30 , pp. 160-168
    • Schutte, R.J.1    Xie, L.2    Klitzman, B.3    Reichert, W.M.4
  • 4
    • 40849094515 scopus 로고    scopus 로고
    • Foreign body reaction to biomaterials
    • Anderson J.M., Rodriguez A., Chang D.T. Foreign body reaction to biomaterials. Semin. Immunol. 2008, 20:86-100. 10.1016/j.smim.2007.11.004.
    • (2008) Semin. Immunol. , vol.20 , pp. 86-100
    • Anderson, J.M.1    Rodriguez, A.2    Chang, D.T.3
  • 5
    • 33750473402 scopus 로고    scopus 로고
    • The role of complement in biomaterial-induced inflammation
    • Nilsson B., Ekdahl K.N., Mollnes T.E., Lambris J.D. The role of complement in biomaterial-induced inflammation. Mol. Immunol. 2007, 44:82-94. 10.1016/j.molimm.2006.06.020.
    • (2007) Mol. Immunol. , vol.44 , pp. 82-94
    • Nilsson, B.1    Ekdahl, K.N.2    Mollnes, T.E.3    Lambris, J.D.4
  • 6
    • 0030934532 scopus 로고    scopus 로고
    • Wound Healing-Aiming for Perfect Skin Regeneration
    • Martin P. Wound Healing-Aiming for Perfect Skin Regeneration. Science 1997, 80(276):75-81. 10.1126/science.276.5309.75.
    • (1997) Science , vol.80 , Issue.276 , pp. 75-81
    • Martin, P.1
  • 8
    • 0042170050 scopus 로고    scopus 로고
    • Collagen morphology in human skin and scar tissue: no adaptations in response to mechanical loading at joints
    • Van Zuijlen P.P., Ruurda J.J., van Veen H.A., van Marle J., van Trier A.J., Groenevelt F., et al. Collagen morphology in human skin and scar tissue: no adaptations in response to mechanical loading at joints. Burns 2003, 29:423-431. 10.1016/S0305-4179(03)00052-4.
    • (2003) Burns , vol.29 , pp. 423-431
    • Van Zuijlen, P.P.1    Ruurda, J.J.2    van Veen, H.A.3    van Marle, J.4    van Trier, A.J.5    Groenevelt, F.6
  • 9
    • 52449133379 scopus 로고    scopus 로고
    • Eccleston GM. wound healing dressings and drug delivery systems: a review
    • Boateng J.S., Matthews K.H., Stevens H.N.E. Eccleston GM. wound healing dressings and drug delivery systems: a review. J. Pharm. Sci. 2008, 97:2892-2923. 10.1002/jps.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 2892-2923
    • Boateng, J.S.1    Matthews, K.H.2    Stevens, H.N.E.3
  • 10
    • 67849115975 scopus 로고    scopus 로고
    • Protein transport in human cells mediated by covalently and noncovalently conjugated arginine-rich intracellular delivery peptides
    • Hu J.-W., Liu B.R., Wu C.-Y., Lu S.-W., Lee H.-J. Protein transport in human cells mediated by covalently and noncovalently conjugated arginine-rich intracellular delivery peptides. Peptides 2009, 30:1669-1678. 10.1016/j.peptides.2009.06.006.
    • (2009) Peptides , vol.30 , pp. 1669-1678
    • Hu, J.-W.1    Liu, B.R.2    Wu, C.-Y.3    Lu, S.-W.4    Lee, H.-J.5
  • 11
    • 38949188925 scopus 로고    scopus 로고
    • Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides
    • Nakase I., Takeuchi T., Tanaka G., Futaki S. Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides. Adv. Drug Deliv. Rev. 2008, 60:598-607. 10.1016/j.addr.2007.10.006.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 598-607
    • Nakase, I.1    Takeuchi, T.2    Tanaka, G.3    Futaki, S.4
  • 13
    • 1542719813 scopus 로고    scopus 로고
    • The nature of water on surfaces of laboratory systems and implications for heterogeneous chemistry in the troposphere
    • Sumner A.L., Menke E.J., Dubowski Y., Newberg J.T., Penner R.M., Hemminger J.C., et al. The nature of water on surfaces of laboratory systems and implications for heterogeneous chemistry in the troposphere. Phys. Chem. Chem. Phys. 2004, 604-613.
    • (2004) Phys. Chem. Chem. Phys. , pp. 604-613
    • Sumner, A.L.1    Menke, E.J.2    Dubowski, Y.3    Newberg, J.T.4    Penner, R.M.5    Hemminger, J.C.6
  • 15
    • 0014862141 scopus 로고
    • The locomotion of mouse fibroblasts in tissue culture
    • Gail M.H., Boone C.W. The locomotion of mouse fibroblasts in tissue culture. Biophys. J. 1970, 10:980-993. 10.1016/S0006-3495(70)86347-0.
    • (1970) Biophys. J. , vol.10 , pp. 980-993
    • Gail, M.H.1    Boone, C.W.2
  • 16
    • 0037986215 scopus 로고    scopus 로고
    • Temporal variations in cell migration and traction during fibroblast-mediated gel compaction
    • Shreiber D.I., Barocas V.H., Tranquillo R.T. Temporal variations in cell migration and traction during fibroblast-mediated gel compaction. Biophys. J. 2003, 84:4102-4114. 10.1016/S0006-3495(03)75135-2.
    • (2003) Biophys. J. , vol.84 , pp. 4102-4114
    • Shreiber, D.I.1    Barocas, V.H.2    Tranquillo, R.T.3
  • 17
    • 52049121792 scopus 로고    scopus 로고
    • Endothelial cell adhesion and migration
    • Reinhart-King C.A. Endothelial cell adhesion and migration. Methods Enzymol. 2008, 443:45-64. 10.1016/S0076-6879(08)02003-X.
    • (2008) Methods Enzymol. , vol.443 , pp. 45-64
    • Reinhart-King, C.A.1
  • 19
    • 33847639336 scopus 로고    scopus 로고
    • Non-Invasive evaluation of algiante/Poly-L-lysine/alginate microcapsules by magnetic resonance microscopy
    • Constantinidis I., Grant S.C., Celper S., Gauffin-Holmberg I., Agering K., Oca-cossio J.A., et al. Non-Invasive evaluation of algiante/Poly-L-lysine/alginate microcapsules by magnetic resonance microscopy. Biomaterials 2007, 28:2438-2445.
    • (2007) Biomaterials , vol.28 , pp. 2438-2445
    • Constantinidis, I.1    Grant, S.C.2    Celper, S.3    Gauffin-Holmberg, I.4    Agering, K.5    Oca-cossio, J.A.6
  • 20
    • 84863238548 scopus 로고    scopus 로고
    • Second harmonic generation microscopy for quantitative analysis of collagen fibrillar structure
    • Chen X., Nadiarynkh O., Plotnikov S., Campagnola P.J. Second harmonic generation microscopy for quantitative analysis of collagen fibrillar structure. Nat. Protoc. 2012, 7:654-669. 10.1038/nprot.2012.009.
    • (2012) Nat. Protoc. , vol.7 , pp. 654-669
    • Chen, X.1    Nadiarynkh, O.2    Plotnikov, S.3    Campagnola, P.J.4
  • 21
    • 79959711674 scopus 로고    scopus 로고
    • Determination of collagen nanostructure from second-order susceptibility tensor analysis
    • Su P.-J., Chen W.-L., Chen Y.-F., Dong C.-Y. Determination of collagen nanostructure from second-order susceptibility tensor analysis. Biophys. J. 2011, 100:2053-2062. 10.1016/j.bpj.2011.02.015.
    • (2011) Biophys. J. , vol.100 , pp. 2053-2062
    • Su, P.-J.1    Chen, W.-L.2    Chen, Y.-F.3    Dong, C.-Y.4
  • 22
    • 33646172938 scopus 로고    scopus 로고
    • Characterization of the myosin-based source for second-harmonic generation from muscle sarcomeres
    • Plotnikov S.V., Millard A.C., Campagnola P.J., Mohler W.A. Characterization of the myosin-based source for second-harmonic generation from muscle sarcomeres. Biophys. J. 2006, 90:693-703. 10.1529/biophysj.105.071555.
    • (2006) Biophys. J. , vol.90 , pp. 693-703
    • Plotnikov, S.V.1    Millard, A.C.2    Campagnola, P.J.3    Mohler, W.A.4
  • 23
    • 33646155102 scopus 로고    scopus 로고
    • Optical clearing for improved contrast in second harmonic generation imaging of skeletal muscle
    • Plotnikov S., Juneja V., Isaacson A.B., Mohler W.A., Campagnola P.J. Optical clearing for improved contrast in second harmonic generation imaging of skeletal muscle. Biophys. J. 2006, 90:328-339. 10.1529/biophysj.105.066944.
    • (2006) Biophys. J. , vol.90 , pp. 328-339
    • Plotnikov, S.1    Juneja, V.2    Isaacson, A.B.3    Mohler, W.A.4    Campagnola, P.J.5
  • 25
    • 0022801395 scopus 로고
    • Optical second-harmonic microscopy, crossed-beam Summation, and small-angle scattering in rat-tail tendon
    • Freund I., Deutsch M. Optical second-harmonic microscopy, crossed-beam Summation, and small-angle scattering in rat-tail tendon. J. Biophys. 1986, 50:693-712.
    • (1986) J. Biophys. , vol.50 , pp. 693-712
    • Freund, I.1    Deutsch, M.2
  • 26
    • 2442676767 scopus 로고    scopus 로고
    • Characterization of collagen orientation in human dermis by two-dimensional second-harmonic-generation polarimetry
    • Yasui T., Tohno Y., Araki T. Characterization of collagen orientation in human dermis by two-dimensional second-harmonic-generation polarimetry. J. Biomed. Opt. 2004, 9:259-264. 10.1117/1.1644116.
    • (2004) J. Biomed. Opt. , vol.9 , pp. 259-264
    • Yasui, T.1    Tohno, Y.2    Araki, T.3
  • 27
    • 84894487742 scopus 로고    scopus 로고
    • Description of shape characteristics through Fourier and wavelet analysis
    • Yuan Z., Li F., Zhang P., Chen B. Description of shape characteristics through Fourier and wavelet analysis. Chin. J. Aeronaut. 2014, 27:160-168. 10.1016/j.cja.2013.07.011.
    • (2014) Chin. J. Aeronaut. , vol.27 , pp. 160-168
    • Yuan, Z.1    Li, F.2    Zhang, P.3    Chen, B.4
  • 29
    • 0030111469 scopus 로고    scopus 로고
    • Studies on the biocompatibility of materials: fibroblast reorganization of substratum-bound fibronectin on surfaces varying in wettability
    • Altankov G., Grinnell F., Groth T. Studies on the biocompatibility of materials: fibroblast reorganization of substratum-bound fibronectin on surfaces varying in wettability. J. Biomed. Mater. Res. 1996, 30:385-391. 10.1002/(SICI)1097-4636(199603)30:3<385::AID-JBM13>3.0.CO;2-J.
    • (1996) J. Biomed. Mater. Res. , vol.30 , pp. 385-391
    • Altankov, G.1    Grinnell, F.2    Groth, T.3
  • 31
    • 19944428596 scopus 로고    scopus 로고
    • Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion
    • Yeung T., Georges P.C., Flanagan L.A., Marg B., Ortiz M., Funaki M., et al. Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion. Cell. Motil. Cytoskelet. 2005, 60:24-34. 10.1002/cm.20041.
    • (2005) Cell. Motil. Cytoskelet. , vol.60 , pp. 24-34
    • Yeung, T.1    Georges, P.C.2    Flanagan, L.A.3    Marg, B.4    Ortiz, M.5    Funaki, M.6
  • 32
    • 79958096451 scopus 로고    scopus 로고
    • Bioactive plasma-polymerized bipolar films for enhanced endothelial cell mobility
    • Yang Z., Tu Q., Wang J., Lei X., He T., Sun H., et al. Bioactive plasma-polymerized bipolar films for enhanced endothelial cell mobility. Macromol. Biosci. 2011, 11:797-805. 10.1002/mabi.201000474.
    • (2011) Macromol. Biosci. , vol.11 , pp. 797-805
    • Yang, Z.1    Tu, Q.2    Wang, J.3    Lei, X.4    He, T.5    Sun, H.6
  • 33
    • 64849109856 scopus 로고    scopus 로고
    • A novel, non-angiogenic, mechanism of VEGF: Stimulation of keratinocyte and fibroblast migration
    • A30-A30
    • Stojadinovic O.K.A., Kodra A., Golinko M., Tomic-Canic M., Brem H. A novel, non-angiogenic, mechanism of VEGF: Stimulation of keratinocyte and fibroblast migration. Wound Repair Regen. 2007, 15. A30-A30.
    • (2007) Wound Repair Regen. , vol.15
    • Stojadinovic, O.K.A.1    Kodra, A.2    Golinko, M.3    Tomic-Canic, M.4    Brem, H.5
  • 34
    • 2642565248 scopus 로고    scopus 로고
    • Therapeutic angiogenesis and vasculogenesis for ischemic disease. Part I: angiogenic cytokines
    • Losordo D.W., Dimmeler S. Therapeutic angiogenesis and vasculogenesis for ischemic disease. Part I: angiogenic cytokines. Circulation 2004, 109:2487-2491. 10.1161/01.CIR.0000128595.79378.FA.
    • (2004) Circulation , vol.109 , pp. 2487-2491
    • Losordo, D.W.1    Dimmeler, S.2
  • 35
    • 33749015187 scopus 로고    scopus 로고
    • Temporally regulated delivery of VEGF in vitro and in vivo
    • Ennett A.B., Kaigler D., Mooney D.J. Temporally regulated delivery of VEGF in vitro and in vivo. J. Biomed. Mater. Res. Part A 2006, 79A:176-184. 10.1002/jbm.a.
    • (2006) J. Biomed. Mater. Res. Part A , vol.79A , pp. 176-184
    • Ennett, A.B.1    Kaigler, D.2    Mooney, D.J.3
  • 36
    • 85047694677 scopus 로고    scopus 로고
    • Microenvironmental VEGF concentration, not total dose, determines a threshold between normal and aberrant angiogenesis
    • Ozawa C.R., Banfi A., Glazer N.L., Thurston G., Springer M.L., Kraft P.E., et al. Microenvironmental VEGF concentration, not total dose, determines a threshold between normal and aberrant angiogenesis. J. Clin. Invest. 2004, 113:516-527. 10.1172/JCI200418420.Introduction.
    • (2004) J. Clin. Invest. , vol.113 , pp. 516-527
    • Ozawa, C.R.1    Banfi, A.2    Glazer, N.L.3    Thurston, G.4    Springer, M.L.5    Kraft, P.E.6
  • 38
    • 0031034352 scopus 로고    scopus 로고
    • Integrin - ligand binding properties govern cell migration speed through cell - substratum adhesiveness
    • Palecek S.P., Loftus J.C., Ginsberg M.H., Lauffenburger D.A., Horwitz A.F., Deshpande P.P., et al. Integrin - ligand binding properties govern cell migration speed through cell - substratum adhesiveness. Nature 1997, 385:537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5    Deshpande, P.P.6
  • 39
    • 77954676151 scopus 로고    scopus 로고
    • Integrins and ion channels in cell migration: implications for neuronal development, wound healing and metastatic spread
    • Becchetti A., Arcangeli A. Integrins and ion channels in cell migration: implications for neuronal development, wound healing and metastatic spread. Adv. Exp. Med. Biol. 2010, 674:107-123.
    • (2010) Adv. Exp. Med. Biol. , vol.674 , pp. 107-123
    • Becchetti, A.1    Arcangeli, A.2
  • 40
    • 0036159511 scopus 로고    scopus 로고
    • Cell adhesion peptides alter smooth muscle cell adhesion, proliferation, migration, and matrix protein synthesis on modified surfaces and in polymer scaffolds
    • Mann B.K., West J.L. Cell adhesion peptides alter smooth muscle cell adhesion, proliferation, migration, and matrix protein synthesis on modified surfaces and in polymer scaffolds. J. Biomed. Mater. Res. 2002, 60:86-93. 10.1002/jbm.10042.
    • (2002) J. Biomed. Mater. Res. , vol.60 , pp. 86-93
    • Mann, B.K.1    West, J.L.2
  • 41
    • 0033794698 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis and recycling of autocrine motility factor receptor to fibronectin fibrils is a limiting factor for NIH-3T3 cell motility
    • Le P.U., Benlimame N., Lagana A., Raz A., Nabi I.R. Clathrin-mediated endocytosis and recycling of autocrine motility factor receptor to fibronectin fibrils is a limiting factor for NIH-3T3 cell motility. J. Cell. Sci. 2000, 113(Pt 1):3227-3240.
    • (2000) J. Cell. Sci. , vol.113 , Issue.Pt 1 , pp. 3227-3240
    • Le, P.U.1    Benlimame, N.2    Lagana, A.3    Raz, A.4    Nabi, I.R.5
  • 42
    • 0037076354 scopus 로고    scopus 로고
    • Beta-Catenin stabilization dysregulates mesenchymal cell proliferation, motility, and invasiveness and causes aggressive fibromatosis and hyperplastic cutaneous wounds
    • Cheon S.S., Cheah A.Y.L., Turley S., Nadesan P., Poon R., Clevers H., et al. beta-Catenin stabilization dysregulates mesenchymal cell proliferation, motility, and invasiveness and causes aggressive fibromatosis and hyperplastic cutaneous wounds. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:6973-6978. 10.1073/pnas.102657399.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6973-6978
    • Cheon, S.S.1    Cheah, A.Y.L.2    Turley, S.3    Nadesan, P.4    Poon, R.5    Clevers, H.6
  • 43
    • 84862171167 scopus 로고    scopus 로고
    • Passive control of cell locomotion using micropatterns: the effect of micropattern geometry on the migratory behavior of adherent cells
    • Yoon S.-H., Kim Y.K., Han E.D., Seo Y.-H., Kim B.H., Mofrad M.R.K. Passive control of cell locomotion using micropatterns: the effect of micropattern geometry on the migratory behavior of adherent cells. Lab. Chip 2012, 12:2391-2402. 10.1039/c2lc40084g.
    • (2012) Lab. Chip , vol.12 , pp. 2391-2402
    • Yoon, S.-H.1    Kim, Y.K.2    Han, E.D.3    Seo, Y.-H.4    Kim, B.H.5    Mofrad, M.R.K.6
  • 44
    • 0346123091 scopus 로고    scopus 로고
    • Biocompatibility of collagen membranes crosslinked with glutaraldehyde or diphenylphosphoryl azide: An in vitro study
    • Marinucci L., Lilli C., Guerra M., Belcastro S., Becchetti E., Stabellini G., et al. Biocompatibility of collagen membranes crosslinked with glutaraldehyde or diphenylphosphoryl azide: An in vitro study. J. Biomed. Mater. Part A 2003, 67:504-509.
    • (2003) J. Biomed. Mater. Part A , vol.67 , pp. 504-509
    • Marinucci, L.1    Lilli, C.2    Guerra, M.3    Belcastro, S.4    Becchetti, E.5    Stabellini, G.6
  • 45
    • 0347674325 scopus 로고    scopus 로고
    • Matricellular proteins as modulators of wound healing and the foreign body response
    • Kyriakides T.R., Bornstein P. Matricellular proteins as modulators of wound healing and the foreign body response. Thromb. Haemost. 2003, 986-992. 10.1160/TH03-06-0399.
    • (2003) Thromb. Haemost. , pp. 986-992
    • Kyriakides, T.R.1    Bornstein, P.2
  • 46
    • 0032487118 scopus 로고    scopus 로고
    • Relative importance of surface wettability and charged functional groups on NIH 3T3 fibroblast attachment, spreading, and cytoskeletal organization
    • Webb K., Hlady V., Tresco P.A. Relative importance of surface wettability and charged functional groups on NIH 3T3 fibroblast attachment, spreading, and cytoskeletal organization. J. Biomed. Mater. Res. 1998, 41:422-430.
    • (1998) J. Biomed. Mater. Res. , vol.41 , pp. 422-430
    • Webb, K.1    Hlady, V.2    Tresco, P.A.3
  • 47
    • 0019534204 scopus 로고
    • Hydrophilic-Hydrophobic Copolymers as Cell Substrates: Effect on 3T3 Cell Growth Rates
    • Horbett T.A., Schway M.B., Ratner B.D. Hydrophilic-Hydrophobic Copolymers as Cell Substrates: Effect on 3T3 Cell Growth Rates. J. Colloid Interface Sci. 1985, 104:28-39.
    • (1985) J. Colloid Interface Sci. , vol.104 , pp. 28-39
    • Horbett, T.A.1    Schway, M.B.2    Ratner, B.D.3
  • 49
    • 0028474211 scopus 로고
    • Fibroblast growth on polymer surfaces and biosynthesis of collage
    • Tamada Y., Ikada Y. Fibroblast growth on polymer surfaces and biosynthesis of collage. J. Biomed. Mater. Res. 1994, 28:783-789.
    • (1994) J. Biomed. Mater. Res. , vol.28 , pp. 783-789
    • Tamada, Y.1    Ikada, Y.2
  • 51
    • 0022785853 scopus 로고
    • Collagen at interfaces I. In situ collagen adsorption at solution/air and solution/polymer interfaces
    • Deyme M., Baszkin A., Proust J.E., Perez E., Boissonnade M.M. Collagen at interfaces I. In situ collagen adsorption at solution/air and solution/polymer interfaces. J. Biomed. Mater. Res. 1986, 20:951-962.
    • (1986) J. Biomed. Mater. Res. , vol.20 , pp. 951-962
    • Deyme, M.1    Baszkin, A.2    Proust, J.E.3    Perez, E.4    Boissonnade, M.M.5
  • 52
    • 0021285534 scopus 로고
    • Reorganization of hydrated collagen lattices by human skin fibroblasts
    • Grinnell F., Lamke C.R. Reorganization of hydrated collagen lattices by human skin fibroblasts. J. Cell. Sci. 1984, 66:51-63.
    • (1984) J. Cell. Sci. , vol.66 , pp. 51-63
    • Grinnell, F.1    Lamke, C.R.2
  • 53
    • 0024543691 scopus 로고
    • Collagen processing, crosslinking, and fibril bundle assembly in matrix produced by fibroblasts in long-term cultures supplemented with ascorbic acid
    • Grinnell F., Fukamizu H., Pawelek P., Nakagawa S. Collagen processing, crosslinking, and fibril bundle assembly in matrix produced by fibroblasts in long-term cultures supplemented with ascorbic acid. Exp. Cell. Res. 1989, 181:483-491.
    • (1989) Exp. Cell. Res. , vol.181 , pp. 483-491
    • Grinnell, F.1    Fukamizu, H.2    Pawelek, P.3    Nakagawa, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.