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Volumn 33, Issue 30, 2012, Pages 7366-7374

Molecular crowding of collagen: A pathway to produce highly-organized collagenous structures

Author keywords

Collagen; Corneal tissue engineering; Extracellular matrix; Molecular crowding; Organized matrix

Indexed keywords

ANNULUS FIBROSUS; BIOLOGICAL TISSUES; CELL SURFACES; CELL-FREE; COLLAGEN MOLECULES; CONNECTIVE TISSUES; CONTROL OF STRUCTURE; CORNEAL TISSUE ENGINEERING; EMBRYONIC DEVELOPMENT; EXTRACELLULAR MATRICES; GEOMETRIC CONFINEMENT; IN-VITRO; IN-VIVO; INDIVIDUAL CELLS; LOAD-BEARING; MECHANICAL LOADS; MOLECULAR CROWDING; NANO SCALE; ORGANIZATIONAL INFORMATION; ORGANIZED STRUCTURE; PHYSIO-CHEMICAL PROPERTIES; PLANAR CELLS; PLANAR GEOMETRIES; SIMPLE APPROACH; TISSUE ENGINEERS; TYPE I COLLAGEN;

EID: 84864988082     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2012.06.041     Document Type: Article
Times cited : (85)

References (66)
  • 1
    • 0033028909 scopus 로고    scopus 로고
    • Role of actin stress fibres in the development of the intervertebral disc: cytoskeletal control of extracellular matrix assembly
    • Hayes A.J., Benjamin M., Ralphs J.R. Role of actin stress fibres in the development of the intervertebral disc: cytoskeletal control of extracellular matrix assembly. Dev Dyn 1999, 215:179-189.
    • (1999) Dev Dyn , vol.215 , pp. 179-189
    • Hayes, A.J.1    Benjamin, M.2    Ralphs, J.R.3
  • 2
    • 0032907513 scopus 로고    scopus 로고
    • Reaction-diffusion microtubule concentration patterns occur during biological morphogenesis
    • Papaseit C., Vuillard L., Tabony J. Reaction-diffusion microtubule concentration patterns occur during biological morphogenesis. Biophys Chem 1999, 79:33-39.
    • (1999) Biophys Chem , vol.79 , pp. 33-39
    • Papaseit, C.1    Vuillard, L.2    Tabony, J.3
  • 3
    • 23944494639 scopus 로고    scopus 로고
    • Morphogenesis of the anterior segment in the zebrafish eye
    • Soules K.A., Link B.A. Morphogenesis of the anterior segment in the zebrafish eye. BMC Dev Biol 2005, 5:12.
    • (2005) BMC Dev Biol , vol.5 , pp. 12
    • Soules, K.A.1    Link, B.A.2
  • 4
    • 0028235645 scopus 로고
    • Assembly of the tendon extracellular matrix during development
    • Birk D.E., Zycband E. Assembly of the tendon extracellular matrix during development. J Anat 1994, 184(Pt 3):457-463.
    • (1994) J Anat , vol.184 , Issue.PART 3 , pp. 457-463
    • Birk, D.E.1    Zycband, E.2
  • 5
    • 27144435592 scopus 로고    scopus 로고
    • The hierarchical architecture of nacre and its mimetic material
    • Oaki Y., Imai H. The hierarchical architecture of nacre and its mimetic material. Angew Chem Int Ed Engl 2005, 44:6571-6575.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 6571-6575
    • Oaki, Y.1    Imai, H.2
  • 6
    • 0034526523 scopus 로고    scopus 로고
    • How is a tissue built?
    • Cowin S.C. How is a tissue built?. J Biomech Eng 2000, 122:553-569.
    • (2000) J Biomech Eng , vol.122 , pp. 553-569
    • Cowin, S.C.1
  • 7
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • Silver F.H., Freeman J.W., Seehra G.P. Collagen self-assembly and the development of tendon mechanical properties. J Biomech 2003, 36:1529-1553.
    • (2003) J Biomech , vol.36 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 8
    • 4444277314 scopus 로고    scopus 로고
    • Tissue growth and remodeling
    • Cowin S.C. Tissue growth and remodeling. Annu Rev Biomed Eng 2004, 6:77-107.
    • (2004) Annu Rev Biomed Eng , vol.6 , pp. 77-107
    • Cowin, S.C.1
  • 9
    • 0025020148 scopus 로고
    • Temporal relationships of F-actin bundle formation, collagen and fibronectin matrix assembly, and fibronectin receptor expression to wound contraction
    • Welch M.P., Odland G.F., Clark R.A. Temporal relationships of F-actin bundle formation, collagen and fibronectin matrix assembly, and fibronectin receptor expression to wound contraction. J Cell Biol 1990, 110:133-145.
    • (1990) J Cell Biol , vol.110 , pp. 133-145
    • Welch, M.P.1    Odland, G.F.2    Clark, R.A.3
  • 10
    • 0034964447 scopus 로고    scopus 로고
    • The structure and biological features of fibrinogen and fibrin
    • Mosesson M.W., Siebenlist K.R., Meh D.A. The structure and biological features of fibrinogen and fibrin. Ann N Y Acad Sci 2001, 936:11-30.
    • (2001) Ann N Y Acad Sci , vol.936 , pp. 11-30
    • Mosesson, M.W.1    Siebenlist, K.R.2    Meh, D.A.3
  • 11
    • 0031304319 scopus 로고    scopus 로고
    • Mechanical remodeling of the endothelial surface and actin cytoskeleton induced by fluid flow
    • Satcher R., Dewey C.F., Hartwig J.H. Mechanical remodeling of the endothelial surface and actin cytoskeleton induced by fluid flow. Microcirculation 1997, 4:439-453.
    • (1997) Microcirculation , vol.4 , pp. 439-453
    • Satcher, R.1    Dewey, C.F.2    Hartwig, J.H.3
  • 12
    • 33644850341 scopus 로고    scopus 로고
    • Endothelial actin cytoskeleton remodeling during mechanostimulation with fluid shear stress
    • Osborn E.A., Rabodzey A., Dewey C.F., Hartwig J.H. Endothelial actin cytoskeleton remodeling during mechanostimulation with fluid shear stress. Am J Physiol Cell Physiol 2006, 290:C444-C452.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Osborn, E.A.1    Rabodzey, A.2    Dewey, C.F.3    Hartwig, J.H.4
  • 13
    • 0036349419 scopus 로고    scopus 로고
    • Eukaryotic cell locomotion depends on the propagation of self-organized reaction-diffusion waves and oscillations of actin filament assembly
    • Vicker M.G. Eukaryotic cell locomotion depends on the propagation of self-organized reaction-diffusion waves and oscillations of actin filament assembly. Exp Cell Res 2002, 275:54-66.
    • (2002) Exp Cell Res , vol.275 , pp. 54-66
    • Vicker, M.G.1
  • 14
    • 0037005987 scopus 로고    scopus 로고
    • F-actin assembly in Dictyostelium cell locomotion and shape oscillations propagates as a self-organized reaction-diffusion wave
    • Vicker M.G. F-actin assembly in Dictyostelium cell locomotion and shape oscillations propagates as a self-organized reaction-diffusion wave. FEBS Lett 2002, 510:5-9.
    • (2002) FEBS Lett , vol.510 , pp. 5-9
    • Vicker, M.G.1
  • 15
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • Mogilner A., Oster G. Cell motility driven by actin polymerization. Biophys J 1996, 71:3030-3045.
    • (1996) Biophys J , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 16
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but under appreciated
    • Ellis R.J. Macromolecular crowding: obvious but under appreciated. Trends Biochem Sci 2001, 26:597-604.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 17
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations
    • Minton A.P. Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J Pharm Sci 2005, 94:1668-1675.
    • (2005) J Pharm Sci , vol.94 , pp. 1668-1675
    • Minton, A.P.1
  • 18
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences
    • Zhou H.X., Rivas G., Minton A.P. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 2008, 37:375-397.
    • (2008) Annu Rev Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 19
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton A.P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Biol Chem 2001, 276:10577-10580.
    • (2001) J Biol Chem , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 20
    • 0026541125 scopus 로고
    • 'Macromolecular crowding' is a primary factor in the organization of the cytoskeleton
    • Cuneo P., Magri E., Verzola A., Grazi E. 'Macromolecular crowding' is a primary factor in the organization of the cytoskeleton. Biochem J 1992, 281(Pt 2):507-512.
    • (1992) Biochem J , vol.281 , Issue.PART 2 , pp. 507-512
    • Cuneo, P.1    Magri, E.2    Verzola, A.3    Grazi, E.4
  • 21
    • 1842579704 scopus 로고    scopus 로고
    • Matrix loading: assembly of extracellular matrix collagen fibrils during embryogenesis
    • Kadler K. Matrix loading: assembly of extracellular matrix collagen fibrils during embryogenesis. Birth Defects Res C Embryo Today 2004, 72:1-11.
    • (2004) Birth Defects Res C Embryo Today , vol.72 , pp. 1-11
    • Kadler, K.1
  • 22
    • 32544452057 scopus 로고    scopus 로고
    • Collagen fibril morphology and organization: implications for force transmission in ligament and tendon
    • Provenzano P.P., Vanderby R. Collagen fibril morphology and organization: implications for force transmission in ligament and tendon. Matrix Biol 2006, 25:71-84.
    • (2006) Matrix Biol , vol.25 , pp. 71-84
    • Provenzano, P.P.1    Vanderby, R.2
  • 23
    • 0014611096 scopus 로고
    • Fine structure of the developing avian cornea
    • Hay E.D., Revel J.P. Fine structure of the developing avian cornea. Monogr Dev Biol 1969, 1:1-144.
    • (1969) Monogr Dev Biol , vol.1 , pp. 1-144
    • Hay, E.D.1    Revel, J.P.2
  • 24
    • 0018633357 scopus 로고
    • Ultrastructural observations on collagen and proteoglycans in the annulus fibrosus of the intervertebral disc
    • Marchini M., Strocchi R., Castellani P.P., Riva R. Ultrastructural observations on collagen and proteoglycans in the annulus fibrosus of the intervertebral disc. Basic Appl Histochem 1979, 23:137-148.
    • (1979) Basic Appl Histochem , vol.23 , pp. 137-148
    • Marchini, M.1    Strocchi, R.2    Castellani, P.P.3    Riva, R.4
  • 25
    • 2942594377 scopus 로고    scopus 로고
    • Theoretical model and experimental results for the nonlinear elastic behavior of human annulus fibrosus
    • Wagner D.R., Lotz J.C. Theoretical model and experimental results for the nonlinear elastic behavior of human annulus fibrosus. J Orthop Res 2004, 22:901-909.
    • (2004) J Orthop Res , vol.22 , pp. 901-909
    • Wagner, D.R.1    Lotz, J.C.2
  • 26
    • 0022470549 scopus 로고
    • Extracellular compartments in tendon morphogenesis: collagen fibril, bundle, and macroaggregate formation
    • Birk D.E., Trelstad R.L. Extracellular compartments in tendon morphogenesis: collagen fibril, bundle, and macroaggregate formation. J Cell Biol 1986, 103:231-240.
    • (1986) J Cell Biol , vol.103 , pp. 231-240
    • Birk, D.E.1    Trelstad, R.L.2
  • 27
    • 0022271435 scopus 로고
    • Fibroblasts create compartments in the extracellular space where collagen polymerizes into fibrils and fibrils associate into bundles
    • Birk D.E., Trelstad R.L. Fibroblasts create compartments in the extracellular space where collagen polymerizes into fibrils and fibrils associate into bundles. Ann N Y Acad Sci 1985, 460:258-266.
    • (1985) Ann N Y Acad Sci , vol.460 , pp. 258-266
    • Birk, D.E.1    Trelstad, R.L.2
  • 28
    • 0021687083 scopus 로고
    • Extracellular compartments in matrix morphogenesis: collagen fibril, bundle, and lamellar formation by corneal fibroblasts
    • Birk D.E., Trelstad R.L. Extracellular compartments in matrix morphogenesis: collagen fibril, bundle, and lamellar formation by corneal fibroblasts. J Cell Biol 1984, 99:2024-2033.
    • (1984) J Cell Biol , vol.99 , pp. 2024-2033
    • Birk, D.E.1    Trelstad, R.L.2
  • 30
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty E.G., Lu Y., Meadows R.S., Shaw M.K., Holmes D.F., Kadler K.E. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J Cell Biol 2004, 165:553-563.
    • (2004) J Cell Biol , vol.165 , pp. 553-563
    • Canty, E.G.1    Lu, Y.2    Meadows, R.S.3    Shaw, M.K.4    Holmes, D.F.5    Kadler, K.E.6
  • 31
    • 33845966742 scopus 로고    scopus 로고
    • Actin filaments are required for fibripositor-mediated collagen fibril alignment in tendon
    • Canty E.G., Starborg T., Lu Y., Humphries S.M., Holmes D.F., Meadows R.S., et al. Actin filaments are required for fibripositor-mediated collagen fibril alignment in tendon. J Biol Chem 2006, 281:38592-38598.
    • (2006) J Biol Chem , vol.281 , pp. 38592-38598
    • Canty, E.G.1    Starborg, T.2    Lu, Y.3    Humphries, S.M.4    Holmes, D.F.5    Meadows, R.S.6
  • 33
    • 0038300772 scopus 로고    scopus 로고
    • Degeneration of the intervertebral disc
    • Urban J.P., Roberts S. Degeneration of the intervertebral disc. Arthritis Res Ther 2003, 5:120-130.
    • (2003) Arthritis Res Ther , vol.5 , pp. 120-130
    • Urban, J.P.1    Roberts, S.2
  • 34
    • 69649102613 scopus 로고    scopus 로고
    • Mechanical strain enhances survivability of collagen micronetworks in the presence of collagenase: implications for load-bearing matrix growth and stability
    • Bhole A.P., Flynn B.P., Liles M., Saeidi N., Dimarzio C.A., Ruberti J.W. Mechanical strain enhances survivability of collagen micronetworks in the presence of collagenase: implications for load-bearing matrix growth and stability. Philos Transact A Math Phys Eng Sci 2009, 367:3339-3362.
    • (2009) Philos Transact A Math Phys Eng Sci , vol.367 , pp. 3339-3362
    • Bhole, A.P.1    Flynn, B.P.2    Liles, M.3    Saeidi, N.4    Dimarzio, C.A.5    Ruberti, J.W.6
  • 35
    • 24644452139 scopus 로고    scopus 로고
    • Strain-controlled enzymatic cleavage of collagen in loaded matrix
    • Ruberti J.W., Hallab N.J. Strain-controlled enzymatic cleavage of collagen in loaded matrix. Biochem Biophys Res Commun 2005, 336:483-489.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 483-489
    • Ruberti, J.W.1    Hallab, N.J.2
  • 36
    • 67651180947 scopus 로고    scopus 로고
    • Deformation-dependent enzyme mechanokinetic cleavage of type I collagen
    • Wyatt K.E., Bourne J.W., Torzilli P.A. Deformation-dependent enzyme mechanokinetic cleavage of type I collagen. J Biomech Eng 2009, 131:051004.
    • (2009) J Biomech Eng , vol.131 , pp. 051004
    • Wyatt, K.E.1    Bourne, J.W.2    Torzilli, P.A.3
  • 37
    • 79952750509 scopus 로고    scopus 로고
    • Molecular mechanochemistry: low force switch slows enzymatic cleavage of human type I collagen monomer
    • Camp R.J., Liles M., Beale J., Saeidi N., Flynn B.P., Moore E., et al. Molecular mechanochemistry: low force switch slows enzymatic cleavage of human type I collagen monomer. J Am Chem Soc 2011, 133:4073-4078.
    • (2011) J Am Chem Soc , vol.133 , pp. 4073-4078
    • Camp, R.J.1    Liles, M.2    Beale, J.3    Saeidi, N.4    Flynn, B.P.5    Moore, E.6
  • 38
    • 77957873845 scopus 로고    scopus 로고
    • Mechanical strain stabilizes reconstituted collagen fibrils against enzymatic degradation by mammalian collagenase matrix metalloproteinase 8 (MMP-8)
    • Flynn B.P., Bhole A.P., Saeidi N., Liles M., Dimarzio C.A., Ruberti J.W. Mechanical strain stabilizes reconstituted collagen fibrils against enzymatic degradation by mammalian collagenase matrix metalloproteinase 8 (MMP-8). PLoS ONE 2010, 5:e12337.
    • (2010) PLoS ONE , vol.5
    • Flynn, B.P.1    Bhole, A.P.2    Saeidi, N.3    Liles, M.4    Dimarzio, C.A.5    Ruberti, J.W.6
  • 39
    • 77956093051 scopus 로고    scopus 로고
    • Probing collagen/enzyme mechanochemistry in native tissue with dynamic, enzyme-induced creep
    • Zareian R., Church K.P., Saeidi N., Flynn B.P., Beale J.W., Ruberti J.W. Probing collagen/enzyme mechanochemistry in native tissue with dynamic, enzyme-induced creep. Langmuir 2010, 26:9917-9926.
    • (2010) Langmuir , vol.26 , pp. 9917-9926
    • Zareian, R.1    Church, K.P.2    Saeidi, N.3    Flynn, B.P.4    Beale, J.W.5    Ruberti, J.W.6
  • 40
    • 0018648051 scopus 로고
    • The synthesis of hyaluronic acid by ectoderm during early organogenesis in the chick embryo
    • Solursh M., Fisher M., Singley C.T. The synthesis of hyaluronic acid by ectoderm during early organogenesis in the chick embryo. Differentiation 1979, 14:77-85.
    • (1979) Differentiation , vol.14 , pp. 77-85
    • Solursh, M.1    Fisher, M.2    Singley, C.T.3
  • 41
    • 0023229488 scopus 로고
    • The synthesis of hyaluronic acid by human synovial fibroblasts is influenced by the nature of the hyaluronate in the extracellular environment
    • Smith M.M., Ghosh P. The synthesis of hyaluronic acid by human synovial fibroblasts is influenced by the nature of the hyaluronate in the extracellular environment. Rheumatol Int 1987, 7:113-122.
    • (1987) Rheumatol Int , vol.7 , pp. 113-122
    • Smith, M.M.1    Ghosh, P.2
  • 42
    • 0015124266 scopus 로고
    • Hyaluronate production and removal during corneal development in the chick
    • Toole B.P., Trelstad R.L. Hyaluronate production and removal during corneal development in the chick. Dev Biol 1971, 26:28-35.
    • (1971) Dev Biol , vol.26 , pp. 28-35
    • Toole, B.P.1    Trelstad, R.L.2
  • 43
    • 35148841944 scopus 로고    scopus 로고
    • Morphologic characterization of organized extracellular matrix deposition by ascorbic acid-stimulated human corneal fibroblasts
    • Guo X., Hutcheon A.E., Melotti S.A., Zieske J.D., Trinkaus-Randall V., Ruberti J.W. Morphologic characterization of organized extracellular matrix deposition by ascorbic acid-stimulated human corneal fibroblasts. Invest Ophthalmol Vis Sci 2007, 48:4050-4060.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 4050-4060
    • Guo, X.1    Hutcheon, A.E.2    Melotti, S.A.3    Zieske, J.D.4    Trinkaus-Randall, V.5    Ruberti, J.W.6
  • 44
    • 49749087995 scopus 로고    scopus 로고
    • Solutions to the problem of substitution of ERL 4221 for vinyl cyclohexene dioxide in spurr low viscosity embedding formulations
    • Ellis E.A. Solutions to the problem of substitution of ERL 4221 for vinyl cyclohexene dioxide in spurr low viscosity embedding formulations. Micros Today 2006, 14:32-33.
    • (2006) Micros Today , vol.14 , pp. 32-33
    • Ellis, E.A.1
  • 45
    • 0842310255 scopus 로고    scopus 로고
    • The organization of collagen in the corneal stroma
    • Meek K.M., Boote C. The organization of collagen in the corneal stroma. Exp Eye Res 2004, 78:503-512.
    • (2004) Exp Eye Res , vol.78 , pp. 503-512
    • Meek, K.M.1    Boote, C.2
  • 46
    • 0024782770 scopus 로고
    • Hierarchical structure of the intervertebral disc
    • Cassidy J.J., Hiltner A., Baer E. Hierarchical structure of the intervertebral disc. Connect Tissue Res 1989, 23:75-88.
    • (1989) Connect Tissue Res , vol.23 , pp. 75-88
    • Cassidy, J.J.1    Hiltner, A.2    Baer, E.3
  • 47
    • 33748316797 scopus 로고    scopus 로고
    • Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea
    • Chakravarti S., Zhang G., Chervoneva I., Roberts L., Birk D.E. Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea. Dev Dyn 2006, 235:2493-2506.
    • (2006) Dev Dyn , vol.235 , pp. 2493-2506
    • Chakravarti, S.1    Zhang, G.2    Chervoneva, I.3    Roberts, L.4    Birk, D.E.5
  • 49
    • 0033779690 scopus 로고    scopus 로고
    • Corneal opacity in lumican-null mice: defects in collagen fibril structure and packing in the posterior stroma
    • Chakravarti S., Petroll W.M., Hassell J.R., Jester J.V., Lass J.H., Paul J., et al. Corneal opacity in lumican-null mice: defects in collagen fibril structure and packing in the posterior stroma. Invest Ophthalmol Vis Sci 2000, 41:3365-3373.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 3365-3373
    • Chakravarti, S.1    Petroll, W.M.2    Hassell, J.R.3    Jester, J.V.4    Lass, J.H.5    Paul, J.6
  • 50
    • 84971301149 scopus 로고
    • The effects of shape on the interaction of colloidal particles
    • Onsager L. The effects of shape on the interaction of colloidal particles. Ann N Y Acad Sci 1949, 51:627-659.
    • (1949) Ann N Y Acad Sci , vol.51 , pp. 627-659
    • Onsager, L.1
  • 51
    • 0027235856 scopus 로고
    • Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles
    • Madden T.L., Herzfeld J. Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles. Biophys J 1993, 65:1147-1154.
    • (1993) Biophys J , vol.65 , pp. 1147-1154
    • Madden, T.L.1    Herzfeld, J.2
  • 52
    • 4544297320 scopus 로고    scopus 로고
    • Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points
    • Herzfeld J. Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points. J Mol Recognit 2004, 17:376-381.
    • (2004) J Mol Recognit , vol.17 , pp. 376-381
    • Herzfeld, J.1
  • 53
    • 0024462019 scopus 로고
    • Liquid crystalline phases of sonicated type I collagen
    • Giraud-Guille M.M. Liquid crystalline phases of sonicated type I collagen. Biol Cell 1989, 67:97-101.
    • (1989) Biol Cell , vol.67 , pp. 97-101
    • Giraud-Guille, M.M.1
  • 56
    • 0025288016 scopus 로고
    • The comparative chemical morphology of the mammalian cornea
    • Scott J.E., Bosworth T.R. The comparative chemical morphology of the mammalian cornea. Basic Appl Histochem 1990, 34:35-42.
    • (1990) Basic Appl Histochem , vol.34 , pp. 35-42
    • Scott, J.E.1    Bosworth, T.R.2
  • 57
    • 0025075184 scopus 로고
    • A comparative biochemical and ultrastructural study of proteoglycan-collagen interactions in corneal stroma. Functional and metabolic implications
    • Scott J.E., Bosworth T.R. A comparative biochemical and ultrastructural study of proteoglycan-collagen interactions in corneal stroma. Functional and metabolic implications. Biochem J 1990, 270:491-497.
    • (1990) Biochem J , vol.270 , pp. 491-497
    • Scott, J.E.1    Bosworth, T.R.2
  • 58
    • 0025214344 scopus 로고
    • Proteoglycan:collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues
    • Scott J.E. Proteoglycan:collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues. J Anat 1990, 169:23-35.
    • (1990) J Anat , vol.169 , pp. 23-35
    • Scott, J.E.1
  • 59
    • 78651170957 scopus 로고
    • Biosynthesis of collagen and non-collagen protein during development of the chick cornea
    • Coleman J.R., Herrmann H., Bess B. Biosynthesis of collagen and non-collagen protein during development of the chick cornea. J Cell Biol 1965, 25:69-78.
    • (1965) J Cell Biol , vol.25 , pp. 69-78
    • Coleman, J.R.1    Herrmann, H.2    Bess, B.3
  • 60
    • 0013771903 scopus 로고
    • Problems in corneal morphogenesis
    • Coulombre A. Problems in corneal morphogenesis. Adv Morphog 1965, 4:81-109.
    • (1965) Adv Morphog , vol.4 , pp. 81-109
    • Coulombre, A.1
  • 61
    • 0020164349 scopus 로고
    • The bilaterally asymmetrical architecture of the submammalian corneal stroma resembles a cholesteric liquid crystal
    • Trelstad R.L. The bilaterally asymmetrical architecture of the submammalian corneal stroma resembles a cholesteric liquid crystal. Dev Biol 1982, 92:133-134.
    • (1982) Dev Biol , vol.92 , pp. 133-134
    • Trelstad, R.L.1
  • 62
    • 0036447070 scopus 로고    scopus 로고
    • Building collagen molecules, fibrils, and suprafibrillar structures
    • Hulmes D.J. Building collagen molecules, fibrils, and suprafibrillar structures. J Struct Biol 2002, 137:2-10.
    • (2002) J Struct Biol , vol.137 , pp. 2-10
    • Hulmes, D.J.1
  • 63
    • 70349944038 scopus 로고    scopus 로고
    • Dynamic shear-influenced collagen self-assembly
    • Saeidi N., Sander E.A., Ruberti J.W. Dynamic shear-influenced collagen self-assembly. Biomaterials 2009, 30:6581-6592.
    • (2009) Biomaterials , vol.30 , pp. 6581-6592
    • Saeidi, N.1    Sander, E.A.2    Ruberti, J.W.3
  • 64
    • 79955591923 scopus 로고    scopus 로고
    • Production of highly aligned collagen lamellae by combining shear force and thin film confinement
    • Saeidi N., Sander E.A., Zareian R., Ruberti J.W. Production of highly aligned collagen lamellae by combining shear force and thin film confinement. Acta Biomater 2011, 7:2437-2447.
    • (2011) Acta Biomater , vol.7 , pp. 2437-2447
    • Saeidi, N.1    Sander, E.A.2    Zareian, R.3    Ruberti, J.W.4
  • 65
    • 85027942825 scopus 로고    scopus 로고
    • Disorganized collagen scaffold interferes with fibroblast mediated deposition of organized extracellular matrix in vitro
    • Saeidi N., Guo X., Hutcheon A.E., Sander E.A., Bale S.S., Melotti S.A., et al. Disorganized collagen scaffold interferes with fibroblast mediated deposition of organized extracellular matrix in vitro. Biotechnol Bioeng 2012, http://dx.doi.org/10.1002/bit.24533.
    • (2012) Biotechnol Bioeng
    • Saeidi, N.1    Guo, X.2    Hutcheon, A.E.3    Sander, E.A.4    Bale, S.S.5    Melotti, S.A.6
  • 66
    • 0015020484 scopus 로고
    • Vacuoles in the embryonic chick corneal epithelium, an epithelium which produces collagen
    • Trelstad R.L. Vacuoles in the embryonic chick corneal epithelium, an epithelium which produces collagen. J Cell Biol 1971, 48:689.
    • (1971) J Cell Biol , vol.48 , pp. 689
    • Trelstad, R.L.1


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