메뉴 건너뛰기




Volumn 36, Issue 10, 2003, Pages 1529-1553

Collagen self-assembly and the development of tendon mechanical properties

Author keywords

[No Author keywords available]

Indexed keywords

BIOMEDICAL ENGINEERING; CELLS; COLLAGEN; ELASTICITY; SELF ASSEMBLY; STRENGTH OF MATERIALS; TENDONS;

EID: 0141453852     PISSN: 00219290     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0021-9290(03)00135-0     Document Type: Article
Times cited : (479)

References (130)
  • 2
    • 77957209794 scopus 로고
    • Elastic energy stores in running vertebrates
    • Alexander R.M. Elastic energy stores in running vertebrates. Acta Zoologica. 24:1984;85-94.
    • (1984) Acta Zoologica , vol.24 , pp. 85-94
    • Alexander, R.M.1
  • 3
    • 84966163623 scopus 로고
    • Targeted mutation in the col5α2 gene reveals a regulatory role for type V collagen during matrix assembly
    • Andrikopoulos K., Liu X., Keene D.R., Jaenisch R., Ramirez F. Targeted mutation in the col5α2 gene reveals a regulatory role for type V collagen during matrix assembly. Nature Genetics. 9:1995;31-36.
    • (1995) Nature Genetics , vol.9 , pp. 31-36
    • Andrikopoulos, K.1    Liu, X.2    Keene, D.R.3    Jaenisch, R.4    Ramirez, F.5
  • 4
    • 0005332625 scopus 로고
    • Fiber formation from solutions of collagen. II. The role of tyrosyl residues
    • Bensusan H.B., Scanu A.J. Fiber formation from solutions of collagen. II. The role of tyrosyl residues. Journal of American Chemical Society. 82:1960;4990-4998.
    • (1960) Journal of American Chemical Society , vol.82 , pp. 4990-4998
    • Bensusan, H.B.1    Scanu, A.J.2
  • 5
    • 0022648763 scopus 로고
    • Physical characterization of type I procollagen in solution: Evidence that the propeptides limit self-assembly
    • Berg R.A., Birk D.E., Silver F.H. Physical characterization of type I procollagen in solution. evidence that the propeptides limit self-assembly International Journal of Biological Macromolecules. 8:1986;177-182.
    • (1986) International Journal of Biological Macromolecules , vol.8 , pp. 177-182
    • Berg, R.A.1    Birk, D.E.2    Silver, F.H.3
  • 6
    • 0017885882 scopus 로고
    • Intermolecular interactions studies on native and enzyme-treated acid-soluble collagen
    • Bernengo J.C., Herbage D., Marion C., Roux B. Intermolecular interactions studies on native and enzyme-treated acid-soluble collagen. Biochimica Biophysica Acta. 532:1978;305-314.
    • (1978) Biochimica Biophysica Acta , vol.532 , pp. 305-314
    • Bernengo, J.C.1    Herbage, D.2    Marion, C.3    Roux, B.4
  • 9
    • 0023873382 scopus 로고
    • Collagen type I and type V are present in the same fibril in the avian corneal stroma
    • Birk D.E., Fitch J.M., Babiarz J.P., Linsenmayer T.F. Collagen type I and type V are present in the same fibril in the avian corneal stroma. Journal of Cell Biology. 106:1988;999-1008.
    • (1988) Journal of Cell Biology , vol.106 , pp. 999-1008
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.P.3    Linsenmayer, T.F.4
  • 13
    • 0028923480 scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments undergo post-depositional modifications resulting in linear and lateral growth during matrix development
    • Birk D.E., Nurminskaya M.V., Zycband E.I. Collagen fibrillogenesis in situ. fibril segments undergo post-depositional modifications resulting in linear and lateral growth during matrix development Development Dynamics. 202:1995;229-243.
    • (1995) Development Dynamics , vol.202 , pp. 229-243
    • Birk, D.E.1    Nurminskaya, M.V.2    Zycband, E.I.3
  • 14
    • 0031042279 scopus 로고    scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures
    • Birk D.E., Zycband E.I., Woodruff S., Winkelmann D.A., Trelstad R.L. Collagen fibrillogenesis in situ. fibril segments become long fibrils as the developing tendon matures Developmental Dynamics. 208:1997;291-298.
    • (1997) Developmental Dynamics , vol.208 , pp. 291-298
    • Birk, D.E.1    Zycband, E.I.2    Woodruff, S.3    Winkelmann, D.A.4    Trelstad, R.L.5
  • 15
    • 0033954677 scopus 로고    scopus 로고
    • Mechanical strain increases type I collagen expression in pulmonary fibroblasts in vitro
    • Breen E.C. Mechanical strain increases type I collagen expression in pulmonary fibroblasts in vitro. Journal of Applied Physiology. 88:2000;203-209.
    • (2000) Journal of Applied Physiology , vol.88 , pp. 203-209
    • Breen, E.C.1
  • 16
    • 0031969588 scopus 로고    scopus 로고
    • Tensional homeostatis in dermal fibroblasts: Mechanical responses to mechanical loading in three-dimensional substrates
    • Brown R.A., Prajapati R., McGrouther D.A., Yananas I.V., Eastwood M. Tensional homeostatis in dermal fibroblasts. mechanical responses to mechanical loading in three-dimensional substrates Journal of Cell Physiology. 175:1998;323-332.
    • (1998) Journal of Cell Physiology , vol.175 , pp. 323-332
    • Brown, R.A.1    Prajapati, R.2    McGrouther, D.A.3    Yananas, I.V.4    Eastwood, M.5
  • 18
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: Skin fragility and corneal opacity in the absence of lumican
    • Chakravarti S., Magnuson T., Lass J.H., Jepsen K.J., LaMantia C., Carroll H. Lumican regulates collagen fibril assembly. skin fragility and corneal opacity in the absence of lumican Journal of Cell Biology. 141:1998;1277-1286.
    • (1998) Journal of Cell Biology , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnuson, T.2    Lass, J.H.3    Jepsen, K.J.4    LaMantia, C.5    Carroll, H.6
  • 19
    • 0032730185 scopus 로고    scopus 로고
    • Regulation of extracellular matrix gene expression by mechanical stress
    • Chiquet M. Regulation of extracellular matrix gene expression by mechanical stress. Matrix Biology. 18:1999;417-425.
    • (1999) Matrix Biology , vol.18 , pp. 417-425
    • Chiquet, M.1
  • 20
    • 0033813556 scopus 로고    scopus 로고
    • Assembly of type I collagen: Fusion of fibril subunits and the influence of fibril diameter on mechanical properties
    • Christiansen D.L., Huang E.K., Silver F.H. Assembly of type I collagen. fusion of fibril subunits and the influence of fibril diameter on mechanical properties Matrix Biology. 19:2000;409-420.
    • (2000) Matrix Biology , vol.19 , pp. 409-420
    • Christiansen, D.L.1    Huang, E.K.2    Silver, F.H.3
  • 21
    • 0017672081 scopus 로고
    • Characterization of nuclei in in vitro collagen fibril formation
    • Comper W.D., Veis A. Characterization of nuclei in in vitro collagen fibril formation. Biopolymers. 16:1977;2133-2142.
    • (1977) Biopolymers , vol.16 , pp. 2133-2142
    • Comper, W.D.1    Veis, A.2
  • 22
    • 0014824074 scopus 로고
    • Thermodynamic studies of the assembly in vitro of native collagen fibrils
    • Cooper A. Thermodynamic studies of the assembly in vitro of native collagen fibrils. Biochemical Journal. 118:1970;355-365.
    • (1970) Biochemical Journal , vol.118 , pp. 355-365
    • Cooper, A.1
  • 23
    • 0028892860 scopus 로고
    • Tendon response to tensile stress: An ultrastructural investigation of collagen: Proteoglycan interactions in stressed tendon
    • Cribb A.M., Scott J.E. Tendon response to tensile stress. an ultrastructural investigation of collagen: proteoglycan interactions in stressed tendon Journal of Anatomy. 187:1995;423-428.
    • (1995) Journal of Anatomy , vol.187 , pp. 423-428
    • Cribb, A.M.1    Scott, J.E.2
  • 24
    • 0019503132 scopus 로고
    • Mechanical properties of reconstituted collagen fibrils: A study on reconstitution methodology and influence of in vitro maturation
    • Danielsen C.D. Mechanical properties of reconstituted collagen fibrils. a study on reconstitution methodology and influence of in vitro maturation Connective Tissue Research. 9:1981;51-57.
    • (1981) Connective Tissue Research , vol.9 , pp. 51-57
    • Danielsen, C.D.1
  • 28
    • 0031956985 scopus 로고    scopus 로고
    • Effect of precise mechanical loading on fibroblast populated collagen lattices: Morphological changes
    • Eastwood M., Mudera V.C., McGrouther D.A., Brown R.A. Effect of precise mechanical loading on fibroblast populated collagen lattices. morphological changes Cell Motility and the Cytoskeleton. 40:1998;13-21.
    • (1998) Cell Motility and the Cytoskeleton , vol.40 , pp. 13-21
    • Eastwood, M.1    Mudera, V.C.2    McGrouther, D.A.3    Brown, R.A.4
  • 30
    • 78651192479 scopus 로고
    • Structure and function of mammalian tendon
    • Elliott D.H. Structure and function of mammalian tendon. Biological Reviews. 40:1965;342-392.
    • (1965) Biological Reviews , vol.40 , pp. 342-392
    • Elliott, D.H.1
  • 31
    • 0030865343 scopus 로고    scopus 로고
    • Versatile collagens in invertebrates
    • Engle J. Versatile collagens in invertebrates. Science. 277:1997;1785-1786.
    • (1997) Science , vol.277 , pp. 1785-1786
    • Engle, J.1
  • 32
    • 0025904728 scopus 로고
    • The zipper-like folding of collagen triple-helices and the effects of mutations that disrupt the zipper
    • Engle J., Prockop D.J. The zipper-like folding of collagen triple-helices and the effects of mutations that disrupt the zipper. Annual Review of Biophysics and Chemistry. 20:1991;137-152.
    • (1991) Annual Review of Biophysics and Chemistry , vol.20 , pp. 137-152
    • Engle, J.1    Prockop, D.J.2
  • 33
    • 0013940719 scopus 로고    scopus 로고
    • Apatite-collagen organization in calcified tendon
    • Engstrom A. Apatite-collagen organization in calcified tendon. Experimental Cell Research. 43:1996;241-245.
    • (1996) Experimental Cell Research , vol.43 , pp. 241-245
    • Engstrom, A.1
  • 38
    • 0023100964 scopus 로고
    • Amino and carboxylpropeptides in bone collagen fibrils during embryogenesis
    • Fleischmajer R., Perlish J.S., Olsen B.R. Amino and carboxylpropeptides in bone collagen fibrils during embryogenesis. Cell Tissue Research. 247:1987;105-109.
    • (1987) Cell Tissue Research , vol.247 , pp. 105-109
    • Fleischmajer, R.1    Perlish, J.S.2    Olsen, B.R.3
  • 41
    • 0017145522 scopus 로고
    • Dynamic light scattering from collagen solutions. I. Translational diffusion coefficient and aggregation effects
    • Fletcher G.C. Dynamic light scattering from collagen solutions. I. Translational diffusion coefficient and aggregation effects. Biopolymers. 15:1976;2201-2217.
    • (1976) Biopolymers , vol.15 , pp. 2201-2217
    • Fletcher, G.C.1
  • 42
    • 0028937108 scopus 로고
    • Sequential assembly of collagen revealed by atomic force microscopy
    • Gale M., Pollanen M.S., Markiewicz P., Goh M.C. Sequential assembly of collagen revealed by atomic force microscopy. Biophysical Journal. 68:1995;2124-2128.
    • (1995) Biophysical Journal , vol.68 , pp. 2124-2128
    • Gale, M.1    Pollanen, M.S.2    Markiewicz, P.3    Goh, M.C.4
  • 43
    • 0034723148 scopus 로고    scopus 로고
    • Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction
    • Graham H.K., Holmes D.F., Watson R.B., Kadler K.E. Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction. Journal of Molecular Biology. 295:2000;891-902.
    • (2000) Journal of Molecular Biology , vol.295 , pp. 891-902
    • Graham, H.K.1    Holmes, D.F.2    Watson, R.B.3    Kadler, K.E.4
  • 45
    • 0017904573 scopus 로고
    • Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system. A correlated interference-reflection and high-voltage electron-microscope study
    • Heath J.P., Dunn G.A. Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system. A correlated interference-reflection and high-voltage electron-microscope study. Journal of Cell Science. 29:1978;197-212.
    • (1978) Journal of Cell Science , vol.29 , pp. 197-212
    • Heath, J.P.1    Dunn, G.A.2
  • 46
    • 0021770213 scopus 로고
    • Localization of flexible sites in thread-like molecules from electron micrographs: Comparison of interstitial, basement membrane and intima collagens
    • Hofmann H., Voss T., Kuhn K., Engle J. Localization of flexible sites in thread-like molecules from electron micrographs. comparison of interstitial, basement membrane and intima collagens Journal of Molecular Biology. 172:1984;325-343.
    • (1984) Journal of Molecular Biology , vol.172 , pp. 325-343
    • Hofmann, H.1    Voss, T.2    Kuhn, K.3    Engle, J.4
  • 47
    • 0025781849 scopus 로고
    • Morphology of sheet-like assemblies of pN-collagen, pC-collagen and procollagen studied by scanning electron microscopy mass measurements
    • Holmes D.F., Mould A.P., Chapman J.A. Morphology of sheet-like assemblies of pN-collagen, pC-collagen and procollagen studied by scanning electron microscopy mass measurements. Journal of Molecular Biology. 220:1991;111-123.
    • (1991) Journal of Molecular Biology , vol.220 , pp. 111-123
    • Holmes, D.F.1    Mould, A.P.2    Chapman, J.A.3
  • 48
    • 0028158454 scopus 로고
    • Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity
    • Holmes D.F., Lowe M.P., Chapman J.A. Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity. Journal of Molecular Biology. 235:1994;80-83.
    • (1994) Journal of Molecular Biology , vol.235 , pp. 80-83
    • Holmes, D.F.1    Lowe, M.P.2    Chapman, J.A.3
  • 49
    • 0032515195 scopus 로고    scopus 로고
    • Collagen fibrils forming in developing tendon show an early and abrupt limitation in diameter at the growing tips
    • Holmes D.F., Graham H.K., Kadler K.E. Collagen fibrils forming in developing tendon show an early and abrupt limitation in diameter at the growing tips. Journal of Molecular Biology. 283:1998;1049-1058.
    • (1998) Journal of Molecular Biology , vol.283 , pp. 1049-1058
    • Holmes, D.F.1    Graham, H.K.2    Kadler, K.E.3
  • 51
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins. versatility, modulation, and signaling in cell adhesion Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 52
    • 0026245524 scopus 로고
    • Integrins as mechanochemical transducers
    • Ingber D. Integrins as mechanochemical transducers. Current Opinion in Cell Biology. 3:1991;841-848.
    • (1991) Current Opinion in Cell Biology , vol.3 , pp. 841-848
    • Ingber, D.1
  • 53
    • 0032952039 scopus 로고    scopus 로고
    • How cells (might) sense microgravity
    • Ingber D. How cells (might) sense microgravity. The FASEB Journal. 13:1999;S3-S15.
    • (1999) The FASEB Journal , vol.13
    • Ingber, D.1
  • 54
    • 0030010512 scopus 로고    scopus 로고
    • Proteogylcans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo R.V., Murdoch A.D. Proteogylcans of the extracellular environment. clues from the gene and protein side offer novel perspectives in molecular diversity and function FASEB Journal. 10:1996;598-614.
    • (1996) FASEB Journal , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 55
    • 0141745523 scopus 로고
    • Isolation and properties of a collagen soluble in salt solution at neutral pH
    • Jackson D.S., Fessler J.H. Isolation and properties of a collagen soluble in salt solution at neutral pH. Nature. 176:1955;68-70.
    • (1955) Nature , vol.176 , pp. 68-70
    • Jackson, D.S.1    Fessler, J.H.2
  • 56
    • 0023656926 scopus 로고
    • Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process
    • Kadler K.E., Hojima Y., Prockop D.J. Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process. Journal of Biological Chemistry. 262:1987;15696-15701.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 15696-15701
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 57
    • 0025358337 scopus 로고
    • Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction
    • Kadler K.E., Hojima Y., Prockop D.J. Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction. Biochemical Journal. 268:1990;339-343.
    • (1990) Biochemical Journal , vol.268 , pp. 339-343
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 58
    • 0025316412 scopus 로고
    • Assembly of type I collagen fibrils de novo by specific enzymatic cleavage of pC-collagen. The fibrils former at about 37°C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue
    • Kadler K.E., Hulmes D.J.S., Hojima Y., Prockop D.J. Assembly of type I collagen fibrils de novo by specific enzymatic cleavage of pC-collagen. The fibrils former at about 37°C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue. Annales of the New York Academy of Sciences. 580:1990;214-224.
    • (1990) Annales of the New York Academy of Sciences , vol.580 , pp. 214-224
    • Kadler, K.E.1    Hulmes, D.J.S.2    Hojima, Y.3    Prockop, D.J.4
  • 60
    • 0029179636 scopus 로고
    • Temporal and spatial expressions of type XII collagen in the remodeling periodontal ligament during experimental tooth movement
    • Karimbux N.Y., Nishimura I. Temporal and spatial expressions of type XII collagen in the remodeling periodontal ligament during experimental tooth movement. Journal of Dental Research. 73:1995;313-318.
    • (1995) Journal of Dental Research , vol.73 , pp. 313-318
    • Karimbux, N.Y.1    Nishimura, I.2
  • 61
    • 0024571494 scopus 로고
    • Mechanical properties of collagen fibers: A comparison of reconstituted and rat tail tendon fibers
    • Kato Y.P., Christiansen D.L., Hahn R.A., Sheih S.J., Goldstein J., Silver F.H. Mechanical properties of collagen fibers. a comparison of reconstituted and rat tail tendon fibers Biomaterials. 10:1989;38-42.
    • (1989) Biomaterials , vol.10 , pp. 38-42
    • Kato, Y.P.1    Christiansen, D.L.2    Hahn, R.A.3    Sheih, S.J.4    Goldstein, J.5    Silver, F.H.6
  • 64
    • 0028982830 scopus 로고
    • Nuclear factor-κB interacts functionally with the platelet-derived growth-B chain shear-stress response element in vascular endothelial cells exposed to shear stress
    • Khachigian L.M., Resnick N., Gimbrone M.A. Jr., Tucker C. Nuclear factor-κB interacts functionally with the platelet-derived growth-B chain shear-stress response element in vascular endothelial cells exposed to shear stress. Journal of Clinical Investigation. 96:1995;1169-1175.
    • (1995) Journal of Clinical Investigation , vol.96 , pp. 1169-1175
    • Khachigian, L.M.1    Resnick, N.2    Gimbrone M.A., Jr.3    Tucker, C.4
  • 65
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrains α1β1 and α2β1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • Knight C.G., Morton L.F., Peachey A.R., Tuckwell D.S., Farndale R.W., Barnes M.J. The collagen-binding A-domains of integrains α1β1 and α2β1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. Journal of Biological Chemistry. 275:2000;35-40.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 66
    • 0021885077 scopus 로고
    • Electron microscopic demonstration of acid-labile, 4D-staggered intermolecular association of collagen formed in vitro
    • Kobayashi K., Ito T., Hoshino T. Electron microscopic demonstration of acid-labile, 4D-staggered intermolecular association of collagen formed in vitro. Collagen and Related Research. 5:1985;253-260.
    • (1985) Collagen and Related Research , vol.5 , pp. 253-260
    • Kobayashi, K.1    Ito, T.2    Hoshino, T.3
  • 69
    • 0029070878 scopus 로고
    • A study of the relationship between mineral content and mechanical properties of turkey gastrocnemius tendon
    • Landis W.J., LiBrizzi J.J., Dunn M.G., Silver F.H. A study of the relationship between mineral content and mechanical properties of turkey gastrocnemius tendon. Journal of Bone and Mineral Research. 10:1995;859-867.
    • (1995) Journal of Bone and Mineral Research , vol.10 , pp. 859-867
    • Landis, W.J.1    LiBrizzi, J.J.2    Dunn, M.G.3    Silver, F.H.4
  • 70
    • 0029585289 scopus 로고
    • Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins
    • Langholz O., Rockel D., Mauch C., Kozlowska E., Bank I., Krieg T. Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins. Journal of Cell Biology. 131:1995;1903-1915.
    • (1995) Journal of Cell Biology , vol.131 , pp. 1903-1915
    • Langholz, O.1    Rockel, D.2    Mauch, C.3    Kozlowska, E.4    Bank, I.5    Krieg, T.6
  • 71
    • 0028967611 scopus 로고
    • Temperature-favored assembly of collagen is driven by hydrophilic not hydrophobic interactions
    • Leiken S., Rau D.C., Parsegian V.A. Temperature-favored assembly of collagen is driven by hydrophilic not hydrophobic interactions. Structural Biology. 2:1995;205-210.
    • (1995) Structural Biology , vol.2 , pp. 205-210
    • Leiken, S.1    Rau, D.C.2    Parsegian, V.A.3
  • 72
    • 0015219009 scopus 로고
    • Collagen made of extended α-chains procollagen in genetically defective dermatosparactic calves
    • Lenaers A., Ansay M., Nusgens B.V., Lapiere C.M. Collagen made of extended α-chains procollagen in genetically defective dermatosparactic calves. European Journal of Biochemistry. 23:1971;533-543.
    • (1971) European Journal of Biochemistry , vol.23 , pp. 533-543
    • Lenaers, A.1    Ansay, M.2    Nusgens, B.V.3    Lapiere, C.M.4
  • 74
    • 0141745524 scopus 로고
    • M.S. Thesis in Physiology, Rutgers University
    • McBridge, D.J., 1984. Hind limb extensor tendon development in the chick: a light and transmission electron microscopic study. M.S. Thesis in Physiology, Rutgers University.
    • (1984)
    • McBridge, D.J.1
  • 75
    • 0022002448 scopus 로고
    • Morphological characterization of tendon development during chick embryogenesis: Measurement of birefringence retardation
    • McBridge D.J., Hahn R., Silver F.H. Morphological characterization of tendon development during chick embryogenesis. measurement of birefringence retardation International Journal of Biological Macromolecules. 7:1985;71-76.
    • (1985) International Journal of Biological Macromolecules , vol.7 , pp. 71-76
    • McBridge, D.J.1    Hahn, R.2    Silver, F.H.3
  • 77
    • 0016775402 scopus 로고
    • Do mineral crystals stiffen bone by straitjacketing its collagen?
    • McCutchen C.W. Do mineral crystals stiffen bone by straitjacketing its collagen? Journal of Theoretical Biology. 51:1975;51-58.
    • (1975) Journal of Theoretical Biology , vol.51 , pp. 51-58
    • McCutchen, C.W.1
  • 78
    • 0023657733 scopus 로고
    • Locus of a histidine-based, stable trifunctional, helix to helix collagen crosslink: Stereospecific collagen structure of type I skin fibrils
    • Mechanic G.L., Katz E.P., Henmi M., Noyes C., Yamauchi M. Locus of a histidine-based, stable trifunctional, helix to helix collagen crosslink. stereospecific collagen structure of type I skin fibrils Biochemistry. 26:1987;3500-3509.
    • (1987) Biochemistry , vol.26 , pp. 3500-3509
    • Mechanic, G.L.1    Katz, E.P.2    Henmi, M.3    Noyes, C.4    Yamauchi, M.5
  • 79
    • 0030839967 scopus 로고
    • Collagen from the Osteogenesis Imperfecta mouse model (oim) shows reduced resistance against tensile stress
    • Misof K., Landis W.J., Klaushofer K., Fratzl P. Collagen from the Osteogenesis Imperfecta mouse model (oim) shows reduced resistance against tensile stress. Journal of Clinical Investigation. 100:1977;40-45.
    • (1977) Journal of Clinical Investigation , vol.100 , pp. 40-45
    • Misof, K.1    Landis, W.J.2    Klaushofer, K.3    Fratzl, P.4
  • 80
    • 0020402498 scopus 로고
    • Formation of collagen fibrils in vitro by cleavage of procollagen with procollagen proteinases
    • Miyahara M., Njieha F.K., Prockop D.J. Formation of collagen fibrils in vitro by cleavage of procollagen with procollagen proteinases. Journal of Biological Chemistry. 257:1982;8442-8448.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 8442-8448
    • Miyahara, M.1    Njieha, F.K.2    Prockop, D.J.3
  • 85
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes C.D., Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 86
    • 0002596706 scopus 로고
    • Mineralization of turkey leg tendon. II. Collagen-mineral relations revealed by electron and X-ray microscopy
    • Sognnaes, R.F. (Ed.). American Academy of Advanced Science, Washington
    • Nylen, M.U., Scott, D.B., Mosley, V.M., 1960. Mineralization of turkey leg tendon. II. Collagen-mineral relations revealed by electron and X-ray microscopy. In: Sognnaes, R.F. (Ed.), Calcification of Biological Systems. American Academy of Advanced Science, Washington, pp. 129-142.
    • (1960) Calcification of Biological Systems , pp. 129-142
    • Nylen, M.U.1    Scott, D.B.2    Mosley, V.M.3
  • 87
    • 0015299229 scopus 로고
    • Non-aggregated tropocollagen at physiological pH and ionic strength: A chemical and physiochemical characterization of tropcollagen isolated from the skin of lathrytic rats
    • Obrink B. Non-aggregated tropocollagen at physiological pH and ionic strength. a chemical and physiochemical characterization of tropcollagen isolated from the skin of lathrytic rats European Journal of Biochemistry. 25:1972;563-572.
    • (1972) European Journal of Biochemistry , vol.25 , pp. 563-572
    • Obrink, B.1
  • 88
    • 0029016973 scopus 로고
    • The energy of formation of internal loops in triple-helical collagen polypeptides
    • Paterlini M.G., Nemethy G., Scheraga H.A. The energy of formation of internal loops in triple-helical collagen polypeptides. Biopolymers. 35:1995;607-619.
    • (1995) Biopolymers , vol.35 , pp. 607-619
    • Paterlini, M.G.1    Nemethy, G.2    Scheraga, H.A.3
  • 89
    • 0030875449 scopus 로고    scopus 로고
    • Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
    • Pins G.D., Christiansen D.L., Patel R., Silver F.H. Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophysical Journal. 73:1997;2164-2172.
    • (1997) Biophysical Journal , vol.73 , pp. 2164-2172
    • Pins, G.D.1    Christiansen, D.L.2    Patel, R.3    Silver, F.H.4
  • 92
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism
    • Riveline D., Zamir E., Balaban N.O., Schwarz U.S., Ishizaki T., Narumiya S., Kam Z., Geiger B., Bershadsky A.D. Focal contacts as mechanosensors. externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism Journal of Cell Biology. 153:2001;1175-1186.
    • (2001) Journal of Cell Biology , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.O.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 93
    • 0031016676 scopus 로고    scopus 로고
    • Muscular force in running turkeys: The economy of minimizing work
    • Roberts T.J., Marsh R.L., Weyand P.G., Taylor C.R. Muscular force in running turkeys. the economy of minimizing work Science. 275:1997;113-115.
    • (1997) Science , vol.275 , pp. 113-115
    • Roberts, T.J.1    Marsh, R.L.2    Weyand, P.G.3    Taylor, C.R.4
  • 94
    • 0024024153 scopus 로고
    • Retention of carboxypropeptides in type-II collagen fibrils in chick embryo chondrocyte cultures
    • Ruggerio F., Pfaffle M., von der Mark K., Garrone R. Retention of carboxypropeptides in type-II collagen fibrils in chick embryo chondrocyte cultures. Cell Tissue Research. 252:1988;619-624.
    • (1988) Cell Tissue Research , vol.252 , pp. 619-624
    • Ruggerio, F.1    Pfaffle, M.2    Von der Mark, K.3    Garrone, R.4
  • 95
    • 0030246115 scopus 로고    scopus 로고
    • Elongation mechanism of collagen fibrils and force-strain relationships of tendon at each level of structural hierarchy
    • Sasakai N., Odajima S. Elongation mechanism of collagen fibrils and force-strain relationships of tendon at each level of structural hierarchy. Journal of Biomechanics. 9:1996;1131-1136.
    • (1996) Journal of Biomechanics , vol.9 , pp. 1131-1136
    • Sasakai, N.1    Odajima, S.2
  • 96
    • 0030152813 scopus 로고    scopus 로고
    • Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique
    • Sasakai N., Odajima S. Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique. Journal of Biomechanics. 29:1996;655-658.
    • (1996) Journal of Biomechanics , vol.29 , pp. 655-658
    • Sasakai, N.1    Odajima, S.2
  • 98
    • 0027769736 scopus 로고
    • The nomenclature of glycosaminoglycans and proteoglycans
    • Scott J.E. The nomenclature of glycosaminoglycans and proteoglycans. Glycoconjugate Journal. 10:1993;419-421.
    • (1993) Glycoconjugate Journal , vol.10 , pp. 419-421
    • Scott, J.E.1
  • 99
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumincan/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen
    • Scott J.E. Proteodermatan and proteokeratan sulfate (decorin, lumincan/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry. 35:1996;8787-8795.
    • (1996) Biochemistry , vol.35 , pp. 8787-8795
    • Scott, J.E.1
  • 100
    • 0019490438 scopus 로고
    • Dermatan sulfate-rich proteoglycan associates with rat tail tendon collagen at the d band in the gap region
    • Scott J.E., Orford C.R. Dermatan sulfate-rich proteoglycan associates with rat tail tendon collagen at the d band in the gap region. Biochemical Journal. 197:1981;213-216.
    • (1981) Biochemical Journal , vol.197 , pp. 213-216
    • Scott, J.E.1    Orford, C.R.2
  • 101
    • 0019862889 scopus 로고
    • Proteoglycan-collagen arrangements in developing rat tail tendon: An electron microscopical and biochemical investigation
    • Scott J.E., Orford C.R., Hughes E.W. Proteoglycan-collagen arrangements in developing rat tail tendon. an electron microscopical and biochemical investigation Biochemical Journal. 195:1981;573-581.
    • (1981) Biochemical Journal , vol.195 , pp. 573-581
    • Scott, J.E.1    Orford, C.R.2    Hughes, E.W.3
  • 102
    • 0025215287 scopus 로고
    • Elastic energy storage in tendons: Mechanical differences related to function and age
    • Shadwick R.E. Elastic energy storage in tendons. mechanical differences related to function and age Journal of Applied Physiology. 68:1990;1033-1040.
    • (1990) Journal of Applied Physiology , vol.68 , pp. 1033-1040
    • Shadwick, R.E.1
  • 104
    • 0021126710 scopus 로고
    • Molecular structure of collagen in solution: Comparison of types I, II, III, and V
    • Silver F.H., Birk D.E. Molecular structure of collagen in solution. comparison of types I, II, III, and V International Journal of Biological Macromolecules. 6:1984;125-132.
    • (1984) International Journal of Biological Macromolecules , vol.6 , pp. 125-132
    • Silver, F.H.1    Birk, D.E.2
  • 106
    • 0018568324 scopus 로고
    • Type I collagen fibrillogenesis: Initiation via a reversible linear growth step
    • Silver F.H., Langley K.H., Trelstad R.L. Type I collagen fibrillogenesis. initiation via a reversible linear growth step Biopolymers. 18:1979;2523-2535.
    • (1979) Biopolymers , vol.18 , pp. 2523-2535
    • Silver, F.H.1    Langley, K.H.2    Trelstad, R.L.3
  • 107
    • 0027006916 scopus 로고
    • Analysis of mammalian connective tissue: Relationship between hierarchical structures and mechanical properties
    • Silver F.H., Kato Y.P., Ohno M., Wasserman A.J. Analysis of mammalian connective tissue. relationship between hierarchical structures and mechanical properties Journal of Long-Term Effects of Medical Implants. 2:1992;165-198.
    • (1992) Journal of Long-Term Effects of Medical Implants , vol.2 , pp. 165-198
    • Silver, F.H.1    Kato, Y.P.2    Ohno, M.3    Wasserman, A.J.4
  • 108
    • 0033870607 scopus 로고    scopus 로고
    • Role of storage on changes in the mechanical properties of tendon and self-assembled collagen fibers
    • Silver F.H., Christiansen D.L., Snowhill P.B., Chen Y. Role of storage on changes in the mechanical properties of tendon and self-assembled collagen fibers. Connective Tissue Research. 42:2000;155-164.
    • (2000) Connective Tissue Research , vol.42 , pp. 155-164
    • Silver, F.H.1    Christiansen, D.L.2    Snowhill, P.B.3    Chen, Y.4
  • 110
    • 0035155477 scopus 로고    scopus 로고
    • Transition from viscous to elastic-dependency of mechanical properties of self-assembled collagen fibers
    • Silver F.H., Christiansen D.L., Snowhill P.B., Chen Y. Transition from viscous to elastic-dependency of mechanical properties of self-assembled collagen fibers. Journal of Polymer Science. 7:2001;134-142.
    • (2001) Journal of Polymer Science , vol.7 , pp. 134-142
    • Silver, F.H.1    Christiansen, D.L.2    Snowhill, P.B.3    Chen, Y.4
  • 112
    • 0036308986 scopus 로고    scopus 로고
    • Mechanical implications of the domain structure of fibril forming collagens: Comparison of the molecular and fibrillar flexibilities of the α-chains found in types I, II, and III collagen
    • Silver F.H., Horvath I., Foran D.J. Mechanical implications of the domain structure of fibril forming collagens. comparison of the molecular and fibrillar flexibilities of the α-chains found in types I, II, and III collagen Journal of Theoretical Biology. 216:2002;243-254.
    • (2002) Journal of Theoretical Biology , vol.216 , pp. 243-254
    • Silver, F.H.1    Horvath, I.2    Foran, D.J.3
  • 113
    • 0036924318 scopus 로고    scopus 로고
    • Viscoelastic properties of self-assembled type I collagen fibers: Molecular basis of elastic and viscous behaviors
    • Silver F.H., Ebrahimi A., Snowhill P.B. Viscoelastic properties of self-assembled type I collagen fibers. molecular basis of elastic and viscous behaviors Connective Tissue Research. 43:2002;569-580.
    • (2002) Connective Tissue Research , vol.43 , pp. 569-580
    • Silver, F.H.1    Ebrahimi, A.2    Snowhill, P.B.3
  • 114
    • 0018354864 scopus 로고
    • Dynamic light scattering from collagen solutions. II. Photon correlation study of the depolarized light
    • Thomas J.C., Fletcher G.C. Dynamic light scattering from collagen solutions. II. Photon correlation study of the depolarized light. Biopolymers. 18:1979;1333-1352.
    • (1979) Biopolymers , vol.18 , pp. 1333-1352
    • Thomas, J.C.1    Fletcher, G.C.2
  • 115
    • 0001322798 scopus 로고
    • Effects of age and of mechanical deformation on the ultrastructure of tendon
    • Torp S., Baer E., Friedman B. Effects of age and of mechanical deformation on the ultrastructure of tendon. Colston Papers. 26:1975;223-250.
    • (1975) Colston Papers , vol.26 , pp. 223-250
    • Torp, S.1    Baer, E.2    Friedman, B.3
  • 116
  • 117
    • 0018762445 scopus 로고
    • Tendon collagen fibrillogenesis: Intracellular subassemblies and cell surface changes associated with fibril growth
    • Trelstad R.L., Hayashi K. Tendon collagen fibrillogenesis. intracellular subassemblies and cell surface changes associated with fibril growth Developmental Biology. 71:1979;228-242.
    • (1979) Developmental Biology , vol.71 , pp. 228-242
    • Trelstad, R.L.1    Hayashi, K.2
  • 119
    • 0141857158 scopus 로고
    • Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen
    • Tuderman L., Kivirikk K.I., Prockop D.J. Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen. Biochemistry. 16:1977;3421-3429.
    • (1977) Biochemistry , vol.16 , pp. 3421-3429
    • Tuderman, L.1    Kivirikk, K.I.2    Prockop, D.J.3
  • 120
    • 0003005891 scopus 로고
    • Fundamentals of interstitial collagen self-assembly
    • P.D. Yurchenco. New York: Academic Press
    • Veis A., George A. Fundamentals of interstitial collagen self-assembly. Yurchenco P.D. Extracellular Matrix Assembly. 1994;15-45 Academic Press, New York.
    • (1994) Extracellular Matrix Assembly , pp. 15-45
    • Veis, A.1    George, A.2
  • 121
    • 0023042512 scopus 로고
    • Collagen self-assembly in vitro: Electron microscopy of initial aggregates formed during the lag phase
    • Ward N.P., Hulmes D.J.S., Chapman J.A. Collagen self-assembly in vitro. electron microscopy of initial aggregates formed during the lag phase Journal of Molecular Biology. 190:1986;107-112.
    • (1986) Journal of Molecular Biology , vol.190 , pp. 107-112
    • Ward, N.P.1    Hulmes, D.J.S.2    Chapman, J.A.3
  • 123
    • 0026794741 scopus 로고
    • Ehlers Danlos syndrome type VIIb. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pN-collagen that are near circular in cross-section
    • Waston R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., Kadler K.E. Ehlers Danlos syndrome type VIIb. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pN-collagen that are near circular in cross-section. Journal of Biological Chemistry. 267:1992;9093-9100.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 9093-9100
    • Waston, R.B.1    Wallis, G.A.2    Holmes, D.F.3    Viljoen, D.4    Byers, P.H.5    Kadler, K.E.6
  • 124
    • 0032562635 scopus 로고    scopus 로고
    • Surface located procollagen N-propeptides on dermatosparactic collagen fibrils are not cleaved by procollagen N-proteinase and do not inhibit binding of decorin to the fibril surface
    • Waston R.B., Holmes D.F., Graham H.K., Nusgens B.V., Kadler K.E. Surface located procollagen N-propeptides on dermatosparactic collagen fibrils are not cleaved by procollagen N-proteinase and do not inhibit binding of decorin to the fibril surface. Journal of Molecular Biology. 278:1998;195-204.
    • (1998) Journal of Molecular Biology , vol.278 , pp. 195-204
    • Waston, R.B.1    Holmes, D.F.2    Graham, H.K.3    Nusgens, B.V.4    Kadler, K.E.5
  • 126
    • 0017616285 scopus 로고
    • Collagen-mineral axial relationship in calcified turkey tendon by X-ray and neutron diffraction
    • White S.W., Hulmes D.J.S., Miller A., Timmins P.A. Collagen-mineral axial relationship in calcified turkey tendon by X-ray and neutron diffraction. Nature. 266:1977;421-425.
    • (1977) Nature , vol.266 , pp. 421-425
    • White, S.W.1    Hulmes, D.J.S.2    Miller, A.3    Timmins, P.A.4
  • 128
    • 0024602960 scopus 로고
    • Microscopical investigation of canine cruciate ligament and patellar tendon: Collagen fascicle morphology and architecture
    • Yahia L.-H., Drouin G. Microscopical investigation of canine cruciate ligament and patellar tendon. collagen fascicle morphology and architecture Journal of Orthopaedic Research. 7:1969;243-251.
    • (1969) Journal of Orthopaedic Research , vol.7 , pp. 243-251
    • Yahia, L.-H.1    Drouin, G.2
  • 130
    • 0015847573 scopus 로고
    • The self-assembly of collagen molecules
    • Yuan L., Veis A. The self-assembly of collagen molecules. Biopolymers. 12:1973;1437-1444.
    • (1973) Biopolymers , vol.12 , pp. 1437-1444
    • Yuan, L.1    Veis, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.