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Volumn 70, Issue , 2005, Pages 341-374

Collagen fibril form and function

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 1; COLLAGEN TYPE 2; PROTEOGLYCAN;

EID: 17444374661     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(05)70010-3     Document Type: Article
Times cited : (159)

References (127)
  • 1
    • 0022605642 scopus 로고
    • In vitro formation of hybrid fibrils of type-V collagen and type-I collagen - Limited growth of type-I collagen into thick fibrils by type-V collagen
    • Adachi E., Hayashi T. In vitro formation of hybrid fibrils of type-V collagen and type-I collagen - Limited growth of type-I collagen into thick fibrils by type-V collagen. Connect. Tissue Res. 14:1986;257-266
    • (1986) Connect. Tissue Res. , vol.14 , pp. 257-266
    • Adachi, E.1    Hayashi, T.2
  • 2
    • 0035978878 scopus 로고    scopus 로고
    • Molecular mechanisms of ageing in connective tissues
    • Bailey A.J. Molecular mechanisms of ageing in connective tissues. Mech. Ageing Dev. 122:2001;735-755
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 735-755
    • Bailey, A.J.1
  • 3
    • 0027136085 scopus 로고
    • Subfibrillar structure of type-I collagen observed by atomic-force microscopy
    • Baselt D.R., Revel J.P., Baldeschwieler J.D. Subfibrillar structure of type-I collagen observed by atomic-force microscopy. Biophys. J. 65:1993;2644-2655
    • (1993) Biophys. J. , vol.65 , pp. 2644-2655
    • Baselt, D.R.1    Revel, J.P.2    Baldeschwieler, J.D.3
  • 4
    • 0035219340 scopus 로고    scopus 로고
    • Type V collagen: Heterotypic type I/V collagen interactions in the regulation of fibril assembly
    • Birk D.E. Type V collagen: Heterotypic type I/V collagen interactions in the regulation of fibril assembly. Micron. 32:2001;223-237
    • (2001) Micron , vol.32 , pp. 223-237
    • Birk, D.E.1
  • 5
    • 0031042279 scopus 로고    scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures
    • Birk D.E., Zychband E.I., Woodruff S., Winkelmann D.A., Trelastd R.L. Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures. Dev. Dynam. 208:1997;291-298
    • (1997) Dev. Dynam. , vol.208 , pp. 291-298
    • Birk, D.E.1    Zychband, E.I.2    Woodruff, S.3    Winkelmann, D.A.4    Trelastd, R.L.5
  • 6
    • 0034003134 scopus 로고    scopus 로고
    • Structural macromolecules and supramolecular organisation of the vitreous gel
    • Bishop P.N. Structural macromolecules and supramolecular organisation of the vitreous gel. Prog. Retin. Eye Res. 19:2000;323-344
    • (2000) Prog. Retin. Eye Res. , vol.19 , pp. 323-344
    • Bishop, P.N.1
  • 7
  • 8
    • 0024564287 scopus 로고
    • Phasing the meridional diffraction pattern of type I collagen using isomorphous derivatives
    • Bradshaw J.P., Miller A., Wess T.J. Phasing the meridional diffraction pattern of type I collagen using isomorphous derivatives. J. Mol. Biol. 205:1989;685-694
    • (1989) J. Mol. Biol. , vol.205 , pp. 685-694
    • Bradshaw, J.P.1    Miller, A.2    Wess, T.J.3
  • 9
    • 0037791886 scopus 로고    scopus 로고
    • SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength
    • Bradshaw A.D., Puolakkainen P., Dasgupta J., Davidson J.M., Wight T.N., Sage E.H. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J. Invest. Dermatol. 120:2003;949-955
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 949-955
    • Bradshaw, A.D.1    Puolakkainen, P.2    Dasgupta, J.3    Davidson, J.M.4    Wight, T.N.5    Sage, E.H.6
  • 11
    • 0030651543 scopus 로고    scopus 로고
    • Model of the helical portion of a type I collagen microfibril
    • Brown E.M., King G., Chen J.M. Model of the helical portion of a type I collagen microfibril. J. Am. Leather Chem. As. 92:1997;1-7
    • (1997) J. Am. Leather Chem. As. , vol.92 , pp. 1-7
    • Brown, E.M.1    King, G.2    Chen, J.M.3
  • 12
    • 0036445444 scopus 로고    scopus 로고
    • Structure of type I and type III heterotypic collagen fibrils: An X-ray diffraction study
    • Cameron G.J., Alberts I.L., Laing J.H., Wess T.J. Structure of type I and type III heterotypic collagen fibrils: An X-ray diffraction study. J. Struct. Biol. 137:2002;15-22
    • (2002) J. Struct. Biol. , vol.137 , pp. 15-22
    • Cameron, G.J.1    Alberts, I.L.2    Laing, J.H.3    Wess, T.J.4
  • 13
    • 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. J. Cell Biol. 141:1998;1277-1286
    • (1998) J. Cell Biol. , 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
  • 15
    • 0024412103 scopus 로고
    • The regulation of size and form in the assembly of collagen fibrils in vivo
    • Chapman J.A. The regulation of size and form in the assembly of collagen fibrils in vivo. Biopolymers. 28:1989;1367-1382
    • (1989) Biopolymers , vol.28 , pp. 1367-1382
    • Chapman, J.A.1
  • 16
    • 0024313452 scopus 로고
    • An estimate of the mean length of collagen fibrils in rat tail tendon as a function of age
    • Craig A.S., Birtles M.J., Conway J.F., Parry D.A.D. An estimate of the mean length of collagen fibrils in rat tail tendon as a function of age. Connect. Tissue Res. 19:1989;51-62
    • (1989) Connect. Tissue Res. , vol.19 , pp. 51-62
    • Craig, A.S.1    Birtles, M.J.2    Conway, J.F.3    Parry, D.A.D.4
  • 17
    • 0032792118 scopus 로고    scopus 로고
    • Decorin, epiphycan, and lumican genes are closely linked on murine chromosome 10 and are deleted in lethal steel mutants
    • Danielson K.G., Siracusa L.D., Donovan P.J., Iozzo R.V. Decorin, epiphycan, and lumican genes are closely linked on murine chromosome 10 and are deleted in lethal steel mutants. Mamm. Genome. 10:1999;201-203
    • (1999) Mamm. Genome. , vol.10 , pp. 201-203
    • Danielson, K.G.1    Siracusa, L.D.2    Donovan, P.J.3    Iozzo, R.V.4
  • 18
    • 0035058027 scopus 로고    scopus 로고
    • Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle
    • Derwin K.A., Soslowsky L.J., Kimura J.H., Plaas A.H. Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle. J. Orthop. Res. 19:2001;269-277
    • (2001) J. Orthop. Res. , vol.19 , pp. 269-277
    • Derwin, K.A.1    Soslowsky, L.J.2    Kimura, J.H.3    Plaas, A.H.4
  • 19
    • 3042699710 scopus 로고    scopus 로고
    • Characterization of whole fibril-forming collagen proteins of types I, III, and V from foetal calf skin by infrared matrix-assisted laser desorption ionization mass spectrometry
    • Dreisewerd K., Rohlfing A., Spottke B., Urbanke C., Henkel W. Characterization of whole fibril-forming collagen proteins of types I, III, and V from foetal calf skin by infrared matrix-assisted laser desorption ionization mass spectrometry. Anal. Chem. 76:2004;3482-3491
    • (2004) Anal. Chem. , vol.76 , pp. 3482-3491
    • Dreisewerd, K.1    Rohlfing, A.2    Spottke, B.3    Urbanke, C.4    Henkel, W.5
  • 22
    • 1642494706 scopus 로고    scopus 로고
    • Covalent cross-linking of the NC1 domain of collagen type IX to collagen type II in cartilage
    • Eyre D.R., Pietka T., Weis M.A., Wu J.J. Covalent cross-linking of the NC1 domain of collagen type IX to collagen type II in cartilage. J. Biol. Chem. 279:2004;2568-2574
    • (2004) J. Biol. Chem. , vol.279 , pp. 2568-2574
    • Eyre, D.R.1    Pietka, T.2    Weis, M.A.3    Wu, J.J.4
  • 24
    • 0000658473 scopus 로고
    • Quantitative analysis of the molecular sliding mechanism in native tendon collagen - Time resolved dynamic studies using synchrotron radiation
    • Folkhard W., Mosler E., Geercken E., Knorzer H., Nemetschek-Gansler H., Nemetschek T. Quantitative analysis of the molecular sliding mechanism in native tendon collagen - Time resolved dynamic studies using synchrotron radiation. Int. J. Biol. Macromol. 9:1987b;169-175
    • (1987) Int. J. Biol. Macromol. , vol.9 , pp. 169-175
    • Folkhard, W.1    Mosler, E.2    Geercken, E.3    Knorzer, H.4    Nemetschek-Gansler, H.5    Nemetschek, T.6
  • 25
    • 0027352739 scopus 로고
    • Ultrastructural evidences of a distinct axial domain within native rat tail tendon collagen fibrils
    • Franc S. Ultrastructural evidences of a distinct axial domain within native rat tail tendon collagen fibrils. J. Submicrosc. Cytol. Path. 25:1993;85-91
    • (1993) J. Submicrosc. Cytol. Path. , vol.25 , pp. 85-91
    • Franc, S.1
  • 26
  • 27
    • 0023119530 scopus 로고
    • Molecular packing in type I collagen fibrils
    • Fraser R.D.B., MacRae T.P., Miller A. Molecular packing in type I collagen fibrils. J. Mol. Biol. 193:1987;115-125
    • (1987) J. Mol. Biol. , vol.193 , pp. 115-125
    • Fraser, R.D.B.1    MacRae, T.P.2    Miller, A.3
  • 28
    • 0038714394 scopus 로고    scopus 로고
    • Cellulose and collagen: From fibres to tissues
    • Fratzl P. Cellulose and collagen: from fibres to tissues. Curr. Opin. Colloid In. 8:2003;32-39
    • (2003) Curr. Opin. Colloid In. , vol.8 , pp. 32-39
    • Fratzl, P.1
  • 29
    • 0027475398 scopus 로고
    • Collagen packing and mineralization. An X-ray scattering investigation of turkey leg tendon
    • Fratzl P., Fratzl-Zelman N., Klaushofer K. Collagen packing and mineralization. An X-ray scattering investigation of turkey leg tendon. Biophys. J. 64:1993;260-266
    • (1993) Biophys. J. , vol.64 , pp. 260-266
    • Fratzl, P.1    Fratzl-Zelman, N.2    Klaushofer, K.3
  • 31
    • 0029870168 scopus 로고    scopus 로고
    • Twisted liquid crystalline supramolecular arrangements in morphogenesis
    • Giraud-Guille M.-M. Twisted liquid crystalline supramolecular arrangements in morphogenesis. Int. Rev. Cytol. 166:1996;59-101
    • (1996) Int. Rev. Cytol. , vol.166 , pp. 59-101
    • Giraud-Guille, M.-M.1
  • 32
    • 0141453851 scopus 로고    scopus 로고
    • Liquid crystalline assemblies of collagen in bone and in vitro systems
    • Giraud-Guille M.M., Besseau L., Martin R. Liquid crystalline assemblies of collagen in bone and in vitro systems. J. Biomech. 36:2003;1571-1579
    • (2003) J. Biomech. , vol.36 , pp. 1571-1579
    • Giraud-Guille, M.M.1    Besseau, L.2    Martin, R.3
  • 35
    • 0032514149 scopus 로고    scopus 로고
    • Cartilage fibrils of mammals are biochemically heterogeneous: Differential distribution of decorin and collagen IX
    • Hagg R., Bruckner P., Hedbom E. Cartilage fibrils of mammals are biochemically heterogeneous: Differential distribution of decorin and collagen IX. J. Cell Biol. 142:1998;285-294
    • (1998) J. Cell Biol. , vol.142 , pp. 285-294
    • Hagg, R.1    Bruckner, P.2    Hedbom, E.3
  • 36
    • 0141621226 scopus 로고    scopus 로고
    • Macromolecular specificity of collagen fibrillogenesis. Fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheath
    • Hansen U., Bruckner P. Macromolecular specificity of collagen fibrillogenesis. Fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheath. J. Biol. Chem. 278:2003;37352-37359
    • (2003) J. Biol. Chem. , vol.278 , pp. 37352-37359
    • Hansen, U.1    Bruckner, P.2
  • 37
    • 0036691214 scopus 로고    scopus 로고
    • Preliminary observations on the influence of rheumatoid alpha-1-acid glycoprotein on collagen fibril formation
    • Haston J.L., FitzGerald O., Kane D., Smith K.D. Preliminary observations on the influence of rheumatoid alpha-1-acid glycoprotein on collagen fibril formation. Biomed. Chromatogr. 16:2002;332-342
    • (2002) Biomed. Chromatogr. , vol.16 , pp. 332-342
    • Haston, J.L.1    Fitzgerald, O.2    Kane, D.3    Smith, K.D.4
  • 40
    • 0019888241 scopus 로고
    • Collagen self-assembly in vitro. Differentiating specific telopeptide dependent interactions using selective enzyme modification and the addition of free amino telopeptide
    • Helseth D.L., Veis A. Collagen self-assembly in vitro. Differentiating specific telopeptide dependent interactions using selective enzyme modification and the addition of free amino telopeptide. J. Biol. Chem. 256:1981;7118-7128
    • (1981) J. Biol. Chem. , vol.256 , pp. 7118-7128
    • Helseth, D.L.1    Veis, A.2
  • 41
    • 0018581198 scopus 로고
    • Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis
    • Helseth D.L. Jr., Lechner J.H., Veis A. Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis. Biopolymers. 18:1979;3005-3014
    • (1979) Biopolymers , vol.18 , pp. 3005-3014
    • Helseth Jr., D.L.1    Lechner, J.H.2    Veis, A.3
  • 42
    • 0029814082 scopus 로고    scopus 로고
    • Cross-link analysis of the C-telopeptide domain from type III collagen
    • Henkel W. Cross-link analysis of the C-telopeptide domain from type III collagen. Biochem. J. 318:1996;497-503
    • (1996) Biochem. J. , vol.318 , pp. 497-503
    • Henkel, W.1
  • 43
    • 0020031151 scopus 로고
    • Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha 1 (I) and alpha 1 (III) chains in the formation of intermolecular crosslinks
    • Henkel W., Glanville R.W. Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha 1 (I) and alpha 1 (III) chains in the formation of intermolecular crosslinks. Eur. J. Biochem. 122:1982;205-213
    • (1982) Eur. J. Biochem. , vol.122 , pp. 205-213
    • Henkel, W.1    Glanville, R.W.2
  • 44
    • 33947456809 scopus 로고
    • Electron microscope observations of certain fibrous structures obtained from connective tissue extracts
    • Highberger J.H., Gross J., Schmitt F.O. Electron microscope observations of certain fibrous structures obtained from connective tissue extracts. J. Am. Chem. Soc. 72:1950;3321-3322
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 3321-3322
    • Highberger, J.H.1    Gross, J.2    Schmitt, F.O.3
  • 45
    • 0002740030 scopus 로고
    • Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule
    • G.N. Ramachandran. London: Academic Press
    • Hodge A.J., Petruska J.A. Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule. Ramachandran G.N. "Aspects of Protein Chemistry" 1963;289-300 Academic Press, London
    • (1963) "aspects of Protein Chemistry" , pp. 289-300
    • Hodge, A.J.1    Petruska, J.A.2
  • 46
    • 0018884576 scopus 로고
    • Comparative analysis of the sequences of the three collagen chains α1(I), α2 and α1(III); Function and genetic aspects
    • Hofmann H., Fietzek P.P., Kuhn K. Comparative analysis of the sequences of the three collagen chains α1(I), α2 and α1(III); Function and genetic aspects. J. Mol. Biol. 141:1980;293-314
    • (1980) J. Mol. Biol. , vol.141 , pp. 293-314
    • Hofmann, H.1    Fietzek, P.P.2    Kuhn, K.3
  • 47
    • 0035912751 scopus 로고    scopus 로고
    • Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organization
    • Holmes D.F., Gilpin C.J., Baldock C., Ziese U., Koster A.J., Kadler K.E. Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organization. Proc. Natl. Acad. Sci. USA. 98:2001;7307-7312
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7307-7312
    • Holmes, D.F.1    Gilpin, C.J.2    Baldock, C.3    Ziese, U.4    Koster, A.J.5    Kadler, K.E.6
  • 48
  • 49
    • 0036447070 scopus 로고    scopus 로고
    • Building collagen molecules, fibrils, and suprafibrillar structures
    • Hulmes D.J.S. Building collagen molecules, fibrils, and suprafibrillar structures. J. Struct. Biol. 137:2002;2-10
    • (2002) J. Struct. Biol. , vol.137 , pp. 2-10
    • Hulmes, D.J.S.1
  • 51
    • 0017329109 scopus 로고
    • Interpretation of the meridional diffraction pattern from collagen fibres in terms of the known amino acid sequence
    • Hulmes D.J.S., Miller A., White S.W., Brodsky-Doyle B. Interpretation of the meridional diffraction pattern from collagen fibres in terms of the known amino acid sequence. J. Mol. Biol. 110:1977;643-666
    • (1977) J. Mol. Biol. , vol.110 , pp. 643-666
    • Hulmes, D.J.S.1    Miller, A.2    White, S.W.3    Brodsky-Doyle, B.4
  • 52
    • 0019179373 scopus 로고
    • Interpretation of the low angle meridional neutron diffraction patterns from collagen fibres in terms of the amino acid sequence
    • Hulmes D.J.S., Miller A., White S.W., Timmins P.A., Berthet-Colominas C. Interpretation of the low angle meridional neutron diffraction patterns from collagen fibres in terms of the amino acid sequence. Int. J. Biol. Macromol. 2:1980;338-345
    • (1980) Int. J. Biol. Macromol. , vol.2 , pp. 338-345
    • Hulmes, D.J.S.1    Miller, A.2    White, S.W.3    Timmins, P.A.4    Berthet-Colominas, C.5
  • 54
    • 0028910961 scopus 로고
    • Radial packing, order and disorder in collagen fibrils
    • Hulmes D.J.S., Wess T.J., Prockop D.J., Fratzl P. Radial packing, order and disorder in collagen fibrils. Biophys. J. 68:1995;1661-1670
    • (1995) Biophys. J. , vol.68 , pp. 1661-1670
    • Hulmes, D.J.S.1    Wess, T.J.2    Prockop, D.J.3    Fratzl, P.4
  • 55
    • 0026774215 scopus 로고
    • Collagen fibril structure of normal, aging, and osteoarthritic cartilage
    • Hwang W.S., Li B., Jin L.H., Ngo K., Schachar N.S., Hughes G.N.F. Collagen fibril structure of normal, aging, and osteoarthritic cartilage. J. Pathol. 167:1992;425-433
    • (1992) J. Pathol. , vol.167 , pp. 425-433
    • Hwang, W.S.1    Li, B.2    Jin, L.H.3    Ngo, K.4    Schachar, N.S.5    Hughes, G.N.F.6
  • 56
    • 0031998352 scopus 로고    scopus 로고
    • The role of intermolecular electrostatic interaction on appearance of the periodic band structure in type I collagen fibril
    • Itoh T., Kobayashi M., Hashimoto M. The role of intermolecular electrostatic interaction on appearance of the periodic band structure in type I collagen fibril. Jpn. J. Appl. Phys. 1. 37:1998;L190-L192
    • (1998) Jpn. J. Appl. Phys. 1. , vol.37
    • Itoh, T.1    Kobayashi, M.2    Hashimoto, M.3
  • 57
    • 17444384721 scopus 로고
    • Crystalline three dimensional packing is a general feature of type I collagen fibrils
    • Jesoir J.C., Miller A., Berthet-Colominas C. Crystalline three dimensional packing is a general feature of type I collagen fibrils. FEBS Lett. 13:1981;238-240
    • (1981) FEBS Lett. , vol.13 , pp. 238-240
    • Jesoir, J.C.1    Miller, A.2    Berthet-Colominas, C.3
  • 58
    • 0023324043 scopus 로고
    • Models for the N-terminal and C-terminal telopeptide regions of interstitial collagens
    • Jones E.Y., Miller A. Models for the N-terminal and C-terminal telopeptide regions of interstitial collagens. Biopolymers. 26:1987;463-480
    • (1987) Biopolymers , vol.26 , pp. 463-480
    • Jones, E.Y.1    Miller, A.2
  • 59
    • 0026036378 scopus 로고
    • Analysis of structural design features in collagen
    • Jones E.Y., Miller A. Analysis of structural design features in collagen. J. Mol. Biol. 218:1991;209-219
    • (1991) J. Mol. Biol. , vol.218 , pp. 209-219
    • Jones, E.Y.1    Miller, A.2
  • 60
    • 0020075761 scopus 로고
    • Fibrous long spacing-like fibers in the bone marrow of myeloproliferative disorder
    • Kamiyama R. Fibrous long spacing-like fibers in the bone marrow of myeloproliferative disorder. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 39:1982;285-291
    • (1982) Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. , vol.39 , pp. 285-291
    • Kamiyama, R.1
  • 61
    • 0034577312 scopus 로고    scopus 로고
    • Structure of the tendon connective tissue
    • Kannus P. Structure of the tendon connective tissue. Scand. J. Med. Sci. Spor. 10:2000;312-320
    • (2000) Scand. J. Med. Sci. Spor. , vol.10 , pp. 312-320
    • Kannus, P.1
  • 64
    • 0035933862 scopus 로고    scopus 로고
    • Alpha 1(XX) collagen, a new member of the collagen subfamily, fibril-associated collagens with interrupted triple helices
    • Koch M., Foley J.E., Hahn R., Zhou P.H., Burgeson R.E., Gerecke D.R., Gordon M.K. Alpha 1(XX) collagen, a new member of the collagen subfamily, fibril-associated collagens with interrupted triple helices. J. Biol. Chem. 276:2001;23120-23126
    • (2001) J. Biol. Chem. , vol.276 , pp. 23120-23126
    • Koch, M.1    Foley, J.E.2    Hahn, R.3    Zhou, P.H.4    Burgeson, R.E.5    Gerecke, D.R.6    Gordon, M.K.7
  • 65
    • 0036758402 scopus 로고    scopus 로고
    • Size control of decorin dermatan sulfate during remodeling of collagen fibrils in healing skin
    • Kuwaba K., Kobayashi M., Nomura Y., Irie S., Koyama Y. Size control of decorin dermatan sulfate during remodeling of collagen fibrils in healing skin. J. Dermatol. Sci. 29:2002;185-194
    • (2002) J. Dermatol. Sci. , vol.29 , pp. 185-194
    • Kuwaba, K.1    Kobayashi, M.2    Nomura, Y.3    Irie, S.4    Koyama, Y.5
  • 66
    • 0030199347 scopus 로고    scopus 로고
    • Mineralization of collagen may occur on fibril surfaces: Evidence from conventional and high-voltage electron microscopy and three-dimensional imaging
    • Landis W.J., Hodgens K.J., Song M.J., Arena J., Kiyonaga S., Marko M., Owen C., McEwen B.F. Mineralization of collagen may occur on fibril surfaces: Evidence from conventional and high-voltage electron microscopy and three-dimensional imaging. J. Struct. Biol. 117:1996;24-35
    • (1996) J. Struct. Biol. , vol.117 , pp. 24-35
    • Landis, W.J.1    Hodgens, K.J.2    Song, M.J.3    Arena, J.4    Kiyonaga, S.5    Marko, M.6    Owen, C.7    McEwen, B.F.8
  • 68
    • 0027732933 scopus 로고
    • Conformational analysis of the type-II and type-III collagen alpha-1 chain C-telopeptides by H-1-nmr and Circular-Dichroism Spectroscopy
    • Liu X.H., Otter A., Scott P.G., Cann J.R., Kotovych G. Conformational analysis of the type-II and type-III collagen alpha-1 chain C-telopeptides by H-1-nmr and Circular-Dichroism Spectroscopy. J. Biomol. Struct. Dyn. 11:1993;541-555
    • (1993) J. Biomol. Struct. Dyn. , vol.11 , pp. 541-555
    • Liu, X.H.1    Otter, A.2    Scott, P.G.3    Cann, J.R.4    Kotovych, G.5
  • 69
    • 0347028682 scopus 로고    scopus 로고
    • N-telopeptide of type II collagen interacts with annexin V on human chondrocytes
    • Lucic D., Mollenhauer J., Kilpatrick K.E., Cole A.A. N-telopeptide of type II collagen interacts with annexin V on human chondrocytes. Connect. Tissue Res. 44:2003;225-239
    • (2003) Connect. Tissue Res. , vol.44 , pp. 225-239
    • Lucic, D.1    Mollenhauer, J.2    Kilpatrick, K.E.3    Cole, A.A.4
  • 70
    • 0027257648 scopus 로고
    • Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro
    • MacBeath J.R., Shackleton D.R., Hulmes D.J.S. Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro. J. Biol. Chem. 268:1993;19826-19832
    • (1993) J. Biol. Chem. , vol.268 , pp. 19826-19832
    • MacBeath, J.R.1    Shackleton, D.R.2    Hulmes, D.J.S.3
  • 71
    • 0342460605 scopus 로고    scopus 로고
    • Altered collagen structure in mouse tail tendon lacking the alpha 2(I) chain
    • McBride D.J., Choe V., Shapiro J.R., Brodsky B. Altered collagen structure in mouse tail tendon lacking the alpha 2(I) chain. J. Mol. Biol. 270:1997;275-284
    • (1997) J. Mol. Biol. , vol.270 , pp. 275-284
    • McBride, D.J.1    Choe, V.2    Shapiro, J.R.3    Brodsky, B.4
  • 72
    • 0347089141 scopus 로고    scopus 로고
    • Type I collagen N-telopeptides adopt an ordered structure when docked to their helix receptor during fibrillogenesis
    • Malone J.P., George A., Veis A. Type I collagen N-telopeptides adopt an ordered structure when docked to their helix receptor during fibrillogenesis. Proteins. 54:2004;206-215
    • (2004) Proteins , vol.54 , pp. 206-215
    • Malone, J.P.1    George, A.2    Veis, A.3
  • 73
    • 0023034390 scopus 로고
    • Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation
    • Marchini M., Morocutti M., Ruggeri A., Koch M.H.J., Bigi A., Roveri N. Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation. Connect. Tissue Res. 15:1986;269-281
    • (1986) Connect. Tissue Res. , vol.15 , pp. 269-281
    • Marchini, M.1    Morocutti, M.2    Ruggeri, A.3    Koch, M.H.J.4    Bigi, A.5    Roveri, N.6
  • 75
    • 0035218928 scopus 로고    scopus 로고
    • Corneal and scleral collagens - A microscopist's perspective
    • Meek K.M., Fullwood N.J. Corneal and scleral collagens - A microscopist's perspective. Micron. 32:2001;261-272
    • (2001) Micron , vol.32 , pp. 261-272
    • Meek, K.M.1    Fullwood, N.J.2
  • 76
    • 0018621677 scopus 로고
    • The staining pattern of collagen fibrils. Improved correlation with sequence data
    • Meek K.M., Chapman J.A., Hardcastle R.A. The staining pattern of collagen fibrils. Improved correlation with sequence data. J. Biol. Chem. 254:1979;10710-10714
    • (1979) J. Biol. Chem. , vol.254 , pp. 10710-10714
    • Meek, K.M.1    Chapman, J.A.2    Hardcastle, R.A.3
  • 77
    • 0021365849 scopus 로고
    • Morphometric analysis of loading-induced changes in collagen-fibril populations in young tendons
    • Michna H. Morphometric analysis of loading-induced changes in collagen-fibril populations in young tendons. Cell Tissue Res. 236:1984;465-470
    • (1984) Cell Tissue Res. , vol.236 , pp. 465-470
    • Michna, H.1
  • 78
    • 0002259625 scopus 로고
    • Calculated X-ray diffraction pattern from a quasi-hexagonal model for the molecular arrangement in collagen
    • Miller A., Tochetti D. Calculated X-ray diffraction pattern from a quasi-hexagonal model for the molecular arrangement in collagen. Int. J. Macromol. 3:1981;9-18
    • (1981) Int. J. Macromol. , vol.3 , pp. 9-18
    • Miller, A.1    Tochetti, D.2
  • 79
    • 0035218501 scopus 로고    scopus 로고
    • The fibril structure of type V collagen triple-helical domain
    • Mizuno K., Adachi E., Imamura Y., Katsumata O., Hayashi T. The fibril structure of type V collagen triple-helical domain. Micron. 32:2001;317-323
    • (2001) Micron , vol.32 , pp. 317-323
    • Mizuno, K.1    Adachi, E.2    Imamura, Y.3    Katsumata, O.4    Hayashi, T.5
  • 80
    • 0018093662 scopus 로고
    • Fibrous long-spacing collagen in human atherosclerosis
    • Morris C.J., Bradby G.V., Walton K.W. Fibrous long-spacing collagen in human atherosclerosis. Atherosclerosis. 31:1978;345-354
    • (1978) Atherosclerosis , vol.31 , pp. 345-354
    • Morris, C.J.1    Bradby, G.V.2    Walton, K.W.3
  • 81
    • 0019792322 scopus 로고
    • Distribution of fibrous long-spacing fibers in normal and pathological lymph nodes
    • Nakanishi S., Masuda T., Kitamura T., Moriizumi K., Kajikawa T. Distribution of fibrous long-spacing fibers in normal and pathological lymph nodes. Acta Pathol. Jpn. 31:1981;733-745
    • (1981) Acta Pathol. Jpn. , vol.31 , pp. 733-745
    • Nakanishi, S.1    Masuda, T.2    Kitamura, T.3    Moriizumi, K.4    Kajikawa, T.5
  • 82
    • 0000663180 scopus 로고
    • Structural units in collagen fibrils
    • North A.C.T., Cowan P.M., Randall J.T. Structural units in collagen fibrils. Nature. 174:1954;1142-1143
    • (1954) Nature , vol.174 , pp. 1142-1143
    • North, A.C.T.1    Cowan, P.M.2    Randall, J.T.3
  • 83
    • 0034864212 scopus 로고    scopus 로고
    • Early anchoring collagen fibres at the bone-tendon interface are conducted by woven bone formation
    • Oguma H., Murakami G., Takahashi-Iwanaga H., Aoki M., Ishii S. Early anchoring collagen fibres at the bone-tendon interface are conducted by woven bone formation. J. Orthopaedic Research. 19:2001;873-880
    • (2001) J. Orthopaedic Research , vol.19 , pp. 873-880
    • Oguma, H.1    Murakami, G.2    Takahashi-Iwanaga, H.3    Aoki, M.4    Ishii, S.5
  • 85
    • 0034651554 scopus 로고    scopus 로고
    • The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen
    • Orgel J.P., Wess T.J., Miller A. The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen. Struct. Fold. Des. 8:2000;137-142
    • (2000) Struct. Fold. Des. , vol.8 , pp. 137-142
    • Orgel, J.P.1    Wess, T.J.2    Miller, A.3
  • 87
    • 0034326762 scopus 로고    scopus 로고
    • A model for type II collagen fibrils: Distinctive D-band patterns in native and reconstituted fibrils compared with sequence data for helix and telopeptide domains
    • Ortolani F., Giordano M., Marchini M. A model for type II collagen fibrils: Distinctive D-band patterns in native and reconstituted fibrils compared with sequence data for helix and telopeptide domains. Biopolymers. 54:2000;448-463
    • (2000) Biopolymers , vol.54 , pp. 448-463
    • Ortolani, F.1    Giordano, M.2    Marchini, M.3
  • 88
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • Ottani V., Raspanti M., Ruggeri A. Collagen structure and functional implications. Micron. 32:2001;251-260
    • (2001) Micron , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 89
    • 0023918370 scopus 로고
    • Type-I collagen α-1chain C-telopeptide - Solution structure determined by 600 MHz proton NMR spectroscopy and implications for its role in collagen fibrillogenesis
    • Otter A., Scott P.G., Kotovych G. Type-I collagen α-1chain C-telopeptide - Solution structure determined by 600 MHz proton NMR spectroscopy and implications for its role in collagen fibrillogenesis. Biochemistry. 27:1988;3560-3567
    • (1988) Biochemistry , vol.27 , pp. 3560-3567
    • Otter, A.1    Scott, P.G.2    Kotovych, G.3
  • 90
    • 0035218512 scopus 로고    scopus 로고
    • A study of fibrous long spacing collagen ultrastructure and assembly by atomic force microscopy
    • Paige M.F., Rainey J.K., Goh M.C. A study of fibrous long spacing collagen ultrastructure and assembly by atomic force microscopy. Micron. 32:2001;341-353
    • (2001) Micron , vol.32 , pp. 341-353
    • Paige, M.F.1    Rainey, J.K.2    Goh, M.C.3
  • 91
    • 0028964849 scopus 로고
    • Simple physical model of collagen fibrillogenesis based on diffusion-limited aggregation
    • Parkinson J., Kadler K.E., Brass A. Simple physical model of collagen fibrillogenesis based on diffusion-limited aggregation. J. Mol. Biol. 247:1995;823-831
    • (1995) J. Mol. Biol. , vol.247 , pp. 823-831
    • Parkinson, J.1    Kadler, K.E.2    Brass, A.3
  • 92
    • 0018219823 scopus 로고
    • A comparison of the size distribution of collagen fibrils in connective tissues as a function of age and a possible relationship between fibril size distribution and mechanical properties
    • Parry D.A.D., Barnes G.R.G., Craig A.S. A comparison of the size distribution of collagen fibrils in connective tissues as a function of age and a possible relationship between fibril size distribution and mechanical properties. Proc. Roy. Soc. Lond. B. 203:1978;305-321
    • (1978) Proc. Roy. Soc. Lond. B. , vol.203 , pp. 305-321
    • Parry, D.A.D.1    Barnes, G.R.G.2    Craig, A.S.3
  • 93
    • 0018614292 scopus 로고
    • Electron microscope evidence for an 80 Angstrom unit in collagen fibrils
    • Parry D.A.D., Craig A.S. Electron microscope evidence for an 80 Angstrom unit in collagen fibrils. Nature. 282:1979;213-225
    • (1979) Nature , vol.282 , pp. 213-225
    • Parry, D.A.D.1    Craig, A.S.2
  • 94
    • 0002458019 scopus 로고
    • Growth and Development of Collagen Fibrils in Connective Tissues
    • A. Ruggeri, & P.M. Motta. Netherlands: Martinus Nijhoff
    • Parry D.A.D., Craig A.S. Growth and Development of Collagen Fibrils in Connective Tissues. Ruggeri A., Motta P.M. "Ultrastructure of the Connective Tissue Matrix" 1984;34-64 Martinus Nijhoff, Netherlands
    • (1984) "ultrastructure of the Connective Tissue Matrix" , pp. 34-64
    • Parry, D.A.D.1    Craig, A.S.2
  • 95
    • 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
  • 96
    • 0031092125 scopus 로고    scopus 로고
    • Comparison of collagen fibril populations in the superficial digital flexor tendons of exercised and non-exercised thoroughbreds
    • Patterson-Kane J.C., Wilson A.M., Firth E.C., Parry D.A.D., Goodship A.E. Comparison of collagen fibril populations in the superficial digital flexor tendons of exercised and non-exercised thoroughbreds. Equine Vet. J. 29:1997;121-125
    • (1997) Equine Vet. J. , vol.29 , pp. 121-125
    • Patterson-Kane, J.C.1    Wilson, A.M.2    Firth, E.C.3    Parry, D.A.D.4    Goodship, A.E.5
  • 98
    • 3543123029 scopus 로고    scopus 로고
    • Histochemical and ultrastructural study of collagen fibers in mouse pubic symphysis during late pregnancy
    • Pinheiro M.C., Moraes S.G., Battlehner C.N., Caldini E.G., Toledo O.M.S., Joazeiro P.P. Histochemical and ultrastructural study of collagen fibers in mouse pubic symphysis during late pregnancy. Micron. 35:2004;685-693
    • (2004) Micron. , vol.35 , pp. 685-693
    • Pinheiro, M.C.1    Moraes, S.G.2    Battlehner, C.N.3    Caldini, E.G.4    Toledo, O.M.S.5    Joazeiro, P.P.6
  • 99
    • 0344787927 scopus 로고
    • Collagen formation by fibroblasts of the chick embryo dermis
    • Porter K.R., Pappas G.D. Collagen formation by fibroblasts of the chick embryo dermis. J. Biophysic. Biochem. Cytol. 5:1958;153-180
    • (1958) J. Biophysic. Biochem. Cytol. , vol.5 , pp. 153-180
    • Porter, K.R.1    Pappas, G.D.2
  • 100
    • 0002751244 scopus 로고
    • Assembly of collagen fibrils de novo from soluble precursors
    • P.D. Yurchenco, D.E. Birk, & R.P. Mecham. San Diego: Academic Press
    • Prockop D.J., Hulmes D.J.S. Assembly of collagen fibrils de novo from soluble precursors. Yurchenco P.D., Birk D.E., Mecham R.P. "Extracellular Matrix Assembly and Structure" 1994;47-90 Academic Press, San Diego
    • (1994) "extracellular Matrix Assembly and Structure" , pp. 47-90
    • Prockop, D.J.1    Hulmes, D.J.S.2
  • 101
  • 102
    • 0141788733 scopus 로고    scopus 로고
    • Possible role of decorin glycosaminoglycans in fibril to fibril force transfer in relative mature tendons: A computational study from molecular to microstructural level
    • Redaelli A., Vesentini S., Soncini M., Vena P., Mantero S., Montevecchi F.M. Possible role of decorin glycosaminoglycans in fibril to fibril force transfer in relative mature tendons: A computational study from molecular to microstructural level. J. Biomech. 36:2003;1555-1569
    • (2003) J. Biomech. , vol.36 , pp. 1555-1569
    • Redaelli, A.1    Vesentini, S.2    Soncini, M.3    Vena, P.4    Mantero, S.5    Montevecchi, F.M.6
  • 103
    • 0023659221 scopus 로고
    • Comparative structural studies of reconstituted and native type I and type II collagen fibrils by low angle X-ray diffraction
    • Ronziere M-C., Berthet-Colominas C., Herbage D. Comparative structural studies of reconstituted and native type I and type II collagen fibrils by low angle X-ray diffraction. Biochim. Biophys. Acta. 916:1987;381-387
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 381-387
    • Ronziere, M.-C.1    Berthet-Colominas, C.2    Herbage, D.3
  • 104
    • 0345451117 scopus 로고    scopus 로고
    • Fourier analysis of electron micrographs of positively stained collagen fibrils: Application to type I and II collagen typing
    • Ronziere M-C., Herbage B., Herbage D., Bernengo J-C. Fourier analysis of electron micrographs of positively stained collagen fibrils: Application to type I and II collagen typing. Int. J. Biol. Macromol. 23:1998;207-213
    • (1998) Int. J. Biol. Macromol. , vol.23 , pp. 207-213
    • Ronziere, M.-C.1    Herbage, B.2    Herbage, D.3    Bernengo, J.-C.4
  • 105
    • 0034763707 scopus 로고    scopus 로고
    • Collagen fibril diameters increase and fibril densities decrease in skin subjected to repetitive compressive and shear stresses
    • Sanders J.E., Goldstein B.S. Collagen fibril diameters increase and fibril densities decrease in skin subjected to repetitive compressive and shear stresses. J. Biomech. 34:2001;1581-1587
    • (2001) J. Biomech. , vol.34 , pp. 1581-1587
    • Sanders, J.E.1    Goldstein, B.S.2
  • 106
    • 0030246115 scopus 로고    scopus 로고
    • Elongation mechanism of collagen fibrils and force-strain relations of tendon at each level of structural hierarchy
    • Sasaki N., Odajima S. Elongation mechanism of collagen fibrils and force-strain relations of tendon at each level of structural hierarchy. J. Biomech. 29:1996;1131-1136
    • (1996) J. Biomech. , vol.29 , pp. 1131-1136
    • Sasaki, N.1    Odajima, S.2
  • 107
    • 0033106177 scopus 로고    scopus 로고
    • Time resolved X-ray diffraction from tendon collagen during creep using synchrotron radiation
    • Sasaki N., Shukunami N., Matsushima N., Izumi Y. Time resolved X-ray diffraction from tendon collagen during creep using synchrotron radiation. J. Biomech. 32:1999;285-292
    • (1999) J. Biomech. , vol.32 , pp. 285-292
    • Sasaki, N.1    Shukunami, N.2    Matsushima, N.3    Izumi, Y.4
  • 108
    • 0031826531 scopus 로고    scopus 로고
    • The structure of interfibrillar proteoglycan bridges ('shape modules') in extracellular matrix of fibrous connective tissues and their stability in various chemical environments
    • Scott J.E., Thomlinson A.M. The structure of interfibrillar proteoglycan bridges ('shape modules') in extracellular matrix of fibrous connective tissues and their stability in various chemical environments. J. Anat. 192:1998;391-405
    • (1998) J. Anat. , vol.192 , pp. 391-405
    • Scott, J.E.1    Thomlinson, A.M.2
  • 109
    • 0035155477 scopus 로고    scopus 로고
    • Transition from viscous to elastic-based dependency of mechanical properties of self-assembled type I collagen fibers
    • Silver F.H., Christiansen D.L., Snowhill P.B., Chen Y. Transition from viscous to elastic-based dependency of mechanical properties of self-assembled type I collagen fibers. J. Appl. Polymer Sci. 79:2001;134-142
    • (2001) J. Appl. Polymer Sci. , vol.79 , pp. 134-142
    • Silver, F.H.1    Christiansen, D.L.2    Snowhill, P.B.3    Chen, Y.4
  • 111
    • 0014412958 scopus 로고
    • Molecular pattern in native collagen
    • Smith J.W. Molecular pattern in native collagen. Nature. 219:1968;157-158
    • (1968) Nature , vol.219 , pp. 157-158
    • Smith, J.W.1
  • 112
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered Lumican deposition in tendon
    • Svensson L., Aszodi A., Reinholt F.P., Fassler R., Heinegard D., Oldberg A. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered Lumican deposition in tendon. J. Biol. Chem. 274:1999;9636-9647
    • (1999) J. Biol. Chem. , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fassler, R.4    Heinegard, D.5    Oldberg, A.6
  • 113
    • 0018947124 scopus 로고
    • Compressed microfibril models of the native collagen fibril
    • Trus B.L., Piez K.A. Compressed microfibril models of the native collagen fibril. Nature. 286:1980;300-301
    • (1980) Nature , vol.286 , pp. 300-301
    • Trus, B.L.1    Piez, K.A.2
  • 116
    • 0028904399 scopus 로고
    • Structure of the type-I collagen molecule based on conformational energy computations: The triple-stranded helix and the N-terminal telopeptide
    • Vitagliano L., Nemethy G., Zagari A., Scheraga H.A. Structure of the type-I collagen molecule based on conformational energy computations: The triple-stranded helix and the N-terminal telopeptide. J. Mol. Biol. 247:1995;69-80
    • (1995) J. Mol. Biol. , vol.247 , pp. 69-80
    • Vitagliano, L.1    Nemethy, G.2    Zagari, A.3    Scheraga, H.A.4
  • 118
    • 0842330464 scopus 로고    scopus 로고
    • AFM nanodissection reveals internal structural details of single collagen fibrils
    • Wen C.K., Goh M.C. AFM nanodissection reveals internal structural details of single collagen fibrils. Nano. Lett. 4:2004;129-132
    • (2004) Nano. Lett. , vol.4 , pp. 129-132
    • Wen, C.K.1    Goh, M.C.2
  • 119
    • 0029023803 scopus 로고
    • Type I collagen packing conformation of the triclinic unit cell
    • Wess T.J., Hammersley A., Wess L., Miller A. Type I collagen packing conformation of the triclinic unit cell. J. Mol. Biol. 248:1995;487-493
    • (1995) J. Mol. Biol. , vol.248 , pp. 487-493
    • Wess, T.J.1    Hammersley, A.2    Wess, L.3    Miller, A.4
  • 120
    • 0031658373 scopus 로고    scopus 로고
    • A consensus model for molecular packing of type I collagen
    • Wess T.J., Hammersley A.P., Wess L., Miller A. A consensus model for molecular packing of type I collagen. J. Struct. Biol. 122:1998;92-100
    • (1998) J. Struct. Biol. , vol.122 , pp. 92-100
    • Wess, T.J.1    Hammersley, A.P.2    Wess, L.3    Miller, A.4
  • 122
    • 0031413563 scopus 로고    scopus 로고
    • Organization of fibrillar collagen in the human and bovine cornea: Collagen types V and III
    • White J., Werkmeister J.A., Ramshaw J.A.M., Birk D.E. Organization of fibrillar collagen in the human and bovine cornea: Collagen types V and III. Connect. Tissue Res. 36:1997;165-174
    • (1997) Connect. Tissue Res. , vol.36 , pp. 165-174
    • White, J.1    Werkmeister, J.A.2    Ramshaw, J.A.M.3    Birk, D.E.4
  • 123
    • 0026478423 scopus 로고
    • Bundle formation of principal fibers in rat molars
    • Yamamoto T., Wakita M. Bundle formation of principal fibers in rat molars. J. Periodont. Res. 27:1992;20-27
    • (1992) J. Periodont. Res. , vol.27 , pp. 20-27
    • Yamamoto, T.1    Wakita, M.2
  • 124
    • 0033910740 scopus 로고    scopus 로고
    • The subfibrillar arrangement of corneal and scleral collagen fibrils as revealed by scanning electron and atomic force microscopy
    • Yamamoto S., Hashizume H., Hitomi J., Shigeno M., Sawaguchi S., Abe H., Ushiki T. The subfibrillar arrangement of corneal and scleral collagen fibrils as revealed by scanning electron and atomic force microscopy. Arch. Histol. Cytol. 63:2000a;127-135
    • (2000) Arch. Histol. Cytol. , vol.63 , pp. 127-135
    • Yamamoto, S.1    Hashizume, H.2    Hitomi, J.3    Shigeno, M.4    Sawaguchi, S.5    Abe, H.6    Ushiki, T.7
  • 125
    • 0034047746 scopus 로고    scopus 로고
    • Twisted plywood structure of an alternating lamellar pattern in cellular cementum of human teeth
    • Yamamoto T., Domon T., Takahashi S., Islam N., Suzuki R. Twisted plywood structure of an alternating lamellar pattern in cellular cementum of human teeth. Anat. Embryol. 202:2000b;25-30
    • (2000) Anat. Embryol. , vol.202 , pp. 25-30
    • Yamamoto, T.1    Domon, T.2    Takahashi, S.3    Islam, N.4    Suzuki, R.5
  • 126
    • 0034097273 scopus 로고    scopus 로고
    • Immunolocalization of collagen types II and III in single fibrils of human articular cartilage
    • Young R.D., Lawrence P.A., Duance V.C., Aigner T., Monaghan P. Immunolocalization of collagen types II and III in single fibrils of human articular cartilage. J. Histochem. Cytochem. 48:2000a;423-432
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 423-432
    • Young, R.D.1    Lawrence, P.A.2    Duance, V.C.3    Aigner, T.4    Monaghan, P.5
  • 127
    • 0034126336 scopus 로고    scopus 로고
    • Expression of type XIV collagen in developing chicken tendons: Association with assembly and growth of collagen fibrils
    • Young B.B., Gordon M.K., Birk D.E. Expression of type XIV collagen in developing chicken tendons: Association with assembly and growth of collagen fibrils. Dev. Dyn. 217:2000b;430-439
    • (2000) Dev. Dyn. , vol.217 , pp. 430-439
    • Young, B.B.1    Gordon, M.K.2    Birk, D.E.3


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