메뉴 건너뛰기




Volumn 84, Issue 4, 2003, Pages 2593-2598

Evidence that collagen fibrils in tendons are inhomogeneously structured in a tubelike manner

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN FIBER;

EID: 0037380983     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)75064-4     Document Type: Article
Times cited : (111)

References (31)
  • 1
    • 0000021064 scopus 로고
    • Long x-ray diffraction spacings of collagen
    • Bear, R. S. 1942. Long x-ray diffraction spacings of collagen. J. Am. Chem. Soc. 64:727-729.
    • (1942) J. Am. Chem. Soc. , vol.64 , pp. 727-729
    • Bear, R.S.1
  • 2
    • 0034464381 scopus 로고    scopus 로고
    • A transmission electron microscope study using vitrified ice sections of predentin: Structural changes in the dentin collagenous matrix prior to mineralization
    • Beniash, E., W. Traub, A. Veis, and S. Weiner. 2000. A transmission electron microscope study using vitrified ice sections of predentin: structural changes in the dentin collagenous matrix prior to mineralization. J. Struct. Biol. 132:212-225.
    • (2000) J. Struct. Biol. , vol.132 , pp. 212-225
    • Beniash, E.1    Traub, W.2    Veis, A.3    Weiner, S.4
  • 3
    • 0031149719 scopus 로고    scopus 로고
    • In vitro calcified tendon collagen: An atomic force and scanning electron microscopy investigation
    • Bigi, A., M. Gandolfi, N. Roveri, and G. Valdre. 1997. In vitro calcified tendon collagen: an atomic force and scanning electron microscopy investigation. Biomaterials. 18:657-665.
    • (1997) Biomaterials , vol.18 , pp. 657-665
    • Bigi, A.1    Gandolfi, M.2    Roveri, N.3    Valdre, G.4
  • 5
    • 0002773858 scopus 로고
    • Electron microscopy of the collagen fibril
    • A. Ruggeri and P. M. Motto, editors. Martinus Nijhoff, Boston
    • Chapman, J. A., and D. J. S. Hulmes. 1984. Electron microscopy of the collagen fibril. In Ultrastructure of the Connective Tissue Matrix. A. Ruggeri and P. M. Motto, editors. Martinus Nijhoff, Boston. 1-33.
    • (1984) Ultrastructure of the Connective Tissue Matrix , pp. 1-33
    • Chapman, J.A.1    Hulmes, D.J.S.2
  • 6
    • 84957349865 scopus 로고
    • Atomic force microscope images of collagen fibers
    • Chernoff, E. A. G., and D. A. Chernoff. 1992. Atomic force microscope images of collagen fibers. J. Vac. Sci. Technol. A. 10:596-599.
    • (1992) J. Vac. Sci. Technol. A , vol.10 , pp. 596-599
    • Chernoff, E.A.G.1    Chernoff, D.A.2
  • 7
    • 0032534706 scopus 로고    scopus 로고
    • Moisture-dependent renaturation of collagen in phosphoric acid etched human dentin
    • El Feninat, F., T. H. Ellis, E. Sacher, and I. Stangel. 1998. Moisture-dependent renaturation of collagen in phosphoric acid etched human dentin. J. Biomed. Mater. Res. 42:549-553.
    • (1998) J. Biomed. Mater. Res. , vol.42 , pp. 549-553
    • El Feninat, F.1    Ellis, T.H.2    Sacher, E.3    Stangel, I.4
  • 8
    • 0027352739 scopus 로고
    • Ultrastructural evidences of a distinct axial domain within native rat tail tendon collagen fibrils
    • Franc, S. 1993. Ultrastructural evidences of a distinct axial domain within native rat tail tendon collagen fibrils. J. Submicrosc. Cytol. Pathol. 25:85-91.
    • (1993) J. Submicrosc. Cytol. Pathol. , vol.25 , pp. 85-91
    • Franc, S.1
  • 9
    • 0020545965 scopus 로고
    • Molecular conformation and packing in collagen fibrils
    • Fraser, R. D., T. P. MacRae, A. Miller, and E. Suzuki. 1983. Molecular conformation and packing in collagen fibrils. J. Mol. Biol. 167:497-521.
    • (1983) J. Mol. Biol. , vol.167 , pp. 497-521
    • Fraser, R.D.1    MacRae, T.P.2    Miller, A.3    Suzuki, E.4
  • 10
    • 0027475398 scopus 로고
    • Collagen packing and mineralization. An x-ray scattering investigation of turkey leg tendon
    • Fratzl, P., N. Fratzl-Zelman, and K. Klaushofer. 1993. Collagen packing and mineralization. An x-ray scattering investigation of turkey leg tendon. Biophys. J. 64:260-266.
    • (1993) Biophys. J. , vol.64 , pp. 260-266
    • Fratzl, P.1    Fratzl-Zelman, N.2    Klaushofer, K.3
  • 12
    • 0028910961 scopus 로고
    • Radial packing, order, and disorder in collagen fibrils
    • Hulmes, D. J., T. J. Wess, D. J. Prockop, and P. Fratzl. 1995. Radial packing, order, and disorder in collagen fibrils. Biophys. J. 68:1661-1670.
    • (1995) Biophys. J. , vol.68 , pp. 1661-1670
    • Hulmes, D.J.1    Wess, T.J.2    Prockop, D.J.3    Fratzl, P.4
  • 13
    • 0028679665 scopus 로고
    • Extracellular Matrix 1: Fibril forming collagens
    • Kadler, K. 1994. Extracellular Matrix 1: fibril forming collagens. Prot. Profile. 1:519-638.
    • (1994) Prot. Profile , vol.1 , pp. 519-638
    • Kadler, K.1
  • 14
    • 0022607621 scopus 로고
    • Preservation of polygonal sections and internal domains by quick-freezing of collagen fibrils
    • Mallein-Gerin, F., and R. Garrone. 1986. Preservation of polygonal sections and internal domains by quick-freezing of collagen fibrils. J. Biol. Macromol. 8:121-124.
    • (1986) J. Biol. Macromol. , vol.8 , pp. 121-124
    • Mallein-Gerin, F.1    Garrone, R.2
  • 16
    • 0000663180 scopus 로고
    • Structural units in collagen fibrils
    • North, A. C. T., P. M. Cowan, and J. T. Randall. 1954. Structural Units in Collagen Fibrils. Nature. 174:1142-1143.
    • (1954) Nature , vol.174 , pp. 1142-1143
    • North, A.C.T.1    Cowan, P.M.2    Randall, J.T.3
  • 17
    • 0035218934 scopus 로고    scopus 로고
    • Ultrastructure and assembly of segmental long spacing collagen studied by atomic force microscopy
    • Paige, M. F., and M. C. Goh. 2001. Ultrastructure and assembly of segmental long spacing collagen studied by atomic force microscopy. Micron. 32:355-361.
    • (2001) Micron. , vol.32 , pp. 355-361
    • Paige, M.F.1    Goh, M.C.2
  • 18
    • 0030935291 scopus 로고    scopus 로고
    • X-ray diffraction analysis of tendon collagen at ambient and cryogenic temperatures: Role of hydration
    • Price, R. I., S. Lees, and D. A. Kirschner. 1997. X-ray diffraction analysis of tendon collagen at ambient and cryogenic temperatures: role of hydration. Int. J. Biol. Macromol. 20:23-33.
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 23-33
    • Price, R.I.1    Lees, S.2    Kirschner, D.A.3
  • 19
    • 0031692465 scopus 로고    scopus 로고
    • The collagen fibril: The almost crystalline structure
    • Prockop, D. J., and A. Fertala. 1998. The collagen fibril: the almost crystalline structure. J. Struct. Biol. 122:111-118.
    • (1998) J. Struct. Biol. , vol.122 , pp. 111-118
    • Prockop, D.J.1    Fertala, A.2
  • 20
    • 0035197704 scopus 로고    scopus 로고
    • Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix
    • Raspanti, M., T. Congiu, and S. Guizzardi. 2001. Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix. Matrix Biol. 20:601-604.
    • (2001) Matrix Biol. , vol.20 , pp. 601-604
    • Raspanti, M.1    Congiu, T.2    Guizzardi, S.3
  • 21
    • 0028223671 scopus 로고
    • Atomic force microscopy study of the collagen fibre structure
    • Revenko, I., F. Sommer, D. T. Minh, R. Garrone, and J. M. Franc. 1994. Atomic force microscopy study of the collagen fibre structure. Biol. Cell. 80:67-69.
    • (1994) Biol. Cell , vol.80 , pp. 67-69
    • Revenko, I.1    Sommer, F.2    Minh, D.T.3    Garrone, R.4    Franc, J.M.5
  • 22
    • 11944250146 scopus 로고
    • Atomic force microscopy
    • Rugar, D., and P. K. Hansma. 1990. Atomic force microscopy. Phys Today. 43:23-30.
    • (1990) Phys. Today , vol.43 , pp. 23-30
    • Rugar, D.1    Hansma, P.K.2
  • 23
    • 0023660998 scopus 로고
    • Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study
    • Sarkar, S. K., Y. Hiyama, C. H. Niu, P. E. Young, J. T. Gerig, and D. A. Torchia. 1987. Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study. Biochemistry. 26:6793-6800.
    • (1987) Biochemistry , vol.26 , pp. 6793-6800
    • Sarkar, S.K.1    Hiyama, Y.2    Niu, C.H.3    Young, P.E.4    Gerig, J.T.5    Torchia, D.A.6
  • 24
    • 0021802517 scopus 로고
    • Nanosecond fluctuations of the molecular backbone of collagen in hard and soft tissues: A carbon-13 nuclear magnetic resonance relaxation study
    • Sarkar, S. K., C. E. Sullivan, and D. A. Torchia. 1985. Nanosecond fluctuations of the molecular backbone of collagen in hard and soft tissues: a carbon-13 nuclear magnetic resonance relaxation study. Biochemistry. 24:2348-2354.
    • (1985) Biochemistry , vol.24 , pp. 2348-2354
    • Sarkar, S.K.1    Sullivan, C.E.2    Torchia, D.A.3
  • 25
    • 0002017332 scopus 로고
    • Electron microscopy investigations of the structure of collagens
    • Schmitt, F. D., C. E. Hall, and M. A. Jakns. 1942. Electron microscopy investigations of the structure of collagens. J. Cell. Comp. Physiol. 20:11-33.
    • (1942) J. Cell. Comp. Physiol. , vol.20 , pp. 11-33
    • Schmitt, F.D.1    Hall, C.E.2    Jakns, M.A.3
  • 26
    • 0025905878 scopus 로고
    • Proteoglycan: Collagen interactions in connective tissues. Ultrastructural, biochemical, functional and evolutionary aspects
    • Scott, J. E. 1991. Proteoglycan: collagen interactions in connective tissues. Ultrastructural, biochemical, functional and evolutionary aspects. Int. J. Biol. Macromol. 13:157-161.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 157-161
    • Scott, J.E.1
  • 30
    • 0000046457 scopus 로고
    • Solid state NMR studies of molecular motion in collagen fibrils
    • Trochia, D. A. 1982. Solid state NMR studies of molecular motion in collagen fibrils. Meth. Enzymol. 82:174-186.
    • (1982) Meth. Enzymol. , vol.82 , pp. 174-186
    • Trochia, D.A.1
  • 31
    • 0033135755 scopus 로고    scopus 로고
    • The role of collagen in the declining mechanical properties of aging human cortical bone
    • Zioupos, P., J. D. Currey, and A. J. Hamer. 1999. The role of collagen in the declining mechanical properties of aging human cortical bone. J. Biomed. Mater. Res. 45:108-116.
    • (1999) J. Biomed. Mater. Res. , vol.45 , pp. 108-116
    • Zioupos, P.1    Currey, J.D.2    Hamer, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.