메뉴 건너뛰기




Volumn 33, Issue 4, 1996, Pages 275-282

Thermal stabilization of collagen fibers by calcification

Author keywords

bone; calcium phosphate; calorimetry; Collagen; denaturation; hydroxyapdtite

Indexed keywords

COLLAGEN; MINERAL;

EID: 0030046726     PISSN: 03008207     EISSN: 16078438     Source Type: Journal    
DOI: 10.3109/03008209609028885     Document Type: Article
Times cited : (86)

References (15)
  • 1
    • 0022429081 scopus 로고
    • Neutron diffraction studies of collagen in fully mineralized bone
    • Bonar, L.C., Lees, S., and Mack, H.A. (1985) Neutron diffraction studies of collagen in fully mineralized bone. J. Mol. Biol. 181, 265-270.
    • (1985) J. Mol. Biol. , vol.181 , pp. 265-270
    • Bonar, L.C.1    Lees, S.2    MacK, H.A.3
  • 2
    • 0014839443 scopus 로고
    • Thermal denatuation of mineralized and dem¡nealized bone collagen
    • Bonar, L.C. and Glimche, M.J. (1978) Thermal denatuation of mineralized and dem¡nealized bone collagen. J. Ullrastrucl. Res. 32, 545-551.
    • (1978) J. Ullrastrucl. Res. , vol.32 , pp. 545-551
    • Bonar, L.C.1    Glimche, M.J.2
  • 5
    • 33745996622 scopus 로고
    • The determination of hydroxyproline in tissue and protein samples containing small proportions of this imine acid
    • Woessner, J.F., Jr. (1961) The determination of hydroxyproline in tissue and protein samples containing small proportions of this imine acid. Arch Biochem. Biophys. 93, 440-447.
    • (1961) Arch Biochem. Biophys. , vol.93 , pp. 440-447
    • Woessner Jr., J.F.1
  • 6
    • 0025637638 scopus 로고
    • Age-related thermal stability and susceptibility to proteolysis of rat bone collagen
    • Danielsen, C.C. (1990) Age-related thermal stability and susceptibility to proteolysis of rat bone collagen. Biochem. J. 272, 697-701.
    • (1990) Biochem. J. , vol.272 , pp. 697-701
    • Danielsen, C.C.1
  • 7
    • 0024265662 scopus 로고
    • The locations of collagens with different thermal stabilities in fibrils of bovine retic-ulardemis
    • Kronick, P.L., Maleeff, B. and Carroll, P. (1988) The locations of collagens with different thermal stabilities in fibrils of bovine retic-ulardemis. Conn. Tissue Res. 18, 123-134.
    • (1988) Conn. Tissue Res. , vol.18 , pp. 123-134
    • Kronick, P.L.1    Maleeff, B.2    Carroll, P.3
  • 8
    • 0026799229 scopus 로고
    • Origin of mineral crystal growth in collagen fibrils
    • Traub, W., Arad, T. and Weier, S. (1992) Origin of mineral crystal growth in collagen fibrils. Matrix, 12, 251-255.
    • (1992) Matrix , vol.12 , pp. 251-255
    • Traub, W.1    Arad, T.2    Weier, S.3
  • 9
    • 0014865103 scopus 로고
    • Calcium phosphate formation in vitro. II. Effects of environment on amorphous-crystalline transformation
    • Termine, J.D., Peckauskas, R.A. and Posne, A.S. (1970) Calcium phosphate formation in vitro. II. Effects of environment on amorphous-crystalline transformation. Arch. Biochem. Biophys. 140, 318-325.
    • (1970) Arch. Biochem. Biophys. , vol.140 , pp. 318-325
    • Termine, J.D.1    Peckauskas, R.A.2    Posne, A.S.3
  • 10
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • DOI 10.1021/bi00165a023
    • Lepock, J.R., Ritchie, K.P., Kolios, M.C., Rodal, A.M., Heinz, K.A. and Kruuv, J. (1992) Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry 31, 12706-12712. (Pubitemid 23016540)
    • (1992) Biochemistry , vol.31 , Issue.50 , pp. 12706-12712
    • Lepock, J.R.1    Ritchie, K.P.2    Kolios, M.C.3    Rodahl, A.M.4    Heinz, K.A.5    Kruuv, J.6
  • 11
    • 0025369268 scopus 로고
    • Glutaraldehyde cross-linking of the sheath-core structures in collagen fibrils of skin
    • DOI 10.1111/j.1749-6632.1990.tb17956.x
    • Kronick, P.L., Cooke, P. and Maleeff, B. (1990) Glutaraldehyde crosslinking of the sheath-core structures in collagen fibrils of skin. Proc. NYAcad. Sci. 580, 448-450. (Pubitemid 20170423)
    • (1990) Annals of the New York Academy of Sciences , vol.580 , pp. 448-450
    • Kronick, P.L.1    Cooke, P.2    Maleeff, B.3
  • 12
    • 9544229754 scopus 로고
    • New evidence on collagen texture in lamellar bone
    • Raspanti, M., Guzzardi, S. and Ruggeri, A. (1993) New evidence on collagen texture in lamellar bone. Eur. J. Histochem. 37, (Suppl. 3):47-48.
    • (1993) Eur. J. Histochem. , vol.37 , Issue.SUPPL. 3 , pp. 47-48
    • Raspanti, M.1    Guzzardi, S.2    Ruggeri, A.3
  • 13
    • 0018908666 scopus 로고
    • 2H NMR study of molecular motion in collagen fibrils
    • 2H NMR study of molecular motion in collagen fibrils. Nature, 284, 531-534. (Pubitemid 10070331)
    • (1980) Nature , vol.284 , Issue.5756 , pp. 531-534
    • Jelinski, L.W.1    Sullivan, C.E.2    Torchia, D.A.3
  • 14
    • 0026438457 scopus 로고
    • Growth of mineral crystals in turkey tendon collagen fibers
    • Traub, W., Aad, T. and Weiner, S. (1992) Growth of mineral crystals in turkey tendon collagen fibers. Conn. Tissue Res. 28, 99-111.
    • (1992) Conn. Tissue Res. , vol.28 , pp. 99-111
    • Traub, W.1    Aad, T.2    Weiner, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.