메뉴 건너뛰기




Volumn 270, Issue 2, 1997, Pages 275-284

Altered collagen structure in mouse tail tendon lacking the α2(I) chain

Author keywords

Collagen; Homotrimer; Osteogenesis imperfecta; Tail tendon; X ray diffraction

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 1;

EID: 0342460605     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1106     Document Type: Article
Times cited : (105)

References (35)
  • 1
    • 0020010987 scopus 로고
    • Characterization of fibrous forms of collagen
    • Brodsky B., Eikenberry E. F. Characterization of fibrous forms of collagen. Methods Enzymol. 82:1982;127-174.
    • (1982) Methods Enzymol. , vol.82 , pp. 127-174
    • Brodsky, B.1    Eikenberry, E.F.2
  • 6
    • 0019880195 scopus 로고
    • Proteolytic enzymes as probes for the triple-helical conformation of procollagen
    • Bruckner P., Prockop D. J. Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal. Biochem. 110:1981;360-368.
    • (1981) Anal. Biochem. , vol.110 , pp. 360-368
    • Bruckner, P.1    Prockop, D.J.2
  • 7
    • 0017137267 scopus 로고
    • Preparation of intact monomeric collagen from rat tail tendon and skin and the structure of the nonhelical ends in solution
    • Chandrakasan G., Torchia D. A., Piez K. A. Preparation of intact monomeric collagen from rat tail tendon and skin and the structure of the nonhelical ends in solution. J. Biol. Chem. 251:1976;6062-6067.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6062-6067
    • Chandrakasan, G.1    Torchia, D.A.2    Piez, K.A.3
  • 9
    • 0021925282 scopus 로고
    • Altered helical structure of a homotrimer of α1(I) chains synthesized by fibroblasts from a variant of osteogenesis imperfecta
    • Deak S. B., Van der Rest M., Prockop D. J. Altered helical structure of a homotrimer of α1(I) chains synthesized by fibroblasts from a variant of osteogenesis imperfecta. Coll. Rel. Res. 5:1985;305-313.
    • (1985) Coll. Rel. Res. , vol.5 , pp. 305-313
    • Deak, S.B.1    Van der Rest, M.2    Prockop, D.J.3
  • 10
    • 0343218318 scopus 로고
    • Absence of the collagen α2(I) chain diminishes mechanical properties of bone
    • Dunn M. G., McBride D. J., Shapiro J. R. Absence of the collagen α2(I) chain diminishes mechanical properties of bone. Trans. Orthop. Res. Soc. 20:1995;153.
    • (1995) Trans. Orthop. Res. Soc. , vol.20 , pp. 153
    • Dunn, M.G.1    McBride, D.J.2    Shapiro, J.R.3
  • 13
    • 0020545965 scopus 로고
    • Molecular conformation and packing in collagen fibrils
    • Fraser R. D., MacRae T. P., Miller A., Suzuki E. Molecular conformation and packing in collagen fibrils. J. Mol. Biol. 167:1983;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
  • 14
    • 0030033534 scopus 로고    scopus 로고
    • Bone mineralization in an osteogenesis imperfecta mouse model studied by small-angle X-ray scattering
    • Fratzl P., Paris O., Klaushofer K., Landis W. J. Bone mineralization in an osteogenesis imperfecta mouse model studied by small-angle X-ray scattering. J. Clin. Invest. 97:1996;396-402.
    • (1996) J. Clin. Invest. , vol.97 , pp. 396-402
    • Fratzl, P.1    Paris, O.2    Klaushofer, K.3    Landis, W.J.4
  • 15
    • 0027292705 scopus 로고
    • Expression of human COL1A1 gene in stably transfected HT 1080 cells, The production of a thermostable homotrimer of type I collagen in a recombinant system
    • Geddis A. E., Prockop D. J. Expression of human COL1A1 gene in stably transfected HT 1080 cells, The production of a thermostable homotrimer of type I collagen in a recombinant system. Matrix. 13:1993;399-405.
    • (1993) Matrix , vol.13 , pp. 399-405
    • Geddis, A.E.1    Prockop, D.J.2
  • 16
    • 0018068793 scopus 로고
    • The role of polar and hydrophobic interactions for the molecular packing of type I collagen. A three-dimensional evaluation of the amino acid sequence
    • Hofmann H., Fietzek P. P., Kühn K. The role of polar and hydrophobic interactions for the molecular packing of type I collagen. A three-dimensional evaluation of the amino acid sequence. J. Mol. Biol. 125:1978;137-165.
    • (1978) J. Mol. Biol. , vol.125 , pp. 137-165
    • Hofmann, H.1    Fietzek, P.P.2    Kühn, K.3
  • 17
    • 0018884576 scopus 로고
    • Comparative analysis of the sequences of the three collagen chains, α1(I), α2 and α1(III). Functional and genetic aspects
    • Hofmann H., Fietzek P. P., Kühn K. Comparative analysis of the sequences of the three collagen chains, α1(I), α2 and α1(III). Functional 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    Kühn, K.3
  • 18
    • 0026740073 scopus 로고
    • The collagen superfamily-diverse structures and assemblies
    • Hulmes D. J. The collagen superfamily-diverse structures and assemblies. Essays Biochem. 27:1992;49-67.
    • (1992) Essays Biochem. , vol.27 , pp. 49-67
    • Hulmes, D.J.1
  • 19
    • 0017329109 scopus 로고
    • Interpretation of the meridional X-ray 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 X-ray 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
  • 20
    • 0028679665 scopus 로고
    • Extracellular matrix 1: Fibril-forming collagens
    • Kadler K. Extracellular matrix 1: fibril-forming collagens. Protein Profile. 1:1994;542-545.
    • (1994) Protein Profile , vol.1 , pp. 542-545
    • Kadler, K.1
  • 21
    • 0001166951 scopus 로고
    • A formaldehyde-glutaraldehyde fixative of high osmolality for use in electron microscopy
    • Karnovsky M. J. A formaldehyde-glutaraldehyde fixative of high osmolality for use in electron microscopy. J. Cell Biol. 27:1965;137A.
    • (1965) J. Cell Biol. , vol.27
    • Karnovsky, M.J.1
  • 24
    • 0019941196 scopus 로고
    • Relationship between amino acid sequence and higher structures of collagen
    • Kühn K. Relationship between amino acid sequence and higher structures of collagen. Connect. Tissue Res. 10:1982;5-10.
    • (1982) Connect. Tissue Res. , vol.10 , pp. 5-10
    • Kühn, K.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0000990149 scopus 로고
    • The characterization of collagen from the skin of the dogfish shark, Squalus acanthias
    • Lewis M. S., Piez K. A. The characterization of collagen from the skin of the dogfish shark, Squalus acanthias. J. Biol. Chem. 239:1964;3336-3340.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3336-3340
    • Lewis, M.S.1    Piez, K.A.2
  • 27
    • 0002407338 scopus 로고
    • Ultrastructural aspects of freeze-etched collagen fibrils
    • A. Ruggeri, & P. M. Motta. Boston: Martinus Nijhoff
    • Marchini M., Ruggeri A. Ultrastructural aspects of freeze-etched collagen fibrils. Ruggeri A., Motta P. M. Ultrastructure of the Connective Tissue Matrix. 1984;Martinus Nijhoff, Boston.
    • (1984) Ultrastructure of the Connective Tissue Matrix
    • Marchini, M.1    Ruggeri, A.2
  • 28
    • 0028181672 scopus 로고
    • Confirmation of a G nucleotide deletion in the Cola-2 gene of mice with the osteogenesis imperfecta mutation
    • McBride D. J., Shapiro J. R. Confirmation of a G nucleotide deletion in the Cola-2 gene of mice with the osteogenesis imperfecta mutation. Genomics. 20:1994;135-137.
    • (1994) Genomics , vol.20 , pp. 135-137
    • McBride, D.J.1    Shapiro, J.R.2
  • 29
    • 0026795775 scopus 로고
    • Self-assembly into fibrils of a homotrimer of type I collagen. Thermodynamic parameters demonstrate that the α2(I) chain is required for the efficient self-assembly of fibrils
    • McBride D. J., Kadler K. E., Hojima Y., Prockop D. J. Self-assembly into fibrils of a homotrimer of type I collagen. Thermodynamic parameters demonstrate that the α2(I) chain is required for the efficient self-assembly of fibrils. Matrix. 12:1992;256-263.
    • (1992) Matrix , vol.12 , pp. 256-263
    • McBride, D.J.1    Kadler, K.E.2    Hojima, Y.3    Prockop, D.J.4
  • 30
    • 0003044268 scopus 로고
    • Molecular packing in collagen fibrils
    • G. N. Ramachandran, & A. H. Reddi. New York: Plenum Press
    • Miller A. Molecular packing in collagen fibrils. Ramachandran G. N., Reddi A. H. Biochemistry of Collagen. 1976;Plenum Press, New York.
    • (1976) Biochemistry of Collagen
    • Miller, A.1
  • 33
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop D. J., Kivirriko K. I. Collagens: molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem. 64:1995;403-434.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirriko, K.I.2
  • 35
    • 0014470466 scopus 로고
    • The formation of triple-helical collagen molecules from α1 or α2 polypeptide chains
    • Tkocz C., Kühn K. The formation of triple-helical collagen molecules from α1 or α2 polypeptide chains. Eur. J. Biochem. 7:1969;454-462.
    • (1969) Eur. J. Biochem. , vol.7 , pp. 454-462
    • Tkocz, C.1    Kühn, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.