메뉴 건너뛰기




Volumn 97, Issue 3, 2015, Pages 229-240

The Role of Collagen Organization on the Properties of Bone

Author keywords

Bone matrix; Bone strength; Collagen organization; Osteogenesis imperfecta; Osteoporosis; Paget s disease; Type I collagen homotrimer

Indexed keywords

BIOLOGICAL MARKER; BISPHOSPHONIC ACID DERIVATIVE; CARBOXY TERMINAL TELOPEPTIDE; COLLAGEN; COLLAGEN TYPE 1; HYDROXYAPATITE; PARATHYROID HORMONE; RALOXIFENE; TELOPEPTIDE;

EID: 84938744080     PISSN: 0171967X     EISSN: 14320827     Source Type: Journal    
DOI: 10.1007/s00223-015-9996-2     Document Type: Article
Times cited : (110)

References (87)
  • 2
    • 25444438208 scopus 로고    scopus 로고
    • Identification of osteopenic women at high risk of fracture: the OFELY Study
    • PID: 16160738
    • Sornay-Rendu E, Munoz F, Garnero P, Duboeuf F, Delmas PD (2005) Identification of osteopenic women at high risk of fracture: the OFELY Study. J Bone Miner Res 20:1813–1819
    • (2005) J Bone Miner Res , vol.20 , pp. 1813-1819
    • Sornay-Rendu, E.1    Munoz, F.2    Garnero, P.3    Duboeuf, F.4    Delmas, P.D.5
  • 3
    • 28544444873 scopus 로고    scopus 로고
    • Effect of ultrastructural changes on the toughness of bone
    • Nyman JS, Reyes M, Wang X (2005) Effect of ultrastructural changes on the toughness of bone. Micron 35:566–582
    • (2005) Micron , vol.35 , pp. 566-582
    • Nyman, J.S.1    Reyes, M.2    Wang, X.3
  • 4
    • 34248353121 scopus 로고    scopus 로고
    • Age-related factors affecting the postyield energy dissipation of human cortical bone
    • PID: 17266142
    • Nyman JS, Roy A, Tyler JH, Acuna RL, Gayle HJ, Wang X (2007) Age-related factors affecting the postyield energy dissipation of human cortical bone. J Orthop Res 25:646–655
    • (2007) J Orthop Res , vol.25 , pp. 646-655
    • Nyman, J.S.1    Roy, A.2    Tyler, J.H.3    Acuna, R.L.4    Gayle, H.J.5    Wang, X.6
  • 5
    • 0035217548 scopus 로고    scopus 로고
    • The role of collagen in determining bone mechanical properties
    • COI: 1:STN:280:DC%2BD38%2FlsFCkug%3D%3D, PID: 11781000
    • Wang X, Bank RA, Tekoppele JM, Agrawal CM (2001) The role of collagen in determining bone mechanical properties. J Orthop Res 19:1021–1026
    • (2001) J Orthop Res , vol.19 , pp. 1021-1026
    • Wang, X.1    Bank, R.A.2    Tekoppele, J.M.3    Agrawal, C.M.4
  • 6
    • 78049437472 scopus 로고    scopus 로고
    • Effects of three different preservation methods on the mechanical properties of human and bovine cortical bone
    • COI: 1:CAS:528:DC%2BC3cXhtlKlsrvK, PID: 20736094
    • Stefan U, Michael B, Werner S (2010) Effects of three different preservation methods on the mechanical properties of human and bovine cortical bone. Bone 47:1048–1053
    • (2010) Bone , vol.47 , pp. 1048-1053
    • Stefan, U.1    Michael, B.2    Werner, S.3
  • 7
    • 0031039779 scopus 로고    scopus 로고
    • Effects of ionizing radiation on the mechanical properties of human bone
    • COI: 1:STN:280:DyaK2s3hvFagtg%3D%3D, PID: 9066534
    • Currey JD, Foreman J, Laketic I, Mitchell J, Pegg DE, Reilly GC (1997) Effects of ionizing radiation on the mechanical properties of human bone. J Orthop Res 15:111–117
    • (1997) J Orthop Res , vol.15 , pp. 111-117
    • Currey, J.D.1    Foreman, J.2    Laketic, I.3    Mitchell, J.4    Pegg, D.E.5    Reilly, G.C.6
  • 8
    • 77953024895 scopus 로고    scopus 로고
    • On the effect of X-ray irradiation on the deformation and fracture behavior of human cortical bone
    • PID: 20206724
    • Barth HD, Launey ME, Macdowell AA, Ager JW 3rd, Ritchie RO (2010) On the effect of X-ray irradiation on the deformation and fracture behavior of human cortical bone. Bone 46:1475–1485
    • (2010) Bone , vol.46 , pp. 1475-1485
    • Barth, H.D.1    Launey, M.E.2    Macdowell, A.A.3    Ager, J.W.4    Ritchie, R.O.5
  • 9
    • 84893371164 scopus 로고    scopus 로고
    • Bone embrittlement and collagen modifications due to high—dose gamma-irradiation sterilization
    • COI: 1:CAS:528:DC%2BC2cXjvFWhsLo%3D, PID: 24440514
    • Burton B, Gaspar A, Josey D, Tupy J, Grynpas MD, Willet T (2014) Bone embrittlement and collagen modifications due to high—dose gamma-irradiation sterilization. Bone 61:71–81
    • (2014) Bone , vol.61 , pp. 71-81
    • Burton, B.1    Gaspar, A.2    Josey, D.3    Tupy, J.4    Grynpas, M.D.5    Willet, T.6
  • 10
    • 84865745554 scopus 로고    scopus 로고
    • Effects of bone matrix proteins on fracture and fragility in osteoporosis
    • Stroga GE, Vashishth D (2012) Effects of bone matrix proteins on fracture and fragility in osteoporosis. Curr Osteoporos Rep 10:141–150
    • (2012) Curr Osteoporos Rep , vol.10 , pp. 141-150
    • Stroga, G.E.1    Vashishth, D.2
  • 11
    • 0024809327 scopus 로고
    • Bone type V collagen: chain composition and location of a trypsin cleavage site
    • COI: 1:STN:280:DyaK3c7isFKguw%3D%3D, PID: 2612158
    • Niyibizi C, Eyre DR (1989) Bone type V collagen: chain composition and location of a trypsin cleavage site. Connect Tissue Res 20:247–250
    • (1989) Connect Tissue Res , vol.20 , pp. 247-250
    • Niyibizi, C.1    Eyre, D.R.2
  • 12
    • 0003133288 scopus 로고
    • Fibrillar collagens: their biosynthesis, molecular structure, and mode of assembly
    • Zern MA, Reid LM, (eds), Marcel Dekker Inc., New York
    • Nimni ME (1993) Fibrillar collagens: their biosynthesis, molecular structure, and mode of assembly. In: Zern MA, Reid LM (eds) Extracellular matrix: chemistry, biology, and pathobiology with emphasis on the liver. Marcel Dekker Inc., New York, pp 121–148
    • (1993) Extracellular matrix: chemistry, biology, and pathobiology with emphasis on the liver , pp. 121-148
    • Nimni, M.E.1
  • 13
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • COI: 1:CAS:528:DyaE3sXktFCksb8%3D, PID: 4712181
    • Berg RA, Prockop DJ (1973) The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem Biophys Res Commun 52:115–120
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 14
    • 0016720469 scopus 로고
    • Studies on the glycosylation of hydroxylysine residues during collagen biosynthesis and the subcellular localization of collagen galactosyltransferase and collagen glucosyltransferase in tendon and cartilage cells
    • COI: 1:CAS:528:DyaE28Xls1OnsA%3D%3D, PID: 1220686
    • Harwood R, Grant ME, Jackson DS (1975) Studies on the glycosylation of hydroxylysine residues during collagen biosynthesis and the subcellular localization of collagen galactosyltransferase and collagen glucosyltransferase in tendon and cartilage cells. Biochem J 152:291–302
    • (1975) Biochem J , vol.152 , pp. 291-302
    • Harwood, R.1    Grant, M.E.2    Jackson, D.S.3
  • 15
    • 0035057739 scopus 로고    scopus 로고
    • Urinary excretion of glucosyl-galactosyl pyridinoline: a specific biochemical marker of synovium degradation
    • COI: 1:CAS:528:DC%2BD3MXjtVOgt7k%3D
    • Gineyts E, Garnero P, Delmas PD (2001) Urinary excretion of glucosyl-galactosyl pyridinoline: a specific biochemical marker of synovium degradation. Rheumatology (Oxford) 40:315–323
    • (2001) Rheumatology (Oxford) , vol.40 , pp. 315-323
    • Gineyts, E.1    Garnero, P.2    Delmas, P.D.3
  • 16
    • 0015231790 scopus 로고
    • Human collagens: differences in glycosylated hydroxylysines in skin and bone
    • COI: 1:CAS:528:DyaE3MXntFOjug%3D%3D, PID: 5101159
    • Pinnell SR, Fox R, Krane SM (1971) Human collagens: differences in glycosylated hydroxylysines in skin and bone. Biochim Biophys Acta 229:119–122
    • (1971) Biochim Biophys Acta , vol.229 , pp. 119-122
    • Pinnell, S.R.1    Fox, R.2    Krane, S.M.3
  • 17
    • 0001113489 scopus 로고
    • A subunit model for the tropocollagen macromolecule
    • COI: 1:CAS:528:DyaF2cXksV2js7o%3D, PID: 14173005
    • Petruska JA, Hodge AJ (1964) A subunit model for the tropocollagen macromolecule. Proc Natl Acad Sci USA 51:871–876
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 871-876
    • Petruska, J.A.1    Hodge, A.J.2
  • 18
    • 0030999235 scopus 로고    scopus 로고
    • Characterization of urinary degradation products derived from type I collagen. Identification of a beta-isomerized Asp-Gly sequence within the C-terminal telopeptides (alpha 1) region
    • COI: 1:CAS:528:DyaK2sXisFOktbo%3D, PID: 9092508
    • Fledelius C, Johnsen AH, Cloos PA, Bode M, Qvist P (1997) Characterization of urinary degradation products derived from type I collagen. Identification of a beta-isomerized Asp-Gly sequence within the C-terminal telopeptides (alpha 1) region. J Biol Chem 272(15):9755–9763
    • (1997) J Biol Chem , vol.272 , Issue.15 , pp. 9755-9763
    • Fledelius, C.1    Johnsen, A.H.2    Cloos, P.A.3    Bode, M.4    Qvist, P.5
  • 19
    • 0034141218 scopus 로고    scopus 로고
    • Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: a biological clock of protein aging with clinical potential
    • COI: 1:CAS:528:DC%2BD3cXisFOlsbw%3D, PID: 10642504
    • Cloos PA, Fledelius C (2000) Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: a biological clock of protein aging with clinical potential. Biochem J 345:473–480
    • (2000) Biochem J , vol.345 , pp. 473-480
    • Cloos, P.A.1    Fledelius, C.2
  • 20
  • 21
    • 32844468206 scopus 로고    scopus 로고
    • Extracellular post-translational modifications of collagen are major determinants of biomechanical properties of fetal bovine cortical bone
    • COI: 1:CAS:528:DC%2BD28Xhslyrt70%3D, PID: 16271523
    • Garnero P, Borel O, Gineyts E, Duboeuf F, Solberg H, Bouxsein ML, Christiansen C, Delmas PD (2006) Extracellular post-translational modifications of collagen are major determinants of biomechanical properties of fetal bovine cortical bone. Bone 38:300–309
    • (2006) Bone , vol.38 , pp. 300-309
    • Garnero, P.1    Borel, O.2    Gineyts, E.3    Duboeuf, F.4    Solberg, H.5    Bouxsein, M.L.6    Christiansen, C.7    Delmas, P.D.8
  • 22
    • 0030763499 scopus 로고    scopus 로고
    • Decreased beta-isomerization of the C-terminal telopeptide of type I collagen alpha 1 chain in Paget’s disease of bone
    • COI: 1:CAS:528:DyaK2sXmt1WksL4%3D, PID: 9286756
    • Garnero P, Fledelius C, Gineyts E, Serre CM, Vignot E, Delmas PD (1997) Decreased beta-isomerization of the C-terminal telopeptide of type I collagen alpha 1 chain in Paget’s disease of bone. J Bone Miner Res 12:1407–1415
    • (1997) J Bone Miner Res , vol.12 , pp. 1407-1415
    • Garnero, P.1    Fledelius, C.2    Gineyts, E.3    Serre, C.M.4    Vignot, E.5    Delmas, P.D.6
  • 24
    • 0035827138 scopus 로고    scopus 로고
    • Osteogenesis imperfecta murine: interaction between type I collagen homotrimers
    • COI: 1:CAS:528:DC%2BD3MXkt1ShtLg%3D, PID: 11397098
    • Kuznetsova N, McBride DJ Jr, Leikin S (2001) Osteogenesis imperfecta murine: interaction between type I collagen homotrimers. J Mol Biol 309:807–815
    • (2001) J Mol Biol , vol.309 , pp. 807-815
    • Kuznetsova, N.1    McBride, D.J.2    Leikin, S.3
  • 25
    • 0017623106 scopus 로고
    • Identification of collagen alpha1(I) trimer in embryonic chick tendons and calvaria
    • COI: 1:CAS:528:DyaE2sXlvFOks70%3D, PID: 562664
    • Jimenez SA, Bashey RI, Yankowski R (1977) Identification of collagen alpha1(I) trimer in embryonic chick tendons and calvaria. Biochem Biophys Res Commun 78:1354–1361
    • (1977) Biochem Biophys Res Commun , vol.78 , pp. 1354-1361
    • Jimenez, S.A.1    Bashey, R.I.2    Yankowski, R.3
  • 26
    • 0018384478 scopus 로고
    • Collagen types in normal and cirrhotic liver
    • COI: 1:CAS:528:DyaE1MXhs1Kjsbc%3D, PID: 421999
    • Rojkind M, Giambrone MA, Biempica L (1979) Collagen types in normal and cirrhotic liver. Gastroenterology 76:710–719
    • (1979) Gastroenterology , vol.76 , pp. 710-719
    • Rojkind, M.1    Giambrone, M.A.2    Biempica, L.3
  • 27
    • 77953163140 scopus 로고    scopus 로고
    • Carcinomas contain a matrix metalloproteinase-resistant isoform of type I collagen exerting selective support to invasion
    • COI: 1:CAS:528:DC%2BC3cXmslWgtr8%3D, PID: 20460529
    • Makareeva E, Han S, Leikin S (2010) Carcinomas contain a matrix metalloproteinase-resistant isoform of type I collagen exerting selective support to invasion. Cancer Res 70:4366–4374
    • (2010) Cancer Res , vol.70 , pp. 4366-4374
    • Makareeva, E.1    Han, S.2    Leikin, S.3
  • 28
    • 0024267459 scopus 로고
    • Synthesis of type I homotrimer collagen molecules by cultured human lung adenocarcinoma cells
    • COI: 1:CAS:528:DyaL1MXlsFWmtw%3D%3D, PID: 3189509
    • Rupard JH, Dimar SJ, Haralson MA (1988) Synthesis of type I homotrimer collagen molecules by cultured human lung adenocarcinoma cells. Am J Pathol 133:316–326
    • (1988) Am J Pathol , vol.133 , pp. 316-326
    • Rupard, J.H.1    Dimar, S.J.2    Haralson, M.A.3
  • 29
    • 0036151165 scopus 로고    scopus 로고
    • Phenotypic expression of osteoblast collagen in osteoarthritic bone: production of type I homotrimer
    • COI: 1:CAS:528:DC%2BD38Xms1aksQ%3D%3D, PID: 11809420
    • Bailey AJ, Sims TJ, Knott L (2002) Phenotypic expression of osteoblast collagen in osteoarthritic bone: production of type I homotrimer. Int J Biochem Cell Biol 34:176–182
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 176-182
    • Bailey, A.J.1    Sims, T.J.2    Knott, L.3
  • 30
    • 0035060434 scopus 로고    scopus 로고
    • A COL1A1 Sp1 binding site polymorphism predisposes to osteoporotic fracture by affecting bone density and quality
    • COI: 1:CAS:528:DC%2BD3MXisFWhtrY%3D, PID: 11285309
    • Mann V, Hobson EE, Li B, Stewart TL, Grant SF, Robins SP, Aspden RM, Ralston SH (2001) A COL1A1 Sp1 binding site polymorphism predisposes to osteoporotic fracture by affecting bone density and quality. J Clin Invest 107:899–907
    • (2001) J Clin Invest , vol.107 , pp. 899-907
    • Mann, V.1    Hobson, E.E.2    Li, B.3    Stewart, T.L.4    Grant, S.F.5    Robins, S.P.6    Aspden, R.M.7    Ralston, S.H.8
  • 31
    • 0029836744 scopus 로고    scopus 로고
    • Reduced bone density and osteoporosis associated with a polymorphic Sp1 binding site in the collagen type I alpha 1 gene
    • COI: 1:CAS:528:DyaK28XmtVKntb4%3D, PID: 8841196
    • Grant SF, Reid DM, Blake G, Herd R, Fogelman I, Ralston SH (1996) Reduced bone density and osteoporosis associated with a polymorphic Sp1 binding site in the collagen type I alpha 1 gene. Nat Genet 14:203–205
    • (1996) Nat Genet , vol.14 , pp. 203-205
    • Grant, S.F.1    Reid, D.M.2    Blake, G.3    Herd, R.4    Fogelman, I.5    Ralston, S.H.6
  • 32
    • 0142124733 scopus 로고    scopus 로고
    • Meta-analysis of COL1A1 Sp1 polymorphism in relation to bone mineral density and osteoporotic fracture
    • COI: 1:CAS:528:DC%2BD3sXks1Wksb0%3D, PID: 12810179
    • Mann V, Ralston SH (2003) Meta-analysis of COL1A1 Sp1 polymorphism in relation to bone mineral density and osteoporotic fracture. Bone 32:711–717
    • (2003) Bone , vol.32 , pp. 711-717
    • Mann, V.1    Ralston, S.H.2
  • 34
    • 0030472747 scopus 로고    scopus 로고
    • Heterozygous oim mice exhibit a mild form of osteogenesis imperfecta
    • COI: 1:STN:280:DyaK2s7it1CjsA%3D%3D, PID: 8968022
    • Saban J, Zussman M, King D (1996) Heterozygous oim mice exhibit a mild form of osteogenesis imperfecta. Bone 19:575–579
    • (1996) Bone , vol.19 , pp. 575-579
    • Saban, J.1    Zussman, M.2    King, D.3
  • 35
    • 0030839967 scopus 로고    scopus 로고
    • Collagen from the osteogenesis imperfecta mouse model (oim) shows reduced resistance against tensile stress
    • COI: 1:CAS:528:DyaK2sXksVKmtbg%3D, PID: 9202055
    • Misof K, Landis WJ, Fratzl P (1997) Collagen from the osteogenesis imperfecta mouse model (oim) shows reduced resistance against tensile stress. J Clin Invest 100:40–45
    • (1997) J Clin Invest , vol.100 , pp. 40-45
    • Misof, K.1    Landis, W.J.2    Fratzl, P.3
  • 36
    • 0032943078 scopus 로고    scopus 로고
    • The material basis for reduced mechanical properties in oim mice bones
    • COI: 1:STN:280:DyaK1M7jt1Gnuw%3D%3D, PID: 9933481
    • Camacho NP, Hou L, Boskey AL (1999) The material basis for reduced mechanical properties in oim mice bones. J Bone Miner Res 14:264–272
    • (1999) J Bone Miner Res , vol.14 , pp. 264-272
    • Camacho, N.P.1    Hou, L.2    Boskey, A.L.3
  • 37
    • 34548514847 scopus 로고    scopus 로고
    • Abnormal mineral-matrix interactions are a significant contributor to fragility in oim/oim bone
    • COI: 1:CAS:528:DC%2BD2sXpvF2rtbo%3D, PID: 17660935
    • Miller E, Delos D, Pleshko Camacho N (2007) Abnormal mineral-matrix interactions are a significant contributor to fragility in oim/oim bone. Calcif Tissue Int 81:206–214
    • (2007) Calcif Tissue Int , vol.81 , pp. 206-214
    • Miller, E.1    Delos, D.2    Pleshko, C.N.3
  • 38
    • 0342460605 scopus 로고    scopus 로고
    • Altered collagen structure in mouse tail tendon lacking the alpha 2(I) chain
    • COI: 1:CAS:528:DyaK2sXkvVWrtr8%3D, PID: 9236128
    • McBride DJ, Choe V, Brodsky B (1997) Altered collagen structure in mouse tail tendon lacking the alpha 2(I) chain. J Mol Biol 270:275–284
    • (1997) J Mol Biol , vol.270 , pp. 275-284
    • McBride, D.J.1    Choe, V.2    Brodsky, B.3
  • 39
    • 0035984335 scopus 로고    scopus 로고
    • The role of the alpha2 chain in the stabilization of the collagen type I heterotrimer: a study of the type I homotrimer in oim mouse tissues
    • COI: 1:CAS:528:DC%2BD38Xms1Wmu78%3D, PID: 12206762
    • Miles CA, Sims TJ, Bailey AJ (2002) The role of the alpha2 chain in the stabilization of the collagen type I heterotrimer: a study of the type I homotrimer in oim mouse tissues. J Mol Biol 321:797–805
    • (2002) J Mol Biol , vol.321 , pp. 797-805
    • Miles, C.A.1    Sims, T.J.2    Bailey, A.J.3
  • 41
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • COI: 1:CAS:528:DyaK1cXivVOlsb4%3D, PID: 24889800
    • MacKerell AD, Bashford D, Karplus M (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102:3586–3616
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1    Bashford, D.2    Karplus, M.3
  • 42
    • 84863012650 scopus 로고    scopus 로고
    • Structural and mechanical differences between collagen homo- and heterotrimers: relevance for the molecular origin of brittle bone disease
    • COI: 1:CAS:528:DC%2BC38XitVWktro%3D, PID: 22325288
    • Chang S-W, Shefelbine SJ, Buehler MJ (2012) Structural and mechanical differences between collagen homo- and heterotrimers: relevance for the molecular origin of brittle bone disease. Biophys J 102:640–648
    • (2012) Biophys J , vol.102 , pp. 640-648
    • Chang, S.-W.1    Shefelbine, S.J.2    Buehler, M.J.3
  • 43
    • 33749518488 scopus 로고    scopus 로고
    • Contribution of the advanced glycation end product pentosidine and of maturation of type I collagen to compressive biomechanical properties of human lumbar vertebrae
    • COI: 1:CAS:528:DC%2BD28XhtVyktrjN, PID: 16829221
    • Viguet-Carrin S, Roux JP, Arlot ME, Merabet Z, Leeming DJ, Byrjalsen I, Delmas PD, Bouxtein M (2006) Contribution of the advanced glycation end product pentosidine and of maturation of type I collagen to compressive biomechanical properties of human lumbar vertebrae. Bone 39:1073–1079
    • (2006) Bone , vol.39 , pp. 1073-1079
    • Viguet-Carrin, S.1    Roux, J.P.2    Arlot, M.E.3    Merabet, Z.4    Leeming, D.J.5    Byrjalsen, I.6    Delmas, P.D.7    Bouxtein, M.8
  • 44
    • 0041379294 scopus 로고    scopus 로고
    • Preferred collagen fiber orientation in the human mid-shaft femur
    • Goldman HM, Bromage TG, Thomas CD, Clement JG (2003) Preferred collagen fiber orientation in the human mid-shaft femur. Anat Rec A 272:434–445
    • (2003) Anat Rec A , vol.272 , pp. 434-445
    • Goldman, H.M.1    Bromage, T.G.2    Thomas, C.D.3    Clement, J.G.4
  • 45
    • 0027949275 scopus 로고
    • Osteon orientation of the diaphysis of the long bones in man
    • COI: 1:STN:280:DyaK2czkslCqug%3D%3D, PID: 8068447
    • Hert J, Fiala P, Petryl M (1994) Osteon orientation of the diaphysis of the long bones in man. Bone 15:269–277
    • (1994) Bone , vol.15 , pp. 269-277
    • Hert, J.1    Fiala, P.2    Petryl, M.3
  • 46
    • 0027656634 scopus 로고
    • The effects of collagen fiber orientation, porosity, density, and mineralization bovine cortical bone bending properties
    • COI: 1:STN:280:DyaK2c%2Fht1yhtA%3D%3D, PID: 8408087
    • Martin RB, Boardman DL (1993) The effects of collagen fiber orientation, porosity, density, and mineralization bovine cortical bone bending properties. J Biomech 26:1047–1054
    • (1993) J Biomech , vol.26 , pp. 1047-1054
    • Martin, R.B.1    Boardman, D.L.2
  • 47
    • 0030560691 scopus 로고    scopus 로고
    • Collagen fiber organization is related to mechanical properties and remodelling in equine bone. A comparison of two methods
    • Martin RB, Lau ST, Mathews PV, Gibson VA, Stovert SM (1996) Collagen fiber organization is related to mechanical properties and remodelling in equine bone. A comparison of two methods. J Biomechanics 29:1515–1521
    • (1996) J Biomechanics , vol.29 , Issue.1515 , pp. 1521
    • Martin, R.B.1    Lau, S.T.2    Mathews, P.V.3    Gibson, V.A.4    Stovert, S.M.5
  • 48
    • 33847052094 scopus 로고    scopus 로고
    • Local variations in the micromechanical properties of mouse femur: the involvement of collagen fiber orientation and mineralization
    • Ramasamya JG, Akkusb O (2007) Local variations in the micromechanical properties of mouse femur: the involvement of collagen fiber orientation and mineralization. J Biomech 40:910–918
    • (2007) J Biomech , vol.40 , pp. 910-918
    • Ramasamya, J.G.1    Akkusb, O.2
  • 49
    • 0036708148 scopus 로고    scopus 로고
    • Long bones from the senescence accelerated mouse SAMP6 have increased size but reduced whole-bone strength and resistance to fracture
    • PID: 12211429
    • Silva MJ, Brodt MB, Ettner SL (2002) Long bones from the senescence accelerated mouse SAMP6 have increased size but reduced whole-bone strength and resistance to fracture. J Bone Miner Res 17:1597–1603
    • (2002) J Bone Miner Res , vol.17 , pp. 1597-1603
    • Silva, M.J.1    Brodt, M.B.2    Ettner, S.L.3
  • 50
  • 52
    • 33645213786 scopus 로고
    • Collagen fractions in lathyritic rats
    • COI: 1:CAS:528:DyaF3MXitlyltQ%3D%3D, PID: 13770529
    • Mikkonen L, Tuominen T, Kulonen E (1960) Collagen fractions in lathyritic rats. Biochem Pharmacol 3:181–183
    • (1960) Biochem Pharmacol , vol.3 , pp. 181-183
    • Mikkonen, L.1    Tuominen, T.2    Kulonen, E.3
  • 53
    • 0023142179 scopus 로고
    • Neutron studies of collagenic lathyritic bone
    • COI: 1:CAS:528:DyaL2sXhsFChsLk%3D
    • Lees S, Barnard S, Mook H (1987) Neutron studies of collagenic lathyritic bone. Int J Biol Macromol 9:32–38
    • (1987) Int J Biol Macromol , vol.9 , pp. 32-38
    • Lees, S.1    Barnard, S.2    Mook, H.3
  • 54
    • 1942501149 scopus 로고    scopus 로고
    • Osteogenesis imperfecta
    • COI: 1:CAS:528:DC%2BD2cXjtl2lsLs%3D, PID: 15110498
    • Rauch F, Glorieux FH (2004) Osteogenesis imperfecta. Lancet 363:1377–1385
    • (2004) Lancet , vol.363 , pp. 1377-1385
    • Rauch, F.1    Glorieux, F.H.2
  • 55
    • 0034022769 scopus 로고    scopus 로고
    • Static and dynamic bone histomorphometry in children with osteogenesis imperfecta
    • COI: 1:STN:280:DC%2BD3c3pt12jsA%3D%3D, PID: 10831929
    • Rauch F, Travers R, Parfitt AM, Glorieux FH (2000) Static and dynamic bone histomorphometry in children with osteogenesis imperfecta. Bone 26:581–589
    • (2000) Bone , vol.26 , pp. 581-589
    • Rauch, F.1    Travers, R.2    Parfitt, A.M.3    Glorieux, F.H.4
  • 56
    • 84886095231 scopus 로고    scopus 로고
    • Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta
    • COI: 1:CAS:528:DC%2BC3sXhsFyntbvN, PID: 23508630
    • Eyre DR, Weis MA (2013) Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta. Calcif Tissue Int 93:338–347
    • (2013) Calcif Tissue Int , vol.93 , pp. 338-347
    • Eyre, D.R.1    Weis, M.A.2
  • 57
    • 0026556220 scopus 로고
    • Abnormal collagen and mineral formation in osteogenesis imperfecta
    • Cassela JP, Yousuf Ali S (1992) Abnormal collagen and mineral formation in osteogenesis imperfecta. Bone Miner 17:123–128
    • (1992) Bone Miner , vol.17 , pp. 123-128
    • Cassela, J.P.1    Yousuf Ali, S.2
  • 58
    • 0029985847 scopus 로고    scopus 로고
    • A morphological and ultrastructural study of bone in osteogenesis imperfecta
    • Cassela JP, Stamp TCB, Ali SY (1996) A morphological and ultrastructural study of bone in osteogenesis imperfecta. Calcif Tissue Int 58:155–165
    • (1996) Calcif Tissue Int , vol.58 , pp. 155-165
    • Cassela, J.P.1    Stamp, T.C.B.2    Ali, S.Y.3
  • 59
    • 0032740139 scopus 로고    scopus 로고
    • Morphometric analysis of type I collagen fibrils in the osteoid of osteogenesis imperfecta
    • COI: 1:CAS:528:DyaK1MXnsV2nu7Y%3D, PID: 10541766
    • Sarathchandra P, Pope FM, Ali SY (1999) Morphometric analysis of type I collagen fibrils in the osteoid of osteogenesis imperfecta. Calcif Tissue Int 65:390–395
    • (1999) Calcif Tissue Int , vol.65 , pp. 390-395
    • Sarathchandra, P.1    Pope, F.M.2    Ali, S.Y.3
  • 60
    • 0019417315 scopus 로고
    • Disorder of collagen metabolism in a patient with osteogenesis imperfecta (lethal type): increased degree of hydroxylation of lysine in collagen type I and III
    • COI: 1:STN:280:DyaL3M7msVKntw%3D%3D, PID: 6783428
    • Kirsch E, Krieg T, Remberger K, Fendel H, Bruckner P, Muller PK (1981) Disorder of collagen metabolism in a patient with osteogenesis imperfecta (lethal type): increased degree of hydroxylation of lysine in collagen type I and III. Eur J Clin Invest 11:39–47
    • (1981) Eur J Clin Invest , vol.11 , pp. 39-47
    • Kirsch, E.1    Krieg, T.2    Remberger, K.3    Fendel, H.4    Bruckner, P.5    Muller, P.K.6
  • 61
    • 59649092309 scopus 로고    scopus 로고
    • Bone turnover and type I collagen C-telopeptide isomerization in adult osteogenesis imperfecta: associations with collagen gene mutations
    • COI: 1:CAS:528:DC%2BD1MXhvF2qsbs%3D, PID: 19071236
    • Garnero P, Schott AM, Prockop D, Chevrel G (2009) Bone turnover and type I collagen C-telopeptide isomerization in adult osteogenesis imperfecta: associations with collagen gene mutations. Bone 44:461–466
    • (2009) Bone , vol.44 , pp. 461-466
    • Garnero, P.1    Schott, A.M.2    Prockop, D.3    Chevrel, G.4
  • 64
    • 0033621331 scopus 로고    scopus 로고
    • Use of the Cre/lox recombination system to develop a non-lethal knock-in murine model for osteogenesis imperfecta with an alpha1(I) G349C substitution. Variability in phenotype in Brtl IV mice
    • COI: 1:CAS:528:DC%2BD3cXkt1GmtQ%3D%3D, PID: 10608859
    • Forlino A, Porter FD, Lee EJ, Westphal H, Marini JC (1999) Use of the Cre/lox recombination system to develop a non-lethal knock-in murine model for osteogenesis imperfecta with an alpha1(I) G349C substitution. Variability in phenotype in Brtl IV mice. J Biol Chem 274:37923–37931
    • (1999) J Biol Chem , vol.274 , pp. 37923-37931
    • Forlino, A.1    Porter, F.D.2    Lee, E.J.3    Westphal, H.4    Marini, J.C.5
  • 66
    • 0037244270 scopus 로고    scopus 로고
    • Properties of collagen in oim mouse tissues
    • COI: 1:CAS:528:DC%2BD3sXjtlamsrs%3D, PID: 12952198
    • Sims TJ, Miles CA, Bailey AJ, Camacho NP (2003) Properties of collagen in oim mouse tissues. Connect Tissue Res 44(Suppl 1):202–205
    • (2003) Connect Tissue Res , vol.44 , pp. 202-205
    • Sims, T.J.1    Miles, C.A.2    Bailey, A.J.3    Camacho, N.P.4
  • 67
    • 34548514847 scopus 로고    scopus 로고
    • Abnormal mineral-matrix interactions are a significant contributor to fragility in oim/oim bone
    • Miller E, Delos D, Baldini T, Wright TM, Camacho NP (2007) Abnormal mineral-matrix interactions are a significant contributor to fragility in oim/oim bone. Calcif Tissue Int 81:206–214
    • (2007) Calcif Tissue Int , vol.2007 , Issue.81 , pp. 206-214
    • Miller, E.1    Delos, D.2    Baldini, T.3    Wright, T.M.4    Camacho, N.P.5
  • 68
    • 0030152687 scopus 로고    scopus 로고
    • Type-I collagen mutation compromises the post-yield behavior of Mov13 long bone
    • COI: 1:CAS:528:DyaK28Xks1Sgu7w%3D, PID: 8676263
    • Jepsen KJ, Goldstein SA, Kuhn JL, Schaffler MB, Bonadio J (1996) Type-I collagen mutation compromises the post-yield behavior of Mov13 long bone. J Orthop Res 14:493–499
    • (1996) J Orthop Res , vol.14 , pp. 493-499
    • Jepsen, K.J.1    Goldstein, S.A.2    Kuhn, J.L.3    Schaffler, M.B.4    Bonadio, J.5
  • 69
    • 3042797594 scopus 로고    scopus 로고
    • Structure, stability and interactions of type I collagen with GLY349-CYS substitution in α1(I) chain in a murine Osteogenesis Imperfecta model
    • Kuznetsovaa NV, Forlinob A, Cabralb WA, Marinib JC, Leikina S (2004) Structure, stability and interactions of type I collagen with GLY349-CYS substitution in α1(I) chain in a murine Osteogenesis Imperfecta model. Matrix Biol 23:101–112
    • (2004) Matrix Biol , vol.23 , pp. 101-112
    • Kuznetsovaa, N.V.1    Forlinob, A.2    Cabralb, W.A.3    Marinib, J.C.4    Leikina, S.5
  • 70
    • 78649906076 scopus 로고    scopus 로고
    • Nanoscale morphology of type I collagen is altered in the Brtl mouse model of Osteogenesis Imperfecta
    • COI: 1:CAS:528:DC%2BC3cXhsFCqur%2FO, PID: 20696252
    • Wallace JM, Orr BG, Marini JC, Banaszak Holl MM (2011) Nanoscale morphology of type I collagen is altered in the Brtl mouse model of Osteogenesis Imperfecta. J Struct Biol 173:146–152
    • (2011) J Struct Biol , vol.173 , pp. 146-152
    • Wallace, J.M.1    Orr, B.G.2    Marini, J.C.3    Banaszak Holl, M.M.4
  • 71
    • 2142758179 scopus 로고    scopus 로고
    • Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organization
    • COI: 1:CAS:528:DC%2BD2cXjvVyisrg%3D, PID: 15111431
    • Gutsmann T, Fantner GE, Kindt JH, Venturoni M, Danielsen S, Hansma PK (2004) Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organization. Biophys J 86:3186–3193
    • (2004) Biophys J , vol.86 , pp. 3186-3193
    • Gutsmann, T.1    Fantner, G.E.2    Kindt, J.H.3    Venturoni, M.4    Danielsen, S.5    Hansma, P.K.6
  • 73
    • 77951253891 scopus 로고    scopus 로고
    • Distribution of type I collagen morphologies in bone: relation to estrogen depletion
    • COI: 1:CAS:528:DC%2BC3cXksFCltbo%3D, PID: 19932773
    • Wallace JM, Erickson B, Les CM, Orr BG, Banaszak Holl MM (2010) Distribution of type I collagen morphologies in bone: relation to estrogen depletion. Bone 46:1349–1354
    • (2010) Bone , vol.46 , pp. 1349-1354
    • Wallace, J.M.1    Erickson, B.2    Les, C.M.3    Orr, B.G.4    Banaszak, H.M.M.5
  • 74
    • 0018968492 scopus 로고
    • Bone histomorphometry in Paget’s disease. Quantitative and dynamic analysis of Pagetic and non-Pagetic bone tissue
    • COI: 1:STN:280:DyaL3M%2FjvV2hsQ%3D%3D, PID: 7426075
    • Meunier PJ, Coindre JM, Edouard CM, Arlot ME (1980) Bone histomorphometry in Paget’s disease. Quantitative and dynamic analysis of Pagetic and non-Pagetic bone tissue. Arthritis Rheum 23:1095–1103
    • (1980) Arthritis Rheum , vol.23 , pp. 1095-1103
    • Meunier, P.J.1    Coindre, J.M.2    Edouard, C.M.3    Arlot, M.E.4
  • 75
    • 0031886744 scopus 로고    scopus 로고
    • Measurement of urinary excretion of nonisomerized an beta-isomerized forms of type I collagen breakdown products to monitor the effects of the bisphosphonate zoledronate in Paget’s disease
    • COI: 1:CAS:528:DyaK1cXhtlSmtL0%3D, PID: 9485094
    • Garnero P, Gineyts E, Schaffer AV, Seaman J, Delmas PD (1998) Measurement of urinary excretion of nonisomerized an beta-isomerized forms of type I collagen breakdown products to monitor the effects of the bisphosphonate zoledronate in Paget’s disease. Arthritis Rheum 41:354–360
    • (1998) Arthritis Rheum , vol.41 , pp. 354-360
    • Garnero, P.1    Gineyts, E.2    Schaffer, A.V.3    Seaman, J.4    Delmas, P.D.5
  • 76
    • 84903272886 scopus 로고    scopus 로고
    • Alfacalcidol enhances collagen quality in ovariectomized rat bones
    • COI: 1:CAS:528:DC%2BC2cXhtVKntr3L, PID: 24809324
    • Nagaoka H, Terajima M, Yamada S, Azuma Y, Chida T, Yamauchi M (2014) Alfacalcidol enhances collagen quality in ovariectomized rat bones. J Orthop Res 32:1030–1036
    • (2014) J Orthop Res , vol.32 , pp. 1030-1036
    • Nagaoka, H.1    Terajima, M.2    Yamada, S.3    Azuma, Y.4    Chida, T.5    Yamauchi, M.6
  • 78
    • 37349054707 scopus 로고    scopus 로고
    • Measurements of mobile and bound water by nuclear magnetic resonance correlate with mechanical properties of bone
    • COI: 1:CAS:528:DC%2BD2sXhsVOrtrvP, PID: 17964874
    • Nyman JS, Ni Q, Nicolella DP, Wang X (2008) Measurements of mobile and bound water by nuclear magnetic resonance correlate with mechanical properties of bone. Bone 42:193–199
    • (2008) Bone , vol.42 , pp. 193-199
    • Nyman, J.S.1    Ni, Q.2    Nicolella, D.P.3    Wang, X.4
  • 79
    • 32644452256 scopus 로고    scopus 로고
    • The influence of water removal on the strength and toughness of cortical bone
    • PID: 16488231
    • Nyman JS, Roy A, Shen X, Acuna RL, Tyler JH, Wang X (2006) The influence of water removal on the strength and toughness of cortical bone. J Biomech 39:931–938
    • (2006) J Biomech , vol.39 , pp. 931-938
    • Nyman, J.S.1    Roy, A.2    Shen, X.3    Acuna, R.L.4    Tyler, J.H.5    Wang, X.6
  • 81
    • 79960558439 scopus 로고    scopus 로고
    • Effect of mineral–collagen interfacial behavior on the microdamage progression in bone using a probabilistic cohesive finite element model
    • COI: 1:CAS:528:DC%2BC3MXht1ejt7rM, PID: 21783104
    • Luo Q, Nakade R, Dong X, Rong Q, Wang X (2011) Effect of mineral–collagen interfacial behavior on the microdamage progression in bone using a probabilistic cohesive finite element model. J Mech Behav Biomed Mater 4:943–952
    • (2011) J Mech Behav Biomed Mater , vol.4 , pp. 943-952
    • Luo, Q.1    Nakade, R.2    Dong, X.3    Rong, Q.4    Wang, X.5
  • 82
    • 0036233579 scopus 로고    scopus 로고
    • Type I collagen racemization and isomerization and the risk of fracture in postmenopausal women: the OFELY prospective study
    • COI: 1:CAS:528:DC%2BD38XktVSktro%3D, PID: 12009013
    • Garnero P, Cloos P, Sornay-Rendu E, Qvist P, Delmas PD (2002) Type I collagen racemization and isomerization and the risk of fracture in postmenopausal women: the OFELY prospective study. J Bone Miner Res 17:826–833
    • (2002) J Bone Miner Res , vol.17 , pp. 826-833
    • Garnero, P.1    Cloos, P.2    Sornay-Rendu, E.3    Qvist, P.4    Delmas, P.D.5
  • 83
    • 0032898411 scopus 로고    scopus 로고
    • The relationships between the degree of beta-isomerization of type I collagen degradation products in the urine and aging, menopause and osteoporosis with fractures
    • COI: 1:STN:280:DC%2BD3c%2FhvFymtw%3D%3D, PID: 10550459
    • Hoshino H, Takahashi M, Kushida K, Ohishi T, Inoue T (1999) The relationships between the degree of beta-isomerization of type I collagen degradation products in the urine and aging, menopause and osteoporosis with fractures. Osteoporos Int 9:405–409
    • (1999) Osteoporos Int , vol.9 , pp. 405-409
    • Hoshino, H.1    Takahashi, M.2    Kushida, K.3    Ohishi, T.4    Inoue, T.5
  • 84
    • 84980475769 scopus 로고    scopus 로고
    • Type I collagen isomerization (alpha/beta CTX ratio) and the risk of new vertebral fracture in men: a prospective study
    • Bauer DC, Garnero P, Litwack S, Cauley JA, Ensrud K, Eastell R, Orwoll E (2010) Type I collagen isomerization (alpha/beta CTX ratio) and the risk of new vertebral fracture in men: a prospective study. J Bone Miner Res 25(Suppl 1):1024
    • (2010) J Bone Miner Res , vol.25 , pp. 1024
    • Bauer, D.C.1    Garnero, P.2    Litwack, S.3    Cauley, J.A.4    Ensrud, K.5    Eastell, R.6    Orwoll, E.7
  • 85
    • 38849202528 scopus 로고    scopus 로고
    • Bone turnover and bone collagen maturation in osteoporosis: effects of antiresorptive therapies
    • COI: 1:CAS:528:DC%2BD1cXhtlOqs7s%3D, PID: 17846859
    • Byrjalsen I, Leeming DJ, Qvist P, Christiansen C, Karsdal MA (2008) Bone turnover and bone collagen maturation in osteoporosis: effects of antiresorptive therapies. Osteoporos Int 19:339–348
    • (2008) Osteoporos Int , vol.19 , pp. 339-348
    • Byrjalsen, I.1    Leeming, D.J.2    Qvist, P.3    Christiansen, C.4    Karsdal, M.A.5
  • 86
    • 44449162249 scopus 로고    scopus 로고
    • Effects of PTH and alendronate on type I collagen isomerization in postmenopausal women with osteoporosis: the PaTH study
    • COI: 1:CAS:528:DC%2BD1cXhtFSlurvL, PID: 18442311
    • Garnero P, Bauer D, Mareau E, Bilezikian JP, Greenspan SL, Rosen C, Black D (2008) Effects of PTH and alendronate on type I collagen isomerization in postmenopausal women with osteoporosis: the PaTH study. J Bone Miner Res 23:1442–1448
    • (2008) J Bone Miner Res , vol.23 , pp. 1442-1448
    • Garnero, P.1    Bauer, D.2    Mareau, E.3    Bilezikian, J.P.4    Greenspan, S.L.5    Rosen, C.6    Black, D.7
  • 87
    • 0034746735 scopus 로고    scopus 로고
    • Aminoterminal propeptide of the alpha1-homotrimer variant of human type I procollagen (hotPINP) in malignant pleural effusion
    • COI: 1:CAS:528:DC%2BD3MXovVOqsbo%3D, PID: 11724285
    • Kauppila S, Jukkola A, Melkko J, Risteli L, Turpeeniemi-Hujanen T, Vuorinen K, Risteli J (2001) Aminoterminal propeptide of the alpha1-homotrimer variant of human type I procollagen (hotPINP) in malignant pleural effusion. Anticancer Res 21(4A):2293–2296
    • (2001) Anticancer Res , vol.21 , Issue.4A , pp. 2293-2296
    • Kauppila, S.1    Jukkola, A.2    Melkko, J.3    Risteli, L.4    Turpeeniemi-Hujanen, T.5    Vuorinen, K.6    Risteli, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.