메뉴 건너뛰기




Volumn 7, Issue 9, 2011, Pages 540-557

New perspectives on osteogenesis imperfecta

Author keywords

[No Author keywords available]

Indexed keywords

BISPHOSPHONIC ACID DERIVATIVE; CHAPERONE; COLLAGEN TYPE 1; COLLAGEN TYPE 3; DENOSUMAB; HUMAN GROWTH HORMONE; PEPTIDYLPROLYL ISOMERASE;

EID: 80052053073     PISSN: 17595029     EISSN: 17595037     Source Type: Journal    
DOI: 10.1038/nrendo.2011.81     Document Type: Review
Times cited : (547)

References (215)
  • 1
    • 0004160328 scopus 로고    scopus 로고
    • (eds Behrman, R. E., Kliegman, R. M. & Jensen, R. M.) Saunders, Philadelphia
    • Marini, J. C. in Nelson Textbook of Pediatrics (eds Behrman, R. E., Kliegman, R. M. & Jensen, R. M.) 2336-2338 (Saunders, Philadelphia, 2004).
    • (2004) Nelson Textbook of Pediatrics , pp. 2336-2338
    • Marini, J.C.1
  • 2
    • 33847227672 scopus 로고    scopus 로고
    • Consortium for osteogenesis imperfecta mutations in the helical domain of type i collagen: Regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans
    • Marini, J. C. et al. Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum. Mutat. 28, 209-221 (2007).
    • (2007) Hum. Mutat. , vol.28 , pp. 209-221
    • Marini, J.C.1
  • 3
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop, D. J. & Kivirikko, K. I. Collagens: molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem. 64, 403-434 (1995).
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 4
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • DOI 10.1016/j.tig.2003.11.004
    • Myllyharju, J. & Kivirikko, K. I. Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet. 20, 33-43 (2004). (Pubitemid 38032818)
    • (2004) Trends in Genetics , vol.20 , Issue.1 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 8
    • 76649130557 scopus 로고    scopus 로고
    • Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding
    • Barnes, A. M. et al. Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N. Engl. J. Med. 362, 521-528 (2010).
    • (2010) N. Engl. J. Med. , vol.362 , pp. 521-528
    • Barnes, A.M.1
  • 9
    • 70350506376 scopus 로고    scopus 로고
    • PPIB mutations cause severe osteogenesis imperfecta
    • van Dijk, F. S. et al. PPIB mutations cause severe osteogenesis imperfecta. Am. J. Hum. Genet. 85, 521-527 (2009).
    • (2009) Am. J. Hum. Genet. , vol.85 , pp. 521-527
    • Van Dijk, F.S.1
  • 11
    • 77950381244 scopus 로고    scopus 로고
    • Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta
    • Alanay, Y. et al. Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta. Am. J. Hum. Genet. 86, 551-559 (2010).
    • (2010) Am. J. Hum. Genet. , vol.86 , pp. 551-559
    • Alanay, Y.1
  • 12
    • 77949262259 scopus 로고    scopus 로고
    • Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta
    • Christiansen, H. E. et al. Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta. Am. J. Hum. Genet. 86, 389-398 (2010).
    • (2010) Am. J. Hum. Genet. , vol.86 , pp. 389-398
    • Christiansen, H.E.1
  • 13
    • 0018267089 scopus 로고
    • Classification of osteogenesis imperfecta
    • Sillence, D. O. & Rimoin, D. L. Classification of osteogenesis imperfecta. Lancet 1, 1041-1042 (1978).
    • (1978) Lancet , vol.1 , pp. 1041-1042
    • Sillence, D.O.1    Rimoin, D.L.2
  • 14
    • 0018416379 scopus 로고
    • Genetic heterogeneity in osteogenesis imperfecta
    • Sillence, D. O., Senn, A. & Danks, D. M. Genetic heterogeneity in osteogenesis imperfecta. J. Med. Genet. 16, 101-116 (1979). (Pubitemid 9164903)
    • (1979) Journal of Medical Genetics , vol.16 , Issue.2 , pp. 101-116
    • Sillence, D.O.1    Senn, A.2    Danks, D.M.3
  • 15
    • 78049259511 scopus 로고    scopus 로고
    • Characterising and treating osteogenesis imperfecta
    • Bishop, N. Characterising and treating osteogenesis imperfecta. Early Hum. Dev. 86, 743-746 (2010).
    • (2010) Early Hum. Dev. , vol.86 , pp. 743-746
    • Bishop, N.1
  • 18
  • 19
    • 0029395773 scopus 로고
    • Osteogenesis imperfecta Type IIA and pulmonary hypoplasia with normal alveolar development
    • Thibeault, D. W., Pettett, G., Mabry, S. M. & Rezaiekhaligh, M. M. Osteogenesis imperfecta Type IIA and pulmonary hypoplasia with normal alveolar development. Pediatr. Pulmonol. 20, 301-306 (1995).
    • (1995) Pediatr. Pulmonol. , vol.20 , pp. 301-306
    • Thibeault, D.W.1    Pettett, G.2    Mabry, S.M.3    Rezaiekhaligh, M.M.4
  • 20
    • 55849131441 scopus 로고    scopus 로고
    • Popcorn calcification in osteogenesis imperfecta: Incidence, progression, and molecular correlation
    • Obafemi, A. A., Bulas, D. I., Troendle, J. & Marini, J. C. Popcorn calcification in osteogenesis imperfecta: incidence, progression, and molecular correlation. Am. J. Med. Genet. A 146A, 2725-2732 (2008).
    • (2008) Am. J. Med. Genet. A , vol.146 A , pp. 2725-2732
    • Obafemi, A.A.1    Bulas, D.I.2    Troendle, J.3    Marini, J.C.4
  • 21
    • 1942501149 scopus 로고    scopus 로고
    • Osteogenesis imperfecta
    • DOI 10.1016/S0140-6736(04)16051-0, PII S0140673604160510
    • Rauch, F. & Glorieux, F. H. Osteogenesis imperfecta. Lancet 363, 1377-1385 (2004). (Pubitemid 38529880)
    • (2004) Lancet , vol.363 , Issue.9418 , pp. 1377-1385
    • Rauch, F.1    Glorieux, F.H.2
  • 22
    • 0034022769 scopus 로고    scopus 로고
    • Static and dynamic bone histomorphometry in children with osteogenesis imperfecta
    • DOI 10.1016/S8756-3282(00)00269-6, PII S8756328200002696
    • Rauch, F., Travers, R., Parfitt, A. M. & Glorieux, F. H. Static and dynamic bone histomorphometry in children with osteogenesis imperfecta. Bone 26, 581-589 (2000). (Pubitemid 30301650)
    • (2000) Bone , vol.26 , Issue.6 , pp. 581-589
    • Rauch, F.1    Travers, R.2    Parfitt, A.M.3    Glorieux, F.H.4
  • 24
    • 77953529873 scopus 로고    scopus 로고
    • Relationship between genotype and skeletal phenotype in children and adolescents with osteogenesis imperfecta
    • Rauch, F., Lalic, L., Roughley, P. & Glorieux, F. H. Relationship between genotype and skeletal phenotype in children and adolescents with osteogenesis imperfecta. J. Bone Miner. Res. 25, 1367-1374 (2010).
    • (2010) J. Bone Miner. Res. , vol.25 , pp. 1367-1374
    • Rauch, F.1    Lalic, L.2    Roughley, P.3    Glorieux, F.H.4
  • 25
    • 34249656211 scopus 로고    scopus 로고
    • Insights into material and structural basis of bone fragility from diseases associated with fractures: How determinants of the biomechanical properties of bone are compromised by disease
    • DOI 10.1210/er.2006-0029
    • Chavassieux, P., Seeman, E. & Delmas, P. D. Insights into material and structural basis of bone fragility from diseases associated with fractures: how determinants of the biomechanical properties of bone are compromised by disease. Endocr. Rev. 28, 151-164 (2007). (Pubitemid 46984832)
    • (2007) Endocrine Reviews , vol.28 , Issue.2 , pp. 151-164
    • Chavassieux, P.1    Seeman, E.2    Delmas, P.D.3
  • 26
    • 56749095463 scopus 로고    scopus 로고
    • Cellular mechanism of decreased bone in Brtl mouse model of OI: Imbalance of decreased osteoblast function and increased osteoclasts and their precursors
    • Uveges, T. E. et al. Cellular mechanism of decreased bone in Brtl mouse model of OI: imbalance of decreased osteoblast function and increased osteoclasts and their precursors. J. Bone Miner. Res. 23, 1983-1994 (2008).
    • (2008) J. Bone Miner. Res. , vol.23 , pp. 1983-1994
    • Uveges, T.E.1
  • 27
    • 77952043631 scopus 로고    scopus 로고
    • Immature osteoblast lineage cells increase osteoclastogenesis in osteogenesis imperfecta murine
    • Li, H. et al. Immature osteoblast lineage cells increase osteoclastogenesis in osteogenesis imperfecta murine. Am. J. Pathol. 176, 2405-2413 (2010).
    • (2010) Am. J. Pathol. , vol.176 , pp. 2405-2413
    • Li, H.1
  • 28
    • 34250337398 scopus 로고    scopus 로고
    • Differential expression of both extracellular and intracellular proteins is involved in the lethal or nonlethal phenotypic variation of BrtlIV, a murine model for osteogenesis imperfecta
    • DOI 10.1002/pmic.200600919
    • Forlino, A. et al. Differential expression of both extracellular and intracellular proteins is involved in the lethal or nonlethal phenotypic variation of BrtlIV, a murine model for osteogenesis imperfecta. Proteomics 7, 1877-1891 (2007). (Pubitemid 46911006)
    • (2007) Proteomics , vol.7 , Issue.11 , pp. 1877-1891
    • Forlino, A.1    Tani, C.2    Rossi, A.3    Lupi, A.4    Campari, E.5    Gualeni, B.6    Bianchi, L.7    Armini, A.8    Cetta, G.9    Bini, L.10    Marini, J.C.11
  • 29
    • 77953463249 scopus 로고    scopus 로고
    • Variable bone fragility associated with an Amish COL1A2 variant and a knock-in mouse model
    • Daley, E. et al. Variable bone fragility associated with an Amish COL1A2 variant and a knock-in mouse model. J. Bone Miner. Res. 25, 247-261 (2010).
    • (2010) J. Bone Miner. Res. , vol.25 , pp. 247-261
    • Daley, E.1
  • 30
    • 40849095647 scopus 로고    scopus 로고
    • Role of genetic background in determining phenotypic severity throughout postnatal development and at peak bone mass in Col1a2 deficient mice (oim)
    • Carleton, S. M. et al. Role of genetic background in determining phenotypic severity throughout postnatal development and at peak bone mass in Col1a2 deficient mice (oim). Bone 42, 681-694 (2008).
    • (2008) Bone , vol.42 , pp. 681-694
    • Carleton, S.M.1
  • 31
    • 36549047084 scopus 로고    scopus 로고
    • Selective retention and degradation of molecules with a single mutant α1(I) chain in the Brtl IV mouse model of OI
    • DOI 10.1016/j.matbio.2007.06.005, PII S0945053X0700087X
    • Forlino, A., Kuznetsova, N. V., Marini, J. C. & Leikin, S. Selective retention and degradation of molecules with a single mutant alpha1(I) chain in the Brtl IV mouse model of OI. Matrix Biol. 26, 604-614 (2007). (Pubitemid 350180392)
    • (2007) Matrix Biology , vol.26 , Issue.8 , pp. 604-614
    • Forlino, A.1    Kuznetsova, N.V.2    Marini, J.C.3    Leikin, S.4
  • 32
    • 40149105885 scopus 로고    scopus 로고
    • ER stress-mediated apoptosis in a new mouse model of osteogenesis imperfecta
    • Lisse, T. S. et al. ER stress-mediated apoptosis in a new mouse model of osteogenesis imperfecta. PLoS Genet. 4, e7 (2008).
    • (2008) PLoS Genet. , vol.4
    • Lisse, T.S.1
  • 33
    • 77953499774 scopus 로고    scopus 로고
    • Amelioration of a mouse model of osteogenesis imperfecta with hematopoietic stem cell transplantation: Microcomputed tomography studies
    • Mehrotra, M., Rosol, M., Ogawa, M. & Larue, A. C. Amelioration of a mouse model of osteogenesis imperfecta with hematopoietic stem cell transplantation: microcomputed tomography studies. Exp. Hematol. 38, 593-602 (2010).
    • (2010) Exp. Hematol. , vol.38 , pp. 593-602
    • Mehrotra, M.1    Rosol, M.2    Ogawa, M.3    Larue, A.C.4
  • 34
    • 67651091674 scopus 로고    scopus 로고
    • In utero transplantation of adult bone marrow decreases perinatal lethality and rescues the bone phenotype in the knockin murine model for classical, dominant osteogenesis imperfecta
    • Panaroni, C. et al. In utero transplantation of adult bone marrow decreases perinatal lethality and rescues the bone phenotype in the knockin murine model for classical, dominant osteogenesis imperfecta. Blood 114, 459-468 (2009).
    • (2009) Blood , vol.114 , pp. 459-468
    • Panaroni, C.1
  • 35
    • 33749172211 scopus 로고    scopus 로고
    • Progenitors systemically transplanted into neonatal mice localize to areas of active bone formation in vivo: Implications of cell therapy for skeletal diseases
    • DOI 10.1634/stemcells.2005-0430
    • Wang, X., Li, F. & Niyibizi, C. Progenitors systemically transplanted into neonatal mice localize to areas of active bone formation in vivo: implications of cell therapy for skeletal diseases. Stem Cells 24, 1869-1878 (2006). (Pubitemid 44474163)
    • (2006) Stem Cells , vol.24 , Issue.8 , pp. 1869-1878
    • Wang, X.1    Li, F.2    Niyibizi, C.3
  • 36
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • DOI 10.1242/jcs.01731
    • Canty, E. G. & Kadler, K. E. Procollagen trafficking, processing and fibrillogenesis. J. Cell Sci. 118, 1341-1353 (2005). (Pubitemid 40585115)
    • (2005) Journal of Cell Science , vol.118 , Issue.7 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 37
    • 0020569249 scopus 로고
    • Embryonic lethal mutation in mice induced by retrovirus insertion into the α1(I) collagen gene
    • Schnieke, A., Harbers, K. & Jaenisch, R. Embryonic lethal mutation in mice induced by retrovirus insertion into the alpha 1(I) collagen gene. Nature 304, 315-320 (1983). (Pubitemid 13072750)
    • (1983) Nature , vol.304 , Issue.5924 , pp. 315-320
    • Schnieke, A.1    Harbers, K.2    Jaenisch, R.3
  • 38
    • 33746813256 scopus 로고    scopus 로고
    • Total absence of the alpha2(I) chain of collagen type i causes a rare form of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac valvular problems
    • Malfait, F. et al. Total absence of the alpha2(I) chain of collagen type I causes a rare form of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac valvular problems. J. Med. Genet. 43, e36 (2006).
    • (2006) J. Med. Genet. , vol.43
    • Malfait, F.1
  • 39
    • 0021252139 scopus 로고
    • The clinical features of homozygous α2(I) collagen deficient osteogenesis imperfecta
    • Nicholls, A. C. et al. The clinical features of homozygous alpha 2(I) collagen deficient osteogenesis imperfecta. J. Med. Genet. 21, 257-262 (1984). (Pubitemid 14094462)
    • (1984) Journal of Medical Genetics , vol.21 , Issue.4 , pp. 257-262
    • Nicholls, A.C.1    Osse, G.2    Schloon, H.G.3
  • 40
    • 0028220202 scopus 로고
    • Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
    • DOI 10.1006/jmbi.1994.1199
    • Raghunath, M., Bruckner, P. & Steinmann, B. Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J. Mol. Biol. 236, 940-949 (1994). (Pubitemid 24146332)
    • (1994) Journal of Molecular Biology , vol.236 , Issue.3 , pp. 940-949
    • Raghunath, M.1    Bruckner, P.2    Steinmann, B.3
  • 41
    • 58749097965 scopus 로고    scopus 로고
    • Mutation and polymorphism spectrum in osteogenesis imperfecta type II: Implications for genotype-phenotype relationships
    • Bodian, D. L. et al. Mutation and polymorphism spectrum in osteogenesis imperfecta type II: implications for genotype-phenotype relationships. Hum. Mol. Genet. 18, 463-471 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 463-471
    • Bodian, D.L.1
  • 42
    • 0037040286 scopus 로고    scopus 로고
    • Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen
    • DOI 10.1074/jbc.M110709200
    • Di Lullo, G. A., Sweeney, S. M., Korkko, J., Ala-Kokko, L. & San Antonio, J. D. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 277, 4223-4231 (2002). (Pubitemid 34968685)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 4223-4231
    • Di Lullo, G.A.1    Sweeney, S.M.2    Korkko, J.3    Ala-Kokko, L.4    San Antonio, J.D.5
  • 43
    • 51049121850 scopus 로고    scopus 로고
    • Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates
    • Sweeney, S. M. et al. Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates. J. Biol. Chem. 283, 21187-21197 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21187-21197
    • Sweeney, S.M.1
  • 45
    • 33646593224 scopus 로고    scopus 로고
    • Molecular mechanism of α1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: Unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix
    • DOI 10.1074/jbc.M511830200
    • Makareeva, E., Cabral, W. A., Marini, J. C. & Leikin, S. Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix. J. Biol. Chem. 281, 6463-6470 (2006). (Pubitemid 43847579)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6463-6470
    • Makareeva, E.1    Cabral, W.A.2    Marini, J.C.3    Leikin, S.4
  • 46
    • 0024448810 scopus 로고
    • Mutations that alter the primary structure of type I procollagen have long-range effects on its cleavage by procollagen N-proteinase
    • Dombrowski, K. E., Vogel, B. E. & Prockop, D. J. Mutations that alter the primary structure of type I procollagen have long-range effects on its cleavage by procollagen N-proteinase. Biochemistry 28, 7107-7112 (1989). (Pubitemid 19219900)
    • (1989) Biochemistry , vol.28 , Issue.17 , pp. 7107-7112
    • Dombrowski, K.E.1    Vogel, B.E.2    Prockop, D.J.3
  • 47
    • 0021679317 scopus 로고
    • A heterozygous defect for structurally altered Pro-α2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinase
    • Sippola, M., Kaffe, S. & Prockop, D. J. A heterozygous defect for structurally altered pro-alpha 2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinase. J. Biol. Chem. 259, 14094-14100 (1984). (Pubitemid 15223981)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.22 , pp. 14094-14100
    • Sippola, M.1    Kaffe, S.2    Prockop, D.J.3
  • 48
    • 18544403981 scopus 로고    scopus 로고
    • Identification of a new heterozygous point mutation in the COL1A2 gene leading to skipping of exon 9 in a patient with joint laxity, hyperextensibility of skin and blue sclerae. Mutations in brief no. 166. Online
    • Feshchenko, S. et al. Identification of a new heterozygous point mutation in the COL1A2 gene leading to skipping of exon 9 in a patient with joint laxity, hyperextensibility of skin and blue sclerae. Mutations in brief no. 166. Online. Hum. Mutat. 12, 138 (1998).
    • (1998) Hum. Mutat. , vol.12 , pp. 138
    • Feshchenko, S.1
  • 49
    • 0026505955 scopus 로고
    • The molecular defect in a family with mild atypical osteogenesis imperfecta and extreme joint hypermobility: Exon skipping caused by an 11-bp deletion from an intron in one COL1A2 allele
    • Nicholls, A. C., Oliver, J., Renouf, D. V., Heath, D. A. & Pope, F. M. The molecular defect in a family with mild atypical osteogenesis imperfecta and extreme joint hypermobility: exon skipping caused by an 11-bp deletion from an intron in one COL1A2 allele. Hum. Genet. 88, 627-633 (1992).
    • (1992) Hum. Genet. , vol.88 , pp. 627-633
    • Nicholls, A.C.1    Oliver, J.2    Renouf, D.V.3    Heath, D.A.4    Pope, F.M.5
  • 50
    • 0034071189 scopus 로고    scopus 로고
    • Partial COL1A2 gene duplication produces features of osteogenesis imperfecta and Ehlers-Danlos syndrome type VII
    • DOI 10.1007/s004390051004
    • Raff, M. L., Craigen, W. J., Smith, L. T., Keene, D. R. & Byers, P. H. Partial COL1A2 gene duplication produces features of osteogenesis imperfecta and Ehlers-Danlos syndrome type VII. Hum. Genet. 106, 19-28 (2000). (Pubitemid 30156389)
    • (2000) Human Genetics , vol.106 , Issue.1 , pp. 19-28
    • Raff, M.L.1    Craigen, W.J.2    Smith, L.T.3    Keene, D.R.4    Byers, P.H.5
  • 51
    • 79957625666 scopus 로고    scopus 로고
    • COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta
    • doi:10.1002/humu.21475
    • Lindahl, K. et al. COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta. Hum. Mutat. doi:10.1002/humu.21475.
    • Hum. Mutat.
    • Lindahl, K.1
  • 52
    • 0025170586 scopus 로고
    • The clinical features of osteogenesis imperfecta resulting from a non-functional carboxy terminal pro alpha 1(I) propeptide of type i procollagen and a severe deficiency of normal type i collagen in tissues
    • Cole, W. G., Campbell, P. E., Rogers, J. G. & Bateman, J. F. The clinical features of osteogenesis imperfecta resulting from a non-functional carboxy terminal pro alpha 1(I) propeptide of type I procollagen and a severe deficiency of normal type I collagen in tissues. J. Med. Genet. 27, 545-551 (1990).
    • (1990) J. Med. Genet. , vol.27 , pp. 545-551
    • Cole, W.G.1    Campbell, P.E.2    Rogers, J.G.3    Bateman, J.F.4
  • 53
    • 0027203904 scopus 로고
    • Mutations in the carboxyl-terminal propeptide of the proα1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta
    • Chessler, S. D., Wallis, G. A. & Byers, P. H. Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta. J. Biol. Chem. 268, 18218-18225 (1993). (Pubitemid 23260346)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 18218-18225
    • Chessler, S.D.1    Wallis, G.A.2    Byers, P.H.3
  • 54
    • 47049089675 scopus 로고    scopus 로고
    • Defective C-propeptides of the proalpha2(I) chain of type i procollagen impede molecular assembly and result in osteogenesis imperfecta
    • Pace, J. M. et al. Defective C-propeptides of the proalpha2(I) chain of type I procollagen impede molecular assembly and result in osteogenesis imperfecta. J. Biol. Chem. 283, 16061-16067 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 16061-16067
    • Pace, J.M.1
  • 55
    • 0025128975 scopus 로고
    • Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen predicts an elongated proα1(I) chain and results in osteogenesis imperfecta type I
    • Willing, M. C., Cohn, D. H. & Byers, P. H. Frameshift mutation near the 3′ end of the COL1A1 gene of type I collagen predicts an elongated Pro alpha 1(I) chain and results in osteogenesis imperfecta type I. J. Clin. Invest. 85, 282-290 (1990). (Pubitemid 20030320)
    • (1990) Journal of Clinical Investigation , vol.85 , Issue.1 , pp. 282-290
    • Willing, M.C.1    Cohn, D.H.2    Byers, P.H.3
  • 56
    • 0034805122 scopus 로고    scopus 로고
    • Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta
    • DOI 10.1002/humu.1193
    • Pace, J. M., Atkinson, M., Willing, M. C., Wallis, G. & Byers, P. H. Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. Hum. Mutat. 18, 319-326 (2001). (Pubitemid 32916862)
    • (2001) Human Mutation , vol.18 , Issue.4 , pp. 319-326
    • Pace, J.M.1    Atkinson, M.2    Willing, M.C.3    Wallis, G.4    Byers, P.H.5
  • 57
    • 0038193527 scopus 로고    scopus 로고
    • Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of α chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix
    • DOI 10.1074/jbc.M212523200
    • Cabral, W. A. et al. Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix. J. Biol. Chem. 278, 10006-10012 (2003). (Pubitemid 36800253)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10006-10012
    • Cabral, W.A.1    Mertts, M.V.2    Makareeva, E.3    Colige, A.4    Tekin, M.5    Pandya, A.6    Leikin, S.7    Marini, J.C.8
  • 59
    • 34047204759 scopus 로고    scopus 로고
    • Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood
    • DOI 10.1002/humu.20455
    • Malfait, F. et al. Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood. Hum. Mutat. 28, 387-395 (2007). (Pubitemid 46542925)
    • (2007) Human Mutation , vol.28 , Issue.4 , pp. 387-395
    • Malfait, F.1    Symoens, S.2    De Backer, J.3    Hermanns-Le, T.4    Sakalihasan, N.5    Lapiere, C.M.6    Coucke, P.7    De Paepe, A.8
  • 61
  • 62
    • 52649097968 scopus 로고    scopus 로고
    • The c.3040C ≥ T mutation in COL1A1 is recurrent in Korean patients with infantile cortical hyperostosis (Caffey disease)
    • Cho, T. J. et al. The c.3040C ≥ T mutation in COL1A1 is recurrent in Korean patients with infantile cortical hyperostosis (Caffey disease). J. Hum. Genet. 53, 947-949 (2008).
    • (2008) J. Hum. Genet. , vol.53 , pp. 947-949
    • Cho, T.J.1
  • 63
    • 72449160579 scopus 로고    scopus 로고
    • The unfolded protein response and its relevance to connective tissue diseases
    • Boot-Handford, R. P. & Briggs, M. D. The unfolded protein response and its relevance to connective tissue diseases. Cell Tissue Res. 339, 197-211 (2009).
    • (2009) Cell Tissue Res. , vol.339 , pp. 197-211
    • Boot-Handford, R.P.1    Briggs, M.D.2
  • 64
    • 66349112572 scopus 로고    scopus 로고
    • Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection
    • Ishida, Y. et al. Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection. Mol. Biol. Cell 20, 2744-2754 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2744-2754
    • Ishida, Y.1
  • 65
    • 0028902639 scopus 로고
    • Endoplasmic reticulum-mediated quality control of type i collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly
    • Lamandé, S. R. et al. Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly. J. Biol. Chem. 270, 8642-8649 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 8642-8649
    • Lamandé, S.R.1
  • 66
    • 0033600789 scopus 로고    scopus 로고
    • Proteasomal degradation of unassembled mutant type i collagen pro-alpha1(I) chains
    • Fitzgerald, J., Lamandé, S. R. & Bateman, J. F. Proteasomal degradation of unassembled mutant type I collagen pro-alpha1(I) chains. J. Biol. Chem. 274, 27392-27398 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27392-27398
    • Fitzgerald, J.1    Lamandé, S.R.2    Bateman, J.F.3
  • 68
    • 0029065173 scopus 로고
    • Extracellular matrix stoichiometry in osteoblasts from patients with osteogenesis imperfecta
    • Fedarko, N. S., Robey, P. G. & Vetter, U. K. Extracellular matrix stoichiometry in osteoblasts from patients with osteogenesis imperfecta. J. Bone Miner. Res. 10, 1122-1129 (1995).
    • (1995) J. Bone Miner. Res. , vol.10 , pp. 1122-1129
    • Fedarko, N.S.1    Robey, P.G.2    Vetter, U.K.3
  • 69
    • 0029900432 scopus 로고    scopus 로고
    • Long-term extracellular matrix metabolism by cultured human osteogenesis imperfecta osteoblasts
    • Fedarko, N. S., Sponseller, P. D. & Shapiro, J. R. Long-term extracellular matrix metabolism by cultured human osteogenesis imperfecta osteoblasts. J. Bone Miner. Res. 11, 800-805 (1996). (Pubitemid 26172804)
    • (1996) Journal of Bone and Mineral Research , vol.11 , Issue.6 , pp. 800-805
    • Fedarko, N.S.1    Sponseller, P.D.2    Shapiro, J.R.3
  • 70
    • 78649906076 scopus 로고    scopus 로고
    • Nanoscale morphology of Type i collagen is altered in the Brtl mouse model of osteogenesis imperfecta
    • Wallace, J. M., Orr, B. G., Marini, J. C. & Holl, M. M. Nanoscale morphology of Type I collagen is altered in the Brtl mouse model of osteogenesis imperfecta. J. Struct. Biol. 173, 146-152 (2011).
    • (2011) J. Struct. Biol. , vol.173 , pp. 146-152
    • Wallace, J.M.1    Orr, B.G.2    Marini, J.C.3    Holl, M.M.4
  • 71
    • 77649182181 scopus 로고    scopus 로고
    • CRTAP deficiency leads to abnormally high bone matrix mineralization in a murine model and in children with osteogenesis imperfecta type VII
    • Fratzl-Zelman, N. et al. CRTAP deficiency leads to abnormally high bone matrix mineralization in a murine model and in children with osteogenesis imperfecta type VII. Bone 46, 820-826 (2009).
    • (2009) Bone , vol.46 , pp. 820-826
    • Fratzl-Zelman, N.1
  • 72
    • 43049121656 scopus 로고    scopus 로고
    • Evidence that abnormal high bone mineralization in growing children with osteogenesis imperfecta is not associated with specific collagen mutations
    • Roschger, P. et al. Evidence that abnormal high bone mineralization in growing children with osteogenesis imperfecta is not associated with specific collagen mutations. Calcif. Tissue Int. 82, 263-270 (2008).
    • (2008) Calcif. Tissue Int. , vol.82 , pp. 263-270
    • Roschger, P.1
  • 73
    • 0025878595 scopus 로고
    • Osteogenesis imperfecta: Changes in noncollagenous proteins in bone
    • Vetter, U. et al. Osteogenesis imperfecta: changes in noncollagenous proteins in bone. J. Bone Miner. Res. 6, 501-505 (1991).
    • (1991) J. Bone Miner. Res. , vol.6 , pp. 501-505
    • Vetter, U.1
  • 75
    • 0030439896 scopus 로고    scopus 로고
    • Mineral changes in a mouse model of osteogenesis imperfecta detected by Fourier transform infrared microscopy
    • Camacho, N. P., Landis, W. J. & Boskey, A. L. Mineral changes in a mouse model of osteogenesis imperfecta detected by Fourier transform infrared microscopy. Connect. Tissue Res. 35, 259-265 (1996). (Pubitemid 27118857)
    • (1996) Connective Tissue Research , vol.35 , Issue.1-4 , pp. 259-265
    • Camacho, N.P.1    Landis, W.J.2    Boskey, A.L.3
  • 77
    • 77649187517 scopus 로고    scopus 로고
    • Bisphosphonate treatment modifies canine bone mineral and matrix properties and their heterogeneity
    • Gourion-Arsiquaud, S. et al. Bisphosphonate treatment modifies canine bone mineral and matrix properties and their heterogeneity. Bone 46, 666-672 (2010).
    • (2010) Bone , vol.46 , pp. 666-672
    • Gourion-Arsiquaud, S.1
  • 78
    • 78651341860 scopus 로고    scopus 로고
    • Cellular communications in bone homeostasis and repair
    • Nakahama, K. I. Cellular communications in bone homeostasis and repair. Cell. Mol. Life Sci. 67, 4001-4009 (2010).
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 4001-4009
    • Nakahama, K.I.1
  • 80
    • 0033657798 scopus 로고    scopus 로고
    • A light and electron microscopic study of osteogenesis imperfecta bone samples, with reference to collagen chemistry and clinical phenotype
    • Sarathchandra, P., Pope, F. M., Kayser, M. V. & Ali, S. Y. A light and electron microscopic study of osteogenesis imperfecta bone samples, with reference to collagen chemistry and clinical phenotype. J. Pathol. 192, 385-395 (2000).
    • (2000) J. Pathol. , vol.192 , pp. 385-395
    • Sarathchandra, P.1    Pope, F.M.2    Kayser, M.V.3    Ali, S.Y.4
  • 81
    • 72049100698 scopus 로고    scopus 로고
    • The role of collagen crosslinking in differentiation of human mesenchymal stem cells and MC3T3-E1 cells
    • Fernandes, H. et al. The role of collagen crosslinking in differentiation of human mesenchymal stem cells and MC3T3-E1 cells. Tissue Eng. Part A 15, 3857-3867 (2009).
    • (2009) Tissue Eng. Part A , vol.15 , pp. 3857-3867
    • Fernandes, H.1
  • 83
    • 2542497037 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
    • DOI 10.1074/jbc.M312807200
    • Vranka, J. A., Sakai, L. Y. & Bächinger, H. P. Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 279, 23615-23621 (2004). (Pubitemid 38685676)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 23615-23621
    • Vranka, J.A.1    Sakai, L.Y.2    Bachinger, H.P.3
  • 84
    • 77449136859 scopus 로고    scopus 로고
    • Location of 3-hydroxyproline residues in collagen types, I, II, III, and V/XI implies a role in fibril supramolecular assembly
    • Weis, M. A. et al. Location of 3-hydroxyproline residues in collagen types, I, II, III, and V/XI implies a role in fibril supramolecular assembly. J. Biol. Chem. 285, 2580-2590 (2009).
    • (2009) J. Biol. Chem. , vol.285 , pp. 2580-2590
    • Weis, M.A.1
  • 85
    • 67650522903 scopus 로고    scopus 로고
    • Biochemical characterization of the prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B complex
    • Ishikawa, Y., Wirz, J., Vranka, J. A., Nagata, K. & Bächinger, H. P. Biochemical characterization of the prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B complex. J. Biol. Chem. 284, 17641-17647 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17641-17647
    • Ishikawa, Y.1    Wirz, J.2    Vranka, J.A.3    Nagata, K.4    Bächinger, H.P.5
  • 87
    • 0033609863 scopus 로고    scopus 로고
    • Molecular characterization of a novel basement membrane-associated proteoglycan, leprecan
    • Wassenhove-McCarthy, D. J. & McCarthy, K. J. Molecular characterization of a novel basement membrane-associated proteoglycan, leprecan. J. Biol. Chem. 274, 25004-25017 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25004-25017
    • Wassenhove-Mccarthy, D.J.1    McCarthy, K.J.2
  • 89
    • 34548240257 scopus 로고    scopus 로고
    • Components of the collagen prolyl 3-hydroxylation complex are crucial for normal bone development
    • Marini, J. C., Cabral, W. A., Barnes, A. M. & Chang, W. Components of the collagen prolyl 3-hydroxylation complex are crucial for normal bone development. Cell Cycle 6, 1675-1681 (2007). (Pubitemid 47327916)
    • (2007) Cell Cycle , vol.6 , Issue.14 , pp. 1675-1681
    • Marini, J.C.1    Cabral, W.A.2    Barnes, A.M.3    Chang, W.4
  • 90
    • 0032805509 scopus 로고    scopus 로고
    • CDNA cloning, characterization and chromosome mapping of Crtap encoding the mouse cartilage associated protein
    • DOI 10.1016/S0945-053X(99)00002-5, PII S0945053X99000025
    • Morello, R. et al. cDNA cloning, characterization and chromosome mapping of Crtap encoding the mouse cartilage associated protein. Matrix Biol. 18, 319-324 (1999). (Pubitemid 29324746)
    • (1999) Matrix Biology , vol.18 , Issue.3 , pp. 319-324
    • Morello, R.1    Tonachini, L.2    Monticone, M.3    Viggiano, L.4    Rocchi, M.5    Cancedda, R.6    Castagnola, P.7
  • 91
    • 72449183578 scopus 로고    scopus 로고
    • Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta
    • Marini, J. C., Cabral, W. A. & Barnes, A. M. Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta. Cell Tissue Res. 339, 59-70 (2009).
    • (2009) Cell Tissue Res. , vol.339 , pp. 59-70
    • Marini, J.C.1    Cabral, W.A.2    Barnes, A.M.3
  • 92
    • 77956271626 scopus 로고    scopus 로고
    • Generalized connective tissue disease in Crtap-/- mouse
    • Baldridge, D. et al. Generalized connective tissue disease in Crtap-/- mouse. PLoS ONE 5, e10560 (2010).
    • (2010) PLoS ONE , vol.5
    • Baldridge, D.1
  • 93
    • 65949109910 scopus 로고    scopus 로고
    • Recessive osteogenesis imperfecta caused by LEPRE1 mutations: Clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation
    • Willaert, A. et al. Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation. J. Med. Genet. 46, 233-241 (2009).
    • (2009) J. Med. Genet. , vol.46 , pp. 233-241
    • Willaert, A.1
  • 94
    • 70350680484 scopus 로고    scopus 로고
    • Expression of prolyl 3-hydroxylase genes in embryonic and adult mouse tissues
    • Vranka, J., Stadler, H. S. & Bächinger, H. P. Expression of prolyl 3-hydroxylase genes in embryonic and adult mouse tissues. Cell Struct. Funct. 34, 97-104 (2009).
    • (2009) Cell Struct. Funct. , vol.34 , pp. 97-104
    • Vranka, J.1    Stadler, H.S.2    Bächinger, H.P.3
  • 95
    • 80052064564 scopus 로고    scopus 로고
    • A founder mutation in LEPRE1 causes lethal recessive type VIII osteogenesis imperfecta and occurs in West Africans and African Americans
    • Gothenburg, Sweden
    • Cabral, W. A. et al. A founder mutation in LEPRE1 causes lethal recessive type VIII osteogenesis imperfecta and occurs in West Africans and African Americans. Presented at the European Society of Human Genetics Annual Conference (Gothenburg, Sweden, 2010).
    • (2010) Presented at the European Society of Human Genetics Annual Conference
    • Cabral, W.A.1
  • 96
    • 77952756514 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones
    • Vranka, J. A. et al. Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones. J. Biol. Chem. 285, 17253-17262 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 17253-17262
    • Vranka, J.A.1
  • 97
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
    • Bächinger, H. P. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem. 262, 17144-17148 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 17144-17148
    • Bächinger, H.P.1
  • 98
    • 0025968746 scopus 로고
    • Cyclosporin a slows collagen triple-helix formation in vivo: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase
    • Steinmann, B., Bruckner, P. & Superti-Furga, A. Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. J. Biol. Chem. 266, 1299-1303 (1991). (Pubitemid 21907258)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.2 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 99
    • 79953087965 scopus 로고    scopus 로고
    • Mutations in PPIB (cyclophilin B) delay type i procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes
    • Pyott, S. M. et al. Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Hum. Mol. Genet. 20, 1595-1609 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1595-1609
    • Pyott, S.M.1
  • 100
    • 77952597930 scopus 로고    scopus 로고
    • Osteogenesis imperfecta, normal collagen folding, and lack of cyclophilin B
    • Van Dijk, F. S., Cobben, J. M. & Pals, G. Osteogenesis imperfecta, normal collagen folding, and lack of cyclophilin B. N. Engl. J. Med. 362, 1940-1941 (2010).
    • (2010) N. Engl. J. Med. , vol.362 , pp. 1940-1941
    • Van Dijk, F.S.1    Cobben, J.M.2    Pals, G.3
  • 101
    • 74249109599 scopus 로고    scopus 로고
    • Severe osteogenesis imperfecta in cyclophilin B-deficient mice
    • Choi, J. W. et al. Severe osteogenesis imperfecta in cyclophilin B-deficient mice. PLoS Genet. 5, e1000750 (2009).
    • (2009) PLoS Genet. , vol.5
    • Choi, J.W.1
  • 102
    • 77949442552 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex
    • Chang, W., Barnes, A. M., Cabral, W. A., Bodurtha, J. N. & Marini, J. C. Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex. Hum. Mol. Genet. 19, 223-234 (2009).
    • (2009) Hum. Mol. Genet. , vol.19 , pp. 223-234
    • Chang, W.1    Barnes, A.M.2    Cabral, W.A.3    Bodurtha, J.N.4    Marini, J.C.5
  • 103
    • 55949095578 scopus 로고    scopus 로고
    • Effect of the -Gly-3(S.)-hydroxyprolyl-4(R.)-hydroxyprolyl-tripeptide unit on the stability of collagen model peptides
    • Mizuno, K., Peyton, D. H., Hayashi, T., Engel, J. & Bächinger, H. P. Effect of the -Gly-3(S.)-hydroxyprolyl-4(R.)-hydroxyprolyl-tripeptide unit on the stability of collagen model peptides. FEBS J. 275, 5830-5840 (2008).
    • (2008) FEBS J. , vol.275 , pp. 5830-5840
    • Mizuno, K.1    Peyton, D.H.2    Hayashi, T.3    Engel, J.4    Bächinger, H.P.5
  • 105
    • 79952489518 scopus 로고    scopus 로고
    • Exome sequencing identifies truncating mutations in human SERPINF1 in autosomal-recessive osteogenesis imperfecta
    • Becker, J. et al. Exome sequencing identifies truncating mutations in human SERPINF1 in autosomal-recessive osteogenesis imperfecta. Am. J. Hum. Genet. 88, 362-371 (2011).
    • (2011) Am. J. Hum. Genet. , vol.88 , pp. 362-371
    • Becker, J.1
  • 107
    • 0029132706 scopus 로고
    • Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum
    • Smith, T., Ferreira, L. R., Hebert, C., Norris, K. & Sauk, J. J. Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J. Biol. Chem. 270, 18323-18328 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18323-18328
    • Smith, T.1    Ferreira, L.R.2    Hebert, C.3    Norris, K.4    Sauk, J.J.5
  • 108
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai, N. et al. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J. Cell Biol. 150, 1499-1506 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 1499-1506
    • Nagai, N.1
  • 109
    • 33745747824 scopus 로고    scopus 로고
    • Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis
    • DOI 10.1091/mbc.E05-11-1065
    • Ishida, Y. et al. Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis. Mol. Biol. Cell 17, 2346-2355 (2006). (Pubitemid 44011749)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2346-2355
    • Ishida, Y.1    Kubota, H.2    Yamamoto, A.3    Kitamura, A.4    Bachinger, H.P.5    Nagata, K.6
  • 110
    • 73449083755 scopus 로고    scopus 로고
    • Autophagy eliminates a specific species of misfolded procollagen and plays a protective role in cell survival against ER stress
    • Ishida, Y. & Nagata, K. Autophagy eliminates a specific species of misfolded procollagen and plays a protective role in cell survival against ER stress. Autophagy 5, 1217-1219 (2009).
    • (2009) Autophagy , vol.5 , pp. 1217-1219
    • Ishida, Y.1    Nagata, K.2
  • 111
    • 68249130696 scopus 로고    scopus 로고
    • A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta
    • Drögemüller, C. et al. A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta. PLoS Genet. 5, e1000579 (2009).
    • (2009) PLoS Genet. , vol.5
    • Drögemüller, C.1
  • 112
    • 57649134970 scopus 로고    scopus 로고
    • The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens
    • Ishikawa, Y., Vranka, J., Wirz, J., Nagata, K. & Bächinger, H. P. The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens. J. Biol. Chem. 283, 31584-31590 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31584-31590
    • Ishikawa, Y.1    Vranka, J.2    Wirz, J.3    Nagata, K.4    Bächinger, H.P.5
  • 114
    • 77957745048 scopus 로고    scopus 로고
    • FKBP10 and bruck syndrome: Phenotypic heterogeneity or call for reclassification?
    • Shaheen, R., Al-Owain, M., Sakati, N., Alzayed, Z. S. & Alkuraya, F. S. FKBP10 and bruck syndrome: Phenotypic heterogeneity or call for reclassification? Am. J. Hum. Genet. 87, 571 (2010).
    • (2010) Am. J. Hum. Genet. , vol.87 , pp. 571
    • Shaheen, R.1    Al-Owain, M.2    Sakati, N.3    Alzayed, Z.S.4    Alkuraya, F.S.5
  • 115
    • 79951842354 scopus 로고    scopus 로고
    • Mutations in FKBP10 cause recessive osteogenesis imperfecta and type 1 Bruck syndrome
    • Kelley, B. P. et al. Mutations in FKBP10 cause recessive osteogenesis imperfecta and type 1 Bruck syndrome. J. Bone Miner. Res. 26, 666-672 (2010).
    • (2010) J. Bone Miner. Res. , vol.26 , pp. 666-672
    • Kelley, B.P.1
  • 117
    • 17044454221 scopus 로고    scopus 로고
    • Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis
    • van der Slot, A. J. et al. Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J. Biol. Chem. 278, 40967-40972 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 40967-40972
    • Van Der Slot, A.J.1
  • 119
    • 77955084141 scopus 로고    scopus 로고
    • Identification of a frameshift mutation in Osterix in a patient with recessive osteogenesis imperfecta
    • Lapunzina, P. et al. Identification of a frameshift mutation in Osterix in a patient with recessive osteogenesis imperfecta. Am. J. Hum. Genet. 87, 110-114 (2010).
    • (2010) Am. J. Hum. Genet. , vol.87 , pp. 110-114
    • Lapunzina, P.1
  • 120
    • 16244405603 scopus 로고    scopus 로고
    • Mammalian SP/KLF transcription factors: Bring in the family
    • DOI 10.1016/j.ygeno.2005.01.005
    • Suske, G., Bruford, E. & Philipsen, S. Mammalian SP/KLF transcription factors: bring in the family. Genomics 85, 551-556 (2005). (Pubitemid 40463690)
    • (2005) Genomics , vol.85 , Issue.5 , pp. 551-556
    • Suske, G.1    Bruford, E.2    Philipsen, S.3
  • 121
    • 0037059614 scopus 로고    scopus 로고
    • The novel zinc finger-containing transcription factor Osterix is required for osteoblast differentiation and bone formation
    • DOI 10.1016/S0092-8674(01)00622-5
    • Nakashima, K. et al. The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation. Cell 108, 17-29 (2002). (Pubitemid 34137009)
    • (2002) Cell , vol.108 , Issue.1 , pp. 17-29
    • Nakashima, K.1    Zhou, X.2    Kunkel, G.3    Zhang, Z.4    Deng, J.M.5    Behringer, R.R.6    De Crombrugghe, B.7
  • 122
    • 0021274458 scopus 로고
    • Hearing loss in patients with osteogenesis imperfecta. A clinical and audiological study of 201 patients
    • Pedersen, U. Hearing loss in patients with osteogenesis imperfecta. A clinical and audiological study of 201 patients. Scand. Audiol. 13, 67-74 (1984). (Pubitemid 14123814)
    • (1984) Scandinavian Audiology , vol.13 , Issue.2 , pp. 67-74
    • Pedersen, U.1
  • 124
    • 0035060813 scopus 로고    scopus 로고
    • How common is hearing impairment in osteogenesis imperfecta?
    • DOI 10.1258/0022215011907442
    • Paterson, C. R., Monk, E. A. & McAllion, S. J. How common is hearing impairment in osteogenesis imperfecta? J. Laryngol. Otol. 115, 280-282 (2001). (Pubitemid 32324594)
    • (2001) Journal of Laryngology and Otology , vol.115 , Issue.4 , pp. 280-282
    • Paterson, C.R.1    Monk, E.A.2    McAllion, S.J.3
  • 128
    • 0021074768 scopus 로고
    • Stapedectomy in osteogenesis imperfecta
    • Pedersen, U. & Elbrønd, O. Stapedectomy in osteogenesis imperfecta. ORL J. Otorhinolaryngol Relat. Spec. 45, 330-337 (1983). (Pubitemid 14243043)
    • (1983) ORL , vol.45 , Issue.6 , pp. 330-337
    • Pedersen, U.1    Elbrond, O.2
  • 129
    • 0030740399 scopus 로고    scopus 로고
    • Hearing loss (in nonoperated ears) in relation to age in osteogenesis imperfecta type, i
    • Garretsen, A. J., Cremers, C. W. & Huygén, P. L. Hearing loss (in nonoperated ears) in relation to age in osteogenesis imperfecta type, I. Ann. Otol. Rhinol. Laryngol. 106, 575-582 (1997).
    • (1997) Ann. Otol. Rhinol. Laryngol. , vol.106 , pp. 575-582
    • Garretsen, A.J.1    Cremers, C.W.2    Huygén, P.L.3
  • 130
    • 0019994983 scopus 로고
    • Findings and long-term surgical results in the hearing loss of osteogenesis imperfecta
    • Shea, J. J. & Postma, D. S. Findings and long-term surgical results in the hearing loss of osteogenesis imperfecta. Arch. Otolaryngol. 108, 467-470 (1982). (Pubitemid 12050357)
    • (1982) Archives of Otolaryngology , vol.108 , Issue.8 , pp. 467-470
    • Shea, J.J.1    Postma, D.S.2
  • 131
    • 0141677662 scopus 로고    scopus 로고
    • Stapes surgery in osteogenesis imperfecta: Results of a new series
    • DOI 10.1097/00129492-200309000-00004
    • van der Rijt, A. J. & Cremers, C. W. Stapes surgery in osteogenesis imperfecta: results of a new series. Otol. Neurootol. 24, 717-722 (2003). (Pubitemid 37122534)
    • (2003) Otology and Neurotology , vol.24 , Issue.5 , pp. 717-722
    • Van Der Rijt, A.J.M.1    Cremers, C.W.R.J.2
  • 134
    • 0017874914 scopus 로고
    • Classification of osteogenesis imperfecta by dental characteristics
    • Levin, L. S., Salinas, C. F. & Jorgenson, R. J. Classification of osteogenesis imperfecta by dental characteristics. Lancet 1, 332-333 (1978). (Pubitemid 8273583)
    • (1978) Lancet , vol.1 , Issue.8059 , pp. 332-333
    • Levin, L.S.1    Salinas, C.F.2    Jorgenson, R.J.3
  • 136
    • 0036518567 scopus 로고    scopus 로고
    • Dental aberrations in children and adolescents with osteogenesis imperfecta
    • Malmgren, B. & Norgren, S. Dental aberrations in children and adolescents with osteogenesis imperfecta. Acta Odontol. Scand. 60, 65-71 (2002).
    • (2002) Acta Odontol. Scand. , vol.60 , pp. 65-71
    • Malmgren, B.1    Norgren, S.2
  • 137
    • 77649320467 scopus 로고    scopus 로고
    • Dentinogenesis imperfecta in children with osteogenesis imperfecta: A clinical and ultrastructural study
    • Majorana, A. et al. Dentinogenesis imperfecta in children with osteogenesis imperfecta: a clinical and ultrastructural study. Int. J. Paediatr. Dent. 20, 112-118 (2010).
    • (2010) Int. J. Paediatr. Dent. , vol.20 , pp. 112-118
    • Majorana, A.1
  • 138
    • 0030136333 scopus 로고    scopus 로고
    • Mild forms of dentinogenesis imperfecta in association with osteogenesis imperfecta as characterized by light and transmission electron microscopy
    • Waltimo, J., Ojanotko-Harri, A. & Lukinmaa, P. L. Mild forms of dentinogenesis imperfecta in association with osteogenesis imperfecta as characterized by light and transmission electron microscopy. J. Oral Pathol. Med. 25, 256-264 (1996). (Pubitemid 126447420)
    • (1996) Journal of Oral Pathology and Medicine , vol.25 , Issue.5 , pp. 256-264
    • Waltimo, J.1    Ojanotko-Harri, A.2    Lukinmaa, P.-L.3
  • 140
    • 77952672567 scopus 로고    scopus 로고
    • Genotype-phenotype correlations in nonlethal osteogenesis imperfecta caused by mutations in the helical domain of collagen type i
    • Rauch, F., Lalic, L., Roughley, P. & Glorieux, F. H. Genotype-phenotype correlations in nonlethal osteogenesis imperfecta caused by mutations in the helical domain of collagen type I. Eur. J. Hum. Genet. 18, 642-647 (2010).
    • (2010) Eur. J. Hum. Genet. , vol.18 , pp. 642-647
    • Rauch, F.1    Lalic, L.2    Roughley, P.3    Glorieux, F.H.4
  • 141
    • 0025270340 scopus 로고
    • Transcription of a mutant collagen i gene is a cell type and stage-specific marker for odontoblast and osteoblast differentiation
    • Schwarz, M., Harbers, K. & Kratochwil, K. Transcription of a mutant collagen I gene is a cell type and stage-specific marker for odontoblast and osteoblast differentiation. Development 108, 717-726 (1990).
    • (1990) Development , vol.108 , pp. 717-726
    • Schwarz, M.1    Harbers, K.2    Kratochwil, K.3
  • 142
    • 0028525579 scopus 로고
    • Hyperfibers and vesicles in dentin matrix in dentinogenesis imperfecta (DI) associated with osteogenesis imperfecta (OI)
    • Waltimo, J. Hyperfibers and vesicles in dentin matrix in dentinogenesis imperfecta (DI) associated with osteogenesis imperfecta (OI). J. Oral Pathol. Med. 23, 389-393 (1994).
    • (1994) J. Oral Pathol. Med. , vol.23 , pp. 389-393
    • Waltimo, J.1
  • 144
    • 0035996545 scopus 로고    scopus 로고
    • Odontoblast dysfunction in osteogenesis imperfecta: An LM, SEM, and ultrastructural study
    • Hall, R. K., Manière, M. C., Palamara, J. & Hemmerle, J. Odontoblast dysfunction in osteogenesis imperfecta: an, LM, SEM, and ultrastructural study. Connect. Tissue Res. 43, 401-405 (2002). (Pubitemid 34777955)
    • (2002) Connective Tissue Research , vol.43 , Issue.2-3 , pp. 401-405
    • Hall, R.K.1    Maniere, M.-C.2    Palamara, J.3    Hemmerle, J.4
  • 145
    • 0027771906 scopus 로고
    • Communicating hydrocephalus, basilar invagination, and other neurologic features in osteogenesis imperfecta
    • 12 I
    • Charnas, L. R. & Marini, J. C. Communicating hydrocephalus, basilar invagination, and other neurologic features in osteogenesis imperfecta. Neurology 43, 2603-2608 (1993). (Pubitemid 24004553)
    • (1993) Neurology , vol.43 , pp. 2603-2608
    • Charnas, L.R.1    Marini, J.C.2
  • 146
    • 0030968189 scopus 로고    scopus 로고
    • Basilar invagination in osteogenesis imperfecta and related osteochondrodysplasias: Medical and surgical management
    • Sawin, P. D. & Menezes, A. H. Basilar invagination in osteogenesis imperfecta and related osteochondrodysplasias: medical and surgical management. J. Neurosurg. 86, 950-960 (1997). (Pubitemid 27230137)
    • (1997) Journal of Neurosurgery , vol.86 , Issue.6 , pp. 950-960
    • Sawin, P.D.1    Menezes, A.H.2
  • 147
    • 51749115116 scopus 로고    scopus 로고
    • Specific entities affecting the craniocervical region: Osteogenesis imperfecta and related osteochondrodysplasias: Medical and surgical management of basilar impression
    • Menezes, A. H. Specific entities affecting the craniocervical region: osteogenesis imperfecta and related osteochondrodysplasias: medical and surgical management of basilar impression. Childs Nerv. Syst. 24, 1169-1172 (2008).
    • (2008) Childs Nerv. Syst. , vol.24 , pp. 1169-1172
    • Menezes, A.H.1
  • 148
    • 0027458499 scopus 로고
    • Evaluation of growth hormone axis and responsiveness to growth stimulation of short children with osteogenesis imperfecta
    • DOI 10.1002/ajmg.1320450223
    • Marini, J. C., Bordenick, S., Heavner, G., Rose, S. & Chrousos, G. P. Evaluation of growth hormone axis and responsiveness to growth stimulation of short children with osteogenesis imperfecta. Am. J. Med. Genet. 45, 261-264 (1993). (Pubitemid 23030706)
    • (1993) American Journal of Medical Genetics , vol.45 , Issue.2 , pp. 261-264
    • Marini, J.C.1    Bordenick, S.2    Heavner, G.3    Rose, S.4    Chrousos, G.P.5
  • 149
    • 0037304052 scopus 로고    scopus 로고
    • Positive linear growth and bone responses to growth hormone treatment in children with types III and IV osteogenesis imperfecta: High predictive value of the carboxyterminal propeptide of type I procollagen
    • DOI 10.1359/jbmr.2003.18.2.237
    • Marini, J. C. et al. Positive linear growth and bone responses to growth hormone treatment in children with types III and IV osteogenesis imperfecta: high predictive value of the carboxyterminal propeptide of type I procollagen. J. Bone Miner. Res. 18, 237-243 (2003). (Pubitemid 36125916)
    • (2003) Journal of Bone and Mineral Research , vol.18 , Issue.2 , pp. 237-243
    • Marini, J.C.1    Hopkins, E.2    Glorieux, F.H.3    Chrousos, G.P.4    Reynolds, J.C.5    Gundberg, C.M.6    Reing, C.M.7
  • 150
    • 0035233144 scopus 로고    scopus 로고
    • Mortality in various types of osteogenesis imperfecta
    • Singer, R. B., Ogston, S. A. & Paterson, C. R. Mortality in various types of osteogenesis imperfecta. J. Insur. Med. 33, 216-220 (2001).
    • (2001) J. Insur. Med. , vol.33 , pp. 216-220
    • Singer, R.B.1    Ogston, S.A.2    Paterson, C.R.3
  • 151
    • 0032770080 scopus 로고    scopus 로고
    • Spinal deformity, pulmonary compromise, and quality of life in osteogenesis imperfecta
    • DOI 10.1097/00007632-199908150-00008
    • Widmann, R. F. et al. Spinal deformity, pulmonary compromise, and quality of life in osteogenesis imperfecta. Spine (Phila. Pa 1976) 24, 1673-1678 (1999). (Pubitemid 29387923)
    • (1999) Spine , vol.24 , Issue.16 , pp. 1673-1678
    • Widmann, R.F.1    Bitan, F.D.2    Laplaza, F.J.3    Burke, S.W.4    DiMaio, M.F.5    Schneider, R.6
  • 152
    • 0024307063 scopus 로고
    • Case report: Pulmonary hypoplasia and osteogenesis imperfecta type II with defective synthesis of alpha I(1) procollagen
    • DOI 10.1016/8756-3282(89)90049-5
    • Shapiro, J. R. et al. Pulmonary hypoplasia and osteogenesis imperfecta type II with defective synthesis of alpha I(1) procollagen. Bone 10, 165-171 (1989). (Pubitemid 19249342)
    • (1989) Bone , vol.10 , Issue.3 , pp. 165-171
    • Shapiro, J.R.1    Burn, V.E.2    Chipman, S.D.3    Jacobs, J.B.4    Schloo, B.5    Reid, L.6    Larsen, N.7    Louis, F.8
  • 153
    • 0022575921 scopus 로고
    • Cardiovascular involvement in osteogenesis imperfecta
    • Hortop, J., Tsipouras, P., Hanley, J. A., Maron, B. J. & Shapiro, J. R. Cardiovascular involvement in osteogenesis imperfecta. Circulation 73, 54-61 (1986). (Pubitemid 16132412)
    • (1986) Circulation , vol.73 , Issue.1 , pp. 54-61
    • Hortop, J.1    Tsipouras, P.2    Hanley, J.A.3
  • 154
    • 76449084511 scopus 로고    scopus 로고
    • Valvular heart disease in osteogenesis imperfecta: Presentation of a case and review of the literature
    • Bonita, R. E., Cohen, I. S. & Berko, B. A. Valvular heart disease in osteogenesis imperfecta: presentation of a case and review of the literature. Echocardiography 27, 69-73 (2010).
    • (2010) Echocardiography , vol.27 , pp. 69-73
    • Bonita, R.E.1    Cohen, I.S.2    Berko, B.A.3
  • 155
    • 57649083318 scopus 로고    scopus 로고
    • Impairment of diastolic function in adult patients affected by osteogenesis imperfecta clinically asymptomatic for cardiac disease: Casuality or causality?
    • Migliaccio, S. et al. Impairment of diastolic function in adult patients affected by osteogenesis imperfecta clinically asymptomatic for cardiac disease: casuality or causality? Int. J. Cardiol. 131, 200-203 (2009).
    • (2009) Int. J. Cardiol. , vol.131 , pp. 200-203
    • Migliaccio, S.1
  • 156
    • 33744805355 scopus 로고    scopus 로고
    • Functional significance of bone density measurements in children with osteogenesis imperfecta
    • DOI 10.2106/JBJS.E.00333
    • Huang, R. P., Ambrose, C. G., Sullivan, E. & Haynes, R. J. Functional significance of bone density measurements in children with osteogenesis imperfecta. J. Bone Joint Surg. Am. 88, 1324-1330 (2006). (Pubitemid 43837128)
    • (2006) Journal of Bone and Joint Surgery - Series A , vol.88 , Issue.6 , pp. 1324-1330
    • Huang, R.P.1    Ambrose, C.G.2    Sullivan, E.3    Haynes, R.J.4
  • 158
    • 2342567864 scopus 로고    scopus 로고
    • Skeletal effects and functional outcome with olpadronate in children with osteogenesis imperfecta: A 2-year randomised placebo-controlled study
    • DOI 10.1016/S0140-6736(04)16101-1, PII S0140673604161011
    • Sakkers, R. et al. Skeletal effects and functional outcome with olpadronate in children with osteogenesis imperfecta: a 2-year randomised placebo-controlled study. Lancet 363, 1427-1431 (2004). (Pubitemid 38586718)
    • (2004) Lancet , vol.363 , Issue.9419 , pp. 1427-1431
    • Sakkers, R.1    Kok, D.2    Engelbert, R.3    Van Dongen, A.4    Jansen, M.5    Pruijs, H.6    Verbout, A.7    Schweitzer, D.8    Uiterwaal, C.9
  • 161
    • 0035106712 scopus 로고    scopus 로고
    • Reliability of the Gross Motor Function Measure for children with osteogenesis imperfecta
    • Ruck-Gibis, J., Plotkin, H., Hanley, J. & Wood-Dauphinee, S. Reliability of the gross motor function measure for children with osteogenesis imperfecta. Pediatr. Phys. Ther. 13, 10-17 (2001). (Pubitemid 32223494)
    • (2001) Pediatric Physical Therapy , vol.13 , Issue.1 , pp. 10-17
    • Ruck-Gibis, J.1    Plotkin, H.2    Hanley, J.3    Wood-Dauphinee, S.4
  • 162
    • 0019376817 scopus 로고
    • Nonoperative treatment of osteogenesis imperfecta: Orthotic and mobility management
    • Bleck, E. E. Nonoperative treatment of osteogenesis imperfecta: orthotic and mobility management. Clin. Orthop. Relat. Res. 111-122 (1981). (Pubitemid 11000297)
    • (1981) Clinical Orthopaedics and Related Research , vol.159 , pp. 111-122
    • Bleck, E.E.1
  • 165
    • 37249024607 scopus 로고    scopus 로고
    • Physical training in children with osteogenesis imperfecta
    • Van Brussel, M. et al. Physical training in children with osteogenesis imperfecta. J. Pediatr. 152, 111-116 (2008).
    • (2008) J. Pediatr. , vol.152 , pp. 111-116
    • Van Brussel, M.1
  • 167
    • 0031976130 scopus 로고    scopus 로고
    • Management of lower-extremity deformities in osteogenesis imperfecta with extensible intramedullary rod technique: A 20-year experience
    • DOI 10.1097/00004694-199801000-00017
    • Luhmann, S. J., Sheridan, J. J., Capelli, A. M. & Schoenecker, P. L. Management of lower-extremity deformities in osteogenesis imperfecta with extensible intramedullary rod technique: a 20-year experience. J. Pediatr. Orthop. 18, 88-94 (1998). (Pubitemid 28051576)
    • (1998) Journal of Pediatric Orthopaedics , vol.18 , Issue.1 , pp. 88-94
    • Luhmann, S.J.1    Sheridan, J.J.2    Capelli, A.M.3    Schoenecker, P.L.4
  • 169
    • 67249089633 scopus 로고    scopus 로고
    • Telescoping versus non-telescoping rods in the treatment of osteogenesis imperfecta
    • El-Adl, G., Khalil, M. A., Enan, A., Mostafa, M. F. & El-Lakkany, M. R. Telescoping versus non-telescoping rods in the treatment of osteogenesis imperfecta. Acta Orthop. Belg. 75, 200-208 (2009).
    • (2009) Acta Orthop. Belg. , vol.75 , pp. 200-208
    • El-Adl, G.1    Khalil, M.A.2    Enan, A.3    Mostafa, M.F.4    El-Lakkany, M.R.5
  • 170
    • 38149052369 scopus 로고    scopus 로고
    • Surgical treatment of osteogenesis imperfecta: Current concepts
    • Esposito, P. & Plotkin, H. Surgical treatment of osteogenesis imperfecta: current concepts. Curr. Opin. Pediatr. 20, 52-57 (2008).
    • (2008) Curr. Opin. Pediatr. , vol.20 , pp. 52-57
    • Esposito, P.1    Plotkin, H.2
  • 171
    • 3042571677 scopus 로고    scopus 로고
    • Elastic sliding central medullary nailing with osteogenesis imperfecta. Fourteen cases at eight years follow-up [French]
    • Boutaud, B. & Laville, J. M. Elastic sliding central medullary nailing with osteogenesis imperfecta. Fourteen cases at eight years follow-up [French]. Rev. Chir. Orthop. Reparatrice Appar. Mot. 90, 304-311 (2004).
    • (2004) Rev. Chir. Orthop. Reparatrice Appar. Mot. , vol.90 , pp. 304-311
    • Boutaud, B.1    Laville, J.M.2
  • 172
    • 16644378418 scopus 로고    scopus 로고
    • Delayed osteotomy but not fracture healing in pediatric osteogenesis imperfecta patients receiving pamidronate
    • DOI 10.1359/JBMR.040814
    • Munns, C. F., Rauch, F., Zeitlin, L., Fassier, F. & Glorieux, F. H. Delayed osteotomy but not fracture healing in pediatric osteogenesis imperfecta patients receiving pamidronate. J. Bone Miner. Res. 19, 1779-1786 (2004). (Pubitemid 41103428)
    • (2004) Journal of Bone and Mineral Research , vol.19 , Issue.11 , pp. 1779-1786
    • Munns, C.F.J.1    Rauch, F.2    Zeitlin, L.3    Fassier, F.4    Glorieux, F.H.5
  • 173
  • 175
    • 0034537061 scopus 로고    scopus 로고
    • Operative treatment of severe scoliosis in osteogenesis imperfecta: Results of 20 patients after halo traction and posterior spondylodesis with instrumentation
    • DOI 10.1007/s005860000165
    • Janus, G. J., Finidori, G., Engelbert, R. H., Pouliquen, M. & Pruijs, J. E. Operative treatment of severe scoliosis in osteogenesis imperfecta: results of 20 patients after halo traction and posterior spondylodesis with instrumentation. Eur. Spine J. 9, 486-491 (2000). (Pubitemid 32005651)
    • (2000) European Spine Journal , vol.9 , Issue.6 , pp. 486-491
    • Janus, G.J.M.1    Finidori, G.2    Engelbert, R.H.H.3    Pouliquen, M.4    Pruijs, J.E.H.5
  • 176
    • 33845960043 scopus 로고    scopus 로고
    • Treatment of children with osteogenesis imperfecta
    • DOI 10.1007/s11914-996-0025-2
    • Rauch, F. & Glorieux, F. H. Treatment of children with osteogenesis imperfecta. Curr. Osteoporos. Rep. 4, 159-164 (2006). (Pubitemid 46030453)
    • (2006) Current Osteoporosis Reports , vol.4 , Issue.4 , pp. 159-164
    • Rauch, F.1    Glorieux, F.H.2
  • 177
    • 42549157989 scopus 로고    scopus 로고
    • Osteogenesis imperfecta: Update on presentation and management
    • Cheung, M. S. & Glorieux, F. H. Osteogenesis imperfecta: update on presentation and management. Rev. Endocr. Metab. Disord. 9, 153-160 (2008).
    • (2008) Rev. Endocr. Metab. Disord. , vol.9 , pp. 153-160
    • Cheung, M.S.1    Glorieux, F.H.2
  • 178
    • 59749088584 scopus 로고    scopus 로고
    • Clinical review 1: Bisphosphonate use in childhood osteoporosis
    • Bachrach, L. K. & Ward, L. M. Clinical review 1: Bisphosphonate use in childhood osteoporosis. J. Clin. Endocrinol. Metab. 94, 400-409 (2009).
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 400-409
    • Bachrach, L.K.1    Ward, L.M.2
  • 179
    • 55049132015 scopus 로고    scopus 로고
    • Bisphosphonate therapy for osteogenesis imperfecta
    • Art. No.: CD005088. doi:10.1002/14651858.CD005088.pub2
    • Phillipi, C. A., Remmington, T. & Steiner, R. D. Bisphosphonate therapy for osteogenesis imperfecta. Cochrane Database of Systematic Reviews, Issue 1. Art. No.: CD005088. doi:10.1002/14651858.CD005088.pub2 (2008).
    • (2008) Cochrane Database of Systematic Reviews , Issue.1
    • Phillipi, C.A.1    Remmington, T.2    Steiner, R.D.3
  • 180
    • 0036841117 scopus 로고    scopus 로고
    • The effects of intravenous pamidronate on the bone tissue of children and adolescents with osteogenesis imperfecta
    • DOI 10.1172/JCI200215952
    • Rauch, F., Travers, R., Plotkin, H. & Glorieux, F. H. The effects of intravenous pamidronate on the bone tissue of children and adolescents with osteogenesis imperfecta. J. Clin. Invest. 110, 1293-1299 (2002). (Pubitemid 35285755)
    • (2002) Journal of Clinical Investigation , vol.110 , Issue.9 , pp. 1293-1299
    • Rauch, F.1    Travers, R.2    Plotkin, H.3    Glorieux, F.H.4
  • 181
    • 33646502801 scopus 로고    scopus 로고
    • Should children with osteogenesis imperfecta be treated with bisphosphonates?
    • Marini, J. C. Should children with osteogenesis imperfecta be treated with bisphosphonates? Nat. Clin. Pract. Endocrinol. Metab. 2, 14-15 (2006).
    • (2006) Nat. Clin. Pract. Endocrinol. Metab. , vol.2 , pp. 14-15
    • Marini, J.C.1
  • 182
    • 33748186513 scopus 로고    scopus 로고
    • Vertebral morphometry in children and adolescents with osteogenesis imperfecta: Effect of intravenous pamidronate treatment
    • DOI 10.1016/j.bone.2006.04.004, PII S8756328206004182
    • Land, C., Rauch, F., Munns, C. F., Sahebjam, S. & Glorieux, F. H. Vertebral morphometry in children and adolescents with osteogenesis imperfecta: effect of intravenous pamidronate treatment. Bone 39, 901-906 (2006). (Pubitemid 44311714)
    • (2006) Bone , vol.39 , Issue.4 , pp. 901-906
    • Land, C.1    Rauch, F.2    Munns, C.F.3    Sahebjam, S.4    Glorieux, F.H.5
  • 183
    • 57949110203 scopus 로고    scopus 로고
    • Effects of bisphosphonates in children with osteogenesis imperfecta: An AACPDM systematic review
    • Castillo, H. & Samson-Fang, L. Effects of bisphosphonates in children with osteogenesis imperfecta: an AACPDM systematic review. Dev. Med. Child. Neurol. 51, 17-29 (2009).
    • (2009) Dev. Med. Child. Neurol. , vol.51 , pp. 17-29
    • Castillo, H.1    Samson-Fang, L.2
  • 184
    • 79951705431 scopus 로고    scopus 로고
    • Alendronate for the treatment of pediatric osteogenesis imperfecta: A randomized placebo-controlled study
    • Ward, L. M. et al. Alendronate for the treatment of pediatric osteogenesis imperfecta: a randomized placebo-controlled study. J. Clin. Endocrinol. Metab. 96, 355-364 (2011).
    • (2011) J. Clin. Endocrinol. Metab. , vol.96 , pp. 355-364
    • Ward, L.M.1
  • 185
    • 67651146677 scopus 로고    scopus 로고
    • Bone: Use of bisphosphonates in children-proceed with caution
    • Marini, J. C. Bone: Use of bisphosphonates in children-proceed with caution. Nat. Rev. Endocrinol. 5, 241-243 (2009).
    • (2009) Nat. Rev. Endocrinol. , vol.5 , pp. 241-243
    • Marini, J.C.1
  • 186
    • 65949110568 scopus 로고    scopus 로고
    • Alendronate treatment of the brtl osteogenesis imperfecta mouse improves femoral geometry and load response before fracture but decreases predicted material properties and has detrimental effects on osteoblasts and bone formation
    • Uveges, T. E. et al. Alendronate treatment of the brtl osteogenesis imperfecta mouse improves femoral geometry and load response before fracture but decreases predicted material properties and has detrimental effects on osteoblasts and bone formation. J. Bone Miner. Res. 24, 849-859 (2009).
    • (2009) J. Bone Miner. Res. , vol.24 , pp. 849-859
    • Uveges, T.E.1
  • 187
    • 40449117671 scopus 로고    scopus 로고
    • No osteonecrosis in jaws of young patients with osteogenesis imperfecta treated with bisphosphonates
    • DOI 10.1111/j.1600-0714.2007.00607.x
    • Malmgren, B., Aström, E. & Söderhäll, S. No osteonecrosis in jaws of young patients with osteogenesis imperfecta treated with bisphosphonates. J. Oral Pathol. Med. 37, 196-200 (2008). (Pubitemid 351347604)
    • (2008) Journal of Oral Pathology and Medicine , vol.37 , Issue.4 , pp. 196-200
    • Malmgren, B.1    Astrom, E.2    Soderhall, S.3
  • 188
    • 34347400066 scopus 로고    scopus 로고
    • Can bisphosphonate treatment be stopped in a growing child with skeletal fragility?
    • DOI 10.1007/s00198-007-0330-3
    • Ward, K. A., Adams, J. E., Freemont, T. J. & Mughal, M. Z. Can. bisphosphonate treatment be stopped in a growing child with skeletal fragility? Osteoporos. Int. 18, 1137-1140 (2007). (Pubitemid 47019997)
    • (2007) Osteoporosis International , vol.18 , Issue.8 , pp. 1137-1140
    • Ward, K.A.1    Adams, J.E.2    Freemont, T.J.3    Mughal, M.Z.4
  • 189
    • 79952782200 scopus 로고    scopus 로고
    • New drugs: Denosumab, dienogest/estradiol valerate, and polidocanol
    • Hussar, D. A. & Stevenson, T. New drugs: Denosumab, dienogest/estradiol valerate, and polidocanol. J. Am. Pharm. Assoc. 50, 658-662 (2003).
    • (2003) J. Am. Pharm. Assoc. , vol.50 , pp. 658-662
    • Hussar, D.A.1    Stevenson, T.2
  • 190
    • 77649317112 scopus 로고    scopus 로고
    • RANKL inhibition improves bone properties in a mouse model of osteogenesis imperfecta
    • Bargman, R., Huang, A., Boskey, A. L., Raggio, C. & Pleshko, N. RANKL inhibition improves bone properties in a mouse model of osteogenesis imperfecta. Connect. Tissue Res. 51, 123-131 (2010).
    • (2010) Connect. Tissue Res. , vol.51 , pp. 123-131
    • Bargman, R.1    Huang, A.2    Boskey, A.L.3    Raggio, C.4    Pleshko, N.5
  • 191
    • 34547590675 scopus 로고    scopus 로고
    • Local delivery of osteoprotegerin inhibits mechanically mediated bone modeling in orthodontic tooth movement
    • DOI 10.1016/j.bone.2007.04.194, PII S8756328207003730
    • Dunn, M. D., Park, C. H., Kostenuik, P. J., Kapila, S. & Giannobile, W. V. Local delivery of osteoprotegerin inhibits mechanically mediated bone modeling in orthodontic tooth movement. Bone 41, 446-455 (2007). (Pubitemid 47199141)
    • (2007) Bone , vol.41 , Issue.3 , pp. 446-455
    • Dunn, M.D.1    Park, C.H.2    Kostenuik, P.J.3    Kapila, S.4    Giannobile, W.V.5
  • 192
    • 43449105043 scopus 로고    scopus 로고
    • Effects of bisphosphonates on tooth eruption in children with osteogenesis imperfecta
    • Kamoun-Goldrat, A., Ginisty, D. & Le Merrer, M. Effects of bisphosphonates on tooth eruption in children with osteogenesis imperfecta. Eur. J. Oral Sci. 116, 195-198 (2008).
    • (2008) Eur. J. Oral Sci. , vol.116 , pp. 195-198
    • Kamoun-Goldrat, A.1    Ginisty, D.2    Le Merrer, M.3
  • 193
    • 77956863339 scopus 로고    scopus 로고
    • Sclerostin: A gem from the genome leads to bone-building antibodies
    • Paszty, C., Turner, C. H. & Robinson, M. K. Sclerostin: a gem from the genome leads to bone-building antibodies. J. Bone Miner. Res. 25, 1897-1904 (2010).
    • (2010) J. Bone Miner. Res. , vol.25 , pp. 1897-1904
    • Paszty, C.1    Turner, C.H.2    Robinson, M.K.3
  • 195
    • 77956285236 scopus 로고    scopus 로고
    • GH in combination with bisphosphonate treatment in osteogenesis imperfecta
    • Antoniazzi, F. et al. GH in combination with bisphosphonate treatment in osteogenesis imperfecta. Eur. J. Endocrinol. 163, 479-487 (2010).
    • (2010) Eur. J. Endocrinol. , vol.163 , pp. 479-487
    • Antoniazzi, F.1
  • 196
    • 1842487509 scopus 로고    scopus 로고
    • High proportion of mutant osteoblasts is compatible with normal skeletal function in mosaic carriers of osteogenesis imperfecta
    • DOI 10.1086/383252
    • Cabral, W. A. & Marini, J. C. High proportion of mutant osteoblasts is compatible with normal skeletal function in mosaic carriers of osteogenesis imperfecta. Am. J. Hum. Genet. 74, 752-760 (2004). (Pubitemid 38420105)
    • (2004) American Journal of Human Genetics , vol.74 , Issue.4 , pp. 752-760
    • Cabral, W.A.1    Marini, J.C.2
  • 197
    • 37349125312 scopus 로고    scopus 로고
    • Distribution of single-cell expanded marrow derived progenitors in a developing mouse model of osteogenesis imperfecta following systemic transplantation
    • DOI 10.1634/stemcells.2007-0466
    • Li, F., Wang, X. & Niyibizi, C. Distribution of single-cell expanded marrow derived progenitors in a developing mouse model of osteogenesis imperfecta following systemic transplantation. Stem Cells 25, 3183-3193 (2007). (Pubitemid 350294444)
    • (2007) Stem Cells , vol.25 , Issue.12 , pp. 3183-3193
    • Li, F.1    Wang, X.2    Niyibizi, C.3
  • 198
  • 200
    • 37549069296 scopus 로고    scopus 로고
    • Gene targeting of mutant COL1A2 alleles in mesenchymal stem cells from individuals with osteogenesis imperfecta
    • Chamberlain, J. R. et al. Gene targeting of mutant COL1A2 alleles in mesenchymal stem cells from individuals with osteogenesis imperfecta. Mol. Ther. 16, 187-193 (2008).
    • (2008) Mol. Ther. , vol.16 , pp. 187-193
    • Chamberlain, J.R.1
  • 201
    • 20444365492 scopus 로고    scopus 로고
    • Emerging therapeutic approaches for osteogenesis imperfecta
    • DOI 10.1016/j.molmed.2005.04.006, PII S1471491405000973
    • Millington-Ward, S., McMahon, H. P. & Farrar, G. J. Emerging therapeutic approaches for osteogenesis imperfecta. Trends Mol. Med. 11, 299-305 (2005). (Pubitemid 40804794)
    • (2005) Trends in Molecular Medicine , vol.11 , Issue.6 , pp. 299-305
    • Millington-Ward, S.1    McMahon, H.P.2    Farrar, G.J.3
  • 202
    • 0034668040 scopus 로고    scopus 로고
    • Hammerhead ribozymes selectively suppress mutant type i collagen mRNA in osteogenesis imperfecta fibroblasts
    • Dawson, P. A. & Marini, J. C. Hammerhead ribozymes selectively suppress mutant type I collagen mRNA in osteogenesis imperfecta fibroblasts. Nucleic Acids Res. 28, 4013-4020 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4013-4020
    • Dawson, P.A.1    Marini, J.C.2
  • 203
    • 71749110782 scopus 로고    scopus 로고
    • The 26 S. proteasome: From basic mechanisms to drug targeting
    • Navon, A. & Ciechanover, A. The 26 S. proteasome: from basic mechanisms to drug targeting. J. Biol. Chem. 284, 33713-33718 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 33713-33718
    • Navon, A.1    Ciechanover, A.2
  • 204
    • 70149093873 scopus 로고    scopus 로고
    • Small-molecule modulation of cellular chaperones to treat protein misfolding disorders
    • Sloan, L. A., Fillmore, M. C. & Churcher, I. Small-molecule modulation of cellular chaperones to treat protein misfolding disorders. Curr. Opin. Drug Discov. Devel. 12, 666-681 (2009).
    • (2009) Curr. Opin. Drug Discov. Devel. , vol.12 , pp. 666-681
    • Sloan, L.A.1    Fillmore, M.C.2    Churcher, I.3
  • 205
    • 34547126694 scopus 로고    scopus 로고
    • Novel therapeutic strategies for the treatment of protein-misfolding diseases
    • Rochet, J. C. Novel therapeutic strategies for the treatment of protein-misfolding diseases. Expert Rev. Mol. Med. 9, 1-34 (2007).
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-34
    • Rochet, J.C.1
  • 207
    • 0023854836 scopus 로고
    • Perinatal lethal osteogenesis imperfecta in transgenic mice bearing an engineered mutant pro-α1(I) collagen gene
    • DOI 10.1038/332131a0
    • Stacey, A. et al. Perinatal lethal osteogenesis imperfecta in transgenic mice bearing an engineered mutant pro-alpha 1(I) collagen gene. Nature 332, 131-136 (1988). (Pubitemid 18083558)
    • (1988) Nature , vol.332 , Issue.6160 , pp. 131-136
    • Stacey, A.1    Bateman, J.2    Choi, T.3    Mascara, T.4    Cole, W.5    Jaenisch, R.6
  • 208
    • 0026327359 scopus 로고
    • Transgenic mice that express a mini-gene version of the human gene for type I procollagen (COL1A1) develop a phenotype resembling a lethal form of osteogenesis imperfecta
    • Khillan, J. S., Olsen, A. S., Kontusaari, S., Sokolov, B. & Prockop, D. J. Transgenic mice that express a mini-gene version of the human gene for type I procollagen (COL1A1) develop a phenotype resembling a lethal form of osteogenesis imperfecta. J. Biol. Chem. 266, 23373-23379 (1991). (Pubitemid 21908803)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.34 , pp. 23373-23379
    • Khillan, J.S.1    Olsen, A.S.2    Kontusaari, S.3    Sokolov, B.4    Prockop, D.J.5
  • 209
    • 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 α1(I) G349C substitution. Variability in phenotype in BrtlIV mice
    • DOI 10.1074/jbc.274.53.37923
    • Forlino, A., Porter, F. D., Lee, E. J., Westphal, H. & Marini, J. C. 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 BrtlIV mice. J. Biol. Chem. 274, 37923-37931 (1999). (Pubitemid 30026860)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.53 , pp. 37923-37931
    • Forlino, A.1    Porter, F.D.2    Eric J, L.3    Westphal, H.4    Marini, J.C.5
  • 210
    • 0021328414 scopus 로고
    • Insertion of retrovirus into the first intron of α1(I) collagen gene leads to embryonic lethal mutation in mice
    • Harbers, K., Kuehn, M., Delius, H. & Jaenisch, R. Insertion of retrovirus into the first intron of alpha 1(I) collagen gene to embryonic lethal mutation in mice. Proc. Natl Acad. Sci. USA 81, 1504-1508 (1984). (Pubitemid 14174531)
    • (1984) ISOTOPENPRAXIS , vol.20 , Issue.1 , pp. 1504-1508
    • Harbers, K.1    Kuehn, M.2    Delius, H.3    Jaenisch, R.4
  • 212
    • 66349127389 scopus 로고    scopus 로고
    • Positive regulation of adult bone formation by osteoblast-specific transcription factor osterix
    • Baek, W. Y. et al. Positive regulation of adult bone formation by osteoblast-specific transcription factor osterix. J. Bone Miner. Res. 24, 1055-1065 (2009).
    • (2009) J. Bone Miner. Res. , vol.24 , pp. 1055-1065
    • Baek, W.Y.1
  • 213
    • 33846029867 scopus 로고    scopus 로고
    • Molecular recognition in the assembly of collagens: Terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers
    • DOI 10.1074/jbc.R600025200
    • Khoshnoodi, J., Cartailler, J. P., Alvares, K., Veis, A. & Hudson, B. G. Molecular recognition in the assembly of collagens: terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers. J. Biol. Chem. 281, 38117-38121 (2006). (Pubitemid 46041935)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38117-38121
    • Khoshnoodi, J.1    Cartailler, J.-P.2    Alvares, K.3    Veis, A.4    Hudson, B.G.5
  • 214
    • 77953138390 scopus 로고    scopus 로고
    • A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47
    • Nishikawa, Y. et al. A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47. Bioorg. Med. Chem. 18, 3767-3775 (2010).
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 3767-3775
    • Nishikawa, Y.1
  • 215
    • 0027182875 scopus 로고
    • BiP binds type I procollagen proα chains with mutations in the carboxyl- terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
    • Chessler, S. D. & Byers, P. H. BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem. 268, 18226-18233 (1993). (Pubitemid 23260347)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 18226-18233
    • Chessler, S.D.1    Byers, P.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.