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Volumn 97, Issue 3, 1996, Pages 287-290

Deletion of a Gly-Pro-Pro repeat in the proα2(I) chain of procollagen I in a family with dominant osteogenesis imperfecta type IV

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; CYANOGEN BROMIDE; PROCOLLAGEN; REPETITIVE DNA;

EID: 0030059552     PISSN: 03406717     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02185755     Document Type: Article
Times cited : (11)

References (13)
  • 1
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    • Proteolytic enzymes as probes for the triple-helical conformation of procollagen
    • Bruckner P, Prockop DJ (1981) Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal Biochem 110:360-368
    • (1981) Anal Biochem , vol.110 , pp. 360-368
    • Bruckner, P.1    Prockop, D.J.2
  • 3
    • 0025827624 scopus 로고
    • A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta
    • Hawkins JR, Superti-Furga A, Steinmann B, Dalgleish R (1991) A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta. J Biol Chem 266:22370-22374
    • (1991) J Biol Chem , vol.266 , pp. 22370-22374
    • Hawkins, J.R.1    Superti-Furga, A.2    Steinmann, B.3    Dalgleish, R.4
  • 5
    • 0027410984 scopus 로고
    • A single amino acid deletion in the α2(I) chain of type I collagen produces osteogenesis imperfecta type III
    • Molyneux K, Starman BJ, Byers PH, Dalgleish R (1993) A single amino acid deletion in the α2(I) chain of type I collagen produces osteogenesis imperfecta type III. Hum Genet 90:621-628
    • (1993) Hum Genet , vol.90 , pp. 621-628
    • Molyneux, K.1    Starman, B.J.2    Byers, P.H.3    Dalgleish, R.4
  • 6
    • 0028220202 scopus 로고
    • Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
    • Raghunath M, Bruckner P, Steinmann B (1994) Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J Mol Biol 236:940-949
    • (1994) J Mol Biol , vol.236 , pp. 940-949
    • Raghunath, M.1    Bruckner, P.2    Steinmann, B.3
  • 7
    • 0021181518 scopus 로고
    • Cysteine in the triple-helical domain of one allelic product of the α1(I) gene of type I collagen produces a lethal form of osteogenesis imperfecta
    • Steinmann B, Rao VH, Vogel A, Bruckner P, Gitzelmann R, Byers PH (1984) Cysteine in the triple-helical domain of one allelic product of the α1(I) gene of type I collagen produces a lethal form of osteogenesis imperfecta. J Biol Chem 259: 11129-11138
    • (1984) J Biol Chem , vol.259 , pp. 11129-11138
    • Steinmann, B.1    Rao, V.H.2    Vogel, A.3    Bruckner, P.4    Gitzelmann, R.5    Byers, P.H.6
  • 8
    • 0025996162 scopus 로고
    • Substitution of cysteine for glycine-α 1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution
    • Steinmann B, Westerhausen A, Constantinou CD, Superti-Furga A, Prockop DJ (1991) Substitution of cysteine for glycine-α 1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution. Biochem J 279:747-752
    • (1991) Biochem J , vol.279 , pp. 747-752
    • Steinmann, B.1    Westerhausen, A.2    Constantinou, C.D.3    Superti-Furga, A.4    Prockop, D.J.5
  • 9
    • 0027509286 scopus 로고
    • Linkage analysis in dominantly inherited osteogenesis imperfecta
    • Sykes B (1993) Linkage analysis in dominantly inherited osteogenesis imperfecta. Am J Med Genet 45:212-216
    • (1993) Am J Med Genet , vol.45 , pp. 212-216
    • Sykes, B.1
  • 10
    • 0022455539 scopus 로고
    • Structural study of a mutant type I collagen from a patient with lethal osteogenesis imperfecta containing an intramolecular disulfide bond in the triple-helical domain
    • Traub W, Steinmann B (1986) Structural study of a mutant type I collagen from a patient with lethal osteogenesis imperfecta containing an intramolecular disulfide bond in the triple-helical domain. FEBS Lett 198:213-216
    • (1986) FEBS Lett , vol.198 , pp. 213-216
    • Traub, W.1    Steinmann, B.2
  • 11
    • 0027303622 scopus 로고
    • Extracellular matrix deposition in cultured dermal fibroblasts from 4 probands affected by osteogenesis imperfecta
    • Valli M, Rossi A, Forlino A, Tenni R, Cetta G (1993) Extracellular matrix deposition in cultured dermal fibroblasts from 4 probands affected by osteogenesis imperfecta. Matrix 13:275-280
    • (1993) Matrix , vol.13 , pp. 275-280
    • Valli, M.1    Rossi, A.2    Forlino, A.3    Tenni, R.4    Cetta, G.5
  • 12
    • 0024230293 scopus 로고
    • A substitution of cysteine for glycine 748 of the α1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away
    • Vogel BE, Doelz R, Kadler KE, Hojima Y, Engel J, Prockop DJ (1988) A substitution of cysteine for glycine 748 of the α1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away J Biol Chem 263:19249-19255
    • (1988) J Biol Chem , vol.263 , pp. 19249-19255
    • Vogel, B.E.1    Doelz, R.2    Kadler, K.E.3    Hojima, Y.4    Engel, J.5    Prockop, D.J.6
  • 13
    • 0026476719 scopus 로고
    • A tripeptide deletion in the triple-helical domain of the proα1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase
    • Wallis GA, Kadler KE, Starman BJ, Byers PH (1992) A tripeptide deletion in the triple-helical domain of the proα1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. J Biol Chem 267:25529-25534
    • (1992) J Biol Chem , vol.267 , pp. 25529-25534
    • Wallis, G.A.1    Kadler, K.E.2    Starman, B.J.3    Byers, P.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.