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- [31] SUBSTITUTION OF SERINE FOR GLYCINE-883 IN THE TRIPLE-HELIX OF THE PRO-ALPHA-1(I) CHAIN OF TYPE-I PROCOLLAGEN PRODUCES OSTEOGENESIS IMPERFECTA TYPE-IV AND INTRODUCES A STRUCTURAL-CHANGE IN THE TRIPLE-HELIX THAT DOES NOT ALTER CLEAVAGE OF THE MOLECULE BY PROCOLLAGEN N-PROTEINASE JOURNAL OF BIOLOGICAL CHEMISTRY, 1994, 269 (48) : 30352 - 30357
- [32] Substitution of serine for glycine 883 in the triple helix of the proα1(I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase Journal of Biological Chemistry, 1994, 269 (48): : 30352 - 30357
- [38] A SHORTENED PRO-ALPHA-2(I) CHAIN IN A MILD VARIANT OF OSTEOGENESIS IMPERFECTA - THE ALTERED STRUCTURE MAKES TYPE-I PROCOLLAGEN RESISTANT TO PROCOLLAGEN N-PROTEINASE JOURNAL OF CELL BIOLOGY, 1983, 97 (05): : A229 - A229
- [39] OSTEOGENESIS IMPERFECTA - THE POSITION OF SUBSTITUTION FOR GLYCINE BY CYSTEINE IN THE TRIPLE HELICAL DOMAIN OF THE PRO-ALPHA-1(I) CHAINS OF TYPE-I COLLAGEN DETERMINES THE CLINICAL PHENOTYPE JOURNAL OF CLINICAL INVESTIGATION, 1989, 84 (04): : 1206 - 1214